|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11091 |
PRK11091 |
aerobic respiration control sensor protein ArcB; Provisional |
5-772 |
0e+00 |
|
aerobic respiration control sensor protein ArcB; Provisional
Pssm-ID: 236842 [Multi-domain] Cd Length: 779 Bit Score: 1003.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 5 SLSPWARVLSSSITRFGEFKTAAICYTLFLTVSLILSSMFYYVAIGELHLVDILAVVFFTAVVSPLIISVLLNSIRQLDA 84
Cdd:PRK11091 3 QIRLLAQYYVDLMVKLGLVRFSLLLALALVVLAMVVQMAVTMVLHGQVESIDVIRSIFFGLLITPWAVYFLSVVVEQLEE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 85 S-------YAYLDSATKQEKLLNQTLKDNINRLNIEIDERKMAFHAKHRAIEELRREIAERKKTQQELAQQSMLQRSIVD 157
Cdd:PRK11091 83 SrqrlsrlVAKLEEMRERDLELNVQLKDNIAQLNQEIAEREKAEEARQEAFEQLKNEIKEREETQIELEQQSSLLRSFLD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 158 SSPDLFYYRDNNGVFAGCNKMFEEVMGKSSSELIGKTVEQIFPSHFLSEVLKTDKEVEQSHKALTIDVGYEV-NGETRWF 236
Cdd:PRK11091 163 ASPDLVYYRNEDGEFSGCNRAMELLTGKSEKQLIGLTPKDVYSPEAAEKVIETDEKVFRHNVSLTYEQWLDYpDGRKACF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 237 ELRKLPFINDEGDYIGLLGFGRDITSRKEAAQALETAYKDKGKFIATLSHELRTPLNGIVGLTRMLLDTDLNKQQRSWGN 316
Cdd:PRK11091 243 ELRKVPFYDRVGKRHGLMGFGRDITERKRYQDALEKASRDKTTFISTISHELRTPLNGIVGLSRILLDTELTAEQRKYLK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 317 TIFSSAETLGNIFNDIIDLDKIDRDQLDIVTNSINVSDFINDVVNFAGLIAEQKELEFDIKRNGVLDIYAQLDPTRLRQV 396
Cdd:PRK11091 323 TIHVSAITLGNIFNDIIDMDKMERRKLQLDNQPIDFTDFLADLENLSGLQAEQKGLRFDLEPLLPLPHKVITDGTRLRQI 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 397 VWNLINNAVKFTQQGKVTLECSREnrvEGPWLVMKVSDTGQGIPPEQLAHIFDMYYKAPDLKGTN-AIGSGIGLAVTKAL 475
Cdd:PRK11091 403 LWNLISNAVKFTQQGGVTVRVRYE---EGDMLTFEVEDSGIGIPEDELDKIFAMYYQVKDSHGGKpATGTGIGLAVSKRL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 476 VSAMKGIITVNSTEGEGSCFTVQIPLSLCV-----APTEQSYVGRGLYILLVEDVPLNAEIATNLLEQRGHEVLWAETGE 550
Cdd:PRK11091 480 AQAMGGDITVTSEEGKGSCFTLTIHAPAVAeevedAFDEDDMPLPALNILLVEDIELNVIVARSVLEKLGNSVDVAMTGK 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 551 DALSFVEtEDDLDLVLLDMQLPDINGDVVAKQIRSDSHFDKL-PIVALTANVRSAEEELEGISIQGALAKPINTVKLDKM 629
Cdd:PRK11091 560 EALEMFD-PDEYDLVLLDIQLPDMTGLDIARELRERYPREDLpPLVALTANVLKDKKEYLDAGMDDVLSKPLSVPALTAM 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 630 LADLFGIKQSECTEPLLKVSEEAlkgiDAHLLDIETIEDFVNSMGLVVFRRSSQLFEKLSPQYQQELLTSLNTGDREEYE 709
Cdd:PRK11091 639 IKKFWDTQDDEESTVTTEESSKA----NEALLDIPMLEQYVELVGPKLITDSLAVFEKMMPGYLSVLDSNLTARDQKGIV 714
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 746446453 710 SVAHKLKGAAGSVGLNDVQLHAKIMEHGAIDESDEVLKQWLDILADKINEGQKALHLFLQQLE 772
Cdd:PRK11091 715 EEAHKIKGAAGSVGLRHLQQLAQQIQSPDLPAWWDNVQDWVEELKNEWRHDVEVLKAWLAQAE 777
|
|
| TMAO_torS |
TIGR02956 |
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ... |
263-730 |
3.79e-79 |
|
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: 273.96 E-value: 3.79e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 263 RKEAAQAlETAYKDKGKFIATLSHELRTPLNGIVGLTRMLLDTDLNKQQRSWGNTIFSSAETLGNIFNDIIDLDKIDRDQ 342
Cdd:TIGR02956 451 AKARAEA-EEANRAKSAFLATMSHEIRTPLNGILGTLELLGDTGLTSQQQQYLQVINRSGESLLDILNDILDYSKIEAGH 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 343 LDIVTNSINVSDFINDVVNFAGLIAEQKELEFDIKRNGVLDIYAQLDPTRLRQVVWNLINNAVKFTQQGKVTLECSRENr 422
Cdd:TIGR02956 530 LSISPRPFDLNALLDDVHHLMVSRAQLKGIQLRLNIPEQLPNWWQGDGPRIRQVLINLVGNAIKFTDRGSVVLRVSLND- 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 423 vEGPWLvMKVSDTGQGIPPEQLAHIFDMYYKAPDLKgtNAIGSGIGLAVTKALVSAMKGIITVNSTEGEGSCFTVQIPls 502
Cdd:TIGR02956 609 -DSSLL-FEVEDTGCGIAEEEQATLFDAFTQADGRR--RSGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTLP-- 682
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 503 LCVAPTEQSYVGR------GLYILLVEDVPLNAEIATNLLEQRGHEVLWAETGEDALSFVEtEDDLDLVLLDMQLPDING 576
Cdd:TIGR02956 683 LTRGKPAEDSATLtvidlpPQRVLLVEDNEVNQMVAQGFLTRLGHKVTLAESGQSALECFH-QHAFDLALLDINLPDGDG 761
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 577 DVVAKQIRS-DSHFDKLPIVALTANVRsaEEELEG---ISIQGALAKPINTVKLDKMLADLFGIKQSECTEPLL--KVSE 650
Cdd:TIGR02956 762 VTLLQQLRAiYGAKNEVKFIAFSAHVF--NEDVAQylaAGFDGFLAKPVVEEQLTAMIAVILAGGKSNTEAPVLsaSPSF 839
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 651 EALKGIDA--------------HLLDIETIEDFVNSMGLVVFRRSSQLFEKLSPQYQQELLTSLNTGDREEYESVAHKLK 716
Cdd:TIGR02956 840 DSASVIENaqaddipesnqaseFLLDEEQLQQDIEVLGVEKVRQLVALFKTSSAEQLEELSAARAVDDDAQIKKLAHKLK 919
|
490
....*....|....
gi 746446453 717 GAAGSVGLndVQLH 730
Cdd:TIGR02956 920 GSAGSLGL--TQLT 931
|
|
| BaeS |
COG0642 |
Signal transduction histidine kinase [Signal transduction mechanisms]; |
202-502 |
1.70e-63 |
|
Signal transduction histidine kinase [Signal transduction mechanisms];
Pssm-ID: 440407 [Multi-domain] Cd Length: 328 Bit Score: 215.54 E-value: 1.70e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 202 HFLSEVLKTDKEVEQSHKALTIDVGYEVNGETRWFELRKLPFINDEGDYIGLLGFGRDITSRKEAAQALETAYKDKGKFI 281
Cdd:COG0642 35 LLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLLLLEEANEAKSRFL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 282 ATLSHELRTPLNGIVGLTRMLLDTdLNKQQRSWGNTIFSSAETLGNIFNDIIDLDKIDRDQLDIVTNSINVSDFINDVVN 361
Cdd:COG0642 115 ANVSHELRTPLTAIRGYLELLLEE-LDEEQREYLETILRSADRLLRLINDLLDLSRLEAGKLELEPEPVDLAELLEEVVE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 362 FAGLIAEQKELEFDIKRNGVLdIYAQLDPTRLRQVVWNLINNAVKFTQQG-KVTLECSRENRvegpWLVMKVSDTGQGIP 440
Cdd:COG0642 194 LFRPLAEEKGIELELDLPDDL-PTVRGDPDRLRQVLLNLLSNAIKYTPEGgTVTVSVRREGD----RVRISVEDTGPGIP 268
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 746446453 441 PEQLAHIFDMYYKAPdlKGTNAIGSGIGLAVTKALVSAMKGIITVNSTEGEGSCFTVQIPLS 502
Cdd:COG0642 269 PEDLERIFEPFFRTD--PSRRGGGTGLGLAIVKRIVELHGGTIEVESEPGKGTTFTVTLPLA 328
|
|
| KdpD |
COG2205 |
K+-sensing histidine kinase KdpD [Signal transduction mechanisms]; |
264-502 |
5.27e-61 |
|
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
Pssm-ID: 441807 [Multi-domain] Cd Length: 239 Bit Score: 205.53 E-value: 5.27e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 264 KEAAQALETAYKDKGKFIATLSHELRTPLNGIVGLTRMLLD--TDLNKQQRSWGNTIFSSAETLGNIFNDIIDLDKIDRD 341
Cdd:COG2205 3 EEALEELEELERLKSEFLANVSHELRTPLTSILGAAELLLDeeDLSPEERRELLEIIRESAERLLRLIEDLLDLSRLESG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 342 QLDIVTNSINVSDFINDVVNFAGLIAEQKELEFDIKRNGVLdIYAQLDPTRLRQVVWNLINNAVKFTQQG-KVTLECSRE 420
Cdd:COG2205 83 KLSLELEPVDLAELLEEAVEELRPLAEEKGIRLELDLPPEL-PLVYADPELLEQVLANLLDNAIKYSPPGgTITISARRE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 421 NRvegpWLVMKVSDTGQGIPPEQLAHIFDMYYKAPDlkGTNAIGSGIGLAVTKALVSAMKGIITVNSTEGEGSCFTVQIP 500
Cdd:COG2205 162 GD----GVRISVSDNGPGIPEEELERIFERFYRGDN--SRGEGGTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFTVTLP 235
|
..
gi 746446453 501 LS 502
Cdd:COG2205 236 LA 237
|
|
| WalK |
COG5002 |
Sensor histidine kinase WalK [Signal transduction mechanisms]; |
213-502 |
2.85e-56 |
|
Sensor histidine kinase WalK [Signal transduction mechanisms];
Pssm-ID: 444026 [Multi-domain] Cd Length: 390 Bit Score: 197.85 E-value: 2.85e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 213 EVEQSHKALTIDVGYEVNGETRWFELRKLPFINDEGDYIGLLGFGRDITSRKEAAQALEtaykdkgKFIATLSHELRTPL 292
Cdd:COG5002 108 LALLILLAALLLLLSELLLLLLLLGRLSLRLSALLLGLLLLAAVERDITELERLEQMRR-------EFVANVSHELRTPL 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 293 NGIVGLTRMLLD--TDLNKQQRSWGNTIFSSAETLGNIFNDIIDLDKIDRDQLDIVTNSINVSDFINDVVNFAGLIAEQK 370
Cdd:COG5002 181 TSIRGYLELLLDgaADDPEERREYLEIILEEAERLSRLVNDLLDLSRLESGELKLEKEPVDLAELLEEVVEELRPLAEEK 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 371 ELEFDIKRNGVlDIYAQLDPTRLRQVVWNLINNAVKFTQQG-KVTLECSRENRvegpWLVMKVSDTGQGIPPEQLAHIFD 449
Cdd:COG5002 261 GIELELDLPED-PLLVLGDPDRLEQVLTNLLDNAIKYTPEGgTITVSLREEDD----QVRISVRDTGIGIPEEDLPRIFE 335
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 746446453 450 MYYKAPDLKGTNAIGSGIGLAVTKALVSAMKGIITVNSTEGEGSCFTVQIPLS 502
Cdd:COG5002 336 RFYRVDKSRSRETGGTGLGLAIVKHIVEAHGGRIWVESEPGKGTTFTITLPLA 388
|
|
| PRK11466 |
PRK11466 |
hybrid sensory histidine kinase TorS; Provisional |
260-750 |
1.15e-53 |
|
hybrid sensory histidine kinase TorS; Provisional
Pssm-ID: 236914 [Multi-domain] Cd Length: 914 Bit Score: 200.13 E-value: 1.15e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 260 ITSRKEAAQAlETAYKDKGKFIATLSHELRTPLNGIVGLTRMLLDTDLNKQQRSWGNTIFSSAETLGNIFNDIIDLDKID 339
Cdd:PRK11466 428 IEHRQARAEA-EKASQAKSAFLAAMSHEIRTPLYGILGTAQLLADNPALNAQRDDLRAITDSGESLLTILNDILDYSAIE 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 340 RDQLDIVTNS--INVSDFINDVVNFAGLIAEQKELEFDIKRNGVLDIYAQLDPTRLRQVVWNLINNAVKFTQQGKVTLEC 417
Cdd:PRK11466 507 AGGKNVSVSDepFEPRPLLESTLQLMSGRVKGRPIRLATDIADDLPTALMGDPRRIRQVITNLLSNALRFTDEGSIVLRS 586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 418 SREnrvEGPWLVmKVSDTGQGIPPEQLAHIFDMYYKAPDLKGtnaiGSGIGLAVTKALVSAMKGIITVNSTEGEGSCFTV 497
Cdd:PRK11466 587 RTD---GEQWLV-EVEDSGCGIDPAKLAEIFQPFVQVSGKRG----GTGLGLTISSRLAQAMGGELSATSTPEVGSCFCL 658
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 498 QIPLSLCVAPTE----QSYVGRGLYILLVEDVPLNAEIATNLLEQRGHEVLWAETGEDALSFVETEDDLDLVLLDMQLPD 573
Cdd:PRK11466 659 RLPLRVATAPVPktvnQAVRLDGLRLLLIEDNPLTQRITAEMLNTSGAQVVAVGNAAQALETLQNSEPFAAALVDFDLPD 738
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 574 INGDVVAKQIRsdSHFDKLPIVALTANV--RSAEEELEGIsIQGALAKPINTVKLDKMLADLFGIKQSectepllkvsee 651
Cdd:PRK11466 739 YDGITLARQLA--QQYPSLVLIGFSAHVidETLRQRTSSL-FRGIIPKPVPREVLGQLLAHYLQLQVN------------ 803
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 652 alkgiDAHLLDIETIEDFVNSMGLVVFRRSSQLFEKLSPQYQQELLTSLNTGDREEYESVAHKLKGAAGSVGLNDVQLHA 731
Cdd:PRK11466 804 -----NDQPLDVSQLNEDAALMGTEKIHEWLALFKQHALPLLDEIDIARASQDSEKIKRAAHQLKSSCSSLGMRQASQAC 878
|
490 500
....*....|....*....|....*...
gi 746446453 732 KIME---------HGAIDESDEVLKQWL 750
Cdd:PRK11466 879 AQLEqqplsaplpHEEITRSVAALEAWL 906
|
|
| PRK15347 |
PRK15347 |
two component system sensor kinase; |
265-737 |
5.99e-53 |
|
two component system sensor kinase;
Pssm-ID: 237951 [Multi-domain] Cd Length: 921 Bit Score: 198.33 E-value: 5.99e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 265 EAAQALETAYKDKGKFIATLSHELRTPLNGIVGLTRMLLDTDLNKQQRSWGNTIFSSAETLGNIFNDIIDLDKIDRDQLD 344
Cdd:PRK15347 386 EAKQRAEQANKRKSEHLTTISHEIRTPLNGVLGALELLQNTPLTAEQMDLADTARQCTLSLLAIINNLLDFSRIESGQMT 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 345 IVTNSINVSDFINDVVNFAGLIAEQKELEFDIKRNGVLDIYAQLDPTRLRQVVWNLINNAVKFTQQGKVTLECSRENRVe 424
Cdd:PRK15347 466 LSLEETALLPLLDQAMLTIQGPAQSKSLTLRTFVGAHVPLYLHLDSLRLRQILVNLLGNAVKFTETGGIRLRVKRHEQQ- 544
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 425 gpwLVMKVSDTGQGIPPEQLAHIFDMYYKApdlkGTNAIGSGIGLAVTKALVSAMKGIITVNSTEGEGSCFTVQIPLS-- 502
Cdd:PRK15347 545 ---LCFTVEDTGCGIDIQQQQQIFTPFYQA----DTHSQGTGLGLTIASSLAKMMGGELTLFSTPGVGSCFSLVLPLNey 617
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 503 -------------------------LCVAPTEQSYV---------GRgLY--------------------------ILLV 522
Cdd:PRK15347 618 appeplkgelsaplalhrqlsawgiTCQPGHQNPALldpelaylpGR-LYdllqqiiqgapnepvinlplqpwqlqILLV 696
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 523 EDVPLNAEIATNLLEQRGHEVLWAETGEDALSfVETEDDLDLVLLDMQLPDINGDVVAKQIRSDShfDKL----PIVALT 598
Cdd:PRK15347 697 DDVETNRDIIGMMLVELGQQVTTAASGTEALE-LGRQHRFDLVLMDIRMPGLDGLETTQLWRDDP--NNLdpdcMIVALT 773
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 599 ANVRSAE-EELEGISIQGALAKPINTVKLDKML---ADL---FGIK---QSECTEPLLKVSEEALKG-IDAHLLD-IETI 666
Cdd:PRK15347 774 ANAAPEEiHRCKKAGMNHYLTKPVTLAQLARALelaAEYqllRGIElspQDSSCSPLLDTDDMALNSkLYQSLLLlLAQI 853
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 746446453 667 EDFVNsmglvvfrrssqlfeklspqyqqelltslntgDREEYESVAHKLKGAAGSVGLNDVQLHAKIMEHG 737
Cdd:PRK15347 854 EQAVE--------------------------------NQEVLSQLLHTLKGCAGQAGLTELQCAVIDLENA 892
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
133-503 |
3.51e-51 |
|
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: 186.33 E-value: 3.51e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 133 REIAERKKTQQELAQQSMLQRSIVDSSPDLFYYRDNNGVFAGCNKMFEEVMGKSSSELIGKTVEQIFPSHFLSEVLKTDK 212
Cdd:COG5809 124 RDITERKRMEEALRESEEKFRLIFNHSPDGIIVTDLDGRIIYANPAACKLLGISIEELIGKSILELIHSDDQENVAAFIS 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 213 EVEQSHKALTIDVGYEV-NGETRWFELRKLPfINDEGDYIGLLGFGRDITSRKEAAQALEtaYKDK----GKFIATLSHE 287
Cdd:COG5809 204 QLLKDGGIAQGEVRFWTkDGRWRLLEASGAP-IKKNGEVDGIVIIFRDITERKKLEELLR--KSEKlsvvGELAAGIAHE 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 288 LRTPLNGIVGLTRMLLDTDlNKQQRSWGNTIFSSAETLGNIFNDIIDLDKIDrdqlDIVTNSINVSDFINDVVNF----A 363
Cdd:COG5809 281 IRNPLTSLKGFIQLLKDTI-DEEQKTYLDIMLSELDRIESIISEFLVLAKPQ----AIKYEPKDLNTLIEEVIPLlqpqA 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 364 GLIAEQKELEFDikrNGVLDIYaqLDPTRLRQVVWNLINNAVKFT-QQGKVTLEcsrENRVEGPWLVMKVSDTGQGIPPE 442
Cdd:COG5809 356 LLKNVQIELELE---DDIPDIL--GDENQLKQVFINLLKNAIEAMpEGGNITIE---TKAEDDDKVVISVTDEGCGIPEE 427
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 746446453 443 QLAHIFDMYYKAPDlKGTnaigsGIGLAVTKALVSAMKGIITVNSTEGEGSCFTVQIPLSL 503
Cdd:COG5809 428 RLKKLGEPFYTTKE-KGT-----GLGLMVSYKIIEEHGGKITVESEVGKGTTFSITLPIKL 482
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
144-502 |
2.28e-50 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 180.43 E-value: 2.28e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 144 ELAQQSMLQRSIVDSSPDLFYYRDNNGVFAGCNKMFEEVMGKSSSELIGKTVEQIFPSHflSEVLKTDKEVEQSHKALTi 223
Cdd:COG3852 1 ALRESEELLRAILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFPED--SPLRELLERALAEGQPVT- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 224 dvGYEV-----NGETRWFELRKLPFINDEGDyIGLLGFGRDITSRKEA------AQALETAykdkGKFIATLSHELRTPL 292
Cdd:COG3852 78 --EREVtlrrkDGEERPVDVSVSPLRDAEGE-GGVLLVLRDITERKRLerelrrAEKLAAV----GELAAGLAHEIRNPL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 293 NGIVGLTRMLLDTDLNKQQRSWGNTIFSSAETLGNIFNDIIDLDKIDRDQLDIVtnsiNVSDFINDVVNFAGL-IAEQKE 371
Cdd:COG3852 151 TGIRGAAQLLERELPDDELREYTQLIIEEADRLNNLVDRLLSFSRPRPPEREPV----NLHEVLERVLELLRAeAPKNIR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 372 LEFDIKrNGVLDIYAqlDPTRLRQVVWNLINNAVK-FTQQGKVTLECSRENRVE------GPWLVMKVSDTGQGIPPEQL 444
Cdd:COG3852 227 IVRDYD-PSLPEVLG--DPDQLIQVLLNLVRNAAEaMPEGGTITIRTRVERQVTlgglrpRLYVRIEVIDNGPGIPEEIL 303
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 445 AHIFDMYY--KApdlKGTnaigsGIGLAVTKALVSAMKGIITVNSTEGEGSCFTVQIPLS 502
Cdd:COG3852 304 DRIFEPFFttKE---KGT-----GLGLAIVQKIVEQHGGTIEVESEPGKGTTFRIYLPLE 355
|
|
| NtrY |
COG5000 |
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
57-502 |
4.27e-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: 164.75 E-value: 4.27e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 57 ILAVVFFTAVVSPLIISVLLNSIRQLDASYAYLDSATKQ------EKLLNQTLKDNINRLnieiderkmafhakHRAIEE 130
Cdd:COG5000 8 LLLLLLIALLLLLLALWLALLLARRLTRPLRRLAEATRAvaagdlSVRLPVTGDDEIGEL--------------ARAFNR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 131 LRREIAERkktQQELAQQSMLQRSIVDSSPDLFYYRDNNGVFAGCNKMFEEVMGKSSSELIGKTVEQIFPSHFLSEVLKt 210
Cdd:COG5000 74 MTDQLKEQ---REELEERRRYLETILENLPAGVIVLDADGRITLANPAAERLLGIPLEELIGKPLEELLPELDLAELLR- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 211 dkEVEQSHKALTIDVgyeVNGETRWFELRKLPFINDegdyiGLLGFGRDITS--RKEAAQALetaykdkGKFIATLSHEL 288
Cdd:COG5000 150 --EALERGWQEEIEL---TRDGRRTLLVRASPLRDD-----GYVIVFDDITEllRAERLAAW-------GELARRIAHEI 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 289 RTPLNGIVGLTRMLLDTDLNKQQ------RSWGNTIFSSAETLGNIFNDIIDLDKIDRDQLDIVtnsiNVSDFINDVVNF 362
Cdd:COG5000 213 KNPLTPIQLSAERLRRKLADKLEedredlERALDTIIRQVDRLKRIVDEFLDFARLPEPQLEPV----DLNELLREVLAL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 363 AGLIAEQKELEFDIKRNGVLdIYAQLDPTRLRQVVWNLINNAVKFT-QQGKVTLECSRENRvegpWLVMKVSDTGQGIPP 441
Cdd:COG5000 289 YEPALKEKDIRLELDLDPDL-PEVLADRDQLEQVLINLLKNAIEAIeEGGEIEVSTRREDG----RVRIEVSDNGPGIPE 363
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 746446453 442 EQLAHIFDMYYKapdlkgTNAIGSGIGLAVTKALVSAMKGIITVNSTEGEGSCFTVQIPLS 502
Cdd:COG5000 364 EVLERIFEPFFT------TKPKGTGLGLAIVKKIVEEHGGTIELESRPGGGTTFTIRLPLA 418
|
|
| PRK09959 |
PRK09959 |
acid-sensing system histidine kinase EvgS; |
131-770 |
8.51e-44 |
|
acid-sensing system histidine kinase EvgS;
Pssm-ID: 182169 [Multi-domain] Cd Length: 1197 Bit Score: 171.07 E-value: 8.51e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 131 LRREIAERKKTQQELAQQSMLQRSIVDSSPDLFYYRDNNGVFAGCNKMFEEVMGK---SSSELIGKTVEQIFPSHFLS-- 205
Cdd:PRK09959 557 LLRSVRRRKVIQGDLENQISFRKALSDSLPNPTYVVNWQGNVISHNSAFEHYFTAdyyKNAMLPLENSDSPFKDVFSNah 636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 206 EVLKTDKEVEQSH-KALTIDVGYEVNGETRWFELRKLPfINDEGDYIglLGFgRDITSRKEAAQALET-------AYKDK 277
Cdd:PRK09959 637 EVTAETKENRTIYtQVFEIDNGIEKRCINHWHTLCNLP-ASDHAVYI--CGW-QDITETRDLIHALEVernkainATVAK 712
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 278 GKFIATLSHELRTPLNGIVGLTRMLLDTDLNKQQRSWGNTI-FSSAETLGNIFNDIIDLDKIDRDQLDIVTNSINVSDFI 356
Cdd:PRK09959 713 SQFLATMSHEIRTPISSIMGFLELLSGSGLSKEQRVEAISLaYATGQSLLGLIGEILDVDKIESGNYQLQPQWVDIPTLV 792
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 357 NDVVNFAGLIAEQKELEFDIKRNGVLDIYAQLDPTRLRQVVWNLINNAVKFTQQGKVTLECSRENRVEGPWLV-MKVSDT 435
Cdd:PRK09959 793 QNTCHSFGAIAASKSIALSCSSTFPDHYLVKIDPQAFKQVLSNLLSNALKFTTEGAVKITTSLGHIDDNHAVIkMTIMDS 872
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 436 GQGIPPEQLAHIFDMYYKAPdlKGTNAIGSGIGLAVTKALVSAMKGIITVNSTEGEGSCFTVQIPLSLC--VAPTEQS-- 511
Cdd:PRK09959 873 GSGLSQEEQQQLFKRYSQTS--AGRQQTGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITIPVEISqqVATVEAKae 950
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 512 ---YVGRGLYILLVEDVPLNAEIATNLLEQRGHEVLWAETGEDALSFVETEdDLDLVLLDMQLPDINGDVVAKQIRSDSh 588
Cdd:PRK09959 951 qpiTLPEKLSILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQ-HYDLLITDVNMPNMDGFELTRKLREQN- 1028
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 589 fDKLPIVALTANVRSAEEElEGIS--IQGALAKPINtvkLDKMLADLFGIKQSECTEPLLK-VSEEALKGIDAHllDIET 665
Cdd:PRK09959 1029 -SSLPIWGLTANAQANERE-KGLScgMNLCLFKPLT---LDVLKTHLSQLHQVAHIAPQYRhLDIEALKNNTAN--DLQL 1101
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 666 IEDFvnsmgLVVFRRSSQlfEKLSPQYQqelltSLNTGDREEYESVAHKLKGAAGSVGLND-VQLHAKIMEHGAIDESDE 744
Cdd:PRK09959 1102 MQEI-----LMTFQHETH--KDLPAAFH-----ALEAGDNRTFHQCIHRIHGAANILNLQKlINISHQLEITPVSDDSKP 1169
|
650 660
....*....|....*....|....*.
gi 746446453 745 VLKQWLDILADKINEGQKALHLFLQQ 770
Cdd:PRK09959 1170 EILQLLNSVKEHIAELDQEIAVFCQK 1195
|
|
| PRK11107 |
PRK11107 |
hybrid sensory histidine kinase BarA; Provisional |
277-632 |
1.33e-43 |
|
hybrid sensory histidine kinase BarA; Provisional
Pssm-ID: 236848 [Multi-domain] Cd Length: 919 Bit Score: 170.03 E-value: 1.33e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 277 KGKFIATLSHELRTPLNGIVGLTRMLLDTDLNKQQRSWGNTIFSSAETLGNIFNDIIDLDKIDRDQLdiVTNSINVS--D 354
Cdd:PRK11107 293 KSEFLANMSHELRTPLNGVIGFTRQTLKTPLTPTQRDYLQTIERSANNLLAIINDILDFSKLEAGKL--VLENIPFSlrE 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 355 FINDVVNFAGLIAEQKELEFdikrngVLDIYAQL------DPTRLRQVVWNLINNAVKFTQQG----KVTLECSRENRVE 424
Cdd:PRK11107 371 TLDEVVTLLAHSAHEKGLEL------TLNIDPDVpdnvigDPLRLQQIITNLVGNAIKFTESGnidiLVELRALSNTKVQ 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 425 gpwLVMKVSDTGQGIPPEQLAHIFDMYYKApDlkgtNAI-----GSGIGLAVTKALVSAMKGIITVNSTEGEGSCFTVQI 499
Cdd:PRK11107 445 ---LEVQIRDTGIGISERQQSQLFQAFRQA-D----ASIsrrhgGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHL 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 500 PLSLCVAPTEQSYVGRGL---YILLVEDVPLNAEIATNLLEQRGHEVlwaeTGEDALSfveteddldlvlldmQLPDING 576
Cdd:PRK11107 517 PLDLNPNPIIDGLPTDCLagkRLLYVEPNSAAAQATLDILSETPLEV----TYSPTLS---------------QLPEAHY 577
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 746446453 577 DVV----------------AKQIRSDSHFDKLpIVALTANVRSAEEELEGISIQGALAKPINTVKLDKMLAD 632
Cdd:PRK11107 578 DILllglpvtfrepltmlhERLAKAKSMTDFL-ILALPCHEQVLAEQLKQDGADACLSKPLSHTRLLPALLE 648
|
|
| KinA |
COG5805 |
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ... |
133-502 |
1.03e-37 |
|
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: 147.96 E-value: 1.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 133 REIAERKKTQQELAQQSMLQRSIVDSSPDLFYYRDNNGVFAGCNKMFEEVMGKSSSELIGKTVEQIFPSHFLSEVLKTDK 212
Cdd:COG5805 140 RDITKKKKIEEILQEQEERLQTLIENSPDLICVIDTDGRILFINESIERLFGAPREELIGKNLLELLHPCDKEEFKERIE 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 213 EVEQSHKALTIDVG-YEVNGETRWFELRKLPFINDEGDYIGLLGFGRDITSRKEAAQALetAYKDK----GKFIATLSHE 287
Cdd:COG5805 220 SITEVWQEFIIEREiITKDGRIRYFEAVIVPLIDTDGSVKGILVILRDITEKKEAEELM--ARSEKlsiaGQLAAGIAHE 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 288 LRTPLNGIVGLTRMLLDTDLNKQQrsWGNTIFSSAETLGNIFNDIIDLDKIDRDQldivTNSINVSDFINDVVNF--AGL 365
Cdd:COG5805 298 IRNPLTSIKGFLQLLQPGIEDKEE--YFDIMLSELDRIESIISEFLALAKPQAVN----KEKENINELIQDVVTLleTEA 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 366 IAEQKELEFDIKRNgvlDIYAQLDPTRLRQVVWNLINNAVK-FTQQGKVTLECsrenRVEGPWLVMKVSDTGQGIPPEQL 444
Cdd:COG5805 372 ILHNIQIRLELLDE---DPFIYCDENQIKQVFINLIKNAIEaMPNGGTITIHT----EEEDNSVIIRVIDEGIGIPEERL 444
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 746446453 445 AHIFDMYYKAPDlKGTnaigsGIGLAVTKALVSAMKGIITVNSTEGEGSCFTVQIPLS 502
Cdd:COG5805 445 KKLGEPFFTTKE-KGT-----GLGLMVSYKIIENHNGTIDIDSKVGKGTTFTITLPLS 496
|
|
| PRK10841 |
PRK10841 |
two-component system sensor histidine kinase RcsC; |
262-501 |
3.67e-37 |
|
two-component system sensor histidine kinase RcsC;
Pssm-ID: 182772 [Multi-domain] Cd Length: 924 Bit Score: 150.12 E-value: 3.67e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 262 SRKEAAQALETAYKDKGKFIATLSHELRTPLNGIVGLTRMLLDTDLNKQQRSWGNTIFSSAETLGNIFNDIIDLDKIDRD 341
Cdd:PRK10841 432 SLQEMAQAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQTKELPKGVDRLVTAMNNSSSLLLKIISDILDFSKIESE 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 342 QLDIVTNSINVSDFINDVV-NFAGLIAeQKEL------EFDIKR--NGvldiyaqlDPTRLRQVVWNLINNAVKFTQQGK 412
Cdd:PRK10841 512 QLKIEPREFSPREVINHITaNYLPLVV-KKRLglycfiEPDVPValNG--------DPMRLQQVISNLLSNAIKFTDTGC 582
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 413 VTLECsrenRVEGPWLVMKVSDTGQGIPPEQLAHIFDMYYKAPDLKGTNAIGSGIGLAVTKALVSAMKGIITVNSTEGEG 492
Cdd:PRK10841 583 IVLHV----RVDGDYLSFRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLINMMDGDISVDSEPGMG 658
|
....*....
gi 746446453 493 SCFTVQIPL 501
Cdd:PRK10841 659 SQFTIRIPL 667
|
|
| COG4251 |
COG4251 |
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ... |
10-502 |
9.43e-37 |
|
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal transduction mechanisms];
Pssm-ID: 443393 [Multi-domain] Cd Length: 503 Bit Score: 144.93 E-value: 9.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 10 ARVLSSSITRFGEFKTAAICYTLFLTVSLILSSMFYYVAIGELHLVDILAVVFFTAVVSPLIISVLLNSIRQLDASYAYL 89
Cdd:COG4251 5 ALLLLLLLLLLLLLLLLLLLLLVLLLALALLLLLALLVLLLLLIRLLLLLLLSLLALLLLLLLLLLLLLVLAALALLLLL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 90 DSATKQEKLLNQTLKDNIN---RLNIEIDERKMAFHAKHRAIEELRREIAERKKTQQELAQQSMLQRSIVDSSPDLFYYR 166
Cdd:COG4251 85 LLLELALVLLALLLVLLLLlalLLLLALLLLLELLLLLLALLLLLLLLALLLLEELALLRLALALLLLLLLLLLLLLLLL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 167 DNNGVFAGCNKMFEEVMGKSSSELIGKTVEQIFPSHFLSEVLKTDKEVEQSHKALTIDVGYEVNGETRWFELRKLPFIND 246
Cdd:COG4251 165 ALILALLLAALAELELLLLLLLVLLLLLLLLLLLLLLLLRLLLELLLLLEAELLLSLGGGLGLLLLLLLLLVLLLLLILL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 247 EGDYIGLLGFGRDI-------TSRKEAAQALETAYKDKGKFIATLSHELRTPLNGIVGLTRMLLD---TDLNKQQRSWGN 316
Cdd:COG4251 245 LLLLILVLELLELRleleeleEELEERTAELERSNEELEQFAYVASHDLREPLRKISGFSQLLEEdygDKLDEEGREYLE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 317 TIFSSAETLGNIFNDIIDLDKIDRDQLDIVTnsINVSDFINDVVNFAGLIAEQKELEFDIkrNGVLDIYAqlDPTRLRQV 396
Cdd:COG4251 325 RIRDAAERMQALIDDLLAYSRVGRQELEFEP--VDLNELLEEVLEDLEPRIEERGAEIEV--GPLPTVRG--DPTLLRQV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 397 VWNLINNAVKFT---QQGKVTLECSREnrveGPWLVMKVSDTGQGIPPEQLAHIFDMYYKapdLKGTNAI-GSGIGLAVT 472
Cdd:COG4251 399 FQNLISNAIKYSrpgEPPRIEIGAERE----GGEWVFSVRDNGIGIDPEYAEKIFEIFQR---LHSRDEYeGTGIGLAIV 471
|
490 500 510
....*....|....*....|....*....|
gi 746446453 473 KALVSAMKGIITVNSTEGEGSCFTVQIPLS 502
Cdd:COG4251 472 KKIVERHGGRIWVESEPGEGATFYFTLPKA 501
|
|
| HATPase_EvgS-ArcB-TorS-like |
cd16922 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ... |
393-501 |
6.93e-35 |
|
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid sensor histidine kinases, similar to Escherichia coli EvgS, ArcB, TorS, BarA, RcsC; This family contains the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinases (HKs), including the following Escherichia coli HKs: EvgS, a HK of the EvgS-EvgA two-component system (TCS) that confers acid resistance; ArcB, a HK of the ArcB-ArcA TCS that modulates the expression of numerous genes in response to respiratory growth conditions; TorS, a HK of the TorS-TorR TCS which is involved in the anaerobic utilization of trimethylamine-N-oxide; BarA, a HK of the BarA-UvrY TCS involved in the regulation of carbon metabolism; and RcsC, a HK of the RcsB-RcsC TCS which regulates the expression of the capsule operon and of the cell division gene ftsZ. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), with most having accessory sensor domain(s) such as GAF, PAS and CHASE; many are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.
Pssm-ID: 340399 [Multi-domain] Cd Length: 110 Bit Score: 128.38 E-value: 6.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 393 LRQVVWNLINNAVKFTQQGKVTLECSRENRVEGP-WLVMKVSDTGQGIPPEQLAHIFDMYYKAPDLKGTNAIGSGIGLAV 471
Cdd:cd16922 1 LRQILLNLLGNAIKFTEEGEVTLRVSLEEEEEDGvQLRFSVEDTGIGIPEEQQARLFEPFSQADSSTTRKYGGTGLGLAI 80
|
90 100 110
....*....|....*....|....*....|
gi 746446453 472 TKALVSAMKGIITVNSTEGEGSCFTVQIPL 501
Cdd:cd16922 81 SKKLVELMGGDISVESEPGQGSTFTFTLPL 110
|
|
| PRK11360 |
PRK11360 |
two-component system sensor histidine kinase AtoS; |
167-501 |
5.77e-33 |
|
two-component system sensor histidine kinase AtoS;
Pssm-ID: 236901 [Multi-domain] Cd Length: 607 Bit Score: 135.10 E-value: 5.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 167 DNNGVFAGCNKMFEEVMGKSSSELIGKTVEQIFP--SHFLSEVLKTDKEVEQsHKALTIDvgYEVNGETRWFELRKLPFI 244
Cdd:PRK11360 279 DRQGKITTMNPAAEVITGLQRHELVGKPYSELFPpnTPFASPLLDTLEHGTE-HVDLEIS--FPGRDRTIELSVSTSLLH 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 245 NDEGDYIGLLGFGRDITSRKEA----AQALETAykDKGKFIATLSHELRTPLNGIVGLTRMLLDTDLNKQQRSWGNTIFS 320
Cdd:PRK11360 356 NTHGEMIGALVIFSDLTERKRLqrrvARQERLA--ALGELVAGVAHEIRNPLTAIRGYVQIWRQQTSDPPSQEYLSVVLR 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 321 SAETLGNIFNDIIDLDKIDRDQLDivtnSINVSDFINDVVNFAGLIAEQKELEFDIKRNGVLDIyAQLDPTRLRQVVWNL 400
Cdd:PRK11360 434 EVDRLNKVIDQLLEFSRPRESQWQ----PVSLNALVEEVLQLFQTAGVQARVDFETELDNELPP-IWADPELLKQVLLNI 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 401 INNAVK-FTQQGKVTLECSRENRVEgpwLVMKVSDTGQGIPPEQLAHIFDMYYKapdlkgTNAIGSGIGLAVTKALVSAM 479
Cdd:PRK11360 509 LINAVQaISARGKIRIRTWQYSDGQ---VAVSIEDNGCGIDPELLKKIFDPFFT------TKAKGTGLGLALSQRIINAH 579
|
330 340
....*....|....*....|..
gi 746446453 480 KGIITVNSTEGEGSCFTVQIPL 501
Cdd:PRK11360 580 GGDIEVESEPGVGTTFTLYLPI 601
|
|
| COG4191 |
COG4191 |
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ... |
197-502 |
2.77e-32 |
|
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal transduction mechanisms];
Pssm-ID: 443345 [Multi-domain] Cd Length: 361 Bit Score: 128.76 E-value: 2.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 197 QIFPSHFLSEVLKTDKEVEQSHKALTIDVGYEVNGETRWFELRKLPFINDEGDYIGLLGFGRDITSRKEAAQALETAYK- 275
Cdd:COG4191 53 LLLLLLLLLLELLLLLLALLGGLLRLLLLLGLLLLLLLEALLLLLLAALDAEENAELEELERDITELERAEEELRELQEq 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 276 ----DK----GKFIATLSHELRTPLNGIVG---LTRMLLDTDLNKQQ-RSWGNTIFSSAETLGNIFNDIIDLdkIDRDQL 343
Cdd:COG4191 133 lvqsEKlaalGELAAGIAHEINNPLAAILGnaeLLRRRLEDEPDPEElREALERILEGAERAAEIVRSLRAF--SRRDEE 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 344 DIVTnsINVSDFINDVVNFAGLIAEQK--ELEFDIKRNgVLDIYAqlDPTRLRQVVWNLINN---AVKFTQQGKVTLECs 418
Cdd:COG4191 211 EREP--VDLNELIDEALELLRPRLKARgiEVELDLPPD-LPPVLG--DPGQLEQVLLNLLINaidAMEEGEGGRITIST- 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 419 renRVEGPWLVMKVSDTGQGIPPEQLAHIFDMYY--KAPDlKGTnaigsGIGLAVTKALVSAMKGIITVNSTEGEGSCFT 496
Cdd:COG4191 285 ---RREGDYVVISVRDNGPGIPPEVLERIFEPFFttKPVG-KGT-----GLGLSISYGIVEKHGGRIEVESEPGGGTTFT 355
|
....*.
gi 746446453 497 VQIPLS 502
Cdd:COG4191 356 ITLPLA 361
|
|
| HATPase_c |
smart00387 |
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases. |
389-502 |
1.18e-31 |
|
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
Pssm-ID: 214643 [Multi-domain] Cd Length: 111 Bit Score: 118.91 E-value: 1.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 389 DPTRLRQVVWNLINNAVKFT-QQGKVTLECSRENRvegpWLVMKVSDTGQGIPPEQLAHIFDMYYKApDLKGTNAIGSGI 467
Cdd:smart00387 2 DPDRLRQVLSNLLDNAIKYTpEGGRITVTLERDGD----HVEITVEDNGPGIPPEDLEKIFEPFFRT-DKRSRKIGGTGL 76
|
90 100 110
....*....|....*....|....*....|....*
gi 746446453 468 GLAVTKALVSAMKGIITVNSTEGEGSCFTVQIPLS 502
Cdd:smart00387 77 GLSIVKKLVELHGGEISVESEPGGGTTFTITLPLE 111
|
|
| phoR_proteo |
TIGR02966 |
phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory ... |
153-499 |
6.14e-29 |
|
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: 118.47 E-value: 6.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 153 RSIVDSSPDLFYYRDNNGVFAGCNKMFEEVMGKSSSELIGKTV-EQIFPSHFLsEVLKTDKeveqSHKALTIDVGyevNG 231
Cdd:TIGR02966 9 RAAAQALPDAVVVLDEEGQIEWCNPAAERLLGLRWPDDLGQRItNLIRHPEFV-EYLAAGR----FSEPLELPSP---IN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 232 ETRWFELRKLPFinDEGDYigLLGFgRDITSRKEaaqaLETAYKDkgkFIATLSHELRTPLNGIVGLTRMLLDT--DLNK 309
Cdd:TIGR02966 81 SERVLEIRIAPY--GEEQK--LLVA-RDVTRLRR----LEQMRRD---FVANVSHELRTPLTVLRGYLETLADGpdEDPE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 310 QQRSWGNTIFSSAETLGNIFNDIIDLDKIDRDQLDIVTNSINVSDFINDVVNFAGLIAEQKELEFDIKRNGVLDIYAqlD 389
Cdd:TIGR02966 149 EWNRALEIMLEQSQRMQSLVEDLLTLSRLESAASPLEDEPVDMPALLDHLRDEAEALSQGKNHQITFEIDGGVDVLG--D 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 390 PTRLRQVVWNLINNAVKFTQ-QGKVTLECSRENrvEGPwlVMKVSDTGQGIPPEQLAHIFDMYYKAPDLKGTNAIGSGIG 468
Cdd:TIGR02966 227 EDELRSAFSNLVSNAIKYTPeGGTITVRWRRDG--GGA--EFSVTDTGIGIAPEHLPRLTERFYRVDKSRSRDTGGTGLG 302
|
330 340 350
....*....|....*....|....*....|.
gi 746446453 469 LAVTKALVSAMKGIITVNSTEGEGSCFTVQI 499
Cdd:TIGR02966 303 LAIVKHVLSRHHARLEIESELGKGSTFSFIF 333
|
|
| HATPase_c |
pfam02518 |
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ... |
389-501 |
2.21e-27 |
|
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.
Pssm-ID: 460579 [Multi-domain] Cd Length: 109 Bit Score: 106.68 E-value: 2.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 389 DPTRLRQVVWNLINNAVKFT-QQGKVTLECSRENrvegpWLVMKVSDTGQGIPPEQLAHIFDMYYKAPDLKGTnaiGSGI 467
Cdd:pfam02518 2 DELRLRQVLSNLLDNALKHAaKAGEITVTLSEGG-----ELTLTVEDNGIGIPPEDLPRIFEPFSTADKRGGG---GTGL 73
|
90 100 110
....*....|....*....|....*....|....
gi 746446453 468 GLAVTKALVSAMKGIITVNSTEGEGSCFTVQIPL 501
Cdd:pfam02518 74 GLSIVRKLVELLGGTITVESEPGGGTTVTLTLPL 107
|
|
| HATPase |
cd00075 |
Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ... |
393-499 |
2.31e-26 |
|
Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ATPase (HATPase) domains of several ATP-binding proteins such as histidine kinase, DNA gyrase B, topoisomerases, heat shock protein 90 (HSP90), phytochrome-like ATPases and DNA mismatch repair proteins. Domains belonging to this superfamily are also referred to as GHKL (gyrase, heat-shock protein 90, histidine kinase, MutL) ATPase domains.
Pssm-ID: 340391 [Multi-domain] Cd Length: 102 Bit Score: 103.84 E-value: 2.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 393 LRQVVWNLINNAVKFT-QQGKVTLECSREnrveGPWLVMKVSDTGQGIPPEQLAHIFDMYYKAPdlKGTNAIGSGIGLAV 471
Cdd:cd00075 1 LEQVLSNLLDNALKYSpPGGTIEISLRQE----GDGVVLEVEDNGPGIPEEDLERIFERFYRGD--KSREGGGTGLGLAI 74
|
90 100
....*....|....*....|....*...
gi 746446453 472 TKALVSAMKGIITVNSTEGEGSCFTVQI 499
Cdd:cd00075 75 VRRIVEAHGGRITVESEPGGGTTFTVTL 102
|
|
| PRK10364 |
PRK10364 |
two-component system sensor histidine kinase ZraS; |
263-501 |
6.19e-26 |
|
two-component system sensor histidine kinase ZraS;
Pssm-ID: 236674 [Multi-domain] Cd Length: 457 Bit Score: 111.80 E-value: 6.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 263 RKEAAQALetaykdkGKFIATLSHELRTPLNGIVGLTRMLLD-TDLNKQQRSWGNTIFSSAETLGNIFNDIIDLDKIDRD 341
Cdd:PRK10364 230 RKEKLVAL-------GHLAAGVAHEIRNPLSSIKGLAKYFAErAPAGGEAHQLAQVMAKEADRLNRVVSELLELVKPTHL 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 342 QLDIVtnsiNVSDFINDVVNFAGLIAEQKELEFDIKRNGVLDIyAQLDPTRLRQVVWNLINNAVK-FTQQGKVTLECSRE 420
Cdd:PRK10364 303 ALQAV----DLNDLINHSLQLVSQDANSREIQLRFTANDTLPE-IQADPDRLTQVLLNLYLNAIQaIGQHGVISVTASES 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 421 nrveGPWLVMKVSDTGQGIPPEQLAHIFDMYYKapdlkgTNAIGSGIGLAVTKALVSAMKGIITVNSTEGEGSCFTVQIP 500
Cdd:PRK10364 378 ----GAGVKISVTDSGKGIAADQLEAIFTPYFT------TKAEGTGLGLAVVHNIVEQHGGTIQVASQEGKGATFTLWLP 447
|
.
gi 746446453 501 L 501
Cdd:PRK10364 448 V 448
|
|
| cztS_silS_copS |
TIGR01386 |
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ... |
270-500 |
1.87e-22 |
|
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain (pfam00512) and a domain found in bacterial signal proteins (pfam00672). This group is separated phylogenetically from related proteins with similar architecture and contains a number of proteins associated with heavy metal resistance efflux systems for copper, silver, cadmium, and/or zinc.
Pssm-ID: 273593 [Multi-domain] Cd Length: 457 Bit Score: 101.31 E-value: 1.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 270 LETAYKDKGKFIATLSHELRTPLNGIVGLTRMLLDTDlnKQQRSWGNTIFSSAET---LGNIFNDIIDLDKIDRDQLDIV 346
Cdd:TIGR01386 234 LEDAFQRLSQFSADLAHELRTPLTNLLGQTQVALSQP--RTGEEYREVLESNLEElerLSRMVSDMLFLARADNGQLALE 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 347 TNSINVSDFINDVVNFAGLIAEQKELEFDIKRNGVLdiyaQLDPTRLRQVVWNLINNAVKFTQQG-KVTLECSREnrvEG 425
Cdd:TIGR01386 312 RVRLDLAAELAKVAEYFEPLAEERGVRIRVEGEGLV----RGDPQMFRRAISNLLSNALRHTPDGgTITVRIERR---SD 384
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 746446453 426 PWLVMkVSDTGQGIPPEQLAHIFDMYYKAPDLKGTNAIGSGIGLAVTKALVSAMKGIITVNSTEGEgSCFTVQIP 500
Cdd:TIGR01386 385 EVRVS-VSNPGPGIPPEHLSRLFDRFYRVDPARSNSGEGTGLGLAIVRSIMEAHGGRASAESPDGK-TRFILRFP 457
|
|
| phoR |
PRK11006 |
phosphate regulon sensor histidine kinase PhoR; |
234-505 |
2.72e-22 |
|
phosphate regulon sensor histidine kinase PhoR;
Pssm-ID: 182895 [Multi-domain] Cd Length: 430 Bit Score: 100.47 E-value: 2.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 234 RWFELRKLPFINDEgdyigLLGFGRDITSRKEaaqaLETAYKDkgkFIATLSHELRTPLNGIVGLTRMLLDTDLNKQQRS 313
Cdd:PRK11006 173 RHLEIRVMPYTEGQ-----LLMVARDVTQMHQ----LEGARRN---FFANVSHELRTPLTVLQGYLEMMQDQPLEGALRE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 314 WG-NTIFSSAETLGNIFNDIIDLDKID-RDQLDIvtnsinvsdfiNDVVNF-----------AGLIAEQKELEFDIKRNg 380
Cdd:PRK11006 241 KAlHTMREQTQRMEGLVKQLLTLSKIEaAPTIDL-----------NEKVDVpmmlrvlereaQTLSQGKHTITFEVDNS- 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 381 vLDIYAQLDptRLRQVVWNLINNAVKFTQQGkVTLECSRENRVEGPWLvmKVSDTGQGIPPEQLAHIFDMYYKAPDLKGT 460
Cdd:PRK11006 309 -LKVFGNED--QLRSAISNLVYNAVNHTPEG-THITVRWQRVPQGAEF--SVEDNGPGIAPEHIPRLTERFYRVDKARSR 382
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 746446453 461 NAIGSGIGLAVTKALVSAMKGIITVNSTEGEGSCFTVQIPLSLCV 505
Cdd:PRK11006 383 QTGGSGLGLAIVKHALSHHDSRLEIESEVGKGTRFSFVLPERLIA 427
|
|
| AdeS_HK |
NF012226 |
two-component sensor histidine kinase AdeS; Mutations in this component of the two-component ... |
267-501 |
2.40e-21 |
|
two-component sensor histidine kinase AdeS; Mutations in this component of the two-component regulatory system for the AdeABC efflux pump can confer adaptive resistance to certain antibiotics, including tigecycline.
Pssm-ID: 411090 [Multi-domain] Cd Length: 353 Bit Score: 96.22 E-value: 2.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 267 AQALETAYKDKGKFIATLSHELRTP-------LNGIV--------GLTRMLLdtdlnkqqrswgntifSSAETLGNIFND 331
Cdd:NF012226 128 AQKLESSVKNAQVWNAAIAHELRTPitilqgrLQGILdgvfepdpALFKSLL----------------NQVEGLSHLVED 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 332 IIDLDKIDRDQLDIVTNSINVSDFINDVVNFAGLIAEQKELEFdikrngVLDIYAQL---DPTRLRQVVWNLINNAVKFT 408
Cdd:NF012226 192 LRTLSLVENQQLRLNYESVDLKDSIEKVLKMFEDRLEQAQLTI------VLNLTATPvfcDRRRIEQVLIALIDNAIRYA 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 409 QQGKVTLecsRENRVEGPWlVMKVSDTGQGIPPEQLAHIFDMYYKAPDLKGTNAIGSGIGLAVTKALVSAMKGIITVnST 488
Cdd:NF012226 266 NAGKLKI---SSSVIQDDW-ILQIEDEGPGIAEEYQQDLFNPFFRLEQSRNKEFGGTGLGLAVVHAIVIAHKGSIEY-SN 340
|
250
....*....|...
gi 746446453 489 EGEGSCFTVQIPL 501
Cdd:NF012226 341 SQGNSVFTIKLPA 353
|
|
| PRK09835 |
PRK09835 |
Cu(+)/Ag(+) sensor histidine kinase; |
270-500 |
2.07e-20 |
|
Cu(+)/Ag(+) sensor histidine kinase;
Pssm-ID: 182101 [Multi-domain] Cd Length: 482 Bit Score: 95.22 E-value: 2.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 270 LETAYKDKGKFIATLSHELRTPLNGIVGLTRMLLDTdlNKQQRSWGNTIFSSAETLG---NIFNDIIDLDKIDRDQLDIV 346
Cdd:PRK09835 255 IEDVFTRQSNFSADIAHEIRTPITNLITQTEIALSQ--SRSQKELEDVLYSNLEELTrmaKMVSDMLFLAQADNNQLIPE 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 347 TNSINVSDFINDVVNFAGLIAEQKELEFDIKRNGVLdiyAQLDPTRLRQVVWNLINNAVKFTQQGK-VTLECS-RENRVE 424
Cdd:PRK09835 333 KKMLDLADEVGKVFDFFEAWAEERGVELRFVGDPCQ---VAGDPLMLRRAISNLLSNALRYTPAGEaITVRCQeVDHQVQ 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 746446453 425 gpwlvMKVSDTGQGIPPEQLAHIFDMYYKAPDLKGTNAIGSGIGLAVTKALVSAMKGIITVNStEGEGSCFTVQIP 500
Cdd:PRK09835 410 -----LVVENPGTPIAPEHLPRLFDRFYRVDPSRQRKGEGSGIGLAIVKSIVVAHKGTVAVTS-DARGTRFVISLP 479
|
|
| CitA |
COG3290 |
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ... |
128-502 |
2.20e-20 |
|
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction mechanisms];
Pssm-ID: 442519 [Multi-domain] Cd Length: 389 Bit Score: 94.14 E-value: 2.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 128 IEELRREIAERKKTQQELAQQSMLQRSIVDSSPDLFYYRDNNGVFAGCNKMFEEVMGKsssELIGKTVEQIFPshflsEV 207
Cdd:COG3290 62 LLLLLLLAALLLKLLEEIARLVEEREAVLESIREGVIAVDRDGRITLINDAARRLLGL---DAIGRPIDEVLA-----EV 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 208 LKTDKEVEqshkaltidvgyEVNGETRWFELRKLPfINDEGDYIGLLGFGRDITSRKEAAQALETAYKdkgkFIATL--- 284
Cdd:COG3290 134 LETGERDE------------EILLNGRVLVVNRVP-IRDDGRVVGAVATFRDRTELERLEEELEGVKE----LAEALraq 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 285 SHELRTPLNGIVGLTRMLLDTDLnkqqrswgntifssAETLGNIFNDIIDLDkidrDQLDIVTNSINVSDFINDVVNfag 364
Cdd:COG3290 197 RHDFRNHLHTISGLLQLGEYDEA--------------LEYIDEISEELQELI----DSLLSRIGNPVLAALLLGKAA--- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 365 lIAEQKELEFDIKRNGVLDiYAQLDPTRLRQVVWNLINNAV-----KFTQQGKVTLECSRENRvegpWLVMKVSDTGQGI 439
Cdd:COG3290 256 -RARERGIDLTIDIDSDLP-DLPLSDTDLVTILGNLLDNAIeavekLPEEERRVELSIRDDGD----ELVIEVEDSGPGI 329
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 746446453 440 PPEQLAHIFDMYY--KAPDlkgtnaiGSGIGLAVTKALVSAMKGIITVNSTEGEGSCFTVQIPLS 502
Cdd:COG3290 330 PEELLEKIFERGFstKLGE-------GRGLGLALVKQIVEKYGGTIEVESEEGEGTVFTVRLPKE 387
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
140-271 |
2.91e-20 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 91.24 E-value: 2.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 140 KTQQELAQQSMLQRSIVDSSPDLFYYRDNNGVFAGCNKMFEEVMGKSSSELIGKTVEQIFPSHFLSEVLKTDKEVEQSHK 219
Cdd:COG2202 1 TAEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 746446453 220 ALTIDV-GYEVNGETRWFELRKLPFINDEGDYIGLLGFGRDITSRKEAAQALE 271
Cdd:COG2202 81 VWRGELrNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALR 133
|
|
| HATPase_TutC-TodS-like |
cd16925 |
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ... |
389-500 |
6.48e-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: 85.62 E-value: 6.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 389 DPTRLRQVVWNLINNAVKFTQQG---KVTLECSRENRVegpwlVMKVSDTGQGIPPEQLAHIFDMYYKAPDLKGTNAIGS 465
Cdd:cd16925 1 DAEKYERVVLNLLSNAFKFTPDGgriRCILEKFRLNRF-----LLTVSDSGPGIPPNLREEIFERFRQGDGSSTRAHGGT 75
|
90 100 110
....*....|....*....|....*....|....*
gi 746446453 466 GIGLAVTKALVSAMKGIITVNSTEGEGSCFTVQIP 500
Cdd:cd16925 76 GLGLSIVKEFVELHGGTVTVSDAPGGGALFQVELP 110
|
|
| PRK13837 |
PRK13837 |
two-component system VirA-like sensor kinase; |
262-632 |
1.88e-19 |
|
two-component system VirA-like sensor kinase;
Pssm-ID: 237526 [Multi-domain] Cd Length: 828 Bit Score: 93.59 E-value: 1.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 262 SRKEAAQALETAykdkGKFIATLSHELRTPLNGIVGLTRMLLDT-DLNKQQRSWGNTIFSSAETLGNIFNDIIDLDKidr 340
Cdd:PRK13837 439 RRLEHARRLEAV----GTLASGIAHNFNNILGAILGYAEMALNKlARHSRAARYIDEIISAGARARLIIDQILAFGR--- 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 341 dQLDIVTNSINVSDFINDVVNF--AGLiAEQKELEFDIKRNGVLdiyAQLDPTRLRQVVWNLINNAVK-FTQQGKVTLEC 417
Cdd:PRK13837 512 -KGERNTKPFDLSELVTEIAPLlrVSL-PPGVELDFDQDQEPAV---VEGNPAELQQVLMNLCSNAAQaMDGAGRVDISL 586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 418 SR-ENRVE----------GPWLVMKVSDTGQGIPPEQLAHIFDMYYKapdlkgTNAIGSGIGLAVTKALVSAMKGIITVN 486
Cdd:PRK13837 587 SRaKLRAPkvlshgvlppGRYVLLRVSDTGAGIDEAVLPHIFEPFFT------TRAGGTGLGLATVHGIVSAHAGYIDVQ 660
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 487 STEGEGSCFTVQIPLSLCVAPTEQSY-------VGRGLYILLVEDVPLNAEIATNLLEQRGHEVLWAETGEDALSFVeTE 559
Cdd:PRK13837 661 STVGRGTRFDVYLPPSSKVPVAPQAFfgpgplpRGRGETVLLVEPDDATLERYEEKLAALGYEPVGFSTLAAAIAWI-SK 739
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 746446453 560 DDLDLVLLDMQLP--DINGDVVAKQirsdSHFDKLPIVALTANVRSAEEELEGISIQGALAKPINTVKLDKMLAD 632
Cdd:PRK13837 740 GPERFDLVLVDDRllDEEQAAAALH----AAAPTLPIILGGNSKTMALSPDLLASVAEILAKPISSRTLAYALRT 810
|
|
| CheY |
COG0784 |
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ... |
514-639 |
2.03e-19 |
|
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator Spo0F [Signal transduction mechanisms];
Pssm-ID: 440547 [Multi-domain] Cd Length: 128 Bit Score: 84.90 E-value: 2.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 514 GRGLYILLVEDVPLNAEIATNLLEQRGHEVLWAETGEDALSFVETEDdldlvlldMQLPDINGDVVAKQIRSDSHFDKLP 593
Cdd:COG0784 3 LGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPpdli-lldINMPGMDGLELLRRIRALPRLPDIP 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 746446453 594 IVALTANVRSAEEElEGIS--IQGALAKPINTVKLDKMLADLFGIKQS 639
Cdd:COG0784 82 IIALTAYADEEDRE-RALEagADDYLTKPVDPEELLEALRRLLARASA 128
|
|
| PRK13557 |
PRK13557 |
histidine kinase; Provisional |
167-584 |
2.26e-19 |
|
histidine kinase; Provisional
Pssm-ID: 237425 [Multi-domain] Cd Length: 540 Bit Score: 92.43 E-value: 2.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 167 DNNGVFAgcNKMFEEVMGKSSSELIGKTVEqifpshFLsEVLKTDKEVEQS-------HKALTIDV-GYEVNGETRWFEL 238
Cdd:PRK13557 52 DNPIVFA--NRAFLEMTGYAAEEIIGNNCR------FL-QGPETDRATVAEvrdaiaeRREIATEIlNYRKDGSSFWNAL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 239 RKLPFINDEGDYIGLLGFGRDITSRKEAAQALETAYKDK--GKFIATLSHELRTPLNGIVGLTRMLL------DTDLNKQ 310
Cdd:PRK13557 123 FVSPVYNDAGDLVYFFGSQLDVSRRRDAEDALRQAQKMEalGQLTGGIAHDFNNLLQVMSGYLDVIQaalshpDADRGRM 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 311 QRSWGNtIFSSAE---TLGNifndiiDLDKIDRDQ-LDIVTnsINVSDFINDVVNFA-----GLIAEQKELEFDIKRngv 381
Cdd:PRK13557 203 ARSVEN-IRAAAEraaTLTQ------QLLAFARKQrLEGRV--LNLNGLVSGMGELAertlgDAVTIETDLAPDLWN--- 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 382 ldiyAQLDPTRLRQVVWN-LINNAVKFTQQGKVT-----LECSRENRV------EGPWLVMKVSDTGQGIPPEQLAHIFD 449
Cdd:PRK13557 271 ----CRIDPTQAEVALLNvLINARDAMPEGGRVTirtrnVEIEDEDLAmyhglpPGRYVSIAVTDTGSGMPPEILARVMD 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 450 MYYKAPDlKGTnaiGSGIGLAVTKALVSAMKGIITVNSTEGEGSCFTVQIPLSLCVAPTEQSYVGRGL------YILLVE 523
Cdd:PRK13557 347 PFFTTKE-EGK---GTGLGLSMVYGFAKQSGGAVRIYSEVGEGTTVRLYFPASDQAENPEQEPKARAIdrggteTILIVD 422
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 746446453 524 DVPLNAEIATNLLEQRGHEVLWAETGEDALSFVETEDDLDLVLLDMQLP-DINGDVVAKQIR 584
Cdd:PRK13557 423 DRPDVAELARMILEDFGYRTLVASNGREALEILDSHPEVDLLFTDLIMPgGMNGVMLAREAR 484
|
|
| PRK09303 |
PRK09303 |
histidine kinase; |
263-500 |
1.41e-18 |
|
histidine kinase;
Pssm-ID: 236462 [Multi-domain] Cd Length: 380 Bit Score: 88.47 E-value: 1.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 263 RKEAAQALE-TAYKDKgkFIATLSHELRTPLNGivglTRMLLDTdlnKQQRSWGNTIFSSAETLGNIFNDIID-LDKIDR 340
Cdd:PRK09303 138 RQENETLLEqLKFKDR--VLAMLAHDLRTPLTA----ASLALET---LELGQIDEDTELKPALIEQLQDQARRqLEEIER 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 341 ---DQLDIVTNSINVSDFINDVVNFAGLIAE------------QKELEFDIKRNgVLDIYAqlDPTRLRQVVWNLINNAV 405
Cdd:PRK09303 209 litDLLEVGRTRWEALRFNPQKLDLGSLCQEvilelekrwlakSLEIQTDIPSD-LPSVYA--DQERIRQVLLNLLDNAI 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 406 KFTQ-QGKVTLEC-SRENRvegpWLVMKVSDTGQGIPPEQLAHIFDMYYKAPDLKGTnaIGSGIGLAVTKALVSAMKGII 483
Cdd:PRK09303 286 KYTPeGGTITLSMlHRTTQ----KVQVSICDTGPGIPEEEQERIFEDRVRLPRDEGT--EGYGIGLSVCRRIVRVHYGQI 359
|
250
....*....|....*..
gi 746446453 484 TVNSTEGEGSCFTVQIP 500
Cdd:PRK09303 360 WVDSEPGQGSCFHFTLP 376
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
133-270 |
2.62e-18 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 85.46 E-value: 2.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 133 REIAERKKTQQELAQQSMLQRSIVDSSPDLFYYRDNNGVFAGCNKMFEEVMGKSSSELIGKTVEQIFPSHFLSEVLKTDK 212
Cdd:COG2202 120 RDITERKRAEEALRESEERLRLLVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLR 199
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 746446453 213 EVEQSHKALTIDVGYEVNGETRWFELR-KLPFINDEGDYIGLLGFGRDITSRKEAAQAL 270
Cdd:COG2202 200 RLLEGGRESYELELRLKDGDGRWVWVEaSAVPLRDGGEVIGVLGIVRDITERKRAEEAL 258
|
|
| REC_DivK-like |
cd17548 |
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ... |
518-626 |
6.32e-18 |
|
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: 79.89 E-value: 6.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 518 YILLVEDVPLNAEIATNLLEQRGHEVLWAETGEDALSFVEtEDDLDLVLLDMQLPDINGDVVAKQIRSDSHFDKLPIVAL 597
Cdd:cd17548 1 KILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIAR-KEKPDLILMDIQLPGMDGLEATRLLKEDPATRDIPVIAL 79
|
90 100 110
....*....|....*....|....*....|.
gi 746446453 598 TANVRSAEEE--LEGiSIQGALAKPINTVKL 626
Cdd:cd17548 80 TAYAMKGDREkiLEA-GCDGYISKPIDTREF 109
|
|
| BaeS_SmeS |
NF012163 |
sensor histidine kinase efflux regulator BaeS; |
267-500 |
8.68e-18 |
|
sensor histidine kinase efflux regulator BaeS;
Pssm-ID: 411086 [Multi-domain] Cd Length: 457 Bit Score: 86.80 E-value: 8.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 267 AQALETAYKDKGKFIATLSHELRTPL-----------NGIVGLTRMLLDTdLNKQQRswgntifssaeTLGNIFNDIIDL 335
Cdd:NF012163 230 ASTLEKNEQMRRDFMADISHELRTPLavlraeleaiqDGIRKFTPESLDS-LQAEVG-----------TLTKLVDDLHDL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 336 DKIDRDQLDIVTNSINVSDFINDVVNFAGLIAEQKELEFDIKRNGVLDIYAqlDPTRLRQVVWNLINNAVKFTQQ-GKVT 414
Cdd:NF012163 298 SMSDEGALAYQKASVDLVPLLEVEGGAFRERFASAGLELEVSLPDSSLVFG--DRDRLMQLFNNLLENSLRYTDSgGSLH 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 415 LECSRENRVegpwLVMKVSDTGQGIPPEQLAHIFDMYYKAPDLKGTNAIGSGIGLAVTKALVSAMKGIITVNSTEGEGSC 494
Cdd:NF012163 376 ISASQRPKE----VTLTVADSAPGVSDEQLARLFERFYRVEVSRNRASGGSGLGLAISLNIVQAHGGTLHAAHSPLGGLR 451
|
....*.
gi 746446453 495 FTVQIP 500
Cdd:NF012163 452 IVVTLP 457
|
|
| PAS_4 |
pfam08448 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
156-265 |
1.09e-17 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain is associated to signalling systems and works as a signal sensor domain. It recognizes differently substituted aromatic hydrocarbons, oxygen, different dodecanoic acids, autoinducers, 3,5-dimethyl-pyrazin-2-ol and N-alanyl-aminoacetone (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 312075 [Multi-domain] Cd Length: 110 Bit Score: 79.38 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 156 VDSSPDLFYYRDNNGVFAGCNKMFEEVMGKSSSELIGKTVEQIFPSHFLSEVLKTDKEVEQSHKALTIDVGYEVNGETRW 235
Cdd:pfam08448 1 LDSLPDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAELLPPEDAARLERALRRALEGEEPIDFLEELLLNGEERH 80
|
90 100 110
....*....|....*....|....*....|
gi 746446453 236 FELRKLPFINDEGDYIGLLGFGRDITSRKE 265
Cdd:pfam08448 81 YELRLTPLRDPDGEVIGVLVISRDITERRR 110
|
|
| REC_hyHK_CKI1_RcsC-like |
cd17546 |
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ... |
519-630 |
2.24e-17 |
|
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: 78.28 E-value: 2.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 519 ILLVEDVPLNAEIATNLLEQRGHEVLWAETGEDALSFVETEddldlvllD-------MQLPDINGDVVAKQIRSDSHFDK 591
Cdd:cd17546 1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEE--------PfdlvlmdLQMPVMDGLEATRRIRELEGGGR 72
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 746446453 592 -LPIVALTANVRSAE-EELEGISIQGALAKPINTVKLDKML 630
Cdd:cd17546 73 rTPIIALTANALEEDrEKCLEAGMDDYLSKPVKLDQLKEVL 113
|
|
| HATPase_DpiB-CitA-like |
cd16915 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
396-500 |
7.32e-17 |
|
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: 76.56 E-value: 7.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 396 VVWNLINNAVKF---TQQGKVTLECSRenRVEGPWLVMKVSDTGQGIPPEQLAHIFDMYYKApdlKGTNaiGSGIGLAVT 472
Cdd:cd16915 4 IVGNLIDNALDAlaaTGAPNKQVEVFL--RDEGDDLVIEVRDTGPGIAPELRDKVFERGVST---KGQG--ERGIGLALV 76
|
90 100
....*....|....*....|....*...
gi 746446453 473 KALVSAMKGIITVNSTEGEGSCFTVQIP 500
Cdd:cd16915 77 RQSVERLGGSITVESEPGGGTTFSIRIP 104
|
|
| HATPase_BasS-like |
cd16940 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
383-498 |
7.93e-17 |
|
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: 77.06 E-value: 7.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 383 DIYAQLDPTRLRQVVWNLINNAVKFTQQGKVtLECSRENRVEGpwlVMKVSDTGQGIPPEQLAHIFDMYYKAPdlkGTNA 462
Cdd:cd16940 4 DIQVQGDALLLFLLLRNLVDNAVRYSPQGSR-VEIKLSADDGA---VIRVEDNGPGIDEEELEALFERFYRSD---GQNY 76
|
90 100 110
....*....|....*....|....*....|....*.
gi 746446453 463 IGSGIGLAVTKALVSAMKGIITVNSTEGEGSCFTVQ 498
Cdd:cd16940 77 GGSGLGLSIVKRIVELHGGQIFLGNAQGGGLEAWVR 112
|
|
| HATPase_BaeS-like |
cd16946 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
389-500 |
1.02e-16 |
|
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: 76.35 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 389 DPTRLRQVVWNLINNAVKFTQQG-KVTLECSRENRVegpwLVMKVSDTGQGIPPEQLAHIFDMYYKAPDLKGTNAIGSGI 467
Cdd:cd16946 1 DRDRLQQLFVNLLENSLRYTDTGgKLRIRAAQTPQE----VRLDVEDSAPGVSDDQLARLFERFYRVESSRNRASGGSGL 76
|
90 100 110
....*....|....*....|....*....|...
gi 746446453 468 GLAVTKALVSAMKGIITVNSTEGEGSCFTVQIP 500
Cdd:cd16946 77 GLAICHNIALAHGGTISAEHSPLGGLRLVLTLP 109
|
|
| HATPase_AtoS-like |
cd16943 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
390-501 |
3.34e-16 |
|
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: 74.77 E-value: 3.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 390 PTRLRQVVWNLINNAVK-FTQQGKVTLECSRENRVegpwLVMKVSDTGQGIPPEQLAHIFDMYYKA-PDLKGTnaigsGI 467
Cdd:cd16943 1 PSQLNQVLLNLLVNAAQaMEGRGRITIRTWAHVDQ----VLIEVEDTGSGIDPEILGRIFDPFFTTkPVGEGT-----GL 71
|
90 100 110
....*....|....*....|....*....|....
gi 746446453 468 GLAVTKALVSAMKGIITVNSTEGEGSCFTVQIPL 501
Cdd:cd16943 72 GLSLSYRIIQKHGGTIRVASVPGGGTRFTIILPI 105
|
|
| PEP_his_kin |
TIGR02916 |
putative PEP-CTERM system histidine kinase; Members of this protein family have a novel ... |
262-500 |
3.51e-16 |
|
putative PEP-CTERM system histidine kinase; Members of this protein family have a novel N-terminal domain, a single predicted membrane-spanning helix, and a predicted cystosolic histidine kinase domain. We designate this protein PrsK, and its companion DNA-binding response regulator protein (TIGR02915) PrsR. These predicted signal-transducing proteins appear to enable enhancer-dependent transcriptional activation. The prsK gene is often associated with exopolysaccharide biosynthesis genes. [Protein fate, Protein and peptide secretion and trafficking, Signal transduction, Two-component systems]
Pssm-ID: 274349 [Multi-domain] Cd Length: 679 Bit Score: 82.85 E-value: 3.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 262 SRKEAAQALETAYKDK--GKFIATLSHELRtplNGIVGLTRMLLDTDLNKQQRSWGNTIFssaETLGNIFNDIIDL-DKI 338
Cdd:TIGR02916 458 AQMEASEALAEARQFEafNRMSAFVVHDLK---NLVAQLSLLLRNAERHKDNPEFQDDML---ETVENAVNRMKKLlAQL 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 339 DRDQLDIVTNSINVSDFINDVVNFAGLIAEQKELEFDIkrngvlDIYAQLDPTRLRQVVWNLINNAVKFTQQ-GKVTLEC 417
Cdd:TIGR02916 532 RSKGLEEEKLCVDLVDLLRRAIASKRAQGPRPEVSIDT------DLSVRADRERLERVLGHLVQNALEATPGeGRVAIRV 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 418 SREnrveGPWLVMKVSDTGQGIPPEQL-AHIFDMYykapdlKGTNAIGSGIGLAVTKALVSAMKGIITVNSTEGEGSCFT 496
Cdd:TIGR02916 606 ERE----CGAARIEIEDSGCGMSPAFIrERLFKPF------DTTKGAGMGIGVYECRQYVEEIGGRIEVESTPGQGTIFT 675
|
....
gi 746446453 497 VQIP 500
Cdd:TIGR02916 676 LVLP 679
|
|
| HisKA |
pfam00512 |
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ... |
277-339 |
6.37e-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: 6.37e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 746446453 277 KGKFIATLSHELRTPLNGIVGLTRMLLDTDLNKQQRSWGNTIFSSAETLGNIFNDIIDLDKID 339
Cdd:pfam00512 2 KSEFLANLSHELRTPLTAIRGYLELLRDEKLDEEQREYLETILRSAERLLRLINDLLDLSRIE 64
|
|
| HATPase_YcbM-like |
cd16947 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
384-499 |
1.11e-15 |
|
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis YcbM; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Bacillus subtilis YcbM, a HK of the two-component system YcbM-YcbL. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA).
Pssm-ID: 340423 [Multi-domain] Cd Length: 125 Bit Score: 74.09 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 384 IYAQLDPTRLRQVVWNLINNAVKFTQQGK---VTLECSRENrvegpwLVMKVSDTGQGIPPEQLAHIFDMYYKAPDLKGT 460
Cdd:cd16947 12 IYANANTEALQRILKNLISNAIKYGSDGKflgMTLREDEKH------VYIDIWDKGKGISETEKDHVFERLYTLEDSRNS 85
|
90 100 110
....*....|....*....|....*....|....*....
gi 746446453 461 NAIGSGIGLAVTKALVSAMKGIITVNSTEGEGSCFTVQI 499
Cdd:cd16947 86 AKQGNGLGLTITKRLAESMGGSIYVNSKPYEKTVFTVTL 124
|
|
| HATPase_FilI-like |
cd16921 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
393-500 |
1.35e-15 |
|
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: 73.13 E-value: 1.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 393 LRQVVWNLINNAVKFTQQG---KVTLECSRenrVEGPWlVMKVSDTGQGIPPEQLAHIFDMYYKapdLKGTNAI-GSGIG 468
Cdd:cd16921 1 LGQVLTNLLGNAIKFRRPRrppRIEVGAED---VGEEW-TFYVRDNGIGIDPEYAEKVFGIFQR---LHSREEYeGTGVG 73
|
90 100 110
....*....|....*....|....*....|..
gi 746446453 469 LAVTKALVSAMKGIITVNSTEGEGSCFTVQIP 500
Cdd:cd16921 74 LAIVRKIIERHGGRIWLESEPGEGTTFYFTLP 105
|
|
| HATPase_EnvZ-like |
cd16950 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
393-500 |
1.98e-15 |
|
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: 72.48 E-value: 1.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 393 LRQVVWNLINNAVKFTQqgkvtLECSRENRVEGPWLVMKVSDTGQGIPPEQLAHIFDMYYKAPDLKGTNaiGSGIGLAVT 472
Cdd:cd16950 1 LKRVLSNLVDNALRYGG-----GWVEVSSDGEGNRTRIQVLDNGPGIAPEEVDELFQPFYRGDNARGTS--GTGLGLAIV 73
|
90 100
....*....|....*....|....*...
gi 746446453 473 KALVSAMKGIITVNSTEGEGSCFTVQIP 500
Cdd:cd16950 74 QRISDAHGGSLTLANRAGGGLCARIELP 101
|
|
| HisKA |
smart00388 |
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ... |
277-339 |
4.19e-15 |
|
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine kinases.
Pssm-ID: 214644 [Multi-domain] Cd Length: 66 Bit Score: 70.29 E-value: 4.19e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 746446453 277 KGKFIATLSHELRTPLNGIVGLTRMLLDTDLNKQQRSWGNTIFSSAETLGNIFNDIIDLDKID 339
Cdd:smart00388 2 KREFLANLSHELRTPLTAIRGYLELLLDTELSEEQREYLETILREAERLLRLINDLLDLSRIE 64
|
|
| MtrAB_MtrB |
NF040691 |
MtrAB system histidine kinase MtrB; |
279-500 |
5.20e-15 |
|
MtrAB system histidine kinase MtrB;
Pssm-ID: 468655 [Multi-domain] Cd Length: 507 Bit Score: 78.53 E-value: 5.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 279 KFIATLSHELRTPLNGIvgltRMLLDT------DLNKQQRswgntifSSAETLGN-------IFNDIIDLDKIDRDQLDI 345
Cdd:NF040691 273 RFVSDVSHELRTPLTTI----RMAADVihdsrdDFDPATA-------RSAELLHTeldrfesLLSDLLEISRFDAGAAEL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 346 VTNSINVSDFINDVVNFAGLIAEQKELEFDIKRNGVlDIYAQLDPTRLRQVVWNLINNAVKFTQQGKVTLEC-SRENRVe 424
Cdd:NF040691 342 DVEPVDLRPLVRRVVDALRQLAERAGVELRVDAPGT-PVVAEVDPRRVERVLRNLVVNAIEHGEGKPVVVTVaQDDTAV- 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 746446453 425 gpwlVMKVSDTGQGIPPEQLAHIFDMYYKAPDLKGTNAIGSGIGLAVtkALVSAM--KGIITVNSTEGEGSCFTVQIP 500
Cdd:NF040691 420 ----AVTVRDHGVGLKPGEVALVFDRFWRADPARARTTGGTGLGLAI--ALEDARlhGGWLEAWGRPGQGSQFRLTLP 491
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
153-270 |
6.13e-15 |
|
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions]
Pssm-ID: 272971 [Multi-domain] Cd Length: 124 Bit Score: 71.94 E-value: 6.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 153 RSIVDSSPDLFYYRDNNGVFAGCNKMFEEVMGKSSSELIGKTVEQIFPSHFLS---EVLKTDKEVEQShkaltiDVGYEV 229
Cdd:TIGR00229 6 RAIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREevrERIERRLEGEPE------PVSEER 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 746446453 230 -----NGETRWFELRKLPfINDEGDYIGLLGFGRDITSRKEAAQAL 270
Cdd:TIGR00229 80 rvrrkDGSEIWVEVSVSP-IRTNGGELGVVGIVRDITERKEAEEAL 124
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
519-626 |
8.69e-15 |
|
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: 73.02 E-value: 8.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 519 ILLVEDVPLNAEIATNLLEQRGHEVLWAETGEDALSFVETEDdldlvlldMQLPDINGDVVAKQIRSDSHFDKLPIVALT 598
Cdd:COG3706 4 ILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHRpdli-lldLEMPDMDGLELCRRLRADPRTADIPIIFLT 82
|
90 100 110
....*....|....*....|....*....|.
gi 746446453 599 ANvRSAEEELEGISiQGA---LAKPINTVKL 626
Cdd:COG3706 83 AL-DDEEDRARALE-AGAddyLTKPFDPEEL 111
|
|
| envZ |
PRK09467 |
osmolarity sensor protein; Provisional |
281-502 |
1.31e-14 |
|
osmolarity sensor protein; Provisional
Pssm-ID: 236531 [Multi-domain] Cd Length: 435 Bit Score: 76.87 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 281 IATLSHELRTPLngivglTRMLLDTDLNKQQRSW-GNTIFSSAETLGNIFNDIIDLDKIDRDQldiVTNSINVSDFINDV 359
Cdd:PRK09467 233 MAGVSHDLRTPL------TRIRLATEMMSEEDGYlAESINKDIEECNAIIEQFIDYLRTGQEM---PMEMADLNALLGEV 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 360 VNfagliAE---QKELEFDIKrNGVLDIYAQldPTRLRQVVWNLINNAVKFTQqGKVTLECsrenRVEGPWLVMKVSDTG 436
Cdd:PRK09467 304 IA-----AEsgyEREIETALQ-PGPIEVPMN--PIAIKRALANLVVNAARYGN-GWIKVSS----GTEGKRAWFQVEDDG 370
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 437 QGIPPEQLAHIFDmyykaPDLKGTNA---IGSGIGLAVTKALVSAMKGIITV-NSTEGeGSCFTVQIPLS 502
Cdd:PRK09467 371 PGIPPEQLKHLFQ-----PFTRGDSArgsSGTGLGLAIVKRIVDQHNGKVELgNSEEG-GLSARAWLPLT 434
|
|
| PRK10549 |
PRK10549 |
two-component system sensor histidine kinase BaeS; |
267-501 |
2.74e-14 |
|
two-component system sensor histidine kinase BaeS;
Pssm-ID: 182539 [Multi-domain] Cd Length: 466 Bit Score: 75.83 E-value: 2.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 267 AQALETAYKDKGKFIATLSHELRTPLNGIVGLTRMLLDtDLNKQQRSWGNTIFSSAETLGNIFNDIIDLDKIDRDQLDIV 346
Cdd:PRK10549 230 ASTLEKNEQMRRDFMADISHELRTPLAVLRGELEAIQD-GVRKFTPESVASLQAEVGTLTKLVDDLHQLSLSDEGALAYR 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 347 TNSINVSDFINDVV-NFAGLIAeQKELEFDIKRNGVLDIYAqlDPTRLRQVVWNLINNAVKFT-QQGKVTLE-CSRENRv 423
Cdd:PRK10549 309 KTPVDLVPLLEVAGgAFRERFA-SRGLTLQLSLPDSATVFG--DPDRLMQLFNNLLENSLRYTdSGGSLHISaEQRDKT- 384
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 746446453 424 egpwLVMKVSDTGQGIPPEQLAHIFDMYYKAPDLKGTNAIGSGIGLAVTKALVSAMKGIITVNSTEGEGSCFTVQIPL 501
Cdd:PRK10549 385 ----LRLTFADSAPGVSDEQLQKLFERFYRTEGSRNRASGGSGLGLAICLNIVEAHNGRIIAAHSPFGGVSITVELPL 458
|
|
| HATPase_BvrS-ChvG-like |
cd16953 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
393-500 |
4.13e-14 |
|
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: 69.14 E-value: 4.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 393 LRQVVWNLINNAVKFTQQGKVTLECSRENrvEGPWLVMKVSDTGQGIPPEQLAHIFDMYYK---APDLKGTNaigSGIGL 469
Cdd:cd16953 1 LGQVLRNLIGNAISFSPPDTGRITVSAMP--TGKMVTISVEDEGPGIPQEKLESIFDRFYTerpANEAFGQH---SGLGL 75
|
90 100 110
....*....|....*....|....*....|....*
gi 746446453 470 AVTKALVSAMKGIITVNSTE----GEGSCFTVQIP 500
Cdd:cd16953 76 SISRQIIEAHGGISVAENHNqpgqVIGARFTVQLP 110
|
|
| HATPase_EcPhoR-like |
cd16952 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
393-503 |
6.06e-14 |
|
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: 68.38 E-value: 6.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 393 LRQVVWNLINNAVKFT-QQGKVTLECSRENrvEGPWLvmKVSDTGQGIPPEQLAHIFDMYYKAPDLKGTNAIGSGIGLAV 471
Cdd:cd16952 1 LRSAFSNLVSNAVKYTpPSDTITVRWSQEE--SGARL--SVEDTGPGIPPEHIPRLTERFYRVDIERCRNTGGTGLGLAI 76
|
90 100 110
....*....|....*....|....*....|..
gi 746446453 472 TKALVSAMKGIITVNSTEGEGSCFTVQIPLSL 503
Cdd:cd16952 77 VKHVMSRHDARLLIASELGKGSRFTCLFPSSR 108
|
|
| OmpR |
COG0745 |
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ... |
519-626 |
9.62e-14 |
|
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain [Signal transduction mechanisms, Transcription];
Pssm-ID: 440508 [Multi-domain] Cd Length: 204 Bit Score: 70.76 E-value: 9.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 519 ILLVEDVPLNAEIATNLLEQRGHEVLWAETGEDALSFVETEddldlvllD-------MQLPDINGDVVAKQIRSDSHfdK 591
Cdd:COG0745 4 ILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEE--------RpdlilldLMLPGMDGLEVCRRLRARPS--D 73
|
90 100 110
....*....|....*....|....*....|....*...
gi 746446453 592 LPIVALTANVrSAEEELEGISIqGA---LAKPINTVKL 626
Cdd:COG0745 74 IPIIMLTARD-DEEDRVRGLEA-GAddyLTKPFDPEEL 109
|
|
| PRK10604 |
PRK10604 |
sensor protein RstB; Provisional |
277-507 |
1.24e-13 |
|
sensor protein RstB; Provisional
Pssm-ID: 236724 [Multi-domain] Cd Length: 433 Bit Score: 73.87 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 277 KGKFIATLSHELRTPLngiVGLT-RMLLDTDLNKQQRSWGNTIFSSAETLgniFNDIIDLDKIDRDQLDIVTNSINVSDF 355
Cdd:PRK10604 212 KKQLIDGIAHELRTPL---VRLRyRLEMSDNLSAAESQALNRDIGQLEAL---IEELLTYARLDRPQNELHLSEPDLPAW 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 356 INDVVNFAGLIAEQKELEFDIKRNGvldIYAQLDPTRLRQVVWNLINNAVKFTQQgKVTLECSREnrveGPWLVMKVSDT 435
Cdd:PRK10604 286 LSTHLADIQAVTPEKTVRLDTPHQG---DYGALDMRLMERVLDNLLNNALRYAHS-RVRVSLLLD----GNQACLIVEDD 357
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 746446453 436 GQGIPPEQLAHIFDMYYKAPDLKGTNAIGSGIGLAVTKALVSAMKGIITVNSTEGEGSCFTVQIPLSLCVAP 507
Cdd:PRK10604 358 GPGIPPEERERVFEPFVRLDPSRDRATGGCGLGLAIVHSIALAMGGSVNCDESELGGARFSFSWPVWHNLPQ 429
|
|
| HATPase_TmoS-FixL-DctS-like |
cd16920 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
393-500 |
1.39e-13 |
|
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: 67.42 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 393 LRQVVWNLINNAVKFTQQGKVTlecSRE-----NRVEGPWLVMKVSDTGQGIPPEQLAHIFDMYYKapdlkgTNAIGSGI 467
Cdd:cd16920 1 IQQVLINLVRNGIEAMSEGGCE---RREltirtSPADDRAVTISVKDTGPGIAEEVAGQLFDPFYT------TKSEGLGM 71
|
90 100 110
....*....|....*....|....*....|...
gi 746446453 468 GLAVTKALVSAMKGIITVNSTEGEGSCFTVQIP 500
Cdd:cd16920 72 GLSICRSIIEAHGGRLSVESPAGGGATFQFTLP 104
|
|
| PRK10490 |
PRK10490 |
sensor protein KdpD; Provisional |
281-501 |
3.92e-13 |
|
sensor protein KdpD; Provisional
Pssm-ID: 236701 [Multi-domain] Cd Length: 895 Bit Score: 73.15 E-value: 3.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 281 IATLSHELRTPLNGIVGLTRMLLdTDLNKQQRSW---GNTIFSSAETLGNIFNDIIDLDKIDRD--QLDIVTNSINvsdf 355
Cdd:PRK10490 668 LAALSHDLRTPLTVLFGQAEILT-LDLASEGSPHarqASEIRQQVLNTTRLVNNLLDMARIQSGgfNLRKEWLTLE---- 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 356 inDVVNFAgliaeQKELEFDIKRNGV-LDIYAQL-----DPTRLRQVVWNLINNAVKFT-QQGKVTLECsrenRVEGPWL 428
Cdd:PRK10490 743 --EVVGSA-----LQMLEPGLSGHPInLSLPEPLtlihvDGPLFERVLINLLENAVKYAgAQAEIGIDA----HVEGERL 811
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 746446453 429 VMKVSDTGQGIPPEQLAHIFDMYYKApdLKGTNAIGSGIGLAVTKALVSAMKGIITVNSTEGEGSCFTVQIPL 501
Cdd:PRK10490 812 QLDVWDNGPGIPPGQEQLIFDKFARG--NKESAIPGVGLGLAICRAIVEVHGGTIWAENRPEGGACFRVTLPL 882
|
|
| RpfG |
COG3437 |
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ... |
519-640 |
4.50e-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: 69.42 E-value: 4.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 519 ILLVEDVPLNAEIATNLLEQRGHEVLWAETGEDALSFVETEDdldlvlldMQLPDINGDVVAKQIRSDSHFDKLPIVALT 598
Cdd:COG3437 9 VLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAPpdli-lldVRMPGMDGFELLRLLRADPSTRDIPVIFLT 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 746446453 599 ANVrSAEEELEGISiQGA---LAKPINTVKLDKMLADLFGIKQSE 640
Cdd:COG3437 88 ALA-DPEDRERALE-AGAddyLTKPFDPEELLARVRNALELRRLQ 130
|
|
| HATPase_CpxA-like |
cd16949 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
399-501 |
4.88e-13 |
|
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: 65.81 E-value: 4.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 399 NLINNAVKFTQQgKVTLECSRENRvegpWLVMKVSDTGQGIPPEQLAHIFDMYYKAPDLKGTNAIGSGIGLAVTKALVSA 478
Cdd:cd16949 7 NVLRNALRYSPS-KILLDISQDGD----QWTITITDDGPGVPEDQLEQIFLPFYRVDSARDRESGGTGLGLAIAERAIEQ 81
|
90 100
....*....|....*....|...
gi 746446453 479 MKGIITVNSTEGEGSCFTVQIPL 501
Cdd:cd16949 82 HGGKIKASNRKPGGLRVRIWLPA 104
|
|
| REC_D1_PleD-like |
cd17538 |
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ... |
519-621 |
5.08e-13 |
|
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar domains; PleD contains a REC domain (D1) with the phosphorylatable aspartate, a REC-like adaptor domain (D2), and the enzymatic diguanylate cyclase (DGC) domain, also called the GGDEF domain according to a conserved sequence motif, as its output domain. The GGDEF-containing PleD response regulators are global regulators of cell metabolism in some important human pathogens. This model describes D1 of PleD and similar domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381093 [Multi-domain] Cd Length: 104 Bit Score: 65.60 E-value: 5.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 519 ILLVEDVPLNAEIATNLLEQRGHEVLWAETGEDALSFVETEDDLDLVLLDMqLPDINGDVVAKQIRSDSHFDKLPIVALT 598
Cdd:cd17538 2 ILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELPDLILLDVM-MPGMDGFEVCRRLKEDPETRHIPVIMIT 80
|
90 100
....*....|....*....|....*.
gi 746446453 599 AnVRSAEEELEGISIqGA---LAKPI 621
Cdd:cd17538 81 A-LDDREDRIRGLEA-GAddfLSKPI 104
|
|
| PRK11086 |
PRK11086 |
sensory histidine kinase DcuS; Provisional |
177-500 |
5.31e-13 |
|
sensory histidine kinase DcuS; Provisional
Pssm-ID: 236839 [Multi-domain] Cd Length: 542 Bit Score: 72.25 E-value: 5.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 177 KMFEEVMGKSSsELIGKTVEQIFPSHFLSEVLKTdKEVEQshkaltiDVGYEVNGETRWFElrKLPFINDeGDYIGLLGF 256
Cdd:PRK11086 252 RLFNYKKGLED-DPLGTDVESWMPVSRLKEVLRT-GTPRR-------DEEININGRLLLTN--TVPVRVN-GEIIGAIAT 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 257 GRDITSRKEAAQALeTAYKDKGKFIATLSHELRTPLNGIVGLTRMlldtdlnKQQRSWGNTIFSSA----ETLGNIFNDI 332
Cdd:PRK11086 320 FRDKTEVRQLAQRL-DGMVNYADALRAQSHEFMNKLHVILGLLHL-------KSYDQLEDYILKTAnnyqEEIGSLLGKI 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 333 ID-------LDKIDRDQLDIVTNSINVSDFINDVVNfagliaEQKELEfdikrngvldiyaqldptrLRQVVWNLINN-- 403
Cdd:PRK11086 392 KSpviagflLGKISRARELGITLIISEDSQLPDSGD------EDQVHE-------------------LITILGNLIENal 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 404 -AVKFTQQGKVTLECSRENRvegpWLVMKVSDTGQGIPPEQLAHIFDMYYKApdlKGTNaigSGIGLAVTKALVSAMKGI 482
Cdd:PRK11086 447 eAVGGEEGGEISVSLHYRNG----WLHCEVSDDGPGIAPDEIDAIFDKGYST---KGSN---RGVGLYLVKQSVENLGGS 516
|
330
....*....|....*...
gi 746446453 483 ITVNSTEGEGSCFTVQIP 500
Cdd:PRK11086 517 IAVESEPGVGTQFFVQIP 534
|
|
| PRK11100 |
PRK11100 |
sensory histidine kinase CreC; Provisional |
267-502 |
6.24e-13 |
|
sensory histidine kinase CreC; Provisional
Pssm-ID: 236846 [Multi-domain] Cd Length: 475 Bit Score: 71.80 E-value: 6.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 267 AQALETAyKDK--GK-----FIATLSHELRTPLNGIVGLTRmLLDTDL--NKQQRSWGNtIFSSAETLGNIFNDIIDLDK 337
Cdd:PRK11100 240 AQALESM-RVKleGKayveqYVQTLTHELKSPLAAIRGAAE-LLQEDPppEDRARFTGN-ILTQSARLQQLIDRLLELAR 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 338 ID-RDQLDIVTNsINVSDFINDVVNFAGLIAEQKELEFDIkrnGVLDIYAQLDPTRLRQVVWNLINNAVKFT-QQGKVTL 415
Cdd:PRK11100 317 LEqRQELEVLEP-VALAALLEELVEAREAQAAAKGITLRL---RPDDARVLGDPFLLRQALGNLLDNAIDFSpEGGTITL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 416 ECSRENrvEGPWLVmkVSDTGQGIPPEQLAHIFDMYYKAPDlKGTNAIGSGIGLAVTKALVSAMKGIITVNSTEGEGSCF 495
Cdd:PRK11100 393 SAEVDG--EQVALS--VEDQGPGIPDYALPRIFERFYSLPR-PANGRKSTGLGLAFVREVARLHGGEVTLRNRPEGGVLA 467
|
....*..
gi 746446453 496 TVQIPLS 502
Cdd:PRK11100 468 TLTLPRH 474
|
|
| HPtr |
COG2198 |
HPt (histidine-containing phosphotransfer) domain [Signal transduction mechanisms]; |
25-771 |
1.10e-12 |
|
HPt (histidine-containing phosphotransfer) domain [Signal transduction mechanisms];
Pssm-ID: 441800 [Multi-domain] Cd Length: 871 Bit Score: 71.62 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 25 TAAICYTLFLTVSLILSSMFYYVAIGELHLVDILAVVFFTAVVSPLIISVLLNSIRQLDASYAYLDSATKQEKLLNQTLK 104
Cdd:COG2198 126 LLLLLLLALLLLLLLLLALLLLLLLLLVLAALLLLLLLALLLALLLLVLLVLLLLLLLLLLLLLLLLLLLLLLLLALTLA 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 105 DNINRLNIEIDERKMAFHAKHRAIEELRREIAERKKTQQELAQQSMLQRSIVDSSPDLFYYRDNNGVFAGCNKMFEEVMG 184
Cdd:COG2198 206 ALLELLAAELALEALLAELAAEAAAALAAELALAELAALLLLLLLLLLLLILLLLLLLLLLLLLLLLLLLLLLLLLLLLL 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 185 KSSSELIGKTVEQIFPSHFLSEVLKTDKEVEQSHKALTIDVGYEVNGETRWFELRKLPFINDEGDYIGLLGFGRDITSRK 264
Cdd:COG2198 286 LLLLLLLLLLLLLLELLLLLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLLLALLLALLLAAA 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 265 EAAQALETAyKDKGKFIATLSHELRTPLNGIVGLTRMLLDTDLNKQQRSWGNTIFSSAETLGNIFNDIIDLDKIDRDQLD 344
Cdd:COG2198 366 AALAAALEA-LLTELALILLLLLLLLLLLILLGLLLLLLLSLLLSLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLGLLL 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 345 IVTNSINVSDFINDVVNFAGLIAEQKELEFDIKRNGVLDIYAQLDPTRLRQVVWNLINNAVKFTQQGKVTLECSRENRVE 424
Cdd:COG2198 445 LLLLLLGLLLLLLLGLLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVAAALAALALLLLLALLL 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 425 GPWLVMKVSDTGQGIPPEQLAHIFDMY--YKAPDLKGTNAIGSGIGLAVTKALVSAMKGIITVNSTEGEGSCFTVQIPLS 502
Cdd:COG2198 525 LLLLDLLILGLLLILLLLLLGLLALGLaaLLLLLALLLGLGLLLGLLLGGLLLLLLLLLLLLLLLLLLLLLLLLLLALLL 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 503 LCVAPTEQSYVGRGLYILLVEDVPLNAEIATNLLEQRGHEVLWAETGEDALSFVETEDDLDLVLLDMQLPDINGDVVAKQ 582
Cdd:COG2198 605 ALLAAAAALLLLLLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAVLLAAAAAAAALAALDLLLDLDDMMMMLDDM 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 583 IRSDSHFDKLPIVALTANVRSAEEELEGISIQGALAKPINTVKLDKMLADLFGIKQSECTEPLLKVSEEALKGIDAHLLD 662
Cdd:COG2198 685 MAEAARARALAARAAAIAAAAAAAAAAAAAAAAAAAALLAALLLLLLLLLLLLLLLLLLLLAAAAAAAASPAAPALPVLD 764
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 663 IETIEDFVNSMGLvvFRRSSQLFEKLSPQYQQELLTSLNTGDREEYESVAHKLKGAAGSVGLNDVQLHAKIMEHGAIDES 742
Cdd:COG2198 765 LEALRRLGGDPEL--LRELLELFLEELPELLAELRQALAAGDLEALARLAHKLKGSAGNLGAPRLAELAAELEQAARAGD 842
|
730 740
....*....|....*....|....*....
gi 746446453 743 DEVLKQWLDILADKINEGQKALHLFLQQL 771
Cdd:COG2198 843 LEEAEELLAELEAELERVLAALEALLAEE 871
|
|
| HATPase_RstB-like |
cd16939 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
393-501 |
4.26e-12 |
|
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: 63.22 E-value: 4.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 393 LRQVVWNLINNAVKFTQQgkvTLECSRenRVEGPWLVMKVSDTGQGIPPEQLAHIFDMYYKAPDLKGTNAIGSGIGLAVT 472
Cdd:cd16939 1 MARALDNLLRNALRYAHR---TVRIAL--LVSGGRLTLIVEDDGPGIPAAARERVFEPFVRLDPSRDRATGGFGLGLAIV 75
|
90 100
....*....|....*....|....*....
gi 746446453 473 KALVSAMKGIITVNSTEGEGSCFTVQIPL 501
Cdd:cd16939 76 HRVALWHGGHVECDDSELGGACFRLTWPR 104
|
|
| PRK13560 |
PRK13560 |
hypothetical protein; Provisional |
134-270 |
7.27e-12 |
|
hypothetical protein; Provisional
Pssm-ID: 106506 [Multi-domain] Cd Length: 807 Bit Score: 68.93 E-value: 7.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 134 EIAERKKTQQELAQQSMLQRSIVDSSPDLFYYRDNNGVFAGCNKMFEEVMGKSSSELIGKTVEQIFPSHFLSEVLKTDKE 213
Cdd:PRK13560 188 DITERKRAEERIDEALHFLQQLLDNIADPAFWKDEDAKVFGCNDAACLACGFRREEIIGMSIHDFAPAQPADDYQEADAA 267
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 214 VEQSHKALTIDVGYEV-NGETRWFELR--KLPFINDEGDYIGLLGFGRDITSRKEAAQAL 270
Cdd:PRK13560 268 KFDADGSQIIEAEFQNkDGRTRPVDVIfnHAEFDDKENHCAGLVGAITDISGRRAAEREL 327
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
153-260 |
7.42e-12 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 395786 [Multi-domain] Cd Length: 113 Bit Score: 62.82 E-value: 7.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 153 RSIVDSSPDLFYYRDNNGVFAGCNKMFEEVMGKSSSELIGKT-VEQIFPSHFLSEVLKTDKEVEQSHKALTIDVGYEV-N 230
Cdd:pfam00989 4 RAILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSlLDLIPEEDDAEVAELLRQALLQGEESRGFEVSFRVpD 83
|
90 100 110
....*....|....*....|....*....|
gi 746446453 231 GETRWFELRKLPFINDEGDYIGLLGFGRDI 260
Cdd:pfam00989 84 GRPRHVEVRASPVRDAGGEILGFLGVLRDI 113
|
|
| HATPase_NtrY-like |
cd16944 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
389-500 |
1.14e-11 |
|
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: 62.17 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 389 DPTRLRQVVWNLINNAVKFTQ-------QGKVTLECSRENRvegpwLVMKVSDTGQGIPPEQLAHIFDMYYKapdlkgTN 461
Cdd:cd16944 1 DTTQISQVLTNILKNAAEAIEgrpsdvgEVRIRVEADQDGR-----IVLIVCDNGKGFPREMRHRATEPYVT------TR 69
|
90 100 110
....*....|....*....|....*....|....*....
gi 746446453 462 AIGSGIGLAVTKALVSAMKGIITVNSTEGEGSCFTVQIP 500
Cdd:cd16944 70 PKGTGLGLAIVKKIMEEHGGRISLSNREAGGACIRIILP 108
|
|
| REC_2_DhkD-like |
cd17580 |
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ... |
519-630 |
2.67e-11 |
|
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: 60.93 E-value: 2.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 519 ILLVEDVPLNAEIATNLLEQRGHEVLWAETGEDALSFVETeddldlvlldmQLPDI----------NGDVVAKQIRSDSH 588
Cdd:cd17580 1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQR-----------FRPDVilsdigmpgmDGYELARRLRELPW 69
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 746446453 589 FDKLPIVALTANVRsaEEELEGISIQG---ALAKPINTVKLDKML 630
Cdd:cd17580 70 LANTPAIALTGYGQ--PEDRERALEAGfdaHLVKPVDPDELIELI 112
|
|
| RocR |
COG3829 |
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ... |
142-297 |
4.18e-11 |
|
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis domains [Transcription, Signal transduction mechanisms];
Pssm-ID: 443041 [Multi-domain] Cd Length: 448 Bit Score: 65.95 E-value: 4.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 142 QQELAQQSMLQRSIVDSSPDLFYYRDNNGVFAGCNKMFEEVMGKSSSELIGKTVEQIFPSHFLSEVLKTDKEVeqshkal 221
Cdd:COG3829 3 ELELKELEEELEAILDSLDDGIIVVDADGRITYVNRAAERILGLPREEVIGKNVTELIPNSPLLEVLKTGKPV------- 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 746446453 222 tIDVGYEVNGETRWFELRKLPfINDEGDYIGLLGFGRDITSRKEAAQALETAYKDKGkfiatlsHELRTPLNGIVG 297
Cdd:COG3829 76 -TGVIQKTGGKGKTVIVTAIP-IFEDGEVIGAVETFRDITELKRLERKLREEELERG-------LSAKYTFDDIIG 142
|
|
| PRK10618 |
PRK10618 |
phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional |
284-511 |
4.47e-11 |
|
phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional
Pssm-ID: 236726 [Multi-domain] Cd Length: 894 Bit Score: 66.49 E-value: 4.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 284 LSHELRTPLNGIVGLTRMLLDTDLNKQQRSWGNTIFSSAETLGNIFNDIIDLDKIDRDQLDIVTNSINVSDFINDVVnfa 363
Cdd:PRK10618 457 IGDELKQPLQSLAQLAAQLRQTSDEEQQQPELDQLAEQSDVLVRLVDNIQLLNMLETQDWKPEQELFSLQDLIDEVL--- 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 364 gliaeqKELEFDIKRNGV-LDIYAQLDPTR--------LRQVVWNLINNAVKFTQQGKVTLECSRENRVEGPwLVMKVSD 434
Cdd:PRK10618 534 ------PEVLPAIKRKGLqLLIHNHLKAEQlrigdrdaLRKILLLLLNYAITTTAYGKITLEVDQDESSPDR-LTIRILD 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 435 TGQGIPPEQLAHI---------FDMYYKApdlkgtnaigSGIGLAVTKALVSAMKGIITVNSTEGEGSCFTVQIPLSLCV 505
Cdd:PRK10618 607 TGAGVSIKELDNLhfpflnqtqGDRYGKA----------SGLTFFLCNQLCRKLGGHLTIKSREGLGTRYSIHLKMLAAD 676
|
....*.
gi 746446453 506 APTEQS 511
Cdd:PRK10618 677 PEVEEE 682
|
|
| Response_reg |
pfam00072 |
Response regulator receiver domain; This domain receives the signal from the sensor partner in ... |
519-631 |
7.05e-11 |
|
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: 59.86 E-value: 7.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 519 ILLVEDVPLNAEIATNLLEQRGHEVLWAETGEDALSFVETEdDLDLVLLDMQLPDINGDVVAKQIRsdSHFDKLPIVALT 598
Cdd:pfam00072 1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEE-RPDLILLDINMPGMDGLELLKRIR--RRDPTTPVIILT 77
|
90 100 110
....*....|....*....|....*....|....
gi 746446453 599 ANVRSAE-EELEGISIQGALAKPINTVKLDKMLA 631
Cdd:pfam00072 78 AHGDEDDaVEALEAGADDFLSKPFDPDELLAAIR 111
|
|
| HATPase_HupT_MifS-like |
cd16976 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
393-499 |
9.19e-11 |
|
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: 59.39 E-value: 9.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 393 LRQVVWNLINNA---VKFTQQGKVTLECSRENrveGPWlVMKVSDTGQGIPPEQLAHIFDMYYKAPDL-KGTnaigsGIG 468
Cdd:cd16976 1 IQQVLMNLLQNAldaMGKVENPRIRIAARRLG---GRL-VLVVRDNGPGIAEEHLSRVFDPFFTTKPVgKGT-----GLG 71
|
90 100 110
....*....|....*....|....*....|.
gi 746446453 469 LAVTKALVSAMKGIITVNSTEGEGSCFTVQI 499
Cdd:cd16976 72 LSISYGIVEEHGGRLSVANEEGAGARFTFDL 102
|
|
| HisKA |
cd00082 |
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ... |
277-335 |
1.53e-10 |
|
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: 57.22 E-value: 1.53e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 277 KGKFIATLSHELRTPLNGIVGLTRMLLDTDL-NKQQRSWGNTIFSSAETLGNIFNDIIDL 335
Cdd:cd00082 4 KGEFLANVSHELRTPLTAIRGALELLEEELLdDEEQREYLERIREEAERLLRLINDLLDL 63
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
175-261 |
6.05e-10 |
|
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 463873 [Multi-domain] Cd Length: 93 Bit Score: 56.70 E-value: 6.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 175 CNKMFEEVMGKSSSELIGKTVEQIFP----SHFLSEVLKTDKEVEQSHKALTIDvgyevNGETRWFELRKLPFINDEGDY 250
Cdd:pfam13426 7 VNDAALRLLGYTREELLGKSITDLFAepedSERLREALREGKAVREFEVVLYRK-----DGEPFPVLVSLAPIRDDGGEL 81
|
90
....*....|.
gi 746446453 251 IGLLGFGRDIT 261
Cdd:pfam13426 82 VGIIAILRDIT 92
|
|
| cpxA |
PRK09470 |
envelope stress sensor histidine kinase CpxA; |
285-502 |
7.33e-10 |
|
envelope stress sensor histidine kinase CpxA;
Pssm-ID: 236532 [Multi-domain] Cd Length: 461 Bit Score: 61.87 E-value: 7.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 285 SHELRTPLngivglTRMLLDTDLNKQQRSWGNT---IFSSAETLGNIFNDIIDLDkidRDQLD--IVTNSINVSDFINDV 359
Cdd:PRK09470 251 SHELRTPL------TRLQLATALLRRRQGESKElerIETEAQRLDSMINDLLVLS---RNQQKnhLERETFKANSLWSEV 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 360 VNFAGLIAEQkelefdikRNGVLDIYAQL-------DPTRLRQVVWNLINNAVKFTQQG-KVTLECSRENrvegpwLVMK 431
Cdd:PRK09470 322 LEDAKFEAEQ--------MGKSLTVSAPPgpwpingNPNALASALENIVRNALRYSHTKiEVAFSVDKDG------LTIT 387
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 746446453 432 VSDTGQGIPPEQLAHIFDMYYKAPDLKGTNAIGSGIGLAVTKALVSAMKGIITVNSTEGEGSCFTVQIPLS 502
Cdd:PRK09470 388 VDDDGPGVPEEEREQIFRPFYRVDEARDRESGGTGLGLAIVENAIQQHRGWVKAEDSPLGGLRLTIWLPLY 458
|
|
| HATPase_BceS-YxdK-YvcQ-like |
cd16948 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
393-500 |
9.65e-10 |
|
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: 56.53 E-value: 9.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 393 LRQVVWNLINNAVKFTQQ-GKVTLECSRENrvEGPWLVmkVSDTGQGIPPEQLAHIFDMYYKAPDLKGTNAiGSGIGLAV 471
Cdd:cd16948 6 LSFIIGQIVSNALKYSKQgGKIEIYSETNE--QGVVLS--IKDFGIGIPEEDLPRVFDKGFTGENGRNFQE-STGMGLYL 80
|
90 100
....*....|....*....|....*....
gi 746446453 472 TKALVSAMKGIITVNSTEGEGSCFTVQIP 500
Cdd:cd16948 81 VKKLCDKLGHKIDVESEVGEGTTFTITFP 109
|
|
| REC_OmpR_EcPhoP-like |
cd19934 |
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ... |
519-620 |
1.02e-09 |
|
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: 56.52 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 519 ILLVED-VPLNAEIATNLLEQrGHEVLWAETGEDALSFVETEdDLDLVLLDMQLPDINGDVVAKQIRSDSHfdKLPIVAL 597
Cdd:cd19934 1 LLLVEDdALLAAQLKEQLSDA-GYVVDVAEDGEEALFQGEEE-PYDLVVLDLGLPGMDGLSVLRRWRSEGR--ATPVLIL 76
|
90 100
....*....|....*....|....*..
gi 746446453 598 TAnvRSAE-EELEGISiQGA---LAKP 620
Cdd:cd19934 77 TA--RDSWqDKVEGLD-AGAddyLTKP 100
|
|
| REC |
cd00156 |
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ... |
520-620 |
1.76e-09 |
|
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: 55.31 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 520 LLVEDVPLNAEIATNLLEQRGHEVLWAETGEDALSFVETEddldlvllD-------MQLPDINGDVVAKQIRsdSHFDKL 592
Cdd:cd00156 1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREE--------RpdlvlldLMMPGMDGLELLRKLR--ELPPDI 70
|
90 100 110
....*....|....*....|....*....|.
gi 746446453 593 PIVALTANVrSAEEELEGISiQGA---LAKP 620
Cdd:cd00156 71 PVIVLTAKA-DEEDAVRALE-LGAddyLVKP 99
|
|
| REC_OmpR |
cd17574 |
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ... |
520-620 |
2.24e-09 |
|
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: 55.11 E-value: 2.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 520 LLVEDVPLNAEIATNLLEQRGHEVLWAETGEDALSFVETEDDLDLVLLDMqLPDINGDVVAKQIRSDSHfdKLPIVALTA 599
Cdd:cd17574 1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQPDLIILDVM-LPGMDGFEVCRRLREKGS--DIPIIMLTA 77
|
90 100
....*....|....*....|....*
gi 746446453 600 nvRSAEEE-LEGISIqGA---LAKP 620
Cdd:cd17574 78 --KDEEEDkVLGLEL-GAddyITKP 99
|
|
| AtoC |
COG2204 |
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ... |
519-640 |
8.31e-09 |
|
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: 58.44 E-value: 8.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 519 ILLVEDVPLNAEIATNLLEQRGHEVLWAETGEDALSFVETEddldlvllD-------MQLPDINGDVVAKQIRsdSHFDK 591
Cdd:COG2204 5 ILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREE--------PpdlvlldLRMPGMDGLELLRELR--ALDPD 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 746446453 592 LPIVALTA--NVRSAEEELEgisiQGA---LAKPINTVKLDKMLADLFGIKQSE 640
Cdd:COG2204 75 LPVILLTGygDVETAVEAIK----AGAfdyLTKPFDLEELLAAVERALERRRLR 124
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
159-260 |
1.11e-08 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.
Pssm-ID: 238075 [Multi-domain] Cd Length: 103 Bit Score: 53.41 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 159 SPDLFYYRDNNGVFAGCNKMFEEVMGKSSSELIGKTVEQIFPSHFLSEVLKTDKEVEQSHKALTIDVGYEV-NGETRWFE 237
Cdd:cd00130 1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRkDGSVIWVL 80
|
90 100
....*....|....*....|...
gi 746446453 238 LRKLPFINDEGDYIGLLGFGRDI 260
Cdd:cd00130 81 VSLTPIRDEGGEVIGLLGVVRDI 103
|
|
| HATPase_CckA-like |
cd16919 |
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ... |
393-500 |
2.81e-08 |
|
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: 52.38 E-value: 2.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 393 LRQVVWNLINNAVKFTQQ-GKVTLECSRENR-----------VEGPWLVMKVSDTGQGIPPEQLAHIFDMYYKApdlKGT 460
Cdd:cd16919 1 LELAILNLAVNARDAMPEgGRLTIETSNQRVdadyalnyrdlIPGNYVCLEVSDTGSGMPAEVLRRAFEPFFTT---KEV 77
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 746446453 461 NAiGSGIGLAVTKALVSAMKGIITVNSTEGEGSCFTVQIP 500
Cdd:cd16919 78 GK-GTGLGLSMVYGFVKQSGGHLRIYSEPGVGTTVRIYLP 116
|
|
| HATPase_CreC-like |
cd16945 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
389-490 |
2.92e-08 |
|
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: 52.08 E-value: 2.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 389 DPTRLRQVVWNLINNAVKFTQQ-GKVTLECsrenRVEGPWLVMKVSDTGQGIPPEQLAHIFDMYYKAPDlKGTNAIGSGI 467
Cdd:cd16945 1 DPFLLRQAINNLLDNAIDFSPEgGLIALQL----EADTEGIELLVFDEGSGIPDYALNRVFERFYSLPR-PHSGQKSTGL 75
|
90 100
....*....|....*....|....
gi 746446453 468 GLAVTKALVSAMKGIITV-NSTEG 490
Cdd:cd16945 76 GLAFVQEVAQLHGGRITLrNRPDG 99
|
|
| Hpt |
pfam01627 |
Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module ... |
683-755 |
6.67e-08 |
|
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: 50.43 E-value: 6.67e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 746446453 683 QLFEKLSPQYQQELLTSLNTGDREEYESVAHKLKGAAGSVGLNDVQLHAKIMEH----GAIDESDEVLKQWLDILAD 755
Cdd:pfam01627 4 ELFLEEAPELLEQLEQALDAEDLEALFRAAHTLKGSAGSLGLPALAELAHELEDllreGELPLDPELLEALRDLLEA 80
|
|
| HATPase_Glnl-NtrB-like |
cd16918 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
393-500 |
6.94e-08 |
|
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: 51.25 E-value: 6.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 393 LRQVVWNLINNAVKFT--QQGKVTLECSRENRV----EGPWLVMKVS--DTGQGIPPEQLAHIFDmyykapDLKGTNAIG 464
Cdd:cd16918 1 LIQVFLNLVRNAAQALagSGGEIILRTRTQRQVtlghPRHRLALRVSviDNGPGIPPDLQDTIFY------PMVSGRENG 74
|
90 100 110
....*....|....*....|....*....|....*.
gi 746446453 465 SGIGLAVTKALVSAMKGIITVNSTEGEgSCFTVQIP 500
Cdd:cd16918 75 TGLGLAIAQNIVSQHGGVIECDSQPGH-TVFSVSLP 109
|
|
| REC_OmpR_PhoB |
cd17618 |
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ... |
518-607 |
1.07e-07 |
|
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: 51.10 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 518 YILLVED-VPLNAEIATNLlEQRGHEVLWAETGEDALSFVEtEDDLDLVLLDMQLPDINGDVVAKQIRSDSHFDKLPIVA 596
Cdd:cd17618 2 TILIVEDePAIREMIAFNL-ERAGFDVVEAEDAESAVNLIV-EPRPDLILLDWMLPGGSGIQFIRRLKRDEMTRDIPIIM 79
|
90
....*....|.
gi 746446453 597 LTAnvRSAEEE 607
Cdd:cd17618 80 LTA--RGEEED 88
|
|
| REC_PA4781-like |
cd19920 |
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ... |
519-621 |
1.11e-07 |
|
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: 50.59 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 519 ILLVEDVPLNAEIATNLLEQRGHEVLWAETGEDALSFVETEDDLDLVLLdMQLPDINGDVVAKQIRSDSHFDKLPIVALT 598
Cdd:cd19920 1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEPPDLILLD-VMMPGMDGFEVCRRLKADPATRHIPVIFLT 79
|
90 100
....*....|....*....|....*
gi 746446453 599 AnVRSAEEELEGISIQGA--LAKPI 621
Cdd:cd19920 80 A-LTDTEDKVKGFELGAVdyITKPF 103
|
|
| REC_Rcp-like |
cd17557 |
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ... |
519-607 |
1.81e-07 |
|
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: 50.49 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 519 ILLVEDVPLNAEIATNLLEQRG--HEVLWAETGEDALSFVETEDDLDLVLLD------MQLPDINGDVVAKQIRSDSHFD 590
Cdd:cd17557 2 ILLVEDNPGDAELIQEAFKEAGvpNELHVVRDGEEALDFLRGEGEYADAPRPdlilldLNMPRMDGFEVLREIKADPDLR 81
|
90
....*....|....*..
gi 746446453 591 KLPIVALTAnvrSAEEE 607
Cdd:cd17557 82 RIPVVVLTT---SDAEE 95
|
|
| PRK10337 |
PRK10337 |
sensor protein QseC; Provisional |
279-473 |
4.20e-07 |
|
sensor protein QseC; Provisional
Pssm-ID: 182388 [Multi-domain] Cd Length: 449 Bit Score: 53.11 E-value: 4.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 279 KFIATLSHELRTPLNGIVGLTRM--LLDTDLNKQQRSWGNtifssaetlgnifndiidLDK-IDR-----DQLdiVTNS- 349
Cdd:PRK10337 239 RFTSDAAHELRSPLAALKVQTEVaqLSDDDPQARKKALLQ------------------LHAgIDRatrlvDQL--LTLSr 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 350 INVSDFINDV--VNFAGLI----------AEQKELEFDIKRNGVlDIYAQLDPTRLRQVVWNLINNAVKFTQQG---KVT 414
Cdd:PRK10337 299 LDSLDNLQDVaeIPLEDLLqsavmdiyhtAQQAGIDVRLTLNAH-PVIRTGQPLLLSLLVRNLLDNAIRYSPQGsvvDVT 377
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 746446453 415 LECSRenrvegpwlvMKVSDTGQGIPPEQLAHIFDMYYKAPdlkGTNAIGSGIGLAVTK 473
Cdd:PRK10337 378 LNARN----------FTVRDNGPGVTPEALARIGERFYRPP---GQEATGSGLGLSIVR 423
|
|
| COG4567 |
COG4567 |
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ... |
519-645 |
4.37e-07 |
|
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: 50.69 E-value: 4.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 519 ILLVEDVPLNAEIATNLLEQRGHEVLWAETGEDALSFVETEdDLDLVLLDMQLPDINGDVVAKQIRsdSHFDKLPIVALT 598
Cdd:COG4567 7 LLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQA-PPDYAVLDLRLGDGSGLDLIEALR--ERDPDARIVVLT 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 746446453 599 --ANVRSAEEelegiSIQ-GA---LAKPINTVKLDKMLADLFGIKQSECTEPL 645
Cdd:COG4567 84 gyASIATAVE-----AIKlGAddyLAKPADADDLLAALERAEGDAPAPPENPM 131
|
|
| REC_RR468-like |
cd17552 |
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ... |
519-635 |
4.68e-07 |
|
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and similar domains; Thermotoga maritima RR468 (encoded by gene TM0468) is the cognate response regulator (RR) of the class I histidine kinase HK853 (product of gene TM0853). HK853/RR468 comprise a two-component system (TCS) that couples environmental stimuli to adaptive responses. This subfamily also includes Fremyella diplosiphon complementary adaptation response regulator homolog RcaF, a small RR that is involved in four-step phosphorelays of the complementary chromatic adaptation (CCA) system that occurs in many cyanobacteria. Both RR468 and RcaF are stand-alone RRs containing only a REC domain with no output/effector domain. The REC domain itself functions as an effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381104 [Multi-domain] Cd Length: 121 Bit Score: 49.09 E-value: 4.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 519 ILLVEDVPLNAEIA-TNLLEQRGHEVLWAETGEDALSFVETEDDLDLVLLdMQLPDINGDVVAKQIRSDSHFDKLPIVAL 597
Cdd:cd17552 4 ILVIDDEEDIREVVqACLEKLAGWEVLTASSGQEGLEKAATEQPDAILLD-VMMPDMDGLATLKKLQANPETQSIPVILL 82
|
90 100 110
....*....|....*....|....*....|....*....
gi 746446453 598 TANVRSAE-EELEGISIQGALAKPINTVKLDKMLADLFG 635
Cdd:cd17552 83 TAKAQPSDrQRFASLGVAGVIAKPFDPLTLAEQIAKLLG 121
|
|
| CitB |
COG4565 |
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ... |
519-638 |
1.24e-06 |
|
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal transduction mechanisms];
Pssm-ID: 443622 [Multi-domain] Cd Length: 138 Bit Score: 48.43 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 519 ILLVEDVPLNAEIATNLLEQ-RGHEVLW-AETGEDALSFVETEDdldlvlldMQLPDINGDVVAKQIRsdSHFDKLPIVA 596
Cdd:COG4565 6 VLIVEDDPMVAELLRRYLERlPGFEVVGvASSGEEALALLAEHRpdli-lldIYLPDGDGLELLRELR--ARGPDVDVIV 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 746446453 597 LTA--NVRSAEEELEGiSIQGALAKPINTVKLDKMLADLFGIKQ 638
Cdd:COG4565 83 ITAarDPETVREALRA-GVVDYLIKPFTFERLREALERYLEYRR 125
|
|
| CheA |
COG0643 |
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms]; |
410-503 |
2.29e-06 |
|
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
Pssm-ID: 440408 [Multi-domain] Cd Length: 563 Bit Score: 50.95 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 410 QGKVTLECSRE-NRVegpwlVMKVSDTGQGI---------------PPEQLAH---------IFdmyykAPdlkG----- 459
Cdd:COG0643 308 TGTITLSAYHEgGRV-----VIEVSDDGRGLdlekirakaiekgliTAEEAAAlsdeellelIF-----AP---Gfstae 374
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 746446453 460 --TNAIGSGIGLAVTKALVSAMKGIITVNSTEGEGSCFTVQIPLSL 503
Cdd:COG0643 375 evTDLSGRGVGMDVVKTNIEALGGTIEIESEPGKGTTFTLRLPLTL 420
|
|
| REC_hyHK |
cd17598 |
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ... |
519-599 |
2.96e-06 |
|
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase/response regulators; Typically, two-component regulatory systems (TCSs) consist of a sensor (histidine kinase) that responds to specific input(s) by modifying the output of a cognate response regulator (RR). TCSs allow organisms to sense and respond to changes in environmental conditions. Hybrid sensor histidine kinase/response regulators contain all the elements of a classical TCS in a single polypeptide chain. RRs share the common phosphoacceptor REC domain and different effector/output domains such as DNA, RNA, ligand-binding, protein-binding, or enzymatic domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381128 [Multi-domain] Cd Length: 118 Bit Score: 46.94 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 519 ILLVEDVPLNAEIATNLLEQRGHEVLWAETGEDALSFVeTEDDLDLVLLDMQLPDINGDVVAKQIRSDSHFDKLPIVALT 598
Cdd:cd17598 1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAML-AEHRPTLVISDIVMPEMDGYELCRKIKSDPDLKDIPVILLT 79
|
.
gi 746446453 599 A 599
Cdd:cd17598 80 T 80
|
|
| HATPase_VanS-like |
cd16923 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
393-500 |
3.39e-06 |
|
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Enterococcus faecium VanS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Enterococcus faecium VanS HK of the VanS-VanR two-component regulatory system (TCS) which activates the transcription of vanH, vanA and vanX vancomycin resistance genes. It also contains Ecoli YedV and PcoS, probable members of YedW-YedV TCS and PcoS-PcoR TCS, repectively. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); most also have a HAMP sensor domain.
Pssm-ID: 340400 [Multi-domain] Cd Length: 102 Bit Score: 46.23 E-value: 3.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 393 LRQVVWNLINNAVKFTqqgkvtLECSR---ENRVEGPWLVMKVSDTGQGIPPEQLAHIFDMYYKAPdlKGTNAIGSGIGL 469
Cdd:cd16923 1 LQRVFSNLLSNAIKYS------PENTRiyiTSFLTDDVVNIMFKNPSSHPLDFKLEKLFERFYRGD--NSRNTEGAGLGL 72
|
90 100 110
....*....|....*....|....*....|.
gi 746446453 470 AVTKALVSAMKGIITVNStEGEGSCFTVQIP 500
Cdd:cd16923 73 SIAKAIIELHGGSASAEY-DDNHDLFKVRLP 102
|
|
| REC_OmpR_BsPhoP-like |
cd19937 |
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ... |
520-599 |
3.46e-06 |
|
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus subtilis PhoP (BsPhoP) is part of the PhoPR two-component system that participates in a signal transduction network that controls adaptation of the bacteria to phosphate deficiency by regulating (activating or repressing) genes of the Pho regulon upon phosphorylation by PhoR. When activated, PhoPR directs expression of phosphate scavenging enzymes, lowers synthesis of the phosphate-rich wall teichoic acid (WTA) and initiates synthesis of teichuronic acid, a non-phosphate containing replacement anionic polymer. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381164 [Multi-domain] Cd Length: 116 Bit Score: 46.50 E-value: 3.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 520 LLVEDVPLNAEIATNLLEQRGHEVLWAETGEDALSFVETEDDLDLVLLdMQLPDINGDVVAKQIRSDSHFDKLPIVALTA 599
Cdd:cd19937 1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDEKPDLIILD-LMLPGIDGLEVCRILRSDPKTSSIPIIMLTA 79
|
|
| REC_OmpR_CusR-like |
cd19935 |
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ... |
519-620 |
3.95e-06 |
|
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: 45.89 E-value: 3.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 519 ILLVEDVPLNAEIATNLLEQRGHEVLWAETGEDALSFVETEDDLDLVLLDMqLPDINGDVVAKQIRsdSHFDKLPIVALT 598
Cdd:cd19935 1 ILVVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLHLALTNEYDLIILDVM-LPGLDGLEVLRRLR--AAGKQTPVLMLT 77
|
90 100
....*....|....*....|....*.
gi 746446453 599 AnvRSA-EEELEGISIqGA---LAKP 620
Cdd:cd19935 78 A--RDSvEDRVKGLDL-GAddyLVKP 100
|
|
| REC_ETR-like |
cd19933 |
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ... |
517-633 |
4.39e-06 |
|
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: 46.24 E-value: 4.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 517 LYILLVEDVPLNAEIATNLLEQRGHEVLWAETGEDALSFVET-EDDLDLVLLDMQLPDINGDVVAKQIRSDSHFDKLP-I 594
Cdd:cd19933 1 LKVLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLLASaEHSFQLVLLDLCMPEMDGFEVALRIRKLFGRRERPlI 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 746446453 595 VALTAN-VRSAEEELEGISIQGALAKPintVKLDKMLADL 633
Cdd:cd19933 81 VALTANtDDSTREKCLSLGMNGVITKP---VSLHALGDEL 117
|
|
| COG3920 |
COG3920 |
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ... |
38-502 |
6.35e-06 |
|
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction mechanisms];
Pssm-ID: 443125 [Multi-domain] Cd Length: 495 Bit Score: 49.52 E-value: 6.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 38 LILSSMFYYVAIGELHLVDILAVVFFTAVVSPLIISVLLNSIRQLDASYAYLDSATKQEKLLNQTLKDNINRLNIEIDER 117
Cdd:COG3920 56 LALSAAALAAALAVALAAAVGAAAALLALLVLLLLLLLAAAALALALLLAALAGLLLLAALLLLRLVALLAALALLALLL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 118 KMAFHAKHRAIEELRREIAERKKTQQELAQQSMLQRSIVDSSPDLFYYRDNNGVFAGCNKMFEEVMGKSSSELIGKTVEQ 197
Cdd:COG3920 136 LLLLLLAILALAELAVALAELAAALLLLAEELAALRLAAAALLLLLAALLDLGLALAALAAAALLALLLALELLLALLLL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 198 IFPSHFLSEVLKTDKEVEQSHKALTIDVGYEVNGETRWFELRKLPFINDEGDYIGLLGFGRDITSRKEAAQALETAYKDK 277
Cdd:COG3920 216 LLLLLALLLVLLAALLRLRAAVLEELERRRRARGLGRLLLLLLLLLLLLRALLLLAAGIRLVITERKRAEEELEASLEEK 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 278 GKFIATLSHELRTPLNGIVGLTRMlldtdlnkQQRSwgntifSSAETLGNIFNDIIDldkidR--------DQL--DIVT 347
Cdd:COG3920 296 ELLLRELHHRVKNNLQVVSSLLRL--------QARR------ADDPEAREALEESQN-----RiqalalvhELLyqSEDW 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 348 NSINVSDFINDVVNFAGLIAEQKELEFDIkrngvldiyaQLDPTRLRQ--------VVWNLINNAVKF----TQQGKVTL 415
Cdd:COG3920 357 EGVDLRDYLRELLEPLRDSYGGRGIRIEL----------DGPDVELPAdaavplglILNELVTNALKHaflsGEGGRIRV 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 416 ECSREnrveGPWLVMKVSDTGQGIPPEqlahiFDMyykapdlkgtnAIGSGIGLAVTKALVSAMKGIITVNSteGEGSCF 495
Cdd:COG3920 427 SWRRE----DGRLRLTVSDNGVGLPED-----VDP-----------PARKGLGLRLIRALVRQLGGTLELDR--PEGTRV 484
|
....*..
gi 746446453 496 TVQIPLS 502
Cdd:COG3920 485 RITFPLA 491
|
|
| PRK13560 |
PRK13560 |
hypothetical protein; Provisional |
134-502 |
6.62e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 106506 [Multi-domain] Cd Length: 807 Bit Score: 49.67 E-value: 6.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 134 EIAERKKTQQELAQQSMlqrsIVDSSP-DLFYYRDNNG------------------VFAGCNKMFEEVMGKSSSELIGKT 194
Cdd:PRK13560 461 DITERKQVEEQLLLANL----IVENSPlVLFRWKAEEGwpvelvsknitqfgyepdEFISGKRMFAAIIHPADLEQVAAE 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 195 VEQIfpshflseVLKTDKEVEQSHKALTidvgyeVNGETRWFELRKLPFINDEGDYIGLLGFGRDITSRKEAAQALETAY 274
Cdd:PRK13560 537 VAEF--------AAQGVDRFEQEYRILG------KGGAVCWIDDQSAAERDEEGQISHFEGIVIDISERKHAEEKIKAAL 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 275 KDKGKFIATLSHELRTPLNgivgLTRMLLDTDLNKQQRSWGNTIFssAETLGNIFNDIIDLDKIDRDQlDIvtNSINVSD 354
Cdd:PRK13560 603 TEKEVLLKEIHHRVKNNLQ----IISSLLDLQAEKLHDEEAKCAF--AESQDRICAMALAHEKLYQSE-DL--ADIDFLD 673
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 355 FINDVVN--FAGLIAEQKELEFDIKR-NGVLDIyAQLDPTRLrqVVWNLINNAVKFTQQGKVTLECSRENRVEGPWLV-M 430
Cdd:PRK13560 674 YIESLTAhlKNSFAIDFGRIDCKIDAdDGCLDI-DKAIPCGL--IISELLSNALKHAFPDGAAGNIKVEIREQGDGMVnL 750
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 746446453 431 KVSDTGQGIPPEqlahiFDmYYKAPDLkgtnaigsgiGLAVTKALVSAMKGIITVNSTegEGSCFTVQIPLS 502
Cdd:PRK13560 751 CVADDGIGLPAG-----FD-FRAAETL----------GLQLVCALVKQLDGEIALDSR--GGARFNIRFPMS 804
|
|
| REC_DC-like |
cd17534 |
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ... |
519-600 |
1.04e-05 |
|
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: 45.09 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 519 ILLVEDVPLNAEIATNLLEQRGHEVL-WAETGEDALSFVETEDdldlvlldmqlPD-----------INGDVVAKQIRSD 586
Cdd:cd17534 3 ILIVEDEAIIALDLKEILESLGYEVVgIADSGEEAIELAEENK-----------PDlilmdinlkgdMDGIEAAREIREK 71
|
90
....*....|....
gi 746446453 587 SHfdkLPIVALTAN 600
Cdd:cd17534 72 FD---IPVIFLTAY 82
|
|
| REC |
smart00448 |
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ... |
519-553 |
1.19e-05 |
|
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar motors. This domain contains a phosphoacceptor site that is phosphorylated by histidine kinase homologues.
Pssm-ID: 214668 [Multi-domain] Cd Length: 55 Bit Score: 43.33 E-value: 1.19e-05
10 20 30
....*....|....*....|....*....|....*
gi 746446453 519 ILLVEDVPLNAEIATNLLEQRGHEVLWAETGEDAL 553
Cdd:smart00448 3 ILVVDDDPLLRELLKALLEKEGYEVDEATDGEEAL 37
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
153-216 |
1.23e-05 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.
Pssm-ID: 214512 Cd Length: 67 Bit Score: 43.54 E-value: 1.23e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 746446453 153 RSIVDSSPDLFYYRDNNGVFAGCNKMFEEVMGKSSSELIGKTVEQIFPSHFLSEVLKTDKEVEQ 216
Cdd:smart00091 4 RAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLLS 67
|
|
| HATPase_SpaK_NisK-like |
cd16975 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
389-499 |
1.30e-05 |
|
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis SpaK and Lactococcus lactis NisK; This family includes histidine kinase-like ATPase (HATPase) domain of two-component sensor histidine kinases similar to Bacillus subtilis SpaK and Lactococcus lactis NisK. SpaK is the histidine kinase (HK) of the SpaK-SpaR two-component regulatory system (TCS), which is involved in the regulation of the biosynthesis of lantibiotic subtilin. NisK is the HK of the NisK-NisR TCS, which is involved in the regulation of the biosynthesis of lantibiotic nisin. SpaK and NisK may function as membrane-associated protein kinases that phosphorylate SpaR and NisR, respectively, in response to environmental signals.
Pssm-ID: 340434 [Multi-domain] Cd Length: 107 Bit Score: 44.76 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 389 DPTRLRQVVWNLINNAVKFTQQGK---VTLECSREnrvegpWLVMKVSDTGQGIPPEQLAHIFDMYYKAPDLKGTNAiGS 465
Cdd:cd16975 1 DTLLLSRALINIISNACQYAPEGGtvsISIYDEEE------YLYFEIWDNGHGFSEQDLKKALELFYRDDTSRRSGG-HY 73
|
90 100 110
....*....|....*....|....*....|....
gi 746446453 466 GIGLAVTKALVSAMKGIITVNSTEGEGSCFTVQI 499
Cdd:cd16975 74 GMGLYIAKNLVEKHGGSLIIENSQKGGAEVTVKI 107
|
|
| HATPase_PhoQ-like |
cd16954 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
389-499 |
3.72e-05 |
|
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: 44.16 E-value: 3.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 389 DPTRLRQVVWNLINNAVKFtqqgkvtleCSRENRV---EGP-WLVMKVSDTGQGIPPEQLAHIFDmyykapdlKGTNA-- 462
Cdd:cd16954 34 ERNDLMELLGNLLDNACKW---------CLEFVEVtarQTDgGLHLIVDDDGPGVPESQRSKIFQ--------RGQRLde 96
|
90 100 110
....*....|....*....|....*....|....*....
gi 746446453 463 --IGSGIGLAVTKALVSAMKGIITVNSTEGEGSCFTVQI 499
Cdd:cd16954 97 qrPGQGLGLAIAKEIVEQYGGELSLSDSPLGGARFEVVF 135
|
|
| YesM |
COG2972 |
Sensor histidine kinase YesM [Signal transduction mechanisms]; |
383-501 |
3.83e-05 |
|
Sensor histidine kinase YesM [Signal transduction mechanisms];
Pssm-ID: 442211 [Multi-domain] Cd Length: 445 Bit Score: 46.93 E-value: 3.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 383 DIYAQLDPTRLRQVvwnLINNAVKF-----TQQGKVTLECSRENRvegpWLVMKVSDTGQGIPPEQLAHIFDMYYKAPDl 457
Cdd:COG2972 330 ELLDLLIPKLILQP---LVENAIEHgiepkEGGGTIRISIRKEGD----RLVITVEDNGVGMPEEKLEKLLEELSSKGE- 401
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 746446453 458 kgtnaiGSGIGLAVTKALVSAMKGI---ITVNSTEGEGSCFTVQIPL 501
Cdd:COG2972 402 ------GRGIGLRNVRERLKLYYGEeygLEIESEPGEGTTVTIRIPL 442
|
|
| HATPase_PDK-like |
cd16929 |
Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain ... |
351-492 |
4.21e-05 |
|
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: 44.64 E-value: 4.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 351 NVSDFINDVVNFAGLIAEQKELEF-DIKRNGVLDIYAQLDPTRLRQVVWNLINNAVKFTQQG-----------KVTLECS 418
Cdd:cd16929 1 SPKKVVEDASEEARVLCDDYYLSSpELEIEGDPSIRFPYVPSHLYYILFELLKNAMRATVEShgddsddlppiKVTVAKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 419 REnrvegpWLVMKVSDTGQGIPPEQLAHIFD-MYYKAP------------DLKGTNAIGSGIGLAVTKALVSAMKGIITV 485
Cdd:cd16929 81 DE------DLTIKISDRGGGIPREDLARLFSyMYSTAPqpslddfsdlisGTQPSPLAGFGYGLPMSRLYAEYFGGDLDL 154
|
....*..
gi 746446453 486 NSTEGEG 492
Cdd:cd16929 155 QSMEGYG 161
|
|
| HPT |
cd00088 |
Histidine Phosphotransfer domain, involved in signalling through a two part component systems ... |
675-765 |
8.20e-05 |
|
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: 41.98 E-value: 8.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 675 LVVFRRSSQ-LFEKLspqyQQELLTSLNTGDREEYESVAHKLKGAAGSVGLNDVQLHAKIMEH--GAIDESDEVLKQWLD 751
Cdd:cd00088 5 LELFLEEAEeLLEEL----ERALLELEDAEDLNEIFRAAHTLKGSAASLGLQRLAQLAHQLEDllDALRDGLEVTPELID 80
|
90
....*....|....
gi 746446453 752 ILADKINEGQKALH 765
Cdd:cd00088 81 LLLDALDALKAELE 94
|
|
| PRK10610 |
PRK10610 |
chemotaxis protein CheY; |
515-634 |
8.40e-05 |
|
chemotaxis protein CheY;
Pssm-ID: 170568 [Multi-domain] Cd Length: 129 Bit Score: 43.04 E-value: 8.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 515 RGLYILLVEDVPLNAEIATNLLEQRG-HEVLWAETGEDALSFVETeDDLDLVLLDMQLPDINGDVVAKQIRSDSHFDKLP 593
Cdd:PRK10610 4 KELKFLVVDDFSTMRRIVRNLLKELGfNNVEEAEDGVDALNKLQA-GGFGFVISDWNMPNMDGLELLKTIRADGAMSALP 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 746446453 594 IVALTANVRsaEEELEGISIQGA---LAKPINTVKLDKMLADLF 634
Cdd:PRK10610 83 VLMVTAEAK--KENIIAAAQAGAsgyVVKPFTAATLEEKLNKIF 124
|
|
| REC_OmpR_PmrA-like |
cd17624 |
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ... |
519-620 |
8.41e-05 |
|
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This subfamily contains various OmpR family response regulators including PmrA, BasR, QseB, tctD, and RssB, which are components of two-component regulatory systems (TCSs). The PmrA/PmrB TCS controls transcription of genes that are involved in lipopolysaccharide modification in the outer membrane of bacteria, increasing bacterial resistance to host-derived antimicrobial peptides. The BasS/BasR TCS functions as an iron- and zinc-sensing transcription regulator. The QseB/QseC TCS activates the flagella regulon by activating transcription of FlhDC. The RssA/RssB TCS regulates swarming behavior in Serratia marcescens. OmpR family DNA-binding response regulators contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381139 [Multi-domain] Cd Length: 115 Bit Score: 42.47 E-value: 8.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 519 ILLVEDVPLNAEIATNLLEQRGHEVLWAETGEDALSFVETEDDLDLVLLDMqLPDINGDVVAKQIRSDShfDKLPIVALT 598
Cdd:cd17624 1 ILLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALASGPYDLVILDLG-LPDGDGLDLLRRWRRQG--QSLPVLILT 77
|
90 100
....*....|....*....|....*.
gi 746446453 599 AnvRSAEEE-LEGISiQGA---LAKP 620
Cdd:cd17624 78 A--RDGVDDrVAGLD-AGAddyLVKP 100
|
|
| ComP |
COG4585 |
Signal transduction histidine kinase ComP [Signal transduction mechanisms]; |
400-501 |
8.98e-05 |
|
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
Pssm-ID: 443642 [Multi-domain] Cd Length: 252 Bit Score: 44.99 E-value: 8.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 400 LINNAVKFTQQGKVTLECSRENRvegpWLVMKVSDTGQGIPPEQLAhifdmyykapdlkgtnaiGSGIGLAVTKALVSAM 479
Cdd:COG4585 170 ALTNALKHAGATRVTVTLEVDDG----ELTLTVRDDGVGFDPEAAP------------------GGGLGLRGMRERAEAL 227
|
90 100
....*....|....*....|..
gi 746446453 480 KGIITVNSTEGEGSCFTVQIPL 501
Cdd:COG4585 228 GGTLTIGSAPGGGTRVRATLPL 249
|
|
| PRK13558 |
PRK13558 |
bacterio-opsin activator; Provisional |
176-271 |
1.23e-04 |
|
bacterio-opsin activator; Provisional
Pssm-ID: 237426 [Multi-domain] Cd Length: 665 Bit Score: 45.60 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 176 NKMFEEVMGKSSSELIGKTveqifpSHFLsEVLKTDKE--------VEQSHKALTIDVGYEVNGETRWFELRKLPFINDE 247
Cdd:PRK13558 177 NDAFERITGYSPDEVLGRN------CRFL-QGEDTNEErvaelreaIDEERPTSVELRNYRKDGSTFWNQVDIAPIRDED 249
|
90 100
....*....|....*....|....
gi 746446453 248 GDYIGLLGFGRDITSRKEAAQALE 271
Cdd:PRK13558 250 GTVTHYVGFQTDVTERKEAELALQ 273
|
|
| REC_OmpR_DrrD-like |
cd17625 |
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ... |
520-627 |
1.27e-04 |
|
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a OmpR/PhoB homolog from Thermotoga maritima whose function is not yet known. This subfamily also includes Streptococcus agalactiae transcriptional regulatory protein DltR, part of the DltS/DltR two-component system (TCS), and Pseudomonas aeruginosa transcriptional activator protein PfeR, part of the PfeR/PfeS TCS, which activates expression of the ferric enterobactin receptor. The DltS/DltR TCS regulates the expression of the dlt operon, which comprises four genes (dltA, dltB, dltC, and dltD) that catalyze the incorporation of D-alanine residues into the lipoteichoic acids. Members of this subfamily belong to the OmpR/PhoB family, which comprises of two domains, an N-terminal receiver domain and a C-terminal DNA-binding winged helix-turn-helix effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381140 [Multi-domain] Cd Length: 115 Bit Score: 42.21 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 520 LLVEDVPLNAEIATNLLEQRGHEVLWAETGEDALSFVETEDDLDLVLLDMqLPDINGDVVAKQIRSDShfDKLPIVALTA 599
Cdd:cd17625 1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEYALSGIYDLIILDIM-LPGMDGLEVLKSLREEG--IETPVLLLTA 77
|
90 100 110
....*....|....*....|....*....|..
gi 746446453 600 nvRSAEEE-LEGISiQGA---LAKPINTVKLD 627
Cdd:cd17625 78 --LDAVEDrVKGLD-LGAddyLPKPFSLAELL 106
|
|
| REC_OmpR_YycF-like |
cd17614 |
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ... |
519-599 |
1.39e-04 |
|
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF appears to play an important role in cell wall integrity in a wide range of gram-positive bacteria, and may also modulate cell membrane integrity. It functions as part of a phosphotransfer system that ultimately controls the levels of competence within the bacteria. YycF belongs to the OmpR family of response regulators, which are characterized by a REC domain and a winged helix-turn-helix effector domain involved in DNA binding. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381130 [Multi-domain] Cd Length: 115 Bit Score: 42.03 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 519 ILLVEDVPLNAEIATNLLEQRGHEVLWAETGEDALSFVETEDDLDLVLLdMQLPDINGDVVAKQIRSDSHfdkLPIVALT 598
Cdd:cd17614 1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVEEEQPDLILLD-LMLPEKDGLEVCREVRKTSN---VPIIMLT 76
|
.
gi 746446453 599 A 599
Cdd:cd17614 77 A 77
|
|
| dpiB |
PRK15053 |
sensor histidine kinase DpiB; Provisional |
386-500 |
1.52e-04 |
|
sensor histidine kinase DpiB; Provisional
Pssm-ID: 185013 [Multi-domain] Cd Length: 545 Bit Score: 45.21 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 386 AQLDPTRLRQVVWNLINNAVKF---TQQGKVTLECSRENrvEGPWLVMKVSDTGQGIPPEQLAHIFDmyyKAPDLKGTNA 462
Cdd:PRK15053 426 PGLDSTEFAAIVGNLLDNAFEAslrSDEGNKIVELFLSD--EGDDVVIEVADQGCGVPESLRDKIFE---QGVSTRADEP 500
|
90 100 110
....*....|....*....|....*....|....*...
gi 746446453 463 IGSGIGLAVTKALVSAMKGIITVNSTEGEGSCFTVQIP 500
Cdd:PRK15053 501 GEHGIGLYLIASYVTRCGGVITLEDNDPCGTLFSIFIP 538
|
|
| REC_hyHK_blue-like |
cd18161 |
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ... |
519-620 |
1.87e-04 |
|
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: 41.18 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 519 ILLVEDVPLNAEIATNLLEQRGHEVLWAETGEDALSFVETEDDLDLVLLDMQLPD-INGDVVAKQIRsdSHFDKLPIVAL 597
Cdd:cd18161 1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLESGPDIDLLVTDVIMPGgMNGSQLAEEAR--RRRPDLKVLLT 78
|
90 100
....*....|....*....|....*.
gi 746446453 598 T--ANVRSAEEELE-GISIqgaLAKP 620
Cdd:cd18161 79 SgyAENAIEGGDLApGVDV---LSKP 101
|
|
| RsbW |
COG2172 |
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms]; |
391-501 |
2.12e-04 |
|
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
Pssm-ID: 441775 [Multi-domain] Cd Length: 127 Bit Score: 41.82 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 391 TRLRQVVWNLINNAVKFTQQ----GKVTLECsrenRVEGPWLVMKVSDTGQGIPPEQLahifdmyykaPDLKGTNAIGsG 466
Cdd:COG2172 33 DDLVLAVSEAVTNAVRHAYGgdpdGPVEVEL----ELDPDGLEIEVRDEGPGFDPEDL----------PDPYSTLAEG-G 97
|
90 100 110
....*....|....*....|....*....|....*
gi 746446453 467 IGLAVTKALVSAMkgiiTVNSTEGeGSCFTVQIPL 501
Cdd:COG2172 98 RGLFLIRRLMDEV----EYESDPG-GTTVRLVKRL 127
|
|
| PRK11083 |
PRK11083 |
DNA-binding response regulator CreB; Provisional |
519-620 |
2.25e-04 |
|
DNA-binding response regulator CreB; Provisional
Pssm-ID: 236838 [Multi-domain] Cd Length: 228 Bit Score: 43.41 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 519 ILLVEDVPLNAEIATNLLEQRGHEVLWAETGEDALSFVETeDDLDLVLLDMQLPDINGDVVAKQIRsdSHFDKLPIVALT 598
Cdd:PRK11083 6 ILLVEDEQAIADTLVYALQSEGFTVEWFERGLPALDKLRQ-QPPDLVILDVGLPDISGFELCRQLL--AFHPALPVIFLT 82
|
90 100
....*....|....*....|....*.
gi 746446453 599 AnvRSAE-EELEGISIqGA---LAKP 620
Cdd:PRK11083 83 A--RSDEvDRLVGLEI-GAddyVAKP 105
|
|
| COG4192 |
COG4192 |
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ... |
278-500 |
2.36e-04 |
|
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal transduction mechanisms];
Pssm-ID: 443346 [Multi-domain] Cd Length: 640 Bit Score: 44.68 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 278 GKFIATLSHELRTPLNGI---VGLTRMLLDTDLNKQQRSWGNTIFSSAETLGNIFNDIIDLDKIDRDQLDIVTnsinvsd 354
Cdd:COG4192 434 GQTMTSLAHELNQPLNAMsmyLFSAKKALEQENYAQLPTSLDKIEGLIERMDKIIKSLRQFSRKSDTPLQPVD------- 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 355 fINDVVNFAGLIAEQKELEFDIKRNGVLDIYAQLDPTRLRQVVWNLINNAVK-FTQQGKVTLECSRENRVegpwLVMKVS 433
Cdd:COG4192 507 -LRQVIEQAWELVESRAKPQQITLHIPDDLMVQGDQVLLEQVLVNLLVNALDaVATQPQISVDLLSNAEN----LRVAIS 581
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 746446453 434 DTGQGIPpeQLAHIFDMYYKapdlkgTNAIGSGIGLAVTKALVSAMKGIITVNSTEGEGSCFTVQIP 500
Cdd:COG4192 582 DNGNGWP--LVDKLFTPFTT------TKEVGLGLGLSICRSIMQQFGGDLYLASTLERGAMVILEFN 640
|
|
| REC_CheV-like |
cd19924 |
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ... |
519-598 |
2.40e-04 |
|
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This subfamily includes the REC domains of Bacillus subtilis chemotaxis protein CheV, Myxococcus xanthus gliding motility regulatory protein FrzE, and similar proteins. CheV is a hybrid protein with an N-terminal CheW-like domain and a C-terminal CheY-like REC domain. The CheV pathway is one of three systems employed by B. subtilis for sensory adaptation that contribute to chemotaxis. It is involved in the transmission of sensory signals from chemoreceptors to flagellar motors. Together with CheW, it is involved in the coupling of methyl-accepting chemoreceptors to the central two-component histidine kinase CheA. FrzE is a hybrid sensor histidine kinase/response regulator that is part of the Frz pathway that controls cell reversal frequency to support directional motility during swarming and fruiting body formation. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381151 [Multi-domain] Cd Length: 111 Bit Score: 41.21 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 519 ILLVEDVPLNAEIATNLLEQRGHEVLWAETGEDALSFVETEDDLDLVLLD--------MQLPDINGDVVAKQIRSDSHFD 590
Cdd:cd19924 1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLENLAKEGNDLSKeldliitdIEMPKMDGYELTFELRDDPRLA 80
|
....*...
gi 746446453 591 KLPIVALT 598
Cdd:cd19924 81 NIPVILNS 88
|
|
| REC_OmpR_CpxR |
cd17623 |
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ... |
519-599 |
3.54e-04 |
|
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: 40.75 E-value: 3.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 519 ILLVEDVPLNAEIATNLLEQRGHEVLWAETGEDALSFVeTEDDLDLVLLDMQLPDINGDVVAKQIRSDShfdKLPIVALT 598
Cdd:cd17623 1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAAL-LEGSPDLVVLDVMLPKMNGLDVLKELRKTS---QVPVLMLT 76
|
.
gi 746446453 599 A 599
Cdd:cd17623 77 A 77
|
|
| REC_OmpR_KdpE-like |
cd17620 |
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ... |
519-607 |
3.62e-04 |
|
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a component of the KdpD/KdpE two-component system (TCS) and is activated when histidine kinase KdpD senses a drop in external K+ concentration or upshift in ionic osmolarity, resulting in the expression of a heterooligomeric transporter KdpFABC. In addition, the KdpD/KdpE TCS is also an adaptive regulator involved in the virulence and intracellular survival of pathogenic bacteria. KdpE is a member of the OmpR family of DNA-binding response regulators that contain REC and winged helix-turn-helix (wHTH) DNA-binding output effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381135 [Multi-domain] Cd Length: 99 Bit Score: 40.23 E-value: 3.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 519 ILLVEDVP--LNAEIATnlLEQRGHEVLWAETGEDALSFVETEDDLDLVLLdMQLPDINGDVVAKQIRSDShfdKLPIVA 596
Cdd:cd17620 1 ILVIEDEPqiRRFLRTA--LEAHGYRVFEAETGQEGLLEAATRKPDLIILD-LGLPDMDGLEVIRRLREWS---AVPVIV 74
|
90
....*....|.
gi 746446453 597 LTAnvRSAEEE 607
Cdd:cd17620 75 LSA--RDEESD 83
|
|
| REC_NtrC1-like |
cd17572 |
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ... |
519-599 |
6.20e-04 |
|
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: 40.26 E-value: 6.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 519 ILLVEDVPLNAEIATNLLEQRGHEVLWAETGEDALSFVEtEDDLDLVLLDMQLPDINGDVVAKQIRSDShfDKLPIVALT 598
Cdd:cd17572 1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLS-DQPPDVVLLDLKLPDMSGMEILKWIQERS--LPTSVIVIT 77
|
.
gi 746446453 599 A 599
Cdd:cd17572 78 A 78
|
|
| HATPase_UhpB-NarQ-NarX-like |
cd16917 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
393-500 |
6.98e-04 |
|
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: 39.07 E-value: 6.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 393 LRQVVWNLINNAVKFTQQGKVTLECSRENRvegpWLVMKVSDTGQGIPPEQlahifdmyyKAPdlkgtnaiGSGIGLAVT 472
Cdd:cd16917 1 LYRIVQEALTNALKHAGASRVRVTLSYTAD----ELTLTVVDDGVGFDGPA---------PPG--------GGGFGLLGM 59
|
90 100
....*....|....*....|....*...
gi 746446453 473 KALVSAMKGIITVNSTEGEGSCFTVQIP 500
Cdd:cd16917 60 RERAELLGGTLTIGSRPGGGTRVTARLP 87
|
|
| HKR_ArcB_TM |
pfam18415 |
Histidine kinase receptor ArcB trans-membrane domain; Histidine kinase receptors (HKRs) are ... |
17-85 |
7.23e-04 |
|
Histidine kinase receptor ArcB trans-membrane domain; Histidine kinase receptors (HKRs) are part of a two-component system, in which an HKR in the bacterial inner membrane transmits a signal to a response regulator located in the cytoplasm. This is a trans-membrane domain (TM) found in ArcB (class 2, aerobic respiratory control sensor). ArcB has two TM helices connected by a short periplasmic loop. TM domain structures suggests a loose helical packing which provides an inherent flexibility in the TM domains and that this is perhaps essential to the mechanism of signal transduction across the membrane.
Pssm-ID: 436484 Cd Length: 75 Bit Score: 38.67 E-value: 7.23e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 746446453 17 ITRFGEFKTAAICYTLFLTVSLILSSMFYYVAIGELHLVDILAVVFFTAVVSPLIISVLLNSIRQLDAS 85
Cdd:pfam18415 1 VIRLGTVRFSLLLAILLILFALLIQILLSLLLTGEVHWEDLLRSIFFGLLSAPWVLYFFSVVVEQLERS 69
|
|
| HATPase_CheA-like |
cd16916 |
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ... |
410-500 |
8.98e-04 |
|
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: 41.03 E-value: 8.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 410 QGKVTLECSREnrveGPWLVMKVSDTGQGIPPEQL--------------------AHIFDMYYkAPDL----KGTNAIGS 465
Cdd:cd16916 69 EGTITLRAEHQ----GNQVVIEVSDDGRGIDREKIrekaierglitadeaatlsdDEVLNLIF-APGFstaeQVTDVSGR 143
|
90 100 110
....*....|....*....|....*....|....*
gi 746446453 466 GIGLAVTKALVSAMKGIITVNSTEGEGSCFTVQIP 500
Cdd:cd16916 144 GVGMDVVKRSIESLGGTIEVESEPGQGTTFTIRLP 178
|
|
| glnL |
PRK11073 |
nitrogen regulation protein NR(II); |
180-501 |
2.30e-03 |
|
nitrogen regulation protein NR(II);
Pssm-ID: 182947 [Multi-domain] Cd Length: 348 Bit Score: 40.83 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 180 EEVMGKSSSELIGKTVEQIFpSHFlSEVLKTDKEVEQSHKALT-IDVGYEVNGETRWFELRKLPFINDEgdyigLLGFGR 258
Cdd:PRK11073 37 QQLLAQSSRKLFGTPLPELL-SYF-SLNIELMRESLQAGQGFTdNEVTLVIDGRSHILSLTAQRLPEGM-----ILLEMA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 259 DITSRKEAAQ-----ALETAYKDkgkFIATLSHELRTPLNGIVG----LTRMLLDTDLnkqqRSWGNTIFSSAETLGNIF 329
Cdd:PRK11073 110 PMDNQRRLSQeqlqhAQQVAARD---LVRGLAHEIKNPLGGLRGaaqlLSKALPDPAL----TEYTKVIIEQADRLRNLV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 330 NDIIDLDKIDRDQLDivtnsiNVSDFINDVVNfagLIAEQKELEFDIKRN---GVLDIYaqLDPTRLRQVVWNLINNAVK 406
Cdd:PRK11073 183 DRLLGPQRPGTHVTE------SIHKVAERVVQ---LVSLELPDNVRLIRDydpSLPELA--HDPDQIEQVLLNIVRNALQ 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 407 FTQQ--GKVTLECSRENRV----EGPWLV--MKVSDTGQGIPPeqlaHIFD-MYYkaPDLKGTNAiGSGIGLAVTKALVS 477
Cdd:PRK11073 252 ALGPegGTITLRTRTAFQLtlhgERYRLAarIDIEDNGPGIPP----HLQDtLFY--PMVSGREG-GTGLGLSIARNLID 324
|
330 340
....*....|....*....|....
gi 746446453 478 AMKGIITVNSTEGEgSCFTVQIPL 501
Cdd:PRK11073 325 QHSGKIEFTSWPGH-TEFSVYLPI 347
|
|
| HATPase_Phy-like |
cd16932 |
Histidine kinase-like ATPase domain of plant phytochromes similar to Arabidopsis thaliana ... |
389-501 |
3.16e-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: 38.02 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 389 DPTRLRQVVWNLINNAVKFTQ--QGKVTLECS-RENRVEGPWLVM----KVSDTGQGIPPEQLAHIFDmyykapdlKGTN 461
Cdd:cd16932 3 DQIRLQQVLADFLLNAVRFTPspGGWVEIKVSpTKKQIGDGVHVIhlefRITHPGQGLPEELVQEMFE--------ENQW 74
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 746446453 462 AIGSGIGLAVTKALVSAMKGiiTVN-STEGEGSCFTVQIPL 501
Cdd:cd16932 75 TTQEGLGLSISRKLVKLMNG--DVRyLREAGRSYFLITLEL 113
|
|
| REC_OmpR_kpRstA-like |
cd17622 |
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ... |
519-600 |
3.17e-03 |
|
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: 38.13 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 519 ILLVEDVPLNAEIATNLLEQRGHEVLWAETGEDALSFVETEDDLDLVLLDMqLPDINGDVVAKQIRSdshFDKLPIVALT 598
Cdd:cd17622 3 ILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIAREKPDAVLLDIM-LPGIDGLTLCRDLRP---KYQGPILLLT 78
|
..
gi 746446453 599 AN 600
Cdd:cd17622 79 AL 80
|
|
| HATPase_ETR2_ERS2-EIN4-like |
cd16938 |
Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related ... |
389-497 |
3.40e-03 |
|
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: 38.59 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 389 DPTRLRQVVWNLINNAVKFTQQG-----KVTLECSRENRVEGPWLVMKVSDTGQGIPP----------EQLAHIFDMYYK 453
Cdd:cd16938 8 DERRVFQVLLHMLGNLLKMRNGGgnitfRVFLEGGSEDRSDRDWGPWRPSMSDESVEIrfeveindsgSPSIESASMRNS 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 746446453 454 APDLKGTNAIGSGIGLAVTKALVSAMKGIITVNSTEGEGSCFTV 497
Cdd:cd16938 88 LNRRYNLSELGEHLSFSICKQLVQLMGGNIWIVPGSGLGTTMSL 131
|
|
| REC_RpfG-like |
cd17551 |
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ... |
519-626 |
4.36e-03 |
|
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: 37.81 E-value: 4.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 519 ILLVEDVPLNAEIATNLLEQRG----------HEVL-WAETGEDALSFVEteddldlvlldMQLPDINGDVVAKQIRSDS 587
Cdd:cd17551 3 ILIVDDNPTNLLLLEALLRSAGylevvsftdpREALaWCRENPPDLILLD-----------YMMPGMDGLEFIRRLRALP 71
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 746446453 588 HFDKLPIVALTAN----VRsaEEELEGisiqGA---LAKPINTVKL 626
Cdd:cd17551 72 GLEDVPIVMITADtdreVR--LRALEA----GAtdfLTKPFDPVEL 111
|
|
| REC_RegA-like |
cd17563 |
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ... |
519-623 |
5.29e-03 |
|
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: 37.42 E-value: 5.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 519 ILLVEDVPLNAEIATNLLEQRGHEVLWAETGEDALSFVETEdDLDLVLLDMQLPDINGDVVAKQIRsdSHFDKLPIVALT 598
Cdd:cd17563 3 LLLVDDDEVFAERLARALERRGFEVETAHSVEEALALAREE-KPDYAVLDLRLGGDSGLDLIPPLR--ALQPDARIVVLT 79
|
90 100 110
....*....|....*....|....*....|
gi 746446453 599 --ANVRSAeeeLEGISIqGA---LAKPINT 623
Cdd:cd17563 80 gyASIATA---VEAIKL-GAddyLAKPADA 105
|
|
| REC_Ycf29 |
cd19927 |
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ... |
519-599 |
6.43e-03 |
|
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a probable response regulator of a two-component system (TCS), typically consisting a sensor and a response regulator, that functions in adaptation to changing environments. Processes regulated by TCSs in bacteria include sporulation, pathogenicity, virulence, chemotaxis, and membrane transport. Ycf29 contains an N-terminal REC domain and a LuxR-type helix-turn-helix DNA-binding output domain. REC domains function as phosphorylation-mediated switches within RRs, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381154 [Multi-domain] Cd Length: 102 Bit Score: 36.97 E-value: 6.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 519 ILLVEDVPLNAEIATNLLEQRGHEVLWAETGEDALSFVETEDDLDLVLLDMqLPDINGDVVAKQIRSDSHFDKLPIVALT 598
Cdd:cd19927 1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQYIPDLIISDII-MPGVDGYSLLGKLRKNADFDTIPVIFLT 79
|
.
gi 746446453 599 A 599
Cdd:cd19927 80 A 80
|
|
| REC_CheY_CheY3 |
cd19923 |
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ... |
519-599 |
8.14e-03 |
|
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY family proteins; CheY family chemotaxis response regulators (RRs) comprise about 17% of bacterial RRs and almost half of all RRs in archaea. This subfamily contains Vibrio cholerae CheY3, Escherichia coli CheY, and similar CheY family RRs. CheY proteins control bacterial motility and participate in signaling phosphorelays and in protein-protein interactions. CheY RRs contain only the REC domain with no output/effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381150 [Multi-domain] Cd Length: 119 Bit Score: 36.93 E-value: 8.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 519 ILLVEDVPLNAEIATNLLEQRGHE-VLWAETGEDALS--------FVETEddldlvlldMQLPDINGDVVAKQIRSDSHF 589
Cdd:cd19923 3 VLVVDDFSTMRRIIKNLLKELGFNnVEEAEDGVDALEklkaggfdFVITD---------WNMPNMDGLELLKTIRADGAL 73
|
90
....*....|
gi 746446453 590 DKLPIVALTA 599
Cdd:cd19923 74 SHLPVLMVTA 83
|
|
| AmiR |
COG3707 |
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ... |
515-622 |
9.06e-03 |
|
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: 38.01 E-value: 9.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746446453 515 RGLYILLVEDVPLNAEIATNLLEQRGHEVL-WAETGEDALSFVEtEDDLDLVLLDMQLPDINGDVVAKQIRSDSHfdkLP 593
Cdd:COG3707 2 RGLRVLVVDDEPLRRADLREGLREAGYEVVaEAADGEDAVELVR-ELKPDLVIVDIDMPDRDGLEAARQISEERP---AP 77
|
90 100 110
....*....|....*....|....*....|..
gi 746446453 594 IVALTAnvRSAEEELEGISIQGALA---KPIN 622
Cdd:COG3707 78 VILLTA--YSDPELIERALEAGVSAylvKPLD 107
|
|
| |
