|
Name |
Accession |
Description |
Interval |
E-value |
| CheA |
COG0643 |
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms]; |
4-689 |
0e+00 |
|
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
Pssm-ID: 440408 [Multi-domain] Cd Length: 563 Bit Score: 562.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 4 ENEPMLEVYIFETTQNLEQLEQVIIYSEKNGGfSAEDVSEIFRFMHTIKGSSAMMLFNNIEMVAHSMEDIFYFIREQKPE 83
Cdd:COG0643 2 DMDELLEIFLEEARELLEQLEEGLLALEQDPD-DPELLNAIFRAAHTLKGSAGMLGLDALAELAHALEDLLDALRNGELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 84 gLNySAVSDLVLACVDFIKEEIDKIIQKNNADGDPSFLIESLKLFLDELRNLFGEEktqlkdpqkqqyyISQEKKQPSSS 163
Cdd:COG0643 81 -LT-PELIDLLLEALDALRALLDALEAGGEPPADISALLARLDASEEAIEEVVADE-------------VEISPPAPAAL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 164 Eanfyyhinvsyeddcmmeniraytlifgltelvdelyffpaditensetaeyirengfdiylkaaiedeeleaylnkil 243
Cdd:COG0643 146 E------------------------------------------------------------------------------- 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 244 yiekfsinnidktvfddfkkeqteiksvesfilnpneickPDLTPPPISFTEKNTKNDNVNAQKMISVNVDRLDNLMNLV 323
Cdd:COG0643 147 ----------------------------------------PAPAAAPPAEAAAAAAEAAAAASETVRVDVERLDRLMNLV 186
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 324 GELMITESMVTQCP-EVEVIESENFHKASIELHKITEELQDMVMSIRMVPLSTTFVKMNRIVRDMCKKLTREVILDLHGE 402
Cdd:COG0643 187 GELVITRARLEQLAeELEDESLRELEEALEQLSRLTRELQDGVMRLRMVPISTVFNRFPRMVRDLARELGKEVELVIEGE 266
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 403 ETEVDKNIIEHISDPLMHIIRNAIDHGIENESERLKKGKEKAGRIILEAKNIGSDVLIIIKDDGRGLDKIRIIEKAQQNG 482
Cdd:COG0643 267 ETELDRTVLERLGDPLVHLVRNAVDHGIETPEERLAAGKPETGTITLSAYHEGGRVVIEVSDDGRGLDLEKIRAKAIEKG 346
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 483 LLTK-SVEEMSDREIFKLILLPGFSTNESVTEFSGRGVGMDVVTKNIEAIGGTVLIDSEKDKGTIITLKIPLTLAIVEGM 561
Cdd:COG0643 347 LITAeEAAALSDEELLELIFAPGFSTAEEVTDLSGRGVGMDVVKTNIEALGGTIEIESEPGKGTTFTLRLPLTLAIIDGL 426
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 562 NIRVGRSRYTIPINTISESFRPEKKDcIIDPDDNEMVMIRGVCYPILRLHQYYHIKNAETDLTKGILIMVEQEEKVICIF 641
Cdd:COG0643 427 LVRVGGETYAIPLSSVEEVLRLDPDD-IETVEGREVIRLRGELLPLVRLGELLGLPGAEPEGERGPVVVVRSGGRRVALV 505
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 504122286 642 ADELLGQQQVVVKALPNYVNSIKnilGLAGCTLLPDGSISLIMDISGL 689
Cdd:COG0643 506 VDELLGQQEVVIKPLGPLLRRVP---GISGATILGDGRVALILDVAAL 550
|
|
| PRK10547 |
PRK10547 |
chemotaxis protein CheA; Provisional |
38-692 |
3.75e-113 |
|
chemotaxis protein CheA; Provisional
Pssm-ID: 236712 [Multi-domain] Cd Length: 670 Bit Score: 355.58 E-value: 3.75e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 38 AEDVSEIFRFMHTIKGSSAMMLFNNIEMVAHSMEDIFYFIREQKPEgLNySAVSDLVLACVDFIKEEID--KIIQKNNAd 115
Cdd:PRK10547 35 AEQLNAIFRAAHSIKGGAGTFGFTVLQETTHLMENLLDEARRGEMQ-LN-TDIINLFLETKDIMQEQLDayKTSQEPDA- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 116 gdpsfliESLKLFLDELRNLF----GEEKTQLKDPQKQQYyISQEKKQPSSSEANFYYHINVSyeddcmmeniraytlif 191
Cdd:PRK10547 112 -------ASFEYICQALRQLAleakGETPSAVTRLSVVAI-QEKSEPQDESPRSQSGLRIILS----------------- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 192 GLTE-----LVDELyffpADITENSETAEyiRENGFDIYLKAAIEDEELEAYLNKILYIEKFSinnidktvfddFKKEQT 266
Cdd:PRK10547 167 RLKAgevdlLEEEL----GNLGTLTDVVK--GADSLEATLPGSVAEDDITAVLCFVIEADQIT-----------FETAVA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 267 EIKSVESFILNPNEICKPDLTPP----PISFTEKNTKNDNVNAQKM----ISVNVDRLDNLMNLVGELMITESMVTQ-CP 337
Cdd:PRK10547 230 APQEKAEETTEVVEVSPKISVPPvlklAAEQAPAGRVEREKTARSSestsIRVAVEKVDQLINLVGELVITQSMLAQrSS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 338 EVEVIESENFHKASIELHKITEELQDMVMSIRMVPLSTTFVKMNRIVRDMCKKLTREVILDLHGEETEVDKNIIEHISDP 417
Cdd:PRK10547 310 ELDPVNHGDLITSMGQLQRNARDLQESVMSIRMMPMEYVFSRFPRLVRDLAGKLGKQVELTLVGSSTELDKSLIERIIDP 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 418 LMHIIRNAIDHGIENESERLKKGKEKAGRIILEAKNIGSDVLIIIKDDGRGLDKIRIIEKAQQNGLltkSVEE-MSDREI 496
Cdd:PRK10547 390 LTHLVRNSLDHGIELPEKRLAAGKNSVGNLILSAEHQGGNICIEVTDDGAGLNRERILAKAASQGL---AVSEnMSDEEV 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 497 FKLILLPGFSTNESVTEFSGRGVGMDVVTKNIEAIGGTVLIDSEKDKGTIITLKIPLTLAIVEGMNIRVGRSRYTIPINT 576
Cdd:PRK10547 467 GMLIFAPGFSTAEQVTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQGKGTTIRILLPLTLAILDGMSVRVADEVFILPLNA 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 577 ISESFRPEKKDCIIDPDDNEMVMIRGVCYPILRLHQYYHIKNAETDLTKGILIMVEQEEKVICIFADELLGQQQVVVKAL 656
Cdd:PRK10547 547 VMESLQPREEDLHPLAGGERVLEVRGEYLPLVELWKVFDVAGAKTEATQGIVVILQSAGRRYALLVDQLIGQHQVVVKNL 626
|
650 660 670
....*....|....*....|....*....|....*..
gi 504122286 657 -PNYvnsiKNILGLAGCTLLPDGSISLIMDISGLTGL 692
Cdd:PRK10547 627 eSNY----RKVPGISAATILGDGSVALIVDVSALQAL 659
|
|
| CheA_Halo |
NF041336 |
chemotaxis protein CheA; |
9-689 |
2.52e-103 |
|
chemotaxis protein CheA;
Pssm-ID: 469233 [Multi-domain] Cd Length: 666 Bit Score: 329.69 E-value: 2.52e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 9 LEVYIFETTQNLEQLEQVIIYSEKNGGfSAEDVSEIFRFMHTIKGSSAMMLFNNIEMVAHSMEDIFYFIREQKPEGLnyS 88
Cdd:NF041336 5 LDAFVRESEEAITELNNSLLELESDPE-NEEAMETIFRTAHTLKGNFGAMGFDDASNLAHAIEDLLDEIRQGELAVT--P 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 89 AVSDLVLACVDFIKEEIDKIIQKNNADGDPSFLIESLKLFLDELRNLFGEEKTQLKDPQKQQYYISQEKKQPSSSEANFY 168
Cdd:NF041336 82 ERMDLIFEGVDQLEAIVDEIEADGETQTDPEATIEEIRASIEEGADAGASGAVEDGDAGDSSADDGIVDADVVVDDVVVP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 169 --------YHINVSYEDDcMMENIRAYTLIFGLTELVDELYFFPADitENSETAEYirENGFDIYL--KAAIEDEELEAY 238
Cdd:NF041336 162 elaadgevYHARVEIGDS-DMPGVDAMLVLEAIEDEFDLLGTVPDR--DAIEDGEF--EDTFDLYVatDNDVDSDDVEAF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 239 LNKILYIEKFSINNIDKTVFDDFKKEQTEIKSvesfilnpneickPDLTPPPISFTEKNTKNDNVNAQKMISVNVDRLDN 318
Cdd:NF041336 237 YELNGYVDTVDVEDVTDEVAAGDLKDGPTEDD-------------DDAGADTDDSGSSSSMAHSVQEIESVRVDVDQLDQ 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 319 LMNLVgelmitESMVTQCPEVE-VIESENFHKASI---ELHKITEELQDMVMSIRMVPLSTTFVKMNRIVRDMCKKLTRE 394
Cdd:NF041336 304 LYGLV------EQLVTSRIKLRrAVEEEDLVSAEDeleELGKITASLQDTVMDMRLVPLKKIVGKFPRLVRDLARDQGKE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 395 VILDLHGEETEVDKNIIEHISDPLMHIIRNAIDHGIENESERLKKGKEKAGRIILEAKNIGSDVLIIIKDDGRGLDKIRI 474
Cdd:NF041336 378 IDFTIEGEDIELDRTILTELSDPLMHLLRNAVDHGIEPPEEREAKGKPREGTIELRAERERDHVSITVEDDGAGLDVEEI 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 475 IEKAQQNGLLTKS-VEEMSDREIFKLILLPGFSTNESVTEFSGRGVGMDVVTKNIEAIGGTVLIDSEKDKGTIITLKIPL 553
Cdd:NF041336 458 REKAIEKGVKTEEeLEAMDDSEVYDLVFHPGFSTTEEVTDVSGRGVGMDVVHQTVRGLDGSVNVESEPGEGTTVTLRLPV 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 554 TLAIVEGMNIRVGRSRYTIPINTISESFRPEKKDCIidpDDNEMVMIRGVCYPILRLHQYYHIKNAETDlTKGILIMVEQ 633
Cdd:NF041336 538 TVAIVKVLFVTVGDEEYGIPIKNVDEISRLEDVETV---NGREVITHDDEIYPLVSLGDALDVPGETRN-GDGMLVRIRE 613
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 504122286 634 EEKVICIFADELLGQQQVVVKALPNYVNsikNILGLAGCTLLPDGSISLIMDISGL 689
Cdd:NF041336 614 SERQVALHCDDVVGQEEVVVKPFEGILS---GTPGLSGTAVLGDGEVVHILDVVTL 666
|
|
| HATPase_CheA-like |
cd16916 |
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ... |
377-552 |
6.93e-82 |
|
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: 257.13 E-value: 6.93e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 377 FVKMNRIVRDMCKKLTREVILDLHGEETEVDKNIIEHISDPLMHIIRNAIDHGIENESERLKKGKEKAGRIILEAKNIGS 456
Cdd:cd16916 2 FSRFPRLVRDLARELGKQVELVVEGEDTELDKSVLEKLADPLTHLLRNAVDHGIEAPEERLAAGKPPEGTITLRAEHQGN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 457 DVLIIIKDDGRGLDKIRIIEKAQQNGLLT-KSVEEMSDREIFKLILLPGFSTNESVTEFSGRGVGMDVVTKNIEAIGGTV 535
Cdd:cd16916 82 QVVIEVSDDGRGIDREKIREKAIERGLITaDEAATLSDDEVLNLIFAPGFSTAEQVTDVSGRGVGMDVVKRSIESLGGTI 161
|
170
....*....|....*..
gi 504122286 536 LIDSEKDKGTIITLKIP 552
Cdd:cd16916 162 EVESEPGQGTTFTIRLP 178
|
|
| HATPase_c |
smart00387 |
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases. |
416-554 |
4.68e-20 |
|
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
Pssm-ID: 214643 [Multi-domain] Cd Length: 111 Bit Score: 85.78 E-value: 4.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 416 DPLMHIIRNAIDHGIENeserlkkgKEKAGRIILEAKNIGSDVLIIIKDDGRGLDKiriiekaqqnglltksveemsdrE 495
Cdd:smart00387 4 DRLRQVLSNLLDNAIKY--------TPEGGRITVTLERDGDHVEITVEDNGPGIPP-----------------------E 52
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 504122286 496 IFKLILLPGFSTNESVTEFSGRGVGMDVVTKNIEAIGGTVLIDSEKDKGTIITLKIPLT 554
Cdd:smart00387 53 DLEKIFEPFFRTDKRSRKIGGTGLGLSIVKKLVELHGGEISVESEPGGGTTFTITLPLE 111
|
|
| CheW |
pfam01584 |
CheW-like domain; CheW proteins are part of the chemotaxis signaling mechanism in bacteria. ... |
560-689 |
5.37e-15 |
|
CheW-like domain; CheW proteins are part of the chemotaxis signaling mechanism in bacteria. CheW interacts with the methyl accepting chemotaxis proteins (MCPs) and relays signals to CheY, which affects flageller rotation. This family includes CheW and other related proteins that are involved in chemotaxis. The CheW-like regulatory domain in CheA binds to CheW, suggesting that these domains can interact with each other.
Pssm-ID: 460257 [Multi-domain] Cd Length: 131 Bit Score: 72.23 E-value: 5.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 560 GMNIRVGRSRYTIPINTISESFRPEKKDCIIDPDDN--EMVMIRGVCYPILRLHQYYHIKNAETDlTKGILIMVEQEEKV 637
Cdd:pfam01584 1 GLLFRLGGETFAIPISKVREILRPPPITPIPGAPGYvlGVINLRGEVLPVIDLRRLLGLPPTEPR-ERTRVVVVEVGGQV 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 504122286 638 ICIFADELLGQQQVVVKALPNYVNSIKNILGLAGCTLLPDGSISLIMDISGL 689
Cdd:pfam01584 80 VGLLVDEVIGVLEIVIKQIEPPLGLGRVAGYISGATILGDGRVVLILDVEAL 131
|
|
| P2 |
pfam07194 |
P2 response regulator binding domain; The response regulators for CheA bind to the P2 domain, ... |
169-251 |
1.06e-09 |
|
P2 response regulator binding domain; The response regulators for CheA bind to the P2 domain, which is found between pfam01627 and pfam02895 as either one or two copies. Highly flexible linkers connect P2 to the rest of CheA and impart remarkable mobility to the P2 domain. This feature is thought to enhance the inter CheA dimer phosphotransfer reactions within the signalling complex, thereby amplifying the phosphorylation signal.
Pssm-ID: 462116 [Multi-domain] Cd Length: 80 Bit Score: 55.21 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 169 YHINVSYEDDCMMENIRAYTLIFGLTELVDELYFFPAdiTENSETAEYirENGFDIYLKAAIEDEELEAYLNKILYIEKF 248
Cdd:pfam07194 1 YEITVTLDEDCLMKAVRAFLVFKALEELGEIIKSIPS--VEDIEDEKF--DGGFEVVLVTKESAEEIEEALLNISEIEEV 76
|
...
gi 504122286 249 SIN 251
Cdd:pfam07194 77 EVE 79
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CheA |
COG0643 |
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms]; |
4-689 |
0e+00 |
|
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
Pssm-ID: 440408 [Multi-domain] Cd Length: 563 Bit Score: 562.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 4 ENEPMLEVYIFETTQNLEQLEQVIIYSEKNGGfSAEDVSEIFRFMHTIKGSSAMMLFNNIEMVAHSMEDIFYFIREQKPE 83
Cdd:COG0643 2 DMDELLEIFLEEARELLEQLEEGLLALEQDPD-DPELLNAIFRAAHTLKGSAGMLGLDALAELAHALEDLLDALRNGELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 84 gLNySAVSDLVLACVDFIKEEIDKIIQKNNADGDPSFLIESLKLFLDELRNLFGEEktqlkdpqkqqyyISQEKKQPSSS 163
Cdd:COG0643 81 -LT-PELIDLLLEALDALRALLDALEAGGEPPADISALLARLDASEEAIEEVVADE-------------VEISPPAPAAL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 164 Eanfyyhinvsyeddcmmeniraytlifgltelvdelyffpaditensetaeyirengfdiylkaaiedeeleaylnkil 243
Cdd:COG0643 146 E------------------------------------------------------------------------------- 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 244 yiekfsinnidktvfddfkkeqteiksvesfilnpneickPDLTPPPISFTEKNTKNDNVNAQKMISVNVDRLDNLMNLV 323
Cdd:COG0643 147 ----------------------------------------PAPAAAPPAEAAAAAAEAAAAASETVRVDVERLDRLMNLV 186
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 324 GELMITESMVTQCP-EVEVIESENFHKASIELHKITEELQDMVMSIRMVPLSTTFVKMNRIVRDMCKKLTREVILDLHGE 402
Cdd:COG0643 187 GELVITRARLEQLAeELEDESLRELEEALEQLSRLTRELQDGVMRLRMVPISTVFNRFPRMVRDLARELGKEVELVIEGE 266
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 403 ETEVDKNIIEHISDPLMHIIRNAIDHGIENESERLKKGKEKAGRIILEAKNIGSDVLIIIKDDGRGLDKIRIIEKAQQNG 482
Cdd:COG0643 267 ETELDRTVLERLGDPLVHLVRNAVDHGIETPEERLAAGKPETGTITLSAYHEGGRVVIEVSDDGRGLDLEKIRAKAIEKG 346
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 483 LLTK-SVEEMSDREIFKLILLPGFSTNESVTEFSGRGVGMDVVTKNIEAIGGTVLIDSEKDKGTIITLKIPLTLAIVEGM 561
Cdd:COG0643 347 LITAeEAAALSDEELLELIFAPGFSTAEEVTDLSGRGVGMDVVKTNIEALGGTIEIESEPGKGTTFTLRLPLTLAIIDGL 426
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 562 NIRVGRSRYTIPINTISESFRPEKKDcIIDPDDNEMVMIRGVCYPILRLHQYYHIKNAETDLTKGILIMVEQEEKVICIF 641
Cdd:COG0643 427 LVRVGGETYAIPLSSVEEVLRLDPDD-IETVEGREVIRLRGELLPLVRLGELLGLPGAEPEGERGPVVVVRSGGRRVALV 505
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 504122286 642 ADELLGQQQVVVKALPNYVNSIKnilGLAGCTLLPDGSISLIMDISGL 689
Cdd:COG0643 506 VDELLGQQEVVIKPLGPLLRRVP---GISGATILGDGRVALILDVAAL 550
|
|
| PRK10547 |
PRK10547 |
chemotaxis protein CheA; Provisional |
38-692 |
3.75e-113 |
|
chemotaxis protein CheA; Provisional
Pssm-ID: 236712 [Multi-domain] Cd Length: 670 Bit Score: 355.58 E-value: 3.75e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 38 AEDVSEIFRFMHTIKGSSAMMLFNNIEMVAHSMEDIFYFIREQKPEgLNySAVSDLVLACVDFIKEEID--KIIQKNNAd 115
Cdd:PRK10547 35 AEQLNAIFRAAHSIKGGAGTFGFTVLQETTHLMENLLDEARRGEMQ-LN-TDIINLFLETKDIMQEQLDayKTSQEPDA- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 116 gdpsfliESLKLFLDELRNLF----GEEKTQLKDPQKQQYyISQEKKQPSSSEANFYYHINVSyeddcmmeniraytlif 191
Cdd:PRK10547 112 -------ASFEYICQALRQLAleakGETPSAVTRLSVVAI-QEKSEPQDESPRSQSGLRIILS----------------- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 192 GLTE-----LVDELyffpADITENSETAEyiRENGFDIYLKAAIEDEELEAYLNKILYIEKFSinnidktvfddFKKEQT 266
Cdd:PRK10547 167 RLKAgevdlLEEEL----GNLGTLTDVVK--GADSLEATLPGSVAEDDITAVLCFVIEADQIT-----------FETAVA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 267 EIKSVESFILNPNEICKPDLTPP----PISFTEKNTKNDNVNAQKM----ISVNVDRLDNLMNLVGELMITESMVTQ-CP 337
Cdd:PRK10547 230 APQEKAEETTEVVEVSPKISVPPvlklAAEQAPAGRVEREKTARSSestsIRVAVEKVDQLINLVGELVITQSMLAQrSS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 338 EVEVIESENFHKASIELHKITEELQDMVMSIRMVPLSTTFVKMNRIVRDMCKKLTREVILDLHGEETEVDKNIIEHISDP 417
Cdd:PRK10547 310 ELDPVNHGDLITSMGQLQRNARDLQESVMSIRMMPMEYVFSRFPRLVRDLAGKLGKQVELTLVGSSTELDKSLIERIIDP 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 418 LMHIIRNAIDHGIENESERLKKGKEKAGRIILEAKNIGSDVLIIIKDDGRGLDKIRIIEKAQQNGLltkSVEE-MSDREI 496
Cdd:PRK10547 390 LTHLVRNSLDHGIELPEKRLAAGKNSVGNLILSAEHQGGNICIEVTDDGAGLNRERILAKAASQGL---AVSEnMSDEEV 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 497 FKLILLPGFSTNESVTEFSGRGVGMDVVTKNIEAIGGTVLIDSEKDKGTIITLKIPLTLAIVEGMNIRVGRSRYTIPINT 576
Cdd:PRK10547 467 GMLIFAPGFSTAEQVTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQGKGTTIRILLPLTLAILDGMSVRVADEVFILPLNA 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 577 ISESFRPEKKDCIIDPDDNEMVMIRGVCYPILRLHQYYHIKNAETDLTKGILIMVEQEEKVICIFADELLGQQQVVVKAL 656
Cdd:PRK10547 547 VMESLQPREEDLHPLAGGERVLEVRGEYLPLVELWKVFDVAGAKTEATQGIVVILQSAGRRYALLVDQLIGQHQVVVKNL 626
|
650 660 670
....*....|....*....|....*....|....*..
gi 504122286 657 -PNYvnsiKNILGLAGCTLLPDGSISLIMDISGLTGL 692
Cdd:PRK10547 627 eSNY----RKVPGISAATILGDGSVALIVDVSALQAL 659
|
|
| CheA_Halo |
NF041336 |
chemotaxis protein CheA; |
9-689 |
2.52e-103 |
|
chemotaxis protein CheA;
Pssm-ID: 469233 [Multi-domain] Cd Length: 666 Bit Score: 329.69 E-value: 2.52e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 9 LEVYIFETTQNLEQLEQVIIYSEKNGGfSAEDVSEIFRFMHTIKGSSAMMLFNNIEMVAHSMEDIFYFIREQKPEGLnyS 88
Cdd:NF041336 5 LDAFVRESEEAITELNNSLLELESDPE-NEEAMETIFRTAHTLKGNFGAMGFDDASNLAHAIEDLLDEIRQGELAVT--P 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 89 AVSDLVLACVDFIKEEIDKIIQKNNADGDPSFLIESLKLFLDELRNLFGEEKTQLKDPQKQQYYISQEKKQPSSSEANFY 168
Cdd:NF041336 82 ERMDLIFEGVDQLEAIVDEIEADGETQTDPEATIEEIRASIEEGADAGASGAVEDGDAGDSSADDGIVDADVVVDDVVVP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 169 --------YHINVSYEDDcMMENIRAYTLIFGLTELVDELYFFPADitENSETAEYirENGFDIYL--KAAIEDEELEAY 238
Cdd:NF041336 162 elaadgevYHARVEIGDS-DMPGVDAMLVLEAIEDEFDLLGTVPDR--DAIEDGEF--EDTFDLYVatDNDVDSDDVEAF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 239 LNKILYIEKFSINNIDKTVFDDFKKEQTEIKSvesfilnpneickPDLTPPPISFTEKNTKNDNVNAQKMISVNVDRLDN 318
Cdd:NF041336 237 YELNGYVDTVDVEDVTDEVAAGDLKDGPTEDD-------------DDAGADTDDSGSSSSMAHSVQEIESVRVDVDQLDQ 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 319 LMNLVgelmitESMVTQCPEVE-VIESENFHKASI---ELHKITEELQDMVMSIRMVPLSTTFVKMNRIVRDMCKKLTRE 394
Cdd:NF041336 304 LYGLV------EQLVTSRIKLRrAVEEEDLVSAEDeleELGKITASLQDTVMDMRLVPLKKIVGKFPRLVRDLARDQGKE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 395 VILDLHGEETEVDKNIIEHISDPLMHIIRNAIDHGIENESERLKKGKEKAGRIILEAKNIGSDVLIIIKDDGRGLDKIRI 474
Cdd:NF041336 378 IDFTIEGEDIELDRTILTELSDPLMHLLRNAVDHGIEPPEEREAKGKPREGTIELRAERERDHVSITVEDDGAGLDVEEI 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 475 IEKAQQNGLLTKS-VEEMSDREIFKLILLPGFSTNESVTEFSGRGVGMDVVTKNIEAIGGTVLIDSEKDKGTIITLKIPL 553
Cdd:NF041336 458 REKAIEKGVKTEEeLEAMDDSEVYDLVFHPGFSTTEEVTDVSGRGVGMDVVHQTVRGLDGSVNVESEPGEGTTVTLRLPV 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 554 TLAIVEGMNIRVGRSRYTIPINTISESFRPEKKDCIidpDDNEMVMIRGVCYPILRLHQYYHIKNAETDlTKGILIMVEQ 633
Cdd:NF041336 538 TVAIVKVLFVTVGDEEYGIPIKNVDEISRLEDVETV---NGREVITHDDEIYPLVSLGDALDVPGETRN-GDGMLVRIRE 613
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 504122286 634 EEKVICIFADELLGQQQVVVKALPNYVNsikNILGLAGCTLLPDGSISLIMDISGL 689
Cdd:NF041336 614 SERQVALHCDDVVGQEEVVVKPFEGILS---GTPGLSGTAVLGDGEVVHILDVVTL 666
|
|
| HATPase_CheA-like |
cd16916 |
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ... |
377-552 |
6.93e-82 |
|
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: 257.13 E-value: 6.93e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 377 FVKMNRIVRDMCKKLTREVILDLHGEETEVDKNIIEHISDPLMHIIRNAIDHGIENESERLKKGKEKAGRIILEAKNIGS 456
Cdd:cd16916 2 FSRFPRLVRDLARELGKQVELVVEGEDTELDKSVLEKLADPLTHLLRNAVDHGIEAPEERLAAGKPPEGTITLRAEHQGN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 457 DVLIIIKDDGRGLDKIRIIEKAQQNGLLT-KSVEEMSDREIFKLILLPGFSTNESVTEFSGRGVGMDVVTKNIEAIGGTV 535
Cdd:cd16916 82 QVVIEVSDDGRGIDREKIREKAIERGLITaDEAATLSDDEVLNLIFAPGFSTAEQVTDVSGRGVGMDVVKRSIESLGGTI 161
|
170
....*....|....*..
gi 504122286 536 LIDSEKDKGTIITLKIP 552
Cdd:cd16916 162 EVESEPGQGTTFTIRLP 178
|
|
| CheA_reg |
cd00731 |
CheA regulatory domain; CheA is a histidine protein kinase present in bacteria and archea. ... |
555-689 |
1.93e-27 |
|
CheA regulatory domain; CheA is a histidine protein kinase present in bacteria and archea. Activated by the chemotaxis receptor a histidine phosphoryl group from CheA is passed directly to an aspartate in the response regulator CheY. This signalling mechanism is modulated by the methyl accepting chemotaxis proteins (MCPs). MCPs form a highly interconnected, tightly packed array within the membrane that is organized, at least in part, through interactions with CheW and CheA. The CheA regulatory domain belongs to the family of CheW_like proteins and has been proposed to mediate interaction with the kinase regulator CheW.
Pssm-ID: 238373 [Multi-domain] Cd Length: 132 Bit Score: 107.65 E-value: 1.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 555 LAIVEGMNIRVGRSRYTIPINTISESFRPEKKDciIDPDDN--EMVMIRGVCYPILRLHQYYHIKNAETDLTKGILIMVE 632
Cdd:cd00731 1 LAIIKGLLVRVGDETYAIPLSAVVETVRIKPKD--IKRVDGgkEVINVRGELLPLVRLGELFNVRGENEEPDEGVVVVVR 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 504122286 633 QEEKVICIFADELLGQQQVVVKALPNYvnsIKNILGLAGCTLLPDGSISLIMDISGL 689
Cdd:cd00731 79 TGGRKAALVVDQIIGQEEVVIKPLGGF---LSNIPGISGATILGDGRVALILDVPAL 132
|
|
| HATPase_c |
smart00387 |
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases. |
416-554 |
4.68e-20 |
|
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
Pssm-ID: 214643 [Multi-domain] Cd Length: 111 Bit Score: 85.78 E-value: 4.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 416 DPLMHIIRNAIDHGIENeserlkkgKEKAGRIILEAKNIGSDVLIIIKDDGRGLDKiriiekaqqnglltksveemsdrE 495
Cdd:smart00387 4 DRLRQVLSNLLDNAIKY--------TPEGGRITVTLERDGDHVEITVEDNGPGIPP-----------------------E 52
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 504122286 496 IFKLILLPGFSTNESVTEFSGRGVGMDVVTKNIEAIGGTVLIDSEKDKGTIITLKIPLT 554
Cdd:smart00387 53 DLEKIFEPFFRTDKRSRKIGGTGLGLSIVKKLVELHGGEISVESEPGGGTTFTITLPLE 111
|
|
| CheW |
pfam01584 |
CheW-like domain; CheW proteins are part of the chemotaxis signaling mechanism in bacteria. ... |
560-689 |
5.37e-15 |
|
CheW-like domain; CheW proteins are part of the chemotaxis signaling mechanism in bacteria. CheW interacts with the methyl accepting chemotaxis proteins (MCPs) and relays signals to CheY, which affects flageller rotation. This family includes CheW and other related proteins that are involved in chemotaxis. The CheW-like regulatory domain in CheA binds to CheW, suggesting that these domains can interact with each other.
Pssm-ID: 460257 [Multi-domain] Cd Length: 131 Bit Score: 72.23 E-value: 5.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 560 GMNIRVGRSRYTIPINTISESFRPEKKDCIIDPDDN--EMVMIRGVCYPILRLHQYYHIKNAETDlTKGILIMVEQEEKV 637
Cdd:pfam01584 1 GLLFRLGGETFAIPISKVREILRPPPITPIPGAPGYvlGVINLRGEVLPVIDLRRLLGLPPTEPR-ERTRVVVVEVGGQV 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 504122286 638 ICIFADELLGQQQVVVKALPNYVNSIKNILGLAGCTLLPDGSISLIMDISGL 689
Cdd:pfam01584 80 VGLLVDEVIGVLEIVIKQIEPPLGLGRVAGYISGATILGDGRVVLILDVEAL 131
|
|
| HPT |
cd00088 |
Histidine Phosphotransfer domain, involved in signalling through a two part component systems ... |
6-106 |
1.74e-14 |
|
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: 69.33 E-value: 1.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 6 EPMLEVYIFETTQNLEQLEQVIIYSEknggfSAEDVSEIFRFMHTIKGSSAMMLFNNIEMVAHSMEDIFYFIREQKPEGl 85
Cdd:cd00088 2 EELLELFLEEAEELLEELERALLELE-----DAEDLNEIFRAAHTLKGSAASLGLQRLAQLAHQLEDLLDALRDGLEVT- 75
|
90 100
....*....|....*....|.
gi 504122286 86 nySAVSDLVLACVDFIKEEID 106
Cdd:cd00088 76 --PELIDLLLDALDALKAELE 94
|
|
| CheW_like |
cd00588 |
CheW-like domain. CheW proteins are part of the chemotaxis signalling mechanism in bacteria. ... |
557-689 |
2.87e-14 |
|
CheW-like domain. CheW proteins are part of the chemotaxis signalling mechanism in bacteria. CheW interacts with the methyl accepting chemotaxis proteins (MCPs) and relays signals to CheY, which affects flageller rotation. This family includes CheW and other related proteins that are involved in chemotaxis. The CheW-like regulatory domain in the chemotaxis associated histidine kinase CheA binds to CheW, suggesting that these domains can interact with each other.
Pssm-ID: 238331 Cd Length: 136 Bit Score: 70.00 E-value: 2.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 557 IVEGMNIRVGRSRYTIPINTIsESFRPEKKDCII---DPDDNEMVMIRGVCYPILRLHQYYHIKNAETDLTKGILIMVEQ 633
Cdd:cd00588 1 ILQVLLFRVGDELYAIPIAVV-EEILPLPPITRVpnaPDYVLGVINLRGEILPVIDLRRLFGLEAAEPDTDETRIVVVEV 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 504122286 634 EEKVICIFADELLGQQQVVVKAL-PNYVNSIKNILGLAGCTLLPDGSISLIMDISGL 689
Cdd:cd00588 80 GDRKVGLVVDSVLGVLEVVIKDIePPPDVGSSNAPGISGATILGDGRVVLILDVDKL 136
|
|
| HATPase_c |
pfam02518 |
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ... |
415-554 |
7.56e-13 |
|
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: 65.08 E-value: 7.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 415 SDPLMHIIRNAIDHGIENeserlkKGKEKAGRIILEAKNigsDVLIIIKDDGRGLDKIRIiekaqqnglltksveemsdR 494
Cdd:pfam02518 3 ELRLRQVLSNLLDNALKH------AAKAGEITVTLSEGG---ELTLTVEDNGIGIPPEDL-------------------P 54
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 495 EIFKlillpGFSTNESvTEFSGRGVGMDVVTKNIEAIGGTVLIDSEKDKGTIITLKIPLT 554
Cdd:pfam02518 55 RIFE-----PFSTADK-RGGGGTGLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLPLA 108
|
|
| H-kinase_dim |
pfam02895 |
Signal transducing histidine kinase, homodimeric domain; This helical bundle domain is the ... |
309-368 |
1.24e-12 |
|
Signal transducing histidine kinase, homodimeric domain; This helical bundle domain is the homodimer interface of the signal transducing histidine kinase family.
Pssm-ID: 427045 [Multi-domain] Cd Length: 66 Bit Score: 63.03 E-value: 1.24e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504122286 309 ISVNVDRLDNLMNLVGELMITESMVTQCPE-VEVIES----ENFHKASIELHKITEELQDMVMSI 368
Cdd:pfam02895 2 IRVDVEKLDRLMNLVGELVIARNRLVQLLErLEEYGGdtllEELKEALQQLDRLTRELQEAVMKI 66
|
|
| BaeS |
COG0642 |
Signal transduction histidine kinase [Signal transduction mechanisms]; |
348-554 |
3.01e-12 |
|
Signal transduction histidine kinase [Signal transduction mechanisms];
Pssm-ID: 440407 [Multi-domain] Cd Length: 328 Bit Score: 68.40 E-value: 3.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 348 HKASIELHKITEELQDMV-MSIRMVPLSTTFVKMNRIVRDMCKKLTR-------EVILDLHGEETEV--DKNIIEHIsdp 417
Cdd:COG0642 151 LRSADRLLRLINDLLDLSrLEAGKLELEPEPVDLAELLEEVVELFRPlaeekgiELELDLPDDLPTVrgDPDRLRQV--- 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 418 LMHIIRNAIDHGieneserlkkgkEKAGRIILEAKNIGSDVLIIIKDDGRGLDkiriiekaqqnglltksvEEMSDReIF 497
Cdd:COG0642 228 LLNLLSNAIKYT------------PEGGTVTVSVRREGDRVRISVEDTGPGIP------------------PEDLER-IF 276
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504122286 498 KlillPGFSTNESvTEFSGRGVGMDVVTKNIEAIGGTVLIDSEKDKGTIITLKIPLT 554
Cdd:COG0642 277 E----PFFRTDPS-RRGGGTGLGLAIVKRIVELHGGTIEVESEPGKGTTFTVTLPLA 328
|
|
| KdpD |
COG2205 |
K+-sensing histidine kinase KdpD [Signal transduction mechanisms]; |
348-554 |
5.15e-12 |
|
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
Pssm-ID: 441807 [Multi-domain] Cd Length: 239 Bit Score: 66.08 E-value: 5.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 348 HKASIELHKITEELQDMV-MSIRMVPLSTTFVKMNRIVRDMCKKLT-------REVILDLHGEETEV--DKNIIEHIsdp 417
Cdd:COG2205 60 RESAERLLRLIEDLLDLSrLESGKLSLELEPVDLAELLEEAVEELRplaeekgIRLELDLPPELPLVyaDPELLEQV--- 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 418 LMHIIRNAIDHGIENeserlkkgkekaGRIILEAKNIGSDVLIIIKDDGRGldkiriIEKAQQNglltksveemsdrEIF 497
Cdd:COG2205 137 LANLLDNAIKYSPPG------------GTITISARREGDGVRISVSDNGPG------IPEEELE-------------RIF 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504122286 498 KLillpgFSTNESVTEFSGRGVGMDVVTKNIEAIGGTVLIDSEKDKGTIITLKIPLT 554
Cdd:COG2205 186 ER-----FYRGDNSRGEGGTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFTVTLPLA 237
|
|
| HPT |
smart00073 |
Histidine Phosphotransfer domain; Contains an active histidine residue that mediates ... |
8-102 |
2.35e-11 |
|
Histidine Phosphotransfer domain; Contains an active histidine residue that mediates phosphotransfer reactions. Domain detected only in eubacteria. This alignment is an extension to that shown in the Cell structure paper.
Pssm-ID: 197502 [Multi-domain] Cd Length: 92 Bit Score: 60.34 E-value: 2.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 8 MLEVYIFETTQNLEQLEQVIIYSEKNGGfsAEDVSEIFRFMHTIKGSSAMMLFNNIEMVAHSMEDIFYFIREQKPEGLNY 87
Cdd:smart00073 2 GLELFREELAEFLQSLEEGLLELEKALD--AQDVNEIFRAAHTLKGSAGSLGLQQLAQLCHQLENLLDALRSGEVELTPD 79
|
90
....*....|....*
gi 504122286 88 saVSDLVLACVDFIK 102
Cdd:smart00073 80 --LLDLLLELVDVLK 92
|
|
| P2 |
pfam07194 |
P2 response regulator binding domain; The response regulators for CheA bind to the P2 domain, ... |
169-251 |
1.06e-09 |
|
P2 response regulator binding domain; The response regulators for CheA bind to the P2 domain, which is found between pfam01627 and pfam02895 as either one or two copies. Highly flexible linkers connect P2 to the rest of CheA and impart remarkable mobility to the P2 domain. This feature is thought to enhance the inter CheA dimer phosphotransfer reactions within the signalling complex, thereby amplifying the phosphorylation signal.
Pssm-ID: 462116 [Multi-domain] Cd Length: 80 Bit Score: 55.21 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 169 YHINVSYEDDCMMENIRAYTLIFGLTELVDELYFFPAdiTENSETAEYirENGFDIYLKAAIEDEELEAYLNKILYIEKF 248
Cdd:pfam07194 1 YEITVTLDEDCLMKAVRAFLVFKALEELGEIIKSIPS--VEDIEDEKF--DGGFEVVLVTKESAEEIEEALLNISEIEEV 76
|
...
gi 504122286 249 SIN 251
Cdd:pfam07194 77 EVE 79
|
|
| Hpt |
pfam01627 |
Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module ... |
8-110 |
1.32e-09 |
|
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: 55.05 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 8 MLEVYIFETTQNLEQLEQVIiyseknggfSAEDVSEIFRFMHTIKGSSAMMLFNNIEMVAHSMEDIFyfiREQKpeglny 87
Cdd:pfam01627 2 LLELFLEEAPELLEQLEQAL---------DAEDLEALFRAAHTLKGSAGSLGLPALAELAHELEDLL---REGE------ 63
|
90 100
....*....|....*....|...
gi 504122286 88 savSDLVLACVDFIKEEIDKIIQ 110
Cdd:pfam01627 64 ---LPLDPELLEALRDLLEALRA 83
|
|
| NtrY |
COG5000 |
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
359-554 |
2.45e-09 |
|
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: 59.98 E-value: 2.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 359 EELQDMVMSI----RMVPLSTTFVKMNRIVRDM-------CKKLTREVILDLHGEETEV--DKNIIEHIsdpLMHIIRNA 425
Cdd:COG5000 253 DRLKRIVDEFldfaRLPEPQLEPVDLNELLREVlalyepaLKEKDIRLELDLDPDLPEVlaDRDQLEQV---LINLLKNA 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 426 IDHGieneserlkkgkEKAGRIILEAKNIGSDVLIIIKDDGRGLDkiriiekaqqnglltksvEEMSDReifklILLPGF 505
Cdd:COG5000 330 IEAI------------EEGGEIEVSTRREDGRVRIEVSDNGPGIP------------------EEVLER-----IFEPFF 374
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 504122286 506 STNESvtefsGRGVGMDVVTKNIEAIGGTVLIDSEKDKGTIITLKIPLT 554
Cdd:COG5000 375 TTKPK-----GTGLGLAIVKKIVEEHGGTIELESRPGGGTTFTIRLPLA 418
|
|
| CitA |
COG3290 |
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ... |
421-556 |
1.09e-08 |
|
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction mechanisms];
Pssm-ID: 442519 [Multi-domain] Cd Length: 389 Bit Score: 57.94 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 421 IIRNAIDHgieneserLKKGKEKAGRIILEAKNIGSDVLIIIKDDGRGLDKiriiekaqqnglltksveemsdrEIFKLI 500
Cdd:COG3290 289 LLDNAIEA--------VEKLPEEERRVELSIRDDGDELVIEVEDSGPGIPE-----------------------ELLEKI 337
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 504122286 501 LLPGFSTNESvtefSGRGVGMDVVTKNIEAIGGTVLIDSEKDKGTIITLKIPLTLA 556
Cdd:COG3290 338 FERGFSTKLG----EGRGLGLALVKQIVEKYGGTIEVESEEGEGTVFTVRLPKEGE 389
|
|
| COG4191 |
COG4191 |
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ... |
382-554 |
1.46e-08 |
|
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal transduction mechanisms];
Pssm-ID: 443345 [Multi-domain] Cd Length: 361 Bit Score: 57.12 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 382 RIVRDMCKKLTREVILDLHGEETEV--DKNIIEHIsdpLMHIIRNAIDhGIENESErlkkgkekaGRIILEAKNIGSDVL 459
Cdd:COG4191 226 ELLRPRLKARGIEVELDLPPDLPPVlgDPGQLEQV---LLNLLINAID-AMEEGEG---------GRITISTRREGDYVV 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 460 IIIKDDGRGLDkiriiekaqqnglltksvEEMSDReIFKlillPGFSTNEsvtEFSGRGVGMDVVTKNIEAIGGTVLIDS 539
Cdd:COG4191 293 ISVRDNGPGIP------------------PEVLER-IFE----PFFTTKP---VGKGTGLGLSISYGIVEKHGGRIEVES 346
|
170
....*....|....*
gi 504122286 540 EKDKGTIITLKIPLT 554
Cdd:COG4191 347 EPGGGTTFTITLPLA 361
|
|
| ComP |
COG4585 |
Signal transduction histidine kinase ComP [Signal transduction mechanisms]; |
359-554 |
4.29e-06 |
|
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
Pssm-ID: 443642 [Multi-domain] Cd Length: 252 Bit Score: 48.85 E-value: 4.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 359 EELQDMVMSIRmvPLSTTFVKMNRIVRDMCKKLTR----EVILDLHGEETEVDKNIIEHisdpLMHIIR----NAIDHGi 430
Cdd:COG4585 106 AELRRLVRGLR--PPALDDLGLAAALEELAERLLRaagiRVELDVDGDPDRLPPEVELA----LYRIVQealtNALKHA- 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 431 eneserlkkgkeKAGRIILEAKNIGSDVLIIIKDDGRGLDKIRIieKAQQNGLLTksveeMSDReifklillpgfstnes 510
Cdd:COG4585 179 ------------GATRVTVTLEVDDGELTLTVRDDGVGFDPEAA--PGGGLGLRG-----MRER---------------- 223
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 504122286 511 vtefsgrgvgmdvvtknIEAIGGTVLIDSEKDKGTIITLKIPLT 554
Cdd:COG4585 224 -----------------AEALGGTLTIGSAPGGGTRVRATLPLA 250
|
|
| WalK |
COG5002 |
Sensor histidine kinase WalK [Signal transduction mechanisms]; |
299-553 |
1.21e-05 |
|
Sensor histidine kinase WalK [Signal transduction mechanisms];
Pssm-ID: 444026 [Multi-domain] Cd Length: 390 Bit Score: 48.01 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 299 KNDNVNAQKMISVNVDRLDNLMNLVGELMitesmvtqcpEVEVIESENF--HKASIELHKITEELQDMVmsirmvplstt 376
Cdd:COG5002 195 ADDPEERREYLEIILEEAERLSRLVNDLL----------DLSRLESGELklEKEPVDLAELLEEVVEEL----------- 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 377 fvkmnrivRDMCKKLTREVILDLHGEETEV--DKNIIEHIsdpLMHIIRNAIDHGIENeserlkkgkekaGRIILEAKNI 454
Cdd:COG5002 254 --------RPLAEEKGIELELDLPEDPLLVlgDPDRLEQV---LTNLLDNAIKYTPEG------------GTITVSLREE 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 455 GSDVLIIIKDDGRGldkiriIEKAQQNglltksveemsdrEIFKlillPGFSTNESVT-EFSGRGVGMDVVTKNIEAIGG 533
Cdd:COG5002 311 DDQVRISVRDTGIG------IPEEDLP-------------RIFE----RFYRVDKSRSrETGGTGLGLAIVKHIVEAHGG 367
|
250 260
....*....|....*....|
gi 504122286 534 TVLIDSEKDKGTIITLKIPL 553
Cdd:COG5002 368 RIWVESEPGKGTTFTITLPL 387
|
|
| COG4251 |
COG4251 |
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ... |
418-552 |
1.34e-05 |
|
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal transduction mechanisms];
Pssm-ID: 443393 [Multi-domain] Cd Length: 503 Bit Score: 48.24 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 418 LMHIIRNAIDHGieneserlkkGKEKAGRIILEAKNIGSDVLIIIKDDGRGLDkiriiekaqqnglltksvEEMSDReIF 497
Cdd:COG4251 399 FQNLISNAIKYS----------RPGEPPRIEIGAEREGGEWVFSVRDNGIGID------------------PEYAEK-IF 449
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 504122286 498 KLillpgFSTNESVTEFSGRGVGMDVVTKNIEAIGGTVLIDSEKDKGTIITLKIP 552
Cdd:COG4251 450 EI-----FQRLHSRDEYEGTGIGLAIVKKIVERHGGRIWVESEPGEGATFYFTLP 499
|
|
| PRK11086 |
PRK11086 |
sensory histidine kinase DcuS; Provisional |
430-552 |
2.59e-05 |
|
sensory histidine kinase DcuS; Provisional
Pssm-ID: 236839 [Multi-domain] Cd Length: 542 Bit Score: 47.22 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 430 IENESERLKKGKEKAGRIILEAKNigSDVLIIIKDDGRGldkiriIEKAQQNGLLTKsveemsdreifklillpGFSTNE 509
Cdd:PRK11086 442 IENALEAVGGEEGGEISVSLHYRN--GWLHCEVSDDGPG------IAPDEIDAIFDK-----------------GYSTKG 496
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 504122286 510 SvtefsGRGVGMDVVTKNIEAIGGTVLIDSEKDKGTIITLKIP 552
Cdd:PRK11086 497 S-----NRGVGLYLVKQSVENLGGSIAVESEPGVGTQFFVQIP 534
|
|
| PRK10364 |
PRK10364 |
two-component system sensor histidine kinase ZraS; |
445-553 |
4.91e-05 |
|
two-component system sensor histidine kinase ZraS;
Pssm-ID: 236674 [Multi-domain] Cd Length: 457 Bit Score: 46.32 E-value: 4.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 445 GRIILEAKNIGSDVLIIIKDDGRGldkiriiekaqqnglltksveeMSDREIfKLILLPGFSTNESvtefsGRGVGMDVV 524
Cdd:PRK10364 368 GVISVTASESGAGVKISVTDSGKG----------------------IAADQL-EAIFTPYFTTKAE-----GTGLGLAVV 419
|
90 100
....*....|....*....|....*....
gi 504122286 525 TKNIEAIGGTVLIDSEKDKGTIITLKIPL 553
Cdd:PRK10364 420 HNIVEQHGGTIQVASQEGKGATFTLWLPV 448
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
369-554 |
5.71e-05 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 45.99 E-value: 5.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 369 RMVPLSTTFVKMNRIVRDMCKKLTRE------VILDLHGE--ETEVDKniiEHISDPLMHIIRNAIDHGieneserlkkg 440
Cdd:COG3852 195 RPRPPEREPVNLHEVLERVLELLRAEapknirIVRDYDPSlpEVLGDP---DQLIQVLLNLVRNAAEAM----------- 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 441 kEKAGRIILEAKNIGSD----------VLIIIKDDGRGLDkiriiekaqqnglltksvEEMSDReIFklilLPGFSTNES 510
Cdd:COG3852 261 -PEGGTITIRTRVERQVtlgglrprlyVRIEVIDNGPGIP------------------EEILDR-IF----EPFFTTKEK 316
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 504122286 511 vtefsGRGVGMDVVTKNIEAIGGTVLIDSEKDKGTIITLKIPLT 554
Cdd:COG3852 317 -----GTGLGLAIVQKIVEQHGGTIEVESEPGKGTTFRIYLPLE 355
|
|
| HATPase_DpiB-CitA-like |
cd16915 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
418-552 |
9.47e-05 |
|
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli K-12 DpiB, DcuS, and Bacillus subtilis CitS, DctS, and YufL; This family includes histidine kinase-like ATPase domains of Escherichia coli K-12 DpiB and DcuS, and Bacillus subtilis CitS, DctS and MalK histidine kinases (HKs) all of which are two component transduction systems (TCSs). E. coli K-12 DpiB (also known as CitA) is the histidine kinase (HK) of DpiA-DpiB, a two-component signal transduction system (TCS) required for the expression of citrate-specific fermentation genes and genes involved in plasmid inheritance. E. coli K-12 DcuS (also known as YjdH) is the HK of DcuS-DcuR, a TCS that in the presence of the extracellular C4-dicarboxlates, activates the expression of the genes of anaerobic fumarate respiration and of aerobic C4-dicarboxylate uptake. CitS is the HK of Bacillus subtilis CitS-CitT, a TCS which regulates expression of CitM, the Mg-citrate transporter. Bacillus subtilis DctS forms a tripartite sensor unit (DctS/DctA/DctB) for sensing C4 dicarboxylates. Bacillus subtilis MalK (also known as YfuL) is the HK of MalK-MalR (YufL-YufM) a TCS which regulates the expression of the malate transporters MaeN (YufR) and YflS, and is essential for utilization of malate in minimal medium. Proteins having this DpiB-CitA-like HATPase domain generally have sensor domains such as Cache and PAS, and a histidine kinase A (HisKA)-like SpoOB-type, alpha-helical domain.
Pssm-ID: 340392 [Multi-domain] Cd Length: 104 Bit Score: 41.89 E-value: 9.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 418 LMHIIRNAIDHGIENESERLKKGKekagRIILEAKNIGSDVLIIIKDDGRGLDkiriiekaqqnglltksvEEMSDReIF 497
Cdd:cd16915 1 LITIVGNLIDNALDALAATGAPNK----QVEVFLRDEGDDLVIEVRDTGPGIA------------------PELRDK-VF 57
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 504122286 498 KlillPGFSTNESvtefSGRGVGMDVVTKNIEAIGGTVLIDSEKDKGTIITLKIP 552
Cdd:cd16915 58 E----RGVSTKGQ----GERGIGLALVRQSVERLGGSITVESEPGGGTTFSIRIP 104
|
|
| KinA |
COG5805 |
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ... |
353-554 |
1.35e-04 |
|
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: 45.11 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 353 ELHKITEELQDMVMSIRMVPLSTTFVKMNRIVRDMCKKLTREVILD---LHGEETEVDKNII---EHISDPLMHIIRNAI 426
Cdd:COG5805 329 ELDRIESIISEFLALAKPQAVNKEKENINELIQDVVTLLETEAILHniqIRLELLDEDPFIYcdeNQIKQVFINLIKNAI 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 427 DhGIENEserlkkgkekaGRIILEAKNIGSDVLIIIKDDGRGLDKiriiekaqqnglltksveemsdrEIFKLILLPGFS 506
Cdd:COG5805 409 E-AMPNG-----------GTITIHTEEEDNSVIIRVIDEGIGIPE-----------------------ERLKKLGEPFFT 453
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 504122286 507 TNESvtefsGRGVGMDVVTKNIEAIGGTVLIDSEKDKGTIITLKIPLT 554
Cdd:COG5805 454 TKEK-----GTGLGLMVSYKIIENHNGTIDIDSKVGKGTTFTITLPLS 496
|
|
| YesM |
COG2972 |
Sensor histidine kinase YesM [Signal transduction mechanisms]; |
421-554 |
1.55e-04 |
|
Sensor histidine kinase YesM [Signal transduction mechanisms];
Pssm-ID: 442211 [Multi-domain] Cd Length: 445 Bit Score: 44.62 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 421 IIRNAIDHGIENeserlkkgKEKAGRIILEAKNIGSDVLIIIKDDGRGLDKIRIIEkaqqnglltksveemsdreifkli 500
Cdd:COG2972 344 LVENAIEHGIEP--------KEGGGTIRISIRKEGDRLVITVEDNGVGMPEEKLEK------------------------ 391
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 504122286 501 LLPGFSTNEsvtefSGRGVGMDVVTKNIEAI---GGTVLIDSEKDKGTIITLKIPLT 554
Cdd:COG2972 392 LLEELSSKG-----EGRGIGLRNVRERLKLYygeEYGLEIESEPGEGTTVTIRIPLE 443
|
|
| HATPase_AtoS-like |
cd16943 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
418-553 |
1.74e-03 |
|
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: 38.56 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 418 LMHIIRNAIdHGIENEserlkkgkekaGRIILEAKNIGSDVLIIIKDDGRGLDKiriiekaqqnglltksveemsdrEIF 497
Cdd:cd16943 8 LLNLLVNAA-QAMEGR-----------GRITIRTWAHVDQVLIEVEDTGSGIDP-----------------------EIL 52
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 504122286 498 KLILLPGFSTNESVTefsGRGVGMDVVTKNIEAIGGTVLIDSEKDKGTIITLKIPL 553
Cdd:cd16943 53 GRIFDPFFTTKPVGE---GTGLGLSLSYRIIQKHGGTIRVASVPGGGTRFTIILPI 105
|
|
| LytS |
COG3275 |
Sensor histidine kinase, LytS/YehU family [Signal transduction mechanisms]; |
400-553 |
2.14e-03 |
|
Sensor histidine kinase, LytS/YehU family [Signal transduction mechanisms];
Pssm-ID: 442506 [Multi-domain] Cd Length: 352 Bit Score: 41.01 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 400 HGEETEVDKNIIEHISD----PLM--HIIRNAIDHGIENeserlkkgKEKAGRIILEAKNIGSDVLIIIKDDGRGLDKIR 473
Cdd:COG3275 234 FGDRLQVEIDIDEELLDllipPLLlqPLVENAIKHGISS--------KEGGGTISISIEVEGDRLVIEVENNGVGIQPKK 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504122286 474 IIEkaqqnglltksveemsdreifklillpgfstnesvtefsGRGVGMDVVTKNIEAIGG---TVLIDSEKDKGTIITLK 550
Cdd:COG3275 306 KKK---------------------------------------GSGIGLKNVRERLELLYGdkySLEIESTDGGGTKVTLK 346
|
...
gi 504122286 551 IPL 553
Cdd:COG3275 347 IPL 349
|
|
| |
