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Conserved domains on  [gi|1308984722|gb|PKO90040|]
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hypothetical protein CVU18_02180 [Betaproteobacteria bacterium HGW-Betaproteobacteria-12]

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 ...
501-907 3.88e-98

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: 331.36  E-value: 3.88e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 501 DQRRIEEELAAHRQHLQQLVDQRTGELAQATAAAES--------------ANLAKSAFLANMSHEIRTPMNAIIGLNYLL 566
Cdd:TIGR02956 410 DERQVAQELQEHKESLEQLVAQRTQELAETNERLNAevknhakaraeaeeANRAKSAFLATMSHEIRTPLNGILGTLELL 489
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 567 LKSPLEPAQRDKLLKVTSASEHLLQVINDILDLSKIESGKLELENQTFDPREVLQAAAAVIRDQALGKGLLVGVD-GGKL 645
Cdd:TIGR02956 490 GDTGLTSQQQQYLQVINRSGESLLDILNDILDYSKIEAGHLSISPRPFDLNALLDDVHHLMVSRAQLKGIQLRLNiPEQL 569
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 646 PALAIGDAKRLRQVLINFAGNALKFTRAGSIHLSGELlaNDGENVtcRFVVSDTGLGIRPEDVPRLFKPFEQLDASttRQ 725
Cdd:TIGR02956 570 PNWWQGDGPRIRQVLINLVGNAIKFTDRGSVVLRVSL--NDDSSL--LFEVEDTGCGIAEEEQATLFDAFTQADGR--RR 643
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 726 YGGTGLGLAIARHLAHLMDGEVGVDSTPGQGSSFWITARLkaaglpPENAAGSSPALSQRLF---GRVLLVEDEPLNREI 802
Cdd:TIGR02956 644 SGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTLPL------TRGKPAEDSATLTVIDlppQRVLLVEDNEVNQMV 717
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 803 GCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRAL-PGGAAIPIVALTANAYSEDRQRCLA 881
Cdd:TIGR02956 718 AQGFLTRLGHKVTLAESGQSALECFHQHAFDLALLDINLPDGDGVTLLQQLRAIyGAKNEVKFIAFSAHVFNEDVAQYLA 797
                         410       420
                  ....*....|....*....|....*.
gi 1308984722 882 AGMNDFLAKPVDPEALYTILGKYLAG 907
Cdd:TIGR02956 798 AGFDGFLAKPVVEEQLTAMIAVILAG 823
PAS COG2202
PAS domain [Signal transduction mechanisms];
378-522 8.71e-37

PAS domain [Signal transduction mechanisms];


:

Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 139.39  E-value: 8.71e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 378 AALEIAEQDLRRLSTAVEQSPASIVITDINARITYVNLAFCVTSGYFPDEVIGENPRILQSGNTPPATYQAMWQTLTAGE 457
Cdd:COG2202     1 TAEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGG 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1308984722 458 IWRGELVNRRKDGSHYIERATISPVRGSDGTTSQYVAVKEDISDQRRIEEELAAHRQHLQQLVDQ 522
Cdd:COG2202    81 VWRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEERLRLLVEN 145
dCache_1 pfam02743
Cache domain; Double cache domain 1 covers the last three strands from the membrane distal ...
30-264 4.98e-12

Cache domain; Double cache domain 1 covers the last three strands from the membrane distal PAS-like domain, the first two strands of the membrane proximal domain, and the connecting elements between the two domains. This domain when present in chemoreceptors recognize several signals such as proteinogenic amino acids, GABA, Histamine and polyamines, decanoic acid, Autoinducer-2, purine derivatives, quaternary amines, citrate and taurine, among others. When associated with histidine kinases, it recognizes C3/C4-dicarboxylic acids, Spermine, guanosine and Autoinducer-2 (Mantilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1 https://doi.org/10.1093/femsre/fuab043).


:

Pssm-ID: 460673 [Multi-domain]  Cd Length: 237  Bit Score: 66.98  E-value: 4.98e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722  30 RHERRLATDHIVTLGKSLlqAARIEEEaaLRQVREMLHIMAGADNMRSLDADDCSGLAKRL---LSVTHDIANIGAALAN 106
Cdd:pfam02743   1 KAIKEQAEEQLLSLAKQL--AENIESY--LDSLEEILELLASNPDLQDLLSAPAEEELAKLeslLRSNPGISSIYLVDAD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 107 GDVFCSAH--PITRPVNVADRPWFQEALTATDITS---GHYQTGLISGKRGITIGLPVRDAEGKLQAALYLASDIAWFDR 181
Cdd:pfam02743  77 GRVLASSDesPSYPGLDVSERPWYKEALKGGGGIIwvfSSPYPSSESGEPVLTIARPIYDDDGEVIGVLVADLDLDTLQE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 182 ISRNQQLPKGWTSLLVTDDGSVVSRHPDPDIWRGSAFDAAsrERLLAALRHDDDRVVMNGLDGIERLYLLQRLQIADGHL 261
Cdd:pfam02743 157 LLSQIKLGEGGYVFIVDSDGRILAHPLGKNLRSLLAPFLG--KSLADALPGSGITEIAVDLDGEDYLVAYAPIPGTGWTL 234

                  ...
gi 1308984722 262 VAA 264
Cdd:pfam02743 235 VVV 237
 
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 ...
501-907 3.88e-98

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: 331.36  E-value: 3.88e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 501 DQRRIEEELAAHRQHLQQLVDQRTGELAQATAAAES--------------ANLAKSAFLANMSHEIRTPMNAIIGLNYLL 566
Cdd:TIGR02956 410 DERQVAQELQEHKESLEQLVAQRTQELAETNERLNAevknhakaraeaeeANRAKSAFLATMSHEIRTPLNGILGTLELL 489
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 567 LKSPLEPAQRDKLLKVTSASEHLLQVINDILDLSKIESGKLELENQTFDPREVLQAAAAVIRDQALGKGLLVGVD-GGKL 645
Cdd:TIGR02956 490 GDTGLTSQQQQYLQVINRSGESLLDILNDILDYSKIEAGHLSISPRPFDLNALLDDVHHLMVSRAQLKGIQLRLNiPEQL 569
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 646 PALAIGDAKRLRQVLINFAGNALKFTRAGSIHLSGELlaNDGENVtcRFVVSDTGLGIRPEDVPRLFKPFEQLDASttRQ 725
Cdd:TIGR02956 570 PNWWQGDGPRIRQVLINLVGNAIKFTDRGSVVLRVSL--NDDSSL--LFEVEDTGCGIAEEEQATLFDAFTQADGR--RR 643
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 726 YGGTGLGLAIARHLAHLMDGEVGVDSTPGQGSSFWITARLkaaglpPENAAGSSPALSQRLF---GRVLLVEDEPLNREI 802
Cdd:TIGR02956 644 SGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTLPL------TRGKPAEDSATLTVIDlppQRVLLVEDNEVNQMV 717
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 803 GCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRAL-PGGAAIPIVALTANAYSEDRQRCLA 881
Cdd:TIGR02956 718 AQGFLTRLGHKVTLAESGQSALECFHQHAFDLALLDINLPDGDGVTLLQQLRAIyGAKNEVKFIAFSAHVFNEDVAQYLA 797
                         410       420
                  ....*....|....*....|....*.
gi 1308984722 882 AGMNDFLAKPVDPEALYTILGKYLAG 907
Cdd:TIGR02956 798 AGFDGFLAKPVVEEQLTAMIAVILAG 823
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
541-904 7.05e-93

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 315.64  E-value: 7.05e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 541 KSAFLANMSHEIRTPMNAIIGLNYLLLKSPLEPAQRDKLLKVTSASEHLLQVINDILDLSKIESGKLELENQTFDPREVL 620
Cdd:PRK11107  293 KSEFLANMSHELRTPLNGVIGFTRQTLKTPLTPTQRDYLQTIERSANNLLAIINDILDFSKLEAGKLVLENIPFSLRETL 372
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 621 QAAAAVIRDQALGKGL--LVGVDGgKLPALAIGDAKRLRQVLINFAGNALKFTRAGSIHLSGELLANDGENVTCRFVVSD 698
Cdd:PRK11107  373 DEVVTLLAHSAHEKGLelTLNIDP-DVPDNVIGDPLRLQQIITNLVGNAIKFTESGNIDILVELRALSNTKVQLEVQIRD 451
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 699 TGLGIRPEDVPRLFKPFEQLDASTTRQYGGTGLGLAIARHLAHLMDGEVGVDSTPGQGSSFWITARLKaaglPPENAAGS 778
Cdd:PRK11107  452 TGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHLPLD----LNPNPIID 527
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 779 SPALsQRLFG-RVLLVEDEPLNREIGCDLLAATGLEVA------------------------------------------ 815
Cdd:PRK11107  528 GLPT-DCLAGkRLLYVEPNSAAAQATLDILSETPLEVTysptlsqlpeahydilllglpvtfrepltmlherlakaksmt 606
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722     --------------------------------------------------------------------------------
Cdd:PRK11107  607 dflilalpcheqvlaeqlkqdgadaclskplshtrllpallepchhkqppllpptdesrlpltvmavddnpanlkligal 686
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 816 ---------TADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALPGGAAIPIVALTANAYSEDRQRCLAAGMND 886
Cdd:PRK11107  687 leeqvehvvLCDSGHQAVEQAKQRPFDLILMDIQMPGMDGIRACELIRQLPHNQNTPIIAVTAHAMAGERERLLSAGMDD 766
                         490
                  ....*....|....*...
gi 1308984722 887 FLAKPVDPEALYTILGKY 904
Cdd:PRK11107  767 YLAKPIDEAMLKQVLLRY 784
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
448-762 4.91e-68

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 230.57  E-value: 4.91e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 448 AMWQTLTAGEIWRGELVNRRKDGSHYIERATISPVRGSDGTTSQYVAVKEDISDQRRIEEELAAHRQHLQQLVDQRTGEL 527
Cdd:COG0642    17 LLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLL 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 528 AQATAAAESANLAKSAFLANMSHEIRTPMNAIIGLNYLLLKSPlEPAQRDKLLKVTSASEHLLQVINDILDLSKIESGKL 607
Cdd:COG0642    97 LALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLEEL-DEEQREYLETILRSADRLLRLINDLLDLSRLEAGKL 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 608 ELENQTFDPREVLQAAAAVIRDQALGKGLLVGVDGGKLPALAIGDAKRLRQVLINFAGNALKFTRAGS-IHLSGELland 686
Cdd:COG0642   176 ELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDDLPTVRGDPDRLRQVLLNLLSNAIKYTPEGGtVTVSVRR---- 251
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1308984722 687 gENVTCRFVVSDTGLGIRPEDVPRLFKPFEQLDASttRQYGGTGLGLAIARHLAHLMDGEVGVDSTPGQGSSFWIT 762
Cdd:COG0642   252 -EGDRVRISVEDTGPGIPPEDLERIFEPFFRTDPS--RRGGGTGLGLAIVKRIVELHGGTIEVESEPGKGTTFTVT 324
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
656-765 5.99e-51

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: 174.22  E-value: 5.99e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 656 LRQVLINFAGNALKFTRAGSIHLSGELLANDGENVTCRFVVSDTGLGIRPEDVPRLFKPFEQLDASTTRQYGGTGLGLAI 735
Cdd:cd16922     1 LRQILLNLLGNAIKFTEEGEVTLRVSLEEEEEDGVQLRFSVEDTGIGIPEEQQARLFEPFSQADSSTTRKYGGTGLGLAI 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 1308984722 736 ARHLAHLMDGEVGVDSTPGQGSSFWITARL 765
Cdd:cd16922    81 SKKLVELMGGDISVESEPGQGSTFTFTLPL 110
PAS COG2202
PAS domain [Signal transduction mechanisms];
378-522 8.71e-37

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 139.39  E-value: 8.71e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 378 AALEIAEQDLRRLSTAVEQSPASIVITDINARITYVNLAFCVTSGYFPDEVIGENPRILQSGNTPPATYQAMWQTLTAGE 457
Cdd:COG2202     1 TAEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGG 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1308984722 458 IWRGELVNRRKDGSHYIERATISPVRGSDGTTSQYVAVKEDISDQRRIEEELAAHRQHLQQLVDQ 522
Cdd:COG2202    81 VWRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEERLRLLVEN 145
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
790-901 1.70e-33

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: 124.57  E-value: 1.70e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 790 VLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALPGGaaIPIVALTA 869
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDPT--TPVIILTA 78
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1308984722 870 NAYSEDRQRCLAAGMNDFLAKPVDPEALYTIL 901
Cdd:pfam00072  79 HGDEDDAVEALEAGADDFLSKPFDPDELLAAI 110
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
651-766 1.96e-31

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 118.91  E-value: 1.96e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722  651 GDAKRLRQVLINFAGNALKFTRA-GSIHLSgelLANDGENVtcRFVVSDTGLGIRPEDVPRLFKPFEQLDaSTTRQYGGT 729
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIKYTPEgGRITVT---LERDGDHV--EITVEDNGPGIPPEDLEKIFEPFFRTD-KRSRKIGGT 74
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1308984722  730 GLGLAIARHLAHLMDGEVGVDSTPGQGSSFWITARLK 766
Cdd:smart00387  75 GLGLSIVKKLVELHGGEISVESEPGGGTTFTITLPLE 111
nifL_nitrog TIGR02938
nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation ...
393-521 8.25e-30

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: 124.63  E-value: 8.25e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 393 AVEQSPASIVITDINARITYVNLAFCVTSGYFPDEVIGENPRILQSGNTPPATYQAMWQTLTAGEIWRGELVNRRKDGSH 472
Cdd:TIGR02938   9 TVDQAPLAISITDLKANILYANDAFTRITGYTKEEIIGKNESVLSNHTTPPEVYQALWGSLAEQKPWAGKLLNRRKDGEL 88
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1308984722 473 YIERATISPVRGSDGTTSQYVAVKEDISDQRRIEEELAAHRQHLQQLVD 521
Cdd:TIGR02938  89 YLAELTVAPVLNEAGETTHFLGMHRDITELHRLEQVVANQKLLIESVVD 137
HK_WalK NF033092
cell wall metabolism sensor histidine kinase WalK; This model describes WalK as found in ...
463-762 7.34e-27

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: 116.78  E-value: 7.34e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 463 LVNRRKDGSHYIERATISPVRGSDGTTSQYVAVKEDISDQRRIEEElaaHRQhlqqlvdqrtgelaqataaaesanlaks 542
Cdd:NF033092  326 LLDFSTEEEPLILRANFSVIQRESGFINGLIAVLHDVTEQEKIEQE---RRE---------------------------- 374
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 543 aFLANMSHEIRTPMNAIiglnylllKSPLEP----AQRD-----KLLKVT-SASEHLLQVINDILDLSKIESGKLELENQ 612
Cdd:NF033092  375 -FVANVSHELRTPLTTM--------RSYLEAladgAWKDpelapRFLGVTqNETERMIRLVNDLLQLSRMDSKDYKLNKE 445
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 613 TFDPREVLQAAA------------AVIRDqaLGKGLL-VGVDGGKlpalaigdakrLRQVLINFAGNALKFTRagsihls 679
Cdd:NF033092  446 WVNFNEFFNYIIdrfemilknkniTFKRE--FPKRDLwVEIDTDK-----------ITQVLDNIISNAIKYSP------- 505
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 680 gellanDGENVTCR---------FVVSDTGLGIRPEDVPRLFKPFEQLDASTTRQYGGTGLGLAIARHLAHLMDGEVGVD 750
Cdd:NF033092  506 ------EGGTITFRllethnriiISISDQGLGIPKKDLDKIFDRFYRVDKARSRKMGGTGLGLAIAKEVVEAHGGRIWAE 579
                         330
                  ....*....|..
gi 1308984722 751 STPGQGSSFWIT 762
Cdd:NF033092  580 SEEGKGTTIYFT 591
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
544-762 4.08e-26

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 113.58  E-value: 4.08e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 544 FLANMSHEIRTPMNAIiglnylLLKSPLEPAQRDKLLKVTSASEHLLQ--------VINDILDLSKIESGKLELENQTFD 615
Cdd:NF040691  274 FVSDVSHELRTPLTTI------RMAADVIHDSRDDFDPATARSAELLHteldrfesLLSDLLEISRFDAGAAELDVEPVD 347
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 616 PREVLQAAAAVIRDQALGKGLLVGVDGGKLPALAIGDAKRLRQVLINFAGNALKFTRAGSIHLSgelLANDGENVTcrFV 695
Cdd:NF040691  348 LRPLVRRVVDALRQLAERAGVELRVDAPGTPVVAEVDPRRVERVLRNLVVNAIEHGEGKPVVVT---VAQDDTAVA--VT 422
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1308984722 696 VSDTGLGIRPEDVPRLFKPFEQLDASTTRQYGGTGLGLAIARHLAHLMDGEVGVDSTPGQGSSFWIT 762
Cdd:NF040691  423 VRDHGVGLKPGEVALVFDRFWRADPARARTTGGTGLGLAIALEDARLHGGWLEAWGRPGQGSQFRLT 489
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
541-762 3.09e-23

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 104.14  E-value: 3.09e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 541 KSAFLANMSHEIRTPMnAIIGLNYLLLKSPLEPAQRDKLLKVTSASEHLLQVINDILDLSKIESGKLELENQTFDPREVL 620
Cdd:NF012163  240 RRDFMADISHELRTPL-AVLRAELEAIQDGIRKFTPESLDSLQAEVGTLTKLVDDLHDLSMSDEGALAYQKASVDLVPLL 318
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 621 QAAAAVIRDQALGKGLLVGVDGGKLPaLAIGDAKRLRQVLINFAGNALKFTRA-GSIHLSGELLANdgenvTCRFVVSDT 699
Cdd:NF012163  319 EVEGGAFRERFASAGLELEVSLPDSS-LVFGDRDRLMQLFNNLLENSLRYTDSgGSLHISASQRPK-----EVTLTVADS 392
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1308984722 700 GLGIRPEDVPRLFKPFEQLDASTTRQYGGTGLGLAIARHLAHLMDGEVGVDSTPGQGSSFWIT 762
Cdd:NF012163  393 APGVSDEQLARLFERFYRVEVSRNRASGGSGLGLAISLNIVQAHGGTLHAAHSPLGGLRIVVT 455
PRK13558 PRK13558
bacterio-opsin activator; Provisional
345-525 6.82e-23

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 104.92  E-value: 6.82e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 345 FNEMISALGERENEHAADHQAIETLNNqlaerlaalEIAEQDLRRLSTAVEQSPASIVITDINAR---ITYVNLAFCVTS 421
Cdd:PRK13558  114 TAAIAERIESAVPEHSRDTEARMPISD---------LTVESDRRLKERALDEAPVGITIADATLPdepLIYINDAFERIT 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 422 GYFPDEVIGENPRILQSGNTPPATYQAMWQTLTAGEIWRGELVNRRKDGSHYIERATISPVRGSDGTTSQYVAVKEDISD 501
Cdd:PRK13558  185 GYSPDEVLGRNCRFLQGEDTNEERVAELREAIDEERPTSVELRNYRKDGSTFWNQVDIAPIRDEDGTVTHYVGFQTDVTE 264
                         170       180
                  ....*....|....*....|....
gi 1308984722 502 QRRIEEELAAHRQHLQQLVDQRTG 525
Cdd:PRK13558  265 RKEAELALQRERRKLQRLLERVEG 288
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
388-499 1.80e-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: 73.22  E-value: 1.80e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 388 RRLSTAVEQSPASIVITDINARITYVNLAFCVTSGYFPDEVIGENPRILQSGNTPPATYQAMWQTLTAGEIWRGELVN-R 466
Cdd:pfam00989   1 EDLRAILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALLQGEESRGFEVSfR 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1308984722 467 RKDGSHYIERATISPVRGSDGTTSQYVAVKEDI 499
Cdd:pfam00989  81 VPDGRPRHVEVRASPVRDAGGEILGFLGVLRDI 113
dCache_1 pfam02743
Cache domain; Double cache domain 1 covers the last three strands from the membrane distal ...
30-264 4.98e-12

Cache domain; Double cache domain 1 covers the last three strands from the membrane distal PAS-like domain, the first two strands of the membrane proximal domain, and the connecting elements between the two domains. This domain when present in chemoreceptors recognize several signals such as proteinogenic amino acids, GABA, Histamine and polyamines, decanoic acid, Autoinducer-2, purine derivatives, quaternary amines, citrate and taurine, among others. When associated with histidine kinases, it recognizes C3/C4-dicarboxylic acids, Spermine, guanosine and Autoinducer-2 (Mantilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1 https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 460673 [Multi-domain]  Cd Length: 237  Bit Score: 66.98  E-value: 4.98e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722  30 RHERRLATDHIVTLGKSLlqAARIEEEaaLRQVREMLHIMAGADNMRSLDADDCSGLAKRL---LSVTHDIANIGAALAN 106
Cdd:pfam02743   1 KAIKEQAEEQLLSLAKQL--AENIESY--LDSLEEILELLASNPDLQDLLSAPAEEELAKLeslLRSNPGISSIYLVDAD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 107 GDVFCSAH--PITRPVNVADRPWFQEALTATDITS---GHYQTGLISGKRGITIGLPVRDAEGKLQAALYLASDIAWFDR 181
Cdd:pfam02743  77 GRVLASSDesPSYPGLDVSERPWYKEALKGGGGIIwvfSSPYPSSESGEPVLTIARPIYDDDGEVIGVLVADLDLDTLQE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 182 ISRNQQLPKGWTSLLVTDDGSVVSRHPDPDIWRGSAFDAAsrERLLAALRHDDDRVVMNGLDGIERLYLLQRLQIADGHL 261
Cdd:pfam02743 157 LLSQIKLGEGGYVFIVDSDGRILAHPLGKNLRSLLAPFLG--KSLADALPGSGITEIAVDLDGEDYLVAYAPIPGTGWTL 234

                  ...
gi 1308984722 262 VAA 264
Cdd:pfam02743 235 VVV 237
PDC1_DGC_like cd12914
first PDC (PhoQ/DcuS/CitA) domain of diguanylate-cyclase and similar domains; Members of this ...
56-173 6.92e-11

first PDC (PhoQ/DcuS/CitA) domain of diguanylate-cyclase and similar domains; Members of this subfamily display varying domain architectures but all contain double PDC (PhoQ/DcuS/CitA) sensor domains. This model represents the first PDC domain of Diguanylate-cyclases (DGCs), Histidine kinases (HKs), and other similar domains. Many members of this subfamily contain a C-terminal DGC (also called GGDEF) domain. DGCs regulate the turnover of cyclic diguanosine monophosphate. 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. In the case of HKs, 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.


Pssm-ID: 350339  Cd Length: 123  Bit Score: 60.48  E-value: 6.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722  56 EAALRQVREMLHIMAgadnMRSLDADDCSGLAKRLLSVTHDIANIGAALANGDVFCSAHP-ITRPVNVADRPWFQEALTA 134
Cdd:cd12914     5 DLLLRSLADDLEARG----AASADPAALQALLRRLLARLPEVRSIFVVDADGRVVASSGPgPAPGLDVSDRDYFQAARAG 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1308984722 135 TDITS-GHYQTGLISGKRGITIGLPVRDAEGKLQAALYLA 173
Cdd:cd12914    81 GGGLFiSEPVISRVTGKPVIPLSRPIRDADGRFAGVVVAS 120
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
397-499 3.79e-09

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: 54.95  E-value: 3.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 397 SPASIVITDINARITYVNLAFCVTSGYFPDEVIGENPRILQSGNTPPATYQAMWQTLTAGEIWRGELVNRRKDGSHYIER 476
Cdd:cd00130     1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVL 80
                          90       100
                  ....*....|....*....|...
gi 1308984722 477 ATISPVRGSDGTTSQYVAVKEDI 499
Cdd:cd00130    81 VSLTPIRDEGGEVIGLLGVVRDI 103
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
461-502 9.36e-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: 40.63  E-value: 9.36e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1308984722  461 GELVNRRKDGSHYIERATISPVRGSDGTTSQYVAVKEDISDQ 502
Cdd:smart00086   2 VEYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITER 43
 
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 ...
501-907 3.88e-98

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: 331.36  E-value: 3.88e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 501 DQRRIEEELAAHRQHLQQLVDQRTGELAQATAAAES--------------ANLAKSAFLANMSHEIRTPMNAIIGLNYLL 566
Cdd:TIGR02956 410 DERQVAQELQEHKESLEQLVAQRTQELAETNERLNAevknhakaraeaeeANRAKSAFLATMSHEIRTPLNGILGTLELL 489
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 567 LKSPLEPAQRDKLLKVTSASEHLLQVINDILDLSKIESGKLELENQTFDPREVLQAAAAVIRDQALGKGLLVGVD-GGKL 645
Cdd:TIGR02956 490 GDTGLTSQQQQYLQVINRSGESLLDILNDILDYSKIEAGHLSISPRPFDLNALLDDVHHLMVSRAQLKGIQLRLNiPEQL 569
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 646 PALAIGDAKRLRQVLINFAGNALKFTRAGSIHLSGELlaNDGENVtcRFVVSDTGLGIRPEDVPRLFKPFEQLDASttRQ 725
Cdd:TIGR02956 570 PNWWQGDGPRIRQVLINLVGNAIKFTDRGSVVLRVSL--NDDSSL--LFEVEDTGCGIAEEEQATLFDAFTQADGR--RR 643
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 726 YGGTGLGLAIARHLAHLMDGEVGVDSTPGQGSSFWITARLkaaglpPENAAGSSPALSQRLF---GRVLLVEDEPLNREI 802
Cdd:TIGR02956 644 SGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTLPL------TRGKPAEDSATLTVIDlppQRVLLVEDNEVNQMV 717
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 803 GCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRAL-PGGAAIPIVALTANAYSEDRQRCLA 881
Cdd:TIGR02956 718 AQGFLTRLGHKVTLAESGQSALECFHQHAFDLALLDINLPDGDGVTLLQQLRAIyGAKNEVKFIAFSAHVFNEDVAQYLA 797
                         410       420
                  ....*....|....*....|....*.
gi 1308984722 882 AGMNDFLAKPVDPEALYTILGKYLAG 907
Cdd:TIGR02956 798 AGFDGFLAKPVVEEQLTAMIAVILAG 823
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
541-904 7.05e-93

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 315.64  E-value: 7.05e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 541 KSAFLANMSHEIRTPMNAIIGLNYLLLKSPLEPAQRDKLLKVTSASEHLLQVINDILDLSKIESGKLELENQTFDPREVL 620
Cdd:PRK11107  293 KSEFLANMSHELRTPLNGVIGFTRQTLKTPLTPTQRDYLQTIERSANNLLAIINDILDFSKLEAGKLVLENIPFSLRETL 372
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 621 QAAAAVIRDQALGKGL--LVGVDGgKLPALAIGDAKRLRQVLINFAGNALKFTRAGSIHLSGELLANDGENVTCRFVVSD 698
Cdd:PRK11107  373 DEVVTLLAHSAHEKGLelTLNIDP-DVPDNVIGDPLRLQQIITNLVGNAIKFTESGNIDILVELRALSNTKVQLEVQIRD 451
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 699 TGLGIRPEDVPRLFKPFEQLDASTTRQYGGTGLGLAIARHLAHLMDGEVGVDSTPGQGSSFWITARLKaaglPPENAAGS 778
Cdd:PRK11107  452 TGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHLPLD----LNPNPIID 527
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 779 SPALsQRLFG-RVLLVEDEPLNREIGCDLLAATGLEVA------------------------------------------ 815
Cdd:PRK11107  528 GLPT-DCLAGkRLLYVEPNSAAAQATLDILSETPLEVTysptlsqlpeahydilllglpvtfrepltmlherlakaksmt 606
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722     --------------------------------------------------------------------------------
Cdd:PRK11107  607 dflilalpcheqvlaeqlkqdgadaclskplshtrllpallepchhkqppllpptdesrlpltvmavddnpanlkligal 686
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 816 ---------TADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALPGGAAIPIVALTANAYSEDRQRCLAAGMND 886
Cdd:PRK11107  687 leeqvehvvLCDSGHQAVEQAKQRPFDLILMDIQMPGMDGIRACELIRQLPHNQNTPIIAVTAHAMAGERERLLSAGMDD 766
                         490
                  ....*....|....*...
gi 1308984722 887 FLAKPVDPEALYTILGKY 904
Cdd:PRK11107  767 YLAKPIDEAMLKQVLLRY 784
PRK15347 PRK15347
two component system sensor kinase;
509-901 4.40e-84

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 291.16  E-value: 4.40e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 509 LAAHRQHLQQLVDQRTGELAQATAAAESANLAKSAFLANMSHEIRTPMNAIIGLNYLLLKSPLEPAQRDKLLKVTSASEH 588
Cdd:PRK15347  366 LNEQYDTLENKVAERTQALAEAKQRAEQANKRKSEHLTTISHEIRTPLNGVLGALELLQNTPLTAEQMDLADTARQCTLS 445
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 589 LLQVINDILDLSKIESGKLELENQTFDPREVLQAAAAVIRDQALGKGL----LVGVDggkLPALAIGDAKRLRQVLINFA 664
Cdd:PRK15347  446 LLAIINNLLDFSRIESGQMTLSLEETALLPLLDQAMLTIQGPAQSKSLtlrtFVGAH---VPLYLHLDSLRLRQILVNLL 522
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 665 GNALKFTRAGSIHLSGELlandgENVTCRFVVSDTGLGIRPEDVPRLFKPFEQldASTTRQygGTGLGLAIARHLAHLMD 744
Cdd:PRK15347  523 GNAVKFTETGGIRLRVKR-----HEQQLCFTVEDTGCGIDIQQQQQIFTPFYQ--ADTHSQ--GTGLGLTIASSLAKMMG 593
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 745 GEVGVDSTPGQGSSFWIT-----------------------ARLKAAGLPP----ENAAGSSPALS-------QRLFG-- 788
Cdd:PRK15347  594 GELTLFSTPGVGSCFSLVlplneyappeplkgelsaplalhRQLSAWGITCqpghQNPALLDPELAylpgrlyDLLQQii 673
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 ------------------RVLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDAT 850
Cdd:PRK15347  674 qgapnepvinlplqpwqlQILLVDDVETNRDIIGMMLVELGQQVTTAASGTEALELGRQHRFDLVLMDIRMPGLDGLETT 753
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1308984722 851 RRIRALPGG--AAIPIVALTANAYSEDRQRCLAAGMNDFLAKPVDPEALYTIL 901
Cdd:PRK15347  754 QLWRDDPNNldPDCMIVALTANAAPEEIHRCKKAGMNHYLTKPVTLAQLARAL 806
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
328-904 2.06e-77

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 269.89  E-value: 2.06e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 328 YLGDTRlpEELALLNQRFNEMISAL----GERENEHAADHQAIETLNNQLAERlaalEIAEQDLRRLSTA----VEQSPA 399
Cdd:PRK11091   93 KLEEMR--ERDLELNVQLKDNIAQLnqeiAEREKAEEARQEAFEQLKNEIKER----EETQIELEQQSSLlrsfLDASPD 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 400 SIVITDINARITYVNLAFCVTSGYFPDEVIGENPRILQSgntPPATYQAMW---------QTLTAgEIWRgELVNRRKdg 470
Cdd:PRK11091  167 LVYYRNEDGEFSGCNRAMELLTGKSEKQLIGLTPKDVYS---PEAAEKVIEtdekvfrhnVSLTY-EQWL-DYPDGRK-- 239
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 471 sHYIERATIsPVRGSDGTTSQYVAVKEDISDQRRIEEELA-AHRQhlqqlvdqrtgelaqataaaesanlaKSAFLANMS 549
Cdd:PRK11091  240 -ACFELRKV-PFYDRVGKRHGLMGFGRDITERKRYQDALEkASRD--------------------------KTTFISTIS 291
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 550 HEIRTPMNAIIGLNYLLLKSPLEPAQRDKLLKVTSASEHLLQVINDILDLSKIESGKLELENQTFDPREVLQAAAAVIRD 629
Cdd:PRK11091  292 HELRTPLNGIVGLSRILLDTELTAEQRKYLKTIHVSAITLGNIFNDIIDMDKMERRKLQLDNQPIDFTDFLADLENLSGL 371
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 630 QALGKGL-LVGVDGGKLPALAIGDAKRLRQVLINFAGNALKFTRAGSIHLSgeLLANDGENVTcrFVVSDTGLGIRPEDV 708
Cdd:PRK11091  372 QAEQKGLrFDLEPLLPLPHKVITDGTRLRQILWNLISNAVKFTQQGGVTVR--VRYEEGDMLT--FEVEDSGIGIPEDEL 447
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 709 PRLFKPFEQL-DASTTRQYGGTGLGLAIARHLAHLMDGEVGVDSTPGQGSSFWITARL----KAAGLPPENAAGSSPALs 783
Cdd:PRK11091  448 DKIFAMYYQVkDSHGGKPATGTGIGLAVSKRLAQAMGGDITVTSEEGKGSCFTLTIHApavaEEVEDAFDEDDMPLPAL- 526
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 784 qrlfgRVLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALPGGAAI- 862
Cdd:PRK11091  527 -----NILLVEDIELNVIVARSVLEKLGNSVDVAMTGKEALEMFDPDEYDLVLLDIQLPDMTGLDIARELRERYPREDLp 601
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|..
gi 1308984722 863 PIVALTANAYSeDRQRCLAAGMNDFLAKPVDPEALYTILGKY 904
Cdd:PRK11091  602 PLVALTANVLK-DKKEYLDAGMDDVLSKPLSVPALTAMIKKF 642
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
498-904 3.78e-68

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 246.04  E-value: 3.78e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 498 DISDQRRIEEELaahrQHLQQLVDQrtgelaqataaaesANLAKSAFLANMSHEIRTPMNAIIGlNYLLLKSPLEPAQRD 577
Cdd:PRK10841  422 DVSARVKMEESL----QEMAQAAEQ--------------ASQSKSMFLATVSHELRTPLYGIIG-NLDLLQTKELPKGVD 482
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 578 KLLKVTS-ASEHLLQVINDILDLSKIESGKLELENQTFDPREVLQAAAA-----VIRDQAlgkGLLVGVDGgKLPALAIG 651
Cdd:PRK10841  483 RLVTAMNnSSSLLLKIISDILDFSKIESEQLKIEPREFSPREVINHITAnylplVVKKRL---GLYCFIEP-DVPVALNG 558
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 652 DAKRLRQVLINFAGNALKFTRAGSIHLsgellandgeNVTCR-----FVVSDTGLGIRPEDVPRLFKPFEQLDASTTRQY 726
Cdd:PRK10841  559 DPMRLQQVISNLLSNAIKFTDTGCIVL----------HVRVDgdylsFRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNF 628
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 727 GGTGLGLAIARHLAHLMDGEVGVDSTPGQGSSF-------------------------WITAR-----------LKAAGL 770
Cdd:PRK10841  629 QGTGLGLAICEKLINMMDGDISVDSEPGMGSQFtiriplygaqypqkkgveglqgkrcWLAVRnasleqfletlLQRSGI 708
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 771 -----------------------------------------PPENAAG----------SSPALSQRLFG----------- 788
Cdd:PRK10841  709 qvqryegqeptpedvlitddpvqkkwqgravitfcrrhigiPLEIAPGewvhstatphELPALLARIYRielesddsana 788
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 --------------RVLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIR 854
Cdd:PRK10841  789 lpstdkavsdnddmMILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLTDVNMPNMDGYRLTQRLR 868
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 1308984722 855 ALpgGAAIPIVALTANAYSEDRQRCLAAGMNDFLAKPVDPEALYTILGKY 904
Cdd:PRK10841  869 QL--GLTLPVIGVTANALAEEKQRCLEAGMDSCLSKPVTLDVLKQTLTVY 916
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
448-762 4.91e-68

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 230.57  E-value: 4.91e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 448 AMWQTLTAGEIWRGELVNRRKDGSHYIERATISPVRGSDGTTSQYVAVKEDISDQRRIEEELAAHRQHLQQLVDQRTGEL 527
Cdd:COG0642    17 LLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLL 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 528 AQATAAAESANLAKSAFLANMSHEIRTPMNAIIGLNYLLLKSPlEPAQRDKLLKVTSASEHLLQVINDILDLSKIESGKL 607
Cdd:COG0642    97 LALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLEEL-DEEQREYLETILRSADRLLRLINDLLDLSRLEAGKL 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 608 ELENQTFDPREVLQAAAAVIRDQALGKGLLVGVDGGKLPALAIGDAKRLRQVLINFAGNALKFTRAGS-IHLSGELland 686
Cdd:COG0642   176 ELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDDLPTVRGDPDRLRQVLLNLLSNAIKYTPEGGtVTVSVRR---- 251
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1308984722 687 gENVTCRFVVSDTGLGIRPEDVPRLFKPFEQLDASttRQYGGTGLGLAIARHLAHLMDGEVGVDSTPGQGSSFWIT 762
Cdd:COG0642   252 -EGDRVRISVEDTGPGIPPEDLERIFEPFFRTDPS--RRGGGTGLGLAIVKRIVELHGGTIEVESEPGKGTTFTVT 324
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
540-762 1.25e-61

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 209.38  E-value: 1.25e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 540 AKSAFLANMSHEIRTPMNAIIGLNYLLLKSP-LEPAQRDKLLK-VTSASEHLLQVINDILDLSKIESGKLELENQTFDPR 617
Cdd:COG2205    15 LKSEFLANVSHELRTPLTSILGAAELLLDEEdLSPEERRELLEiIRESAERLLRLIEDLLDLSRLESGKLSLELEPVDLA 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 618 EVLQAAAAVIRDQALGKGLLVGVDGGKLPALAIGDAKRLRQVLINFAGNALKFTRAGS-IHLSGEllaNDGENVtcRFVV 696
Cdd:COG2205    95 ELLEEAVEELRPLAEEKGIRLELDLPPELPLVYADPELLEQVLANLLDNAIKYSPPGGtITISAR---REGDGV--RISV 169
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1308984722 697 SDTGLGIRPEDVPRLFKPFEQldASTTRQYGGTGLGLAIARHLAHLMDGEVGVDSTPGQGSSFWIT 762
Cdd:COG2205   170 SDNGPGIPEEELERIFERFYR--GDNSRGEGGTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFTVT 233
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
373-762 1.47e-61

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 214.80  E-value: 1.47e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 373 LAERLAALEIAEQDLRRLSTAVEQSPASIVITDINARITYVNLAFCVTSGYFPDEVIGENPRILQSGNTPPATYQAMWQT 452
Cdd:COG5002    29 LLLLLLLLLLLLLLLLLLLLLLLLALLLLLLLLLLLLLALLLLLLLLLLLLALALLLLALLLLLLLLLLLLALLILLLLL 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 453 LTAGEIWRGELVNRRKDGSHYIERATISPVRGSDGTTSQYVAVKEDISDQRRIEEelaahrqhlqqlvdqrtgelaqata 532
Cdd:COG5002   109 ALLILLAALLLLLSELLLLLLLLGRLSLRLSALLLGLLLLAAVERDITELERLEQ------------------------- 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 533 aaesanlAKSAFLANMSHEIRTPMNAIIGLNYLLLKSPLE-PAQRDKLLKV-TSASEHLLQVINDILDLSKIESGKLELE 610
Cdd:COG5002   164 -------MRREFVANVSHELRTPLTSIRGYLELLLDGAADdPEERREYLEIiLEEAERLSRLVNDLLDLSRLESGELKLE 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 611 NQTFDPREVLQAAAAVIRDQALGKGLLVGVDGGKLPALAIGDAKRLRQVLINFAGNALKFTRAGS-IHLSgelLANDGEN 689
Cdd:COG5002   237 KEPVDLAELLEEVVEELRPLAEEKGIELELDLPEDPLLVLGDPDRLEQVLTNLLDNAIKYTPEGGtITVS---LREEDDQ 313
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1308984722 690 VtcRFVVSDTGLGIRPEDVPRLFKPFEQLDASTTRQYGGTGLGLAIARHLAHLMDGEVGVDSTPGQGSSFWIT 762
Cdd:COG5002   314 V--RISVRDTGIGIPEEDLPRIFERFYRVDKSRSRETGGTGLGLAIVKHIVEAHGGRIWVESEPGKGTTFTIT 384
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
509-907 2.81e-61

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 225.55  E-value: 2.81e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 509 LAAHRQHLQQLVDQRTGELAQ-------ATAAAESANLAKSAFLANMSHEIRTPMNAIIGLNYLLLKSPLEPAQRDKLLK 581
Cdd:PRK11466  405 LNRHREQLAAQVKARTAELQElviehrqARAEAEKASQAKSAFLAAMSHEIRTPLYGILGTAQLLADNPALNAQRDDLRA 484
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 582 VTSASEHLLQVINDILDLSKIESG--KLELENQTFDPREVLQAAAAVIRDQALGKGLLVGVD-GGKLPALAIGDAKRLRQ 658
Cdd:PRK11466  485 ITDSGESLLTILNDILDYSAIEAGgkNVSVSDEPFEPRPLLESTLQLMSGRVKGRPIRLATDiADDLPTALMGDPRRIRQ 564
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 659 VLINFAGNALKFTRAGSIHLSGellandGENVTCRFV-VSDTGLGIRPEDVPRLFKPFEQLDAsttrQYGGTGLGLAIAR 737
Cdd:PRK11466  565 VITNLLSNALRFTDEGSIVLRS------RTDGEQWLVeVEDSGCGIDPAKLAEIFQPFVQVSG----KRGGTGLGLTISS 634
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 738 HLAHLMDGEVGVDSTPGQGSSFWITARLKAAGLPPENAAGSSPALSQRlfgRVLLVEDEPLNREIGCDLLAATGLEVATA 817
Cdd:PRK11466  635 RLAQAMGGELSATSTPEVGSCFCLRLPLRVATAPVPKTVNQAVRLDGL---RLLLIEDNPLTQRITAEMLNTSGAQVVAV 711
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 818 DDGFAAIARFQEG-GFDLILMDIQMPGLDGLDATRRI-RALPGGAAIPIVALTANAYSEDRQRCLAAGMndfLAKPVDPE 895
Cdd:PRK11466  712 GNAAQALETLQNSePFAAALVDFDLPDYDGITLARQLaQQYPSLVLIGFSAHVIDETLRQRTSSLFRGI---IPKPVPRE 788
                         410
                  ....*....|..
gi 1308984722 896 ALYTILGKYLAG 907
Cdd:PRK11466  789 VLGQLLAHYLQL 800
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
656-765 5.99e-51

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: 174.22  E-value: 5.99e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 656 LRQVLINFAGNALKFTRAGSIHLSGELLANDGENVTCRFVVSDTGLGIRPEDVPRLFKPFEQLDASTTRQYGGTGLGLAI 735
Cdd:cd16922     1 LRQILLNLLGNAIKFTEEGEVTLRVSLEEEEEDGVQLRFSVEDTGIGIPEEQQARLFEPFSQADSSTTRKYGGTGLGLAI 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 1308984722 736 ARHLAHLMDGEVGVDSTPGQGSSFWITARL 765
Cdd:cd16922    81 SKKLVELMGGDISVESEPGQGSTFTFTLPL 110
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
539-903 4.20e-50

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 193.03  E-value: 4.20e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722  539 LAKSAFLANMSHEIRTPMNAIIGLNYLLLKSPLEPAQRDKLLKVTSAS-EHLLQVINDILDLSKIESGKLELENQTFDPR 617
Cdd:PRK09959   710 VAKSQFLATMSHEIRTPISSIMGFLELLSGSGLSKEQRVEAISLAYATgQSLLGLIGEILDVDKIESGNYQLQPQWVDIP 789
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722  618 EVLQAAAAVIRDQALGKGLLVGVDGgKLPA--LAIGDAKRLRQVLINFAGNALKFTRAGSIHLSGELLANDGENVTCRFV 695
Cdd:PRK09959   790 TLVQNTCHSFGAIAASKSIALSCSS-TFPDhyLVKIDPQAFKQVLSNLLSNALKFTTEGAVKITTSLGHIDDNHAVIKMT 868
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722  696 VSDTGLGIRPEDVPRLFKPFEQldASTTRQYGGTGLGLAIARHLAHLMDGEVGVDSTPGQGSSFWITARLK-AAGLPPEN 774
Cdd:PRK09959   869 IMDSGSGLSQEEQQQLFKRYSQ--TSAGRQQTGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITIPVEiSQQVATVE 946
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722  775 AAGSSP-ALSQRLfgRVLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRI 853
Cdd:PRK09959   947 AKAEQPiTLPEKL--SILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKL 1024
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 1308984722  854 RAlpGGAAIPIVALTANAYSEDRQRCLAAGMNDFLAKPVDPEALYTILGK 903
Cdd:PRK09959  1025 RE--QNSSLPIWGLTANAQANEREKGLSCGMNLCLFKPLTLDVLKTHLSQ 1072
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
384-759 3.27e-49

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 178.50  E-value: 3.27e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 384 EQDLRRLSTAVEQSPASIVITDINARITYVNLAFCVTSGYFPDEVIGENPRILQSGNTPPAtyQAMWQTLTAGE-IWRGE 462
Cdd:COG3852     3 RESEELLRAILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFPEDSPLR--ELLERALAEGQpVTERE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 463 LVNRRKDGSHYIERATISPVRGSDGTTSqYVAVKEDISDQRRIEEELaahrQHLQQLvdQRTGELaqataaaesanlaks 542
Cdd:COG3852    81 VTLRRKDGEERPVDVSVSPLRDAEGEGG-VLLVLRDITERKRLEREL----RRAEKL--AAVGEL--------------- 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 543 afLANMSHEIRTPMNAIIGLNYLLLKSPLEPAQRDKLLKVTSASEHLLQVINDILDLSKIESGKLelenQTFDPREVLQA 622
Cdd:COG3852   139 --AAGLAHEIRNPLTGIRGAAQLLERELPDDELREYTQLIIEEADRLNNLVDRLLSFSRPRPPER----EPVNLHEVLER 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 623 AAAVIRDQAlGKGLLVGVD-GGKLPALaIGDAKRLRQVLINFAGNALK-FTRAGSIHLS-----GELLANDGENVTCRFV 695
Cdd:COG3852   213 VLELLRAEA-PKNIRIVRDyDPSLPEV-LGDPDQLIQVLLNLVRNAAEaMPEGGTITIRtrverQVTLGGLRPRLYVRIE 290
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1308984722 696 VSDTGLGIRPEDVPRLFKPFEqldasTTRQyGGTGLGLAIARHLAHLMDGEVGVDSTPGQGSSF 759
Cdd:COG3852   291 VIDNGPGIPEEILDRIFEPFF-----TTKE-KGTGLGLAIVQKIVEQHGGTIEVESEPGKGTTF 348
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
790-901 1.75e-47

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: 164.56  E-value: 1.75e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 790 VLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALPGGAA-IPIVALT 868
Cdd:cd17546     1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRELEGGGRrTPIIALT 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1308984722 869 ANAYSEDRQRCLAAGMNDFLAKPVDPEALYTIL 901
Cdd:cd17546    81 ANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
789-907 2.12e-47

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: 165.02  E-value: 2.12e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALPGGAAIPIVALT 868
Cdd:COG0784     7 RILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALPRLPDIPIIALT 86
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1308984722 869 ANAYSEDRQRCLAAGMNDFLAKPVDPEALYTILGKYLAG 907
Cdd:COG0784    87 AYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLAR 125
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
273-762 2.77e-45

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


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 171.12  E-value: 2.77e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 273 LHAIERAFMLHVLLLVTVALLSILLSRYYLYRLIERWVGQLKGATASVASGDFAVYLGDTRLPEELALLNQRFNEMISAL 352
Cdd:COG4251    21 LLLLLLVLLLALALLLLLALLVLLLLLIRLLLLLLLSLLALLLLLLLLLLLLLVLAALALLLLLLLLELALVLLALLLVL 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 353 GERENEHAADHQAIETLNNQLAERLAALEIAEQDLRRLSTAVEQSPASIVITDINARITYVNLAFCVTSGYFPDEVIGEN 432
Cdd:COG4251   101 LLLLALLLLLALLLLLELLLLLLALLLLLLLLALLLLEELALLRLALALLLLLLLLLLLLLLLLALILALLLAALAELEL 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 433 PRILQSGNTPPATYQAMWQTLTAGEIWRGELVNRRKDGSHYIERATISPVRGSDGTTSQYVAVKEDISDQRRIEEELAAH 512
Cdd:COG4251   181 LLLLLLVLLLLLLLLLLLLLLLLRLLLELLLLLEAELLLSLGGGLGLLLLLLLLLVLLLLLILLLLLLILVLELLELRLE 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 513 RQHLQQLVDQRTGELAQAtaaaesaNLAKSAFLANMSHEIRTPMNAIIGLNYLL---LKSPLEPAQRDKLLKVTSASEHL 589
Cdd:COG4251   261 LEELEEELEERTAELERS-------NEELEQFAYVASHDLREPLRKISGFSQLLeedYGDKLDEEGREYLERIRDAAERM 333
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 590 LQVINDILDLSKIesGKLELENQTFDPREVLQAAAAVIRDQALGKGLLVGVDggKLPALaIGDAKRLRQVLINFAGNALK 669
Cdd:COG4251   334 QALIDDLLAYSRV--GRQELEFEPVDLNELLEEVLEDLEPRIEERGAEIEVG--PLPTV-RGDPTLLRQVFQNLISNAIK 408
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 670 FTRAGS---IHLSGELLANDgenvtCRFVVSDTGLGIRPEDVPRLFKPFEQLDasTTRQYGGTGLGLAIARHLAHLMDGE 746
Cdd:COG4251   409 YSRPGEpprIEIGAEREGGE-----WVFSVRDNGIGIDPEYAEKIFEIFQRLH--SRDEYEGTGIGLAIVKKIVERHGGR 481
                         490
                  ....*....|....*.
gi 1308984722 747 VGVDSTPGQGSSFWIT 762
Cdd:COG4251   482 IWVESEPGEGATFYFT 497
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
294-762 7.05e-44

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: 165.14  E-value: 7.05e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 294 SILLSrYYLYRLIERWVGQLKGATASVASGDFAVYLgDTRLPEELALLNQRFNEMIsalgerenehaadhQAIETLNNQL 373
Cdd:COG5000    22 ALWLA-LLLARRLTRPLRRLAEATRAVAAGDLSVRL-PVTGDDEIGELARAFNRMT--------------DQLKEQREEL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 374 AERLAALEiaeqdlrrlsTAVEQSPASIVITDINARITYVNLAFCVTSGYFPDEVIGenpRILQSGNTPPATYQAMWQTL 453
Cdd:COG5000    86 EERRRYLE----------TILENLPAGVIVLDADGRITLANPAAERLLGIPLEELIG---KPLEELLPELDLAELLREAL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 454 TAGeiWRGELVNRRKDGSHYIERATISPVRGsdgttsqYVAVKEDISDQRRiEEELAAHRQhlqqlvdqrtgelaqataa 533
Cdd:COG5000   153 ERG--WQEEIELTRDGRRTLLVRASPLRDDG-------YVIVFDDITELLR-AERLAAWGE------------------- 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 534 aesanLAKSaflanMSHEIRTPMNAIIGLNYLLLK--SPLEPAQRDKLLKVTS----ASEHLLQVINDILDLSKIEsgkl 607
Cdd:COG5000   204 -----LARR-----IAHEIKNPLTPIQLSAERLRRklADKLEEDREDLERALDtiirQVDRLKRIVDEFLDFARLP---- 269
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 608 ELENQTFDPREVLQAAAAVIRDQALGKGLLVGVDGGKLPALAIGDAKRLRQVLINFAGNALKFTRA-GSIHLSgelLAND 686
Cdd:COG5000   270 EPQLEPVDLNELLREVLALYEPALKEKDIRLELDLDPDLPEVLADRDQLEQVLINLLKNAIEAIEEgGEIEVS---TRRE 346
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1308984722 687 GENVtcRFVVSDTGLGIRPEDVPRLFKPFEqldasTTRQyGGTGLGLAIARHLAHLMDGEVGVDSTPGQGSSFWIT 762
Cdd:COG5000   347 DGRV--RIEVSDNGPGIPEEVLERIFEPFF-----TTKP-KGTGLGLAIVKKIVEEHGGTIELESRPGGGTTFTIR 414
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
384-762 9.29e-44

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: 166.30  E-value: 9.29e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 384 EQDLR----RLSTAVEQSPASIVITDINARITYVNLAFCVTSGYFPDEVIG----ENPRILQSGNTppatYQAMWQTLTA 455
Cdd:COG5809   133 EEALReseeKFRLIFNHSPDGIIVTDLDGRIIYANPAACKLLGISIEELIGksilELIHSDDQENV----AAFISQLLKD 208
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 456 GEIWRGELVNRRKDGSHYIERATISPVrGSDGTTSQYVAVKEDISDQRRIEEELaahrQHLQQLvdQRTGELaqataaae 535
Cdd:COG5809   209 GGIAQGEVRFWTKDGRWRLLEASGAPI-KKNGEVDGIVIIFRDITERKKLEELL----RKSEKL--SVVGEL-------- 273
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 536 sanlaksafLANMSHEIRTPMNAIIGLNYLLLKSPLEpaQRDKLLKV-TSASEHLLQVINDILDLSKIESGKLElenqTF 614
Cdd:COG5809   274 ---------AAGIAHEIRNPLTSLKGFIQLLKDTIDE--EQKTYLDImLSELDRIESIISEFLVLAKPQAIKYE----PK 338
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 615 DPREVLQAAAAVIRDQALGKGLLVGVD-GGKLPALaIGDAKRLRQVLINFAGNALKFT-RAGSIHLSGELLANDGenvtC 692
Cdd:COG5809   339 DLNTLIEEVIPLLQPQALLKNVQIELElEDDIPDI-LGDENQLKQVFINLLKNAIEAMpEGGNITIETKAEDDDK----V 413
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 693 RFVVSDTGLGIRPEDVPRLFKPFeqldasTTRQYGGTGLGLAIARHLAHLMDGEVGVDSTPGQGSSFWIT 762
Cdd:COG5809   414 VISVTDEGCGIPEERLKKLGEPF------YTTKEKGTGLGLMVSYKIIEEHGGKITVESEVGKGTTFSIT 477
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
789-897 1.75e-37

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: 138.50  E-value: 1.75e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALPGGAAIPIVALT 868
Cdd:COG3706     3 RILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRADPRTADIPIIFLT 82
                          90       100
                  ....*....|....*....|....*....
gi 1308984722 869 ANAYSEDRQRCLAAGMNDFLAKPVDPEAL 897
Cdd:COG3706    83 ALDDEEDRARALEAGADDYLTKPFDPEEL 111
PAS COG2202
PAS domain [Signal transduction mechanisms];
378-522 8.71e-37

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 139.39  E-value: 8.71e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 378 AALEIAEQDLRRLSTAVEQSPASIVITDINARITYVNLAFCVTSGYFPDEVIGENPRILQSGNTPPATYQAMWQTLTAGE 457
Cdd:COG2202     1 TAEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGG 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1308984722 458 IWRGELVNRRKDGSHYIERATISPVRGSDGTTSQYVAVKEDISDQRRIEEELAAHRQHLQQLVDQ 522
Cdd:COG2202    81 VWRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEERLRLLVEN 145
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
789-903 2.72e-36

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: 132.66  E-value: 2.72e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALPGGAAIPIVALT 868
Cdd:cd17548     1 KILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKEDPATRDIPVIALT 80
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1308984722 869 ANAYSEDRQRCLAAGMNDFLAKPVDPEALYTILGK 903
Cdd:cd17548    81 AYAMKGDREKILEAGCDGYISKPIDTREFLETVAK 115
phoR_proteo TIGR02966
phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory ...
544-759 7.61e-36

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: 138.88  E-value: 7.61e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 544 FLANMSHEIRTPMNAIIGlnYL--LLKSP-LEPAQRDKLLKVTSA-SEHLLQVINDILDLSKIESGKLELENQTFDPREV 619
Cdd:TIGR02966 117 FVANVSHELRTPLTVLRG--YLetLADGPdEDPEEWNRALEIMLEqSQRMQSLVEDLLTLSRLESAASPLEDEPVDMPAL 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 620 LQAaaavIRD--QALGKGLLVGVDGGKLPALAI-GDAKRLRQVLINFAGNALKFTRAG-SIHLSGELLANDGenvtcRFV 695
Cdd:TIGR02966 195 LDH----LRDeaEALSQGKNHQITFEIDGGVDVlGDEDELRSAFSNLVSNAIKYTPEGgTITVRWRRDGGGA-----EFS 265
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1308984722 696 VSDTGLGIRPEDVPRLFKPFEQLDASTTRQYGGTGLGLAIARHLAHLMDGEVGVDSTPGQGSSF 759
Cdd:TIGR02966 266 VTDTGIGIAPEHLPRLTERFYRVDKSRSRDTGGTGLGLAIVKHVLSRHHARLEIESELGKGSTF 329
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
790-901 1.70e-33

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: 124.57  E-value: 1.70e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 790 VLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALPGGaaIPIVALTA 869
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDPT--TPVIILTA 78
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1308984722 870 NAYSEDRQRCLAAGMNDFLAKPVDPEALYTIL 901
Cdd:pfam00072  79 HGDEDDAVEALEAGADDFLSKPFDPDELLAAI 110
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
789-897 2.42e-33

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: 127.76  E-value: 2.42e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALPggAAIPIVALT 868
Cdd:COG0745     3 RILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRARP--SDIPIIMLT 80
                          90       100
                  ....*....|....*....|....*....
gi 1308984722 869 ANAYSEDRQRCLAAGMNDFLAKPVDPEAL 897
Cdd:COG0745    81 ARDDEEDRVRGLEAGADDYLTKPFDPEEL 109
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
789-906 3.15e-33

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: 127.97  E-value: 3.15e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALPGGAAIPIVALT 868
Cdd:COG3437     8 TVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPSTRDIPVIFLT 87
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1308984722 869 ANAYSEDRQRCLAAGMNDFLAKPVDPEALYTILGKYLA 906
Cdd:COG3437    88 ALADPEDRERALEAGADDYLTKPFDPEELLARVRNALE 125
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
790-901 1.53e-31

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: 119.10  E-value: 1.53e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 790 VLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALPGGAAIPIVALTA 869
Cdd:cd17580     1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPWLANTPAIALTG 80
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1308984722 870 NAYSEDRQRCLAAGMNDFLAKPVDPEALYTIL 901
Cdd:cd17580    81 YGQPEDRERALEAGFDAHLVKPVDPDELIELI 112
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
651-766 1.96e-31

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 118.91  E-value: 1.96e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722  651 GDAKRLRQVLINFAGNALKFTRA-GSIHLSgelLANDGENVtcRFVVSDTGLGIRPEDVPRLFKPFEQLDaSTTRQYGGT 729
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIKYTPEgGRITVT---LERDGDHV--EITVEDNGPGIPPEDLEKIFEPFFRTD-KRSRKIGGT 74
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1308984722  730 GLGLAIARHLAHLMDGEVGVDSTPGQGSSFWITARLK 766
Cdd:smart00387  75 GLGLSIVKKLVELHGGEISVESEPGGGTTFTITLPLE 111
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
494-762 2.54e-30

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 123.76  E-value: 2.54e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 494 AVKEDISDQRRIEEELAAHRQHLQQLvdQRT---GELaqataaaesanlaksafLANMSHEIRTPMNAIIGLNYLL---L 567
Cdd:COG4191   111 ELERDITELERAEEELRELQEQLVQS--EKLaalGEL-----------------AAGIAHEINNPLAAILGNAELLrrrL 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 568 KSPLEPAQRDKLL-KVTSASEHLLQVINDILDLSKIESGKLElenqTFDPREVLQAAAAVIRDQALGKGLLVGVDGGKLP 646
Cdd:COG4191   172 EDEPDPEELREALeRILEGAERAAEIVRSLRAFSRRDEEERE----PVDLNELIDEALELLRPRLKARGIEVELDLPPDL 247
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 647 ALAIGDAKRLRQVLINFAGN---ALKFTRAGSIHLSgelLANDGENVtcRFVVSDTGLGIRPEDVPRLFKPFeqldaSTT 723
Cdd:COG4191   248 PPVLGDPGQLEQVLLNLLINaidAMEEGEGGRITIS---TRREGDYV--VISVRDNGPGIPPEVLERIFEPF-----FTT 317
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1308984722 724 RQYG-GTGLGLAIARHLAHLMDGEVGVDSTPGQGSSFWIT 762
Cdd:COG4191   318 KPVGkGTGLGLSISYGIVEKHGGRIEVESEPGGGTTFTIT 357
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
359-762 4.89e-30

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: 125.61  E-value: 4.89e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 359 HAADHQAIETLNNqLAERLAALEIAEQDLRRLSTAVEQSPASIVITDINARITYVNLAFCVTSGYFPDEVIGENPRILQS 438
Cdd:COG5805   129 NQNGQAAILALRD-ITKKKKIEEILQEQEERLQTLIENSPDLICVIDTDGRILFINESIERLFGAPREELIGKNLLELLH 207
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 439 GNTPPATYQAMWQTLTAGEiwRGELVNRR--KDGSHYIERATISPVRGSDGTTSQYVAVKEDISDQRRIEEELAahrqHL 516
Cdd:COG5805   208 PCDKEEFKERIESITEVWQ--EFIIEREIitKDGRIRYFEAVIVPLIDTDGSVKGILVILRDITEKKEAEELMA----RS 281
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 517 QQLvdQRTGELAqataaaesanlaksaflANMSHEIRTPMNAIIGLNYLLlksPLEPAQRDKLLKV-TSASEHLLQVIND 595
Cdd:COG5805   282 EKL--SIAGQLA-----------------AGIAHEIRNPLTSIKGFLQLL---QPGIEDKEEYFDImLSELDRIESIISE 339
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 596 ILDLSKIESGKLELENQTfdprEVLQAAAAVIRDQALGKGLLVGVDG-GKLPALaIGDAKRLRQVLINFAGNALK-FTRA 673
Cdd:COG5805   340 FLALAKPQAVNKEKENIN----ELIQDVVTLLETEAILHNIQIRLELlDEDPFI-YCDENQIKQVFINLIKNAIEaMPNG 414
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 674 GSIHLSGELlandgENVTCRFVVSDTGLGIRPEDVPRLFKPFeqldaSTTRQyGGTGLGLA-----IARHlahlmDGEVG 748
Cdd:COG5805   415 GTITIHTEE-----EDNSVIIRVIDEGIGIPEERLKKLGEPF-----FTTKE-KGTGLGLMvsykiIENH-----NGTID 478
                         410
                  ....*....|....
gi 1308984722 749 VDSTPGQGSSFWIT 762
Cdd:COG5805   479 IDSKVGKGTTFTIT 492
nifL_nitrog TIGR02938
nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation ...
393-521 8.25e-30

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: 124.63  E-value: 8.25e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 393 AVEQSPASIVITDINARITYVNLAFCVTSGYFPDEVIGENPRILQSGNTPPATYQAMWQTLTAGEIWRGELVNRRKDGSH 472
Cdd:TIGR02938   9 TVDQAPLAISITDLKANILYANDAFTRITGYTKEEIIGKNESVLSNHTTPPEVYQALWGSLAEQKPWAGKLLNRRKDGEL 88
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1308984722 473 YIERATISPVRGSDGTTSQYVAVKEDISDQRRIEEELAAHRQHLQQLVD 521
Cdd:TIGR02938  89 YLAELTVAPVLNEAGETTHFLGMHRDITELHRLEQVVANQKLLIESVVD 137
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
789-894 2.08e-29

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: 113.31  E-value: 2.08e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDEPLNREIGCDLLA-ATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALPGGAAIPIVAL 867
Cdd:cd17551     2 RILIVDDNPTNLLLLEALLRsAGYLEVVSFTDPREALAWCRENPPDLILLDYMMPGMDGLEFIRRLRALPGLEDVPIVMI 81
                          90       100
                  ....*....|....*....|....*..
gi 1308984722 868 TANAYSEDRQRCLAAGMNDFLAKPVDP 894
Cdd:cd17551    82 TADTDREVRLRALEAGATDFLTKPFDP 108
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
789-892 3.74e-29

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: 111.82  E-value: 3.74e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALPGGAAIPIVALT 868
Cdd:cd17538     1 KILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKEDPETRHIPVIMIT 80
                          90       100
                  ....*....|....*....|....
gi 1308984722 869 ANAYSEDRQRCLAAGMNDFLAKPV 892
Cdd:cd17538    81 ALDDREDRIRGLEAGADDFLSKPI 104
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
651-766 5.79e-27

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: 105.91  E-value: 5.79e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 651 GDAKRLRQVLINFAGNALKFTRAGSihlSGELLANDGENVtcRFVVSDTGLGIRPEDVPRLFKPFEQLDastTRQYGGTG 730
Cdd:pfam02518   1 GDELRLRQVLSNLLDNALKHAAKAG---EITVTLSEGGEL--TLTVEDNGIGIPPEDLPRIFEPFSTAD---KRGGGGTG 72
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1308984722 731 LGLAIARHLAHLMDGEVGVDSTPGQGSSFWITARLK 766
Cdd:pfam02518  73 LGLSIVRKLVELLGGTITVESEPGGGTTVTLTLPLA 108
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
791-891 6.40e-27

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: 105.39  E-value: 6.40e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 791 LLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALPggAAIPIVALTAN 870
Cdd:cd00156     1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELP--PDIPVIVLTAK 78
                          90       100
                  ....*....|....*....|.
gi 1308984722 871 AYSEDRQRCLAAGMNDFLAKP 891
Cdd:cd00156    79 ADEEDAVRALELGADDYLVKP 99
HK_WalK NF033092
cell wall metabolism sensor histidine kinase WalK; This model describes WalK as found in ...
463-762 7.34e-27

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: 116.78  E-value: 7.34e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 463 LVNRRKDGSHYIERATISPVRGSDGTTSQYVAVKEDISDQRRIEEElaaHRQhlqqlvdqrtgelaqataaaesanlaks 542
Cdd:NF033092  326 LLDFSTEEEPLILRANFSVIQRESGFINGLIAVLHDVTEQEKIEQE---RRE---------------------------- 374
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 543 aFLANMSHEIRTPMNAIiglnylllKSPLEP----AQRD-----KLLKVT-SASEHLLQVINDILDLSKIESGKLELENQ 612
Cdd:NF033092  375 -FVANVSHELRTPLTTM--------RSYLEAladgAWKDpelapRFLGVTqNETERMIRLVNDLLQLSRMDSKDYKLNKE 445
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 613 TFDPREVLQAAA------------AVIRDqaLGKGLL-VGVDGGKlpalaigdakrLRQVLINFAGNALKFTRagsihls 679
Cdd:NF033092  446 WVNFNEFFNYIIdrfemilknkniTFKRE--FPKRDLwVEIDTDK-----------ITQVLDNIISNAIKYSP------- 505
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 680 gellanDGENVTCR---------FVVSDTGLGIRPEDVPRLFKPFEQLDASTTRQYGGTGLGLAIARHLAHLMDGEVGVD 750
Cdd:NF033092  506 ------EGGTITFRllethnriiISISDQGLGIPKKDLDKIFDRFYRVDKARSRKMGGTGLGLAIAKEVVEAHGGRIWAE 579
                         330
                  ....*....|..
gi 1308984722 751 STPGQGSSFWIT 762
Cdd:NF033092  580 SEEGKGTTIYFT 591
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
791-891 7.52e-27

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: 105.18  E-value: 7.52e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 791 LLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALPggAAIPIVALTAN 870
Cdd:cd17574     1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREKG--SDIPIIMLTAK 78
                          90       100
                  ....*....|....*....|.
gi 1308984722 871 AYSEDRQRCLAAGMNDFLAKP 891
Cdd:cd17574    79 DEEEDKVLGLELGADDYITKP 99
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
543-903 1.01e-26

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 117.47  E-value: 1.01e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 543 AFLANMSHEIRTPMNAIIGLNYLLL-KSPLEPAQRDKLLKVTSASEHLLQVINDILDLSKiesgKLELENQTFDPREVLQ 621
Cdd:PRK13837  452 TLASGIAHNFNNILGAILGYAEMALnKLARHSRAARYIDEIISAGARARLIIDQILAFGR----KGERNTKPFDLSELVT 527
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 622 AAAAVIRdQALGKGLLVGVDGGKLPALAIGDAKRLRQVLINFAGNALKFTRAGS--------IHLSGELLANDGENVTCR 693
Cdd:PRK13837  528 EIAPLLR-VSLPPGVELDFDQDQEPAVVEGNPAELQQVLMNLCSNAAQAMDGAGrvdislsrAKLRAPKVLSHGVLPPGR 606
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 694 FV---VSDTGLGIRPEDVPRLFKPFeqldaSTTRQyGGTGLGLAIARHLAHLMDGEVGVDSTPGQGSSF--WITARLKAA 768
Cdd:PRK13837  607 YVllrVSDTGAGIDEAVLPHIFEPF-----FTTRA-GGTGLGLATVHGIVSAHAGYIDVQSTVGRGTRFdvYLPPSSKVP 680
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 769 GLPpeNAAGSSPALSQRLFGRVLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGG--FDLILmdIQMPGLDG 846
Cdd:PRK13837  681 VAP--QAFFGPGPLPRGRGETVLLVEPDDATLERYEEKLAALGYEPVGFSTLAAAIAWISKGPerFDLVL--VDDRLLDE 756
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1308984722 847 LDAtrrIRALPGGAAIPIVALTANAYSEDRQRCLAAGMNDFLAKPVDPEAL-YTILGK 903
Cdd:PRK13837  757 EQA---AAALHAAAPTLPIILGGNSKTMALSPDLLASVAEILAKPISSRTLaYALRTA 811
phoR PRK11006
phosphate regulon sensor histidine kinase PhoR;
540-765 1.89e-26

phosphate regulon sensor histidine kinase PhoR;


Pssm-ID: 182895 [Multi-domain]  Cd Length: 430  Bit Score: 113.57  E-value: 1.89e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 540 AKSAFLANMSHEIRTPMNAIIGLNYLLLKSPLEPAQRDKLLKVTSASEHLLQ-VINDILDLSKIESGKLELENQTFD-PR 617
Cdd:PRK11006  203 ARRNFFANVSHELRTPLTVLQGYLEMMQDQPLEGALREKALHTMREQTQRMEgLVKQLLTLSKIEAAPTIDLNEKVDvPM 282
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 618 --EVLQAAAavirdQALGKG---LLVGVDggklPALAI-GDAKRLRQVLINFAGNALKFTRAGS-IHLSGELLANDGEnv 690
Cdd:PRK11006  283 mlRVLEREA-----QTLSQGkhtITFEVD----NSLKVfGNEDQLRSAISNLVYNAVNHTPEGThITVRWQRVPQGAE-- 351
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1308984722 691 tcrFVVSDTGLGIRPEDVPRLFKPFEQLDASTTRQYGGTGLGLAIARHLAHLMDGEVGVDSTPGQGS--SFWITARL 765
Cdd:PRK11006  352 ---FSVEDNGPGIAPEHIPRLTERFYRVDKARSRQTGGSGLGLAIVKHALSHHDSRLEIESEVGKGTrfSFVLPERL 425
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
544-762 4.08e-26

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 113.58  E-value: 4.08e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 544 FLANMSHEIRTPMNAIiglnylLLKSPLEPAQRDKLLKVTSASEHLLQ--------VINDILDLSKIESGKLELENQTFD 615
Cdd:NF040691  274 FVSDVSHELRTPLTTI------RMAADVIHDSRDDFDPATARSAELLHteldrfesLLSDLLEISRFDAGAAELDVEPVD 347
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 616 PREVLQAAAAVIRDQALGKGLLVGVDGGKLPALAIGDAKRLRQVLINFAGNALKFTRAGSIHLSgelLANDGENVTcrFV 695
Cdd:NF040691  348 LRPLVRRVVDALRQLAERAGVELRVDAPGTPVVAEVDPRRVERVLRNLVVNAIEHGEGKPVVVT---VAQDDTAVA--VT 422
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1308984722 696 VSDTGLGIRPEDVPRLFKPFEQLDASTTRQYGGTGLGLAIARHLAHLMDGEVGVDSTPGQGSSFWIT 762
Cdd:NF040691  423 VRDHGVGLKPGEVALVFDRFWRADPARARTTGGTGLGLAIALEDARLHGGWLEAWGRPGQGSQFRLT 489
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
788-906 1.37e-24

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: 107.74  E-value: 1.37e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 788 GRVLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALpgGAAIPIVAL 867
Cdd:COG2204     3 ARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRAL--DPDLPVILL 80
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1308984722 868 TANAYSEDRQRCLAAGMNDFLAKPVDPEALYTILGKYLA 906
Cdd:COG2204    81 TGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALE 119
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
789-891 4.41e-24

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: 97.54  E-value: 4.41e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDEPLNREIGCDLL-AATGLE-VATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALpgGAAIPIVA 866
Cdd:COG4753     1 KVLIVDDEPLIREGLKRILeWEAGFEvVGEAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIREL--DPDTKIII 78
                          90       100
                  ....*....|....*....|....*
gi 1308984722 867 LTANAYSEDRQRCLAAGMNDFLAKP 891
Cdd:COG4753    79 LSGYSDFEYAQEAIKLGADDYLLKP 103
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
790-892 1.65e-23

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: 96.04  E-value: 1.65e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 790 VLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALPGGAAIPIVALTA 869
Cdd:cd19920     1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLKADPATRHIPVIFLTA 80
                          90       100
                  ....*....|....*....|...
gi 1308984722 870 NAYSEDRQRCLAAGMNDFLAKPV 892
Cdd:cd19920    81 LTDTEDKVKGFELGAVDYITKPF 103
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
541-762 3.09e-23

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 104.14  E-value: 3.09e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 541 KSAFLANMSHEIRTPMnAIIGLNYLLLKSPLEPAQRDKLLKVTSASEHLLQVINDILDLSKIESGKLELENQTFDPREVL 620
Cdd:NF012163  240 RRDFMADISHELRTPL-AVLRAELEAIQDGIRKFTPESLDSLQAEVGTLTKLVDDLHDLSMSDEGALAYQKASVDLVPLL 318
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 621 QAAAAVIRDQALGKGLLVGVDGGKLPaLAIGDAKRLRQVLINFAGNALKFTRA-GSIHLSGELLANdgenvTCRFVVSDT 699
Cdd:NF012163  319 EVEGGAFRERFASAGLELEVSLPDSS-LVFGDRDRLMQLFNNLLENSLRYTDSgGSLHISASQRPK-----EVTLTVADS 392
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1308984722 700 GLGIRPEDVPRLFKPFEQLDASTTRQYGGTGLGLAIARHLAHLMDGEVGVDSTPGQGSSFWIT 762
Cdd:NF012163  393 APGVSDEQLARLFERFYRVEVSRNRASGGSGLGLAISLNIVQAHGGTLHAAHSPLGGLRIVVT 455
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
371-759 3.32e-23

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 105.44  E-value: 3.32e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 371 NQLAERLaaleiaeQDLRRLSTAVEQSPASIVIT-DINARITYVNLAFCVTSGYFPDEVIGENPRILQSGNTPPATYqaM 449
Cdd:PRK11360  251 NNLAQAL-------RETRSLNELILESIADGVIAiDRQGKITTMNPAAEVITGLQRHELVGKPYSELFPPNTPFASP--L 321
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 450 WQTLTAGEIWRGELVNRRKDGSHYIERATISPVRGSDGTTSQYVAVKEDISDQRRIEEELaaHRQ-HLQQLvdqrtGELa 528
Cdd:PRK11360  322 LDTLEHGTEHVDLEISFPGRDRTIELSVSTSLLHNTHGEMIGALVIFSDLTERKRLQRRV--ARQeRLAAL-----GEL- 393
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 529 qataaaesanlaksafLANMSHEIRTPMNAIIGLNYLLLKSPLEPAQRDKLLKVTSASEHLLQVINDILDLSKiesgKLE 608
Cdd:PRK11360  394 ----------------VAGVAHEIRNPLTAIRGYVQIWRQQTSDPPSQEYLSVVLREVDRLNKVIDQLLEFSR----PRE 453
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 609 LENQTFDPREVLQAAAAVIRDQALGKGLLVGVD-GGKLPALAIgDAKRLRQVLINFAGNALK-FTRAGSIHLSGELLAND 686
Cdd:PRK11360  454 SQWQPVSLNALVEEVLQLFQTAGVQARVDFETElDNELPPIWA-DPELLKQVLLNILINAVQaISARGKIRIRTWQYSDG 532
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1308984722 687 GENVTcrfvVSDTGLGIRPEDVPRLFKPFeqldaSTTRQyGGTGLGLAIARHLAHLMDGEVGVDSTPGQGSSF 759
Cdd:PRK11360  533 QVAVS----IEDNGCGIDPELLKKIFDPF-----FTTKA-KGTGLGLALSQRIINAHGGDIEVESEPGVGTTF 595
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
789-906 3.92e-23

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 96.19  E-value: 3.92e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDEPLNREIGCDLLAATGL--EVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALpgGAAIPIVA 866
Cdd:COG4565     5 RVLIVEDDPMVAELLRRYLERLPGfeVVGVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRAR--GPDVDVIV 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1308984722 867 LTANAYSEDRQRCLAAGMNDFLAKPVDPEALYTILGKYLA 906
Cdd:COG4565    83 ITAARDPETVREALRAGVVDYLIKPFTFERLREALERYLE 122
PRK13558 PRK13558
bacterio-opsin activator; Provisional
345-525 6.82e-23

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 104.92  E-value: 6.82e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 345 FNEMISALGERENEHAADHQAIETLNNqlaerlaalEIAEQDLRRLSTAVEQSPASIVITDINAR---ITYVNLAFCVTS 421
Cdd:PRK13558  114 TAAIAERIESAVPEHSRDTEARMPISD---------LTVESDRRLKERALDEAPVGITIADATLPdepLIYINDAFERIT 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 422 GYFPDEVIGENPRILQSGNTPPATYQAMWQTLTAGEIWRGELVNRRKDGSHYIERATISPVRGSDGTTSQYVAVKEDISD 501
Cdd:PRK13558  185 GYSPDEVLGRNCRFLQGEDTNEERVAELREAIDEERPTSVELRNYRKDGSTFWNQVDIAPIRDEDGTVTHYVGFQTDVTE 264
                         170       180
                  ....*....|....*....|....
gi 1308984722 502 QRRIEEELAAHRQHLQQLVDQRTG 525
Cdd:PRK13558  265 RKEAELALQRERRKLQRLLERVEG 288
cztS_silS_copS TIGR01386
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...
542-762 2.07e-22

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: 101.70  E-value: 2.07e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 542 SAFLANMSHEIRTPMNAIIGLNYLLLKSPLE-PAQRDKLLKVTSASEHLLQVINDILDLSKIESGKLELENQTFDprevL 620
Cdd:TIGR01386 242 SQFSADLAHELRTPLTNLLGQTQVALSQPRTgEEYREVLESNLEELERLSRMVSDMLFLARADNGQLALERVRLD----L 317
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 621 QAAAAVIRD--QALG--KGLLVGVDGGklpALAIGDAKRLRQVLINFAGNALKFTRAGS-IHLSGELLANDgenvtCRFV 695
Cdd:TIGR01386 318 AAELAKVAEyfEPLAeeRGVRIRVEGE---GLVRGDPQMFRRAISNLLSNALRHTPDGGtITVRIERRSDE-----VRVS 389
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1308984722 696 VSDTGLGIRPEDVPRLFKPFEQLDASTTRQYGGTGLGLAIARHLAHLMDGEVGVDStPGQGSSFWIT 762
Cdd:TIGR01386 390 VSNPGPGIPPEHLSRLFDRFYRVDPARSNSGEGTGLGLAIVRSIMEAHGGRASAES-PDGKTRFILR 455
PRK13557 PRK13557
histidine kinase; Provisional
375-891 1.33e-21

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 100.13  E-value: 1.33e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 375 ERLAALEIAEQDLRRLSTAVEQSPASIVITDINAR---ITYVNLAFCVTSGYFPDEVIGENPRILQSGNTPPATYQAMWQ 451
Cdd:PRK13557   17 DESAAGDVSDHRSDIFFAAVETTRMPMIVTDPNQPdnpIVFANRAFLEMTGYAAEEIIGNNCRFLQGPETDRATVAEVRD 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 452 TLTAGEIWRGELVNRRKDGSHYIERATISPVRGSDGTTSQYVAVKEDISDQRRIEEELaaHRQHLQQLVDQRTGelaqat 531
Cdd:PRK13557   97 AIAERREIATEILNYRKDGSSFWNALFVSPVYNDAGDLVYFFGSQLDVSRRRDAEDAL--RQAQKMEALGQLTG------ 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 532 aaaesanlaksaflaNMSHEIrtpmnaiiglnylllksplepaqrdkllkvtsasEHLLQVINDILDLskIESGkleLEN 611
Cdd:PRK13557  169 ---------------GIAHDF----------------------------------NNLLQVMSGYLDV--IQAA---LSH 194
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 612 QTFDP----REVLQAAAAVIRDQALGKGLL------------VGVDG-----GKLPALAIGDAKRLRQVLinfaGNALKF 670
Cdd:PRK13557  195 PDADRgrmaRSVENIRAAAERAATLTQQLLafarkqrlegrvLNLNGlvsgmGELAERTLGDAVTIETDL----APDLWN 270
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 671 TRAGSIHLSGELL-----AND----GENVTC---------------------RFV---VSDTGLGIRPEDVPRLFKPFeq 717
Cdd:PRK13557  271 CRIDPTQAEVALLnvlinARDampeGGRVTIrtrnveiededlamyhglppgRYVsiaVTDTGSGMPPEILARVMDPF-- 348
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 718 ldaSTTRQYG-GTGLGLAIARHLAHLMDGEVGVDSTPGQGSsfwiTARLK-AAGLPPENAAGSSPALSQRLFG--RVLLV 793
Cdd:PRK13557  349 ---FTTKEEGkGTGLGLSMVYGFAKQSGGAVRIYSEVGEGT----TVRLYfPASDQAENPEQEPKARAIDRGGteTILIV 421
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 794 EDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGG-FDLILMDIQMPG-LDGLDATRRIR-ALPGgaaipIVALTAN 870
Cdd:PRK13557  422 DDRPDVAELARMILEDFGYRTLVASNGREALEILDSHPeVDLLFTDLIMPGgMNGVMLAREARrRQPK-----IKVLLTT 496
                         570       580
                  ....*....|....*....|...
gi 1308984722 871 AYSEDR-QRCLAAGMN-DFLAKP 891
Cdd:PRK13557  497 GYAEASiERTDAGGSEfDILNKP 519
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
790-897 1.44e-21

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: 90.65  E-value: 1.44e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 790 VLLVEDEPLNRE-IGCDLLAATGLE-VATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALPGGAaiPIVAL 867
Cdd:cd17535     1 VLIVDDHPLVREgLRRLLESEPDIEvVGEAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRRRYPDL--KVIVL 78
                          90       100       110
                  ....*....|....*....|....*....|
gi 1308984722 868 TANAYSEDRQRCLAAGMNDFLAKPVDPEAL 897
Cdd:cd17535    79 TAHDDPEYVLRALKAGAAGYLLKDSSPEEL 108
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
789-897 1.11e-20

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: 88.46  E-value: 1.11e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALPGGAAIPIVALT 868
Cdd:cd17618     2 TILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKRDEMTRDIPIIMLT 81
                          90       100
                  ....*....|....*....|....*....
gi 1308984722 869 ANAYSEDRQRCLAAGMNDFLAKPVDPEAL 897
Cdd:cd17618    82 ARGEEEDKVRGLEAGADDYITKPFSPREL 110
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
789-897 2.15e-20

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: 87.45  E-value: 2.15e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQ--EGGFDLILMDIQMPGLDGLDATRRIRALPGGAAIP-IV 865
Cdd:cd19933     2 KVLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLLAsaEHSFQLVLLDLCMPEMDGFEVALRIRKLFGRRERPlIV 81
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1308984722 866 ALTANAYSEDRQRCLAAGMNDFLAKPVDPEAL 897
Cdd:cd19933    82 ALTANTDDSTREKCLSLGMNGVITKPVSLHAL 113
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
789-897 9.43e-20

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


Pssm-ID: 381108 [Multi-domain]  Cd Length: 129  Bit Score: 85.93  E-value: 9.43e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDEPLNREIGCDLLAATGL--EVATADDGFAAIAR-FQEGGF------DLILMDIQMPGLDGLDATRRIRALPGG 859
Cdd:cd17557     1 TILLVEDNPGDAELIQEAFKEAGVpnELHVVRDGEEALDFlRGEGEYadaprpDLILLDLNMPRMDGFEVLREIKADPDL 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1308984722 860 AAIPIVALTANAYSEDRQRCLAAGMNDFLAKPVDPEAL 897
Cdd:cd17557    81 RRIPVVVLTTSDAEEDIERAYELGANSYIVKPVDFEEF 118
PRK09303 PRK09303
histidine kinase;
545-762 9.49e-20

histidine kinase;


Pssm-ID: 236462 [Multi-domain]  Cd Length: 380  Bit Score: 92.32  E-value: 9.49e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 545 LANMSHEIRTPMNAI------IGLNYLLLKSPLEPAQRDKLLKVTSASehlLQVIN----DILDLSKIESGKLELENQTF 614
Cdd:PRK09303  155 LAMLAHDLRTPLTAAslaletLELGQIDEDTELKPALIEQLQDQARRQ---LEEIErlitDLLEVGRTRWEALRFNPQKL 231
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 615 DPREVLQAAAAVIRDQALGKGLLVGVD-GGKLPaLAIGDAKRLRQVLINFAGNALKFTRA-GSIHLSGelLANDGENVtc 692
Cdd:PRK09303  232 DLGSLCQEVILELEKRWLAKSLEIQTDiPSDLP-SVYADQERIRQVLLNLLDNAIKYTPEgGTITLSM--LHRTTQKV-- 306
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1308984722 693 RFVVSDTGLGIRPEDVPRLFKPFEQL--DASTTrqygGTGLGLAIARHLAHLMDGEVGVDSTPGQGSSFWIT 762
Cdd:PRK09303  307 QVSICDTGPGIPEEEQERIFEDRVRLprDEGTE----GYGIGLSVCRRIVRVHYGQIWVDSEPGQGSCFHFT 374
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
789-901 1.66e-19

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: 87.32  E-value: 1.66e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDEPLNREIGCDLLAATGLEV-ATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALPggaAIPIVAL 867
Cdd:COG3707     5 RVLVVDDEPLRRADLREGLREAGYEVvAEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQISEER---PAPVILL 81
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1308984722 868 TANAYSEDRQRCLAAGMNDFLAKPVDPEALYTIL 901
Cdd:COG3707    82 TAYSDPELIERALEAGVSAYLVKPLDPEDLLPAL 115
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
789-905 1.67e-19

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


Pssm-ID: 381110 [Multi-domain]  Cd Length: 118  Bit Score: 85.04  E-value: 1.67e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALPGGAAIPIVALT 868
Cdd:cd17562     2 KILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKELRKLPAYKFTPILMLT 81
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1308984722 869 ANAYSEDRQRCLAAGMNDFLAKPVDPEALYTILGKYL 905
Cdd:cd17562    82 TESSDEKKQEGKAAGATGWLVKPFDPEQLLEVVKKVL 118
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
790-903 5.76e-19

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: 83.54  E-value: 5.76e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 790 VLLVEDEPLNRE----------IGCDLlaatgleVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALpgG 859
Cdd:cd17536     1 VLIVDDEPLIREglkklidweeLGFEV-------VGEAENGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIREL--Y 71
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1308984722 860 AAIPIVALTanAYSEDR--QRCLAAGMNDFLAKPVDPEALYTILGK 903
Cdd:cd17536    72 PDIKIIILS--GYDDFEyaQKAIRLGVVDYLLKPVDEEELEEALEK 115
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
387-509 7.02e-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: 83.49  E-value: 7.02e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 387 LRRLSTAVEQSPASIVITDINARITYVNLAFCVTSGYFPDEVIGENPRILQSGNTPPATYQAMWQTLTAGEIWRGELVN- 465
Cdd:TIGR00229   2 EERYRAIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEPEPVSEERRv 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1308984722 466 RRKDGSHYIERATISPVRgSDGTTSQYVAVKEDISDQRRIEEEL 509
Cdd:TIGR00229  82 RRKDGSEIWVEVSVSPIR-TNGGELGVVGIVRDITERKEAEEAL 124
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
789-909 8.68e-19

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 86.41  E-value: 8.68e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDEPLNREIGCDLLAAT-GLE-VATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALPggAAIPIVA 866
Cdd:COG3279     3 KILIVDDEPLARERLERLLEKYpDLEvVGEASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRELD--PPPPIIF 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1308984722 867 LTA------NAYSEDrqrclAAgmnDFLAKPVDPEALYTILGKYLAGIA 909
Cdd:COG3279    81 TTAydeyalEAFEVN-----AV---DYLLKPIDEERLAKALEKAKERLE 121
PRK10549 PRK10549
two-component system sensor histidine kinase BaeS;
543-765 1.25e-18

two-component system sensor histidine kinase BaeS;


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 90.08  E-value: 1.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 543 AFLANMSHEIRTPMnAIiglnyllLKSPLEPAQrDKLLKVTSASEHLLQ--------VINDILDLSKIESGKLELENQTF 614
Cdd:PRK10549  242 DFMADISHELRTPL-AV-------LRGELEAIQ-DGVRKFTPESVASLQaevgtltkLVDDLHQLSLSDEGALAYRKTPV 312
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 615 DPREVLQAAAAVIRDQALGKGLLVGVDggkLP--ALAIGDAKRLRQVLINFAGNALKFTRA-GSIHLSGELlanDGENVT 691
Cdd:PRK10549  313 DLVPLLEVAGGAFRERFASRGLTLQLS---LPdsATVFGDPDRLMQLFNNLLENSLRYTDSgGSLHISAEQ---RDKTLR 386
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1308984722 692 CRFvvSDTGLGIRPEDVPRLFKPFEQLDASTTRQYGGTGLGLAIARHLAHLMDGEVGVDSTPGQGSSfwITARL 765
Cdd:PRK10549  387 LTF--ADSAPGVSDEQLQKLFERFYRTEGSRNRASGGSGLGLAICLNIVEAHNGRIIAAHSPFGGVS--ITVEL 456
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
789-905 3.42e-18

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: 81.23  E-value: 3.42e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDEPLNREIGCDLLAATGLE-VATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALPGGAAIPIVAL 867
Cdd:cd19923     2 KVLVVDDFSTMRRIIKNLLKELGFNnVEEAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIRADGALSHLPVLMV 81
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1308984722 868 TANAYSEDRQRCLAAGMNDFLAKPVDPEALYTILGKYL 905
Cdd:cd19923    82 TAEAKKENVIAAAQAGVNNYIVKPFTAATLKEKLEKIF 119
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
789-877 4.62e-18

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: 80.73  E-value: 4.62e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALpgGAAIPIVALT 868
Cdd:cd17554     2 KILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIREK--KPDLPVIICT 79

                  ....*....
gi 1308984722 869 anAYSEDRQ 877
Cdd:cd17554    80 --AYSEYKS 86
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
789-891 5.56e-18

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: 80.90  E-value: 5.56e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDEPLNREIGCDLLAAT-GLEV-ATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALpggAAIPIVA 866
Cdd:cd17541     2 RVLIVDDSAVMRKLLSRILESDpDIEVvGTARDGEEALEKIKELKPDVITLDIEMPVMDGLEALRRIMAE---RPTPVVM 78
                          90       100
                  ....*....|....*....|....*...
gi 1308984722 867 LTANAySEDRQ---RCLAAGMNDFLAKP 891
Cdd:cd17541    79 VSSLT-EEGAEitlEALELGAVDFIAKP 105
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
656-762 1.08e-17

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: 79.29  E-value: 1.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 656 LRQVLINFAGNALKFTRAGSiHLSGELLANDGENVTcRFVVSDTGLGIRPEDVPRLFKPFEQLDasTTRQYGGTGLGLAI 735
Cdd:cd16921     1 LGQVLTNLLGNAIKFRRPRR-PPRIEVGAEDVGEEW-TFYVRDNGIGIDPEYAEKVFGIFQRLH--SREEYEGTGVGLAI 76
                          90       100
                  ....*....|....*....|....*..
gi 1308984722 736 ARHLAHLMDGEVGVDSTPGQGSSFWIT 762
Cdd:cd16921    77 VRKIIERHGGRIWLESEPGEGTTFYFT 103
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
547-756 1.23e-17

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 87.21  E-value: 1.23e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 547 NMSHEIRTPMNAIIGLNYLLlKSPLEPAQRDKLLK-VTSASEHLLQVINDILDLSKIESGKLELENQTFDPREVLQAAAA 625
Cdd:PRK11100  262 TLTHELKSPLAAIRGAAELL-QEDPPPEDRARFTGnILTQSARLQQLIDRLLELARLEQRQELEVLEPVALAALLEELVE 340
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 626 VIRDQALGKGLLVGVDGGklPALAIGDAKRLRQVLINFAGNALKFTRAGS-IHLSGELlanDGENVtcRFVVSDTGLGIr 704
Cdd:PRK11100  341 AREAQAAAKGITLRLRPD--DARVLGDPFLLRQALGNLLDNAIDFSPEGGtITLSAEV---DGEQV--ALSVEDQGPGI- 412
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1308984722 705 PE-DVPRLFKPFeqldASTTRQYGG---TGLGLAIARHLAHLMDGEVGVDSTPGQG 756
Cdd:PRK11100  413 PDyALPRIFERF----YSLPRPANGrksTGLGLAFVREVARLHGGEVTLRNRPEGG 464
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
789-897 1.43e-17

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: 79.44  E-value: 1.43e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALPGgaaIPIVALT 868
Cdd:cd17626     2 RILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIRAESG---VPIVMLT 78
                          90       100
                  ....*....|....*....|....*....
gi 1308984722 869 ANAYSEDRQRCLAAGMNDFLAKPVDPEAL 897
Cdd:cd17626    79 AKSDTVDVVLGLESGADDYVAKPFKPKEL 107
pleD PRK09581
response regulator PleD; Reviewed
789-897 1.45e-17

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 86.49  E-value: 1.45e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALPGGAAIPIVALT 868
Cdd:PRK09581    4 RILVVDDIPANVKLLEAKLLAEYYTVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLKSDPATTHIPVVMVT 83
                          90       100
                  ....*....|....*....|....*....
gi 1308984722 869 ANAYSEDRQRCLAAGMNDFLAKPVDPEAL 897
Cdd:PRK09581   84 ALDDPEDRVRGLEAGADDFLTKPINDVAL 112
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
789-897 1.96e-17

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: 79.13  E-value: 1.96e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDEPLNREIGC-DLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALPGGAAIPIVAL 867
Cdd:cd17552     3 RILVIDDEEDIREVVQaCLEKLAGWEVLTASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKKLQANPETQSIPVILL 82
                          90       100       110
                  ....*....|....*....|....*....|
gi 1308984722 868 TANAYSEDRQRCLAAGMNDFLAKPVDPEAL 897
Cdd:cd17552    83 TAKAQPSDRQRFASLGVAGVIAKPFDPLTL 112
PRK10604 PRK10604
sensor protein RstB; Provisional
547-759 2.30e-17

sensor protein RstB; Provisional


Pssm-ID: 236724 [Multi-domain]  Cd Length: 433  Bit Score: 85.81  E-value: 2.30e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 547 NMSHEIRTPmnaIIGLNYLLLKSP-LEPAQRDKLLKVTSASEHLlqvINDILDLSKIESGKLELENQTFDPREVLQAAAA 625
Cdd:PRK10604  218 GIAHELRTP---LVRLRYRLEMSDnLSAAESQALNRDIGQLEAL---IEELLTYARLDRPQNELHLSEPDLPAWLSTHLA 291
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 626 VIrdQALGKGLLVGVDGGKLPALAIGDAKRLRQVLINFAGNALKFTRaGSIHLSgelLANDGENVTcrFVVSDTGLGIRP 705
Cdd:PRK10604  292 DI--QAVTPEKTVRLDTPHQGDYGALDMRLMERVLDNLLNNALRYAH-SRVRVS---LLLDGNQAC--LIVEDDGPGIPP 363
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1308984722 706 EDVPRLFKPFEQLDASTTRQYGGTGLGLAIARHLAHLMDGEVGVDSTPGQGSSF 759
Cdd:PRK10604  364 EERERVFEPFVRLDPSRDRATGGCGLGLAIVHSIALAMGGSVNCDESELGGARF 417
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
790-897 2.35e-17

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: 78.68  E-value: 2.35e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 790 VLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRAlpGGAAIPIVALTA 869
Cdd:cd17624     1 ILLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRR--QGQSLPVLILTA 78
                          90       100
                  ....*....|....*....|....*...
gi 1308984722 870 NAYSEDRQRCLAAGMNDFLAKPVDPEAL 897
Cdd:cd17624    79 RDGVDDRVAGLDAGADDYLVKPFALEEL 106
Spo0F COG5803
Stage 0 sporulation initiation response regulator Spo0F [Cell cycle control, cell division, ...
788-906 3.69e-17

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: 78.30  E-value: 3.69e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 788 GRVLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALpgGAAIPIVAL 867
Cdd:COG5803     3 KKILIVDDQAGIRMLLKEVLKKEGYEVFQAANGKEALEKVKELKPDLVLLDMKMPGMDGIEILKEIKEI--DPDIPVIMM 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1308984722 868 TanAYSEDR--QRCLAAGMNDFLAKPVDPEALYTILGKYLA 906
Cdd:COG5803    81 T--AYGELDmvEEAKELGAKGYFTKPFDIDELREAVNKLLK 119
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
790-897 3.76e-17

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: 78.12  E-value: 3.76e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 790 VLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALPggaAIPIVALTA 869
Cdd:cd17623     1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELRKTS---QVPVLMLTA 77
                          90       100
                  ....*....|....*....|....*...
gi 1308984722 870 NAYSEDRQRCLAAGMNDFLAKPVDPEAL 897
Cdd:cd17623    78 RGDDIDRILGLELGADDYLPKPFNPREL 105
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
791-897 4.07e-17

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: 78.03  E-value: 4.07e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 791 LLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRAlpGGAAIPIVALTAN 870
Cdd:cd17625     1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLRE--EGIETPVLLLTAL 78
                          90       100
                  ....*....|....*....|....*..
gi 1308984722 871 AYSEDRQRCLAAGMNDFLAKPVDPEAL 897
Cdd:cd17625    79 DAVEDRVKGLDLGADDYLPKPFSLAEL 105
HATPase_TutC-TodS-like cd16925
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ...
652-761 5.45e-17

Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas putida TodS and Thauera aromatica TutC; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinase (HKs) such Pseudomonas putida TodS HK of the TodS-TodT two-component regulatory system (TCS) which controls the expression of a toluene degradation pathway. Thauera aromatica TutC may be part of a TCS that is involved in anaerobic toluene metabolism. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), PAS sensor domain(s) and a REC domain.


Pssm-ID: 340402 [Multi-domain]  Cd Length: 110  Bit Score: 77.53  E-value: 5.45e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 652 DAKRLRQVLINFAGNALKFT-RAGSIHLSGELLANDGenvtCRFVVSDTGLGIRPEDVPRLFKPFEQLDASTTRQYGGTG 730
Cdd:cd16925     1 DAEKYERVVLNLLSNAFKFTpDGGRIRCILEKFRLNR----FLLTVSDSGPGIPPNLREEIFERFRQGDGSSTRAHGGTG 76
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1308984722 731 LGLAIARHLAHLMDGEVGVDSTPGQGSSFWI 761
Cdd:cd16925    77 LGLSIVKEFVELHGGTVTVSDAPGGGALFQV 107
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
790-897 6.76e-17

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: 77.42  E-value: 6.76e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 790 VLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRAlpGGAAIPIVALTA 869
Cdd:cd17627     1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRA--AGNDLPILVLTA 78
                          90       100
                  ....*....|....*....|....*...
gi 1308984722 870 NAYSEDRQRCLAAGMNDFLAKPVDPEAL 897
Cdd:cd17627    79 RDSVSDRVAGLDAGADDYLVKPFALEEL 106
HATPase_EcPhoR-like cd16952
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
656-759 9.63e-17

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: 76.86  E-value: 9.63e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 656 LRQVLINFAGNALKFTRagsihlsgellanDGENVTCR---------FVVSDTGLGIRPEDVPRLFKPFEQLDASTTRQY 726
Cdd:cd16952     1 LRSAFSNLVSNAVKYTP-------------PSDTITVRwsqeesgarLSVEDTGPGIPPEHIPRLTERFYRVDIERCRNT 67
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1308984722 727 GGTGLGLAIARHLAHLMDGEVGVDSTPGQGSSF 759
Cdd:cd16952    68 GGTGLGLAIVKHVMSRHDARLLIASELGKGSRF 100
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
791-897 9.75e-17

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: 76.93  E-value: 9.75e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 791 LLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALPGGAAIPIVALTAN 870
Cdd:cd19937     1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRSDPKTSSIPIIMLTAK 80
                          90       100
                  ....*....|....*....|....*..
gi 1308984722 871 AYSEDRQRCLAAGMNDFLAKPVDPEAL 897
Cdd:cd19937    81 GEEFDKVLGLELGADDYITKPFSPREL 107
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
789-897 1.23e-16

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: 77.01  E-value: 1.23e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRAlpGGAAIPIVALT 868
Cdd:cd17615     1 RVLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRA--DGPDVPVLFLT 78
                          90       100
                  ....*....|....*....|....*....
gi 1308984722 869 ANAYSEDRQRCLAAGMNDFLAKPVDPEAL 897
Cdd:cd17615    79 AKDSVEDRIAGLTAGGDDYVTKPFSLEEV 107
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
789-895 1.35e-16

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: 76.55  E-value: 1.35e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDEPLNREIGCDLLAATGLEVA-TADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALPGGAAipIVAL 867
Cdd:cd17542     2 KVLIVDDAAFMRMMLKDILTKAGYEVVgEAANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIKKIDPNAK--VIMC 79
                          90       100
                  ....*....|....*....|....*...
gi 1308984722 868 TANAYSEDRQRCLAAGMNDFLAKPVDPE 895
Cdd:cd17542    80 SAMGQEEMVKEAIKAGAKDFIVKPFQPE 107
HisKA pfam00512
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ...
540-605 1.92e-16

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


Pssm-ID: 459839 [Multi-domain]  Cd Length: 66  Bit Score: 74.56  E-value: 1.92e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1308984722 540 AKSAFLANMSHEIRTPMNAIIGLNYLLLKSPLEPAQRDKLLKVTSASEHLLQVINDILDLSKIESG 605
Cdd:pfam00512   1 AKSEFLANLSHELRTPLTAIRGYLELLRDEKLDEEQREYLETILRSAERLLRLINDLLDLSRIEAG 66
HisKA smart00388
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ...
540-605 2.50e-16

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


Pssm-ID: 214644 [Multi-domain]  Cd Length: 66  Bit Score: 74.14  E-value: 2.50e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1308984722  540 AKSAFLANMSHEIRTPMNAIIGLNYLLLKSPLEPAQRDKLLKVTSASEHLLQVINDILDLSKIESG 605
Cdd:smart00388   1 AKREFLANLSHELRTPLTAIRGYLELLLDTELSEEQREYLETILREAERLLRLINDLLDLSRIEAG 66
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
790-891 4.04e-16

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


Pssm-ID: 381151 [Multi-domain]  Cd Length: 111  Bit Score: 75.11  E-value: 4.04e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 790 VLLVEDEPLNREIGCDLLAATGLEVATADDG---------FAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALPGGA 860
Cdd:cd19924     1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGeealnklenLAKEGNDLSKELDLIITDIEMPKMDGYELTFELRDDPRLA 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1308984722 861 AIPIVALTANAYSEDRQRCLAAGMNDFLAKP 891
Cdd:cd19924    81 NIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
789-901 5.99e-16

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: 74.75  E-value: 5.99e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDEPLNREIGCDLLAATGLEV-ATADDGFAAIARFQEGGFDLILMDIQMPG-LDGLDATRRIRALPGgaaIPIVA 866
Cdd:cd17534     2 KILIVEDEAIIALDLKEILESLGYEVvGIADSGEEAIELAEENKPDLILMDINLKGdMDGIEAAREIREKFD---IPVIF 78
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1308984722 867 LTANAYSEDRQRCLAAGMNDFLAKPVDPEALYTIL 901
Cdd:cd17534    79 LTAYSDEETLERAKETNPYGYLVKPFNERELKAAI 113
PRK13559 PRK13559
hypothetical protein; Provisional
360-525 9.87e-16

hypothetical protein; Provisional


Pssm-ID: 237427 [Multi-domain]  Cd Length: 361  Bit Score: 79.86  E-value: 9.87e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 360 AADHQAIETLNNQLAERLAALEIAEQDLRRLSTAVEQSPASIVITDinAR-----ITYVNLAFCVTSGYFPDEVIGENPR 434
Cdd:PRK13559   15 AASSKAFSADRKELAAIHDPRDFRGASGRLFEQAMEQTRMAMCITD--PHqpdlpIVLANQAFLDLTGYAAEEVVGRNCR 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 435 ILQSGNTPPATYQAMWQTLTAGEIWRGELVNRRKDGSHYIERATISPVRGSDGTTSQYVAVKEDISDQRRIEEELAAHRQ 514
Cdd:PRK13559   93 FLQGAATDPIAVAKIRAAIAAEREIVVELLNYRKDGEPFWNALHLGPVYGEDGRLLYFFGSQWDVTDIRAVRALEAHERR 172
                         170
                  ....*....|.
gi 1308984722 515 HLQQlVDQRTG 525
Cdd:PRK13559  173 LARE-VDHRSK 182
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
546-761 1.23e-15

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 80.60  E-value: 1.23e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 546 ANMSHEIRTPMNAIIGL-NYLLLKSPLEPAQRDKLLKVTSASEHLLQVINDILDLSKiesgKLELENQTFDPREVLQAAA 624
Cdd:PRK10364  242 AGVAHEIRNPLSSIKGLaKYFAERAPAGGEAHQLAQVMAKEADRLNRVVSELLELVK----PTHLALQAVDLNDLINHSL 317
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 625 AVIRDQALGKGLLVGVDGGKLPALAIGDAKRLRQVLINFAGNALK-FTRAGSIHLSGEllaNDGENVtcRFVVSDTGLGI 703
Cdd:PRK10364  318 QLVSQDANSREIQLRFTANDTLPEIQADPDRLTQVLLNLYLNAIQaIGQHGVISVTAS---ESGAGV--KISVTDSGKGI 392
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1308984722 704 RPEDVPRLFKPFeqldasTTRQYGGTGLGLAIARHLAHLMDGEVGVDSTPGQGSSFWI 761
Cdd:PRK10364  393 AADQLEAIFTPY------FTTKAEGTGLGLAVVHNIVEQHGGTIQVASQEGKGATFTL 444
HATPase_RstB-like cd16939
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
656-762 1.39e-15

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: 73.23  E-value: 1.39e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 656 LRQVLINFAGNALKFTRAgSIHLSgeLLANDGEnvtCRFVVSDTGLGIRPEDVPRLFKPFEQLDASTTRQYGGTGLGLAI 735
Cdd:cd16939     1 MARALDNLLRNALRYAHR-TVRIA--LLVSGGR---LTLIVEDDGPGIPAAARERVFEPFVRLDPSRDRATGGFGLGLAI 74
                          90       100
                  ....*....|....*....|....*..
gi 1308984722 736 ARHLAHLMDGEVGVDSTPGQGSSFWIT 762
Cdd:cd16939    75 VHRVALWHGGHVECDDSELGGACFRLT 101
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
790-897 1.68e-15

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: 73.47  E-value: 1.68e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 790 VLLVEDE-PLNREIGCDLLAAtGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRAlpGGAAIPIVALT 868
Cdd:cd19934     1 LLLVEDDaLLAAQLKEQLSDA-GYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRS--EGRATPVLILT 77
                          90       100
                  ....*....|....*....|....*....
gi 1308984722 869 ANAYSEDRQRCLAAGMNDFLAKPVDPEAL 897
Cdd:cd19934    78 ARDSWQDKVEGLDAGADDYLTKPFHIEEL 106
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
388-499 1.80e-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: 73.22  E-value: 1.80e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 388 RRLSTAVEQSPASIVITDINARITYVNLAFCVTSGYFPDEVIGENPRILQSGNTPPATYQAMWQTLTAGEIWRGELVN-R 466
Cdd:pfam00989   1 EDLRAILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALLQGEESRGFEVSfR 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1308984722 467 RKDGSHYIERATISPVRGSDGTTSQYVAVKEDI 499
Cdd:pfam00989  81 VPDGRPRHVEVRASPVRDAGGEILGFLGVLRDI 113
HATPase_BaeS-like cd16946
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
652-766 1.84e-15

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: 73.27  E-value: 1.84e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 652 DAKRLRQVLINFAGNALKFTRAG-SIHLSGEllandGENVTCRFVVSDTGLGIRPEDVPRLFKPFEQLDASTTRQYGGTG 730
Cdd:cd16946     1 DRDRLQQLFVNLLENSLRYTDTGgKLRIRAA-----QTPQEVRLDVEDSAPGVSDDQLARLFERFYRVESSRNRASGGSG 75
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1308984722 731 LGLAIARHLAHLMDGEVGVDSTPGQGssFWITARLK 766
Cdd:cd16946    76 LGLAICHNIALAHGGTISAEHSPLGG--LRLVLTLP 109
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
790-891 2.12e-15

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: 72.47  E-value: 2.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 790 VLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALpgGAAIPIVALTA 869
Cdd:cd19935     1 ILVVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLRRLRAA--GKQTPVLMLTA 78
                          90       100
                  ....*....|....*....|..
gi 1308984722 870 NAYSEDRQRCLAAGMNDFLAKP 891
Cdd:cd19935    79 RDSVEDRVKGLDLGADDYLVKP 100
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
789-897 3.30e-15

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: 72.83  E-value: 3.30e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDEPLNREIGCDLLAATGLEV-ATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRalpGGAAIPIVAL 867
Cdd:cd19932     2 RVLIAEDEALIRMDLREMLEEAGYEVvGEASDGEEAVELAKKHKPDLVIMDVKMPRLDGIEAAKIIT---SENIAPIVLL 78
                          90       100       110
                  ....*....|....*....|....*....|
gi 1308984722 868 TANAYSEDRQRCLAAGMNDFLAKPVDPEAL 897
Cdd:cd19932    79 TAYSQQDLVERAKEAGAMAYLVKPFSESDL 108
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
789-897 3.54e-15

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 75.91  E-value: 3.54e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALPGGAAIPIVALT 868
Cdd:PRK10161    4 RILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKRESMTRDIPVVMLT 83
                          90       100
                  ....*....|....*....|....*....
gi 1308984722 869 ANAYSEDRQRCLAAGMNDFLAKPVDPEAL 897
Cdd:PRK10161   84 ARGEEEDRVRGLETGADDYITKPFSPKEL 112
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
790-891 3.71e-15

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


Pssm-ID: 381136 [Multi-domain]  Cd Length: 99  Bit Score: 71.85  E-value: 3.71e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 790 VLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRAlpgGAAIPIVALTA 869
Cdd:cd17621     1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQLRA---RSNVPVIMVTA 77
                          90       100
                  ....*....|....*....|..
gi 1308984722 870 NAYSEDRQRCLAAGMNDFLAKP 891
Cdd:cd17621    78 KDSEIDKVVGLELGADDYVTKP 99
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
789-894 3.79e-15

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: 72.41  E-value: 3.79e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALPggaAIPIVALT 868
Cdd:cd19938     1 RILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCREIRRFS---DVPIIMVT 77
                          90       100
                  ....*....|....*....|....*.
gi 1308984722 869 ANAYSEDRQRCLAAGMNDFLAKPVDP 894
Cdd:cd19938    78 ARVEEIDRLLGLELGADDYICKPYSP 103
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
789-897 3.81e-15

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: 72.41  E-value: 3.81e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALPGGaaiPIVALT 868
Cdd:cd17622     2 RILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRDLRPKYQG---PILLLT 78
                          90       100
                  ....*....|....*....|....*....
gi 1308984722 869 ANAYSEDRQRCLAAGMNDFLAKPVDPEAL 897
Cdd:cd17622    79 ALDSDIDHILGLELGADDYVVKPVEPAVL 107
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
789-897 7.55e-15

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: 71.64  E-value: 7.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALpggAAIPIVALT 868
Cdd:cd19939     1 RILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVREH---SHVPILMLT 77
                          90       100
                  ....*....|....*....|....*....
gi 1308984722 869 ANAYSEDRQRCLAAGMNDFLAKPVDPEAL 897
Cdd:cd19939    78 ARTEEMDRVLGLEMGADDYLCKPFSPREL 106
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
790-897 9.72e-15

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: 71.59  E-value: 9.72e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 790 VLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALPGGAAIPIVALTA 869
Cdd:cd17598     1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKSDPDLKDIPVILLTT 80
                          90       100
                  ....*....|....*....|....*...
gi 1308984722 870 NAYSEDRQRCLAAGMNDFLAKPVDPEAL 897
Cdd:cd17598    81 LSDPRDVIRGLECGADNFITKPYDEKYL 108
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
789-897 1.79e-14

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: 70.49  E-value: 1.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRAlpgGAAIPIVALT 868
Cdd:cd17619     2 HILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELRE---QSEVGIILVT 78
                          90       100
                  ....*....|....*....|....*....
gi 1308984722 869 ANAYSEDRQRCLAAGMNDFLAKPVDPEAL 897
Cdd:cd17619    79 GRDDEVDRIVGLEIGADDYVTKPFNPREL 107
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
790-897 1.84e-14

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: 70.35  E-value: 1.84e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 790 VLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIA--RFQEGGFDLILMDIQMPGLDGLDATRRIRALPGgaaIPIVAL 867
Cdd:cd17584     1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSmlRENKDEFDLVITDVHMPDMDGFEFLELIRLEMD---LPVIMM 77
                          90       100       110
                  ....*....|....*....|....*....|
gi 1308984722 868 TANAYSEDRQRCLAAGMNDFLAKPVDPEAL 897
Cdd:cd17584    78 SADGSTSTVMKGLAHGACDYLLKPVSIEDL 107
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
789-842 2.38e-14

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: 67.98  E-value: 2.38e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1308984722  789 RVLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMP 842
Cdd:smart00448   2 RILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
651-761 3.41e-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: 69.74  E-value: 3.41e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 651 GDAKRLRQVLINFAGNALKFTRAGS---IHLSGELLANdgenvtcrFVVSDTGLGIRPEDVPRLFKPFEQLDASTtrqYG 727
Cdd:cd16940     9 GDALLLFLLLRNLVDNAVRYSPQGSrveIKLSADDGAV--------IRVEDNGPGIDEEELEALFERFYRSDGQN---YG 77
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1308984722 728 GTGLGLAIARHLAHLMDGEVGVDSTPGQGSSFWI 761
Cdd:cd16940    78 GSGLGLSIVKRIVELHGGQIFLGNAQGGGLEAWV 111
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
789-905 6.00e-14

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 75.27  E-value: 6.00e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALPGGAaiPIVALT 868
Cdd:PRK11361    6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETRT--PVILMT 83
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1308984722 869 ANAYSEDRQRCLAAGMNDFLAKPVDPEALYTILGKYL 905
Cdd:PRK11361   84 AYAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRAL 120
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
656-756 7.76e-14

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: 68.51  E-value: 7.76e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 656 LRQVLINFAGNALKFTRaGSIHLSGEllaNDGENVTcrFVVSDTGLGIRPEDVPRLFKPFEQLDASTTRQYGGTGLGLAI 735
Cdd:cd16949     1 LARALENVLRNALRYSP-SKILLDIS---QDGDQWT--ITITDDGPGVPEDQLEQIFLPFYRVDSARDRESGGTGLGLAI 74
                          90       100
                  ....*....|....*....|.
gi 1308984722 736 ARHLAHLMDGEVGVDSTPGQG 756
Cdd:cd16949    75 AERAIEQHGGKIKASNRKPGG 95
PRK10610 PRK10610
chemotaxis protein CheY;
789-903 8.03e-14

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 69.23  E-value: 8.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDEPLNREIGCDLLAATGLE-VATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALPGGAAIPIVAL 867
Cdd:PRK10610    7 KFLVVDDFSTMRRIVRNLLKELGFNnVEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIRADGAMSALPVLMV 86
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1308984722 868 TANAYSEDRQRCLAAGMNDFLAKPVDPEALYTILGK 903
Cdd:PRK10610   87 TAEAKKENIIAAAQAGASGYVVKPFTAATLEEKLNK 122
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
790-897 8.10e-14

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: 69.06  E-value: 8.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 790 VLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALpgGAAIPIVALTA 869
Cdd:cd17549     1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIREL--DPDLPVILITG 78
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1308984722 870 --------NAysedrqrcLAAGMNDFLAKPVDPEAL 897
Cdd:cd17549    79 hgdvpmavEA--------MRAGAYDFLEKPFDPERL 106
PRK09835 PRK09835
Cu(+)/Ag(+) sensor histidine kinase;
541-753 8.27e-14

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


Pssm-ID: 182101 [Multi-domain]  Cd Length: 482  Bit Score: 75.19  E-value: 8.27e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 541 KSAFLANMSHEIRTPMNAIIGLNYLLLKSPLEPAQRDKLLkVTSASEH--LLQVINDILDLSKIESGKLELENQTFDPRE 618
Cdd:PRK09835  262 QSNFSADIAHEIRTPITNLITQTEIALSQSRSQKELEDVL-YSNLEELtrMAKMVSDMLFLAQADNNQLIPEKKMLDLAD 340
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 619 VLQAAAAVIRDQALGKGLLVGVDGgkLPALAIGDAKRLRQVLINFAGNALKFTRAG---SIHLSgellanDGENvTCRFV 695
Cdd:PRK09835  341 EVGKVFDFFEAWAEERGVELRFVG--DPCQVAGDPLMLRRAISNLLSNALRYTPAGeaiTVRCQ------EVDH-QVQLV 411
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1308984722 696 VSDTGLGIRPEDVPRLFKPFEQLDASTTRQYGGTGLGLAIARHLAHLMDGEVGVDSTP 753
Cdd:PRK09835  412 VENPGTPIAPEHLPRLFDRFYRVDPSRQRKGEGSGIGLAIVKSIVVAHKGTVAVTSDA 469
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
790-891 8.50e-14

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: 67.96  E-value: 8.50e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 790 VLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRalpGGAAIPIVALTA 869
Cdd:cd17620     1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLR---EWSAVPVIVLSA 77
                          90       100
                  ....*....|....*....|..
gi 1308984722 870 NAYSEDRQRCLAAGMNDFLAKP 891
Cdd:cd17620    78 RDEESDKIAALDAGADDYLTKP 99
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
409-501 2.27e-13

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: 66.72  E-value: 2.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 409 RITYVNLAFCVTSGYFPDEVIGENPRILQSGNTPPATYQAMWQTLTAGeiWRGELVNRRKDGSHYIERATISPVRGSDGT 488
Cdd:pfam13426   3 RIIYVNDAALRLLGYTREELLGKSITDLFAEPEDSERLREALREGKAV--REFEVVLYRKDGEPFPVLVSLAPIRDDGGE 80
                          90
                  ....*....|...
gi 1308984722 489 TSQYVAVKEDISD 501
Cdd:pfam13426  81 LVGIIAILRDITE 93
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
789-904 3.59e-13

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


Pssm-ID: 381124 [Multi-domain]  Cd Length: 117  Bit Score: 66.79  E-value: 3.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDEPLNR-EIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALpgGAAIPIVAL 867
Cdd:cd17593     2 KVLICDDSSMARkQLARALPADWDVEITFAENGEEALEILREGRIDVLFLDLTMPVMDGYEVLEALPVE--QLETKVIVV 79
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1308984722 868 TANAYSEDRQRCLAAGMNDFLAKPVDPEALYTILGKY 904
Cdd:cd17593    80 SGDVQPEAKERVLELGALAFLKKPFDPEKLAQLLEEL 116
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
656-761 3.82e-13

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: 66.29  E-value: 3.82e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 656 LRQVLINFAGNAlkftrAGSIHLSGELLANDGENVTCRFV-VSDTGLGIRPEDVPRLFKPFeqldaSTTRQYG-GTGLGL 733
Cdd:cd16943     4 LNQVLLNLLVNA-----AQAMEGRGRITIRTWAHVDQVLIeVEDTGSGIDPEILGRIFDPF-----FTTKPVGeGTGLGL 73
                          90       100
                  ....*....|....*....|....*...
gi 1308984722 734 AIARHLAHLMDGEVGVDSTPGQGSSFWI 761
Cdd:cd16943    74 SLSYRIIQKHGGTIRVASVPGGGTRFTI 101
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
789-892 3.98e-13

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


Pssm-ID: 381107 [Multi-domain]  Cd Length: 116  Bit Score: 66.84  E-value: 3.98e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALpgGAAIPIVALT 868
Cdd:cd17555     2 TILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITKE--SPDTPVIVVS 79
                          90       100
                  ....*....|....*....|....
gi 1308984722 869 ANAYSEDRQRCLAAGMNDFLAKPV 892
Cdd:cd17555    80 GAGVMSDAVEALRLGAWDYLTKPI 103
PAS COG2202
PAS domain [Signal transduction mechanisms];
383-509 6.53e-13

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 70.05  E-value: 6.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 383 AEQDLR----RLSTAVEQSPASIVITDINARITYVNLAFCVTSGYFPDEVIGENPRILQSGNTPPAtYQAMWQTLTAGEI 458
Cdd:COG2202   128 AEEALReseeRLRLLVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRER-LLELLRRLLEGGR 206
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1308984722 459 WRGELVNRRKDGSHYIERATISPVRGSDGTTSQ-YVAVKEDISDQRRIEEEL 509
Cdd:COG2202   207 ESYELELRLKDGDGRWVWVEASAVPLRDGGEVIgVLGIVRDITERKRAEEAL 258
HisKA cd00082
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ...
538-601 8.88e-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: 64.16  E-value: 8.88e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1308984722 538 NLAKSAFLANMSHEIRTPMNAIIGLNYLLLKSPLEPAQRDKLLK-VTSASEHLLQVINDILDLSK 601
Cdd:cd00082     1 LQAKGEFLANVSHELRTPLTAIRGALELLEEELLDDEEQREYLErIREEAERLLRLINDLLDLSR 65
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
790-891 1.78e-12

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: 64.32  E-value: 1.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 790 VLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALPGGAAIPIVALTA 869
Cdd:cd19927     1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLRKNADFDTIPVIFLTA 80
                          90       100
                  ....*....|....*....|..
gi 1308984722 870 NAYSEDRQRCLAAGMNDFLAKP 891
Cdd:cd19927    81 KGMTSDRIKGYNAGCDGYLSKP 102
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
790-897 1.78e-12

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: 67.05  E-value: 1.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 790 VLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALpgGAAIPIVALTA 869
Cdd:COG4566     2 VYIVDDDEAVRDSLAFLLESAGLRVETFASAEAFLAALDPDRPGCLLLDVRMPGMSGLELQEELAAR--GSPLPVIFLTG 79
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1308984722 870 NAyseDRQRCLAA---GMNDFLAKPVDPEAL 897
Cdd:COG4566    80 HG---DVPMAVRAmkaGAVDFLEKPFDDQAL 107
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
790-906 2.41e-12

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 70.06  E-value: 2.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 790 VLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALpgGAAIPIVALTA 869
Cdd:PRK10365    8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKAL--NPAIPVLIMTA 85
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1308984722 870 NAYSEDRQRCLAAGMNDFLAKPVDPEALYTILGKYLA 906
Cdd:PRK10365   86 YSSVETAVEALKTGALDYLIKPLDFDNLQATLEKALA 122
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
789-853 2.45e-12

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


Pssm-ID: 441799 [Multi-domain]  Cd Length: 131  Bit Score: 64.91  E-value: 2.45e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1308984722 789 RVLLVEDEPLNREIGCDLLAAT-GLEV-ATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRI 853
Cdd:COG2197     3 RVLIVDDHPLVREGLRALLEAEpDIEVvGEAADGEEALELLEELRPDVVLLDIRMPGMDGLEALRRL 69
HATPase_YcbM-like cd16947
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
646-762 2.54e-12

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: 64.84  E-value: 2.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 646 PALAIGDAKRLRQVLINFAGNALKFTRAGSIhlSGELLANDGENVTcrFVVSDTGLGIRPEDVPRLFKPFEQLDASTTRQ 725
Cdd:cd16947    11 PIYANANTEALQRILKNLISNAIKYGSDGKF--LGMTLREDEKHVY--IDIWDKGKGISETEKDHVFERLYTLEDSRNSA 86
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1308984722 726 YGGTGLGLAIARHLAHLMDGEVGVDSTPGQGSSFWIT 762
Cdd:cd16947    87 KQGNGLGLTITKRLAESMGGSIYVNSKPYEKTVFTVT 123
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
656-756 2.81e-12

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: 64.01  E-value: 2.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 656 LRQVLINFAGNALKFTRaGSIHLSgellaNDGENVTCRFVVSDTGLGIRPEDVPRLFKPFEQLDASttRQYGGTGLGLAI 735
Cdd:cd16950     1 LKRVLSNLVDNALRYGG-GWVEVS-----SDGEGNRTRIQVLDNGPGIAPEEVDELFQPFYRGDNA--RGTSGTGLGLAI 72
                          90       100
                  ....*....|....*....|.
gi 1308984722 736 ARHLAHLMDGEVGVDSTPGQG 756
Cdd:cd16950    73 VQRISDAHGGSLTLANRAGGG 93
ompR PRK09468
osmolarity response regulator; Provisional
789-897 3.36e-12

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 67.31  E-value: 3.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRAlpGGAAIPIVALT 868
Cdd:PRK09468    7 KILVVDDDMRLRALLERYLTEQGFQVRSAANAEQMDRLLTRESFHLMVLDLMLPGEDGLSICRRLRS--QNNPTPIIMLT 84
                          90       100
                  ....*....|....*....|....*....
gi 1308984722 869 ANAYSEDRQRCLAAGMNDFLAKPVDPEAL 897
Cdd:PRK09468   85 AKGEEVDRIVGLEIGADDYLPKPFNPREL 113
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
790-891 3.49e-12

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: 63.98  E-value: 3.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 790 VLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALpggAAIPIVALTA 869
Cdd:cd17614     1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVRKT---SNVPIIMLTA 77
                          90       100
                  ....*....|....*....|..
gi 1308984722 870 NAYSEDRQRCLAAGMNDFLAKP 891
Cdd:cd17614    78 KDSEVDKVLGLELGADDYVTKP 99
orf27 CHL00148
Ycf27; Reviewed
789-897 4.85e-12

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 67.05  E-value: 4.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRAlpgGAAIPIVALT 868
Cdd:CHL00148    8 KILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIRK---ESDVPIIMLT 84
                          90       100
                  ....*....|....*....|....*....
gi 1308984722 869 ANAYSEDRQRCLAAGMNDFLAKPVDPEAL 897
Cdd:CHL00148   85 ALGDVSDRITGLELGADDYVVKPFSPKEL 113
dCache_1 pfam02743
Cache domain; Double cache domain 1 covers the last three strands from the membrane distal ...
30-264 4.98e-12

Cache domain; Double cache domain 1 covers the last three strands from the membrane distal PAS-like domain, the first two strands of the membrane proximal domain, and the connecting elements between the two domains. This domain when present in chemoreceptors recognize several signals such as proteinogenic amino acids, GABA, Histamine and polyamines, decanoic acid, Autoinducer-2, purine derivatives, quaternary amines, citrate and taurine, among others. When associated with histidine kinases, it recognizes C3/C4-dicarboxylic acids, Spermine, guanosine and Autoinducer-2 (Mantilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1 https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 460673 [Multi-domain]  Cd Length: 237  Bit Score: 66.98  E-value: 4.98e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722  30 RHERRLATDHIVTLGKSLlqAARIEEEaaLRQVREMLHIMAGADNMRSLDADDCSGLAKRL---LSVTHDIANIGAALAN 106
Cdd:pfam02743   1 KAIKEQAEEQLLSLAKQL--AENIESY--LDSLEEILELLASNPDLQDLLSAPAEEELAKLeslLRSNPGISSIYLVDAD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 107 GDVFCSAH--PITRPVNVADRPWFQEALTATDITS---GHYQTGLISGKRGITIGLPVRDAEGKLQAALYLASDIAWFDR 181
Cdd:pfam02743  77 GRVLASSDesPSYPGLDVSERPWYKEALKGGGGIIwvfSSPYPSSESGEPVLTIARPIYDDDGEVIGVLVADLDLDTLQE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 182 ISRNQQLPKGWTSLLVTDDGSVVSRHPDPDIWRGSAFDAAsrERLLAALRHDDDRVVMNGLDGIERLYLLQRLQIADGHL 261
Cdd:pfam02743 157 LLSQIKLGEGGYVFIVDSDGRILAHPLGKNLRSLLAPFLG--KSLADALPGSGITEIAVDLDGEDYLVAYAPIPGTGWTL 234

                  ...
gi 1308984722 262 VAA 264
Cdd:pfam02743 235 VVV 237
PRK15479 PRK15479
transcriptional regulator TctD;
789-897 8.99e-12

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 65.90  E-value: 8.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDeplNREIGCDL---LAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALpgGAAIPIV 865
Cdd:PRK15479    2 RLLLAED---NRELAHWLekaLVQNGFAVDCVFDGLAADHLLQSEMYALAVLDINMPGMDGLEVLQRLRKR--GQTLPVL 76
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1308984722 866 ALTANAYSEDRQRCLAAGMNDFLAKPVDPEAL 897
Cdd:PRK15479   77 LLTARSAVADRVKGLNVGADDYLPKPFELEEL 108
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
790-894 1.03e-11

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: 62.77  E-value: 1.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 790 VLLVEDEPLNREIGCDLLAATGLEVATADDGFAAI-----------ARFQEGGFDLILMDIQMPGLDGLDATRRIRALPG 858
Cdd:cd17581     1 VLAVDDSLVDRKVIERLLRISSCRVTAVDSGKRALeflgledeedsSNFNEPKVNMIITDYCMPGMTGYDLLKKVKESSA 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1308984722 859 GAAIPIVALTANAYSEDRQRCLAAGMNDFLAKPVDP 894
Cdd:cd17581    81 LKEIPVVIMSSENIPTRISRCLEEGAEDFLLKPVKL 116
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
656-762 1.07e-11

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


Pssm-ID: 340397 [Multi-domain]  Cd Length: 104  Bit Score: 62.41  E-value: 1.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 656 LRQVLINFAGNALKFTRAGSIHlSGELL----ANDGENVTcrFVVSDTGLGIRPEDVPRLFKPFeqldasTTRQYGGTGL 731
Cdd:cd16920     1 IQQVLINLVRNGIEAMSEGGCE-RRELTirtsPADDRAVT--ISVKDTGPGIAEEVAGQLFDPF------YTTKSEGLGM 71
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1308984722 732 GLAIARHLAHLMDGEVGVDSTPGQGSSFWIT 762
Cdd:cd16920    72 GLSICRSIIEAHGGRLSVESPAGGGATFQFT 102
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
789-898 1.37e-11

second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This family is composed of uncharacterized PleD-like response regulators that contain two N-terminal REC domains and a C-terminal diguanylate cyclase output domain with the characteristic GGDEF motif at the active site. Unlike PleD which contains a REC-like adaptor domain, the second REC domain of these uncharacterized GGDEF domain proteins, described in this model, contains characteristic metal-binding and active site residues. PleD response regulators are global regulators of cell metabolism in some important human pathogens. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381098 [Multi-domain]  Cd Length: 122  Bit Score: 62.54  E-value: 1.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQE-GGFDLILMDIQMPGLDGLDATRRIRALPGGAAIPIVAL 867
Cdd:cd17544     2 KVLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLEQhPDIKLVITDYNMPEMDGFELVREIRKKYSRDQLAIIGI 81
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1308984722 868 TAnaySEDRQ---RCLAAGMNDFLAKPVDPEALY 898
Cdd:cd17544    82 SA---SGDNAlsaRFIKAGANDFLTKPFLPEEFY 112
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
790-901 1.64e-11

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: 62.13  E-value: 1.64e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 790 VLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALpgGAAIPIVALTA 869
Cdd:cd17550     1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKEK--YPDLPVIMISG 78
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1308984722 870 NAYSEDRQRCLAAGMNDFLAKPVDPEALYTIL 901
Cdd:cd17550    79 HGTIETAVKATKLGAYDFIEKPLSLDRLLLTI 110
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
789-906 2.18e-11

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: 63.40  E-value: 2.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALpgGAAIPIVALT 868
Cdd:COG4567     6 SLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALRER--DPDARIVVLT 83
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1308984722 869 ANAYSEDRQRCLAAGMNDFLAKPVDPEALYTILGKYLA 906
Cdd:COG4567    84 GYASIATAVEAIKLGADDYLAKPADADDLLAALERAEG 121
PRK10618 PRK10618
phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional
540-773 3.69e-11

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


Pssm-ID: 236726 [Multi-domain]  Cd Length: 894  Bit Score: 67.26  E-value: 3.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 540 AKSAFLANMSHEIRTPMNAIIGLNYLLLKSPLEPAQRDKLLKVTSASEHLLQVINDILDLSKIESGKLELENQTFDPR-- 617
Cdd:PRK10618  449 ARKAFLQNIGDELKQPLQSLAQLAAQLRQTSDEEQQQPELDQLAEQSDVLVRLVDNIQLLNMLETQDWKPEQELFSLQdl 528
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 618 --EVLQAAAAVIRDQALgkGLLVGVdggKLPA--LAIGDAKRLRQV---LINFagnALKFTRAGSIHLSGELLANDGENV 690
Cdd:PRK10618  529 idEVLPEVLPAIKRKGL--QLLIHN---HLKAeqLRIGDRDALRKIlllLLNY---AITTTAYGKITLEVDQDESSPDRL 600
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 691 TcrFVVSDTGLGIRPEDVPRLFKPFEQlDASTTRQYGGTGLGLAIARHLAHLMDGEVGVDSTPGQGSSFWITARLKAAGL 770
Cdd:PRK10618  601 T--IRILDTGAGVSIKELDNLHFPFLN-QTQGDRYGKASGLTFFLCNQLCRKLGGHLTIKSREGLGTRYSIHLKMLAADP 677

                  ...
gi 1308984722 771 PPE 773
Cdd:PRK10618  678 EVE 680
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
789-891 5.55e-11

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 63.40  E-value: 5.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRAlpGGAAIPIVALT 868
Cdd:PRK09836    2 KLLIVEDEKKTGEYLTKGLTEAGFVVDLADNGLNGYHLAMTGDYDLIILDIMLPDVNGWDIVRMLRS--ANKGMPILLLT 79
                          90       100
                  ....*....|....*....|...
gi 1308984722 869 ANAYSEDRQRCLAAGMNDFLAKP 891
Cdd:PRK09836   80 ALGTIEHRVKGLELGADDYLVKP 102
PDC1_DGC_like cd12914
first PDC (PhoQ/DcuS/CitA) domain of diguanylate-cyclase and similar domains; Members of this ...
56-173 6.92e-11

first PDC (PhoQ/DcuS/CitA) domain of diguanylate-cyclase and similar domains; Members of this subfamily display varying domain architectures but all contain double PDC (PhoQ/DcuS/CitA) sensor domains. This model represents the first PDC domain of Diguanylate-cyclases (DGCs), Histidine kinases (HKs), and other similar domains. Many members of this subfamily contain a C-terminal DGC (also called GGDEF) domain. DGCs regulate the turnover of cyclic diguanosine monophosphate. 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. In the case of HKs, 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.


Pssm-ID: 350339  Cd Length: 123  Bit Score: 60.48  E-value: 6.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722  56 EAALRQVREMLHIMAgadnMRSLDADDCSGLAKRLLSVTHDIANIGAALANGDVFCSAHP-ITRPVNVADRPWFQEALTA 134
Cdd:cd12914     5 DLLLRSLADDLEARG----AASADPAALQALLRRLLARLPEVRSIFVVDADGRVVASSGPgPAPGLDVSDRDYFQAARAG 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1308984722 135 TDITS-GHYQTGLISGKRGITIGLPVRDAEGKLQAALYLA 173
Cdd:cd12914    81 GGGLFiSEPVISRVTGKPVIPLSRPIRDADGRFAGVVVAS 120
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
652-762 7.79e-11

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


Pssm-ID: 340424 [Multi-domain]  Cd Length: 109  Bit Score: 59.99  E-value: 7.79e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 652 DAKRLRQVLINFAGNALKFTRagsihLSGEL---LANDGENVtcRFVVSDTGLGIRPEDVPRLFKPFeqLDASTTRQYG- 727
Cdd:cd16948     2 DAKWLSFIIGQIVSNALKYSK-----QGGKIeiySETNEQGV--VLSIKDFGIGIPEEDLPRVFDKG--FTGENGRNFQe 72
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1308984722 728 GTGLGLAIARHLAHLMDGEVGVDSTPGQGSSFWIT 762
Cdd:cd16948    73 STGMGLYLVKKLCDKLGHKIDVESEVGEGTTFTIT 107
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
778-894 1.17e-10

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 62.78  E-value: 1.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 778 SSPALSQRLFGRVLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALp 857
Cdd:PRK10710    1 MTELPIDENTPRILIVEDEPKLGQLLIDYLQAASYATTLLSHGDEVLPYVRQTPPDLILLDLMLPGTDGLTLCREIRRF- 79
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1308984722 858 ggAAIPIVALTANAYSEDRQRCLAAGMNDFLAKPVDP 894
Cdd:PRK10710   80 --SDIPIVMVTAKIEEIDRLLGLEIGADDYICKPYSP 114
cpxA PRK09470
envelope stress sensor histidine kinase CpxA;
545-735 1.30e-10

envelope stress sensor histidine kinase CpxA;


Pssm-ID: 236532 [Multi-domain]  Cd Length: 461  Bit Score: 64.95  E-value: 1.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 545 LANMSHEIRTPmnaiigLNYLLLKSPLepAQR-----DKLLKVTSASEHLLQVINDILDLSKIESgKLELEnqtfdpREV 619
Cdd:PRK09470  247 LSDISHELRTP------LTRLQLATAL--LRRrqgesKELERIETEAQRLDSMINDLLVLSRNQQ-KNHLE------RET 311
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 620 LQAA---AAVIRD-----QALGKGLLVGVDGGKLPALaiGDAKRLRQVLINFAGNALKFTRAgSIHLSGELlandgENVT 691
Cdd:PRK09470  312 FKANslwSEVLEDakfeaEQMGKSLTVSAPPGPWPIN--GNPNALASALENIVRNALRYSHT-KIEVAFSV-----DKDG 383
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1308984722 692 CRFVVSDTGLGIRPEDVPRLFKPFEQLDASTTRQYGGTGLGLAI 735
Cdd:PRK09470  384 LTITVDDDGPGVPEEEREQIFRPFYRVDEARDRESGGTGLGLAI 427
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
790-897 1.50e-10

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


Pssm-ID: 381087 [Multi-domain]  Cd Length: 118  Bit Score: 59.47  E-value: 1.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 790 VLLVEDEPLNREIGCDLLAATG--LEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALPGGAAipIVAL 867
Cdd:cd17532     1 ALIVDDEPLAREELRYLLEEHPdiEIVGEAENGEEALEAIEELKPDVVFLDIQMPGLDGLELAKKLSKLAKPPL--IVFV 78
                          90       100       110
                  ....*....|....*....|....*....|
gi 1308984722 868 TanAYSEDRQRCLAAGMNDFLAKPVDPEAL 897
Cdd:cd17532    79 T--AYDEYAVEAFELNAVDYLLKPFSEERL 106
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
790-897 2.26e-10

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: 58.96  E-value: 2.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 790 VLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRAlpGGAAIPIVALTA 869
Cdd:cd17616     1 VLLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGLDLGKLYDYDIILLDLNLPDMSGYEVLRTLRL--AKVKTPILILSG 78
                          90       100
                  ....*....|....*....|....*...
gi 1308984722 870 NAYSEDRQRCLAAGMNDFLAKPVDPEAL 897
Cdd:cd17616    79 LADIEDKVKGLGFGADDYMTKPFHKDEL 106
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
789-897 4.81e-10

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 60.43  E-value: 4.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDEPLNREIGCDLLA-ATGLE-VATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRAlpGGAAIPIVA 866
Cdd:PRK10651    8 TILLIDDHPMLRTGVKQLISmAPDITvVGEASNGEQGIELAESLDPDLILLDLNMPGMNGLETLDKLRE--KSLSGRIVV 85
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1308984722 867 LTANAYSEDRQRCLAAGMNDFLAKPVDPEAL 897
Cdd:PRK10651   86 FSVSNHEEDVVTALKRGADGYLLKDMEPEDL 116
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
790-891 5.41e-10

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


Pssm-ID: 381129 [Multi-domain]  Cd Length: 102  Bit Score: 57.38  E-value: 5.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 790 VLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALPGGAAIPIVALTA 869
Cdd:cd17602     1 VACVDDRPSIQKMIEYFLEKQGFRVVVIDDPLRALTTLLNSKPDLILIDIDMPDLDGYELCSLLRKSSALKDTPIIMLTG 80
                          90       100
                  ....*....|....*....|..
gi 1308984722 870 NAYSEDRQRCLAAGMNDFLAKP 891
Cdd:cd17602    81 KDGLVDRIRAKMAGASGYLTKP 102
PRK11517 PRK11517
DNA-binding response regulator HprR;
789-891 5.43e-10

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 60.68  E-value: 5.43e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDAtrrIRALPGGAAIPIVALT 868
Cdd:PRK11517    2 KILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYLALKDDYALIILDIMLPGMDGWQI---LQTLRTAKQTPVICLT 78
                          90       100
                  ....*....|....*....|...
gi 1308984722 869 ANAYSEDRQRCLAAGMNDFLAKP 891
Cdd:PRK11517   79 ARDSVDDRVRGLDSGANDYLVKP 101
PRK10490 PRK10490
sensor protein KdpD; Provisional
541-773 5.47e-10

sensor protein KdpD; Provisional


Pssm-ID: 236701 [Multi-domain]  Cd Length: 895  Bit Score: 63.52  E-value: 5.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 541 KSAFLANMSHEIRTPMNAIIGLNYLLLKSpLEPAQRDKLLKVTSASEHLL---QVINDILDLSKIESGKLELENQTFDPR 617
Cdd:PRK10490  664 RNALLAALSHDLRTPLTVLFGQAEILTLD-LASEGSPHARQASEIRQQVLnttRLVNNLLDMARIQSGGFNLRKEWLTLE 742
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 618 EVLQAAAavirdQALGKGLL---VGVDggkLPA---LAIGDAKRLRQVLINFAGNALKFtrAGSIHLSGELLANDGENVt 691
Cdd:PRK10490  743 EVVGSAL-----QMLEPGLSghpINLS---LPEpltLIHVDGPLFERVLINLLENAVKY--AGAQAEIGIDAHVEGERL- 811
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 692 cRFVVSDTGLGIRPEDVPRLFKPFEQLDASTTrqYGGTGLGLAIARHLAHLMDGEVGVDSTPGQGSSFWITARLKAaglP 771
Cdd:PRK10490  812 -QLDVWDNGPGIPPGQEQLIFDKFARGNKESA--IPGVGLGLAICRAIVEVHGGTIWAENRPEGGACFRVTLPLET---P 885

                  ..
gi 1308984722 772 PE 773
Cdd:PRK10490  886 PE 887
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
789-891 8.08e-10

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: 56.74  E-value: 8.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGG-FDLILMDIQMPGLDGLDATRRIRALpgGAAIPIVAL 867
Cdd:cd18160     1 TILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQQGKdIDIVVTDIVMPEMDGIELAREARKI--DPDVKILFI 78
                          90       100
                  ....*....|....*....|....
gi 1308984722 868 TANAYSEDRQRCLAAGMNDFLAKP 891
Cdd:cd18160    79 SGGAAAAPELLSDAVGDNATLKKP 102
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
790-897 9.32e-10

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


Pssm-ID: 381114 [Multi-domain]  Cd Length: 121  Bit Score: 57.21  E-value: 9.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 790 VLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRI--RALPggaaIPIVAL 867
Cdd:cd17572     1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIqeRSLP----TSVIVI 76
                          90       100       110
                  ....*....|....*....|....*....|
gi 1308984722 868 TANAYSEDRQRCLAAGMNDFLAKPVDPEAL 897
Cdd:cd17572    77 TAHGSVDIAVEAMRLGAYDFLEKPFDADRL 106
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
789-894 9.86e-10

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 59.98  E-value: 9.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALPggAAIPIVALT 868
Cdd:PRK11083    5 TILLVEDEQAIADTLVYALQSEGFTVEWFERGLPALDKLRQQPPDLVILDVGLPDISGFELCRQLLAFH--PALPVIFLT 82
                          90       100
                  ....*....|....*....|....*.
gi 1308984722 869 ANAYSEDRQRCLAAGMNDFLAKPVDP 894
Cdd:PRK11083   83 ARSDEVDRLVGLEIGADDYVAKPFSP 108
envZ PRK09467
osmolarity sensor protein; Provisional
545-756 1.07e-09

osmolarity sensor protein; Provisional


Pssm-ID: 236531 [Multi-domain]  Cd Length: 435  Bit Score: 61.85  E-value: 1.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 545 LANMSHEIRTP----------------------------MNAIIG--LNYLLL--KSPLEPAQrdkllkvtsasehllqv 592
Cdd:PRK09467  233 MAGVSHDLRTPltrirlatemmseedgylaesinkdieeCNAIIEqfIDYLRTgqEMPMEMAD----------------- 295
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 593 INDILdlskiesgklelenqtfdpREVLQAAAavirdqalGKGLLVGVDGGKLPALAIGDAKRLRQVLINFAGNALKFTR 672
Cdd:PRK09467  296 LNALL-------------------GEVIAAES--------GYEREIETALQPGPIEVPMNPIAIKRALANLVVNAARYGN 348
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 673 aGSIHLSgelLANDGENVtcRFVVSDTGLGIRPEDVPRLFKPFEQLDasTTRQYGGTGLGLAIARHLAHLMDGEVGVDST 752
Cdd:PRK09467  349 -GWIKVS---SGTEGKRA--WFQVEDDGPGIPPEQLKHLFQPFTRGD--SARGSSGTGLGLAIVKRIVDQHNGKVELGNS 420

                  ....
gi 1308984722 753 PGQG 756
Cdd:PRK09467  421 EEGG 424
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
789-892 1.19e-09

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 61.05  E-value: 1.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDEPLNREIGCDLLA-ATGLEVA-TADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALpggAAIPIVA 866
Cdd:PRK12555    2 RIGIVNDSPLAVEALRRALArDPDHEVVwVATDGAQAVERCAAQPPDVILMDLEMPRMDGVEATRRIMAE---RPCPILI 78
                          90       100
                  ....*....|....*....|....*...
gi 1308984722 867 LTAN--AYSEDRQRCLAAGMNDFLAKPV 892
Cdd:PRK12555   79 VTSLteRNASRVFEAMGAGALDAVDTPT 106
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
789-891 1.45e-09

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 60.93  E-value: 1.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDEPLNREIGCDLLAAT-GLEV-ATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRAL-PggaaIPIV 865
Cdd:PRK00742    5 RVLVVDDSAFMRRLISEILNSDpDIEVvGTAPDGLEAREKIKKLNPDVITLDVEMPVMDGLDALEKIMRLrP----TPVV 80
                          90       100
                  ....*....|....*....|....*....
gi 1308984722 866 ---ALTANAySEDRQRCLAAGMNDFLAKP 891
Cdd:PRK00742   81 mvsSLTERG-AEITLRALELGAVDFVTKP 108
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
790-897 1.80e-09

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: 56.20  E-value: 1.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 790 VLLVEDEPLNREIGCDLL--AATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRAlpGGAAIPIVAL 867
Cdd:cd19931     1 VLLIDDHPLLRKGIKQLIelDPDFTVVGEASSGEEGIELAERLDPDLILLDLNMKGMSGLDTLKALRE--EGVSARIVIL 78
                          90       100       110
                  ....*....|....*....|....*....|
gi 1308984722 868 TANAYSEDRQRCLAAGMNDFLAKPVDPEAL 897
Cdd:cd19931    79 TVSDAEDDVVTALRAGADGYLLKDMEPEDL 108
HATPase_ETR2_ERS2-EIN4-like cd16938
Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related ...
645-759 1.93e-09

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: 56.70  E-value: 1.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 645 LPALAIGDAKRLRQVLINFAGNALKFTR-AGSIHL-----SGELLANDGENVTCRFVVSDTGLGIR------PEDVPRLF 712
Cdd:cd16938     1 LPDVVVGDERRVFQVLLHMLGNLLKMRNgGGNITFrvfleGGSEDRSDRDWGPWRPSMSDESVEIRfeveinDSGSPSIE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1308984722 713 KPFeqLDASTTRQYG----GTGLGLAIARHLAHLMDGEVGVDSTPGQGSSF 759
Cdd:cd16938    81 SAS--MRNSLNRRYNlselGEHLSFSICKQLVQLMGGNIWIVPGSGLGTTM 129
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
790-891 3.05e-09

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: 55.14  E-value: 3.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 790 VLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALpggAAIPIVALTA 869
Cdd:cd19936     1 IALVDDDRNILTSVSMALEAEGFSVETYTDGASALDGLNARPPDLAILDIKMPRMDGMELLQRLRQK---STLPVIFLTS 77
                          90       100
                  ....*....|....*....|..
gi 1308984722 870 NAYSEDRQRCLAAGMNDFLAKP 891
Cdd:cd19936    78 KDDEIDEVFGLRMGADDYITKP 99
HATPase_Glnl-NtrB-like cd16918
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
656-754 3.22e-09

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: 55.48  E-value: 3.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 656 LRQVLINFAGNALKFT--RAGSIHLS-----GELLANDGENVTCRFVVSDTGLGIRPEDVPRLFKPFeqldaSTTRQyGG 728
Cdd:cd16918     1 LIQVFLNLVRNAAQALagSGGEIILRtrtqrQVTLGHPRHRLALRVSVIDNGPGIPPDLQDTIFYPM-----VSGRE-NG 74
                          90       100
                  ....*....|....*....|....*.
gi 1308984722 729 TGLGLAIARHLAHLMDGEVGVDSTPG 754
Cdd:cd16918    75 TGLGLAIAQNIVSQHGGVIECDSQPG 100
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
789-906 3.43e-09

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


Pssm-ID: 381113 [Multi-domain]  Cd Length: 118  Bit Score: 55.49  E-value: 3.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRAL-PggAAIPIVaL 867
Cdd:cd17569     2 TILLVDDEPNILKALKRLLRREGYEVLTATSGEEALEILKQEPVDVVISDQRMPGMDGAELLKRVRERyP--DTVRIL-L 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1308984722 868 TANAyseDRQRCLAAgMND-----FLAKPVDPEALYTILGKYLA 906
Cdd:cd17569    79 TGYA---DLDAAIEA-INEgeiyrFLTKPWDDEELKETIRQALE 118
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
366-762 3.66e-09

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 59.86  E-value: 3.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 366 IETLNNQLAERLAALEIAEqdLRRLSTAVEQS-PASIVITDINARITYVNLAFCVTSGYfpdEVIGENPRILqsgntppa 444
Cdd:COG3290    63 LLLLLLAALLLKLLEEIAR--LVEEREAVLESiREGVIAVDRDGRITLINDAARRLLGL---DAIGRPIDEV-------- 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 445 tyqaMWQTLTAGEIWRGELVNRRkdgshyIERATISPVRgSDGTTSQYVAVKEDISDQRRIEEELAAHRQHLQQLVDQRt 524
Cdd:COG3290   130 ----LAEVLETGERDEEILLNGR------VLVVNRVPIR-DDGRVVGAVATFRDRTELERLEEELEGVKELAEALRAQR- 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 525 gelaqataaaesanlaksaflanmsHEIRTPMNAIIGLnyLLLKSPlepaqrdkllkvtsasEHLLQVINDILDLSKIES 604
Cdd:COG3290   198 -------------------------HDFRNHLHTISGL--LQLGEY----------------DEALEYIDEISEELQELI 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 605 GKLELENQTFDPREVLQAAAAvirdQALGKGLLVGVD-GGKLPALAIGDAKrLRQVLINFAGNAL-----KFTRAGSIHL 678
Cdd:COG3290   235 DSLLSRIGNPVLAALLLGKAA----RARERGIDLTIDiDSDLPDLPLSDTD-LVTILGNLLDNAIeavekLPEEERRVEL 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 679 SgeLLANDGEnvtCRFVVSDTGLGIRPEDVPRLFKP-FeqldasTTRQYGGTGLGLAIARHLAHLMDGEVGVDSTPGQGS 757
Cdd:COG3290   310 S--IRDDGDE---LVIEVEDSGPGIPEELLEKIFERgF------STKLGEGRGLGLALVKQIVEKYGGTIEVESEEGEGT 378

                  ....*
gi 1308984722 758 SFWIT 762
Cdd:COG3290   379 VFTVR 383
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
397-499 3.79e-09

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: 54.95  E-value: 3.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 397 SPASIVITDINARITYVNLAFCVTSGYFPDEVIGENPRILQSGNTPPATYQAMWQTLTAGEIWRGELVNRRKDGSHYIER 476
Cdd:cd00130     1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVL 80
                          90       100
                  ....*....|....*....|...
gi 1308984722 477 ATISPVRGSDGTTSQYVAVKEDI 499
Cdd:cd00130    81 VSLTPIRDEGGEVIGLLGVVRDI 103
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
656-761 4.04e-09

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: 55.46  E-value: 4.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 656 LRQVLINFAGNALK-FTRAGSIHL--SGELLANDGENVTCR--------FVVSDTGLGIRPEDVPRLFKPFeqldaSTTR 724
Cdd:cd16919     1 LELAILNLAVNARDaMPEGGRLTIetSNQRVDADYALNYRDlipgnyvcLEVSDTGSGMPAEVLRRAFEPF-----FTTK 75
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1308984722 725 QYG-GTGLGLAIARHLAHLMDGEVGVDSTPGQGSSFWI 761
Cdd:cd16919    76 EVGkGTGLGLSMVYGFVKQSGGHLRIYSEPGVGTTVRI 113
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
656-759 5.42e-09

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


Pssm-ID: 340435 [Multi-domain]  Cd Length: 102  Bit Score: 54.39  E-value: 5.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 656 LRQVLINFAGNAL----KFTRaGSIHLSGELLANDGEnvtcrFVVSDTGLGIRPEDVPRLFKPFeqldaSTTRQYG-GTG 730
Cdd:cd16976     1 IQQVLMNLLQNALdamgKVEN-PRIRIAARRLGGRLV-----LVVRDNGPGIAEEHLSRVFDPF-----FTTKPVGkGTG 69
                          90       100
                  ....*....|....*....|....*....
gi 1308984722 731 LGLAIARHLAHLMDGEVGVDSTPGQGSSF 759
Cdd:cd16976    70 LGLSISYGIVEEHGGRLSVANEEGAGARF 98
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
790-897 5.64e-09

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


Pssm-ID: 381157 [Multi-domain]  Cd Length: 117  Bit Score: 54.97  E-value: 5.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 790 VLLVEDEPLNREIGCDLLaatGLE-----VATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRAlpGGAAIPI 864
Cdd:cd19930     1 VLIAEDQEMVRGALAALL---ELEddlevVAQASNGQEALRLVLKHSPDVAILDIEMPGRTGLEVAAELRE--ELPDTKV 75
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1308984722 865 VALTANAYSEDRQRCLAAGMNDFLAKPVDPEAL 897
Cdd:cd19930    76 LIVTTFGRPGYFRRALAAGVDGYVLKDRPIEEL 108
PRK10766 PRK10766
two-component system response regulator TorR;
789-897 8.50e-09

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 56.97  E-value: 8.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRAlpgGAAIPIVALT 868
Cdd:PRK10766    4 HILVVEDEPVTRARLQGYFEQEGYTVSEAASGAGMREIMQNQHVDLILLDINLPGEDGLMLTRELRS---RSTVGIILVT 80
                          90       100
                  ....*....|....*....|....*....
gi 1308984722 869 ANAYSEDRQRCLAAGMNDFLAKPVDPEAL 897
Cdd:PRK10766   81 GRTDSIDRIVGLEMGADDYVTKPLELREL 109
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
790-891 1.08e-08

pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response regulators (PRRs), also called APRRs, comprise a core group of clock components that controls the pace of the central oscillator of the circadian clock, an endogenous time-keeping mechanism that enables organisms to adapt to external daily cycles. The coordinated sequential expression of PRR9 (APRR9), PRR7 (APRR7), PRR5 (APRR5), PRR3 (APRR3), and PRR1 (APRR1) results in circadian waves that may be at the basis of the endogenous circadian clock. PRRs contain an N-terminal pseudo receiver (psREC) domain that resembles the receiver domain of a two-component response regulator, but lacks an aspartate residue that accepts a phosphoryl group from the sensor kinase, and a CCT motif at the C-terminus that contains a putative nuclear localization signal. The psREC domain is involved in protein-protein interactions.


Pssm-ID: 381120 [Multi-domain]  Cd Length: 104  Bit Score: 53.56  E-value: 1.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 790 VLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGF--DLILMDIQMPGLDGLDATRRIRALPGGAAIPIVAL 867
Cdd:cd17582     1 VLLVENDDSTRQIVTALLRKCSYEVTAASDGLQAWDVLEDEQNeiDLILTEVDLPVSSGFKLLSYIMRHKICKNIPVIMM 80
                          90       100
                  ....*....|....*....|....
gi 1308984722 868 TANAYSEDRQRCLAAGMNDFLAKP 891
Cdd:cd17582    81 SSQDSVGVVFKCLSKGAADYLVKP 104
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
790-897 1.11e-08

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: 54.14  E-value: 1.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 790 VLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALpgGAAIPIVALTA 869
Cdd:cd17537     3 VYVVDDDEAVRDSLAFLLRSVGLAVKTFTSASAFLAAAPPDQPGCLVLDVRMPGMSGLELQDELLAR--GSNIPIIFITG 80
                          90       100
                  ....*....|....*....|....*...
gi 1308984722 870 NAYSEDRQRCLAAGMNDFLAKPVDPEAL 897
Cdd:cd17537    81 HGDVPMAVEAMKAGAVDFLEKPFRDQVL 108
PRK10755 PRK10755
two-component system sensor histidine kinase PmrB;
544-746 1.79e-08

two-component system sensor histidine kinase PmrB;


Pssm-ID: 236751 [Multi-domain]  Cd Length: 356  Bit Score: 57.67  E-value: 1.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 544 FLANMSHEIRTPMnAIIGLNyLLLKSPLEPAQRDKLLKVTsasEHLLQVINDILDLSKIE----SG---KLELENQTFDP 616
Cdd:PRK10755  140 FTADVAHELRTPL-AGIRLH-LELLEKQHHIDVAPLIARL---DQMMHTVEQLLQLARAGqsfsSGhyqTVKLLEDVILP 214
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 617 -REVLQAAAAViRDQALGkgllvgVDGGKLPALAIGDAKRLRQVLINFAGNALKFTRAGS---IHLSgelLANDGenvtC 692
Cdd:PRK10755  215 sQDELSEMLEQ-RQQTLL------LPESAADITVQGDATLLRLLLRNLVENAHRYSPEGStitIKLS---QEDGG----A 280
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1308984722 693 RFVVSDTGLGIRPEDVPRLFKPFEQLDasttRQYGGTGLGLAIARHLAHLMDGE 746
Cdd:PRK10755  281 VLAVEDEGPGIDESKCGELSKAFVRMD----SRYGGIGLGLSIVSRITQLHHGQ 330
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
790-893 2.00e-08

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


Pssm-ID: 381125 [Multi-domain]  Cd Length: 113  Bit Score: 53.22  E-value: 2.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 790 VLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRAlpgGAAIPIVALTA 869
Cdd:cd17594     2 VLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRTIRA---RSDVPIIIISG 78
                          90       100
                  ....*....|....*....|....*
gi 1308984722 870 NAYSE-DRQRCLAAGMNDFLAKPVD 893
Cdd:cd17594    79 DRRDEiDRVVGLELGADDYLAKPFG 103
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
789-904 2.10e-08

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: 53.40  E-value: 2.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDEPLNREIGCDLLAAT-GLEV-ATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRAlpGGAAIPIVA 866
Cdd:cd19925     2 NVLIVEDDPMVAEIHRAYVEQVpGFTViGTAGTGEEALKLLKERQPDLILLDIYLPDGNGLDLLRELRA--AGHDVDVIV 79
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1308984722 867 LTANAYSEDRQRCLAAGMNDFLAKPVDPEALYTILGKY 904
Cdd:cd19925    80 VTAANDVETVREALRLGVVDYLIKPFTFERLRQRLERY 117
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
789-904 2.38e-08

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


Pssm-ID: 381086 [Multi-domain]  Cd Length: 123  Bit Score: 53.21  E-value: 2.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDEPLNREIGCDLLAATG-LEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALPGGAAIPIV-A 866
Cdd:cd17530     2 RVLVLDDDPFQCMMAATILEDLGpGNVDEADDGREALVILLCNAPDIIICDLKMPDMDGIEFLRHLAESHSNAAVILMsG 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1308984722 867 LTANAYSEDRQRCLAAGMN--DFLAKPVDPEALYTILGKY 904
Cdd:cd17530    82 LDGGILESAETLAGANGLNllGTLSKPFSPEELTELLTKY 121
PDC1_HK_sensor cd18773
first PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins, diguanylate-cyclase ...
56-170 2.63e-08

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: 53.33  E-value: 2.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722  56 EAALRQVREMLHIMAGADNMRSLDADDCSGLAKRLLSVTHDIANIGAALANGDVFCSAHPITRPVNVAD---RPWFQEAL 132
Cdd:cd18773     2 EEADLLLRSLASALEALAALGSADREELQALLRRLLERNPEISGIYVVDADGRVVASSDRDPGGGDDDDdrdRFWYQAAK 81
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1308984722 133 TATDITSGHYQTGLISGKRGITIGLPVRDAEGKLQAAL 170
Cdd:cd18773    82 ATGKLVISEPYISRVTGKPVITLSRPIRDADGRFIGVV 119
COG4192 COG4192
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...
496-752 2.87e-08

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


Pssm-ID: 443346 [Multi-domain]  Cd Length: 640  Bit Score: 57.77  E-value: 2.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 496 KEDISDQRRIEEELAAHRQHLQQ-----LVDQRTGELaqataaaesanlaksaflanmSHEIRTPMNAIIGLNYLLLKSp 570
Cdd:COG4192   404 ETEIEERKRIEKNLRQTQDELIQaakmaVVGQTMTSL---------------------AHELNQPLNAMSMYLFSAKKA- 461
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 571 LEPAQRDKLLKVTSASEHLLQVINDILDLSKIESGKLELENQTFDPREVLQAAAAVIRDQALGKGLLVGVDGgklPALAI 650
Cdd:COG4192   462 LEQENYAQLPTSLDKIEGLIERMDKIIKSLRQFSRKSDTPLQPVDLRQVIEQAWELVESRAKPQQITLHIPD---DLMVQ 538
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 651 GDAKRLRQVLINFAGNALKfTRAGSIHLSGELLANDGenvTCRFVVSDTGLGIrpEDVPRLFKPFeqldasTTRQYGGTG 730
Cdd:COG4192   539 GDQVLLEQVLVNLLVNALD-AVATQPQISVDLLSNAE---NLRVAISDNGNGW--PLVDKLFTPF------TTTKEVGLG 606
                         250       260
                  ....*....|....*....|..
gi 1308984722 731 LGLAIARHLAHLMDGEVGVDST 752
Cdd:COG4192   607 LGLSICRSIMQQFGGDLYLAST 628
PRK10403 PRK10403
nitrate/nitrite response regulator protein NarP;
789-897 3.00e-08

nitrate/nitrite response regulator protein NarP;


Pssm-ID: 182431 [Multi-domain]  Cd Length: 215  Bit Score: 55.24  E-value: 3.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDEPLNREIGCDLLAA-TGLEV-ATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRAlpGGAAIPIVA 866
Cdd:PRK10403    8 QVLIVDDHPLMRRGVRQLLELdPGFEVvAEAGDGASAIDLANRLDPDVILLDLNMKGMSGLDTLNALRR--DGVTAQIII 85
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1308984722 867 LTANAYSEDRQRCLAAGMNDFLAKPVDPEAL 897
Cdd:PRK10403   86 LTVSDASSDVFALIDAGADGYLLKDSDPEVL 116
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
384-514 3.33e-08

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


Pssm-ID: 443041 [Multi-domain]  Cd Length: 448  Bit Score: 57.09  E-value: 3.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 384 EQDLRRLSTAVEQSPASIVITDINARITYVNLAFCVTSGYFPDEVIGENPRILqSGNTPpatyqaMWQTLTAGEIWRGEL 463
Cdd:COG3829     7 KELEEELEAILDSLDDGIIVVDADGRITYVNRAAERILGLPREEVIGKNVTEL-IPNSP------LLEVLKTGKPVTGVI 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1308984722 464 VNRRKDGSHYIerATISPVRgSDGTTSQYVAVKEDISDQRRIEEELAAHRQ 514
Cdd:COG3829    80 QKTGGKGKTVI--VTAIPIF-EDGEVIGAVETFRDITELKRLERKLREEEL 127
PEP_his_kin TIGR02916
putative PEP-CTERM system histidine kinase; Members of this protein family have a novel ...
575-759 3.74e-08

putative PEP-CTERM system histidine kinase; Members of this protein family have a novel N-terminal domain, a single predicted membrane-spanning helix, and a predicted cystosolic histidine kinase domain. We designate this protein PrsK, and its companion DNA-binding response regulator protein (TIGR02915) PrsR. These predicted signal-transducing proteins appear to enable enhancer-dependent transcriptional activation. The prsK gene is often associated with exopolysaccharide biosynthesis genes. [Protein fate, Protein and peptide secretion and trafficking, Signal transduction, Two-component systems]


Pssm-ID: 274349 [Multi-domain]  Cd Length: 679  Bit Score: 57.42  E-value: 3.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 575 QRDKLLKVTSASEHLLQVindildLSKIESGKLELENQTFDPREVLQAAAAvirdQALGKGLLVGVDGGklPALAI-GDA 653
Cdd:TIGR02916 510 QDDMLETVENAVNRMKKL------LAQLRSKGLEEEKLCVDLVDLLRRAIA----SKRAQGPRPEVSID--TDLSVrADR 577
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 654 KRLRQVLINFAGNALKFT-RAGSIHLSgelLANDGENVtcRFVVSDTGLGIRPEDV-PRLFKPFEqldastTRQYGGTGL 731
Cdd:TIGR02916 578 ERLERVLGHLVQNALEATpGEGRVAIR---VERECGAA--RIEIEDSGCGMSPAFIrERLFKPFD------TTKGAGMGI 646
                         170       180
                  ....*....|....*....|....*...
gi 1308984722 732 GLAIARHLAHLMDGEVGVDSTPGQGSSF 759
Cdd:TIGR02916 647 GVYECRQYVEEIGGRIEVESTPGQGTIF 674
PRK15115 PRK15115
response regulator GlrR; Provisional
789-906 4.28e-08

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 56.77  E-value: 4.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDEP-LNREIGCDLlAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALPGGaaIPIVAL 867
Cdd:PRK15115    7 HLLLVDDDPgLLKLLGMRL-TSEGYSVVTAESGQEALRVLNREKVDLVISDLRMDEMDGMQLFAEIQKVQPG--MPVIIL 83
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1308984722 868 TANAYSEDRQRCLAAGMNDFLAKPVDPEALYTILGKYLA 906
Cdd:PRK15115   84 TAHGSIPDAVAATQQGVFSFLTKPVDRDALYKAIDDALE 122
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
789-897 4.82e-08

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 54.81  E-value: 4.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDEplnREIGC---DLLAATGLEVATADDGFAAIARFQEGgFDLILMDIQMPGLDGLDATRRIRAlpgGAAIPIV 865
Cdd:PRK10955    3 KILLVDDD---RELTSllkELLEMEGFNVIVAHDGEQALDLLDDS-IDLLLLDVMMPKKNGIDTLKELRQ---THQTPVI 75
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1308984722 866 ALTANAYSEDRQRCLAAGMNDFLAKPVDPEAL 897
Cdd:PRK10955   76 MLTARGSELDRVLGLELGADDYLPKPFNDREL 107
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
790-891 5.00e-08

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


Pssm-ID: 381153 [Multi-domain]  Cd Length: 100  Bit Score: 51.77  E-value: 5.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 790 VLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRA-LPGgaaIPIVALT 868
Cdd:cd19926     1 VLVVDDEPDIRELLEITLGRMGLDVRSARNVKEARELLASEPYDLCLTDMRLPDGSGLELVQHIQQrLPQ---TPVAVIT 77
                          90       100
                  ....*....|....*....|...
gi 1308984722 869 ANAYSEDRQRCLAAGMNDFLAKP 891
Cdd:cd19926    78 AYGSLDTAIEALKAGAFDFLTKP 100
fixJ PRK09390
response regulator FixJ; Provisional
788-897 5.84e-08

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 54.24  E-value: 5.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 788 GRVLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALpgGAAIPIVAL 867
Cdd:PRK09390    4 GVVHVVDDDEAMRDSLAFLLDSAGFEVRLFESAQAFLDALPGLRFGCVVTDVRMPGIDGIELLRRLKAR--GSPLPVIVM 81
                          90       100       110
                  ....*....|....*....|....*....|
gi 1308984722 868 TANAYSEDRQRCLAAGMNDFLAKPVDPEAL 897
Cdd:PRK09390   82 TGHGDVPLAVEAMKLGAVDFIEKPFEDERL 111
PRK10643 PRK10643
two-component system response regulator PmrA;
789-891 8.47e-08

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 53.89  E-value: 8.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDeplnreigcDLLAATGLEVATADDGFA---------AIARFQEGGFDLILMDIQMPGLDGLDATRRIRAlpGG 859
Cdd:PRK10643    2 KILIVED---------DTLLLQGLILALQTEGYAcdcastareAEALLESGHYSLVVLDLGLPDEDGLHLLRRWRQ--KK 70
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1308984722 860 AAIPIVALTANAYSEDRQRCLAAGMNDFLAKP 891
Cdd:PRK10643   71 YTLPVLILTARDTLEDRVAGLDVGADDYLVKP 102
PRK11697 PRK11697
two-component system response regulator BtsR;
789-897 8.99e-08

two-component system response regulator BtsR;


Pssm-ID: 236956 [Multi-domain]  Cd Length: 238  Bit Score: 54.08  E-value: 8.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDEPLNREIGCDLLAATG-LEV----ATADDGFAAIARFQEggfDLILMDIQMPGLDG------LDATRRIRalp 857
Cdd:PRK11697    3 KVLIVDDEPLAREELRELLQEEGdIEIvgecSNAIEAIGAIHRLKP---DVVFLDIQMPRISGlelvgmLDPEHMPY--- 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1308984722 858 ggaaipIVALTA------NAYSEDrqrclAAgmnDFLAKPVDPEAL 897
Cdd:PRK11697   77 ------IVFVTAfdeyaiKAFEEH-----AF---DYLLKPIDPARL 108
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
410-495 1.46e-07

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: 50.03  E-value: 1.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 410 ITYVNLAFCVTSGYFPDEVIGENPRILQS--GNTPPATYQAMWQTLTAGEIWRGELVNRRKDGSHYIERATISPVRGSDG 487
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELLGKGESWLDLvhPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDENG 80

                  ....*...
gi 1308984722 488 TTSQYVAV 495
Cdd:pfam08447  81 KPVRVIGV 88
REC_WspR-like cd17575
phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The ...
789-894 1.47e-07

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: 51.25  E-value: 1.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDEPLNREIGCDLLAA-TGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALPGGAAIPIVAL 867
Cdd:cd17575     2 MVLLVDDQAIIGEAVRRALADeEDIDFHYCSDPTEAIEVASQIKPTVILQDLVMPGVDGLTLVRFFRANPATRDIPIIVL 81
                          90       100
                  ....*....|....*....|....*..
gi 1308984722 868 TANAYSEDRQRCLAAGMNDFLAKPVDP 894
Cdd:cd17575    82 STKEEPEVKSEAFALGANDYLVKLPDK 108
PDC2_DGC_like cd12915
second PDC (PhoQ/DcuS/CitA) domain of diguanylate-cyclase and similar domains; Members of this ...
178-275 2.25e-07

second PDC (PhoQ/DcuS/CitA) domain of diguanylate-cyclase and similar domains; Members of this subfamily display varying domain architectures but all contain double PDC (PhoQ/DcuS/CitA) sensor domains. This model represents the second PDC domain of Diguanylate-cyclases (DGCs), Histidine kinases (HKs), and other similar domains. Many members of this subfamily contain a C-terminal DGC (also called GGDEF) domain. DGCs regulate the turnover of cyclic diguanosine monophosphate. 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. In the case of HKs, 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.


Pssm-ID: 350340 [Multi-domain]  Cd Length: 96  Bit Score: 49.66  E-value: 2.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 178 WFDRISRNQQLPKGWTSLLVTDDGSVVSRHPDPDIWRGSAFDAASRERLLAALRHDDDRVVMnGLDGIERLYLLQRLqiA 257
Cdd:cd12915     1 YFSRLYRSLDLGPGGAVALLRRDGTVLARYPDDEGAVGRSLADPLFRALLAAAPSGTFRAVS-PLDGVERLYAYRRL--P 77
                          90
                  ....*....|....*...
gi 1308984722 258 DGHLVAAIGAPVNETLHA 275
Cdd:cd12915    78 GYPLVVVVGLSEDDVLAP 95
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
790-897 3.43e-07

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


Pssm-ID: 381143 [Multi-domain]  Cd Length: 113  Bit Score: 49.59  E-value: 3.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 790 VLLVED-EPLNREIGcDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALpggAAIPIVALT 868
Cdd:cd18159     1 ILIVEDdETIASLLK-KHLEKWGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYFDGFYWCREIRQI---SNVPIIFIS 76
                          90       100
                  ....*....|....*....|....*....
gi 1308984722 869 ANAYSEDRQRCLAAGMNDFLAKPVDPEAL 897
Cdd:cd18159    77 SRDDNMDQVMAINMGGDDYITKPFDLDVL 105
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
790-897 3.43e-07

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


Pssm-ID: 381115 [Multi-domain]  Cd Length: 110  Bit Score: 49.74  E-value: 3.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 790 VLLVEDE-PLNREIGcDLLAATGLEVATAD---DG--FAAIARFqeggfDLILMDIQMPGLDGLDATRRIRAlpGGAAIP 863
Cdd:cd17573     1 ILLIEDDsTLGKEIS-KGLNEKGYQADVAEslkDGeyYIDIRNY-----DLVLVSDKLPDGNGLSIVSRIKE--KHPSIV 72
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1308984722 864 IVALTANAYSEDRQRCLAAGMNDFLAKPVDPEAL 897
Cdd:cd17573    73 VIVLSDNPKTEQEIEAFKEGADDYIAKPFDFKVL 106
PLN03029 PLN03029
type-a response regulator protein; Provisional
790-892 3.76e-07

type-a response regulator protein; Provisional


Pssm-ID: 215544 [Multi-domain]  Cd Length: 222  Bit Score: 51.96  E-value: 3.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 790 VLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIaRF---------------------QEGGFDLILMDIQMPGLDGLD 848
Cdd:PLN03029   11 VLAVDDSLIDRKLIEKLLKTSSYQVTTVDSGSKAL-KFlglheddrsnpdtpsvspnshQEVEVNLIITDYCMPGMTGYD 89
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1308984722 849 ATRRIRALPGGAAIPIVALTANAYSEDRQRCLAAGMNDFLAKPV 892
Cdd:PLN03029   90 LLKKIKESSSLRNIPVVIMSSENVPSRITRCLEEGAEEFFLKPV 133
psREC-like_D2_PleD cd17539
REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with ...
790-897 4.05e-07

REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with the phosphorylatable aspartate, a pseudo receiver (psREC)-like adaptor domain (D2), and the enzymatic diguanylate cyclase (DGC) domain, also called the GGDEF domain according to a conserved sequence motif, as its output domain. The GGDEF-containing PleD response regulators are global regulators of cell metabolism in some important human pathogens. This model describes the REC-like adaptor domain D2 of PleD, which is an inactive domain.


Pssm-ID: 381094 [Multi-domain]  Cd Length: 124  Bit Score: 49.62  E-value: 4.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 790 VLLVEDEPLNRE-IGCDLLAATGLEVATadDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALPGGAAIPIVALt 868
Cdd:cd17539     1 VLLVDDRPSSAErIAAMLSSEHEVVVEA--DPDEALFRAAEGPFDLVIVSLALEDFDGLRLCSQLRSLERTRQLPILAV- 77
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1308984722 869 anAYSEDRQRCLAA---GMNDFLAKPVDPEAL 897
Cdd:cd17539    78 --ADPGDRGRLIRAleiGVNDYLVRPIDPNEL 107
PRK11173 PRK11173
two-component response regulator; Provisional
789-900 6.07e-07

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 51.55  E-value: 6.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRAlpgGAAIPIVALT 868
Cdd:PRK11173    5 HILIVEDELVTRNTLKSIFEAEGYDVFEATDGAEMHQILSENDINLVIMDINLPGKNGLLLARELRE---QANVALMFLT 81
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1308984722 869 ANAYSEDRQRCLAAGMNDFLAKPVDPEALyTI 900
Cdd:PRK11173   82 GRDNEVDKILGLEIGADDYITKPFNPREL-TI 112
PRK10816 PRK10816
two-component system response regulator PhoP;
789-891 6.45e-07

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 51.28  E-value: 6.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRAlpGGAAIPIVALT 868
Cdd:PRK10816    2 RVLVVEDNALLRHHLKVQLQDAGHQVDAAEDAKEADYYLNEHLPDIAIVDLGLPDEDGLSLIRRWRS--NDVSLPILVLT 79
                          90       100
                  ....*....|....*....|...
gi 1308984722 869 ANAYSEDRQRCLAAGMNDFLAKP 891
Cdd:PRK10816   80 ARESWQDKVEVLSAGADDYVTKP 102
HATPase_VanS-like cd16923
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
656-746 6.72e-07

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: 48.54  E-value: 6.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 656 LRQVLINFAGNALKFTRAGS-IHLSgelLANDGENVTCRFvvSDTGLGIRPEDVPRLFKPFEQLDASttRQYGGTGLGLA 734
Cdd:cd16923     1 LQRVFSNLLSNAIKYSPENTrIYIT---SFLTDDVVNIMF--KNPSSHPLDFKLEKLFERFYRGDNS--RNTEGAGLGLS 73
                          90
                  ....*....|..
gi 1308984722 735 IARHLAHLMDGE 746
Cdd:cd16923    74 IAKAIIELHGGS 85
HATPase_CreC-like cd16945
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
652-759 9.16e-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: 48.23  E-value: 9.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 652 DAKRLRQVLINFAGNALKFTRA-GSIHLSGELlanDGENVTCRfvVSDTGLGIRPEDVPRLFKPFEQLDASTTRQYGgTG 730
Cdd:cd16945     1 DPFLLRQAINNLLDNAIDFSPEgGLIALQLEA---DTEGIELL--VFDEGSGIPDYALNRVFERFYSLPRPHSGQKS-TG 74
                          90       100
                  ....*....|....*....|....*....
gi 1308984722 731 LGLAIARHLAHLMDGEVGVDSTPGQGSSF 759
Cdd:cd16945    75 LGLAFVQEVAQLHGGRITLRNRPDGVLAF 103
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
790-892 1.46e-06

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


Pssm-ID: 381145 [Multi-domain]  Cd Length: 102  Bit Score: 47.73  E-value: 1.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 790 VLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGG-FDLILMDIQMPG-LDGLDATRRIRALpgGAAIPIVAL 867
Cdd:cd18161     1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLESGPdIDLLVTDVIMPGgMNGSQLAEEARRR--RPDLKVLLT 78
                          90       100
                  ....*....|....*....|....*
gi 1308984722 868 TANAYSEDRQRCLAAGMnDFLAKPV 892
Cdd:cd18161    79 SGYAENAIEGGDLAPGV-DVLSKPF 102
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
790-891 1.55e-06

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 50.19  E-value: 1.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 790 VLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALpggAAIPIVALTA 869
Cdd:PRK10529    4 VLIVEDEQAIRRFLRTALEGDGMRVFEAETLQRGLLEAATRKPDLIILDLGLPDGDGIEFIRDLRQW---SAIPVIVLSA 80
                          90       100
                  ....*....|....*....|..
gi 1308984722 870 NAYSEDRQRCLAAGMNDFLAKP 891
Cdd:PRK10529   81 RSEESDKIAALDAGADDYLSKP 102
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
789-891 1.59e-06

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


Pssm-ID: 381109 [Multi-domain]  Cd Length: 108  Bit Score: 47.60  E-value: 1.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDeplNREIgCDLLAA-----TGLEV-ATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALPGGAAI 862
Cdd:cd17561     3 KVLIADD---NREF-VQLLEEylnsqPDMEVvGVAHNGQEALELIEEKEPDVLLLDIIMPHLDGIGVLEKLRRMRLEKRP 78
                          90       100
                  ....*....|....*....|....*....
gi 1308984722 863 PIVALTANAYSEDRQRCLAAGMNDFLAKP 891
Cdd:cd17561    79 KIIMLTAFGQEDITQRAVELGASYYILKP 107
PRK10336 PRK10336
two-component system response regulator QseB;
789-891 1.76e-06

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 49.89  E-value: 1.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDEPLnreIGCDL---LAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRAlpGGAAIPIV 865
Cdd:PRK10336    2 RILLIEDDML---IGDGIktgLSKMGFSVDWFTQGRQGKEALYSAPYDAVILDLTLPGMDGRDILREWRE--KGQREPVL 76
                          90       100
                  ....*....|....*....|....*.
gi 1308984722 866 ALTANAYSEDRQRCLAAGMNDFLAKP 891
Cdd:PRK10336   77 ILTARDALAERVEGLRLGADDYLCKP 102
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
807-893 1.77e-06

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: 47.65  E-value: 1.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 807 LAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRA-LPGgaaIPIVALTanAYSeDRQRCLAA--- 882
Cdd:cd19919    20 LAGAGLTVTSFENAQEALAALASSQPDVLISDIRMPGMDGLALLAQIKQrHPD---LPVIIMT--AHS-DLDSAVSAyqg 93
                          90
                  ....*....|.
gi 1308984722 883 GMNDFLAKPVD 893
Cdd:cd19919    94 GAFEYLPKPFD 104
PRK09483 PRK09483
response regulator; Provisional
790-895 2.86e-06

response regulator; Provisional


Pssm-ID: 236538 [Multi-domain]  Cd Length: 217  Bit Score: 49.33  E-value: 2.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 790 VLLVEDEPLNRE-IGCDLLAATGLEVA-TADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRI-RALPGgaaIPIVA 866
Cdd:PRK09483    4 VLLVDDHELVRAgIRRILEDIKGIKVVgEACCGEDAVKWCRTNAVDVVLMDMNMPGIGGLEATRKIlRYTPD---VKIIM 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1308984722 867 LTanAYSED--RQRCLAAGMNDFLAKPVDPE 895
Cdd:PRK09483   81 LT--VHTENplPAKVMQAGAAGYLSKGAAPQ 109
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
789-897 4.14e-06

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


Pssm-ID: 381111 [Multi-domain]  Cd Length: 112  Bit Score: 46.67  E-value: 4.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALpgGAAIPIVALT 868
Cdd:cd17563     2 SLLLVDDDEVFAERLARALERRGFEVETAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPPLRAL--QPDARIVVLT 79
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1308984722 869 -----ANAysedrqrcLAA---GMNDFLAKPVDPEAL 897
Cdd:cd17563    80 gyasiATA--------VEAiklGADDYLAKPADADEI 108
PRK13560 PRK13560
hypothetical protein; Provisional
355-521 6.47e-06

hypothetical protein; Provisional


Pssm-ID: 106506 [Multi-domain]  Cd Length: 807  Bit Score: 50.06  E-value: 6.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 355 RENEHAADHQAIETLNNQLAERLAALEIAEQDLRRLSTAVEQSPASIVITDINARITYVNLAFCVTSGYFPDEVIGENPR 434
Cdd:PRK13560  171 RFERHAHADDQVDGFAEDITERKRAEERIDEALHFLQQLLDNIADPAFWKDEDAKVFGCNDAACLACGFRREEIIGMSIH 250
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 435 ILQSGNTPPATYQAMWQTLTAGEIWRGELVNRRKDGSHYIERATISPVR--GSDGTTSQYVAVKEDISDQRRIEEELAAH 512
Cdd:PRK13560  251 DFAPAQPADDYQEADAAKFDADGSQIIEAEFQNKDGRTRPVDVIFNHAEfdDKENHCAGLVGAITDISGRRAAERELLEK 330

                  ....*....
gi 1308984722 513 RQHLQQLVD 521
Cdd:PRK13560  331 EDMLRAIIE 339
glnL PRK11073
nitrogen regulation protein NR(II);
447-754 7.76e-06

nitrogen regulation protein NR(II);


Pssm-ID: 182947 [Multi-domain]  Cd Length: 348  Bit Score: 49.31  E-value: 7.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 447 QAMWQTLTAGEIWRGELVNRRKDGSHYIERATISPVrgsdgtTSQYVAVK-EDISDQRRIEEELaahRQHLQQLvdqrtg 525
Cdd:PRK11073   64 ELMRESLQAGQGFTDNEVTLVIDGRSHILSLTAQRL------PEGMILLEmAPMDNQRRLSQEQ---LQHAQQV------ 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 526 elaqataaaesanlAKSAFLANMSHEIRTPMNAIIGLNYLLLKSPLEPA----------QRDKLLKV-----------TS 584
Cdd:PRK11073  129 --------------AARDLVRGLAHEIKNPLGGLRGAAQLLSKALPDPAlteytkviieQADRLRNLvdrllgpqrpgTH 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 585 ASEHLLQVINDILDLSKIESG-KLELEnQTFDPrevlqaaaavirdqalgkgllvgvdggKLPALAIgDAKRLRQVLINF 663
Cdd:PRK11073  195 VTESIHKVAERVVQLVSLELPdNVRLI-RDYDP---------------------------SLPELAH-DPDQIEQVLLNI 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 664 AGNALKF-----------TR-AGSIHLSGE---LLAndgenvtcRFVVSDTGLGIRPEDVPRLFKPFeqldasTTRQYGG 728
Cdd:PRK11073  246 VRNALQAlgpeggtitlrTRtAFQLTLHGEryrLAA--------RIDIEDNGPGIPPHLQDTLFYPM------VSGREGG 311
                         330       340
                  ....*....|....*....|....*.
gi 1308984722 729 TGLGLAIARHLAHLMDGEVGVDSTPG 754
Cdd:PRK11073  312 TGLGLSIARNLIDQHSGKIEFTSWPG 337
PRK09958 PRK09958
acid-sensing system DNA-binding response regulator EvgA;
791-890 1.41e-05

acid-sensing system DNA-binding response regulator EvgA;


Pssm-ID: 182168 [Multi-domain]  Cd Length: 204  Bit Score: 47.20  E-value: 1.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 791 LLVEDEPLNREIGCDLLAATGLEV-ATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALPGGAAIPIVALTA 869
Cdd:PRK09958    4 IIIDDHPLAIAAIRNLLIKNDIEIlAELTEGGSAVQRVETLKPDIVIIDVDIPGVNGIQVLETLRKRQYSGIIIIVSAKN 83
                          90       100
                  ....*....|....*....|.
gi 1308984722 870 NAYSEdrQRCLAAGMNDFLAK 890
Cdd:PRK09958   84 DHFYG--KHCADAGANGFVSK 102
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
376-505 1.50e-05

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 49.00  E-value: 1.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 376 RLAALEIAEQDLRRLST-AVEQSPASIVITDINARITYVNLAFCVTSGYFPDEVIGENP-RILQSGNTPPATYQAMWQTL 453
Cdd:PRK11359  123 RDASVEMAQKEQTRQLIiAVDHLDRPVIVLDPERRIVQCNRAFTEMFGYCISEASGMQPdTLLNIPEFPADNRIRLQQLL 202
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1308984722 454 TAGEIWRGELVNRRKDGSHYIERATISPVRGSDGTTSQYVAVKEDISDQRRI 505
Cdd:PRK11359  203 WKTARDQDEFLLLTRTGEKIWIKASISPVYDVLAHLQNLVMTFSDITEERQI 254
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
788-905 1.71e-05

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: 44.85  E-value: 1.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 788 GRVLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALpgGAAIPIVAL 867
Cdd:cd17553     1 EKILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMKVI--DENIRVIIM 78
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1308984722 868 TANAYSEDRQRCLAAGMNDFLAKPVDPEALYTILGKYL 905
Cdd:cd17553    79 TAYGELDMIQESKELGALTHFAKPFDIDEIRDAVKKYL 116
PRK10701 PRK10701
DNA-binding transcriptional regulator RstA; Provisional
789-897 2.25e-05

DNA-binding transcriptional regulator RstA; Provisional


Pssm-ID: 236738 [Multi-domain]  Cd Length: 240  Bit Score: 46.94  E-value: 2.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDEPLNREIGCDLLAATGLEV---ATADDGFAAIARFQEggfDLILMDIQMPGLDGLDATRRIRALPGGaaiPIV 865
Cdd:PRK10701    3 KIVFVEDDAEVGSLIAAYLAKHDIDVtvePRGDRAEATILREQP---DLVLLDIMLPGKDGMTICRDLRPKWQG---PIV 76
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1308984722 866 ALTanAYSEDRQRCLA--AGMNDFLAKPVDPEAL 897
Cdd:PRK10701   77 LLT--SLDSDMNHILAleMGACDYILKTTPPAVL 108
PRK10337 PRK10337
sensor protein QseC; Provisional
544-756 2.64e-05

sensor protein QseC; Provisional


Pssm-ID: 182388 [Multi-domain]  Cd Length: 449  Bit Score: 47.72  E-value: 2.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 544 FLANMSHEIRTPMNAiiglnyllLKSPLEPAQ--------RDK-LLKVTSASEHLLQVINDILDLSKIESGKLELENQTF 614
Cdd:PRK10337  240 FTSDAAHELRSPLAA--------LKVQTEVAQlsdddpqaRKKaLLQLHAGIDRATRLVDQLLTLSRLDSLDNLQDVAEI 311
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 615 DPREVLQAAAAVIRDQALGKGLLVGVDGGKLPALAIGDAKRLRQVLINFAGNALKFTRAGSIhLSGELLANdgenvtcRF 694
Cdd:PRK10337  312 PLEDLLQSAVMDIYHTAQQAGIDVRLTLNAHPVIRTGQPLLLSLLVRNLLDNAIRYSPQGSV-VDVTLNAR-------NF 383
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1308984722 695 VVSDTGLGIRPEDVPRL----FKPFEQlDASttrqygGTGLGLAIARHLAHLMDGEVGVDSTPGQG 756
Cdd:PRK10337  384 TVRDNGPGVTPEALARIgerfYRPPGQ-EAT------GSGLGLSIVRRIAKLHGMNVSFGNAPEGG 442
PRK09191 PRK09191
two-component response regulator; Provisional
781-869 4.11e-05

two-component response regulator; Provisional


Pssm-ID: 236402 [Multi-domain]  Cd Length: 261  Bit Score: 46.38  E-value: 4.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 781 ALSQRLFGRVLLVEDEPLnreIGCDL---LAATGLEV----ATADDgfaAIARFQEGGFDLILMDIQM-PGLDGLDATRR 852
Cdd:PRK09191  131 EIARQVATRVLIIEDEPI---IAMDLeqlVESLGHRVtgiaRTRAE---AVALAKKTRPGLILADIQLaDGSSGIDAVND 204
                          90
                  ....*....|....*..
gi 1308984722 853 IRAlpgGAAIPIVALTA 869
Cdd:PRK09191  205 ILK---TFDVPVIFITA 218
HATPase_Phy-like cd16932
Histidine kinase-like ATPase domain of plant phytochromes similar to Arabidopsis thaliana ...
651-765 4.69e-05

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


Pssm-ID: 340409 [Multi-domain]  Cd Length: 113  Bit Score: 43.41  E-value: 4.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 651 GDAKRLRQVLINFAGNALKFTRAG----SIHLS--GELLANDGENVTCRFVVSDTGLGIRPEDVPRLFKPfeqlDASTTR 724
Cdd:cd16932     2 GDQIRLQQVLADFLLNAVRFTPSPggwvEIKVSptKKQIGDGVHVIHLEFRITHPGQGLPEELVQEMFEE----NQWTTQ 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1308984722 725 QyggtGLGLAIARHLAHLMDGEVGVDSTPGQgSSFWITARL 765
Cdd:cd16932    78 E----GLGLSISRKLVKLMNGDVRYLREAGR-SYFLITLEL 113
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
394-504 5.21e-05

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain 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: 43.56  E-value: 5.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 394 VEQSPASIVITDINARITYVNLAFCVTSGYFPDEVIGENPRILQSGNTPPAtYQAMWQTLTAGE--IWRGELVNRrkDGS 471
Cdd:pfam08448   1 LDSLPDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAELLPPEDAAR-LERALRRALEGEepIDFLEELLL--NGE 77
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1308984722 472 HYIERATISPVRGSDGTTSQYVAVKEDISDQRR 504
Cdd:pfam08448  78 ERHYELRLTPLRDPDGEVIGVLVISRDITERRR 110
PDC2_HK_sensor cd18774
second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins, ...
178-269 5.87e-05

second 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: 350342 [Multi-domain]  Cd Length: 89  Bit Score: 42.82  E-value: 5.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 178 WFDRISRNQQLPKGWTSLLVTDDGSVVSRHPDPDIWRGSAFDAASrERLLAALRHDDDRVVMNGLDGIERLYLLQRLQIA 257
Cdd:cd18774     1 YLSDLLSSIKLGETGYAFLVDSDGTILAHPPKELVGKGKSLDDLA-LLAALLLAGESGTFEYTSDDGVERLVAYRPVPGT 79
                          90
                  ....*....|..
gi 1308984722 258 DghLVAAIGAPV 269
Cdd:cd18774    80 P--WVVVVGVPE 89
HATPase_SpaK_NisK-like cd16975
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
652-761 6.01e-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: 43.22  E-value: 6.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 652 DAKRLRQVLINFAGNALKFTRAG---SIHLSgellaNDGENVTcrFVVSDTGLGIRPEDVPRLFKPFEQLDASTTRQyGG 728
Cdd:cd16975     1 DTLLLSRALINIISNACQYAPEGgtvSISIY-----DEEEYLY--FEIWDNGHGFSEQDLKKALELFYRDDTSRRSG-GH 72
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1308984722 729 TGLGLAIARHLAHLMDGEVGVDSTPGQGS--SFWI 761
Cdd:cd16975    73 YGMGLYIAKNLVEKHGGSLIIENSQKGGAevTVKI 107
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
660-762 6.15e-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: 43.04  E-value: 6.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 660 LINFAGNALKFTRAGS--IHLSgelLANDGENVTCRfvVSDTGLGIRPEDVPRLfkpFEQldASTTRQYGGTGLGLAIAR 737
Cdd:cd16915     8 LIDNALDALAATGAPNkqVEVF---LRDEGDDLVIE--VRDTGPGIAPELRDKV---FER--GVSTKGQGERGIGLALVR 77
                          90       100
                  ....*....|....*....|....*
gi 1308984722 738 HLAHLMDGEVGVDSTPGQGSSFWIT 762
Cdd:cd16915    78 QSVERLGGSITVESEPGGGTTFSIR 102
pleD PRK09581
response regulator PleD; Reviewed
788-897 6.89e-05

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 46.43  E-value: 6.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 788 GRVLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIaRFQEGGFDLILMDIQMPGLDGLDATRRIRALPGGAAIPIVAL 867
Cdd:PRK09581  156 GRILLVDDDVSQAERIANILKEEFRVVVVSDPSEALF-NAAETNYDLVIVSANFENYDPLRLCSQLRSKERTRYVPILLL 234
                          90       100       110
                  ....*....|....*....|....*....|
gi 1308984722 868 TANAYSEDRQRCLAAGMNDFLAKPVDPEAL 897
Cdd:PRK09581  235 VDEDDDPRLVKALELGVNDYLMRPIDKNEL 264
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
788-897 7.53e-05

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


Pssm-ID: 381127 [Multi-domain]  Cd Length: 133  Bit Score: 43.51  E-value: 7.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 788 GRVLLVEDEPLNREiGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRAL-PGGAAIPIVA 866
Cdd:cd17596     1 PTILVVDDEVRSLE-ALRRTLEEDFDVLTAASAEEALAILEEEWVQVILCDQRMPGTTGVEFLKEVRERwPEVVRIIISG 79
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1308984722 867 LTAnaySEDRQRCL-AAGMNDFLAKPVDPEAL 897
Cdd:cd17596    80 YTD---SEDIIAGInEAGIYQYLTKPWHPDQL 108
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
788-893 9.34e-05

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 46.02  E-value: 9.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 788 GRVLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRAlpGGAAIPIVAL 867
Cdd:PRK10923    4 GIVWVVDDDSSIRWVLERALAGAGLTCTTFENGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQ--RHPMLPVIIM 81
                          90       100
                  ....*....|....*....|....*.
gi 1308984722 868 TANAYSEDRQRCLAAGMNDFLAKPVD 893
Cdd:PRK10923   82 TAHSDLDAAVSAYQQGAFDYLPKPFD 107
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
461-502 9.36e-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: 40.63  E-value: 9.36e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1308984722  461 GELVNRRKDGSHYIERATISPVRGSDGTTSQYVAVKEDISDQ 502
Cdd:smart00086   2 VEYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITER 43
PRK09935 PRK09935
fimbriae biosynthesis transcriptional regulator FimZ;
814-907 1.74e-04

fimbriae biosynthesis transcriptional regulator FimZ;


Pssm-ID: 182154 [Multi-domain]  Cd Length: 210  Bit Score: 44.10  E-value: 1.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 814 VATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRALpgGAAIPIVALTANAYSEDRQRCLAAGMNDFLAKPVD 893
Cdd:PRK09935   32 VLKTDDYRITIDYLRTRPVDLIIMDIDLPGTDGFTFLKRIKQI--QSTVKVLFLSSKSECFYAGRAIQAGANGFVSKCND 109
                          90
                  ....*....|....
gi 1308984722 894 PEALYTILGKYLAG 907
Cdd:PRK09935  110 QNDIFHAVQMILSG 123
PRK15369 PRK15369
two component system response regulator;
789-890 1.98e-04

two component system response regulator;


Pssm-ID: 185267 [Multi-domain]  Cd Length: 211  Bit Score: 43.91  E-value: 1.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDEPL--NREIGCdLLAATGLE-VATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRA-LPggaAIPI 864
Cdd:PRK15369    5 KILLVDDHELiiNGIKNM-LAPYPRYKiVGQVDNGLEVYNACRQLEPDIVILDLGLPGMNGLDVIPQLHQrWP---AMNI 80
                          90       100
                  ....*....|....*....|....*...
gi 1308984722 865 VALTanAYSEDR--QRCLAAGMNDFLAK 890
Cdd:PRK15369   81 LVLT--ARQEEHmaSRTLAAGALGYVLK 106
PRK10693 PRK10693
two-component system response regulator RssB;
817-892 2.11e-04

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 44.60  E-value: 2.11e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1308984722 817 ADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRAlpGGAAIPIVALTANAYSEDRQRCLAAGMNDFLAKPV 892
Cdd:PRK10693    3 AANGVDALELLGGFTPDLIICDLAMPRMNGIEFVEHLRN--RGDQTPVLVISATENMADIAKALRLGVQDVLLKPV 76
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
388-432 2.29e-04

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


Pssm-ID: 214512  Cd Length: 67  Bit Score: 40.46  E-value: 2.29e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1308984722  388 RRLSTAVEQSPASIVITDINARITYVNLAFCVTSGYFPDEVIGEN 432
Cdd:smart00091   1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKS 45
HATPase_NtrY-like cd16944
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
652-766 3.55e-04

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


Pssm-ID: 340420 [Multi-domain]  Cd Length: 108  Bit Score: 40.98  E-value: 3.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 652 DAKRLRQVLINF---AGNALKFTRAGSIHLSGELLANDGENVTcrFVVSDTGLGIRPEDVPRLFKPFeqldaSTTRQyGG 728
Cdd:cd16944     1 DTTQISQVLTNIlknAAEAIEGRPSDVGEVRIRVEADQDGRIV--LIVCDNGKGFPREMRHRATEPY-----VTTRP-KG 72
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1308984722 729 TGLGLAIARHLAHLMDGEVGVDSTPGQGSsfWITARLK 766
Cdd:cd16944    73 TGLGLAIVKKIMEEHGGRISLSNREAGGA--CIRIILP 108
HATPase_BvrS-ChvG-like cd16953
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
656-745 4.98e-04

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: 40.63  E-value: 4.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 656 LRQVLINFAGNALKFTRAGSIHLSgelLANDGENVTCRFVVSDTGLGIRPEDVPRLFKPFEQlDASTTRQYG-GTGLGLA 734
Cdd:cd16953     1 LGQVLRNLIGNAISFSPPDTGRIT---VSAMPTGKMVTISVEDEGPGIPQEKLESIFDRFYT-ERPANEAFGqHSGLGLS 76
                          90
                  ....*....|.
gi 1308984722 735 IARHLAHLMDG 745
Cdd:cd16953    77 ISRQIIEAHGG 87
PAS_8 pfam13188
PAS domain; PAS domains are involved in many signalling proteins where they are used as a ...
388-437 6.37e-04

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


Pssm-ID: 463802 [Multi-domain]  Cd Length: 65  Bit Score: 39.07  E-value: 6.37e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1308984722 388 RRLSTAVEQSPASIVITDINARITYVNLAFCVTSGY-FPDEVIGENPRILQ 437
Cdd:pfam13188   1 ERLRALFESSPDGILVLDEGGRIIYVNPAALELLGYeLLGELLGELLDLLD 51
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
792-892 1.61e-03

phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar proteins; Bacillus subtilis GlnL is part of the GlnK-GlnL (formerly YcbA-YcbB) two-component system that positively regulates the expression of the glsA-glnT (formerly ybgJ-ybgH) operon in response to glutamine. It contains a REC domain and a DNA-binding output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381112 [Multi-domain]  Cd Length: 103  Bit Score: 38.79  E-value: 1.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 792 LVEDEPLNREIGcdllaatglevaTADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRIRalPGGAAIPIVALTANA 871
Cdd:cd17565    17 IIEDDDLGEVVG------------EADNGAQAYDEILFLQPDIVLIDLLMPGMDGIQLVRKLK--DTGSNGKFIMISQVS 82
                          90       100
                  ....*....|....*....|.
gi 1308984722 872 YSEDRQRCLAAGMNDFLAKPV 892
Cdd:cd17565    83 DKEMIGKAYQAGIEFFINKPI 103
marine_sort_HK TIGR03785
proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is ...
544-753 2.22e-03

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: 42.04  E-value: 2.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 544 FLANMS----HEIRTPMnAIIGLNYLLLKS-PLEPAQRDKLLKVTSASEHLLQVINDILDLSKIESGKLELENQTFDPRE 618
Cdd:TIGR03785 484 YLENMSsrlsHELRTPV-AVVRSSLENLELqALEQEKQKYLERAREGTERLSMILNNMSEATRLEQAIQSAEVEDFDLSE 562
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 619 VLQAAAAVIRDqaLGKGLLVGVDGGKLPALAIGDAKRLRQVLINFAGNALKFTRAGS-IHLSgeLLANDGENVtcrFVVS 697
Cdd:TIGR03785 563 VLSGCMQGYQM--TYPPQRFELNIPETPLVMRGSPELIAQMLDKLVDNAREFSPEDGlIEVG--LSQNKSHAL---LTVS 635
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1308984722 698 DTGLGIrPEDVP-RLFKPFEQLDASTTRQYGGTGLGLAIARHLAHLMDGEVGVDSTP 753
Cdd:TIGR03785 636 NEGPPL-PEDMGeQLFDSMVSVRDQGAQDQPHLGLGLYIVRLIADFHQGRIQAENRQ 691
PRK13558 PRK13558
bacterio-opsin activator; Provisional
789-887 2.29e-03

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 41.75  E-value: 2.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 789 RVLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDG---LDATRRIRALPGGAAIPIV 865
Cdd:PRK13558    9 GVLFVGDDPEAGPVDCDLDEDGRLDVTQIRDFVAARDRVEAGEIDCVVADHEPDGFDGlalLEAVRQTTAVPPVVVVPTA 88
                          90       100
                  ....*....|....*....|..
gi 1308984722 866 ALTANAysedrQRCLAAGMNDF 887
Cdd:PRK13558   89 GDEAVA-----RRAVDADAAAY 105
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
381-509 5.71e-03

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 40.81  E-value: 5.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722  381 EIAEQDlRRLSTAVEQSPASIVITDINARITYVNLAFCVTSGYFPDEVigenpRILqsgntppaTYQAM-W--------- 450
Cdd:PRK09776   277 HISESE-TRFRNAMEYSAIGMALVGTEGQWLQVNKALCQFLGYSQEEL-----RGL--------TFQQLtWpedlnkdlq 342
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1308984722  451 --QTLTAGEI--WRGELVNRRKDGSHYIERATISPVRGSDGTTSQYVAVKEDISDQRRIEEEL 509
Cdd:PRK09776   343 qvEKLLSGEInsYSMEKRYYRRDGEVVWALLAVSLVRDTDGTPLYFIAQIEDINELKRTEQVN 405
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
131-401 6.12e-03

Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 40.39  E-value: 6.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 131 ALTATDITSGHYQTGLISGKRGITIGLPVRDAEGKLQAALYLASDIAWFDRISRNQQLPKGWTSLLVTDDGSVVSRHPDP 210
Cdd:COG0840    32 LLALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVVLLALLLALLLLLLALLALALAALALLAALAA 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 211 DIWRGSAFDAASRERLLAALRHDDDRVVMNGLDGIERLYLLQRLQIADGHLVAAIGAPVNETLHAIERAFMLHVLLLVTV 290
Cdd:COG0840   112 LLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAAALAALLEAAALALAAAALALALLAAALLAL 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 291 ALLSILLSrYYLYRLIERWVGQLKGATASVASGDFAVYLgDTRLPEELALLNQRFNEMISALGE--RENEHAADH----- 363
Cdd:COG0840   192 VALAIILA-LLLSRSITRPLRELLEVLERIAEGDLTVRI-DVDSKDEIGQLADAFNRMIENLRElvGQVRESAEQvasas 269
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1308984722 364 QAIETLNNQLAERlaaLEIAEQDLRRLSTAVEQSPASI 401
Cdd:COG0840   270 EELAASAEELAAG---AEEQAASLEETAAAMEELSATV 304
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
790-891 6.21e-03

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


Pssm-ID: 381155 [Multi-domain]  Cd Length: 100  Bit Score: 37.10  E-value: 6.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 790 VLLVEDEPLNREIGCDLLAATGLEVATADDGFAAIARFQEGGFDLILMDIQMPGLDGLDATRRI-RALPGgaaIPIVALT 868
Cdd:cd19928     1 ILVADDDRAIRTVLTQALGRAGYEVRTTGNAATLWRWVEEGEGDLVITDVVMPDENGLDLIPRIkKARPD---LPIIVMS 77
                          90       100
                  ....*....|....*....|...
gi 1308984722 869 ANAYSEDRQRCLAAGMNDFLAKP 891
Cdd:cd19928    78 AQNTLMTAVKAAERGAFEYLPKP 100
REC_PhyR cd17540
phosphoacceptor receiver (REC) domain of response regulator PhyR and similar proteins; PhyR is ...
788-897 6.46e-03

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


Pssm-ID: 381095 [Multi-domain]  Cd Length: 117  Bit Score: 37.61  E-value: 6.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 788 GRVLLVEDEPLnreIGCDL---LAATGLEVA----TADDGFAAIARFQEggfDLILMDIQMP-GLDGLDATRRIRALpgg 859
Cdd:cd17540     1 TRVLIIEDEPL---IAMDLeqiVEDLGHQVVgiarTRDEAVALARRERP---DLILADIQLAdGSSGIDAVNEILTT--- 71
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1308984722 860 AAIPIVALTanAYSEdrqrCLAAGMN---DFL-AKPVDPEAL 897
Cdd:cd17540    72 HDVPVIFVT--AYPE----RLLTGERpepTFLiTKPFDPEMV 107
HATPase_PDK-like cd16929
Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain ...
682-766 8.96e-03

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


Pssm-ID: 340406 [Multi-domain]  Cd Length: 169  Bit Score: 38.09  E-value: 8.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984722 682 LLANDGENVTCRFvvSDTGLGIRPEDVPRLFK------------PFEQLDASTTRQY-GGTGLGLAIARHLAHLMDGEVG 748
Cdd:cd16929    76 TVAKGDEDLTIKI--SDRGGGIPREDLARLFSymystapqpsldDFSDLISGTQPSPlAGFGYGLPMSRLYAEYFGGDLD 153
                          90
                  ....*....|....*...
gi 1308984722 749 VDSTPGQGSSFWItaRLK 766
Cdd:cd16929   154 LQSMEGYGTDVYI--YLK 169
HATPase_PhoQ-like cd16954
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
695-762 9.64e-03

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: 37.61  E-value: 9.64e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1308984722 695 VVSDTGLGIRPEDVPRLFKPFEQLDasttRQYGGTGLGLAIARHLAHLMDGEVGVDSTPGQGSSFWIT 762
Cdd:cd16954    71 IVDDDGPGVPESQRSKIFQRGQRLD----EQRPGQGLGLAIAKEIVEQYGGELSLSDSPLGGARFEVV 134
 
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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