|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11466 |
PRK11466 |
hybrid sensory histidine kinase TorS; Provisional |
1-894 |
0e+00 |
|
hybrid sensory histidine kinase TorS; Provisional
Pssm-ID: 236914 [Multi-domain] Cd Length: 914 Bit Score: 1491.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 1 MALLTLTSTLVGWYNLRFISQVEKDNTQALIPTMNMARQLSEASAWELFAAQNLTSADNEKMWQAQGRMLTAQSLKINAL 80
Cdd:PRK11466 16 MALLTLTSTLVGWYNLRFISQVEKDNTQALIPTMNMARQLSEASAWELFAAQNLTSADNEKMWQAQGRMLTAQSLKINAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 81 LQALREQGFDTTAIEQQEQEISRSLRQQGELVGRRLQLRQQQQRLSQQIVAAADEIARLAQGQANNAATSAGATQAGIYD 160
Cdd:PRK11466 96 LQALREQGFDTTAIEQQEQEISRSLRQQGELVGQRLQLRQQQQQLSQQIVAAADEIARLAQGQANNAATSAGATQAGIYD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 161 LIEQDQRQAAESALDRLIDIDLEYVNQMNELRLSALRVQQMVMNLGLEQIQKNAPTLEKQLNNAVKILQRRQIRIEDPGV 240
Cdd:PRK11466 176 LIEQDQRQAAESALDRLIDIDLEYVNQMNELRLSALRVQQMVMNLGLEQIQKNAPTLEKQLNNAVKILQRRQIRIEDPGV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 241 RAQVATTLTTVSQYSDLLALFQQDSEISNHLQTLAQNNIAQFAQFSSEVSQLVDTIELRNQHGLAHLEKASARGQYSLLL 320
Cdd:PRK11466 256 RAQVATTLTTVSQYSDLLALYQQDSEISNHLQTLAQNNIAQFAQFSSEVSQLVDTIELRNQHGLAHLEKASARGQYSLLL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 321 LGMVSLCALILILWRVVYRSVTRPLAEQTQALQRLLDGDIDSPFPETAGVRELDTIGRLMDAFRSSVHALNRHREQLAAQ 400
Cdd:PRK11466 336 LGMVSLCALILILWRVVYRSVTRPLAEQTQALQRLLDGDIDSPFPETAGVRELDTIGRLMDAFRSNVHALNRHREQLAAQ 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 401 VKARTAELQELVIEHRQARAEAEKASQAKSAFLAAMSHEIRTPLYGILGTAQLLADNPALNAQRDDLRAITDSGESLLTI 480
Cdd:PRK11466 416 VKARTAELQELVIEHRQARAEAEKASQAKSAFLAAMSHEIRTPLYGILGTAQLLADNPALNAQRDDLRAITDSGESLLTI 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 481 LNDILDYSAIEAGGKNVSVSDEPFEPRPLLESTLQLMSGRVKGRPIRLATAIADDVPTALMGDPRRIRQVITNLLSNALR 560
Cdd:PRK11466 496 LNDILDYSAIEAGGKNVSVSDEPFEPRPLLESTLQLMSGRVKGRPIRLATDIADDLPTALMGDPRRIRQVITNLLSNALR 575
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 561 FTDEGQIVLRSRTDGEQWLVEVEDSGCGIDPAKLAEIFQPFIQVSGKRGGTGLGLTISSRLAQAMGGELSATSTPEVGSC 640
Cdd:PRK11466 576 FTDEGSIVLRSRTDGEQWLVEVEDSGCGIDPAKLAEIFQPFVQVSGKRGGTGLGLTISSRLAQAMGGELSATSTPEVGSC 655
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 641 FCLRLPLRVATAPVPKTVNQAVRLDGLRLLLIEDNPLTQRITVEMLNTSGAQVVAIGNAAQALETLQNSEPFAAALVDFD 720
Cdd:PRK11466 656 FCLRLPLRVATAPVPKTVNQAVRLDGLRLLLIEDNPLTQRITAEMLNTSGAQVVAVGNAAQALETLQNSEPFAAALVDFD 735
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 721 LPDVNGITLARQLARQYPSLVLIGFSAHVIDETLRQRTSSLFRGIIPKPVPREVLGQLLAHYLQLQANNDLPLDVSQLNE 800
Cdd:PRK11466 736 LPDYDGITLARQLAQQYPSLVLIGFSAHVIDETLRQRTSSLFRGIIPKPVPREVLGQLLAHYLQLQVNNDQPLDVSQLNE 815
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 801 DAQLMGTEKIHEWLALFTQHALPLLDEIDIARATQDSEKIKRAAHQLKSSCSSLGMRSASQLCAQLEQQPLSAPLPHEEI 880
Cdd:PRK11466 816 DAALMGTEKIHEWLALFKQHALPLLDEIDIARASQDSEKIKRAAHQLKSSCSSLGMRQASQACAQLEQQPLSAPLPHEEI 895
|
890
....*....|....
gi 1447699372 881 TRSVAALEAWLNKK 894
Cdd:PRK11466 896 TRSVAALEAWLAKK 909
|
|
| TMAO_torS |
TIGR02956 |
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ... |
1-890 |
0e+00 |
|
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: 850.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 1 MALLTLTSTLVGWYNLRFISQVEKDNTQALIPTMNMARQLSEASAWELFAAQNLTSADNEKMWQAQGRMLTAQSLKINAL 80
Cdd:TIGR02956 13 MAALLLLSVVIGVLGLSLVAKTERTVTQSALPAMIEARQLSELSNQIIFSVQLLSNVDDERQRQAIGKKLTLQSETLLHS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 81 LQALREQGFDTTAIEQQE---QEISRSLRQQGELVGRRLQLRQQQQRLSQQIVAAADEIARLAQGQANNAATSAGATQAG 157
Cdd:TIGR02956 93 LKALGELPFNEDLLARLEvlvKDIIDTLAQLGLSVGERITLQAQLQQLSRELSEAAQEISELSQSQVANASTIALANVSG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 158 IYDLIEQDQRQAAESALDRLIDIDLEYVNQMNELRLSALRVQQMVMNLGLEQIQKNAPTLEKQLNNAVKILQRRQIRIED 237
Cdd:TIGR02956 173 IYDLIESGKNDQVYQALDDLIEVDLDLAERLNELRLLALRVLNTIDDTKTSQDLAHINQLDEEFNRLVMILSRRVQSIED 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 238 PGVRAQVATTLTTVSQYSDLLALFQQDSEISNHLQTLAQNNIAQFAQFSSEVSQLVDTIELRNQHGLAHLEKASARGQYS 317
Cdd:TIGR02956 253 PTRSNQLKDLLVTLNKTPKLFKLLRQLSQILQKQQRLQQANLEQFTQLNTTVSQLVNAQNQRTEAAVSDLLMTLSVAQFG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 318 LLLLGMVSLCALILILWRVVYRSVTRPLAEQTQALQRLLDGDIDSPFpETAGVRELDTIGRLMDAFRSSVHA-------- 389
Cdd:TIGR02956 333 LLITGMLGLVILVFIMWRVVYRSVILRLNQHTQALLRLALGDLDISL-DARGDDELAHMGRAIEAFRDTAAHnlklqade 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 390 ------LNRHREQLAAQVKARTAELQEL-------VIEHRQARAEAEKASQAKSAFLAAMSHEIRTPLYGILGTAQLLAD 456
Cdd:TIGR02956 412 rqvaqeLQEHKESLEQLVAQRTQELAETnerlnaeVKNHAKARAEAEEANRAKSAFLATMSHEIRTPLNGILGTLELLGD 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 457 NPALNAQRDDLRAITDSGESLLTILNDILDYSAIEAGgkNVSVSDEPFEPRPLLESTLQLMSGRVKGRPIRLATAIADDV 536
Cdd:TIGR02956 492 TGLTSQQQQYLQVINRSGESLLDILNDILDYSKIEAG--HLSISPRPFDLNALLDDVHHLMVSRAQLKGIQLRLNIPEQL 569
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 537 PTALMGDPRRIRQVITNLLSNALRFTDEGQIVLRSRTDGE-QWLVEVEDSGCGIDPAKLAEIFQPFIQVSGKR--GGTGL 613
Cdd:TIGR02956 570 PNWWQGDGPRIRQVLINLVGNAIKFTDRGSVVLRVSLNDDsSLLFEVEDTGCGIAEEEQATLFDAFTQADGRRrsGGTGL 649
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 614 GLTISSRLAQAMGGELSATSTPEVGSCFCLRLPLRVATAPVPKTVNQAVRLDGLRLLLIEDNPLTQRITVEMLNTSGAQV 693
Cdd:TIGR02956 650 GLAISQRLVEAMDGELGVESELGVGSCFWFTLPLTRGKPAEDSATLTVIDLPPQRVLLVEDNEVNQMVAQGFLTRLGHKV 729
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 694 VAIGNAAQALETLQNsEPFAAALVDFDLPDVNGITLARQLARQYPS---LVLIGFSAHVIDETLRQRTSSLFRGIIPKPV 770
Cdd:TIGR02956 730 TLAESGQSALECFHQ-HAFDLALLDINLPDGDGVTLLQQLRAIYGAkneVKFIAFSAHVFNEDVAQYLAAGFDGFLAKPV 808
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 771 PREVLGQLLAHYLQLQANNDLP---------------------------------LDVSQLNEDAQLMGTEKIHEWLALF 817
Cdd:TIGR02956 809 VEEQLTAMIAVILAGGKSNTEApvlsaspsfdsasvienaqaddipesnqaseflLDEEQLQQDIEVLGVEKVRQLVALF 888
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 818 TQHALPLLDEIDIARATQDSEKIKRAAHQLKSSCSSLGMRSASQLCAQLEQQPLSAPLPHEEI-------TRSVAALEAW 890
Cdd:TIGR02956 889 KTSSAEQLEELSAARAVDDDAQIKKLAHKLKGSAGSLGLTQLTQLCQQLEKQGKTGALELSDIdeikqawQASKTALDQW 968
|
|
| TorS_sensor_domain |
cd16172 |
sensor domain of the sensor histidine kinase TorS; TorS is part of the trimethylamine-N-oxide ... |
37-294 |
8.49e-81 |
|
sensor domain of the sensor histidine kinase TorS; TorS is part of the trimethylamine-N-oxide (TMAO) reductase (Tor) pathway, which consists TorT, a periplasmic binding protein that binds TMAO; TorS, a sensor histidine kinase that forms a complex with TorT, and TorR, the response regulator. The Tor pathway is involved in regulating a cellular response to trimethylamine-N-oxide (TMAO), a terminal electron receptor in anaerobic respiration. TorS consists of a periplasmic sensor domain, as well as a HAMP domain, a histidine kinase domain, and a receiver domain.
Pssm-ID: 293930 [Multi-domain] Cd Length: 261 Bit Score: 261.75 E-value: 8.49e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 37 ARQLSEASAWELFAAQNLTSADNEKMWQAQGRMLTAQSLKINALLQALR---EQGFDTTAIEQQEQEISRSLRQQGELVG 113
Cdd:cd16172 1 ARQLSELSSRIIASAQLLANADSEAERQQQGRQLTAQLEALLRLLKALGqdsFDSFLLSRLEQTVQEIIDNLAQLGELVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 114 RRLQLRQQQQRLSQQIVAAADEIARLAQGQANNAATSAGATQAGIYDLIEQDQRQAAESALDRLIDIDLEYVNQMNELRL 193
Cdd:cd16172 81 QRLQLRQQFQQLFERLRAAAGELAQLARTQVANASTIAVANVSGLYDLIEQNDKEAAYQALDRLIEVDLDLLERMHELRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 194 SALRVQQMVMNLGLEQIQKNAPTLEKQLNNAVKILQRRQIRIEDPGVRAQVATTLTTVSQYSDLLALFQQDSEISNHLQT 273
Cdd:cd16172 161 LALQLGNLINELRTASDIARLAELRQQFNANLAILQRRVQAVEDPGRRAQMAQLLSDLEQGQGLFALRRQLLALEQRLQA 240
|
250 260
....*....|....*....|.
gi 1447699372 274 LAQNNIAQFAQFSSEVSQLVD 294
Cdd:cd16172 241 LMQNNLVLFTQLNQTVNALVD 261
|
|
| PRK15347 |
PRK15347 |
two component system sensor kinase; |
323-882 |
1.86e-80 |
|
two component system sensor kinase;
Pssm-ID: 237951 [Multi-domain] Cd Length: 921 Bit Score: 279.60 E-value: 1.86e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 323 MVSLCALILILWRVVYRSVTRPLAEQTQALQRLLDGDIDSPFPETagvRElDTIGRLMDAFRSSVHALNRHREQLAAQVK 402
Cdd:PRK15347 303 LLILVLLTSVLFLLLRRYLAKPLWRFVDIINKTGPAALEPRLPEN---RL-DELGSIAKAYNQLLDTLNEQYDTLENKVA 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 403 ARTAELQElviehrqARAEAEKASQAKSAFLAAMSHEIRTPLYGILGTAQLLADNPALNAQRDDLRAITDSGESLLTILN 482
Cdd:PRK15347 379 ERTQALAE-------AKQRAEQANKRKSEHLTTISHEIRTPLNGVLGALELLQNTPLTAEQMDLADTARQCTLSLLAIIN 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 483 DILDYSAIEAGgkNVSVSDEPFEPRPLLESTLQLMSGRVKGRPIRLATAIADDVPTALMGDPRRIRQVITNLLSNALRFT 562
Cdd:PRK15347 452 NLLDFSRIESG--QMTLSLEETALLPLLDQAMLTIQGPAQSKSLTLRTFVGAHVPLYLHLDSLRLRQILVNLLGNAVKFT 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 563 DEGQIVLRSRTDGEQWLVEVEDSGCGIDPAKLAEIFQPFIQVSGKRGGTGLGLTISSRLAQAMGGELSATSTPEVGSCFC 642
Cdd:PRK15347 530 ETGGIRLRVKRHEQQLCFTVEDTGCGIDIQQQQQIFTPFYQADTHSQGTGLGLTIASSLAKMMGGELTLFSTPGVGSCFS 609
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 643 LRLPLRVATAP------------------------VPKTVNQAV--------------RLDG------------------ 666
Cdd:PRK15347 610 LVLPLNEYAPPeplkgelsaplalhrqlsawgitcQPGHQNPALldpelaylpgrlydLLQQiiqgapnepvinlplqpw 689
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 667 -LRLLLIEDNPLTQRITVEMLNTSGAQVVAIGNAAQALEtLQNSEPFAAALVDFDLPDVNGITLARQ----LARQYPSLV 741
Cdd:PRK15347 690 qLQILLVDDVETNRDIIGMMLVELGQQVTTAASGTEALE-LGRQHRFDLVLMDIRMPGLDGLETTQLwrddPNNLDPDCM 768
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 742 LIGFSAHVIDETlRQRTSSL-FRGIIPKPVPREVLGQLLAHYLQLQANNDLPLdVSQLNEDAQLMGTEKIHEWLALFtQH 820
Cdd:PRK15347 769 IVALTANAAPEE-IHRCKKAgMNHYLTKPVTLAQLARALELAAEYQLLRGIEL-SPQDSSCSPLLDTDDMALNSKLY-QS 845
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1447699372 821 ALPLLDEIDIARATQdsEKIKRAAHQLKSSCSSLGMRSASQLCAQLEQQ-PLSAPLPHEEITR 882
Cdd:PRK15347 846 LLLLLAQIEQAVENQ--EVLSQLLHTLKGCAGQAGLTELQCAVIDLENAlETGEILSLEELTD 906
|
|
| BaeS |
COG0642 |
Signal transduction histidine kinase [Signal transduction mechanisms]; |
329-648 |
3.54e-69 |
|
Signal transduction histidine kinase [Signal transduction mechanisms];
Pssm-ID: 440407 [Multi-domain] Cd Length: 328 Bit Score: 232.88 E-value: 3.54e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 329 LILILWRVVYRSVTRPLAEQTQALQRLLDGDIDSPFPETAGVRELDTIGRLMDAFRSSVHALNRHREQLAAQVKARTAEL 408
Cdd:COG0642 10 LLLLLLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLLLLLLLLLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 409 QELVIEHRQARAEAEKASQAKSAFLAAMSHEIRTPLYGILGTAQLLADNPAlNAQRDDLRAITDSGESLLTILNDILDYS 488
Cdd:COG0642 90 LLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLEELD-EEQREYLETILRSADRLLRLINDLLDLS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 489 AIEAGgkNVSVSDEPFEPRPLLESTLQLMSGRVKGRPIRLATAIADDVPTaLMGDPRRIRQVITNLLSNALRFTDEG-QI 567
Cdd:COG0642 169 RLEAG--KLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDDLPT-VRGDPDRLRQVLLNLLSNAIKYTPEGgTV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 568 VLRSRTDGEQWLVEVEDSGCGIDPAKLAEIFQPFIQVSGKR--GGTGLGLTISSRLAQAMGGELSATSTPEVGSCFCLRL 645
Cdd:COG0642 246 TVSVRREGDRVRISVEDTGPGIPPEDLERIFEPFFRTDPSRrgGGTGLGLAIVKRIVELHGGTIEVESEPGKGTTFTVTL 325
|
...
gi 1447699372 646 PLR 648
Cdd:COG0642 326 PLA 328
|
|
| KdpD |
COG2205 |
K+-sensing histidine kinase KdpD [Signal transduction mechanisms]; |
416-650 |
9.79e-64 |
|
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
Pssm-ID: 441807 [Multi-domain] Cd Length: 239 Bit Score: 214.39 E-value: 9.79e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 416 RQARAEAEKASQAKSAFLAAMSHEIRTPLYGILGTAQLLADNPALNA--QRDDLRAITDSGESLLTILNDILDYSAIEAG 493
Cdd:COG2205 3 EEALEELEELERLKSEFLANVSHELRTPLTSILGAAELLLDEEDLSPeeRRELLEIIRESAERLLRLIEDLLDLSRLESG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 494 gkNVSVSDEPFEPRPLLESTLQLMSGRVKGRPIRLATAIADDVPTaLMGDPRRIRQVITNLLSNALRFTDEG-QIVLRSR 572
Cdd:COG2205 83 --KLSLELEPVDLAELLEEAVEELRPLAEEKGIRLELDLPPELPL-VYADPELLEQVLANLLDNAIKYSPPGgTITISAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 573 TDGEQWLVEVEDSGCGIDPAKLAEIFQPFIQVSGKR--GGTGLGLTISSRLAQAMGGELSATSTPEVGSCFCLRLPLRVA 650
Cdd:COG2205 160 REGDGVRISVSDNGPGIPEEELERIFERFYRGDNSRgeGGTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFTVTLPLAES 239
|
|
| PRK11091 |
PRK11091 |
aerobic respiration control sensor protein ArcB; Provisional |
414-895 |
1.52e-62 |
|
aerobic respiration control sensor protein ArcB; Provisional
Pssm-ID: 236842 [Multi-domain] Cd Length: 779 Bit Score: 226.36 E-value: 1.52e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 414 EHRQARAEAEKASQAKSAFLAAMSHEIRTPLYGILGTAQLLADNPALNAQRDDLRAITDSGESLLTILNDILDYSAIEAg 493
Cdd:PRK11091 268 ERKRYQDALEKASRDKTTFISTISHELRTPLNGIVGLSRILLDTELTAEQRKYLKTIHVSAITLGNIFNDIIDMDKMER- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 494 gKNVSVSDEPFEPRPLLeSTLQLMSGRV---KGrpIRLATAIADDVPTALMGDPRRIRQVITNLLSNALRFTDEGQIVLR 570
Cdd:PRK11091 347 -RKLQLDNQPIDFTDFL-ADLENLSGLQaeqKG--LRFDLEPLLPLPHKVITDGTRLRQILWNLISNAVKFTQQGGVTVR 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 571 -SRTDGEQWLVEVEDSGCGIDPAKLAEIFQPFIQVSGKRG-----GTGLGLTISSRLAQAMGGELSATSTPEVGSCFCLR 644
Cdd:PRK11091 423 vRYEEGDMLTFEVEDSGIGIPEDELDKIFAMYYQVKDSHGgkpatGTGIGLAVSKRLAQAMGGDITVTSEEGKGSCFTLT 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 645 LPL-RVATAPVPKTVNQAVRLDGLRLLLIEDNPLTQRITVEMLNTSGAQVVAIGNAAQALETLQNSEpFAAALVDFDLPD 723
Cdd:PRK11091 503 IHApAVAEEVEDAFDEDDMPLPALNILLVEDIELNVIVARSVLEKLGNSVDVAMTGKEALEMFDPDE-YDLVLLDIQLPD 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 724 VNGITLARQLARQYPSLVL---IGFSAHVIDETLRQRTSSLfRGIIPKP--VP--REVLGQLLAHY----------LQLQ 786
Cdd:PRK11091 582 MTGLDIARELRERYPREDLpplVALTANVLKDKKEYLDAGM-DDVLSKPlsVPalTAMIKKFWDTQddeestvtteESSK 660
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 787 ANNDLpLDVSQLNEDAQLMGTEKIHEWLALFTQHALPLLDEIDIARATQDSEKIKRAAHQLKSSCSSLGMRSASQLcAQL 866
Cdd:PRK11091 661 ANEAL-LDIPMLEQYVELVGPKLITDSLAVFEKMMPGYLSVLDSNLTARDQKGIVEEAHKIKGAAGSVGLRHLQQL-AQQ 738
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1447699372 867 EQQPlsaPLPH---------EEITRS----VAALEAWLNKKD 895
Cdd:PRK11091 739 IQSP---DLPAwwdnvqdwvEELKNEwrhdVEVLKAWLAQAE 777
|
|
| PRK11107 |
PRK11107 |
hybrid sensory histidine kinase BarA; Provisional |
307-797 |
5.56e-60 |
|
hybrid sensory histidine kinase BarA; Provisional
Pssm-ID: 236848 [Multi-domain] Cd Length: 919 Bit Score: 220.88 E-value: 5.56e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 307 LEKASAR-GQYS-------LLLLGMvsLCALILIlWRVVyRSVTRPLAEQTQALQRLLDGDIDSpfpetaGVR-----EL 373
Cdd:PRK11107 164 LDLKSVRlQQYReifiaflMLLLGI--GLALLFA-FRLM-RDVTGPIRNMVNTVDRIRRGQLDS------RVEgnmlgEL 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 374 DTIGRLMDAFRSSvhaLNRHREQLAAQVKARTAELQELV-------IEHRQARAEAEKASQAKSAFLAAMSHEIRTPLYG 446
Cdd:PRK11107 234 DMLKNGINAMAMS---LSAYHEEMQQNIDQATSDLRETLeqmeiqnVELDLAKKRAQEAARIKSEFLANMSHELRTPLNG 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 447 ILGTAQLLADNPALNAQRDDLRAITDSGESLLTILNDILDYSAIEAgGKNVsVSDEPFEPRPLLESTLQLM--SGRVKGr 524
Cdd:PRK11107 311 VIGFTRQTLKTPLTPTQRDYLQTIERSANNLLAIINDILDFSKLEA-GKLV-LENIPFSLRETLDEVVTLLahSAHEKG- 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 525 pIRLATAIADDVPTALMGDPRRIRQVITNLLSNALRFTDEGQIVLRSRT---DGEQWLVEVE--DSGCGIDPAKLAEIFQ 599
Cdd:PRK11107 388 -LELTLNIDPDVPDNVIGDPLRLQQIITNLVGNAIKFTESGNIDILVELralSNTKVQLEVQirDTGIGISERQQSQLFQ 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 600 PFIQ----VSGKRGGTGLGLTISSRLAQAMGGELSATSTPEVGSCFCLRLPLRVATAPVPKTVNQAvRLDGLRLLLIEDN 675
Cdd:PRK11107 467 AFRQadasISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHLPLDLNPNPIIDGLPTD-CLAGKRLLYVEPN 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 676 PLTQRITVEMLNTSGAQVVaignAAQALETLQNSEpFAAALVDFDLPDVNGIT-LARQLARQYPS----LVLIGFSAHVI 750
Cdd:PRK11107 546 SAAAQATLDILSETPLEVT----YSPTLSQLPEAH-YDILLLGLPVTFREPLTmLHERLAKAKSMtdflILALPCHEQVL 620
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1447699372 751 DETLRQR--TSSLFrgiipKPVPREVLGQLLAHYLQLQANNDLPLDVSQ 797
Cdd:PRK11107 621 AEQLKQDgaDACLS-----KPLSHTRLLPALLEPCHHKQPPLLPPTDES 664
|
|
| WalK |
COG5002 |
Sensor histidine kinase WalK [Signal transduction mechanisms]; |
328-648 |
5.77e-60 |
|
Sensor histidine kinase WalK [Signal transduction mechanisms];
Pssm-ID: 444026 [Multi-domain] Cd Length: 390 Bit Score: 209.41 E-value: 5.77e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 328 ALILILWRVVYRSVTRPLAEQTQALQRLLDGDIDSPFPETAGVRELDTIGRLMDAFRSSVHALNRHREQLAAQVKARTAE 407
Cdd:COG5002 64 LLLALLLLLLLLLLLLALALLLLALLLLLLLLLLLLALLILLLLLALLILLAALLLLLSELLLLLLLLGRLSLRLSALLL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 408 LQELVIEHRQARAEAEKASQAKSAFLAAMSHEIRTPLYGILGTAQLLADNPALN--AQRDDLRAITDSGESLLTILNDIL 485
Cdd:COG5002 144 GLLLLAAVERDITELERLEQMRREFVANVSHELRTPLTSIRGYLELLLDGAADDpeERREYLEIILEEAERLSRLVNDLL 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 486 DYSAIEAGgkNVSVSDEPFEPRPLLESTLQLMSGRVKGRPIRLATAIADDvPTALMGDPRRIRQVITNLLSNALRFTDEG 565
Cdd:COG5002 224 DLSRLESG--ELKLEKEPVDLAELLEEVVEELRPLAEEKGIELELDLPED-PLLVLGDPDRLEQVLTNLLDNAIKYTPEG 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 566 -QIVLRSRTDGEQWLVEVEDSGCGIDPAKLAEIFQPFIQVSGKR----GGTGLGLTISSRLAQAMGGELSATSTPEVGSC 640
Cdd:COG5002 301 gTITVSLREEDDQVRISVRDTGIGIPEEDLPRIFERFYRVDKSRsretGGTGLGLAIVKHIVEAHGGRIWVESEPGKGTT 380
|
....*...
gi 1447699372 641 FCLRLPLR 648
Cdd:COG5002 381 FTITLPLA 388
|
|
| PRK10841 |
PRK10841 |
two-component system sensor histidine kinase RcsC; |
408-694 |
5.30e-49 |
|
two-component system sensor histidine kinase RcsC;
Pssm-ID: 182772 [Multi-domain] Cd Length: 924 Bit Score: 187.87 E-value: 5.30e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 408 LQELViehrqarAEAEKASQAKSAFLAAMSHEIRTPLYGILGTAQLLaDNPALNAQRDDL-RAITDSGESLLTILNDILD 486
Cdd:PRK10841 433 LQEMA-------QAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLL-QTKELPKGVDRLvTAMNNSSSLLLKIISDILD 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 487 YSAIEAggKNVSVSDEPFEPRPLLE----STLQLMsgrVKGRpIRLATAIADDVPTALMGDPRRIRQVITNLLSNALRFT 562
Cdd:PRK10841 505 FSKIES--EQLKIEPREFSPREVINhitaNYLPLV---VKKR-LGLYCFIEPDVPVALNGDPMRLQQVISNLLSNAIKFT 578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 563 DEGQIVLRSRTDGEQWLVEVEDSGCGIDPAKLAEIFQPFIQV-SGKRG---GTGLGLTISSRLAQAMGGELSATSTPEVG 638
Cdd:PRK10841 579 DTGCIVLHVRVDGDYLSFRVRDTGVGIPAKEVVRLFDPFFQVgTGVQRnfqGTGLGLAICEKLINMMDGDISVDSEPGMG 658
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1447699372 639 SCFCLRLPLRVATAPVPKTVNQavrLDGLRLLLIEDNPLTQRITVEMLNTSGAQVV 694
Cdd:PRK10841 659 SQFTIRIPLYGAQYPQKKGVEG---LQGKRCWLAVRNASLEQFLETLLQRSGIQVQ 711
|
|
| COG4191 |
COG4191 |
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ... |
328-647 |
4.47e-46 |
|
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal transduction mechanisms];
Pssm-ID: 443345 [Multi-domain] Cd Length: 361 Bit Score: 169.21 E-value: 4.47e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 328 ALILILWRVVYRSVTRPLAEQTQALQRLLDGDIDSPFPETAGVRELDTIGRLMDAFRSSVHALNRHREQLAAQVKARTAE 407
Cdd:COG4191 43 LLALLALLLLLLLLLLLLLLELLLLLLALLGGLLRLLLLLGLLLLLLLEALLLLLLAALDAEENAELEELERDITELERA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 408 LQELvIEHRQARAEAEKasqaksafLAAM-------SHEIRTPLYGILGTAQLLADNPALNAQRDDLRA----ITDSGES 476
Cdd:COG4191 123 EEEL-RELQEQLVQSEK--------LAALgelaagiAHEINNPLAAILGNAELLRRRLEDEPDPEELREalerILEGAER 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 477 LLTILNDILDYSAIEAGGKnvsvsdEPFEPRPLLESTLQLMSGRVKGRPIRLATAIADDVPtALMGDPRRIRQVITNLLS 556
Cdd:COG4191 194 AAEIVRSLRAFSRRDEEER------EPVDLNELIDEALELLRPRLKARGIEVELDLPPDLP-PVLGDPGQLEQVLLNLLI 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 557 N---ALRFTDEGQIVLRSRTDGEQWLVEVEDSGCGIDPAKLAEIFQPFiqVSGKR--GGTGLGLTISSRLAQAMGGELSA 631
Cdd:COG4191 267 NaidAMEEGEGGRITISTRREGDYVVISVRDNGPGIPPEVLERIFEPF--FTTKPvgKGTGLGLSISYGIVEKHGGRIEV 344
|
330
....*....|....*.
gi 1447699372 632 TSTPEVGSCFCLRLPL 647
Cdd:COG4191 345 ESEPGGGTTFTITLPL 360
|
|
| COG4251 |
COG4251 |
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ... |
156-648 |
2.57e-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: 2.57e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 156 AGIYDLIEQDQRQAAESALDRLIDIDLEYVNQMNELRLSALRVQQMVMNLGLEQIQKNAPTLEKQLNNAVKILQRRQIRI 235
Cdd:COG4251 1 LLLLALLLLLLLLLLLLLLLLLLLLLVLLLALALLLLLALLVLLLLLIRLLLLLLLSLLALLLLLLLLLLLLLVLAALAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 236 EDPGVRAQVATTLTTVSQYSDLLALFQQDSEISNHLQTLAQNNIAQFAQFSSEVSQLVDTIELRNQHGLAHLEKASARGQ 315
Cdd:COG4251 81 LLLLLLLELALVLLALLLVLLLLLALLLLLALLLLLELLLLLLALLLLLLLLALLLLEELALLRLALALLLLLLLLLLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 316 YSLLLLGMVSLCALILILWRVVYRSVTRPLAEQTQALQRLLDGDIDSPFPETAGVRELDTIGR--------LMDAFRSSV 387
Cdd:COG4251 161 LLLLALILALLLAALAELELLLLLLLVLLLLLLLLLLLLLLLLRLLLELLLLLEAELLLSLGGglglllllLLLLVLLLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 388 HALNRHREQLAAQVKARTAELQELVIEHRQARAEAEKASQAKSAFLAAMSHEIRTPLYGILGTAQLLAD--NPALNAQ-R 464
Cdd:COG4251 241 LILLLLLLILVLELLELRLELEELEEELEERTAELERSNEELEQFAYVASHDLREPLRKISGFSQLLEEdyGDKLDEEgR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 465 DDLRAITDSGESLLTILNDILDYSAIEAGGKNVsvsdEPFEPRPLLESTLQLMSGRVKGRPIRLataIADDVPTaLMGDP 544
Cdd:COG4251 321 EYLERIRDAAERMQALIDDLLAYSRVGRQELEF----EPVDLNELLEEVLEDLEPRIEERGAEI---EVGPLPT-VRGDP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 545 RRIRQVITNLLSNALRFTDEG---QIVLRSRTDGEQWLVEVEDSGCGIDPAKLAEIFQPFIQVSGKR--GGTGLGLTISS 619
Cdd:COG4251 393 TLLRQVFQNLISNAIKYSRPGeppRIEIGAEREGGEWVFSVRDNGIGIDPEYAEKIFEIFQRLHSRDeyEGTGIGLAIVK 472
|
490 500
....*....|....*....|....*....
gi 1447699372 620 RLAQAMGGELSATSTPEVGSCFCLRLPLR 648
Cdd:COG4251 473 KIVERHGGRIWVESEPGEGATFYFTLPKA 501
|
|
| NtrY |
COG5000 |
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
318-652 |
2.42e-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: 165.91 E-value: 2.42e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 318 LLLLGMVSLCALILILW--RVVYRSVTRPLAEQTQALQRLLDGDIDSPFPETAGvrelDTIGRLMDAFRSSVHALNRHRE 395
Cdd:COG5000 8 LLLLLLIALLLLLLALWlaLLLARRLTRPLRRLAEATRAVAAGDLSVRLPVTGD----DEIGELARAFNRMTDQLKEQRE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 396 QLAAQ----------------------------------------------------VKARTAELQELVIEHRQARAE-- 421
Cdd:COG5000 84 ELEERrryletilenlpagvivldadgritlanpaaerllgipleeligkpleellpELDLAELLREALERGWQEEIElt 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 422 ---------------------------AEKASQAKSA---FLAAMSHEIRTPLYGILGTAQLLAD--NPALNAQRDDLRA 469
Cdd:COG5000 164 rdgrrtllvrasplrddgyvivfdditELLRAERLAAwgeLARRIAHEIKNPLTPIQLSAERLRRklADKLEEDREDLER 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 470 ITD----SGESLLTILNDILDYSaieaggKNVSVSDEPFEPRPLLESTLQLMSGRVKGRPIRLATAIADDVPTaLMGDPR 545
Cdd:COG5000 244 ALDtiirQVDRLKRIVDEFLDFA------RLPEPQLEPVDLNELLREVLALYEPALKEKDIRLELDLDPDLPE-VLADRD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 546 RIRQVITNLLSNALRFTDE-GQIVLRSRTDGEQWLVEVEDSGCGIDPAKLAEIFQPFiqVSGKRGGTGLGLTISSRLAQA 624
Cdd:COG5000 317 QLEQVLINLLKNAIEAIEEgGEIEVSTRREDGRVRIEVSDNGPGIPEEVLERIFEPF--FTTKPKGTGLGLAIVKKIVEE 394
|
410 420
....*....|....*....|....*...
gi 1447699372 625 MGGELSATSTPEVGSCFCLRLPLRVATA 652
Cdd:COG5000 395 HGGTIELESRPGGGTTFTIRLPLAEEAE 422
|
|
| HATPase_EvgS-ArcB-TorS-like |
cd16922 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ... |
547-647 |
6.28e-44 |
|
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: 154.19 E-value: 6.28e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 547 IRQVITNLLSNALRFTDEGQIVLRSRTDGE-----QWLVEVEDSGCGIDPAKLAEIFQPFIQV----SGKRGGTGLGLTI 617
Cdd:cd16922 1 LRQILLNLLGNAIKFTEEGEVTLRVSLEEEeedgvQLRFSVEDTGIGIPEEQQARLFEPFSQAdsstTRKYGGTGLGLAI 80
|
90 100 110
....*....|....*....|....*....|
gi 1447699372 618 SSRLAQAMGGELSATSTPEVGSCFCLRLPL 647
Cdd:cd16922 81 SKKLVELMGGDISVESEPGQGSTFTFTLPL 110
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
414-653 |
1.30e-42 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 159.24 E-value: 1.30e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 414 EHRQARAEAEKASQAKSA--FLAAMSHEIRTPLYGILGTAQLLADNPALNAQRDDLRAITDSGESLLTILNDILDYSaie 491
Cdd:COG3852 118 ERKRLERELRRAEKLAAVgeLAAGLAHEIRNPLTGIRGAAQLLERELPDDELREYTQLIIEEADRLNNLVDRLLSFS--- 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 492 aggKNVSVSDEPFEPRPLLESTLQLMSGRVkGRPIRLATAIADDVPtALMGDPRRIRQVITNLLSNALRFTDE-GQIVLR 570
Cdd:COG3852 195 ---RPRPPEREPVNLHEVLERVLELLRAEA-PKNIRIVRDYDPSLP-EVLGDPDQLIQVLLNLVRNAAEAMPEgGTITIR 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 571 SRTD----------GEQWLVEVEDSGCGIDPAKLAEIFQPFiqVSGKRGGTGLGLTISSRLAQAMGGELSATSTPEVGSC 640
Cdd:COG3852 270 TRVErqvtlgglrpRLYVRIEVIDNGPGIPEEILDRIFEPF--FTTKEKGTGLGLAIVQKIVEQHGGTIEVESEPGKGTT 347
|
250
....*....|...
gi 1447699372 641 FCLRLPLRVATAP 653
Cdd:COG3852 348 FRIYLPLEQAEEE 360
|
|
| PRK09959 |
PRK09959 |
acid-sensing system histidine kinase EvgS; |
407-872 |
1.56e-38 |
|
acid-sensing system histidine kinase EvgS;
Pssm-ID: 182169 [Multi-domain] Cd Length: 1197 Bit Score: 155.66 E-value: 1.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 407 ELQELVIEHRQARAEAEKASQAKSAFLAAMSHEIRTPLYGILGTAQLLADNPALNAQRDDLRAIT-DSGESLLTILNDIL 485
Cdd:PRK09959 690 ETRDLIHALEVERNKAINATVAKSQFLATMSHEIRTPISSIMGFLELLSGSGLSKEQRVEAISLAyATGQSLLGLIGEIL 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 486 DYSAIEAGgkNVSVSDEPFEPRPLLESTLQLMSGRVKGRPIRLATAIADDVPTALMGDPRRIRQVITNLLSNALRFTDEG 565
Cdd:PRK09959 770 DVDKIESG--NYQLQPQWVDIPTLVQNTCHSFGAIAASKSIALSCSSTFPDHYLVKIDPQAFKQVLSNLLSNALKFTTEG 847
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 566 QIVLRS---RTDGEQWLVE--VEDSGCGIDPAKLAEIFQPFIQVSGKR--GGTGLGLTISSRLAQAMGGELSATSTPEVG 638
Cdd:PRK09959 848 AVKITTslgHIDDNHAVIKmtIMDSGSGLSQEEQQQLFKRYSQTSAGRqqTGSGLGLMICKELIKNMQGDLSLESHPGIG 927
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 639 SCFCLRLPLRV--ATAPVPKTVNQAVRL-DGLRLLLIEDNPLTQRITVEMLNTSGAQVVAIGNAAQALETLqNSEPFAAA 715
Cdd:PRK09959 928 TTFTITIPVEIsqQVATVEAKAEQPITLpEKLSILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKV-SMQHYDLL 1006
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 716 LVDFDLPDVNGITLARQLARQYPSLVLIGFSAHVideTLRQRTSSLFRGI---IPKPVPREVLGqllAHYLQL-QANNDL 791
Cdd:PRK09959 1007 ITDVNMPNMDGFELTRKLREQNSSLPIWGLTANA---QANEREKGLSCGMnlcLFKPLTLDVLK---THLSQLhQVAHIA 1080
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 792 P----LDVSQLN----EDAQLMgtekiHEWLALFTQHALPLLDEIDIARATQDSEKIKRAAHQLKSSCSSLGMRSASQLC 863
Cdd:PRK09959 1081 PqyrhLDIEALKnntaNDLQLM-----QEILMTFQHETHKDLPAAFHALEAGDNRTFHQCIHRIHGAANILNLQKLINIS 1155
|
....*....
gi 1447699372 864 AQLEQQPLS 872
Cdd:PRK09959 1156 HQLEITPVS 1164
|
|
| HATPase_c |
smart00387 |
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases. |
542-648 |
7.68e-37 |
|
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
Pssm-ID: 214643 [Multi-domain] Cd Length: 111 Bit Score: 133.93 E-value: 7.68e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 542 GDPRRIRQVITNLLSNALRFTDE-GQIVLRSRTDGEQWLVEVEDSGCGIDPAKLAEIFQPFIQVSG---KRGGTGLGLTI 617
Cdd:smart00387 1 GDPDRLRQVLSNLLDNAIKYTPEgGRITVTLERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKrsrKIGGTGLGLSI 80
|
90 100 110
....*....|....*....|....*....|.
gi 1447699372 618 SSRLAQAMGGELSATSTPEVGSCFCLRLPLR 648
Cdd:smart00387 81 VKKLVELHGGEISVESEPGGGTTFTITLPLE 111
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
432-648 |
4.41e-36 |
|
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: 143.19 E-value: 4.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 432 FLAAMSHEIRTPLYGILGTAQLLADNpALNAQRDDLRAITDSGESLLTILNDILDYSaieaggKNVSVSDEPFEPRPLLE 511
Cdd:COG5809 273 LAAGIAHEIRNPLTSLKGFIQLLKDT-IDEEQKTYLDIMLSELDRIESIISEFLVLA------KPQAIKYEPKDLNTLIE 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 512 STLQLMSGRVKGRPIRLATAIADDVPTaLMGDPRRIRQVITNLLSNALRFTDE-GQIVLR-SRTDGEQWLVEVEDSGCGI 589
Cdd:COG5809 346 EVIPLLQPQALLKNVQIELELEDDIPD-ILGDENQLKQVFINLLKNAIEAMPEgGNITIEtKAEDDDKVVISVTDEGCGI 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1447699372 590 DPAKLAEIFQPFIqvSGKRGGTGLGLTISSRLAQAMGGELSATSTPEVGSCFCLRLPLR 648
Cdd:COG5809 425 PEERLKKLGEPFY--TTKEKGTGLGLMVSYKIIEEHGGKITVESEVGKGTTFSITLPIK 481
|
|
| HATPase_c |
pfam02518 |
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ... |
542-648 |
7.26e-31 |
|
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.
Pssm-ID: 460579 [Multi-domain] Cd Length: 109 Bit Score: 117.08 E-value: 7.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 542 GDPRRIRQVITNLLSNALRFT---DEGQIVLRsrtDGEQWLVEVEDSGCGIDPAKLAEIFQPFIQV-SGKRGGTGLGLTI 617
Cdd:pfam02518 1 GDELRLRQVLSNLLDNALKHAakaGEITVTLS---EGGELTLTVEDNGIGIPPEDLPRIFEPFSTAdKRGGGGTGLGLSI 77
|
90 100 110
....*....|....*....|....*....|.
gi 1447699372 618 SSRLAQAMGGELSATSTPEVGSCFCLRLPLR 648
Cdd:pfam02518 78 VRKLVELLGGTITVESEPGGGTTVTLTLPLA 108
|
|
| PRK11360 |
PRK11360 |
two-component system sensor histidine kinase AtoS; |
391-648 |
1.71e-29 |
|
two-component system sensor histidine kinase AtoS;
Pssm-ID: 236901 [Multi-domain] Cd Length: 607 Bit Score: 125.08 E-value: 1.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 391 NRHREQLAAQV--KARTA--ELQELVieHRQARAeaekASQAKsaFLAAMSHEIRTPLYGILGTAQLLADNPALNAQRDD 466
Cdd:PRK11360 356 NTHGEMIGALVifSDLTErkRLQRRV--ARQERL----AALGE--LVAGVAHEIRNPLTAIRGYVQIWRQQTSDPPSQEY 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 467 LRAITDSGESLLTILNDILDYSaieaggKNVSVSDEPFEPRPLLESTLQLMSGRVKGRPIRLATAIADDVPTAlMGDPRR 546
Cdd:PRK11360 428 LSVVLREVDRLNKVIDQLLEFS------RPRESQWQPVSLNALVEEVLQLFQTAGVQARVDFETELDNELPPI-WADPEL 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 547 IRQVITNLLSNALR-FTDEGQIVLRSR--TDGEQwLVEVEDSGCGIDPAKLAEIFQPFIqvSGKRGGTGLGLTISSRLAQ 623
Cdd:PRK11360 501 LKQVLLNILINAVQaISARGKIRIRTWqySDGQV-AVSIEDNGCGIDPELLKKIFDPFF--TTKAKGTGLGLALSQRIIN 577
|
250 260
....*....|....*....|....*
gi 1447699372 624 AMGGELSATSTPEVGSCFCLRLPLR 648
Cdd:PRK11360 578 AHGGDIEVESEPGVGTTFTLYLPIN 602
|
|
| MtrAB_MtrB |
NF040691 |
MtrAB system histidine kinase MtrB; |
315-655 |
9.71e-29 |
|
MtrAB system histidine kinase MtrB;
Pssm-ID: 468655 [Multi-domain] Cd Length: 507 Bit Score: 121.29 E-value: 9.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 315 QYSLLLLGMVSLCALILILWrVVYRSVTRPLAEQTQALQRLLDGDIDspfpETAGVRELDTIGRLMDAFrssvhalnrhr 394
Cdd:NF040691 187 RGTLLLGGLALVVLLGLIAW-LVTRQVVAPVRSAARTAERFAAGDLS----ERMPVKGEDDLARLARSF----------- 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 395 EQLAAQVKARTAELQELviehrqaraeaekaSQAKSAFLAAMSHEIRTPLYGILGTAQLLADnpalnaQRDDLRAITDSG 474
Cdd:NF040691 251 NQMADSLQRQIRQLEEL--------------SRLQQRFVSDVSHELRTPLTTIRMAADVIHD------SRDDFDPATARS 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 475 ESLL--------TILNDILDYSAIEAGGknVSVSDEPFEPRPLLESTLQLMSGRVKGRPIRLaTAIADDVPTALMGDPRR 546
Cdd:NF040691 311 AELLhteldrfeSLLSDLLEISRFDAGA--AELDVEPVDLRPLVRRVVDALRQLAERAGVEL-RVDAPGTPVVAEVDPRR 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 547 IRQVITNLLSNALRFTDEGQIVLRSRTDGEQWLVEVEDSGCGIDPAKLAEIFQPFIQVSGKR----GGTGLGLTISSRLA 622
Cdd:NF040691 388 VERVLRNLVVNAIEHGEGKPVVVTVAQDDTAVAVTVRDHGVGLKPGEVALVFDRFWRADPARarttGGTGLGLAIALEDA 467
|
330 340 350
....*....|....*....|....*....|....*..
gi 1447699372 623 QAMGGELSATSTPEVGSCFCLRLPL----RVATAPVP 655
Cdd:NF040691 468 RLHGGWLEAWGRPGQGSQFRLTLPRvagdRLTTSPLP 504
|
|
| COG4192 |
COG4192 |
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ... |
1-646 |
3.53e-28 |
|
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal transduction mechanisms];
Pssm-ID: 443346 [Multi-domain] Cd Length: 640 Bit Score: 120.95 E-value: 3.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 1 MALLTLTSTLVGWYNLrfiSQVEKDNTQAL---IPTMNMARQLSEASAWELFAAQNLTSADNEKMWQAQGRMLTAQSLKI 77
Cdd:COG4192 21 SALLTLVASLVALFSW---NSLSNQIRYILddsLPKLQASLKLEENSNELVAALPEFAAATNTTERSQLRNQLNTQLADI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 78 NALLQALREQGFDTTAIEQQEQEISRSLRQQGELVGRRLQLRQQQQRLSQQIVAAADEIARLAQGQANNAATSAGATQAG 157
Cdd:COG4192 98 EELLAELEQLTQDAGDLRAAVADLRNLLQQLDSLLTQRIALRRRLQELLEQINWLHQDFNSELTPLLQEASWQQTRLLDS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 158 IYDLIEQDQRQAAESALDRLIDIDLEYVNQMNElRLSALRVQQMVMNLG-----LEQIQKNAPTLEkqlNNAVKILQRRQ 232
Cdd:COG4192 178 VETTESLRNLQNELQLLLRLLAIENQIVSLLRE-VAAARDQADVDNLFDrlqylKDELDRNLQALK---NYPSTITLRQL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 233 IriedpgvraqvATTLTTVSQYSDLLALFQQDSEISNHLQTLAQNNIAQFAQFSSEVSQLVDTIELRNQHGLAHLEKASA 312
Cdd:COG4192 254 I-----------DELLAIGSGEGGLPSLRRDELAAQATLEALAEENNSILEQLRTQISGLVGNSREQLVALNQETAQLVQ 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 313 RGQYSLLLLGMVSLCALILILWRVVYRSVTRPLAEQTQALQRLLDGDIDSPFPeTAGVRELDTIGRLMDAFRSSVhalNR 392
Cdd:COG4192 323 QSGILLLAIALLSLLLAVLINYFYVRRRLVKRLNALSDAMAAIAAGDLDVPIP-VDGNDEIGRIARLLRVFRDQA---IE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 393 HREQLAAQVKARTAelqelvIEHRQARAEAEKASQAKSAFL-AAM---SHEIRTPLYGIlgTAQLLADNPALNAQRDD-L 467
Cdd:COG4192 399 KTQELETEIEERKR------IEKNLRQTQDELIQAAKMAVVgQTMtslAHELNQPLNAM--SMYLFSAKKALEQENYAqL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 468 RAITDSGESLLTILNDILdySAIEAGGKNVSVSDEPFEPRPLLESTLQLMSGRVKGRPIRLAtaIADDVPtaLMGDPRRI 547
Cdd:COG4192 471 PTSLDKIEGLIERMDKII--KSLRQFSRKSDTPLQPVDLRQVIEQAWELVESRAKPQQITLH--IPDDLM--VQGDQVLL 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 548 RQVITNLLSNALR-FTDEGQIVLRSRTDGEQWLVEVEDSGCGIDPAKlaEIFQPFiqVSGKRGGTGLGLTISSRLAQAMG 626
Cdd:COG4192 545 EQVLVNLLVNALDaVATQPQISVDLLSNAENLRVAISDNGNGWPLVD--KLFTPF--TTTKEVGLGLGLSICRSIMQQFG 620
|
650 660
....*....|....*....|
gi 1447699372 627 GELSATSTPEVGSCFCLRLP 646
Cdd:COG4192 621 GDLYLASTLERGAMVILEFN 640
|
|
| phoR_proteo |
TIGR02966 |
phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory ... |
427-641 |
1.02e-26 |
|
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: 112.30 E-value: 1.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 427 QAKSAFLAAMSHEIRTPLYGILGTAQLLADNPALN--AQRDDLRAITDSGESLLTILNDILDYSAIEAGGKNvsVSDEPF 504
Cdd:TIGR02966 112 QMRRDFVANVSHELRTPLTVLRGYLETLADGPDEDpeEWNRALEIMLEQSQRMQSLVEDLLTLSRLESAASP--LEDEPV 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 505 EPRPLLESTLQLMSGRVKGRPIRLATAIadDVPTALMGDPRRIRQVITNLLSNALRFT-DEGQIVLRSRTDGEQWLVEVE 583
Cdd:TIGR02966 190 DMPALLDHLRDEAEALSQGKNHQITFEI--DGGVDVLGDEDELRSAFSNLVSNAIKYTpEGGTITVRWRRDGGGAEFSVT 267
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1447699372 584 DSGCGIDPAKLAEIFQPFIQV----SGKRGGTGLGLTISSRLAQAMGGELSATSTPEVGSCF 641
Cdd:TIGR02966 268 DTGIGIAPEHLPRLTERFYRVdksrSRDTGGTGLGLAIVKHVLSRHHARLEIESELGKGSTF 329
|
|
| BaeS_SmeS |
NF012163 |
sensor histidine kinase efflux regulator BaeS; |
401-646 |
1.91e-25 |
|
sensor histidine kinase efflux regulator BaeS;
Pssm-ID: 411086 [Multi-domain] Cd Length: 457 Bit Score: 110.69 E-value: 1.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 401 VKARTAELQELVIEHRQARAEAEKASQAKSAFLAAMSHEIRTPLYGILGTAQLLADNpALNAQRDDLRAITDSGESLLTI 480
Cdd:NF012163 212 TPTSNDELGKLAQDFNQLASTLEKNEQMRRDFMADISHELRTPLAVLRAELEAIQDG-IRKFTPESLDSLQAEVGTLTKL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 481 LNDILDYSAIEAGGknVSVSDEPFEPRPLLESTLQLMSGRVKGRPIRLATAIADDvpTALMGDPRRIRQVITNLLSNALR 560
Cdd:NF012163 291 VDDLHDLSMSDEGA--LAYQKASVDLVPLLEVEGGAFRERFASAGLELEVSLPDS--SLVFGDRDRLMQLFNNLLENSLR 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 561 FTDE-GQIVLRSRTDGEQWLVEVEDSGCGIDPAKLAEIFQPFIQVSGKR----GGTGLGLTISSRLAQAMGGELSATSTP 635
Cdd:NF012163 367 YTDSgGSLHISASQRPKEVTLTVADSAPGVSDEQLARLFERFYRVEVSRnrasGGSGLGLAISLNIVQAHGGTLHAAHSP 446
|
250
....*....|.
gi 1447699372 636 EVGSCFCLRLP 646
Cdd:NF012163 447 LGGLRIVVTLP 457
|
|
| PRK10549 |
PRK10549 |
two-component system sensor histidine kinase BaeS; |
396-647 |
2.08e-25 |
|
two-component system sensor histidine kinase BaeS;
Pssm-ID: 182539 [Multi-domain] Cd Length: 466 Bit Score: 110.88 E-value: 2.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 396 QLAA-----QVKARTA-ELQELVIEHRQARAEAEKASQAKSAFLAAMSHEIRTPLYGILGTaqlladnpaLNAQRDDLRA 469
Cdd:PRK10549 201 KLAAgdfttRVTPTSRdELGRLAQDFNQLASTLEKNEQMRRDFMADISHELRTPLAVLRGE---------LEAIQDGVRK 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 470 IT-DSGESL------LTILNDILdysaieaggKNVSVSDE--------PFEPRPLLESTLQLMSGRVKGRPIRLATAIAD 534
Cdd:PRK10549 272 FTpESVASLqaevgtLTKLVDDL---------HQLSLSDEgalayrktPVDLVPLLEVAGGAFRERFASRGLTLQLSLPD 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 535 DVPtaLMGDPRRIRQVITNLLSNALRFTDE-GQIVLRSRTDGEQWLVEVEDSGCGIDPAKLAEIFQPFIQVSGKR----G 609
Cdd:PRK10549 343 SAT--VFGDPDRLMQLFNNLLENSLRYTDSgGSLHISAEQRDKTLRLTFADSAPGVSDEQLQKLFERFYRTEGSRnrasG 420
|
250 260 270
....*....|....*....|....*....|....*...
gi 1447699372 610 GTGLGLTISSRLAQAMGGELSATSTPEVGSCFCLRLPL 647
Cdd:PRK10549 421 GSGLGLAICLNIVEAHNGRIIAAHSPFGGVSITVELPL 458
|
|
| PRK11100 |
PRK11100 |
sensory histidine kinase CreC; Provisional |
315-648 |
6.74e-25 |
|
sensory histidine kinase CreC; Provisional
Pssm-ID: 236846 [Multi-domain] Cd Length: 475 Bit Score: 109.16 E-value: 6.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 315 QYSLLLLGMVSLCALILILWrvvyrsVTRPLAEQTQALQRLLDGDIDsPFPETaGVRELDTIGRlmdafrssvhALNRHR 394
Cdd:PRK11100 186 WAGALLLGIALLIGAGVVWW------LNRSIRRLTRYADAVTEGKPV-PLPKL-GSSELRELAQ----------ALESMR 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 395 EQLAAqvkartaelqelviehrqaRAEAEKASQAksaflaaMSHEIRTPLYGILGTAQLLADNPALNAQRDDLRAITDSG 474
Cdd:PRK11100 248 VKLEG-------------------KAYVEQYVQT-------LTHELKSPLAAIRGAAELLQEDPPPEDRARFTGNILTQS 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 475 ESLLTILNDILDYSAIEAGGKNVSVsdEPFEPRPLLESTLQLMSGRVKGRPIRLATAIADdvpTALMGDPRRIRQVITNL 554
Cdd:PRK11100 302 ARLQQLIDRLLELARLEQRQELEVL--EPVALAALLEELVEAREAQAAAKGITLRLRPDD---ARVLGDPFLLRQALGNL 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 555 LSNALRFTDEG-QIVLRSRTDGEQWLVEVEDSGCGI-DPAkLAEIFQPFIQVS---GKRGGTGLGLTISSRLAQAMGGEL 629
Cdd:PRK11100 377 LDNAIDFSPEGgTITLSAEVDGEQVALSVEDQGPGIpDYA-LPRIFERFYSLPrpaNGRKSTGLGLAFVREVARLHGGEV 455
|
330
....*....|....*....
gi 1447699372 630 SATSTPEVGSCFCLRLPLR 648
Cdd:PRK11100 456 TLRNRPEGGVLATLTLPRH 474
|
|
| HATPase_AtoS-like |
cd16943 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
544-647 |
9.73e-25 |
|
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: 99.42 E-value: 9.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 544 PRRIRQVITNLLSNALRFTDE-GQIVLRSRTDGEQWLVEVEDSGCGIDPAKLAEIFQPFIQVSGKRGGTGLGLTISSRLA 622
Cdd:cd16943 1 PSQLNQVLLNLLVNAAQAMEGrGRITIRTWAHVDQVLIEVEDTGSGIDPEILGRIFDPFFTTKPVGEGTGLGLSLSYRII 80
|
90 100
....*....|....*....|....*
gi 1447699372 623 QAMGGELSATSTPEVGSCFCLRLPL 647
Cdd:cd16943 81 QKHGGTIRVASVPGGGTRFTIILPI 105
|
|
| KinA |
COG5805 |
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ... |
433-647 |
1.15e-24 |
|
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: 108.67 E-value: 1.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 433 LAA-MSHEIRTPLYGILGTAQLLadNPALNAQRDDLRAITDSGESLLTILNDILDYSaieaggKNVSVSDEPFEPRPLLE 511
Cdd:COG5805 290 LAAgIAHEIRNPLTSIKGFLQLL--QPGIEDKEEYFDIMLSELDRIESIISEFLALA------KPQAVNKEKENINELIQ 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 512 STLQLMSGRVKGRPIRLATAIADDVPTaLMGDPRRIRQVITNLLSNALR-FTDEGQIVLRSRTDGEQWLVEVEDSGCGID 590
Cdd:COG5805 362 DVVTLLETEAILHNIQIRLELLDEDPF-IYCDENQIKQVFINLIKNAIEaMPNGGTITIHTEEEDNSVIIRVIDEGIGIP 440
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1447699372 591 PAKLAEIFQPFIqvSGKRGGTGLGLTISSRLAQAMGGELSATSTPEVGSCFCLRLPL 647
Cdd:COG5805 441 EERLKKLGEPFF--TTKEKGTGLGLMVSYKIIENHNGTIDIDSKVGKGTTFTITLPL 495
|
|
| PRK10490 |
PRK10490 |
sensor protein KdpD; Provisional |
417-647 |
7.99e-24 |
|
sensor protein KdpD; Provisional
Pssm-ID: 236701 [Multi-domain] Cd Length: 895 Bit Score: 108.20 E-value: 7.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 417 QARAEAEKaSQAKSAFLAAMSHEIRTPLYGILGTAQLL-----ADNPALNAQRDDLRAITDSGESLLtilNDILDYSAIE 491
Cdd:PRK10490 653 QARLASER-EQLRNALLAALSHDLRTPLTVLFGQAEILtldlaSEGSPHARQASEIRQQVLNTTRLV---NNLLDMARIQ 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 492 AGGKNVSVSDEPFEPrpLLESTLQLMSGRVKGRPIRLAtaIADDVpTALMGDPRRIRQVITNLLSNALRFTDEG-QIVLR 570
Cdd:PRK10490 729 SGGFNLRKEWLTLEE--VVGSALQMLEPGLSGHPINLS--LPEPL-TLIHVDGPLFERVLINLLENAVKYAGAQaEIGID 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 571 SRTDGEQWLVEVEDSGCGIDPAKLAEIFQPFiqvsgKRG-------GTGLGLTISSRLAQAMGGELSATSTPEVGSCFCL 643
Cdd:PRK10490 804 AHVEGERLQLDVWDNGPGIPPGQEQLIFDKF-----ARGnkesaipGVGLGLAICRAIVEVHGGTIWAENRPEGGACFRV 878
|
....
gi 1447699372 644 RLPL 647
Cdd:PRK10490 879 TLPL 882
|
|
| PRK10604 |
PRK10604 |
sensor protein RstB; Provisional |
318-655 |
2.15e-23 |
|
sensor protein RstB; Provisional
Pssm-ID: 236724 [Multi-domain] Cd Length: 433 Bit Score: 104.30 E-value: 2.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 318 LLLLGMvSLcALILILWrvvYRSVTRPLAEQTQALQRLLDGDIDS--PFPETagvreldtigrlmdafrSSVHALNRHRE 395
Cdd:PRK10604 142 LALIGL-SL-AFPVFLW---MRPHWQDMLKLEAAAQRLGDGHLAEriHFDEG-----------------SSLERLGVAFN 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 396 QLAAQVKARTAelqelviehrqaraeaekasqAKSAFLAAMSHEIRTPL----YGILGTAQLLADNP-ALNAQRDDLRAI 470
Cdd:PRK10604 200 QMADNINALIA---------------------SKKQLIDGIAHELRTPLvrlrYRLEMSDNLSAAESqALNRDIGQLEAL 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 471 TdsgESLLTilndildYSAIEAggKNVSVSDEPFEPRPLLESTLQLMSGRVKGRPIRLATAIADDVptaLMGDPRRIRQV 550
Cdd:PRK10604 259 I---EELLT-------YARLDR--PQNELHLSEPDLPAWLSTHLADIQAVTPEKTVRLDTPHQGDY---GALDMRLMERV 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 551 ITNLLSNALRFTdEGQIVLRSRTDGEQWLVEVEDSGCGIDPAKLAEIFQPFIQVSGKR----GGTGLGLTISSRLAQAMG 626
Cdd:PRK10604 324 LDNLLNNALRYA-HSRVRVSLLLDGNQACLIVEDDGPGIPPEERERVFEPFVRLDPSRdratGGCGLGLAIVHSIALAMG 402
|
330 340
....*....|....*....|....*....
gi 1447699372 627 GELSATSTPEVGSCFCLRLPLRVATAPVP 655
Cdd:PRK10604 403 GSVNCDESELGGARFSFSWPVWHNLPQFT 431
|
|
| HATPase_BaeS-like |
cd16946 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
543-646 |
1.02e-22 |
|
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: 93.68 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 543 DPRRIRQVITNLLSNALRFTDE-GQIVLRSRTDGEQWLVEVEDSGCGIDPAKLAEIFQPFIQVSGKR----GGTGLGLTI 617
Cdd:cd16946 1 DRDRLQQLFVNLLENSLRYTDTgGKLRIRAAQTPQEVRLDVEDSAPGVSDDQLARLFERFYRVESSRnrasGGSGLGLAI 80
|
90 100
....*....|....*....|....*....
gi 1447699372 618 SSRLAQAMGGELSATSTPEVGSCFCLRLP 646
Cdd:cd16946 81 CHNIALAHGGTISAEHSPLGGLRLVLTLP 109
|
|
| PRK13837 |
PRK13837 |
two-component system VirA-like sensor kinase; |
397-783 |
1.61e-22 |
|
two-component system VirA-like sensor kinase;
Pssm-ID: 237526 [Multi-domain] Cd Length: 828 Bit Score: 103.99 E-value: 1.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 397 LAAQVKARTAELQELVIEHRQARAEAekaSQAKSAFLAAMSHEIRTPLYGILGTAQLLADN-PALNAQRDDLRAITDSGE 475
Cdd:PRK13837 421 LAHAIERRRLETERDALERRLEHARR---LEAVGTLASGIAHNFNNILGAILGYAEMALNKlARHSRAARYIDEIISAGA 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 476 SLLTILNDILDYSAI-EAGGKNVSVSDEPFEPRPLLESTLqlmsgrvkGRPIRLATAIADDvPTALMGDPRRIRQVITNL 554
Cdd:PRK13837 498 RARLIIDQILAFGRKgERNTKPFDLSELVTEIAPLLRVSL--------PPGVELDFDQDQE-PAVVEGNPAELQQVLMNL 568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 555 LSNALR-FTDEGQIVLR-SRTD--------------GEQWLVEVEDSGCGIDPAKLAEIFQPFIqvSGKRGGTGLGLTIS 618
Cdd:PRK13837 569 CSNAAQaMDGAGRVDISlSRAKlrapkvlshgvlppGRYVLLRVSDTGAGIDEAVLPHIFEPFF--TTRAGGTGLGLATV 646
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 619 SRLAQAMGGELSATSTPEVGSCFCLRLPL--RVATAPVPKTVNQAV-RLDGLRLLLIEDNPLTQRITVEMLNTSGAQVVA 695
Cdd:PRK13837 647 HGIVSAHAGYIDVQSTVGRGTRFDVYLPPssKVPVAPQAFFGPGPLpRGRGETVLLVEPDDATLERYEEKLAALGYEPVG 726
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 696 IGNAAQALETL-QNSEPFAAALVDFDLPDVNGITLARQLARQYPSLVLIGFSAHVIDETLRQRTSSLFrgiIPKPVPREV 774
Cdd:PRK13837 727 FSTLAAAIAWIsKGPERFDLVLVDDRLLDEEQAAAALHAAAPTLPIILGGNSKTMALSPDLLASVAEI---LAKPISSRT 803
|
....*....
gi 1447699372 775 LGQLLAHYL 783
Cdd:PRK13837 804 LAYALRTAL 812
|
|
| KinB |
COG5806 |
Sporulation sensor histidine kinase B [Cell cycle control, cell division, chromosome ... |
408-647 |
2.66e-21 |
|
Sporulation sensor histidine kinase B [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 444508 [Multi-domain] Cd Length: 412 Bit Score: 97.63 E-value: 2.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 408 LQELVIEHRQARAEAEKAS--QAKSAFLAAMSHEIRTPLYGILGTAQLLADNPALNAQRDDLRAIT----DSGESlltIL 481
Cdd:COG5806 178 LIENLIENILLRKELQRAEklEVVSELAASIAHEVRNPLTVVRGFIQLLQEPELSDEKRKQYIRIAleelDRAEA---II 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 482 NDILDYSaieaggKNVSVSDEPFEPRPLLESTLQLMSGRVKGRPIRLATAIADDVptALMGDPRRIRQVITNLLSNALR- 560
Cdd:COG5806 255 TDYLTFA------KPQPEKLEKIDVSEELEHVIDVLSPYANMNNVEIQTELEPGL--YIEGDRQKLQQCLINIIKNGIEa 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 561 FTDEGQIVLRSRTDGEQWLVEVEDSGCGIDPAKLAEIFQPFIqvSGKRGGTGLGLTISSRLAQAMGGELSATSTPEVGSC 640
Cdd:COG5806 327 MPNGGTLTIDVSIDKNKVIISIKDTGVGMTKEQLERLGEPYF--STKEKGTGLGTMVSYRIIEAMNGTIRVESEVGKGTT 404
|
....*..
gi 1447699372 641 FCLRLPL 647
Cdd:COG5806 405 FTITLPL 411
|
|
| REC_hyHK_CKI1_RcsC-like |
cd17546 |
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ... |
669-779 |
1.34e-20 |
|
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators similar to Arabidopsis thaliana CKI1 and Escherichia coli RcsC; This family is composed of hybrid sensor histidine kinases/response regulators that are sensor histidine kinases (HKs) fused with a REC domain, similar to the sensor histidine kinase CKI1 from Arabidopsis thaliana, which is involved in multi-step phosphorelay (MSP) signaling that mediates responses to a variety of important stimuli in plants. MSP involves a signal being transferred from HKs via histidine phosphotransfer proteins (AHP1-AHP5) to nuclear response regulators. The CKI1 REC domain specifically interacts with the downstream signaling protein AHP2, AHP3 and AHP5. The plant MSP system has evolved from the prokaryotic two-component system (TCS), which allows organisms to sense and respond to changes in environmental conditions. This family also includes bacterial hybrid sensor HKs such as Escherichia coli RcsC, which is a component of the Rcs signalling pathway that controls a variety of physiological functions like capsule synthesis, cell division, and motility. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381099 [Multi-domain] Cd Length: 113 Bit Score: 87.91 E-value: 1.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 669 LLLIEDNPLTQRITVEMLNTSGAQVVAIGNAAQALETLQnSEPFAAALVDFDLPDVNGITLA---RQLARQYPSLVLIGF 745
Cdd:cd17546 1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLK-EEPFDLVLMDLQMPVMDGLEATrriRELEGGGRRTPIIAL 79
|
90 100 110
....*....|....*....|....*....|....
gi 1447699372 746 SAHVIDETLRQRTSSLFRGIIPKPVPREVLGQLL 779
Cdd:cd17546 80 TANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
|
|
| CheY |
COG0784 |
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ... |
662-788 |
1.35e-20 |
|
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: 88.37 E-value: 1.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 662 VRLDGLRLLLIEDNPLTQRITVEMLNTSGAQVVAIGNAAQALETLQnSEPFAAALVDFDLPDVNGITLARQL--ARQYPS 739
Cdd:COG0784 1 PPLGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLR-AGPPDLILLDINMPGMDGLELLRRIraLPRLPD 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1447699372 740 LVLIGFSAHVIDETLRQRTSSLFRGIIPKPVPREVLGQLLAHYLQLQAN 788
Cdd:COG0784 80 IPIIALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARASA 128
|
|
| HATPase_TutC-TodS-like |
cd16925 |
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ... |
543-646 |
2.89e-20 |
|
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: 86.78 E-value: 2.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 543 DPRRIRQVITNLLSNALRFT-DEGQIVLR-SRTDGEQWLVEVEDSGCGIDPAKLAEIFQPFIQVSG----KRGGTGLGLT 616
Cdd:cd16925 1 DAEKYERVVLNLLSNAFKFTpDGGRIRCIlEKFRLNRFLLTVSDSGPGIPPNLREEIFERFRQGDGsstrAHGGTGLGLS 80
|
90 100 110
....*....|....*....|....*....|
gi 1447699372 617 ISSRLAQAMGGELSATSTPEVGSCFCLRLP 646
Cdd:cd16925 81 IVKEFVELHGGTVTVSDAPGGGALFQVELP 110
|
|
| envZ |
PRK09467 |
osmolarity sensor protein; Provisional |
314-647 |
3.88e-20 |
|
osmolarity sensor protein; Provisional
Pssm-ID: 236531 [Multi-domain] Cd Length: 435 Bit Score: 94.21 E-value: 3.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 314 GQYSLLLLGMVSLCALILI-LWRVVyRSVTRPLAEQTQALQRLLDGDIDSPFPEtAGVRELdtigrlmdafRSSVHALNr 392
Cdd:PRK09467 150 GDFSPLFRYTLAIGLLSVAgGWLFI-RIQNRPLVALEHAALQVGKGEIPPPLRE-YGASEV----------RSVTRAFN- 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 393 hreQLAAQVKartaELQelviehrQARAeaekasqaksAFLAAMSHEIRTPLYGI-LGTA------QLLADnpALNAQRD 465
Cdd:PRK09467 217 ---QMAAGIK----QLE-------DDRT----------LLMAGVSHDLRTPLTRIrLATEmmseedGYLAE--SINKDIE 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 466 DLRAI---------TDSGESL-LTILNDIL-DYSAIEAGGKNVsvsdepfeprplLESTLQLMSGRVKGRPIRlataiad 534
Cdd:PRK09467 271 ECNAIieqfidylrTGQEMPMeMADLNALLgEVIAAESGYERE------------IETALQPGPIEVPMNPIA------- 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 535 dvptalmgdprrIRQVITNLLSNALRFTdEGQIVLRSRTDGEQWLVEVEDSGCGIDPAKLAEIFQPFIQVSGKRG--GTG 612
Cdd:PRK09467 332 ------------IKRALANLVVNAARYG-NGWIKVSSGTEGKRAWFQVEDDGPGIPPEQLKHLFQPFTRGDSARGssGTG 398
|
330 340 350
....*....|....*....|....*....|....*
gi 1447699372 613 LGLTISSRLAQAMGGELSATSTPEVGSCFCLRLPL 647
Cdd:PRK09467 399 LGLAIVKRIVDQHNGKVELGNSEEGGLSARAWLPL 433
|
|
| PRK09303 |
PRK09303 |
histidine kinase; |
416-646 |
3.63e-19 |
|
histidine kinase;
Pssm-ID: 236462 [Multi-domain] Cd Length: 380 Bit Score: 90.40 E-value: 3.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 416 RQARAEAEKASQAKSAFLAAMSHEIRTPLygilgTAQLLA--------------DNPALNAQ-RDDLRAITDSGESLLTi 480
Cdd:PRK09303 138 RQENETLLEQLKFKDRVLAMLAHDLRTPL-----TAASLAletlelgqidedteLKPALIEQlQDQARRQLEEIERLIT- 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 481 lnDILdysaiEAG-GKNvsvSDEPFEPRPL------LESTLQLMSgRVKGRPIRLATAIADDVPTaLMGDPRRIRQVITN 553
Cdd:PRK09303 212 --DLL-----EVGrTRW---EALRFNPQKLdlgslcQEVILELEK-RWLAKSLEIQTDIPSDLPS-VYADQERIRQVLLN 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 554 LLSNALRFTDEG---QIVLRSRTDgeQWL-VEVEDSGCGIDPAKLAEIFQPFI--QVSGKRGGTGLGLTISSRLAQAMGG 627
Cdd:PRK09303 280 LLDNAIKYTPEGgtiTLSMLHRTT--QKVqVSICDTGPGIPEEEQERIFEDRVrlPRDEGTEGYGIGLSVCRRIVRVHYG 357
|
250
....*....|....*....
gi 1447699372 628 ELSATSTPEVGSCFCLRLP 646
Cdd:PRK09303 358 QIWVDSEPGQGSCFHFTLP 376
|
|
| PRK10364 |
PRK10364 |
two-component system sensor histidine kinase ZraS; |
334-649 |
4.89e-19 |
|
two-component system sensor histidine kinase ZraS;
Pssm-ID: 236674 [Multi-domain] Cd Length: 457 Bit Score: 91.00 E-value: 4.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 334 WRVVYRSVTRPLAE---QTQALQRLLDGDID-SPFPETAGVRELDTIGrlmdaFRSSVHALNRHREQ------LAAQVKA 403
Cdd:PRK10364 129 WRRIDSADGEPVLEiyrQFQPMFAAGMHGMRhMQQYAAANTPQAIFIA-----FDASNLVSAQAREQrntliiLFALATV 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 404 RTAELQELVIEHRQARA----EAEKASQAKSAFL----AAMSHEIRTPLYGILGTAQLLADN-PALNAQRDDLRAITDSG 474
Cdd:PRK10364 204 LLASLLAFFWYRRYLRSrqllQDEMKRKEKLVALghlaAGVAHEIRNPLSSIKGLAKYFAERaPAGGEAHQLAQVMAKEA 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 475 ESLLTILNDILDYSaieaggKNVSVSDEPFEPRPLLESTLQLMSGRVKGRPIRLATAIADDVPtALMGDPRRIRQVITNL 554
Cdd:PRK10364 284 DRLNRVVSELLELV------KPTHLALQAVDLNDLINHSLQLVSQDANSREIQLRFTANDTLP-EIQADPDRLTQVLLNL 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 555 LSNALRFTDE-GQIVLRSRTDGEQWLVEVEDSGCGIDPAKLAEIFQPFIqvSGKRGGTGLGLTISSRLAQAMGGELSATS 633
Cdd:PRK10364 357 YLNAIQAIGQhGVISVTASESGAGVKISVTDSGKGIAADQLEAIFTPYF--TTKAEGTGLGLAVVHNIVEQHGGTIQVAS 434
|
330
....*....|....*.
gi 1447699372 634 TPEVGSCFCLRLPLRV 649
Cdd:PRK10364 435 QEGKGATFTLWLPVNI 450
|
|
| cztS_silS_copS |
TIGR01386 |
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ... |
406-646 |
6.45e-19 |
|
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: 90.52 E-value: 6.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 406 AELQELVIEHRQARAEAEKASQAKSAFLAAMSHEIRTPLYGILGTAQLladnpALNAQRD--DLRAITDSG----ESLLT 479
Cdd:TIGR01386 218 AELRELAQSFNAMLGRLEDAFQRLSQFSADLAHELRTPLTNLLGQTQV-----ALSQPRTgeEYREVLESNleelERLSR 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 480 ILNDIL------------DYSAIEAGGKNVSVSDEpFEprPLLESTLQLMSGRVKGRpirlataiaddvptaLMGDPRRI 547
Cdd:TIGR01386 293 MVSDMLflaradngqlalERVRLDLAAELAKVAEY-FE--PLAEERGVRIRVEGEGL---------------VRGDPQMF 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 548 RQVITNLLSNALRFTDEGQ-IVLRSRTDGEQWLVEVEDSGCGIDPAKLAEIFQPFIQVSGKR----GGTGLGLTISSRLA 622
Cdd:TIGR01386 355 RRAISNLLSNALRHTPDGGtITVRIERRSDEVRVSVSNPGPGIPPEHLSRLFDRFYRVDPARsnsgEGTGLGLAIVRSIM 434
|
250 260
....*....|....*....|....
gi 1447699372 623 QAMGGELSATStPEVGSCFCLRLP 646
Cdd:TIGR01386 435 EAHGGRASAES-PDGKTRFILRFP 457
|
|
| HATPase_FilI-like |
cd16921 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
547-646 |
7.57e-19 |
|
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Methanosaeta harundinacea FilI and some hybrid sensor histidine kinases; This family includes FilI, the histidine kinase (HK) component of FilI-FilRs, a two-component signal transduction system (TCS) of the methanogenic archaeon, Methanosaeta harundinacea, which is involved in regulating methanogenesis. The cytoplasmic HK core consists of a C-terminal HK-like ATPase domain (represented here) and a histidine kinase dimerization and phosphoacceptor domain (HisKA) domain, which, in FilI, are coupled to CHASE, HAMP, PAS, and GAF sensor domains. FilI-FilRs catalyzes the phosphotransfer between FilI (HK) and FilRs (FilR1 and FilR2, response regulators) of the TCS. TCSs are predicted to be of bacterial origin, and acquired by archaea by horizontal gene transfer. This model also includes related HATPase domains such as that of Synechocystis sp. PCC6803 phytochrome-like protein Cph1. Proteins having this HATPase domain and HisKA domain also have accessory sensor domains such as CHASE, GAF, HAMP and PAS; some are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.
Pssm-ID: 340398 [Multi-domain] Cd Length: 105 Bit Score: 82.37 E-value: 7.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 547 IRQVITNLLSNALRFTDEG---QIVLRSRTDGEQWLVEVEDSGCGIDP---AKLAEIFQPfIQVSGKRGGTGLGLTISSR 620
Cdd:cd16921 1 LGQVLTNLLGNAIKFRRPRrppRIEVGAEDVGEEWTFYVRDNGIGIDPeyaEKVFGIFQR-LHSREEYEGTGVGLAIVRK 79
|
90 100
....*....|....*....|....*.
gi 1447699372 621 LAQAMGGELSATSTPEVGSCFCLRLP 646
Cdd:cd16921 80 IIERHGGRIWLESEPGEGTTFYFTLP 105
|
|
| HATPase_RstB-like |
cd16939 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
550-647 |
1.71e-18 |
|
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: 81.71 E-value: 1.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 550 VITNLLSNALRFTDEgQIVLRSRTDGEQWLVEVEDSGCGIDPAKLAEIFQPFIQVSGKR----GGTGLGLTISSRLAQAM 625
Cdd:cd16939 4 ALDNLLRNALRYAHR-TVRIALLVSGGRLTLIVEDDGPGIPAAARERVFEPFVRLDPSRdratGGFGLGLAIVHRVALWH 82
|
90 100
....*....|....*....|..
gi 1447699372 626 GGELSATSTPEVGSCFCLRLPL 647
Cdd:cd16939 83 GGHVECDDSELGGACFRLTWPR 104
|
|
| HATPase_TmoS-FixL-DctS-like |
cd16920 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
547-646 |
2.36e-18 |
|
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: 81.29 E-value: 2.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 547 IRQVITNLLSNALRFTDEG-----QIVLRSRTDGEQWL-VEVEDSGCGIDPAKLAEIFQPFiqVSGKRGGTGLGLTISSR 620
Cdd:cd16920 1 IQQVLINLVRNGIEAMSEGgcerrELTIRTSPADDRAVtISVKDTGPGIAEEVAGQLFDPF--YTTKSEGLGMGLSICRS 78
|
90 100
....*....|....*....|....*.
gi 1447699372 621 LAQAMGGELSATSTPEVGSCFCLRLP 646
Cdd:cd16920 79 IIEAHGGRLSVESPAGGGATFQFTLP 104
|
|
| HATPase_CpxA-like |
cd16949 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
549-647 |
1.19e-17 |
|
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: 79.29 E-value: 1.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 549 QVITNLLSNALRFTDEgQIVLRSRTDGEQWLVEVEDSGCGIDPAKLAEIFQPFIQVSGKR----GGTGLGLTISSRLAQA 624
Cdd:cd16949 3 RALENVLRNALRYSPS-KILLDISQDGDQWTITITDDGPGVPEDQLEQIFLPFYRVDSARdresGGTGLGLAIAERAIEQ 81
|
90 100
....*....|....*....|...
gi 1447699372 625 MGGELSATSTPEVGSCFCLRLPL 647
Cdd:cd16949 82 HGGKIKASNRKPGGLRVRIWLPA 104
|
|
| HPT |
smart00073 |
Histidine Phosphotransfer domain; Contains an active histidine residue that mediates ... |
805-891 |
1.23e-17 |
|
Histidine Phosphotransfer domain; Contains an active histidine residue that mediates phosphotransfer reactions. Domain detected only in eubacteria. This alignment is an extension to that shown in the Cell structure paper.
Pssm-ID: 197502 [Multi-domain] Cd Length: 92 Bit Score: 78.44 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 805 MGTEKIHEWLALFTQHALPLLDEIDIARATQDSEKIKRAAHQLKSSCSSLGMRSASQLCAQLEQQPLSAPLPHEEITRSV 884
Cdd:smart00073 1 GGLELFREELAEFLQSLEEGLLELEKALDAQDVNEIFRAAHTLKGSAGSLGLQQLAQLCHQLENLLDALRSGEVELTPDL 80
|
....*..
gi 1447699372 885 AALEAWL 891
Cdd:smart00073 81 LDLLLEL 87
|
|
| HATPase_EnvZ-like |
cd16950 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
547-629 |
2.31e-17 |
|
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: 78.26 E-value: 2.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 547 IRQVITNLLSNALRFTDeGQIVLRSRTDGEQWLVEVEDSGCGIDPAKLAEIFQPFIQVSGKRG--GTGLGLTISSRLAQA 624
Cdd:cd16950 1 LKRVLSNLVDNALRYGG-GWVEVSSDGEGNRTRIQVLDNGPGIAPEEVDELFQPFYRGDNARGtsGTGLGLAIVQRISDA 79
|
....*
gi 1447699372 625 MGGEL 629
Cdd:cd16950 80 HGGSL 84
|
|
| YesM |
COG2972 |
Sensor histidine kinase YesM [Signal transduction mechanisms]; |
172-648 |
2.58e-16 |
|
Sensor histidine kinase YesM [Signal transduction mechanisms];
Pssm-ID: 442211 [Multi-domain] Cd Length: 445 Bit Score: 82.37 E-value: 2.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 172 SALDRLIDIDLEYVNQMNELRLSALRVQQMVMNLGLEQIQKNAPTLEKQLNNAVKILQRRQIRIEDPGVRAQVATTLTTV 251
Cdd:COG2972 7 LLSIVLLLLILLLLVLLILLLSLLLIILLLLLLLILLLLLLILLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLLILLLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 252 SQYSDLLALFQQDSEISNHLQTLAQNNIAQFAQFSSEVSQLVDTIELRNQHGLAHLEK-----ASARGQYSLLLLGMVSL 326
Cdd:COG2972 87 LLLLLLLILLLSLLLLLALILLLALLLLLSILLLILGLLLIILLLLSLLGWTLVSLIPkselfRGLFSLRRLILLIILLL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 327 CALILILWRVVYRSVTRPLAEQTQALQRLLDGDIdspfpETAGVRELDTIGRLMDAFRSSVHALNR-HREQLAAQVKART 405
Cdd:COG2972 167 LLLALLLSYLLSRSITRPIKRLKKAMKKVEKGDL-----VRLEVSGNDEIGILARSFNEMVERIKElIEEVYELELEKKE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 406 AELQELviehrQARaeaekasqaksaflaamsheIRtP--LYGILGTAQLLADnpalnaQRDDLRAitdsgESLLTILND 483
Cdd:COG2972 242 AELKAL-----QAQ--------------------IN-PhfLFNTLNSIRWLAE------LEDPEEA-----EEMLEALSK 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 484 ILDYSaIEAGGKNVSVSDEpFEprpLLESTLQLMSGRVKGRpIRLATAIADDVPTALMgdPRRIRQVitnLLSNALRF-- 561
Cdd:COG2972 285 LLRYS-LSKGDELVTLEEE-LE---LIKSYLEIQKLRFGDR-LEVEIEIDEELLDLLI--PKLILQP---LVENAIEHgi 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 562 ---TDEGQIVLRSRTDGEQWLVEVEDSGCGIDPAKLAEIFQPFiqvSGKRGGTGLGL-TISSRLAQAMGGE--LSATSTP 635
Cdd:COG2972 354 epkEGGGTIRISIRKEGDRLVITVEDNGVGMPEEKLEKLLEEL---SSKGEGRGIGLrNVRERLKLYYGEEygLEIESEP 430
|
490
....*....|...
gi 1447699372 636 EVGSCFCLRLPLR 648
Cdd:COG2972 431 GEGTTVTIRIPLE 443
|
|
| HATPase_HupT_MifS-like |
cd16976 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
547-645 |
4.46e-16 |
|
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: 74.42 E-value: 4.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 547 IRQVITNLLSNALRFT---DEGQIVLRSRTDGEQWLVEVEDSGCGIDPAKLAEIFQPFIQVSGKRGGTGLGLTISSRLAQ 623
Cdd:cd16976 1 IQQVLMNLLQNALDAMgkvENPRIRIAARRLGGRLVLVVRDNGPGIAEEHLSRVFDPFFTTKPVGKGTGLGLSISYGIVE 80
|
90 100
....*....|....*....|..
gi 1447699372 624 AMGGELSATSTPEVGSCFCLRL 645
Cdd:cd16976 81 EHGGRLSVANEEGAGARFTFDL 102
|
|
| CitB |
COG4565 |
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ... |
664-792 |
6.30e-16 |
|
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal transduction mechanisms];
Pssm-ID: 443622 [Multi-domain] Cd Length: 138 Bit Score: 75.39 E-value: 6.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 664 LDGLRLLLIEDNPLTQRITVEMLN-TSGAQVVAI-GNAAQALETLQNSEPfAAALVDFDLPDVNGITLARQLARQYPSLV 741
Cdd:COG4565 1 MKMIRVLIVEDDPMVAELLRRYLErLPGFEVVGVaSSGEEALALLAEHRP-DLILLDIYLPDGDGLELLRELRARGPDVD 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1447699372 742 LIGFSAHVIDETLRQRTSSLFRGIIPKPVPREVLGQLLAHYLQLQA------NNDLP 792
Cdd:COG4565 80 VIVITAARDPETVREALRAGVVDYLIKPFTFERLREALERYLEYRRllredqEEDLP 136
|
|
| HisKA |
pfam00512 |
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ... |
428-493 |
6.74e-16 |
|
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine kinases.
Pssm-ID: 459839 [Multi-domain] Cd Length: 66 Bit Score: 72.63 E-value: 6.74e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1447699372 428 AKSAFLAAMSHEIRTPLYGILGTAQLLADNPALNAQRDDLRAITDSGESLLTILNDILDYSAIEAG 493
Cdd:pfam00512 1 AKSEFLANLSHELRTPLTAIRGYLELLRDEKLDEEQREYLETILRSAERLLRLINDLLDLSRIEAG 66
|
|
| CitA |
COG3290 |
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ... |
414-648 |
1.07e-15 |
|
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction mechanisms];
Pssm-ID: 442519 [Multi-domain] Cd Length: 389 Bit Score: 79.89 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 414 EHRQARAEAEKASQAKSAF--LAAMSHEIRTPLYGILGTAQLladnpalNAQRDDLRAITDSGESLLTILNDILDYSAIe 491
Cdd:COG3290 172 DRTELERLEEELEGVKELAeaLRAQRHDFRNHLHTISGLLQL-------GEYDEALEYIDEISEELQELIDSLLSRIGN- 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 492 aggknvsvsdepfeprPLLESTLQLMSGRVKGRPIRLATAIADDVPTALMgDPRRIRQVITNLLSNALR-----FTDEGQ 566
Cdd:COG3290 244 ----------------PVLAALLLGKAARARERGIDLTIDIDSDLPDLPL-SDTDLVTILGNLLDNAIEaveklPEEERR 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 567 IVLRSRTDGEQWLVEVEDSGCGIDPAKLAEIFQPfiQVSGKRG-GTGLGLTISSRLAQAMGGELSATSTPEVGSCFCLRL 645
Cdd:COG3290 307 VELSIRDDGDELVIEVEDSGPGIPEELLEKIFER--GFSTKLGeGRGLGLALVKQIVEKYGGTIEVESEEGEGTVFTVRL 384
|
...
gi 1447699372 646 PLR 648
Cdd:COG3290 385 PKE 387
|
|
| PRK10755 |
PRK10755 |
two-component system sensor histidine kinase PmrB; |
317-653 |
1.56e-15 |
|
two-component system sensor histidine kinase PmrB;
Pssm-ID: 236751 [Multi-domain] Cd Length: 356 Bit Score: 79.24 E-value: 1.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 317 SLLLLGMVSLCALILILWRVVYRsVTRPLAEQTQALQRLlDGDIDSPFPETAGVRELDTIgrlmdafrssVHALNrhreQ 396
Cdd:PRK10755 62 SLLVPSLVMVSLTLLICFQAVRW-ITRPLAELQKELEAR-TADNLTPIAIHSSTLEIEAV----------TSALN----Q 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 397 LAAQvkartaeLQELVIEHRQaraeaekasqaksaFLAAMSHEIRTPLYGILGTAQLLA-----DNPALNAQRDDLraiT 471
Cdd:PRK10755 126 LVSR-------LTSTLDQERL--------------FTADVAHELRTPLAGIRLHLELLEkqhhiDVAPLIARLDQM---M 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 472 DSGESLLTIlndildySAIE---AGG--KNVSVSDEPFEP-RPLLESTLQLmsgrvKGRPIRLATAIADDVptaLMGDPR 545
Cdd:PRK10755 182 HTVEQLLQL-------ARAGqsfSSGhyQTVKLLEDVILPsQDELSEMLEQ-----RQQTLLLPESAADIT---VQGDAT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 546 RIRQVITNLLSNALRFTDEG-QIVLRSRTDGEQWLVEVEDSGCGIDPAKLAEIFQPFIQVSGKRGGTGLGLTISSRLAQA 624
Cdd:PRK10755 247 LLRLLLRNLVENAHRYSPEGsTITIKLSQEDGGAVLAVEDEGPGIDESKCGELSKAFVRMDSRYGGIGLGLSIVSRITQL 326
|
330 340 350
....*....|....*....|....*....|
gi 1447699372 625 MGGELSATSTPEV-GSCFCLRLPLRVATAP 653
Cdd:PRK10755 327 HHGQFFLQNRQERsGTRAWVWLPKAQNVAN 356
|
|
| HisKA |
smart00388 |
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ... |
428-493 |
3.18e-15 |
|
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine kinases.
Pssm-ID: 214644 [Multi-domain] Cd Length: 66 Bit Score: 70.67 E-value: 3.18e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1447699372 428 AKSAFLAAMSHEIRTPLYGILGTAQLLADNPALNAQRDDLRAITDSGESLLTILNDILDYSAIEAG 493
Cdd:smart00388 1 AKREFLANLSHELRTPLTAIRGYLELLLDTELSEEQREYLETILREAERLLRLINDLLDLSRIEAG 66
|
|
| PRK10618 |
PRK10618 |
phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional |
409-694 |
4.43e-15 |
|
phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional
Pssm-ID: 236726 [Multi-domain] Cd Length: 894 Bit Score: 79.98 E-value: 4.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 409 QELVIEHR--QARAEAEKASQAKSAFLAAMSHEIRTPLYGILGTAQLLADNPALNAQRDDLRAITDSGESLLTILNDILD 486
Cdd:PRK10618 428 REVLVNKKlqQAQREYEKNQQARKAFLQNIGDELKQPLQSLAQLAAQLRQTSDEEQQQPELDQLAEQSDVLVRLVDNIQL 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 487 YSAIEAGgkNVSVSDEPFEPRPLLESTLQLMSGRVKGRPIRLATAIADDVPTALMGDPRRIRQVITNLLSNALRFTDEGQ 566
Cdd:PRK10618 508 LNMLETQ--DWKPEQELFSLQDLIDEVLPEVLPAIKRKGLQLLIHNHLKAEQLRIGDRDALRKILLLLLNYAITTTAYGK 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 567 IVLRSRTDG---EQWLVEVEDSGCGIDPAKLAEIFQPFI-QVSGKRGGTGLGLT--ISSRLAQAMGGELSATSTPEVGSC 640
Cdd:PRK10618 586 ITLEVDQDEsspDRLTIRILDTGAGVSIKELDNLHFPFLnQTQGDRYGKASGLTffLCNQLCRKLGGHLTIKSREGLGTR 665
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1447699372 641 FCLRLPLRVATAPVPKTVNQAvrLDGLRLLLIEDNPLTQRITVEMLNTSGAQVV 694
Cdd:PRK10618 666 YSIHLKMLAADPEVEEEEEKL--LDGVTVLLDITSEEVRKIVTRQLENWGATCI 717
|
|
| AtoC |
COG2204 |
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ... |
668-787 |
8.12e-15 |
|
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, and a Fis-type DNA-binding domains [Signal transduction mechanisms];
Pssm-ID: 441806 [Multi-domain] Cd Length: 418 Bit Score: 77.70 E-value: 8.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 668 RLLLIEDNPLTQRITVEMLNTSGAQVVAIGNAAQALETLQNsEPFAAALVDFDLPDVNGITLARQLARQYPSLVLIGFSA 747
Cdd:COG2204 4 RILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLRE-EPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILLTG 82
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1447699372 748 HVIDETLRQRTSSLFRGIIPKPVPREVLGQLLAHYLQLQA 787
Cdd:COG2204 83 YGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRR 122
|
|
| REC |
cd00156 |
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ... |
670-769 |
9.45e-15 |
|
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: 70.72 E-value: 9.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 670 LLIEDNPLTQRITVEMLNTSGAQVVAIGNAAQALETLQNsEPFAAALVDFDLPDVNGITLARQLARQYPSLVLIGFSAHV 749
Cdd:cd00156 1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLRE-ERPDLVLLDLMMPGMDGLELLRKLRELPPDIPVIVLTAKA 79
|
90 100
....*....|....*....|
gi 1447699372 750 IDETLRQRTSSLFRGIIPKP 769
Cdd:cd00156 80 DEEDAVRALELGADDYLVKP 99
|
|
| glnL |
PRK11073 |
nitrogen regulation protein NR(II); |
344-648 |
3.05e-14 |
|
nitrogen regulation protein NR(II);
Pssm-ID: 182947 [Multi-domain] Cd Length: 348 Bit Score: 75.12 E-value: 3.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 344 PLAEQ--TQALQRLLDgdidSPFPETAGVRELDtIGRLMDAFRSS----------VHALNRHREQLAAQVKARTAELQEL 411
Cdd:PRK11073 34 PAAQQllAQSSRKLFG----TPLPELLSYFSLN-IELMRESLQAGqgftdnevtlVIDGRSHILSLTAQRLPEGMILLEM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 412 VIEHRQARAEAEKASQAKSAflAA------MSHEIRTPLYGILGTAQLLAD---NPALN-------AQRDDLRAITDSge 475
Cdd:PRK11073 109 APMDNQRRLSQEQLQHAQQV--AArdlvrgLAHEIKNPLGGLRGAAQLLSKalpDPALTeytkviiEQADRLRNLVDR-- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 476 sLLtilndildysAIEAGGKNVSVSdepfePRPLLESTLQLMSGRvKGRPIRLATAIADDVPTALMgDPRRIRQVITNLL 555
Cdd:PRK11073 185 -LL----------GPQRPGTHVTES-----IHKVAERVVQLVSLE-LPDNVRLIRDYDPSLPELAH-DPDQIEQVLLNIV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 556 SNALRFTDE--GQIVLRSRTD------GEQWL----VEVEDSGCGIDPAKLAEIFQPFiqVSGKRGGTGLGLTISSRLAQ 623
Cdd:PRK11073 247 RNALQALGPegGTITLRTRTAfqltlhGERYRlaarIDIEDNGPGIPPHLQDTLFYPM--VSGREGGTGLGLSIARNLID 324
|
330 340
....*....|....*....|....*
gi 1447699372 624 AMGGELSATSTPEvGSCFCLRLPLR 648
Cdd:PRK11073 325 QHSGKIEFTSWPG-HTEFSVYLPIR 348
|
|
| PRK13557 |
PRK13557 |
histidine kinase; Provisional |
510-740 |
7.63e-14 |
|
histidine kinase; Provisional
Pssm-ID: 237425 [Multi-domain] Cd Length: 540 Bit Score: 75.09 E-value: 7.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 510 LESTLQLMSGRVKGRPIRLATAIADDVPTALMgDPRRIRQVITNLLSNA-------LRFTDEGQIVLRSRTDGEQWL--- 579
Cdd:PRK13557 242 LVSGMGELAERTLGDAVTIETDLAPDLWNCRI-DPTQAEVALLNVLINArdampegGRVTIRTRNVEIEDEDLAMYHglp 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 580 ------VEVEDSGCGIDPAKLAEIFQPFIQVSGKRGGTGLGLTISSRLAQAMGGELSATSTPEVGSCFCLRLPL-RVATA 652
Cdd:PRK13557 321 pgryvsIAVTDTGSGMPPEILARVMDPFFTTKEEGKGTGLGLSMVYGFAKQSGGAVRIYSEVGEGTTVRLYFPAsDQAEN 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 653 PVPKTVNQAVRLDGL-RLLLIEDNPLTQRITVEMLNTSGAQVVAIGNAAQALETLQNSEPFAAALVDFDLP-DVNGITLA 730
Cdd:PRK13557 401 PEQEPKARAIDRGGTeTILIVDDRPDVAELARMILEDFGYRTLVASNGREALEILDSHPEVDLLFTDLIMPgGMNGVMLA 480
|
250
....*....|
gi 1447699372 731 RQLARQYPSL 740
Cdd:PRK13557 481 REARRRQPKI 490
|
|
| RpfG |
COG3437 |
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ... |
667-805 |
1.01e-13 |
|
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: 71.35 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 667 LRLLLIEDNPLTQRITVEMLNTSGAQVVAIGNAAQALETLQnSEPFAAALVDFDLPDVNGITLARQLaRQYPS---LVLI 743
Cdd:COG3437 7 PTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLL-EAPPDLILLDVRMPGMDGFELLRLL-RADPStrdIPVI 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1447699372 744 GFSAHVIDETLRQRTSSLFRGIIPKPVPREVLGQLLAHYLQLQANNDLPLDVSQLNEDAQLM 805
Cdd:COG3437 85 FLTALADPEDRERALEAGADDYLTKPFDPEELLARVRNALELRRLQRELDDLVLYLKLAAPL 146
|
|
| HATPase_YcbM-like |
cd16947 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
535-645 |
1.79e-13 |
|
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis YcbM; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Bacillus subtilis YcbM, a HK of the two-component system YcbM-YcbL. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA).
Pssm-ID: 340423 [Multi-domain] Cd Length: 125 Bit Score: 67.92 E-value: 1.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 535 DVPTALMGDPRRIRQVITNLLSNALRFTDEGQIV-LRSRTDGEQWLVEVEDSGCGIDPAKLAEIFQPFIQVSGKRG---- 609
Cdd:cd16947 9 DRPIYANANTEALQRILKNLISNAIKYGSDGKFLgMTLREDEKHVYIDIWDKGKGISETEKDHVFERLYTLEDSRNsakq 88
|
90 100 110
....*....|....*....|....*....|....*.
gi 1447699372 610 GTGLGLTISSRLAQAMGGELSATSTPEVGSCFCLRL 645
Cdd:cd16947 89 GNGLGLTITKRLAESMGGSIYVNSKPYEKTVFTVTL 124
|
|
| HisKA |
cd00082 |
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ... |
426-488 |
1.92e-13 |
|
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed through parallel association of 2 domains creating 4-helix bundles; usually these domains contain a conserved His residue and are activated via trans-autophosphorylation by the catalytic domain of the histidine kinase. They subsequently transfer the phosphoryl group to the Asp acceptor residue of a response regulator protein. Two-component signalling systems, consisting of a histidine protein kinase that senses a signal input and a response regulator that mediates the output, are ancient and evolutionarily conserved signaling mechanisms in prokaryotes and eukaryotes.
Pssm-ID: 119399 [Multi-domain] Cd Length: 65 Bit Score: 65.70 E-value: 1.92e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1447699372 426 SQAKSAFLAAMSHEIRTPLYGILGTAQLLADNPALNA-QRDDLRAITDSGESLLTILNDILDYS 488
Cdd:cd00082 1 LQAKGEFLANVSHELRTPLTAIRGALELLEEELLDDEeQREYLERIREEAERLLRLINDLLDLS 64
|
|
| phoR |
PRK11006 |
phosphate regulon sensor histidine kinase PhoR; |
428-649 |
3.35e-13 |
|
phosphate regulon sensor histidine kinase PhoR;
Pssm-ID: 182895 [Multi-domain] Cd Length: 430 Bit Score: 72.74 E-value: 3.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 428 AKSAFLAAMSHEIRTPLYGILGTAQLLADNPALNAQRDD-LRAITDSGESLLTILNDILDYSAIEAGGK---NVSVsDEP 503
Cdd:PRK11006 203 ARRNFFANVSHELRTPLTVLQGYLEMMQDQPLEGALREKaLHTMREQTQRMEGLVKQLLTLSKIEAAPTidlNEKV-DVP 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 504 FEPRPLLESTLQLMSGRVKgrpirlataIADDVPTAL--MGDPRRIRQVITNLLSNALRFTDEG-QIVLRSRTDGEQWLV 580
Cdd:PRK11006 282 MMLRVLEREAQTLSQGKHT---------ITFEVDNSLkvFGNEDQLRSAISNLVYNAVNHTPEGtHITVRWQRVPQGAEF 352
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1447699372 581 EVEDSGCGIDPAKLAEIFQPFIQVSGKR----GGTGLGLTISSRLAQAMGGELSATSTPEVGSCFCLRLPLRV 649
Cdd:PRK11006 353 SVEDNGPGIAPEHIPRLTERFYRVDKARsrqtGGSGLGLAIVKHALSHHDSRLEIESEVGKGTRFSFVLPERL 425
|
|
| HATPase_Glnl-NtrB-like |
cd16918 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
549-635 |
4.18e-13 |
|
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: 66.27 E-value: 4.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 549 QVITNLLSNALRFTDE--GQIVLRSRTDGEQWL----------VEVEDSGCGIDPAKLAEIFQPFiqVSGKRGGTGLGLT 616
Cdd:cd16918 3 QVFLNLVRNAAQALAGsgGEIILRTRTQRQVTLghprhrlalrVSVIDNGPGIPPDLQDTIFYPM--VSGRENGTGLGLA 80
|
90
....*....|....*....
gi 1447699372 617 ISSRLAQAMGGELSATSTP 635
Cdd:cd16918 81 IAQNIVSQHGGVIECDSQP 99
|
|
| PRK09835 |
PRK09835 |
Cu(+)/Ag(+) sensor histidine kinase; |
407-646 |
4.20e-13 |
|
Cu(+)/Ag(+) sensor histidine kinase;
Pssm-ID: 182101 [Multi-domain] Cd Length: 482 Bit Score: 72.50 E-value: 4.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 407 ELQELVIEHRQARAEAEKASQAKSAFLAAMSHEIRTPLYGILGTAQL-LADNPALNAQRDDLRAITDSGESLLTILNDIL 485
Cdd:PRK09835 240 ELEQLVLSFNHMIERIEDVFTRQSNFSADIAHEIRTPITNLITQTEIaLSQSRSQKELEDVLYSNLEELTRMAKMVSDML 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 486 DYSaiEAGGKNVSVSDEPFEPRPLLESTLQLMSGRVKGRPIRLATaiaDDVPTALMGDPRRIRQVITNLLSNALRFTDEG 565
Cdd:PRK09835 320 FLA--QADNNQLIPEKKMLDLADEVGKVFDFFEAWAEERGVELRF---VGDPCQVAGDPLMLRRAISNLLSNALRYTPAG 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 566 Q-IVLRSRTDGEQWLVEVEDSGCGIDPAKLAEIFQPFIQVSGKRG----GTGLGLTISSRLAQAMGGELSATSTPeVGSC 640
Cdd:PRK09835 395 EaITVRCQEVDHQVQLVVENPGTPIAPEHLPRLFDRFYRVDPSRQrkgeGSGIGLAIVKSIVVAHKGTVAVTSDA-RGTR 473
|
....*.
gi 1447699372 641 FCLRLP 646
Cdd:PRK09835 474 FVISLP 479
|
|
| HATPase_BasS-like |
cd16940 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
541-629 |
6.03e-13 |
|
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli BasS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) similar to Escherichia coli BasS HK of the BasS-BasR two-component regulatory system (TCS). Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some contain a HAMP sensory domain, while some an N-terminal two-component sensor kinase domain.
Pssm-ID: 340417 [Multi-domain] Cd Length: 113 Bit Score: 65.89 E-value: 6.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 541 MGDPRRIRQVITNLLSNALRFTDEGQIVLRSRTDGEQWLVEVEDSGCGIDPAKLAEIFQPFIQVSGKR-GGTGLGLTISS 619
Cdd:cd16940 8 QGDALLLFLLLRNLVDNAVRYSPQGSRVEIKLSADDGAVIRVEDNGPGIDEEELEALFERFYRSDGQNyGGSGLGLSIVK 87
|
90
....*....|
gi 1447699372 620 RLAQAMGGEL 629
Cdd:cd16940 88 RIVELHGGQI 97
|
|
| HATPase_NtrY-like |
cd16944 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
543-646 |
7.32e-13 |
|
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: 65.64 E-value: 7.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 543 DPRRIRQVITNLLSNAL-----RFTDEGQIVLRSRTDGEQWLV-EVEDSGCGIDPAKLAEIFQPFIQVSGKrgGTGLGLT 616
Cdd:cd16944 1 DTTQISQVLTNILKNAAeaiegRPSDVGEVRIRVEADQDGRIVlIVCDNGKGFPREMRHRATEPYVTTRPK--GTGLGLA 78
|
90 100 110
....*....|....*....|....*....|
gi 1447699372 617 ISSRLAQAMGGELSATSTPEVGSCFCLRLP 646
Cdd:cd16944 79 IVKKIMEEHGGRISLSNREAGGACIRIILP 108
|
|
| HATPase_BvrS-ChvG-like |
cd16953 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
549-646 |
8.80e-13 |
|
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: 65.29 E-value: 8.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 549 QVITNLLSNALRFT--DEGQIVLRSRTDGEQWLVEVEDSGCGIDPAKLAEIFQPFI--QVSGKRGGT--GLGLTISSRLA 622
Cdd:cd16953 3 QVLRNLIGNAISFSppDTGRITVSAMPTGKMVTISVEDEGPGIPQEKLESIFDRFYteRPANEAFGQhsGLGLSISRQII 82
|
90 100
....*....|....*....|....*...
gi 1447699372 623 QAMGGELSATSTPE----VGSCFCLRLP 646
Cdd:cd16953 83 EAHGGISVAENHNQpgqvIGARFTVQLP 110
|
|
| HATPase_BceS-YxdK-YvcQ-like |
cd16948 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
550-646 |
5.51e-12 |
|
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: 63.07 E-value: 5.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 550 VITNLLSNALRFTDE-GQIVLRSRTDGEQWLVEVEDSGCGIDPAKLAEIFQPFIqvSGKRG-----GTGLGLTISSRLAQ 623
Cdd:cd16948 9 IIGQIVSNALKYSKQgGKIEIYSETNEQGVVLSIKDFGIGIPEEDLPRVFDKGF--TGENGrnfqeSTGMGLYLVKKLCD 86
|
90 100
....*....|....*....|...
gi 1447699372 624 AMGGELSATSTPEVGSCFCLRLP 646
Cdd:cd16948 87 KLGHKIDVESEVGEGTTFTITFP 109
|
|
| Response_reg |
pfam00072 |
Response regulator receiver domain; This domain receives the signal from the sensor partner in ... |
670-775 |
8.29e-12 |
|
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: 62.55 E-value: 8.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 670 LLIEDNPLTQRITVEMLNTSGAQVVAIGNAAQALETLQNsEPFAAALVDFDLPDVNGITLARQLARQYPSLVLIGFSAHV 749
Cdd:pfam00072 2 LIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKE-ERPDLILLDINMPGMDGLELLKRIRRRDPTTPVIILTAHG 80
|
90 100
....*....|....*....|....*.
gi 1447699372 750 IDETLRQRTSSLFRGIIPKPVPREVL 775
Cdd:pfam00072 81 DEDDAVEALEAGADDFLSKPFDPDEL 106
|
|
| HATPase_DpiB-CitA-like |
cd16915 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
550-646 |
3.03e-11 |
|
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli K-12 DpiB, DcuS, and Bacillus subtilis CitS, DctS, and YufL; This family includes histidine kinase-like ATPase domains of Escherichia coli K-12 DpiB and DcuS, and Bacillus subtilis CitS, DctS and MalK histidine kinases (HKs) all of which are two component transduction systems (TCSs). E. coli K-12 DpiB (also known as CitA) is the histidine kinase (HK) of DpiA-DpiB, a two-component signal transduction system (TCS) required for the expression of citrate-specific fermentation genes and genes involved in plasmid inheritance. E. coli K-12 DcuS (also known as YjdH) is the HK of DcuS-DcuR, a TCS that in the presence of the extracellular C4-dicarboxlates, activates the expression of the genes of anaerobic fumarate respiration and of aerobic C4-dicarboxylate uptake. CitS is the HK of Bacillus subtilis CitS-CitT, a TCS which regulates expression of CitM, the Mg-citrate transporter. Bacillus subtilis DctS forms a tripartite sensor unit (DctS/DctA/DctB) for sensing C4 dicarboxylates. Bacillus subtilis MalK (also known as YfuL) is the HK of MalK-MalR (YufL-YufM) a TCS which regulates the expression of the malate transporters MaeN (YufR) and YflS, and is essential for utilization of malate in minimal medium. Proteins having this DpiB-CitA-like HATPase domain generally have sensor domains such as Cache and PAS, and a histidine kinase A (HisKA)-like SpoOB-type, alpha-helical domain.
Pssm-ID: 340392 [Multi-domain] Cd Length: 104 Bit Score: 60.76 E-value: 3.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 550 VITNLLSNAL----RFTDEGQIVLRSRTDGEQWLV-EVEDSGCGIDPAKLAEIFQPfiQVSGK-RGGTGLGLTISSRLAQ 623
Cdd:cd16915 4 IVGNLIDNALdalaATGAPNKQVEVFLRDEGDDLViEVRDTGPGIAPELRDKVFER--GVSTKgQGERGIGLALVRQSVE 81
|
90 100
....*....|....*....|...
gi 1447699372 624 AMGGELSATSTPEVGSCFCLRLP 646
Cdd:cd16915 82 RLGGSITVESEPGGGTTFSIRIP 104
|
|
| HATPase_CreC-like |
cd16945 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
543-636 |
3.38e-11 |
|
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli CreC; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Escherichia coli CreC of the CreC-CreB two-component regulatory system (TCS) involved in catabolic regulation. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and accessory sensory domain(s) such as HAMP, CACHE or PAS.
Pssm-ID: 340421 [Multi-domain] Cd Length: 106 Bit Score: 60.94 E-value: 3.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 543 DPRRIRQVITNLLSNALRFTDEGQIV-LRSRTDGEQWLVEVEDSGCGIDPAKLAEIFQPFIQV----SGKRgGTGLGLTI 617
Cdd:cd16945 1 DPFLLRQAINNLLDNAIDFSPEGGLIaLQLEADTEGIELLVFDEGSGIPDYALNRVFERFYSLprphSGQK-STGLGLAF 79
|
90
....*....|....*....
gi 1447699372 618 SSRLAQAMGGELSATSTPE 636
Cdd:cd16945 80 VQEVAQLHGGRITLRNRPD 98
|
|
| PRK10337 |
PRK10337 |
sensor protein QseC; Provisional |
323-638 |
5.40e-11 |
|
sensor protein QseC; Provisional
Pssm-ID: 182388 [Multi-domain] Cd Length: 449 Bit Score: 65.83 E-value: 5.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 323 MVSLCALILILWRVVYRSVtRPLAEQTQALqRLLDGDIDSPFPETAGVRELdtigrlmdafRSSVHALNrhreqlaaQVK 402
Cdd:PRK10337 168 LVALPIMLIILMVLLGREL-APLKKLALAL-RMRDPDSETPLNATGVPSEV----------RPLVEALN--------QLF 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 403 ARTAELqeLVIEHRqaraeaekasqaksaFLAAMSHEIRTPLYGI---LGTAQLLADNPALnaqRDDLRAITDSGESLLT 479
Cdd:PRK10337 228 ARTHAM--MVRERR---------------FTSDAAHELRSPLAALkvqTEVAQLSDDDPQA---RKKALLQLHAGIDRAT 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 480 ILND-ILDYSAIEAGGKNVSVSDEPFEPrpLLESTL--QLMSGRVKGRPIRLAtaiADDVPTALMGDPRRIRQVITNLLS 556
Cdd:PRK10337 288 RLVDqLLTLSRLDSLDNLQDVAEIPLED--LLQSAVmdIYHTAQQAGIDVRLT---LNAHPVIRTGQPLLLSLLVRNLLD 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 557 NALRFTDEGQIV---LRSRTdgeqwlVEVEDSGCGIDPAKLAEIFQPFIQVSGK-RGGTGLGLTISSRLAQAMGGELSAT 632
Cdd:PRK10337 363 NAIRYSPQGSVVdvtLNARN------FTVRDNGPGVTPEALARIGERFYRPPGQeATGSGLGLSIVRRIAKLHGMNVSFG 436
|
....*.
gi 1447699372 633 STPEVG 638
Cdd:PRK10337 437 NAPEGG 442
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
667-782 |
8.68e-11 |
|
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: 61.85 E-value: 8.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 667 LRLLLIEDNPLTQRITVEMLNTSGAQVVAIGNAAQALETLQnSEPFAAALVDFDLPDVNGITLARQLaRQYPSLV---LI 743
Cdd:COG3706 2 ARILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQ-EHRPDLILLDLEMPDMDGLELCRRL-RADPRTAdipII 79
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1447699372 744 GFSAHVIDETLRQRTSSLFRGIIPKPVPREVLGQ---LLAHY 782
Cdd:COG3706 80 FLTALDDEEDRARALEAGADDYLTKPFDPEELLArvdLVARY 121
|
|
| HATPase_EcPhoR-like |
cd16952 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
547-648 |
1.09e-10 |
|
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli PhoR; This family includes histidine kinase-like ATPase (HATPase) domain of two-component sensor histidine kinases similar to Escherichia coli or Vibrio cholera PhoR, the histidine kinase (HK) of PhoB-PhoR a two-component signal transduction system (TCS) involved in phosphate regulation. PhoR monitors extracellular inorganic phosphate (Pi) availability and PhoB, the response regulator, regulates transcription of genes of the phosphate regulon. PhoR is a bifunctional histidine autokinase/phospho-PhoB phosphatase; in phosphate deficiency, it autophosphorylates and Pi is transferred to PhoB, and when environmental Pi is abundant, it removes the phosphoryl group from phosphorylated PhoB. Other roles of PhoB-PhoR TCS have been described, including motility, biofilm formation, intestinal colonization, and virulence in V. cholera. E.coli PhoR and Bacillus subtilis PhoR (whose HATPase domain belongs to a different family) sense very different signals in each bacterium. In E. coli the PhoR signal comes from phosphate transport mediated by the PstSCAB2 phosphate transporter and the PhoU chaperone-like protein while in B. subtilis, the PhoR activation signal comes from wall teichoic acid (WTA) metabolism.
Pssm-ID: 340428 [Multi-domain] Cd Length: 108 Bit Score: 59.52 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 547 IRQVITNLLSNALRFT-DEGQIVLRSRTDGEQWLVEVEDSGCGIDPAKLAEIFQPFIQVSGKR----GGTGLGLTISSRL 621
Cdd:cd16952 1 LRSAFSNLVSNAVKYTpPSDTITVRWSQEESGARLSVEDTGPGIPPEHIPRLTERFYRVDIERcrntGGTGLGLAIVKHV 80
|
90 100
....*....|....*....|....*..
gi 1447699372 622 AQAMGGELSATSTPEVGSCFCLRLPLR 648
Cdd:cd16952 81 MSRHDARLLIASELGKGSRFTCLFPSS 107
|
|
| HPT |
cd00088 |
Histidine Phosphotransfer domain, involved in signalling through a two part component systems ... |
810-892 |
3.67e-10 |
|
Histidine Phosphotransfer domain, involved in signalling through a two part component systems in which an autophosphorylating histidine protein kinase serves as a phosphoryl donor to a response regulator protein; the response regulator protein is modulated by phosphorylation and dephosphorylation of a conserved aspartic acid residue; two-component proteins are abundant in most eubacteria; In E. coli there are 62 two-component proteins involved in a variety of processes such as chemotaxis, osmoregulation, metabolism and transport 1; also present in both Gram positive and Gram negative pathogenic bacteria where they regulate basic housekeeping functions and control expression of toxins and other proteins important for pathogenesis; in archaea and eukaryotes, two-component pathways constitute a very small number of all signaling systems; in fungi they mediate environmental stress responses and, in pathogenic yeast, hyphal development. In Dictyostelium and in plants, they are involved in important processes such as osmoregulation, cell growth, and differentiation; to date two-component proteins have not been identified in animals; in most prokaryotic systems, the output response is effected directly by the RR, which functions as a transcription factor while in eukaryotic systems, two-component proteins are found at the beginning of signaling pathways where they interface with more conventional eukaryotic signaling strategies such as MAP kinase and cyclic nucleotide cascades
Pssm-ID: 238041 [Multi-domain] Cd Length: 94 Bit Score: 57.39 E-value: 3.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 810 IHEWLALFTQHALPLLDEIDIA----RATQDSEKIKRAAHQLKSSCSSLGMRSASQLCAQLEQQPLSA-------PLPHE 878
Cdd:cd00088 1 MEELLELFLEEAEELLEELERAllelEDAEDLNEIFRAAHTLKGSAASLGLQRLAQLAHQLEDLLDALrdglevtPELID 80
|
90
....*....|....
gi 1447699372 879 EITRSVAALEAWLN 892
Cdd:cd00088 81 LLLDALDALKAELE 94
|
|
| HPtr |
COG2198 |
HPt (histidine-containing phosphotransfer) domain [Signal transduction mechanisms]; |
42-869 |
4.03e-10 |
|
HPt (histidine-containing phosphotransfer) domain [Signal transduction mechanisms];
Pssm-ID: 441800 [Multi-domain] Cd Length: 871 Bit Score: 63.91 E-value: 4.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 42 EASAWELFAAQNLTSADNEKMWQAQGRMLTAQSLKINALLQALREQGFDTTAIEQQEQEISRSLRQQGELVGRRLQLRQQ 121
Cdd:COG2198 3 LLLLALLLLLLLLLLLLLLLLALLALLLLLLLAALALLLLLLLLLALLALLLLLVALALLLALLLLLLGVLLLLLDLLEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 122 QQRLSQQIVAAADEIARLAQGQANNAATSAGATQAGIYDLIEQDQRQAAESALDRLIDIDLEYVNQMNELRLSALRVQQM 201
Cdd:COG2198 83 LLLLLLLLLLLLLLLLLLLLALLLLLLLLLALLLLLLLLLLLLLLLLLLLALLLLLLLLLALLLLLLLLLVLAALLLLLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 202 VMNLGLEQIQKNAPTLEKQLNNAVKILQRRQIRIEDPGVRAQVATTLTTVSQYSDLLALFQQDSEISNHLQTLAQNNIAQ 281
Cdd:COG2198 163 LALLLALLLLVLLVLLLLLLLLLLLLLLLLLLLLLLLLALTLAALLELLAAELALEALLAELAAEAAAALAAELALAELA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 282 FAQFSSEVSQLVDTIELRNQHGLAHLEKASARGQYSLLLLGMVSLCALILILWRVVYRSVTRPLAEQTQALQRLLDGDID 361
Cdd:COG2198 243 ALLLLLLLLLLLLILLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLELLLLLLLALLLLLLLLLLLLLL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 362 SPFPETAGVRELDTIGRLMDAFRSSVHALNRHREQLAAQVKARTAELQELVIEHRQARAEAEKASQAKSAFLAAMSHEIR 441
Cdd:COG2198 323 LLLLLLLLLLLLLLLLLLLLLLLLLLLALLLLALLLALLLAAAAALAAALEALLTELALILLLLLLLLLLLILLGLLLLL 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 442 TPLYGILGTAQLLADNPALNAQRDDLRAITDSGESLLTILNDILDYSAIEAGGKNVSVSDEPFEPRPLLESTLQLMSGRV 521
Cdd:COG2198 403 LLSLLLSLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLGLLLLLLLLLGLLLLLLLGLLLLALLLLLLLLLLLLLLLLLL 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 522 KGRPIRLATAIADDVPTALMGDPRRIRQVITNLLSNALRFTDEGQIVLRSRTDGEQWLVEVEDSGCGIDPAKLAEIFQPF 601
Cdd:COG2198 483 LLLLLLLLLLLLLLLLLLLLLLLLVAAALAALALLLLLALLLLLLLDLLILGLLLILLLLLLGLLALGLAALLLLLALLL 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 602 IQVSGKRGGTGLGLTISSRLAQAMGGELSATSTPEVGSCFCLRLPLRVATAPVPKTVNQAVRLDGLRLLLIEDNPLTQRI 681
Cdd:COG2198 563 GLGLLLGLLLGGLLLLLLLLLLLLLLLLLLLLLLLLLLALLLALLAAAAALLLLLLLLALLLLLLLLLLLLLLLLLLLLL 642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 682 TVEMLNTSGAQVVAIGNAAQALETLQNSEPFAAALVDFDLPDVNGITLARQLARQYPSLVLIGFSAHVIDETLRQRTSSL 761
Cdd:COG2198 643 LLLLLLLLLLAVLLAAAAAAAALAALDLLLDLDDMMMMLDDMMAEAARARALAARAAAIAAAAAAAAAAAAAAAAAAAAL 722
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 762 FRGIIPKPVPREVLGQLLAHYLQLQANNDLPLDVSQ------LNEDAQLMG-TEKIHEWLALFTQHALPLLDEIDIARAT 834
Cdd:COG2198 723 LAALLLLLLLLLLLLLLLLLLLLAAAAAAAASPAAPalpvldLEALRRLGGdPELLRELLELFLEELPELLAELRQALAA 802
|
810 820 830
....*....|....*....|....*....|....*
gi 1447699372 835 QDSEKIKRAAHQLKSSCSSLGMRSASQLCAQLEQQ 869
Cdd:COG2198 803 GDLEALARLAHKLKGSAGNLGAPRLAELAAELEQA 837
|
|
| Hpt |
pfam01627 |
Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module ... |
812-890 |
5.75e-10 |
|
Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module with an active histidine residue that mediates phosphotransfer reactions in the two-component signaling systems. A multistep phosphorelay involving the HPt domain has been suggested for these signaling pathways. The crystal structure of the HPt domain of the anaerobic sensor kinase ArcB has been determined. The domain consists of six alpha helices containing a four-helix bundle-folding. The pattern of sequence similarity of the HPt domains of ArcB and components in other signaling systems can be interpreted in light of the three-dimensional structure and supports the conclusion that the HPt domains have a common structural motif both in prokaryotes and eukaryotes. In S. cerevisiae ypd1p this domain has been shown to contain a binding surface for Ssk1p (response regulator receiver domain containing protein pfam00072).
Pssm-ID: 426352 [Multi-domain] Cd Length: 84 Bit Score: 56.59 E-value: 5.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 812 EWLALFTQHALPLLDEIDIARATQDSEKIKRAAHQLKSSCSSLGMRSASQLCAQLEQQPLSAPLPH-----EEITRSVAA 886
Cdd:pfam01627 1 ELLELFLEEAPELLEQLEQALDAEDLEALFRAAHTLKGSAGSLGLPALAELAHELEDLLREGELPLdpellEALRDLLEA 80
|
....
gi 1447699372 887 LEAW 890
Cdd:pfam01627 81 LRAA 84
|
|
| HATPase_CckA-like |
cd16919 |
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ... |
549-646 |
7.88e-10 |
|
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: 57.39 E-value: 7.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 549 QVITNLLSNAlR--FTDEGQIVLRSRTD---------------GEQWLVEVEDSGCGIDPAKLAEIFQPFIQVSGKRGGT 611
Cdd:cd16919 3 LAILNLAVNA-RdaMPEGGRLTIETSNQrvdadyalnyrdlipGNYVCLEVSDTGSGMPAEVLRRAFEPFFTTKEVGKGT 81
|
90 100 110
....*....|....*....|....*....|....*
gi 1447699372 612 GLGLTISSRLAQAMGGELSATSTPEVGSCFCLRLP 646
Cdd:cd16919 82 GLGLSMVYGFVKQSGGHLRIYSEPGVGTTVRIYLP 116
|
|
| cpxA |
PRK09470 |
envelope stress sensor histidine kinase CpxA; |
433-647 |
9.88e-10 |
|
envelope stress sensor histidine kinase CpxA;
Pssm-ID: 236532 [Multi-domain] Cd Length: 461 Bit Score: 61.87 E-value: 9.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 433 LAAMSHEIRTPLYGI-LGTAQL---LADNPALN-----AQRDDlRAITDsgesLL-------------------TILNDI 484
Cdd:PRK09470 247 LSDISHELRTPLTRLqLATALLrrrQGESKELErieteAQRLD-SMIND----LLvlsrnqqknhleretfkanSLWSEV 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 485 LDYSAIEAG--GKNVSVSDEPfEPRPLLestlqlmsgrvkGRPIRLATAIaddvptalmgdprrirqviTNLLSNALRFT 562
Cdd:PRK09470 322 LEDAKFEAEqmGKSLTVSAPP-GPWPIN------------GNPNALASAL-------------------ENIVRNALRYS 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 563 DEgQIVLRSRTDGEQWLVEVEDSGCGIDPAKLAEIFQPFIQVSGKR----GGTGLGLTISSRLAQAMGGELSATSTPEVG 638
Cdd:PRK09470 370 HT-KIEVAFSVDKDGLTITVDDDGPGVPEEEREQIFRPFYRVDEARdresGGTGLGLAIVENAIQQHRGWVKAEDSPLGG 448
|
....*....
gi 1447699372 639 SCFCLRLPL 647
Cdd:PRK09470 449 LRLTIWLPL 457
|
|
| HATPase_PhoQ-like |
cd16954 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
508-645 |
1.70e-09 |
|
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: 56.87 E-value: 1.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 508 PLLESTLQLMsGRVKGRP-IRLATAIADDVptALMGDPRRIRQVITNLLSNALRFTDEgQIVLRSRTDGEQWLVEVEDSG 586
Cdd:cd16954 1 PLLDSLCSAL-NKVYQRKgVSISLDISPEL--RFPGERNDLMELLGNLLDNACKWCLE-FVEVTARQTDGGLHLIVDDDG 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1447699372 587 CGIDPAKLAEIFQPFIQVSGKRGGTGLGLTISSRLAQAMGGELSATSTPEVGSCFCLRL 645
Cdd:cd16954 77 PGVPESQRSKIFQRGQRLDEQRPGQGLGLAIAKEIVEQYGGELSLSDSPLGGARFEVVF 135
|
|
| REC_CpdR_CckA-like |
cd18160 |
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ... |
668-769 |
1.84e-09 |
|
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: 55.59 E-value: 1.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 668 RLLLIEDNPLTQRITVEMLNTSGAQVVAIGNAAQALETLQNSEPFAAALVDFDLPDVNGITLARQLARQYPSLVLIGFSA 747
Cdd:cd18160 1 TILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQQGKDIDIVVTDIVMPEMDGIELAREARKIDPDVKILFISG 80
|
90 100
....*....|....*....|..
gi 1447699372 748 HVIDETLRQRTSSLFRGIIPKP 769
Cdd:cd18160 81 GAAAAPELLSDAVGDNATLKKP 102
|
|
| marine_sort_HK |
TIGR03785 |
proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is ... |
373-646 |
2.94e-09 |
|
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: 60.91 E-value: 2.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 373 LDTIGRLMDAFRSS-----VHALNRHREQLAAQVKARTAELQelviehrqaraeaekasqaksAFLAAMSHEIRTPLYGI 447
Cdd:TIGR03785 445 IDSQGRISGAIPASrsrdeIGDLSRSFAQMVARLRQYTHYLE---------------------NMSSRLSHELRTPVAVV 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 448 LGTAQLLADNPALNAQRDDLRAITDSGESLLTILNDILDYSAIEAggknvSVSDEPFEPRPLLESTLQLMSGRVKGRPIR 527
Cdd:TIGR03785 504 RSSLENLELQALEQEKQKYLERAREGTERLSMILNNMSEATRLEQ-----AIQSAEVEDFDLSEVLSGCMQGYQMTYPPQ 578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 528 LATAIADDVPTALMGDPRRIRQVITNLLSNALRFT-DEGQIVLRSRTDGEQWLVEVEDSGCGIdPAKLAE-IFQPFIQVS 605
Cdd:TIGR03785 579 RFELNIPETPLVMRGSPELIAQMLDKLVDNAREFSpEDGLIEVGLSQNKSHALLTVSNEGPPL-PEDMGEqLFDSMVSVR 657
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1447699372 606 GKRGGT----GLGLTISSRLAQAMGGELSATSTPE-VGSCFCLRLP 646
Cdd:TIGR03785 658 DQGAQDqphlGLGLYIVRLIADFHQGRIQAENRQQnDGVVFRISLP 703
|
|
| OmpR |
COG0745 |
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ... |
667-781 |
3.26e-09 |
|
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: 57.66 E-value: 3.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 667 LRLLLIEDNPLTQRITVEMLNTSGAQVVAIGNAAQALETLQnSEPFAAALVDFDLPDVNGITLARQLARQYPSLVLIGFS 746
Cdd:COG0745 2 PRILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLE-EERPDLILLDLMLPGMDGLEVCRRLRARPSDIPIIMLT 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 1447699372 747 AHViDETLRQRtsSLFRGI---IPKPV-PREVLGQLLAH 781
Cdd:COG0745 81 ARD-DEEDRVR--GLEAGAddyLTKPFdPEELLARIRAL 116
|
|
| REC_NarL-like |
cd17535 |
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ... |
670-775 |
3.50e-09 |
|
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: 55.21 E-value: 3.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 670 LLIEDNPLTQRITVEMLNT-SGAQVVAI-GNAAQALETLQNSEPfAAALVDFDLPDVNGITLARQLARQYPSLVLIGFSA 747
Cdd:cd17535 2 LIVDDHPLVREGLRRLLESePDIEVVGEaADGEEALALLRELRP-DVVLMDLSMPGMDGIEALRRLRRRYPDLKVIVLTA 80
|
90 100
....*....|....*....|....*...
gi 1447699372 748 HVIDETLRQRTSSLFRGIIPKPVPREVL 775
Cdd:cd17535 81 HDDPEYVLRALKAGAAGYLLKDSSPEEL 108
|
|
| HATPase_VanS-like |
cd16923 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
548-646 |
2.89e-08 |
|
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Enterococcus faecium VanS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Enterococcus faecium VanS HK of the VanS-VanR two-component regulatory system (TCS) which activates the transcription of vanH, vanA and vanX vancomycin resistance genes. It also contains Ecoli YedV and PcoS, probable members of YedW-YedV TCS and PcoS-PcoR TCS, repectively. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); most also have a HAMP sensor domain.
Pssm-ID: 340400 [Multi-domain] Cd Length: 102 Bit Score: 52.39 E-value: 2.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 548 RQVITNLLSNALRFTDEGQIV-LRSRTDGEQWLVEVEDSGCGIDPAKLAEIFQPFIQVSGKR--GGTGLGLTISSRLAQA 624
Cdd:cd16923 2 QRVFSNLLSNAIKYSPENTRIyITSFLTDDVVNIMFKNPSSHPLDFKLEKLFERFYRGDNSRntEGAGLGLSIAKAIIEL 81
|
90 100
....*....|....*....|..
gi 1447699372 625 MGGELSATSTPEvGSCFCLRLP 646
Cdd:cd16923 82 HGGSASAEYDDN-HDLFKVRLP 102
|
|
| YesN |
COG4753 |
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ... |
668-769 |
4.71e-08 |
|
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: 51.70 E-value: 4.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 668 RLLLIEDNPLTQRITVEMLN-TSGAQVVAI-GNAAQALETLQnSEPFAAALVDFDLPDVNGITLARQLARQYPSLVLIGF 745
Cdd:COG4753 1 KVLIVDDEPLIREGLKRILEwEAGFEVVGEaENGEEALELLE-EHKPDLVITDINMPGMDGLELLEAIRELDPDTKIIIL 79
|
90 100
....*....|....*....|....*
gi 1447699372 746 SAHvIDETLRQRTSSL-FRGIIPKP 769
Cdd:COG4753 80 SGY-SDFEYAQEAIKLgADDYLLKP 103
|
|
| COG4567 |
COG4567 |
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ... |
668-746 |
4.90e-08 |
|
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains [Signal transduction mechanisms, Transcription];
Pssm-ID: 443624 [Multi-domain] Cd Length: 177 Bit Score: 53.77 E-value: 4.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 668 RLLLIEDNPLTQRITVEMLNTSGAQVVAIGNAAQALETLQnSEPFAAALVDFDLPDVNGITLARQLARQYPS---LVLIG 744
Cdd:COG4567 6 SLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLE-QAPPDYAVLDLRLGDGSGLDLIEALRERDPDariVVLTG 84
|
..
gi 1447699372 745 FS 746
Cdd:COG4567 85 YA 86
|
|
| COG3920 |
COG3920 |
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ... |
173-652 |
1.17e-07 |
|
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction mechanisms];
Pssm-ID: 443125 [Multi-domain] Cd Length: 495 Bit Score: 55.30 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 173 ALDRLIDIDLEYVNQMNELRLSALRVQQMVMNLGLEQIQKNAPTLEKQLNNAVKILQRRQIRIEDPGVRAQVATTLTTVS 252
Cdd:COG3920 66 ALAVALAAAVGAAAALLALLVLLLLLLLAAAALALALLLAALAGLLLLAALLLLRLVALLAALALLALLLLLLLLLAILA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 253 QYSDLLALFQQDSEISNHLQTLAQNNIAQFAQFSSEVSQLVDTIELRNQHGLAHLEKASARGQYSLLLLGMVSLCALILI 332
Cdd:COG3920 146 LAELAVALAELAAALLLLAEELAALRLAAAALLLLLAALLDLGLALAALAAAALLALLLALELLLALLLLLLLLLALLLV 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 333 LWRVVYRSVTRPLAEQTqaLQRLLDGDIDSPFPETAGVRELDTIGRLMDAFRSSVHALNRHREQLAAQVKARTAELQElv 412
Cdd:COG3920 226 LLAALLRLRAAVLEELE--RRRRARGLGRLLLLLLLLLLLLRALLLLAAGIRLVITERKRAEEELEASLEEKELLLRE-- 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 413 IEHR--------------QAR-AEAEKASQAKSAF---LAAMS--HEIrtpLYgilgtaqlladnpalnaQRDDLRAItd 472
Cdd:COG3920 302 LHHRvknnlqvvssllrlQARrADDPEAREALEESqnrIQALAlvHEL---LY-----------------QSEDWEGV-- 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 473 sgeSLLTILNDILDYSAIEAGGKNVSVsdepfeprpllestlqlmsgRVKGRPIRLATAIAddVPTALmgdprrirqVIT 552
Cdd:COG3920 360 ---DLRDYLRELLEPLRDSYGGRGIRI--------------------ELDGPDVELPADAA--VPLGL---------ILN 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 553 NLLSNALRF----TDEGQIVLRSRTDGEQWLVEVEDSGCGIDPAklaeiFQPfiqvsgkRGGTGLGLTISSRLAQAMGGE 628
Cdd:COG3920 406 ELVTNALKHaflsGEGGRIRVSWRREDGRLRLTVSDNGVGLPED-----VDP-------PARKGLGLRLIRALVRQLGGT 473
|
490 500
....*....|....*....|....
gi 1447699372 629 LSATSTPevGSCFCLRLPLRVATA 652
Cdd:COG3920 474 LELDRPE--GTRVRITFPLAELAA 495
|
|
| HATPase_CheA-like |
cd16916 |
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ... |
564-646 |
1.34e-07 |
|
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some hybrid sensor histidine kinases; This family includes the cytoplasmic histidine kinase (HK) CheA, a transmembrane receptor which, together with cytoplasmic adaptor protein (CheW), forms the lattice at the core of the chemosensory array that controls the cellular chemotaxis of motile bacteria and archaea. CheA forms a two-component signal transduction system (TCS) with the response regulator CheY. Proteins having this CheA-like HATPase domain generally also have a histidine-phosphotransfer domain, a histidine kinase homodimeric domain, and a regulatory domain; some are hybrid sensor histidine kinases as they contain a REC signal receiver domain.
Pssm-ID: 340393 [Multi-domain] Cd Length: 178 Bit Score: 52.58 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 564 EGQIVLRSRTDGEQWLVEVEDSGCGIDPAKLAE------------------------IFQPFI-------QVSGKrggtG 612
Cdd:cd16916 69 EGTITLRAEHQGNQVVIEVSDDGRGIDREKIREkaierglitadeaatlsddevlnlIFAPGFstaeqvtDVSGR----G 144
|
90 100 110
....*....|....*....|....*....|....
gi 1447699372 613 LGLTISSRLAQAMGGELSATSTPEVGSCFCLRLP 646
Cdd:cd16916 145 VGMDVVKRSIESLGGTIEVESEPGQGTTFTIRLP 178
|
|
| REC_ETR-like |
cd19933 |
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ... |
667-779 |
1.38e-07 |
|
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and similar proteins; Plant ethylene receptors contain N-terminal transmembrane domains that contain an ethylene binding site and also serve in localization of the receptor to the endoplasmic reticulum or the Golgi apparatus and a C-terminal histidine kinase (HK)-like domain. There are five ethylene receptors (ETR1, ERS1, ETR2, ERS2, and EIN4) in Arabidopsis thaliana. ETR1, ETR2, and EIN4 also contain REC domains C-terminal to the HK domain. ETR1 and ERS1 belong to subfamily 1, and have functional HK domains while ETR2, ERS2, and EIN4 belong to subfamily 2, and lack the necessary residues for HK activity and may function as serine/threonine kinases. The plant hormone ethylene plays an important role in plant growth and development. It regulates seed germination, seedling growth, leaf and petal abscission, fruit ripening, organ senescence, and pathogen responses. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381160 [Multi-domain] Cd Length: 117 Bit Score: 50.86 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 667 LRLLLIEDNPLTQRITVEMLNTSGAQVVAIGNAAQALETLQNSE-PFAAALVDFDLPDVNGITLARQLARQYPS---LVL 742
Cdd:cd19933 1 LKVLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLLASAEhSFQLVLLDLCMPEMDGFEVALRIRKLFGRrerPLI 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 1447699372 743 IGFSAHVIDETlRQRTSSL-FRGIIPKPVPREVLGQLL 779
Cdd:cd19933 81 VALTANTDDST-REKCLSLgMNGVITKPVSLHALGDEL 117
|
|
| REC_OmpR_PmrA-like |
cd17624 |
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ... |
669-743 |
1.38e-07 |
|
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: 50.56 E-value: 1.38e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1447699372 669 LLLIEDNPLTQRITVEMLNTSGAQVVAIGNAAQALETLQnSEPFAAALVDFDLPDVNGITLARQLARQYPSL-VLI 743
Cdd:cd17624 1 ILLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALA-SGPYDLVILDLGLPDGDGLDLLRRWRRQGQSLpVLI 75
|
|
| LytT |
COG3279 |
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ... |
667-792 |
1.77e-07 |
|
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction mechanisms];
Pssm-ID: 442510 [Multi-domain] Cd Length: 235 Bit Score: 52.90 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 667 LRLLLIEDNPLTQRITVEML-NTSGAQVVAI-GNAAQALETLQNSEPfAAALVDFDLPDVNGITLARQLARQYPSLVLI- 743
Cdd:COG3279 2 MKILIVDDEPLARERLERLLeKYPDLEVVGEaSNGEEALELLEEHKP-DLVFLDIQMPGLDGFELARQLRELDPPPPIIf 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1447699372 744 ----------GFSAHVIDetlrqrtsslfrgIIPKPVPREVLGQLLAHYLQLQANNDLP 792
Cdd:COG3279 81 ttaydeyaleAFEVNAVD-------------YLLKPIDEERLAKALEKAKERLEAKAAA 126
|
|
| REC_citrate_TCS |
cd19925 |
phosphoacceptor receiver (REC) domain of citrate family two-component system response ... |
667-782 |
1.89e-07 |
|
phosphoacceptor receiver (REC) domain of citrate family two-component system response regulators; This family includes Lactobacillus paracasei MaeR, Escherichia coli DcuR and DpiA, Klebsiella pneumoniae CitB, as well as Bacillus DctR, MalR, and CitT. These are all response regulators of two-component systems (TCSs) from the citrate family, and are involved in the transcriptional regulation of genes associated with L-malate catabolism (MaeRK), citrate-specific fermentation (DpiAB, CitAB), plasmid inheritance (DpiAB), anaerobic fumarate respiratory system (DcuRS), and malate transport/utilization (MalKR). REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381152 [Multi-domain] Cd Length: 118 Bit Score: 50.32 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 667 LRLLLIEDNPLTQRITVEMLNT-SGAQVVAI-GNAAQALETLQnSEPFAAALVDFDLPDVNGITLARQLARQYPSLVLIG 744
Cdd:cd19925 1 INVLIVEDDPMVAEIHRAYVEQvPGFTVIGTaGTGEEALKLLK-ERQPDLILLDIYLPDGNGLDLLRELRAAGHDVDVIV 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1447699372 745 FSA----HVIDETLRQrtsslfrGIIP---KPVPREVLGQLLAHY 782
Cdd:cd19925 80 VTAandvETVREALRL-------GVVDyliKPFTFERLRQRLERY 117
|
|
| AmiR |
COG3707 |
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ... |
665-787 |
2.46e-07 |
|
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding antiterminator (ANTAR) domains [Signal transduction mechanisms, Transcription];
Pssm-ID: 442921 [Multi-domain] Cd Length: 194 Bit Score: 51.88 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 665 DGLRLLLIEDNPLTQRITVEMLNTSGAQVVA-IGNAAQALETLQNSEPfAAALVDFDLPDVNGITLARQLARQYPSLVlI 743
Cdd:COG3707 2 RGLRVLVVDDEPLRRADLREGLREAGYEVVAeAADGEDAVELVRELKP-DLVIVDIDMPDRDGLEAARQISEERPAPV-I 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1447699372 744 GFSAHVIDETLRQRTSSLFRGIIPKPVPREVLGQLL----AHYLQLQA 787
Cdd:COG3707 80 LLTAYSDPELIERALEAGVSAYLVKPLDPEDLLPALelalARFRELRA 127
|
|
| REC_2_GGDEF |
cd17544 |
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ... |
670-748 |
2.48e-07 |
|
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: 50.21 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 670 LLIEDNPLTQRITVEMLNTSGAQVVAIGNAAQALETLQNSEPFAAALVDFDLPDVNGITLARQLARQYPS--LVLIGFSA 747
Cdd:cd17544 4 LVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLEQHPDIKLVITDYNMPEMDGFELVREIRKKYSRdqLAIIGISA 83
|
.
gi 1447699372 748 H 748
Cdd:cd17544 84 S 84
|
|
| HATPase_ETR2_ERS2-EIN4-like |
cd16938 |
Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related ... |
536-645 |
2.49e-07 |
|
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: 50.53 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 536 VPTALMGDPRRIRQVITNLLSNALRFTDE-GQIVLR--------SRTDGEQWLVEVEDSGCGIDPAKLAEI--------F 598
Cdd:cd16938 1 LPDVVVGDERRVFQVLLHMLGNLLKMRNGgGNITFRvfleggseDRSDRDWGPWRPSMSDESVEIRFEVEIndsgspsiE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1447699372 599 QPFIQVSGKRG------GTGLGLTISSRLAQAMGGELSATSTPEVGSCFCLRL 645
Cdd:cd16938 81 SASMRNSLNRRynlselGEHLSFSICKQLVQLMGGNIWIVPGSGLGTTMSLLL 133
|
|
| REC_DivK-like |
cd17548 |
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ... |
668-733 |
3.01e-07 |
|
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: 49.85 E-value: 3.01e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1447699372 668 RLLLIEDNPLTQRITVEMLNTSGAQVVAIGNAAQALETLQNSEPfAAALVDFDLPDVNGITLARQL 733
Cdd:cd17548 1 KILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKP-DLILMDIQLPGMDGLEATRLL 65
|
|
| REC_RegA-like |
cd17563 |
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ... |
668-746 |
4.55e-07 |
|
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; Rhodobacter sphaeroides RegA, also called response regulator PrrA, is the DNA binding regulatory protein of a redox-responsive two-component regulatory system RegB/RegA that is involved in transactivating anaerobic expression of the photosynthetic apparatus. It contains a REC domain and a DNA-binding helix-turn-helix output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381111 [Multi-domain] Cd Length: 112 Bit Score: 48.98 E-value: 4.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 668 RLLLIEDNPLTQRITVEMLNTSGAQVVAIGNAAQALETLQnSEPFAAALVDFDLPDVNGITLARQLARQYPS---LVLIG 744
Cdd:cd17563 2 SLLLVDDDEVFAERLARALERRGFEVETAHSVEEALALAR-EEKPDYAVLDLRLGGDSGLDLIPPLRALQPDariVVLTG 80
|
..
gi 1447699372 745 FS 746
Cdd:cd17563 81 YA 82
|
|
| RsbW |
COG2172 |
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms]; |
546-647 |
5.05e-07 |
|
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
Pssm-ID: 441775 [Multi-domain] Cd Length: 127 Bit Score: 49.53 E-value: 5.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 546 RIRQVITNLLSNALR----FTDEGQIVLRSRTDGEQWLVEVEDSGCGIDPAKLAEIFQPfiqvsgkRGGTGLGLTISSRL 621
Cdd:COG2172 34 DLVLAVSEAVTNAVRhaygGDPDGPVEVELELDPDGLEIEVRDEGPGFDPEDLPDPYST-------LAEGGRGLFLIRRL 106
|
90 100
....*....|....*....|....*.
gi 1447699372 622 AQamggELSATSTPEvGSCFCLRLPL 647
Cdd:COG2172 107 MD----EVEYESDPG-GTTVRLVKRL 127
|
|
| HATPase_SpaK_NisK-like |
cd16975 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
543-640 |
6.39e-07 |
|
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: 48.61 E-value: 6.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 543 DPRRIRQVITNLLSNALRFTDEGQIVLRSRTDGEQWL-VEVEDSGCGIDPAKLAEIFQPFI---QVSGKRGGTGLGLTIS 618
Cdd:cd16975 1 DTLLLSRALINIISNACQYAPEGGTVSISIYDEEEYLyFEIWDNGHGFSEQDLKKALELFYrddTSRRSGGHYGMGLYIA 80
|
90 100
....*....|....*....|..
gi 1447699372 619 SRLAQAMGGELSATSTPEVGSC 640
Cdd:cd16975 81 KNLVEKHGGSLIIENSQKGGAE 102
|
|
| REC_2_DhkD-like |
cd17580 |
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ... |
670-779 |
9.06e-07 |
|
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: 48.22 E-value: 9.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 670 LLIEDNPLTQRITVEMLNTSGAQVVAIGNAAQALETLQNSePFAAALVDFDLPDVNGITLARQLaRQYP---SLVLIGFS 746
Cdd:cd17580 2 LVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRF-RPDVILSDIGMPGMDGYELARRL-RELPwlaNTPAIALT 79
|
90 100 110
....*....|....*....|....*....|...
gi 1447699372 747 AHVIDETLRQRTSSLFRGIIPKPVPREVLGQLL 779
Cdd:cd17580 80 GYGQPEDRERALEAGFDAHLVKPVDPDELIELI 112
|
|
| PRK11086 |
PRK11086 |
sensory histidine kinase DcuS; Provisional |
542-646 |
9.12e-07 |
|
sensory histidine kinase DcuS; Provisional
Pssm-ID: 236839 [Multi-domain] Cd Length: 542 Bit Score: 52.61 E-value: 9.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 542 GDPRRIRQVIT---NLLSNALRF---TDEGQIVLRSRTDGEQWLVEVEDSGCGIDPAKLAEIFQPFIQVSGKRGGTGLGL 615
Cdd:PRK11086 426 GDEDQVHELITilgNLIENALEAvggEEGGEISVSLHYRNGWLHCEVSDDGPGIAPDEIDAIFDKGYSTKGSNRGVGLYL 505
|
90 100 110
....*....|....*....|....*....|.
gi 1447699372 616 TISSrlAQAMGGELSATSTPEVGSCFCLRLP 646
Cdd:PRK11086 506 VKQS--VENLGGSIAVESEPGVGTQFFVQIP 534
|
|
| HATPase_YehU-like |
cd16956 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
554-646 |
1.84e-06 |
|
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli YehU; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) including Escherichia coli YehU, a HK of the two-component system (TCS) YehU-YehT which is involved in a nutrient sensing regulatory network. Proteins having this HATPase domain also contain a histidine kinase domain (His-kinase); some have a GAF sensor domain while some have a cupin domain.
Pssm-ID: 340432 [Multi-domain] Cd Length: 101 Bit Score: 47.05 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 554 LLSNALR-----FTDEGQIVLRSRTDGEQWLVEVEDSGCGIDPAKLAEIfqpfiqvsGKRGGTGLGLT-ISSRLAQAMGG 627
Cdd:cd16956 9 IVENAVKhglsgLLDGGRVEITARLDGQHLLLEVEDNGGGMDPDTLARI--------LIRSSNGLGLNlVDKRLRQAFGN 80
|
90 100
....*....|....*....|.
gi 1447699372 628 E--LSATSTPEVGSCFCLRLP 646
Cdd:cd16956 81 DygLDIECAPGEGTRITIRLP 101
|
|
| REC_PatA-like |
cd17602 |
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ... |
672-733 |
2.87e-06 |
|
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) PatA is necessary for proper patterning of heterocysts along filaments. PatA contains phosphoacceptor REC domain at its C-terminus and an N-terminal PATAN (PatA N-terminus) domain, which was proposed in a bioinformatics study to mediate protein-protein interactions. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Some members of this group may have an inactive REC domain, lacking canonical metal-binding and active site residues.
Pssm-ID: 381129 [Multi-domain] Cd Length: 102 Bit Score: 46.59 E-value: 2.87e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1447699372 672 IEDNPLTQRITVEMLNTSGAQVVAIGNAAQALETLQNSEPfAAALVDFDLPDVNGITLARQL 733
Cdd:cd17602 4 VDDRPSIQKMIEYFLEKQGFRVVVIDDPLRALTTLLNSKP-DLILIDIDMPDLDGYELCSLL 64
|
|
| ComP |
COG4585 |
Signal transduction histidine kinase ComP [Signal transduction mechanisms]; |
554-648 |
2.92e-06 |
|
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
Pssm-ID: 443642 [Multi-domain] Cd Length: 252 Bit Score: 49.62 E-value: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 554 LLSNALRFTDEGQIVLRSRTDGEQWLVEVEDSGCGIDPAKLAeifqpfiqvsgkrgGTGLGLT-ISSRlAQAMGGELSAT 632
Cdd:COG4585 170 ALTNALKHAGATRVTVTLEVDDGELTLTVRDDGVGFDPEAAP--------------GGGLGLRgMRER-AEALGGTLTIG 234
|
90
....*....|....*.
gi 1447699372 633 STPEVGSCFCLRLPLR 648
Cdd:COG4585 235 SAPGGGTRVRATLPLA 250
|
|
| CheA |
COG0643 |
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms]; |
564-654 |
3.86e-06 |
|
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
Pssm-ID: 440408 [Multi-domain] Cd Length: 563 Bit Score: 50.57 E-value: 3.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 564 EGQIVLRSRTDGEQWLVEVEDSGCGIDPAKLAE------------------------IFQP-F-----I-QVSGkRGgtg 612
Cdd:COG0643 308 TGTITLSAYHEGGRVVIEVSDDGRGLDLEKIRAkaiekglitaeeaaalsdeellelIFAPgFstaeeVtDLSG-RG--- 383
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1447699372 613 LGLTISSRLAQAMGGELSATSTPEVGSCFCLRLPLRVATAPV 654
Cdd:COG0643 384 VGMDVVKTNIEALGGTIEIESEPGKGTTFTLRLPLTLAIIDG 425
|
|
| REC_OmpR_ArcA_TorR-like |
cd17619 |
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ... |
668-736 |
4.40e-06 |
|
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: 46.23 E-value: 4.40e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1447699372 668 RLLLIEDNPLTQRITVEMLNTSGAQVVAIGNAAQALETLQNsEPFAAALVDFDLPDVNGITLARQLARQ 736
Cdd:cd17619 2 HILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILAR-QDIDLVLLDINLPGKDGLSLTRELREQ 69
|
|
| dpiA |
PRK10046 |
two-component response regulator DpiA; Provisional |
667-784 |
8.91e-06 |
|
two-component response regulator DpiA; Provisional
Pssm-ID: 182208 [Multi-domain] Cd Length: 225 Bit Score: 47.70 E-value: 8.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 667 LRLLLIEDNPLTQRITVEMLN--TSGAQVVAIGNAAQALETLQNSEPfAAALVDFDLPDVNGITLARQLAR-QYPSLVLI 743
Cdd:PRK10046 5 LTLLIVEDETPLAEMHAEYIRhiPGFSQILLAGNLAQARMMIERFKP-GLILLDNYLPDGRGINLLHELVQaHYPGDVVF 83
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1447699372 744 GFSAHVIDETLRQRTSSLFRGIIpKPVPREVLGQLLAHYLQ 784
Cdd:PRK10046 84 TTAASDMETVSEAVRCGVFDYLI-KPIAYERLGQTLTRFRQ 123
|
|
| REC_OmpR_BaeR-like |
cd19938 |
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ... |
668-754 |
1.04e-05 |
|
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: 45.45 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 668 RLLLIEDNPLTQRITVEMLNTSGAQVVAIGNAAQALETLQNSEPfAAALVDFDLPDVNGITLARQLaRQYPSLVLIGFSA 747
Cdd:cd19938 1 RILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPP-DLILLDLMLPGTDGLTLCREI-RRFSDVPIIMVTA 78
|
....*....
gi 1447699372 748 HV--IDETL 754
Cdd:cd19938 79 RVeeIDRLL 87
|
|
| REC_RocR |
cd17530 |
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ... |
667-782 |
1.72e-05 |
|
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: 45.12 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 667 LRLLLIEDNPLTQRITVEMLNTSGA-QVVAIGNAAQALETLQNSEPfAAALVDFDLPDVNGITLARQLARQYPSLVLIGF 745
Cdd:cd17530 1 LRVLVLDDDPFQCMMAATILEDLGPgNVDEADDGREALVILLCNAP-DIIICDLKMPDMDGIEFLRHLAESHSNAAVILM 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1447699372 746 SAhvIDETLRQRTSSL-------FRGIIPKPVPREVLGQLLAHY 782
Cdd:cd17530 80 SG--LDGGILESAETLaganglnLLGTLSKPFSPEELTELLTKY 121
|
|
| REC_1_GGDEF |
cd19921 |
first phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ... |
668-757 |
2.21e-05 |
|
first 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 contains characteristic metal-binding and active site residues. PleD response regulators are global regulators of cell metabolism in some important human pathogens. This model describes the first REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381148 [Multi-domain] Cd Length: 115 Bit Score: 44.48 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 668 RLLLIEDNPLTQRITVEMLNTS-GAQVVAIGNAAQALETLQNSEPFAAALVDFDLPDV-NGITLARQLARQYPSLVLIGf 745
Cdd:cd19921 1 KVLIVEDSKTFSKVLKHLIAQElGLEVDVAETLAEAKALLEEGDDYFAALVDLNLPDApNGEAVDLVLEKGIPVIVLTG- 79
|
90
....*....|..
gi 1447699372 746 sahVIDETLRQR 757
Cdd:cd19921 80 ---SFDEDKRET 88
|
|
| HATPase_RsbT-like |
cd16934 |
Histidine kinase-like ATPase domain of the anti sigma-B factor Bacillus subtilis serine ... |
542-639 |
2.73e-05 |
|
Histidine kinase-like ATPase domain of the anti sigma-B factor Bacillus subtilis serine/threonine-protein kinase RsbT, and related domains; This family includes the histidine kinase-like ATPase (HATPase) domain of Bacillus subtilis serine/threonine-protein kinase RsbT, a component of the stressosome signaling complex of Bacillus subtilis. The stressosome is formed from multiple copies of three proteins, a sensor protein RsbR, a scaffold protein RsbS, and RsbT, and responds to environmental changes by initiating a protein partner switching cascade. Stress perception increases the phosphorylation of RsbR and RsbS, by RsbT. Subsequent dissociation of RsbT from the stressosome activates the sigma-B cascade, leading to the release of the alternative sigma factor, sigma-B.
Pssm-ID: 340411 [Multi-domain] Cd Length: 117 Bit Score: 44.28 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 542 GDPRRIRQVITNLLSNALRFTDEGQIVLRSRTDGEQWLVEV--EDSGCGIdpAKLAEIFQPfiQVSGKrGGTGLGLTISS 619
Cdd:cd16934 21 VRQAEIATAVTELARNLLKHAGGGQVLLEVVAEGGRVALEIlaVDQGPGI--ADVDEALRD--GFSTG-GGLGLGLGGVR 95
|
90 100
....*....|....*....|
gi 1447699372 620 RLAqamgGELSATSTPEVGS 639
Cdd:cd16934 96 RLA----DEFDLHSAPGRGT 111
|
|
| REC_OmpR_kpRstA-like |
cd17622 |
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ... |
668-743 |
3.81e-05 |
|
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: 43.91 E-value: 3.81e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1447699372 668 RLLLIEDNPLTQRITVEMLNTSGAQVVAIGNAAQALETLQNSEPfAAALVDFDLPDVNGITLARQLARQYPSLVLI 743
Cdd:cd17622 2 RILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIAREKP-DAVLLDIMLPGIDGLTLCRDLRPKYQGPILL 76
|
|
| HATPase_UhpB-NarQ-NarX-like |
cd16917 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
549-646 |
4.35e-05 |
|
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli UhpB, NarQ and NarX, and Bacillus subtilis YdfH, YhcY and YfiJ; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs) such as Escherichia coli UhpB, a HK of the UhpB-UhpA TCS, NarQ and NarX, HKs of the NarQ-NarP and NarX-NarL TCSs, respectively, and Bacillus YdfH, YhcY and YfiJ HKs, of the YdfH-YdfI, YhcY-YhcZ and YfiJ-YfiK TCSs, respectively. In addition, it includes Bacillus YxjM, ComP, LiaS and DesK, HKs of the YxjM-YxjML, ComP-ComA, LiaS-LiaR, DesR-DesK TCSs, respectively. Proteins having this HATPase domain have a histidine kinase dimerization and phosphoacceptor domain; some have accessory domains such as GAF, HAMP, PAS and MASE sensor domains.
Pssm-ID: 340394 [Multi-domain] Cd Length: 87 Bit Score: 42.93 E-value: 4.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 549 QVITNLLSNALRFTDEGQIVLRSRTDGEQWLVEVEDSGCGIDPAklaeifqpfiqvsGKRGGTGLGLTISSRLAQAMGGE 628
Cdd:cd16917 3 RIVQEALTNALKHAGASRVRVTLSYTADELTLTVVDDGVGFDGP-------------APPGGGGFGLLGMRERAELLGGT 69
|
90
....*....|....*...
gi 1447699372 629 LSATSTPEVGSCFCLRLP 646
Cdd:cd16917 70 LTIGSRPGGGTRVTARLP 87
|
|
| REC_NtrC1-like |
cd17572 |
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ... |
669-748 |
4.40e-05 |
|
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: 43.73 E-value: 4.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 669 LLLIEDNPLTQRITVEMLNTSGAQVVAIGNAAQALETLQNSePFAAALVDFDLPDVNGITLARQLARQYPSLVLIGFSAH 748
Cdd:cd17572 1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSDQ-PPDVVLLDLKLPDMSGMEILKWIQERSLPTSVIVITAH 79
|
|
| REC_RpfG-like |
cd17551 |
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ... |
668-743 |
4.51e-05 |
|
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: 43.58 E-value: 4.51e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1447699372 668 RLLLIEDNPLTQRITVEMLNTSG-AQVVAIGNAAQALETLQnSEPFAAALVDFDLPDVNGITLARQLaRQYPSLVLI 743
Cdd:cd17551 2 RILIVDDNPTNLLLLEALLRSAGyLEVVSFTDPREALAWCR-ENPPDLILLDYMMPGMDGLEFIRRL-RALPGLEDV 76
|
|
| REC_hyHK_blue-like |
cd18161 |
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ... |
670-740 |
5.00e-05 |
|
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: 43.10 E-value: 5.00e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1447699372 670 LLIEDNPLTQRITVEMLNTSGAQVVAIGNAAQALETLQNSEPFAAALVDFDLPD-VNGITLARQLARQYPSL 740
Cdd:cd18161 2 LVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLESGPDIDLLVTDVIMPGgMNGSQLAEEARRRRPDL 73
|
|
| REC_TrrA-like |
cd17554 |
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ... |
668-747 |
6.27e-05 |
|
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: 42.98 E-value: 6.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 668 RLLLIEDNPLTQRITVEMLNTSGAQVVAIGNAAQALETLQNsEPFAAALVDFDLPDVNGITLARQLARQYPSLVLIGFSA 747
Cdd:cd17554 2 KILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLES-EDPDLVILDIKMPGMDGLETLRKIREKKPDLPVIICTA 80
|
|
| REC_OmpR |
cd17574 |
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ... |
670-743 |
7.08e-05 |
|
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: 42.39 E-value: 7.08e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1447699372 670 LLIEDNPLTQRITVEMLNTSGAQVVAIGNAAQALETLQnSEPFAAALVDFDLPDVNGITLARQLaRQYPSLVLI 743
Cdd:cd17574 1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAR-EEQPDLIILDVMLPGMDGFEVCRRL-REKGSDIPI 72
|
|
| PRK11083 |
PRK11083 |
DNA-binding response regulator CreB; Provisional |
668-747 |
7.93e-05 |
|
DNA-binding response regulator CreB; Provisional
Pssm-ID: 236838 [Multi-domain] Cd Length: 228 Bit Score: 44.95 E-value: 7.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 668 RLLLIEDNPLTQRITVEMLNTSGAQVVAIGNAAQALETLQNSePFAAALVDFDLPDVNGITLARQLARQYPSLVLIGFSA 747
Cdd:PRK11083 5 TILLVEDEQAIADTLVYALQSEGFTVEWFERGLPALDKLRQQ-PPDLVILDVGLPDISGFELCRQLLAFHPALPVIFLTA 83
|
|
| REC_NtrX-like |
cd17550 |
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ... |
684-748 |
2.24e-04 |
|
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and similar proteins; NtrX is part of the two-component regulatory system NtrY/NtrX that is involved in the activation of nitrogen assimilatory genes such as Gln. It is phosphorylated by the histidine kinase NtrY and interacts with sigma-54. NtrX is a member of the NtrC family, characterized by a domain architecture containing an N-terminal REC domain, followed by a central sigma-54 interaction/ATPase domain, and a C-terminal DNA binding domain. NtrC family response regulators are sigma54-dependent transcriptional activators. Also included in this subfamily is Aquifex aeolicus NtrC4. The ability of the central domain to hydrolyze ATP and thus to interact effectively with a complex of RNA polymerase, sigma54, and promoter, is controlled by the phosphorylation status of the REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381102 [Multi-domain] Cd Length: 115 Bit Score: 41.71 E-value: 2.24e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1447699372 684 EMLNTSGAQVVAIGNAAQALETLQNSEPfAAALVDFDLPDVNGITLARQLARQYPSLVLIGFSAH 748
Cdd:cd17550 16 GILEDEGYEVDTAADGEEALKLIKERRP-DLVLLDIWLPDMDGLELLKEIKEKYPDLPVIMISGH 79
|
|
| REC_typeB_ARR-like |
cd17584 |
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ... |
670-753 |
2.98e-04 |
|
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: 41.07 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 670 LLIEDNPLTQRITVEMLNTSGAQVVAIGNAAQALETL-QNSEPFAAALVDFDLPDVNGITLArQLARQYPSLVLIGFSAH 748
Cdd:cd17584 2 LVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLrENKDEFDLVITDVHMPDMDGFEFL-ELIRLEMDLPVIMMSAD 80
|
....*
gi 1447699372 749 VIDET 753
Cdd:cd17584 81 GSTST 85
|
|
| PRK11644 |
PRK11644 |
signal transduction histidine-protein kinase/phosphatase UhpB; |
555-648 |
3.47e-04 |
|
signal transduction histidine-protein kinase/phosphatase UhpB;
Pssm-ID: 236945 [Multi-domain] Cd Length: 495 Bit Score: 44.20 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 555 LSNALRFTDEGQIVLRSRTDGEQWLVEVEDSGCGIDPAklaeifqpfiqvsgkRGGTGLGLT-ISSRLaQAMGGELSATS 633
Cdd:PRK11644 419 LNNIVKHADASAVTLQGWQQDERLMLVIEDDGSGLPPG---------------SGQQGFGLRgMRERV-TALGGTLTISC 482
|
90
....*....|....*
gi 1447699372 634 TPevGSCFCLRLPLR 648
Cdd:PRK11644 483 TH--GTRLSVSLPQR 495
|
|
| CitB |
COG2197 |
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ... |
667-733 |
3.80e-04 |
|
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: 41.42 E-value: 3.80e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1447699372 667 LRLLLIEDNPLTQRITVEMLNTS-GAQVVAI-GNAAQALETLQNSEPfAAALVDFDLPDVNGITLARQL 733
Cdd:COG2197 2 IRVLIVDDHPLVREGLRALLEAEpDIEVVGEaADGEEALELLEELRP-DVVLLDIRMPGMDGLEALRRL 69
|
|
| REC_OmpR_EcPhoP-like |
cd19934 |
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ... |
669-742 |
4.67e-04 |
|
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: 40.73 E-value: 4.67e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1447699372 669 LLLIEDNPLTQRITVEMLNTSGAQVVAIGNAAQALeTLQNSEPFAAALVDFDLPDVNGITLARQLARQ---YPSLVL 742
Cdd:cd19934 1 LLLVEDDALLAAQLKEQLSDAGYVVDVAEDGEEAL-FQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSEgraTPVLIL 76
|
|
| REC_Rcp-like |
cd17557 |
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ... |
668-740 |
4.70e-04 |
|
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: 40.86 E-value: 4.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 668 RLLLIEDNPLTQRITVEML--NTSGAQVVAIGNAAQALETLQNSEPFAAA------LVDFDLPDVNGITLARQLaRQYPS 739
Cdd:cd17557 1 TILLVEDNPGDAELIQEAFkeAGVPNELHVVRDGEEALDFLRGEGEYADAprpdliLLDLNMPRMDGFEVLREI-KADPD 79
|
.
gi 1447699372 740 L 740
Cdd:cd17557 80 L 80
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
136-436 |
4.92e-04 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 43.86 E-value: 4.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 136 IARLAQGQANNAATSAGATQAGIYDLIEQDQRQAAESALDRLIDIDLEYVNQMNELRLSALRVQQMVMNLGLEQIQKNAP 215
Cdd:COG0840 6 LLLALLLALLLLALSLLALLAAALLILLALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVVLLALL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 216 TLEKQLNNAVKILQRRQIRIEDPGVRAQVATTLTTVSQYSDLLALFQQDSEISNHLQTLAQNNIAQFAQFSSEVSQLVDT 295
Cdd:COG0840 86 LALLLLLLALLALALAALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAAALAA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 296 IELRNQhglahLEKASARGQYSLLLLGMVSLCALILILWRVVYRSVTRPLAEQTQALQRLLDGDIDSPFpETAGVRELDT 375
Cdd:COG0840 166 LLEAAA-----LALAAAALALALLAAALLALVALAIILALLLSRSITRPLRELLEVLERIAEGDLTVRI-DVDSKDEIGQ 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1447699372 376 IGRLMDAFRSSVHALNRHREQLAAQVKARTAELQELViehRQARAEAEKASQAKSAFLAAM 436
Cdd:COG0840 240 LADAFNRMIENLRELVGQVRESAEQVASASEELAASA---EELAAGAEEQAASLEETAAAM 297
|
|
| PRK09958 |
PRK09958 |
acid-sensing system DNA-binding response regulator EvgA; |
670-743 |
6.39e-04 |
|
acid-sensing system DNA-binding response regulator EvgA;
Pssm-ID: 182168 [Multi-domain] Cd Length: 204 Bit Score: 41.80 E-value: 6.39e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1447699372 670 LLIEDNPLTQRITVEMLNTSGAQVVA-IGNAAQALETLQNSEPfAAALVDFDLPDVNGITLARQL-ARQYPSLVLI 743
Cdd:PRK09958 4 IIIDDHPLAIAAIRNLLIKNDIEILAeLTEGGSAVQRVETLKP-DIVIIDVDIPGVNGIQVLETLrKRQYSGIIII 78
|
|
| dpiB |
PRK15053 |
sensor histidine kinase DpiB; Provisional |
550-646 |
7.70e-04 |
|
sensor histidine kinase DpiB; Provisional
Pssm-ID: 185013 [Multi-domain] Cd Length: 545 Bit Score: 43.28 E-value: 7.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 550 VITNLLSNA----LRfTDEG--QIVLRSRTDGEQWLVEVEDSGCGIDPAKLAEIFQPFIQV-SGKRGGTGLGLTISSRLA 622
Cdd:PRK15053 436 IVGNLLDNAfeasLR-SDEGnkIVELFLSDEGDDVVIEVADQGCGVPESLRDKIFEQGVSTrADEPGEHGIGLYLIASYV 514
|
90 100
....*....|....*....|....
gi 1447699372 623 QAMGGELSATSTPEVGSCFCLRLP 646
Cdd:PRK15053 515 TRCGGVITLEDNDPCGTLFSIFIP 538
|
|
| REC_DC-like |
cd17534 |
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ... |
668-770 |
8.16e-04 |
|
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: 40.08 E-value: 8.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 668 RLLLIEDNPLTQRITVEMLNTSGAQVVAI-GNAAQALETLQNSEPfAAALVDFDLP-DVNGITLARQLARQY--PSLVLi 743
Cdd:cd17534 2 KILIVEDEAIIALDLKEILESLGYEVVGIaDSGEEAIELAEENKP-DLILMDINLKgDMDGIEAAREIREKFdiPVIFL- 79
|
90 100
....*....|....*....|....*..
gi 1447699372 744 gfSAHVIDETLRQRTSSLFRGIIPKPV 770
Cdd:cd17534 80 --TAYSDEETLERAKETNPYGYLVKPF 104
|
|
| REC_YesN-like |
cd17536 |
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ... |
669-748 |
8.42e-04 |
|
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: 40.01 E-value: 8.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 669 LLLIEDNPLTQRITVEMLNTS--GAQVVAI-GNAAQALETLQNSEPfAAALVDFDLPDVNGITLARQLARQYPSLVLIGF 745
Cdd:cd17536 1 VLIVDDEPLIREGLKKLIDWEelGFEVVGEaENGEEALELIEEHKP-DIVITDIRMPGMDGLELIEKIRELYPDIKIIIL 79
|
...
gi 1447699372 746 SAH 748
Cdd:cd17536 80 SGY 82
|
|
| PRK10816 |
PRK10816 |
two-component system response regulator PhoP; |
667-732 |
1.26e-03 |
|
two-component system response regulator PhoP;
Pssm-ID: 182755 [Multi-domain] Cd Length: 223 Bit Score: 41.26 E-value: 1.26e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1447699372 667 LRLLLIEDNPLTQRITVEMLNTSGAQVVAIGNAAQALETLQNSEPfAAALVDFDLPDVNGITLARQ 732
Cdd:PRK10816 1 MRVLVVEDNALLRHHLKVQLQDAGHQVDAAEDAKEADYYLNEHLP-DIAIVDLGLPDEDGLSLIRR 65
|
|
| REC_OmpR_CusR-like |
cd19935 |
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ... |
669-743 |
1.30e-03 |
|
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: 38.96 E-value: 1.30e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1447699372 669 LLLIEDNPLTQRITVEMLNTSGAQVVAIGNAAQALEtLQNSEPFAAALVDFDLPDVNGITLARQL-ARQYPSLVLI 743
Cdd:cd19935 1 ILVVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLH-LALTNEYDLIILDVMLPGLDGLEVLRRLrAAGKQTPVLM 75
|
|
| REC_OmpR_PhoB |
cd17618 |
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ... |
668-736 |
1.54e-03 |
|
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: 39.15 E-value: 1.54e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1447699372 668 RLLLIEDNPLTQRITVEMLNTSGAQVVAIGNAAQALETLQNSEPfAAALVDFDLPDVNGITLARQLARQ 736
Cdd:cd17618 2 TILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPRP-DLILLDWMLPGGSGIQFIRRLKRD 69
|
|
| REC_PA4781-like |
cd19920 |
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ... |
669-733 |
1.58e-03 |
|
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: 38.65 E-value: 1.58e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1447699372 669 LLLIEDNPLTQRITVEMLNTSGAQVVAIGNAAQALETLQnSEPFAAALVDFDLPDVNGITLARQL 733
Cdd:cd19920 1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQ-AEPPDLILLDVMMPGMDGFEVCRRL 64
|
|
| HAMP |
pfam00672 |
HAMP domain; |
336-392 |
2.02e-03 |
|
HAMP domain;
Pssm-ID: 459898 [Multi-domain] Cd Length: 53 Bit Score: 37.22 E-value: 2.02e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1447699372 336 VVYRSVTRPLAEQTQALQRLLDGDIDSPFPETAGvrelDTIGRLMDAFRSSVHALNR 392
Cdd:pfam00672 1 LLARRILRPLRRLAEAARRIASGDLDVRLPVSGR----DEIGELARAFNQMAERLRE 53
|
|
| HATPase_EL346-LOV-HK-like |
cd16951 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
547-646 |
2.85e-03 |
|
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Erythrobacter litoralis blue light-activated histidine kinase 2; This domain family includes the histidine kinase-like ATPase (HATPase) domain of blue light-activated histidine kinase 2 of Erythrobacter litoralis (EL346). Signaling commonly occurs within HK dimers, however EL346 functions as a monomer. Also included in this family are the HATPase domains of ethanolamine utilization sensory transduction histidine kinase (EutW), whereby regulation of ethanolamine, a carbon and nitrogen source for gut bacteria, results in autophosphorylation and subsequent phosphoryl transfer to a response regulator (EutV) containing an RNA-binding domain. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some have an accessory PAS sensor domain, while some have an N-terminal histidine kinase domain.
Pssm-ID: 340427 [Multi-domain] Cd Length: 131 Bit Score: 38.94 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 547 IRQVITNLLSNALRFTDEGQIVLRSRTDGEQWLVEVEDSGCGIDpaklaEIFQPFIQVSgkrggtgLGLTISSRLAQAMG 626
Cdd:cd16951 44 VNELLQNALKHAFSDREGGTITIRSVVDGDYLRITVIDDGVGLP-----QDEDWPNKGS-------LGLQIVRSLVEGEL 111
|
90 100
....*....|....*....|
gi 1447699372 627 GELSATSTPEVGSCFCLRLP 646
Cdd:cd16951 112 KAFLEVQSAENGTRVNIDIP 131
|
|
| HATPase_PDK-like |
cd16929 |
Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain ... |
544-646 |
2.94e-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: 39.63 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 544 PRRIRQVITNLLSNALRFTDEGQ---------IVLRSRTDGEQWLVEVEDSGCGIDPAKLAEIF--------QPFIQ--- 603
Cdd:cd16929 41 PSHLYYILFELLKNAMRATVESHgddsddlppIKVTVAKGDEDLTIKISDRGGGIPREDLARLFsymystapQPSLDdfs 120
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1447699372 604 ------VSGKRGGTGLGLTISSRLAQAMGGELSATSTPEVGSCFCLRLP 646
Cdd:cd16929 121 dlisgtQPSPLAGFGYGLPMSRLYAEYFGGDLDLQSMEGYGTDVYIYLK 169
|
|
| HATPase_Phy-like |
cd16932 |
Histidine kinase-like ATPase domain of plant phytochromes similar to Arabidopsis thaliana ... |
542-630 |
3.18e-03 |
|
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: 38.41 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 542 GDPRRIRQVITNLLSNALRFT--DEGQIVLRSRTDGEQW-----LVEVE----DSGCGIDPAKLAEIFQPfiqvsgKRGG 610
Cdd:cd16932 2 GDQIRLQQVLADFLLNAVRFTpsPGGWVEIKVSPTKKQIgdgvhVIHLEfritHPGQGLPEELVQEMFEE------NQWT 75
|
90 100
....*....|....*....|..
gi 1447699372 611 T--GLGLTISSRLAQAMGGELS 630
Cdd:cd16932 76 TqeGLGLSISRKLVKLMNGDVR 97
|
|
| REC_PdtaR-like |
cd19932 |
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ... |
667-746 |
3.28e-03 |
|
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: 38.16 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 667 LRLLLIEDNPLTQRITVEMLNTSGAQVVA-IGNAAQALETLQNSEPfAAALVDFDLPDVNGITLARQLARQY--PSLVLI 743
Cdd:cd19932 1 VRVLIAEDEALIRMDLREMLEEAGYEVVGeASDGEEAVELAKKHKP-DLVIMDVKMPRLDGIEAAKIITSENiaPIVLLT 79
|
...
gi 1447699372 744 GFS 746
Cdd:cd19932 80 AYS 82
|
|
| PRK10643 |
PRK10643 |
two-component system response regulator PmrA; |
667-743 |
3.67e-03 |
|
two-component system response regulator PmrA;
Pssm-ID: 182612 [Multi-domain] Cd Length: 222 Bit Score: 40.02 E-value: 3.67e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1447699372 667 LRLLLIEDNPLTQRITVEMLNTSGAQVVAIGNAAQAlETLQNSEPFAAALVDFDLPDVNGITLARQLARQYPSL-VLI 743
Cdd:PRK10643 1 MKILIVEDDTLLLQGLILALQTEGYACDCASTAREA-EALLESGHYSLVVLDLGLPDEDGLHLLRRWRQKKYTLpVLI 77
|
|
| PRK10815 |
PRK10815 |
two-component system sensor histidine kinase PhoQ; |
549-642 |
3.68e-03 |
|
two-component system sensor histidine kinase PhoQ;
Pssm-ID: 182754 [Multi-domain] Cd Length: 485 Bit Score: 40.77 E-value: 3.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 549 QVITNLLSNALRFTDEGQIVLRSRTDGEQWLVeVEDSGCGIDPAKLAEIFQPFIQVSGKRGGTGLGLTISSRLAQAMGGE 628
Cdd:PRK10815 381 EVMGNVLDNACKYCLEFVEISARQTDEHLHIV-VEDDGPGIPESKRELIFDRGQRADTLRPGQGLGLSVAREITEQYEGK 459
|
90
....*....|....
gi 1447699372 629 LSATSTPEVGSCFC 642
Cdd:PRK10815 460 ISAGDSPLGGARME 473
|
|
| HAMP |
smart00304 |
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain; |
339-395 |
4.55e-03 |
|
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
Pssm-ID: 197640 [Multi-domain] Cd Length: 53 Bit Score: 36.07 E-value: 4.55e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1447699372 339 RSVTRPLAEQTQALQRLLDGDIDSPFPETAGvrelDTIGRLMDAFRSSVHALNRHRE 395
Cdd:smart00304 1 RRLLRPLRRLAEAAQRIADGDLTVRLPVDGR----DEIGELARAFNEMADRLEETIA 53
|
|
| REC_OmpR_CpxR |
cd17623 |
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ... |
669-780 |
5.25e-03 |
|
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: 37.67 E-value: 5.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 669 LLLIEDNPLTQRITVEMLNTSGAQVVAIGNAAQALETLQNSEPfAAALVDFDLPDVNGITLARQLaRQYPSLVLIGFSAH 748
Cdd:cd17623 1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEGSP-DLVVLDVMLPKMNGLDVLKEL-RKTSQVPVLMLTAR 78
|
90 100 110
....*....|....*....|....*....|....*.
gi 1447699372 749 ViDETlrQRTSSLFRG---IIPKPV-PREVLGQLLA 780
Cdd:cd17623 79 G-DDI--DRILGLELGaddYLPKPFnPRELVARIRA 111
|
|
| PRK11361 |
PRK11361 |
acetoacetate metabolism transcriptional regulator AtoC; |
668-787 |
7.74e-03 |
|
acetoacetate metabolism transcriptional regulator AtoC;
Pssm-ID: 183099 [Multi-domain] Cd Length: 457 Bit Score: 39.83 E-value: 7.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699372 668 RLLLIEDNPLTQRITVEMLNTSGAQVVAIGNAAQALETLQNSEPfAAALVDFDLPDVNGITLARQLARQYPSLVLIGFSA 747
Cdd:PRK11361 6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHP-DVVLMDIRMPEMDGIKALKEMRSHETRTPVILMTA 84
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1447699372 748 HVIDET-LRQRTSSLFRGIIpKPVPREVLGQLLAHYLQLQA 787
Cdd:PRK11361 85 YAEVETaVEALRCGAFDYVI-KPFDLDELNLIVQRALQLQS 124
|
|
| |
