|
Name |
Accession |
Description |
Interval |
E-value |
| CheA |
COG0643 |
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms]; |
444-761 |
2.47e-55 |
|
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
Pssm-ID: 440408 [Multi-domain] Cd Length: 563 Bit Score: 200.02 E-value: 2.47e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 444 SEADHAAIAELFRNMHTIKGNARTYNLQHLTDVVHETEQSYHELRQ--------------------------------PD 491
Cdd:COG0643 31 DPDDPELLNAIFRAAHTLKGSAGMLGLDALAELAHALEDLLDALRNgelaltpelidlllealdalralldaleaggePP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 492 ADRSWDQEHLMRELTRVREAIESYATIN------------EQSLGRKGKAQRNDAGNAGRYVMVDKEEMQRIVNL----- 554
Cdd:COG0643 111 ADISALLARLDASEEAIEEVVADEVEISppapaalepapaAAPPAEAAAAAAEAAAAASETVRVDVERLDRLMNLvgelv 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 555 ---------LDETNASELHELQAMQKTLRRNLLALgSQSVRDA----LSGVLGSLP----SLAGELGKPApsvhiadngy 617
Cdd:COG0643 191 itrarleqlAEELEDESLRELEEALEQLSRLTREL-QDGVMRLrmvpISTVFNRFPrmvrDLARELGKEV---------- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 618 RLRGKSAGT---------LNNVFMHLLRNSMDHGIESAEARAAKGKTPAGAISIEVGVDGGALQITLSDDGRGLALERIR 688
Cdd:COG0643 260 ELVIEGEETeldrtvlerLGDPLVHLVRNAVDHGIETPEERLAAGKPETGTITLSAYHEGGRVVIEVSDDGRGLDLEKIR 339
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1208343461 689 GIAMERGWIGPDE--TPGDEAIAELIFRPGFSTADTVTAVSGRGVGMDAVRDFLKRENGSIELRFTDDhKGAAFR 761
Cdd:COG0643 340 AKAIEKGLITAEEaaALSDEELLELIFAPGFSTAEEVTDLSGRGVGMDVVKTNIEALGGTIEIESEPG-KGTTFT 413
|
|
| HATPase_CheA-like |
cd16916 |
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ... |
627-761 |
1.02e-44 |
|
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: 158.51 E-value: 1.02e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 627 LNNVFMHLLRNSMDHGIESAEARAAKGKTPAGAISIEVGVDGGALQITLSDDGRGLALERIRGIAMERGWIGPDE--TPG 704
Cdd:cd16916 39 LADPLTHLLRNAVDHGIEAPEERLAAGKPPEGTITLRAEHQGNQVVIEVSDDGRGIDREKIREKAIERGLITADEaaTLS 118
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1208343461 705 DEAIAELIFRPGFSTADTVTAVSGRGVGMDAVRDFLKRENGSIELrFTDDHKGAAFR 761
Cdd:cd16916 119 DDEVLNLIFAPGFSTAEQVTDVSGRGVGMDVVKRSIESLGGTIEV-ESEPGQGTTFT 174
|
|
| PRK10547 |
PRK10547 |
chemotaxis protein CheA; Provisional |
633-761 |
4.44e-28 |
|
chemotaxis protein CheA; Provisional
Pssm-ID: 236712 [Multi-domain] Cd Length: 670 Bit Score: 120.61 E-value: 4.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 633 HLLRNSMDHGIESAEARAAKGKTPAGAISIEVGVDGGALQITLSDDGRGLALERIRGIAMERGwIGPDETPGDEAIAELI 712
Cdd:PRK10547 392 HLVRNSLDHGIELPEKRLAAGKNSVGNLILSAEHQGGNICIEVTDDGAGLNRERILAKAASQG-LAVSENMSDEEVGMLI 470
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1208343461 713 FRPGFSTADTVTAVSGRGVGMDAVRDFLKRENGSIELRFTDDhKGAAFR 761
Cdd:PRK10547 471 FAPGFSTAEQVTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQG-KGTTIR 518
|
|
| NtrY |
COG5000 |
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
187-571 |
9.60e-17 |
|
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: 83.47 E-value: 9.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 187 IAFVTGIAIILLTSIGALLYRQITRPLSRMQAMMSEIASSqDFTRRVPVGRLDEIGHSIVAFNGMIEKIQESSAQLKQKT 266
Cdd:COG5000 11 LLLIALLLLLLALWLALLLARRLTRPLRRLAEATRAVAAG-DLSVRLPVTGDDEIGELARAFNRMTDQLKEQREELEERR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 267 ADIQAMLQNMQQGILTV-IDGAVIHAEYSAylEDIfetkdiagrglmdlvfadtdLGADALSQVDAAAHACLGEDCINFA 345
Cdd:COG5000 90 RYLETILENLPAGVIVLdADGRITLANPAA--ERL--------------------LGIPLEELIGKPLEELLPELDLAEL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 346 FNQHLLVGEISK-RMPDGRVKILDLSWSAITDEDDTIVrlmlcVRDVTELrklaaeasEQRRRLDMIGEI---LAvseek 421
Cdd:COG5000 148 LREALERGWQEEiELTRDGRRTLLVRASPLRDDGYVIV-----FDDITEL--------LRAERLAAWGELarrIA----- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 422 fHHF------IESSAgfisenERIIRKHSEADHAAIAELFRNMHTIKgnARTYNLQHLTDvvheteqSYHEL-RQPDADR 494
Cdd:COG5000 210 -HEIknpltpIQLSA------ERLRRKLADKLEEDREDLERALDTII--RQVDRLKRIVD-------EFLDFaRLPEPQL 273
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1208343461 495 swdQEHLMRELtrVREAIESYatinEQSLGRKGKAQRNDAGNAGRYVMVDKEEMQR-IVNLLDetNAselheLQAMQK 571
Cdd:COG5000 274 ---EPVDLNEL--LREVLALY----EPALKEKDIRLELDLDPDLPEVLADRDQLEQvLINLLK--NA-----IEAIEE 335
|
|
| HATPase_c |
smart00387 |
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases. |
631-761 |
1.25e-13 |
|
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
Pssm-ID: 214643 [Multi-domain] Cd Length: 111 Bit Score: 67.67 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 631 FMHLLRNSMDHGIESAEARaakgktpaGAISIEVGVDGGALQITLSDDGRGLalerirgiamergwigpdetpgDEAIAE 710
Cdd:smart00387 6 LRQVLSNLLDNAIKYTPEG--------GRITVTLERDGDHVEITVEDNGPGI----------------------PPEDLE 55
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1208343461 711 LIFRPGFSTADTVTAVSGRGVGMDAVRDFLKRENGSIELRfTDDHKGAAFR 761
Cdd:smart00387 56 KIFEPFFRTDKRSRKIGGTGLGLSIVKKLVELHGGEISVE-SEPGGGTTFT 105
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
1-287 |
2.30e-10 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 63.89 E-value: 2.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 1 MTIRHRITLLVVLMFVALSAIGAYAVYQTRGSAAEVRKVTEGVVPSALASADLVSQVKDVQLATMTLVYAPDGAVVAQAQ 80
Cdd:COG0840 2 LILLLLLALLLALLLLALSLLALLAAALLILLALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 81 DELKKKRIALQQALALQAKDAASHAQKGLVSQANDSLDNYFSAIAETAKMKADGKNELAQAYLFANVAQYRDELEGIVET 160
Cdd:COG0840 82 LALLLALLLLLLALLALALAALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 161 LRVEKNREKDEAITTLNATLATTTTAIAFVTGIAIIlltsIGALLYRQITRPLSRMQAMMSEIASSqDFTRRVPVGRLDE 240
Cdd:COG0840 162 ALAALLEAAALALAAAALALALLAAALLALVALAII----LALLLSRSITRPLRELLEVLERIAEG-DLTVRIDVDSKDE 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1208343461 241 IGHSIVAFNGMIEKIQESSAQLKQKTADIQAMLQNMQQGILTVIDGA 287
Cdd:COG0840 237 IGQLADAFNRMIENLRELVGQVRESAEQVASASEELAASAEELAAGA 283
|
|
| HAMP |
pfam00672 |
HAMP domain; |
204-257 |
2.98e-08 |
|
HAMP domain;
Pssm-ID: 459898 [Multi-domain] Cd Length: 53 Bit Score: 50.70 E-value: 2.98e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1208343461 204 LLYRQITRPLSRMQAMMSEIASsQDFTRRVPVGRLDEIGHSIVAFNGMIEKIQE 257
Cdd:pfam00672 1 LLARRILRPLRRLAEAARRIAS-GDLDVRLPVSGRDEIGELARAFNQMAERLRE 53
|
|
| HAMP |
smart00304 |
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain; |
207-258 |
1.70e-07 |
|
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
Pssm-ID: 197640 [Multi-domain] Cd Length: 53 Bit Score: 48.40 E-value: 1.70e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1208343461 207 RQITRPLSRMQAMMSEIASsQDFTRRVPVGRLDEIGHSIVAFNGMIEKIQES 258
Cdd:smart00304 1 RRLLRPLRRLAEAAQRIAD-GDLTVRLPVDGRDEIGELARAFNEMADRLEET 51
|
|
| HAMP |
cd06225 |
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; ... |
210-255 |
2.09e-07 |
|
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the Af1503 HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established.
Pssm-ID: 381743 [Multi-domain] Cd Length: 45 Bit Score: 47.82 E-value: 2.09e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1208343461 210 TRPLSRMQAMMSEIASsQDFTRRVPVGRLDEIGHSIVAFNGMIEKI 255
Cdd:cd06225 1 TRPLRRLTEAARRIAE-GDLDVRVPVRSKDEIGELARAFNQMAERL 45
|
|
| HATPase_c |
pfam02518 |
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ... |
631-761 |
1.25e-06 |
|
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: 47.75 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 631 FMHLLRNSMDHGIESAearaakgkTPAGAISIEVgVDGGALQITLSDDGRGLALERIrgiamergwigpdetpgdeaiaE 710
Cdd:pfam02518 6 LRQVLSNLLDNALKHA--------AKAGEITVTL-SEGGELTLTVEDNGIGIPPEDL----------------------P 54
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1208343461 711 LIFRPgFSTADTVTAvSGRGVGMDAVRDFLKRENGSIELRfTDDHKGAAFR 761
Cdd:pfam02518 55 RIFEP-FSTADKRGG-GGTGLGLSIVRKLVELLGGTITVE-SEPGGGTTVT 102
|
|
| 4HB_MCP_1 |
pfam12729 |
Four helix bundle sensory module for signal transduction; This family is a four helix bundle ... |
1-168 |
4.88e-05 |
|
Four helix bundle sensory module for signal transduction; This family is a four helix bundle that operates as a ubiquitous sensory module in prokaryotic signal-transduction. The 4HB_MCP is always found between two predicted transmembrane helices indicating that it detects only extracellular signals. In many cases the domain is associated with a cytoplasmic HAMP domain suggesting that most proteins carrying the bundle might share the mechanism of transmembrane signalling which is well-characterized in E coli chemoreceptors. This domain recognizes citrate and TCA cycle intermediates, cis-aconitate, boric acid, Phenanthrene, pyrene and benzopyrene (Matilla et el., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 432749 [Multi-domain] Cd Length: 181 Bit Score: 44.93 E-value: 4.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 1 MTIRHRITLLVVLMFVALSAIGAYAVYQTRGSAAEVRKVTEGVVPSALASADLVSQVKDVQLATMTLVYAPDGAVVAQAQ 80
Cdd:pfam12729 2 LKIRTKLILLFLLLALLLIIVGVVGLYSLKQINDNLDTMYEDRLLPIKWLGDIRANLLELRANLLELILTTDPAERDELL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 81 DELKKKRIALQQALALQAKDAASHAQKGLVSQANDSLDNYFSAIAETAKMKADGKNELAQAYLFANVAQYRDELEGIVET 160
Cdd:pfam12729 82 KDIEELRAEIDKLLEKYEKTILTDEEKKLFAEFKENLNAYRAVRNKVLELAKAGNKDEAYQLYKTEGRPAREAMIEALEE 161
|
....*...
gi 1208343461 161 LrVEKNRE 168
Cdd:pfam12729 162 L-VDYNLK 168
|
|
| PRK11360 |
PRK11360 |
two-component system sensor histidine kinase AtoS; |
187-416 |
1.35e-04 |
|
two-component system sensor histidine kinase AtoS;
Pssm-ID: 236901 [Multi-domain] Cd Length: 607 Bit Score: 45.34 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 187 IAFVTGIAIIL-LTSIGALLYR------QITRPLSRMqammseiasSQDFTRRVP--VGRLDEIGHSIvafNGMIEKIQE 257
Cdd:PRK11360 192 IYAVLAAGLVIgLLLIFLLSRRfsanvdIIKDGLSTL---------ENDLSTRLPplPGELGEISQAI---NNLAQALRE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 258 SsaqlKQKTADIqamLQNMQQGILTV-IDGAVIHAEYSAylEDIF--ETKDIAGRGLMDLVFADTDLgADALsqvdaaaH 334
Cdd:PRK11360 260 T----RSLNELI---LESIADGVIAIdRQGKITTMNPAA--EVITglQRHELVGKPYSELFPPNTPF-ASPL-------L 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 335 ACLGEDCinfafnQHLLVgEISKRMPDGRVKILdLSWSAITDEDDTIVRLMLCVRDVTELRKLaAEASEQRRRLDMIGEI 414
Cdd:PRK11360 323 DTLEHGT------EHVDL-EISFPGRDRTIELS-VSTSLLHNTHGEMIGALVIFSDLTERKRL-QRRVARQERLAALGEL 393
|
..
gi 1208343461 415 LA 416
Cdd:PRK11360 394 VA 395
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CheA |
COG0643 |
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms]; |
444-761 |
2.47e-55 |
|
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
Pssm-ID: 440408 [Multi-domain] Cd Length: 563 Bit Score: 200.02 E-value: 2.47e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 444 SEADHAAIAELFRNMHTIKGNARTYNLQHLTDVVHETEQSYHELRQ--------------------------------PD 491
Cdd:COG0643 31 DPDDPELLNAIFRAAHTLKGSAGMLGLDALAELAHALEDLLDALRNgelaltpelidlllealdalralldaleaggePP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 492 ADRSWDQEHLMRELTRVREAIESYATIN------------EQSLGRKGKAQRNDAGNAGRYVMVDKEEMQRIVNL----- 554
Cdd:COG0643 111 ADISALLARLDASEEAIEEVVADEVEISppapaalepapaAAPPAEAAAAAAEAAAAASETVRVDVERLDRLMNLvgelv 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 555 ---------LDETNASELHELQAMQKTLRRNLLALgSQSVRDA----LSGVLGSLP----SLAGELGKPApsvhiadngy 617
Cdd:COG0643 191 itrarleqlAEELEDESLRELEEALEQLSRLTREL-QDGVMRLrmvpISTVFNRFPrmvrDLARELGKEV---------- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 618 RLRGKSAGT---------LNNVFMHLLRNSMDHGIESAEARAAKGKTPAGAISIEVGVDGGALQITLSDDGRGLALERIR 688
Cdd:COG0643 260 ELVIEGEETeldrtvlerLGDPLVHLVRNAVDHGIETPEERLAAGKPETGTITLSAYHEGGRVVIEVSDDGRGLDLEKIR 339
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1208343461 689 GIAMERGWIGPDE--TPGDEAIAELIFRPGFSTADTVTAVSGRGVGMDAVRDFLKRENGSIELRFTDDhKGAAFR 761
Cdd:COG0643 340 AKAIEKGLITAEEaaALSDEELLELIFAPGFSTAEEVTDLSGRGVGMDVVKTNIEALGGTIEIESEPG-KGTTFT 413
|
|
| HATPase_CheA-like |
cd16916 |
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ... |
627-761 |
1.02e-44 |
|
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: 158.51 E-value: 1.02e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 627 LNNVFMHLLRNSMDHGIESAEARAAKGKTPAGAISIEVGVDGGALQITLSDDGRGLALERIRGIAMERGWIGPDE--TPG 704
Cdd:cd16916 39 LADPLTHLLRNAVDHGIEAPEERLAAGKPPEGTITLRAEHQGNQVVIEVSDDGRGIDREKIREKAIERGLITADEaaTLS 118
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1208343461 705 DEAIAELIFRPGFSTADTVTAVSGRGVGMDAVRDFLKRENGSIELrFTDDHKGAAFR 761
Cdd:cd16916 119 DDEVLNLIFAPGFSTAEQVTDVSGRGVGMDVVKRSIESLGGTIEV-ESEPGQGTTFT 174
|
|
| PRK10547 |
PRK10547 |
chemotaxis protein CheA; Provisional |
633-761 |
4.44e-28 |
|
chemotaxis protein CheA; Provisional
Pssm-ID: 236712 [Multi-domain] Cd Length: 670 Bit Score: 120.61 E-value: 4.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 633 HLLRNSMDHGIESAEARAAKGKTPAGAISIEVGVDGGALQITLSDDGRGLALERIRGIAMERGwIGPDETPGDEAIAELI 712
Cdd:PRK10547 392 HLVRNSLDHGIELPEKRLAAGKNSVGNLILSAEHQGGNICIEVTDDGAGLNRERILAKAASQG-LAVSENMSDEEVGMLI 470
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1208343461 713 FRPGFSTADTVTAVSGRGVGMDAVRDFLKRENGSIELRFTDDhKGAAFR 761
Cdd:PRK10547 471 FAPGFSTAEQVTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQG-KGTTIR 518
|
|
| NtrY |
COG5000 |
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
187-571 |
9.60e-17 |
|
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: 83.47 E-value: 9.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 187 IAFVTGIAIILLTSIGALLYRQITRPLSRMQAMMSEIASSqDFTRRVPVGRLDEIGHSIVAFNGMIEKIQESSAQLKQKT 266
Cdd:COG5000 11 LLLIALLLLLLALWLALLLARRLTRPLRRLAEATRAVAAG-DLSVRLPVTGDDEIGELARAFNRMTDQLKEQREELEERR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 267 ADIQAMLQNMQQGILTV-IDGAVIHAEYSAylEDIfetkdiagrglmdlvfadtdLGADALSQVDAAAHACLGEDCINFA 345
Cdd:COG5000 90 RYLETILENLPAGVIVLdADGRITLANPAA--ERL--------------------LGIPLEELIGKPLEELLPELDLAEL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 346 FNQHLLVGEISK-RMPDGRVKILDLSWSAITDEDDTIVrlmlcVRDVTELrklaaeasEQRRRLDMIGEI---LAvseek 421
Cdd:COG5000 148 LREALERGWQEEiELTRDGRRTLLVRASPLRDDGYVIV-----FDDITEL--------LRAERLAAWGELarrIA----- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 422 fHHF------IESSAgfisenERIIRKHSEADHAAIAELFRNMHTIKgnARTYNLQHLTDvvheteqSYHEL-RQPDADR 494
Cdd:COG5000 210 -HEIknpltpIQLSA------ERLRRKLADKLEEDREDLERALDTII--RQVDRLKRIVD-------EFLDFaRLPEPQL 273
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1208343461 495 swdQEHLMRELtrVREAIESYatinEQSLGRKGKAQRNDAGNAGRYVMVDKEEMQR-IVNLLDetNAselheLQAMQK 571
Cdd:COG5000 274 ---EPVDLNEL--LREVLALY----EPALKEKDIRLELDLDPDLPEVLADRDQLEQvLINLLK--NA-----IEAIEE 335
|
|
| HATPase_c |
smart00387 |
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases. |
631-761 |
1.25e-13 |
|
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
Pssm-ID: 214643 [Multi-domain] Cd Length: 111 Bit Score: 67.67 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 631 FMHLLRNSMDHGIESAEARaakgktpaGAISIEVGVDGGALQITLSDDGRGLalerirgiamergwigpdetpgDEAIAE 710
Cdd:smart00387 6 LRQVLSNLLDNAIKYTPEG--------GRITVTLERDGDHVEITVEDNGPGI----------------------PPEDLE 55
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1208343461 711 LIFRPGFSTADTVTAVSGRGVGMDAVRDFLKRENGSIELRfTDDHKGAAFR 761
Cdd:smart00387 56 KIFEPFFRTDKRSRKIGGTGLGLSIVKKLVELHGGEISVE-SEPGGGTTFT 105
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
1-287 |
2.30e-10 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 63.89 E-value: 2.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 1 MTIRHRITLLVVLMFVALSAIGAYAVYQTRGSAAEVRKVTEGVVPSALASADLVSQVKDVQLATMTLVYAPDGAVVAQAQ 80
Cdd:COG0840 2 LILLLLLALLLALLLLALSLLALLAAALLILLALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 81 DELKKKRIALQQALALQAKDAASHAQKGLVSQANDSLDNYFSAIAETAKMKADGKNELAQAYLFANVAQYRDELEGIVET 160
Cdd:COG0840 82 LALLLALLLLLLALLALALAALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 161 LRVEKNREKDEAITTLNATLATTTTAIAFVTGIAIIlltsIGALLYRQITRPLSRMQAMMSEIASSqDFTRRVPVGRLDE 240
Cdd:COG0840 162 ALAALLEAAALALAAAALALALLAAALLALVALAII----LALLLSRSITRPLRELLEVLERIAEG-DLTVRIDVDSKDE 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1208343461 241 IGHSIVAFNGMIEKIQESSAQLKQKTADIQAMLQNMQQGILTVIDGA 287
Cdd:COG0840 237 IGQLADAFNRMIENLRELVGQVRESAEQVASASEELAASAEELAAGA 283
|
|
| CitA |
COG3290 |
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ... |
497-770 |
9.10e-09 |
|
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction mechanisms];
Pssm-ID: 442519 [Multi-domain] Cd Length: 389 Bit Score: 58.32 E-value: 9.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 497 DQEHLMRELTRVREAIESYatineqslgrkgKAQRNDAGN-----AGryvMVDKEEMQRIVNLLDEtnaselhELQAMQK 571
Cdd:COG3290 175 ELERLEEELEGVKELAEAL------------RAQRHDFRNhlhtiSG---LLQLGEYDEALEYIDE-------ISEELQE 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 572 TLRRNLLALGSqsvrDALSGVLGSLPSLAGELGkpaPSVHIADNGY-RLRGKSAGTLNNVFMHLLRNSMDHgiesaearA 650
Cdd:COG3290 233 LIDSLLSRIGN----PVLAALLLGKAARARERG---IDLTIDIDSDlPDLPLSDTDLVTILGNLLDNAIEA--------V 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 651 AKGKTPAGAISIEVGVDGGALQITLSDDGRGLalerirgiamergwigpdetpgDEAIAELIFRPGFSTADTvtavSGRG 730
Cdd:COG3290 298 EKLPEEERRVELSIRDDGDELVIEVEDSGPGI----------------------PEELLEKIFERGFSTKLG----EGRG 351
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1208343461 731 VGMDAVRDFLKRENGSIELRfTDDHKGAAFrqfqtIVCLP 770
Cdd:COG3290 352 LGLALVKQIVEKYGGTIEVE-SEEGEGTVF-----TVRLP 385
|
|
| HAMP |
pfam00672 |
HAMP domain; |
204-257 |
2.98e-08 |
|
HAMP domain;
Pssm-ID: 459898 [Multi-domain] Cd Length: 53 Bit Score: 50.70 E-value: 2.98e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1208343461 204 LLYRQITRPLSRMQAMMSEIASsQDFTRRVPVGRLDEIGHSIVAFNGMIEKIQE 257
Cdd:pfam00672 1 LLARRILRPLRRLAEAARRIAS-GDLDVRLPVSGRDEIGELARAFNQMAERLRE 53
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
261-416 |
3.24e-08 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 56.39 E-value: 3.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 261 QLKQKTADIQAMLQNMQQGILTV-IDGAVIHAEYSAylEDIFET--KDIAGRGLMDLVFADTDLgADALSQVdaaahacl 337
Cdd:COG3852 1 ALRESEELLRAILDSLPDAVIVLdADGRITYVNPAA--ERLLGLsaEELLGRPLAELFPEDSPL-RELLERA-------- 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1208343461 338 gedcinFAFNQHLLVGEISKRMPDGRVKILDLSWSAITDEDDTIvRLMLCVRDVTELRKLAAEAsEQRRRLDMIGEILA 416
Cdd:COG3852 70 ------LAEGQPVTEREVTLRRKDGEERPVDVSVSPLRDAEGEG-GVLLVLRDITERKRLEREL-RRAEKLAAVGELAA 140
|
|
| KdpD |
COG2205 |
K+-sensing histidine kinase KdpD [Signal transduction mechanisms]; |
546-770 |
1.19e-07 |
|
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
Pssm-ID: 441807 [Multi-domain] Cd Length: 239 Bit Score: 53.37 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 546 EEMQRIV-NLLDetnaseLHELQAMQKTLRRNLLALgSQSVRDALSGVLGSLPSLAGELgkpapSVHIADNGYRLRGkSA 624
Cdd:COG2205 64 ERLLRLIeDLLD------LSRLESGKLSLELEPVDL-AELLEEAVEELRPLAEEKGIRL-----ELDLPPELPLVYA-DP 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 625 GTLNNVFMHLLRNSMDHGiesaearaakgkTPAGAISIEVGVDGGALQITLSDDGRGLAlerirgiamergwigpdetpg 704
Cdd:COG2205 131 ELLEQVLANLLDNAIKYS------------PPGGTITISARREGDGVRISVSDNGPGIP--------------------- 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1208343461 705 dEAIAELIFRPgFSTADTVTAVSGRGVGMDAVRDFLKRENGSIELRFTDDhKGAAFRqfqtiVCLP 770
Cdd:COG2205 178 -EEELERIFER-FYRGDNSRGEGGTGLGLAIVKRIVEAHGGTIWVESEPG-GGTTFT-----VTLP 235
|
|
| HAMP |
smart00304 |
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain; |
207-258 |
1.70e-07 |
|
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
Pssm-ID: 197640 [Multi-domain] Cd Length: 53 Bit Score: 48.40 E-value: 1.70e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1208343461 207 RQITRPLSRMQAMMSEIASsQDFTRRVPVGRLDEIGHSIVAFNGMIEKIQES 258
Cdd:smart00304 1 RRLLRPLRRLAEAAQRIAD-GDLTVRLPVDGRDEIGELARAFNEMADRLEET 51
|
|
| YesM |
COG2972 |
Sensor histidine kinase YesM [Signal transduction mechanisms]; |
187-274 |
1.99e-07 |
|
Sensor histidine kinase YesM [Signal transduction mechanisms];
Pssm-ID: 442211 [Multi-domain] Cd Length: 445 Bit Score: 54.25 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 187 IAFVTGIAIILLTSIGALLYRQITRPLSRMQAMMSEIaSSQDFTRrVPVGRLDEIGHSIVAFNGMIEKIQE-----SSAQ 261
Cdd:COG2972 159 ILLIILLLLLLALLLSYLLSRSITRPIKRLKKAMKKV-EKGDLVR-LEVSGNDEIGILARSFNEMVERIKElieevYELE 236
|
90
....*....|...
gi 1208343461 262 LKQKTADIQAmLQ 274
Cdd:COG2972 237 LEKKEAELKA-LQ 248
|
|
| HAMP |
cd06225 |
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; ... |
210-255 |
2.09e-07 |
|
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the Af1503 HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established.
Pssm-ID: 381743 [Multi-domain] Cd Length: 45 Bit Score: 47.82 E-value: 2.09e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1208343461 210 TRPLSRMQAMMSEIASsQDFTRRVPVGRLDEIGHSIVAFNGMIEKI 255
Cdd:cd06225 1 TRPLRRLTEAARRIAE-GDLDVRVPVRSKDEIGELARAFNQMAERL 45
|
|
| HATPase_c |
pfam02518 |
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ... |
631-761 |
1.25e-06 |
|
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: 47.75 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 631 FMHLLRNSMDHGIESAearaakgkTPAGAISIEVgVDGGALQITLSDDGRGLALERIrgiamergwigpdetpgdeaiaE 710
Cdd:pfam02518 6 LRQVLSNLLDNALKHA--------AKAGEITVTL-SEGGELTLTVEDNGIGIPPEDL----------------------P 54
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1208343461 711 LIFRPgFSTADTVTAvSGRGVGMDAVRDFLKRENGSIELRfTDDHKGAAFR 761
Cdd:pfam02518 55 RIFEP-FSTADKRGG-GGTGLGLSIVRKLVELLGGTITVE-SEPGGGTTVT 102
|
|
| HAMP |
COG2770 |
HAMP domain [Signal transduction mechanisms]; |
1-604 |
1.91e-06 |
|
HAMP domain [Signal transduction mechanisms];
Pssm-ID: 442051 [Multi-domain] Cd Length: 631 Bit Score: 51.27 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 1 MTIRHRITLLVVLMFVALSAIGAYAVYQTRGSAAEVRKVTEGVVPSALASADLVSQVKDVQLATMTLVYAPDGAVVAQAQ 80
Cdd:COG2770 28 LALISLRLLLALLLLLLLLLALLLLLLLLLLLLLAALVLLALLLAAALLLLLLLLSLVALAALLLALLLLLLLALLLLLA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 81 DELKKKRIALQQALALQAKDAASHAQKGLVSQANDSLDNYFSAIAETAKMKADGKNELAQAYLFANVAQYRDELEGIVET 160
Cdd:COG2770 108 ALLLLLLLAALALLLLLLLLLAALLALLLALALLALLLGLAAARLLLAALLALAAALALALGAGELLLLADLAAAIAALL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 161 LRVEKNREKDEAITTLNATLATTTTAIAFVTGIAIILLTSIGALLYRQITRPLSRMQAMMSEIASsQDFTRRVPVGRLDE 240
Cdd:COG2770 188 AALLLLLLGGLLLVVLLEAALAALLLLLLLALLALLLALLLALLLARRITRPLRRLAEAARRIAA-GDLDVRIPVSRKDE 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 241 IGHSIVAFNGMIEKIQESSAQLKQKTADIQAMLQNMQQGILTVIDGAVIHAEYSAYLEDIFETKDIAGRGLMDLVFADTD 320
Cdd:COG2770 267 IGELARAFNRMADSLRESIEEAEEEEELAEAELARLLEALLELLLALLLLLLALLLLAAAALLLELLLLLLLALLLLLLL 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 321 LGADALSQVDAAAHACLGEDCINFAFNQHLLVGEISKRMPDGRVKILDLSWSAITDEDDTIVRLMLCVRDVTELRKLAAE 400
Cdd:COG2770 347 AADLLLALALAALLLLLALELLLEAELLVLLALEALALEAELAAVLALLAALAAALLLLELALEELVLALLALALLALAA 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 401 ASEQRRRLDMIGEILAVSEEKFHHFIESSAGFISENERIIRKHSEADHAAIAELFRNMHTIKGNARTYNLQHLTDVVHET 480
Cdd:COG2770 427 AAAAAEAAAAALELAAAAIAAAAAAEAEGGLAELEAEELVAAAEALLLLAALLLLAALGALELLLLEEEEEAGAAAEELA 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 481 EQSYHELRQPDADRSWDQEHLMRELTRVREAIESYATINEQSLGRKGKAQRNDAGNAGRYVMVDKEEMQRIVNLLDETNA 560
Cdd:COG2770 507 EELLLLEGLLLLLLLEAEALEVAEELLELEEAALLLAAAAELAALLALLLALAAVEAAALLLAALLLAAVAALLELAALL 586
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1208343461 561 SELHELQAMQKTLRRNLLALGSQSVRDALSGVLGSLPSLAGELG 604
Cdd:COG2770 587 LLLLAAAEALAALELELAAAAEAALAEAELLEVAAAAEAGAALL 630
|
|
| BaeS |
COG0642 |
Signal transduction histidine kinase [Signal transduction mechanisms]; |
554-770 |
2.04e-05 |
|
Signal transduction histidine kinase [Signal transduction mechanisms];
Pssm-ID: 440407 [Multi-domain] Cd Length: 328 Bit Score: 47.60 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 554 LLDETNASELHELQAMQKTLRR------NLLALGSQ------------SVRDALSGVLGSLPSLAGELGkPAPSVHIADN 615
Cdd:COG0642 135 LLEELDEEQREYLETILRSADRllrlinDLLDLSRLeagklelepepvDLAELLEEVVELFRPLAEEKG-IELELDLPDD 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 616 GYRLRGkSAGTLNNVFMHLLRNSMDHGiesaearaakgkTPAGAISIEVGVDGGALQITLSDDGRGLAlerirgiamerg 695
Cdd:COG0642 214 LPTVRG-DPDRLRQVLLNLLSNAIKYT------------PEGGTVTVSVRREGDRVRISVEDTGPGIP------------ 268
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1208343461 696 wigpdetpgdEAIAELIFRPgFSTADTVTAVSGRGVGMDAVRDFLKRENGSIELRFTDDhKGAAFRqfqtiVCLP 770
Cdd:COG0642 269 ----------PEDLERIFEP-FFRTDPSRRGGGTGLGLAIVKRIVELHGGTIEVESEPG-KGTTFT-----VTLP 326
|
|
| KinA |
COG5805 |
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ... |
252-416 |
3.77e-05 |
|
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: 47.03 E-value: 3.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 252 IEKIQESSAQLKQKTADIQAMLQNMQQGILTVIDGAVIHaEYSAYLEDIF--ETKDIAGRGLMDLVfadtdlgadalsqv 329
Cdd:COG5805 142 ITKKKKIEEILQEQEERLQTLIENSPDLICVIDTDGRIL-FINESIERLFgaPREELIGKNLLELL-------------- 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 330 daaaHACLGEDcINFAFNQHLLVG-----EISKRMPDGRVKILDLSWSAITDEDDTIVRLMLCVRDVTElRKLAAEASEQ 404
Cdd:COG5805 207 ----HPCDKEE-FKERIESITEVWqefiiEREIITKDGRIRYFEAVIVPLIDTDGSVKGILVILRDITE-KKEAEELMAR 280
|
170
....*....|..
gi 1208343461 405 RRRLDMIGEILA 416
Cdd:COG5805 281 SEKLSIAGQLAA 292
|
|
| 4HB_MCP_1 |
pfam12729 |
Four helix bundle sensory module for signal transduction; This family is a four helix bundle ... |
1-168 |
4.88e-05 |
|
Four helix bundle sensory module for signal transduction; This family is a four helix bundle that operates as a ubiquitous sensory module in prokaryotic signal-transduction. The 4HB_MCP is always found between two predicted transmembrane helices indicating that it detects only extracellular signals. In many cases the domain is associated with a cytoplasmic HAMP domain suggesting that most proteins carrying the bundle might share the mechanism of transmembrane signalling which is well-characterized in E coli chemoreceptors. This domain recognizes citrate and TCA cycle intermediates, cis-aconitate, boric acid, Phenanthrene, pyrene and benzopyrene (Matilla et el., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 432749 [Multi-domain] Cd Length: 181 Bit Score: 44.93 E-value: 4.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 1 MTIRHRITLLVVLMFVALSAIGAYAVYQTRGSAAEVRKVTEGVVPSALASADLVSQVKDVQLATMTLVYAPDGAVVAQAQ 80
Cdd:pfam12729 2 LKIRTKLILLFLLLALLLIIVGVVGLYSLKQINDNLDTMYEDRLLPIKWLGDIRANLLELRANLLELILTTDPAERDELL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 81 DELKKKRIALQQALALQAKDAASHAQKGLVSQANDSLDNYFSAIAETAKMKADGKNELAQAYLFANVAQYRDELEGIVET 160
Cdd:pfam12729 82 KDIEELRAEIDKLLEKYEKTILTDEEKKLFAEFKENLNAYRAVRNKVLELAKAGNKDEAYQLYKTEGRPAREAMIEALEE 161
|
....*...
gi 1208343461 161 LrVEKNRE 168
Cdd:pfam12729 162 L-VDYNLK 168
|
|
| HPT |
cd00088 |
Histidine Phosphotransfer domain, involved in signalling through a two part component systems ... |
425-513 |
6.14e-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: 42.37 E-value: 6.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 425 FIESSAGFISENERIIRKHSEADhaAIAELFRNMHTIKGNARTYNLQHLTDVVHETEQSYHELRQPDADRSWDQEHLMRE 504
Cdd:cd00088 8 FLEEAEELLEELERALLELEDAE--DLNEIFRAAHTLKGSAASLGLQRLAQLAHQLEDLLDALRDGLEVTPELIDLLLDA 85
|
....*....
gi 1208343461 505 LTRVREAIE 513
Cdd:cd00088 86 LDALKAELE 94
|
|
| Hpt |
pfam01627 |
Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module ... |
432-511 |
1.30e-04 |
|
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: 41.18 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 432 FISENERIIRK-HSEADHAAIAELFRNMHTIKGNARTYNLQHLTDVVHETEQSYHELRQPDADRswDQEHLMRELTRVRE 510
Cdd:pfam01627 6 FLEEAPELLEQlEQALDAEDLEALFRAAHTLKGSAGSLGLPALAELAHELEDLLREGELPLDPE--LLEALRDLLEALRA 83
|
.
gi 1208343461 511 A 511
Cdd:pfam01627 84 A 84
|
|
| PRK11360 |
PRK11360 |
two-component system sensor histidine kinase AtoS; |
187-416 |
1.35e-04 |
|
two-component system sensor histidine kinase AtoS;
Pssm-ID: 236901 [Multi-domain] Cd Length: 607 Bit Score: 45.34 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 187 IAFVTGIAIIL-LTSIGALLYR------QITRPLSRMqammseiasSQDFTRRVP--VGRLDEIGHSIvafNGMIEKIQE 257
Cdd:PRK11360 192 IYAVLAAGLVIgLLLIFLLSRRfsanvdIIKDGLSTL---------ENDLSTRLPplPGELGEISQAI---NNLAQALRE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 258 SsaqlKQKTADIqamLQNMQQGILTV-IDGAVIHAEYSAylEDIF--ETKDIAGRGLMDLVFADTDLgADALsqvdaaaH 334
Cdd:PRK11360 260 T----RSLNELI---LESIADGVIAIdRQGKITTMNPAA--EVITglQRHELVGKPYSELFPPNTPF-ASPL-------L 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 335 ACLGEDCinfafnQHLLVgEISKRMPDGRVKILdLSWSAITDEDDTIVRLMLCVRDVTELRKLaAEASEQRRRLDMIGEI 414
Cdd:PRK11360 323 DTLEHGT------EHVDL-EISFPGRDRTIELS-VSTSLLHNTHGEMIGALVIFSDLTERKRL-QRRVARQERLAALGEL 393
|
..
gi 1208343461 415 LA 416
Cdd:PRK11360 394 VA 395
|
|
| HATPase_DpiB-CitA-like |
cd16915 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
637-749 |
2.65e-04 |
|
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: 40.73 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 637 NSMDHGIESAEARAAKGKTpagaISIEVGVDGGALQITLSDDGRGLalerirgiamergwigpdetpgDEAIAELIFRPG 716
Cdd:cd16915 7 NLIDNALDALAATGAPNKQ----VEVFLRDEGDDLVIEVRDTGPGI----------------------APELRDKVFERG 60
|
90 100 110
....*....|....*....|....*....|...
gi 1208343461 717 FSTadtvTAVSGRGVGMDAVRDFLKRENGSIEL 749
Cdd:cd16915 61 VST----KGQGERGIGLALVRQSVERLGGSITV 89
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
353-433 |
3.40e-04 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 43.09 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 353 GEISKRMPDGRVKILDLSWSAITDEDDTIVRLMLCVRDVTElRKLAAEAseqrrrldmigeiLAVSEEKFHHFIESSAGF 432
Cdd:COG2202 84 GELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITE-RKRAEEA-------------LRESEERLRLLVENAPDG 149
|
.
gi 1208343461 433 I 433
Cdd:COG2202 150 I 150
|
|
| PRK15347 |
PRK15347 |
two component system sensor kinase; |
193-267 |
3.91e-04 |
|
two component system sensor kinase;
Pssm-ID: 237951 [Multi-domain] Cd Length: 921 Bit Score: 44.25 E-value: 3.91e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1208343461 193 IAIILLTSIGA-LLYRQITRPLSRMQAMMSEiASSQDFTRRVPVGRLDEIGHSIVAFNGMIEKIQESSAQLKQKTA 267
Cdd:PRK15347 304 LILVLLTSVLFlLLRRYLAKPLWRFVDIINK-TGPAALEPRLPENRLDELGSIAKAYNQLLDTLNEQYDTLENKVA 378
|
|
| NarQ |
COG3850 |
Signal transduction histidine kinase NarQ, nitrate/nitrite-specific [Signal transduction ... |
100-488 |
7.24e-04 |
|
Signal transduction histidine kinase NarQ, nitrate/nitrite-specific [Signal transduction mechanisms];
Pssm-ID: 443059 [Multi-domain] Cd Length: 448 Bit Score: 42.95 E-value: 7.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 100 DAASHAQKGLVSQANDSLDNYFSAIAETAKMKADGKNELAQAYLFANVAQYRDELEGIVETLRVEKNREKDEAITTLNAT 179
Cdd:COG3850 33 ALLLLLERTLLRLLSLLASAGLLAALLAALLLLLSLGLLALLLALLLLLLLLLLAALLSLLLLLLLLLLLLLLLLLLLLA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 180 LATTTTAIAFVTGIAIILLTSIGALLYRQITRPLSRMQAMMSEIASSqDFTRRVPVGRLDEIGHSIVAFNGMIEKIQESS 259
Cdd:COG3850 113 AAINRKLALLRLLLALLLALLLAYLLRRRIVRPLRRLTQAAERIARG-DFDARVPVSGRDELGTLARAFNRMADELQELY 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 260 AQLKQKTADIQAMLQNMQQGILTVIDGAVIHAEYSAYLEDIFETKDIAGRGLMDLVFADTDLGADALSQVDAAAHACLGE 339
Cdd:COG3850 192 AELEEEEELEAELELLALLDELLLLAALLLLLALLLALLLAALLAALLLLLLLQDALAESELLALNILAGLLELLLALLL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 340 DCINFAFNQHLLVGEISKRMPDGRVKILDLSWSAITDEDDTIVRLMLCVRDVTELRKLAAEASEQRRRLDMIGEILAVSE 419
Cdd:COG3850 272 LLLASALLLLELELLALLLELVELLALAAAEEALLLLVELAALLLLLLLQAIANASLLLIALASVVAALLELASILALQA 351
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1208343461 420 EKFHHFIESSAGFISENERIIRKHSEADHAAIAELFRNMHTIKGNARTYNLQHLTDVVHETEQSYHELR 488
Cdd:COG3850 352 ALEAAAAGAALAAAAAAAGLARALAQAGADAAEALGLLAEASEGAAGQGAGLVDVEGGVAGEGGLVVLI 420
|
|
| COG4191 |
COG4191 |
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ... |
610-761 |
1.10e-03 |
|
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal transduction mechanisms];
Pssm-ID: 443345 [Multi-domain] Cd Length: 361 Bit Score: 42.09 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 610 VHIADNGYRLRGkSAGTLNNVFMHLLRNSMDhgiesaearaAKGKTPAGAISIEVGVDGGALQITLSDDGRGLalerirg 689
Cdd:COG4191 241 LDLPPDLPPVLG-DPGQLEQVLLNLLINAID----------AMEEGEGGRITISTRREGDYVVISVRDNGPGI------- 302
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1208343461 690 iamergwigpdetpgDEAIAELIFRPGFSTADtvtAVSGRGVGMDAVRDFLKRENGSIELRfTDDHKGAAFR 761
Cdd:COG4191 303 ---------------PPEVLERIFEPFFTTKP---VGKGTGLGLSISYGIVEKHGGRIEVE-SEPGGGTTFT 355
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
353-416 |
1.20e-03 |
|
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: 42.27 E-value: 1.20e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1208343461 353 GEISKRMPDGRVKILDLSWSAItDEDDTIVRLMLCVRDVTELRKLaAEASEQRRRLDMIGEILA 416
Cdd:COG5809 214 GEVRFWTKDGRWRLLEASGAPI-KKNGEVDGIVIIFRDITERKKL-EELLRKSEKLSVVGELAA 275
|
|
| HPT |
smart00073 |
Histidine Phosphotransfer domain; Contains an active histidine residue that mediates ... |
447-491 |
1.45e-03 |
|
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: 38.38 E-value: 1.45e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1208343461 447 DHAAIAELFRNMHTIKGNARTYNLQHLTDVVHETEQSYHELRQPD 491
Cdd:smart00073 29 DAQDVNEIFRAAHTLKGSAGSLGLQQLAQLCHQLENLLDALRSGE 73
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
267-391 |
1.73e-03 |
|
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: 38.94 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 267 ADIQAMLQNMQQGILTV-IDGAVIHAeySAYLEDIF--ETKDIAGRGLMDLVFADTDLG-ADALSQVDAAAHACLGedci 342
Cdd:pfam00989 1 EDLRAILESLPDGIFVVdEDGRILYV--NAAAEELLglSREEVIGKSLLDLIPEEDDAEvAELLRQALLQGEESRG---- 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1208343461 343 nfafnqhllvGEISKRMPDGRVKILDLSWSAITDEDDTIVRLMLCVRDV 391
Cdd:pfam00989 75 ----------FEVSFRVPDGRPRHVEVRASPVRDAGGEILGFLGVLRDI 113
|
|
| PRK10600 |
PRK10600 |
nitrate/nitrite two-component system sensor histidine kinase NarX; |
193-270 |
4.45e-03 |
|
nitrate/nitrite two-component system sensor histidine kinase NarX;
Pssm-ID: 182581 [Multi-domain] Cd Length: 569 Bit Score: 40.42 E-value: 4.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208343461 193 IAIILLTSIGALLY--RQITRPLSRMQAMMSEIaSSQDFTRRVPVGRLDEIGHSIVAFNGMIEKIQESSAQLKQ----KT 266
Cdd:PRK10600 131 AVFMALLLVFTIIWlrRRLLQPWRQLLSMANAV-SHRDFTQRANISGRDEMAMLGTALNNMSAELAESYAVLEQrvqeKT 209
|
....
gi 1208343461 267 ADIQ 270
Cdd:PRK10600 210 AGLE 213
|
|
| |
