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Conserved domains on  [gi|27382284|ref|NP_773813|]
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methyl accepting chemotaxis protein [Bradyrhizobium diazoefficiens USDA 110]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility, Signal transduction mechanisms];
265-615 6.32e-46

Methyl-accepting chemotaxis protein [Cell motility, Signal transduction mechanisms];


:

Pssm-ID: 223910  Cd Length: 408  Bit Score: 169.40  E-value: 6.32e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284 265 VELVMDNADYEASADRAWLLAIGIAALglVLAAIVGYLIARSISRPILSITNVMRELADGRLDVAVPTsKANDEVGAMVK 344
Cdd:COG0840  44 LDDAASAEAAALKAVLKFLLISLLVAI--IVVLVLAILLLRAILEPISDLLEVVERIAAGDLTKRIDE-SSNDEFGQLAK 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284 345 AVAVFRDNAVNFDKlqaeqleakaqseaekrrafaaladnfeaSIREVVTTVSAAAVEMEHTARSMSAIVEQSREQTRTV 424
Cdd:COG0840 121 SFNEMILNLRQIID-----------------------------AVQDNAEALSGASEEIAASATELSARADQQAESLEEV 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284 425 SSASALASENVQTVAAAAEELSSSMTEISRRLAHATEVVGKAASD----GRQSNARVQSLADAAQKIGDVVSFINGIAGQ 500
Cdd:COG0840 172 ASAIEELSETVKEVAFNAKEAAALASEASQVAEEGGEEVRQAVEQmqeiAEELAEVVKKLSESSQEIEEITSVINSIAEQ 251
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284 501 TNLLALNATIEAARAGEAGRGFAVVASEVKALATQTAKATEEIGAQVTAVQGETTGAVDGIQS----------------- 563
Cdd:COG0840 252 TNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSADSAKEIGLLIEEIQNEAADAVEHMEEsasevsegvklveetgs 331
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 27382284 564 ----ICATIQQVDEISAAIAAAVGQQGTATQEIAQNVQQAAARTGEVSQNISGVTA 615
Cdd:COG0840 332 slgeIAAAIEEVSQLISEIAAATEEQTAVLEEINASIEELDDVTQENAAAVEELAA 387
dCache_3 super family cl20738
Double sensory domain of two-component sensor kinase; Cache_3 is the periplasmic sensor ...
43-274 9.23e-24

Double sensory domain of two-component sensor kinase; Cache_3 is the periplasmic sensor domains of sensor histidine kinase of E. coli DcuS. This domain forms one of the components of the two-component signalling system that allows bacteria to adapt to changing environments. The ability of bacteria to monitor and adapt to their environment is crucial to their survival, and two-component signal transduction systems mediate most of these adaptive responses. One component is a histidine kinase sensor - this domain - most commonly part of a homodimeric transmembrane sensor protein, and the second component is a cytoplasmic response regulator. The two components interact in tandem through a phospho-transfer cascade.


The actual alignment was detected with superfamily member pfam14827:

Pssm-ID: 317262  Cd Length: 235  Bit Score: 101.75  E-value: 9.23e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284    43 QRELRSHYDALQSRIAEESHRAAAMSAVVAAMPATQEAMAKQDREALVRLFGPVFtaikSDYGVDQFQFHVPPATSYLRV 122
Cdd:pfam14827   5 KEQLEAALQTAENLLEQEEDQLLALARLLASDPGVIEAISTGDREELERLLDSIW----QDLGIEQIVLHDADGTVILRS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284   123 hQPAKFGDDLSGFRKTVVVANQDRKVVVGLEGGVAGLGIRGVVPI-AQGAKHLGTVEFGLTFGQpFLDDFKTNRHVDVAF 201
Cdd:pfam14827  81 -EPGKSGDDLSSFRLTVRSTLRGETPLAGIECGDAGCGFRVVAPVlKDGKDHVGAVEFGVSLDD-LLREFKEDTGADAAI 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27382284   202 HLADGSG--FKLFGGTLKGKSFFDTADYGRAAEGGFTV-RQARLDTTPVAALLGPIRDFSGKPLGAVELVMDNADY 274
Cdd:pfam14827 159 LVRDKRGatSASAATSQLLGAPIDRPLLKALLEQGPVSfRELEIDGRSYLVAYLPLKDYDGEPVGVLVIGKDVTAA 234
 
Name Accession Description Interval E-value
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility, Signal transduction mechanisms];
265-615 6.32e-46

Methyl-accepting chemotaxis protein [Cell motility, Signal transduction mechanisms];


Pssm-ID: 223910  Cd Length: 408  Bit Score: 169.40  E-value: 6.32e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284 265 VELVMDNADYEASADRAWLLAIGIAALglVLAAIVGYLIARSISRPILSITNVMRELADGRLDVAVPTsKANDEVGAMVK 344
Cdd:COG0840  44 LDDAASAEAAALKAVLKFLLISLLVAI--IVVLVLAILLLRAILEPISDLLEVVERIAAGDLTKRIDE-SSNDEFGQLAK 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284 345 AVAVFRDNAVNFDKlqaeqleakaqseaekrrafaaladnfeaSIREVVTTVSAAAVEMEHTARSMSAIVEQSREQTRTV 424
Cdd:COG0840 121 SFNEMILNLRQIID-----------------------------AVQDNAEALSGASEEIAASATELSARADQQAESLEEV 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284 425 SSASALASENVQTVAAAAEELSSSMTEISRRLAHATEVVGKAASD----GRQSNARVQSLADAAQKIGDVVSFINGIAGQ 500
Cdd:COG0840 172 ASAIEELSETVKEVAFNAKEAAALASEASQVAEEGGEEVRQAVEQmqeiAEELAEVVKKLSESSQEIEEITSVINSIAEQ 251
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284 501 TNLLALNATIEAARAGEAGRGFAVVASEVKALATQTAKATEEIGAQVTAVQGETTGAVDGIQS----------------- 563
Cdd:COG0840 252 TNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSADSAKEIGLLIEEIQNEAADAVEHMEEsasevsegvklveetgs 331
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 27382284 564 ----ICATIQQVDEISAAIAAAVGQQGTATQEIAQNVQQAAARTGEVSQNISGVTA 615
Cdd:COG0840 332 slgeIAAAIEEVSQLISEIAAATEEQTAVLEEINASIEELDDVTQENAAAVEELAA 387
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
377-618 5.81e-42

Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.


Pssm-ID: 214599  Cd Length: 262  Bit Score: 154.37  E-value: 5.81e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284    377 AFAALADNFEASIREVVTTVSAAAVEMEHtarsMSAIVEQSREQTRTVSSASALASENVQTVAAAAEELSSSMTEIsrrl 456
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEE----LSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQI---- 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284    457 ahaTEVVGKAASdgrqsnaRVQSLADAAQKIGDVVSFINGIAGQTNLLALNATIEAARAGEAGRGFAVVASEVKALATQT 536
Cdd:smart00283  73 ---REVVEEAVS-------AVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERS 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284    537 AKATEEIGAQVTAVQGETTGAV---------------------DGIQSICATIQQVDEISAAIAAAVGQQGTATQEIAQN 595
Cdd:smart00283 143 AESAKEIESLIKEIQEETNEAVaameessseveegvelveetgDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAA 222
                          250       260
                   ....*....|....*....|...
gi 27382284    596 VQQAAARTGEVSQNISGVTAGIA 618
Cdd:smart00283 223 IDEIAQVTQETAAMSEEISAAAE 245
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
431-614 3.24e-39

Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis proteins (MCPs or chemotaxis receptors) are an integral part of the transmembrane protein complex that controls bacterial chemotaxis, together with the histidine kinase CheA, the receptor-coupling protein CheW, receptor-modification enzymes, and localized phosphatases. MCPs contain a four helix trans membrane region, an N-terminal periplasmic ligand binding domain, and a C-terminal HAMP domain followed by a cytoplasmic signaling domain. This C-terminal signaling domain dimerizes into a four-helix bundle and interacts with CheA through the adaptor protein CheW.


Pssm-ID: 206779  Cd Length: 200  Bit Score: 144.69  E-value: 3.24e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284 431 ASENVQTVAAAAEELSSSMTEISRRLAHATEVVGKAASDGRQS----NARVQSLADAAQKIGDVVSFINGIAGQTNLLAL 506
Cdd:cd11386   6 SIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESvdeaVSAVEELEESSAEIGEIVEVIDDIAEQTNLLAL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284 507 NATIEAARAGEAGRGFAVVASEVKALATQTAKATEEIGAQVTAVQGETTGAVDGIQSICATIQ----QVDEISAA---IA 579
Cdd:cd11386  86 NAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEegveLVEETGRAfeeIV 165
                       170       180       190
                ....*....|....*....|....*....|....*
gi 27382284 580 AAVGQQGTATQEIAQNVQQAAARTGEVSQNISGVT 614
Cdd:cd11386 166 ASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
PRK09793 PRK09793
methyl-accepting protein IV; Provisional
378-620 3.34e-30

methyl-accepting protein IV; Provisional


Pssm-ID: 182079  Cd Length: 533  Bit Score: 125.57  E-value: 3.34e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284  378 FAALaDNFEASIREVVTTVSAAAVEMeHTArsMSAIVEQSRE-QTRTVSSASALAsenvQTvAAAAEELSSSMTEISRRL 456
Cdd:PRK09793 249 FASL-KTMQQALRGTVSDVRKGSQEM-HIG--IAEIVAGNNDlSSRTEQQAASLA----QT-AASMEQLTATVGQNADNA 319
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284  457 AHATEVVGKAASDGRQSNARV-------QSLADAAQKIGDVVSFINGIAGQTNLLALNATIEAARAGEAGRGFAVVASEV 529
Cdd:PRK09793 320 RQASELAKNAATTAQAGGVQVstmthtmQEIATSSQKIGDIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEV 399
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284  530 KALATQTAKATEEIGA----QVTAVQ---GETTGAVDGIQSICATIQQVDEISAAIAAAVGQQGTATQEIAQNVQQAAAR 602
Cdd:PRK09793 400 RNLASRSAQAAKEIKGlieeSVNRVQqgsKLVNNAAATMTDIVSSVTRVNDIMGEIASASEEQRRGIEQVAQAVSQMDQV 479
                        250
                 ....*....|....*...
gi 27382284  603 TgevSQNISGVTAGIAAT 620
Cdd:PRK09793 480 T---QQNASLVEEAAVAT 494
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
464-620 2.82e-28

Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to transduce the signal to CheA since it is highly conserved in very diverse MCPs.


Pssm-ID: 278444  Cd Length: 207  Bit Score: 114.08  E-value: 2.82e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284   464 GKAASDGRQSNARVQS-------LADAAQKIGDVVSFINGIAGQTNLLALNATIEAARAGEAGRGFAVVASEVKALATQT 536
Cdd:pfam00015   9 EEALDEMSQIGQVVDDavetmeeLETSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLAERS 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284   537 AKATEEIGAQVTAVQGETTGAVDGIQSICA-------TIQQVDEISAAIAAAVGQQGTATQEIAQNVQQAAARTGEVSQN 609
Cdd:pfam00015  89 AQAAKEIEALIEEIVKQTNDSTASIQQTRTevevgstIVESTGEALKEIVEAVAEIADIVQEIAAASDEQSAGIDQVNQA 168
                         170
                  ....*....|....
gi 27382284   610 ---ISGVTAGIAAT 620
Cdd:pfam00015 169 varIDQVTQQNAAL 182
dCache_3 pfam14827
Double sensory domain of two-component sensor kinase; Cache_3 is the periplasmic sensor ...
43-274 9.23e-24

Double sensory domain of two-component sensor kinase; Cache_3 is the periplasmic sensor domains of sensor histidine kinase of E. coli DcuS. This domain forms one of the components of the two-component signalling system that allows bacteria to adapt to changing environments. The ability of bacteria to monitor and adapt to their environment is crucial to their survival, and two-component signal transduction systems mediate most of these adaptive responses. One component is a histidine kinase sensor - this domain - most commonly part of a homodimeric transmembrane sensor protein, and the second component is a cytoplasmic response regulator. The two components interact in tandem through a phospho-transfer cascade.


Pssm-ID: 317262  Cd Length: 235  Bit Score: 101.75  E-value: 9.23e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284    43 QRELRSHYDALQSRIAEESHRAAAMSAVVAAMPATQEAMAKQDREALVRLFGPVFtaikSDYGVDQFQFHVPPATSYLRV 122
Cdd:pfam14827   5 KEQLEAALQTAENLLEQEEDQLLALARLLASDPGVIEAISTGDREELERLLDSIW----QDLGIEQIVLHDADGTVILRS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284   123 hQPAKFGDDLSGFRKTVVVANQDRKVVVGLEGGVAGLGIRGVVPI-AQGAKHLGTVEFGLTFGQpFLDDFKTNRHVDVAF 201
Cdd:pfam14827  81 -EPGKSGDDLSSFRLTVRSTLRGETPLAGIECGDAGCGFRVVAPVlKDGKDHVGAVEFGVSLDD-LLREFKEDTGADAAI 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27382284   202 HLADGSG--FKLFGGTLKGKSFFDTADYGRAAEGGFTV-RQARLDTTPVAALLGPIRDFSGKPLGAVELVMDNADY 274
Cdd:pfam14827 159 LVRDKRGatSASAATSQLLGAPIDRPLLKALLEQGPVSfRELEIDGRSYLVAYLPLKDYDGEPVGVLVIGKDVTAA 234
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
283-367 2.88e-07

TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the torCAD operon that encodes the pterin molybdenum cofactor-containing enzyme trimethylamine-N-oxide (TMAO) reductase (TorA), a cognate chaperone (TorD), and a penta-haem cytochrome (TorC). TorS works together with the inducer-binding protein TorT and the response regulator TorR. TorS contains histidine kinase ATPase (pfam02518), HAMP (pfam00672), phosphoacceptor (pfam00512), and phosphotransfer (pfam01627) domains and a response regulator receiver domain (pfam00072). [Signal transduction, Two-component systems]


Pssm-ID: 274362  Cd Length: 968  Bit Score: 54.01  E-value: 2.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284   283 LLAIGIaaLGLVLAAIVGY-LIARSISRPILSITNVMRELADGRLDVAVPTsKANDEVGAMVKAVAVFRDNAVNFDKLQA 361
Cdd:TIGR02956 333 LLITGM--LGLVILVFIMWrVVYRSVILRLNQHTQALLRLALGDLDISLDA-RGDDELAHMGRAIEAFRDTAAHNLKLQA 409

                  ....*.
gi 27382284   362 EQLEAK 367
Cdd:TIGR02956 410 DERQVA 415
 
Name Accession Description Interval E-value
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility, Signal transduction mechanisms];
265-615 6.32e-46

Methyl-accepting chemotaxis protein [Cell motility, Signal transduction mechanisms];


Pssm-ID: 223910  Cd Length: 408  Bit Score: 169.40  E-value: 6.32e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284 265 VELVMDNADYEASADRAWLLAIGIAALglVLAAIVGYLIARSISRPILSITNVMRELADGRLDVAVPTsKANDEVGAMVK 344
Cdd:COG0840  44 LDDAASAEAAALKAVLKFLLISLLVAI--IVVLVLAILLLRAILEPISDLLEVVERIAAGDLTKRIDE-SSNDEFGQLAK 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284 345 AVAVFRDNAVNFDKlqaeqleakaqseaekrrafaaladnfeaSIREVVTTVSAAAVEMEHTARSMSAIVEQSREQTRTV 424
Cdd:COG0840 121 SFNEMILNLRQIID-----------------------------AVQDNAEALSGASEEIAASATELSARADQQAESLEEV 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284 425 SSASALASENVQTVAAAAEELSSSMTEISRRLAHATEVVGKAASD----GRQSNARVQSLADAAQKIGDVVSFINGIAGQ 500
Cdd:COG0840 172 ASAIEELSETVKEVAFNAKEAAALASEASQVAEEGGEEVRQAVEQmqeiAEELAEVVKKLSESSQEIEEITSVINSIAEQ 251
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284 501 TNLLALNATIEAARAGEAGRGFAVVASEVKALATQTAKATEEIGAQVTAVQGETTGAVDGIQS----------------- 563
Cdd:COG0840 252 TNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSADSAKEIGLLIEEIQNEAADAVEHMEEsasevsegvklveetgs 331
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 27382284 564 ----ICATIQQVDEISAAIAAAVGQQGTATQEIAQNVQQAAARTGEVSQNISGVTA 615
Cdd:COG0840 332 slgeIAAAIEEVSQLISEIAAATEEQTAVLEEINASIEELDDVTQENAAAVEELAA 387
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
377-618 5.81e-42

Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.


Pssm-ID: 214599  Cd Length: 262  Bit Score: 154.37  E-value: 5.81e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284    377 AFAALADNFEASIREVVTTVSAAAVEMEHtarsMSAIVEQSREQTRTVSSASALASENVQTVAAAAEELSSSMTEIsrrl 456
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEE----LSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQI---- 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284    457 ahaTEVVGKAASdgrqsnaRVQSLADAAQKIGDVVSFINGIAGQTNLLALNATIEAARAGEAGRGFAVVASEVKALATQT 536
Cdd:smart00283  73 ---REVVEEAVS-------AVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERS 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284    537 AKATEEIGAQVTAVQGETTGAV---------------------DGIQSICATIQQVDEISAAIAAAVGQQGTATQEIAQN 595
Cdd:smart00283 143 AESAKEIESLIKEIQEETNEAVaameessseveegvelveetgDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAA 222
                          250       260
                   ....*....|....*....|...
gi 27382284    596 VQQAAARTGEVSQNISGVTAGIA 618
Cdd:smart00283 223 IDEIAQVTQETAAMSEEISAAAE 245
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
431-614 3.24e-39

Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis proteins (MCPs or chemotaxis receptors) are an integral part of the transmembrane protein complex that controls bacterial chemotaxis, together with the histidine kinase CheA, the receptor-coupling protein CheW, receptor-modification enzymes, and localized phosphatases. MCPs contain a four helix trans membrane region, an N-terminal periplasmic ligand binding domain, and a C-terminal HAMP domain followed by a cytoplasmic signaling domain. This C-terminal signaling domain dimerizes into a four-helix bundle and interacts with CheA through the adaptor protein CheW.


Pssm-ID: 206779  Cd Length: 200  Bit Score: 144.69  E-value: 3.24e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284 431 ASENVQTVAAAAEELSSSMTEISRRLAHATEVVGKAASDGRQS----NARVQSLADAAQKIGDVVSFINGIAGQTNLLAL 506
Cdd:cd11386   6 SIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESvdeaVSAVEELEESSAEIGEIVEVIDDIAEQTNLLAL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284 507 NATIEAARAGEAGRGFAVVASEVKALATQTAKATEEIGAQVTAVQGETTGAVDGIQSICATIQ----QVDEISAA---IA 579
Cdd:cd11386  86 NAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEegveLVEETGRAfeeIV 165
                       170       180       190
                ....*....|....*....|....*....|....*
gi 27382284 580 AAVGQQGTATQEIAQNVQQAAARTGEVSQNISGVT 614
Cdd:cd11386 166 ASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
PRK09793 PRK09793
methyl-accepting protein IV; Provisional
378-620 3.34e-30

methyl-accepting protein IV; Provisional


Pssm-ID: 182079  Cd Length: 533  Bit Score: 125.57  E-value: 3.34e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284  378 FAALaDNFEASIREVVTTVSAAAVEMeHTArsMSAIVEQSRE-QTRTVSSASALAsenvQTvAAAAEELSSSMTEISRRL 456
Cdd:PRK09793 249 FASL-KTMQQALRGTVSDVRKGSQEM-HIG--IAEIVAGNNDlSSRTEQQAASLA----QT-AASMEQLTATVGQNADNA 319
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284  457 AHATEVVGKAASDGRQSNARV-------QSLADAAQKIGDVVSFINGIAGQTNLLALNATIEAARAGEAGRGFAVVASEV 529
Cdd:PRK09793 320 RQASELAKNAATTAQAGGVQVstmthtmQEIATSSQKIGDIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEV 399
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284  530 KALATQTAKATEEIGA----QVTAVQ---GETTGAVDGIQSICATIQQVDEISAAIAAAVGQQGTATQEIAQNVQQAAAR 602
Cdd:PRK09793 400 RNLASRSAQAAKEIKGlieeSVNRVQqgsKLVNNAAATMTDIVSSVTRVNDIMGEIASASEEQRRGIEQVAQAVSQMDQV 479
                        250
                 ....*....|....*...
gi 27382284  603 TgevSQNISGVTAGIAAT 620
Cdd:PRK09793 480 T---QQNASLVEEAAVAT 494
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
464-620 2.82e-28

Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to transduce the signal to CheA since it is highly conserved in very diverse MCPs.


Pssm-ID: 278444  Cd Length: 207  Bit Score: 114.08  E-value: 2.82e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284   464 GKAASDGRQSNARVQS-------LADAAQKIGDVVSFINGIAGQTNLLALNATIEAARAGEAGRGFAVVASEVKALATQT 536
Cdd:pfam00015   9 EEALDEMSQIGQVVDDavetmeeLETSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLAERS 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284   537 AKATEEIGAQVTAVQGETTGAVDGIQSICA-------TIQQVDEISAAIAAAVGQQGTATQEIAQNVQQAAARTGEVSQN 609
Cdd:pfam00015  89 AQAAKEIEALIEEIVKQTNDSTASIQQTRTevevgstIVESTGEALKEIVEAVAEIADIVQEIAAASDEQSAGIDQVNQA 168
                         170
                  ....*....|....
gi 27382284   610 ---ISGVTAGIAAT 620
Cdd:pfam00015 169 varIDQVTQQNAAL 182
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
282-619 3.90e-27

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008  Cd Length: 553  Bit Score: 116.26  E-value: 3.90e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284  282 WLLAIGIAALGLVLAAiVGYLIARSISRPILSITNVMRELADGRLDVAVPTSKANdEVGAMVKAVavfrdnavnfDKLQA 361
Cdd:PRK15048 192 WQLAVIALVVVLILLV-AWYGIRRMLLTPLAKIIAHIREIAGGNLANTLTIDGRS-EMGDLAQSV----------SHMQR 259
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284  362 EQLEAKAQSEaEKRRAFAALADNFEASIREVVTTVSAAAVEMEHTARSM---SAIVEQSREQTRTVSSASALASENVQTV 438
Cdd:PRK15048 260 SLTDTVTHVR-EGSDAIYAGTREIAAGNTDLSSRTEQQASALEETAASMeqlTATVKQNADNARQASQLAQSASDTAQHG 338
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284  439 AAAAEELSSSMTEIsrrlahatevvgkaasdgrqsnarvqslADAAQKIGDVVSFINGIAGQTNLLALNATIEAARAGEA 518
Cdd:PRK15048 339 GKVVDGVVKTMHEI----------------------------ADSSKKIADIISVIDGIAFQTNILALNAAVEAARAGEQ 390
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284  519 GRGFAVVASEVKALATQTAKATEEIGAQVT-AVQGETTGAV------DGIQSICATIQQVDEISAAIAAAVGQQGTA--- 588
Cdd:PRK15048 391 GRGFAVVAGEVRNLASRSAQAAKEIKALIEdSVSRVDTGSVlvesagETMNNIVNAVTRVTDIMGEIASASDEQSRGidq 470
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 27382284  589 -----------TQEIAQNVQQAAARTGEVSQNISGVTAGIAA 619
Cdd:PRK15048 471 valavsemdrvTQQNASLVQESAAAAAALEEQASRLTQAVSA 512
PRK15041 PRK15041
methyl-accepting chemotaxis protein I; Provisional
272-618 2.72e-24

methyl-accepting chemotaxis protein I; Provisional


Pssm-ID: 185001  Cd Length: 554  Bit Score: 107.73  E-value: 2.72e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284  272 ADYEASADRAWLLAIGIAALGLVLAAIVGYLIARSISRPILSITNVMRELADGRLDVAVPTSKANdEVGAMvkavavfrd 351
Cdd:PRK15041 183 SDNNASYSQAMWILVGVMIVVLAVIFAVWFGIKASLVAPMNRLIDSIRHIAGGDLVKPIEVDGSN-EMGQL--------- 252
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284  352 nAVNFDKLQAEQLeakaQSEAEKRRAFAAL---ADNFEASIREVVTTVSAAAVEMEHTARSM---SAIVEQSREQTRTVS 425
Cdd:PRK15041 253 -AESLRHMQGELM----RTVGDVRNGANAIysgASEIATGNNDLSSRTEQQAASLEETAASMeqlTATVKQNAENARQAS 327
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284  426 SASALASENVQTVAAAAEELSSSMTEIsrrlahatevvgkaasdgrqsnarvqslADAAQKIGDVVSFINGIAGQTNLLA 505
Cdd:PRK15041 328 HLALSASETAQRGGKVVDNVVQTMRDI----------------------------STSSQKIADIISVIDGIAFQTNILA 379
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284  506 LNATIEAARAGEAGRGFAVVASEVKALATQTAKATEEI-------------GAQVTAVQGETTG----AVDGIQSICATI 568
Cdd:PRK15041 380 LNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIksliedsvgkvdvGSTLVESAGETMAeivsAVTRVTDIMGEI 459
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 27382284  569 QQV-DEISAAI---AAAVGQQGTATQEIAQNVQQAAARTGEVSQNISGVTAGIA 618
Cdd:PRK15041 460 ASAsDEQSRGIdqvGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRLTEAVA 513
dCache_3 pfam14827
Double sensory domain of two-component sensor kinase; Cache_3 is the periplasmic sensor ...
43-274 9.23e-24

Double sensory domain of two-component sensor kinase; Cache_3 is the periplasmic sensor domains of sensor histidine kinase of E. coli DcuS. This domain forms one of the components of the two-component signalling system that allows bacteria to adapt to changing environments. The ability of bacteria to monitor and adapt to their environment is crucial to their survival, and two-component signal transduction systems mediate most of these adaptive responses. One component is a histidine kinase sensor - this domain - most commonly part of a homodimeric transmembrane sensor protein, and the second component is a cytoplasmic response regulator. The two components interact in tandem through a phospho-transfer cascade.


Pssm-ID: 317262  Cd Length: 235  Bit Score: 101.75  E-value: 9.23e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284    43 QRELRSHYDALQSRIAEESHRAAAMSAVVAAMPATQEAMAKQDREALVRLFGPVFtaikSDYGVDQFQFHVPPATSYLRV 122
Cdd:pfam14827   5 KEQLEAALQTAENLLEQEEDQLLALARLLASDPGVIEAISTGDREELERLLDSIW----QDLGIEQIVLHDADGTVILRS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284   123 hQPAKFGDDLSGFRKTVVVANQDRKVVVGLEGGVAGLGIRGVVPI-AQGAKHLGTVEFGLTFGQpFLDDFKTNRHVDVAF 201
Cdd:pfam14827  81 -EPGKSGDDLSSFRLTVRSTLRGETPLAGIECGDAGCGFRVVAPVlKDGKDHVGAVEFGVSLDD-LLREFKEDTGADAAI 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27382284   202 HLADGSG--FKLFGGTLKGKSFFDTADYGRAAEGGFTV-RQARLDTTPVAALLGPIRDFSGKPLGAVELVMDNADY 274
Cdd:pfam14827 159 LVRDKRGatSASAATSQLLGAPIDRPLLKALLEQGPVSfRELEIDGRSYLVAYLPLKDYDGEPVGVLVIGKDVTAA 234
NtrY COG5000
Signal transduction histidine kinase involved in nitrogen fixation and metabolism regulation ...
283-497 1.34e-09

Signal transduction histidine kinase involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms];


Pssm-ID: 227333  Cd Length: 712  Bit Score: 61.32  E-value: 1.34e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284 283 LLAIGIAALGLVLAAIVGYLIARSISRPILSITNVMRELADGRLDVAVPTSKANDEVGAMVKAvavfrdnavnFDKLQAE 362
Cdd:COG5000 281 LLYLSTALLVLLAAIWTAIAFARRIVRPIRKLIEAADEVADGDLDVQVPVRRVDEDVGRLSKA----------FNKMTEQ 350
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284 363 QLEAKAQSEAEKRRafaalADNFEASIREVVTTVSAAAVEMEHtaRSMSAIVEQSREQTRTVSSASALAsenvQTVAAAA 442
Cdd:COG5000 351 LSSQQEALERAKDA-----LEQRRRFLEAVLSGLTAGVIGFDN--RGCITTVNPSAEQILGKPFDQLLG----QSLSAIA 419
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 27382284 443 EELSSSMTEISRRLAHATEVVGKAASDGRQSNARVQSLADAAQKIGDVVSFINGI 497
Cdd:COG5000 420 PELEEVFAEAGAAARTDKRVEVKLAREGEERTLNVQATREPEDNGNGYVVTFDDI 474
HAMP pfam00672
HAMP domain;
285-352 2.85e-09

HAMP domain;


Pssm-ID: 307012  Cd Length: 69  Bit Score: 55.65  E-value: 2.85e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27382284   285 AIGIAALGLVLAAIVGYLIARSISRPILSITNVMRELADGRLDVAVPTSKanDEVGAMVKAVAVFRDN 352
Cdd:pfam00672   1 LLLVLLIALLLALLLAWLLARRILRPLRRLAEAARRIASGDLDVPLESGR--DEIGELARAFNQMAER 66
VicK COG5002
Signal transduction histidine kinase [Signal transduction mechanisms];
253-382 5.30e-08

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 227335  Cd Length: 459  Bit Score: 55.51  E-value: 5.30e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284 253 PIRDFSgKPLGAVELVMDNAD-YEASADRAWLLAIGIAaLGLVLAAIVGYLIARSISRPILSITNVMRELADGRLDVAVp 331
Cdd:COG5002   1 PIKVEK-KVIGAIYIEASIEDvYNQMNFINNILISGTL-IALIITALLGILLARTITKPITDMRKQAVDMARGNYSRKV- 77
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 27382284 332 TSKANDEVGAMvkavavfrdnAVNFDKLQAEQLEAKAQSEAEKRRAFAALA 382
Cdd:COG5002  78 KVYGTDEIGEL----------ADSFNDLTKRVQEAQANTEQERRKLDSVLA 118
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
283-367 2.88e-07

TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the torCAD operon that encodes the pterin molybdenum cofactor-containing enzyme trimethylamine-N-oxide (TMAO) reductase (TorA), a cognate chaperone (TorD), and a penta-haem cytochrome (TorC). TorS works together with the inducer-binding protein TorT and the response regulator TorR. TorS contains histidine kinase ATPase (pfam02518), HAMP (pfam00672), phosphoacceptor (pfam00512), and phosphotransfer (pfam01627) domains and a response regulator receiver domain (pfam00072). [Signal transduction, Two-component systems]


Pssm-ID: 274362  Cd Length: 968  Bit Score: 54.01  E-value: 2.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284   283 LLAIGIaaLGLVLAAIVGY-LIARSISRPILSITNVMRELADGRLDVAVPTsKANDEVGAMVKAVAVFRDNAVNFDKLQA 361
Cdd:TIGR02956 333 LLITGM--LGLVILVFIMWrVVYRSVILRLNQHTQALLRLALGDLDISLDA-RGDDELAHMGRAIEAFRDTAAHNLKLQA 409

                  ....*.
gi 27382284   362 EQLEAK 367
Cdd:TIGR02956 410 DERQVA 415
PHA03332 PHA03332
membrane glycoprotein; Provisional
375-551 4.07e-06

membrane glycoprotein; Provisional


Pssm-ID: 223047  Cd Length: 1328  Bit Score: 50.35  E-value: 4.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284   375 RRAFAALADNFEASIREVVTTVSAaaVEMEHTARSMSAIVEQSREQTRTVS---SASALASENVQTVAAAAEeLSSSMTE 451
Cdd:PHA03332  806 RVSIAGLLLEFEYSNERYKNTLSV--LDLWHETVKMFAPRRFGGSVMAGDAiglSAAAFTMASAALNAATQA-LAVATLY 882
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284   452 ISRrLAHATEVVGKAASDGRQSNARVQSLADAAQKIGDVVSFInGIAGQTNLLALNATIEAARAgEAGRGFAVVASEVKA 531
Cdd:PHA03332  883 VNQ-LLQATAATAEMASKIGGLNARVDKTSDVITKLGDTIAKI-SATLDNNIRAVNGRVSDLED-QVNLRFLAVATNFNT 959
                         170       180
                  ....*....|....*....|....
gi 27382284   532 LATQTAKA----TEEIGAQVTAVQ 551
Cdd:PHA03332  960 LATQLKELgtttNERIEEVMAAAL 983
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
386-492 1.72e-04

Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.


Pssm-ID: 214599  Cd Length: 262  Bit Score: 43.81  E-value: 1.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284    386 EASIREVVTTVSAAAVEMEHTARSMSAIVEQSREQTRTVSSASALASEN---VQTVAAAAEELSSSMTEISRRLAHATEV 462
Cdd:smart00283 150 ESLIKEIQEETNEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIadlVQEIAAATDEQAAGSEEVNAAIDEIAQV 229
                           90       100       110
                   ....*....|....*....|....*....|
gi 27382284    463 VGKAASDGRQSNARVQSLADAAQKIGDVVS 492
Cdd:smart00283 230 TQETAAMSEEISAAAEELSGLAEELDELVE 259
HAMP COG2770
HAMP domain [Signal transduction mechanisms];
288-359 3.01e-04

HAMP domain [Signal transduction mechanisms];


Pssm-ID: 225359  Cd Length: 83  Bit Score: 40.82  E-value: 3.01e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27382284 288 IAALGLVLAAIVGYLIARSISRPILSITNVMRELADGRLDVAVPTsKANDEVGAMVKAVAVFRDNAVNFDKL 359
Cdd:COG2770  11 LVLALVLILAVLLLAAARRVTRPLRRLADLAQNLALGDLSAEIPQ-PMLDEIGELAKAFNRMRDSLQRALSA 81
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
305-352 3.70e-04

HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;


Pssm-ID: 197640  Cd Length: 53  Bit Score: 40.31  E-value: 3.70e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 27382284    305 RSISRPILSITNVMRELADGRLDVAVPTSkANDEVGAMVKAVAVFRDN 352
Cdd:smart00304   1 RRLLRPLRRLAEAAQRIADGDLTVRLPVD-GRDEIGELARAFNEMADR 47
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
307-352 5.22e-04

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 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: 100122  Cd Length: 48  Bit Score: 39.93  E-value: 5.22e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 27382284 307 ISRPILSITNVMRELADGRLDVAVPTSKaNDEVGAMVKAVAVFRDN 352
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGDLDVRLPVTG-RDEIGELARAFNQMAER 45
PRK10549 PRK10549
signal transduction histidine-protein kinase BaeS; Provisional
253-380 5.76e-04

signal transduction histidine-protein kinase BaeS; Provisional


Pssm-ID: 182539  Cd Length: 466  Bit Score: 42.70  E-value: 5.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284  253 PIRdFSGKPLGAV-----ELVMDNADYeaSADR-----AWLlaigIAALGLVLAAIVGYLIARSISRPILSITNVMRELA 322
Cdd:PRK10549 131 PIL-VNGAEVGWViaspvERLTRNTDI--NFDKqqrrtSWL----IVALSTLLAALATFLLARGLLAPVKRLVEGTHKLA 203
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 27382284  323 DGRLDVAV-PTSKanDEVGAMvkavavfrdnAVNFDKLqAEQLEAKAQSeaekRRAFAA 380
Cdd:PRK10549 204 AGDFTTRVtPTSR--DELGRL----------AQDFNQL-ASTLEKNEQM----RRDFMA 245
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
382-492 1.02e-03

Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to transduce the signal to CheA since it is highly conserved in very diverse MCPs.


Pssm-ID: 278444  Cd Length: 207  Bit Score: 40.89  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284   382 ADNFEASIREVVTTVSAAAVEMEHT---ARSMSAIVEQSREQTRTVSSASALASENVQTVAAAAEELSSSMTEISRRLAH 458
Cdd:pfam00015  92 AKEIEALIEEIVKQTNDSTASIQQTrteVEVGSTIVESTGEALKEIVEAVAEIADIVQEIAAASDEQSAGIDQVNQAVAR 171
                          90       100       110
                  ....*....|....*....|....*....|....
gi 27382284   459 ATEVVGKAASDGRQSNARVQSLADAAQKIGDVVS 492
Cdd:pfam00015 172 IDQVTQQNAALVEESAAAAETLEEQAEELTASVA 205
EspB pfam05802
Enterobacterial EspB protein; EspB is a type-III-secreted pore-forming protein of ...
321-514 1.02e-03

Enterobacterial EspB protein; EspB is a type-III-secreted pore-forming protein of enteropathogenic Escherichia coli (EPEC) which is essential for EPEC pathogenesis. EspB is also found in Citrobacter rodentium.


Pssm-ID: 310415  Cd Length: 317  Bit Score: 41.61  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284   321 LADGRLDVAVPTSKANDEVGAMVKAVAVFRDNAVNfDKLQAEQLEAKAQSEAEKRRAFAALADNFEASIREVVTTVSAAA 400
Cdd:pfam05802  39 LTDGKVDISKLMLEIQKLLGKMVTTLQDYQQRQLA-QSYQIQQAVFESQNKAIEEKKAAATAALVGGAISSVLGILGSFA 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284   401 VeMEHTARSMSAIVEQ-SREQTRTVSSASALASENV----QTVAAAAEELSS----SMTEISRRLAHATEVVGKAASDGR 471
Cdd:pfam05802 118 A-INSATKGASDIAQKaTSASSKAVNAASEVATKALvkatESVADAAEEASStmqqAMATATKAASRTSGVADDVATSAQ 196
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 27382284   472 QSNARVQSLADAAQKIGDVVSFING---IAGQTNLLALNATIEAAR 514
Cdd:pfam05802 197 KASQVAEEAADAAQKASRLSRFTAAvdkITGSTAFVAVTSLAEGTK 242
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility, Signal transduction mechanisms];
343-465 3.48e-03

Methyl-accepting chemotaxis protein [Cell motility, Signal transduction mechanisms];


Pssm-ID: 223910  Cd Length: 408  Bit Score: 40.36  E-value: 3.48e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284 343 VKAVAVFRDNAVNFDKLQAEQLEAKAQSEAEKRRAFAALADNFEASIREVVTTVSAAAVEMEHTARSMSAIVEQSREQTR 422
Cdd:COG0840 280 VRKLAERSADSAKEIGLLIEEIQNEAADAVEHMEESASEVSEGVKLVEETGSSLGEIAAAIEEVSQLISEIAAATEEQTA 359
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 27382284 423 T---VSSASALASENVQTVAAAAEELSSSMTEISRRLAHATEVVGK 465
Cdd:COG0840 360 VleeINASIEELDDVTQENAAAVEELAAASEELKELAEKLLELVAK 405
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
282-423 3.61e-03

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914  Cd Length: 914  Bit Score: 40.66  E-value: 3.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284  282 WLLAIGIAALgLVLAAIVGYLIARSISRPILSITNVMRELADGRLDVAVPTSKANDEVGAMVKAVAVFRDNAVNFDKlQA 361
Cdd:PRK11466 332 SLLLLGMVSL-CALILILWRVVYRSVTRPLAEQTQALQRLLDGDIDSPFPETAGVRELDTIGRLMDAFRSNVHALNR-HR 409
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27382284  362 EQLEAKAQSEAekrrafaaladnfeASIREVVTTVSAAAVEMEHTARSMSAIVEQSREQTRT 423
Cdd:PRK11466 410 EQLAAQVKART--------------AELQELVIEHRQARAEAEKASQAKSAFLAAMSHEIRT 457
PRK12804 PRK12804
flagellin; Provisional
412-621 9.23e-03

flagellin; Provisional


Pssm-ID: 183759  Cd Length: 301  Bit Score: 38.44  E-value: 9.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284  412 AIVEQSREQTRTVSsasaLASENVQTVAAAAEELSSSMTEISRRLAHATEVVGKAASDGRQSNARVQSLADaaqKIGDVV 491
Cdd:PRK12804  47 AISEKMRGQIRGLE----MASKNAQDGISLIQTAEGALTETHSILQRVRELVVQAGNTGTQDGTDLGAIQD---EIKALV 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284  492 SFINGIAGQTNLLA---LNATIEAARAGEAGRGFAVvasEVKALATQT------AKATEEIGAQVTAVQGETTGAVDGIQ 562
Cdd:PRK12804 120 DEIDGISDRTEFNGkklLDGTFKPAAPAAGTKSLTF---QIGANAAQQlsvnieAMSADALGVKDTDGTLVTGKSVSDID 196
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 27382284  563 sicatIQQVDEISAAIAAAVGQQGTATQEIAQNVQQAAARTGEVSQNISGVTAGIAATG 621
Cdd:PRK12804 197 -----VTKFANAAAAADGGFDDQLKIVDGAIKQVSDQRSKLGAVQNRLEHTINNLGASG 250
PRK07735 PRK07735
NADH dehydrogenase subunit C; Validated
358-594 9.26e-03

NADH dehydrogenase subunit C; Validated


Pssm-ID: 236081  Cd Length: 430  Bit Score: 38.81  E-value: 9.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284  358 KLQAEQLEAKAQSEAEKRRAFAAL----ADNFEASIREVVTTVSAAAVEMEHTARSMSAIV---EQSREQTRTVSSASAL 430
Cdd:PRK07735  25 RLVAKHGAEISKLEEENREKEKALpkndDMTIEEAKRRAAAAAKAKAAALAKQKREGTEEVteeEKAKAKAKAAAAAKAK 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284  431 ASENVQTVAAAAEELSSSMTEISRRLAhATEVVGKAASDGRQSNARVQSLADAAQKIGDVVSFINGIAGQTnllALNATI 510
Cdd:PRK07735 105 AAALAKQKREGTEEVTEEEKAAAKAKA-AAAAKAKAAALAKQKREGTEEVTEEEEETDKEKAKAKAAAAAK---AKAAAL 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284  511 EAARAGEAGRGFAVVASEV----KALATQTAKATEEIGAQVTAVQGETTGAVDGIQSICATIQQVDEISAAIAAAVGQQG 586
Cdd:PRK07735 181 AKQKAAEAGEGTEEVTEEEkakaKAKAAAAAKAKAAALAKQKASQGNGDSGDEDAKAKAIAAAKAKAAAAARAKTKGAEG 260

                 ....*...
gi 27382284  587 TATQEIAQ 594
Cdd:PRK07735 261 KKEEEPKQ 268
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
319-562 9.36e-03

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 225177  Cd Length: 548  Bit Score: 39.05  E-value: 9.36e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284 319 RELADGRLDVAVPTSKANDE----VGAMVKAVAVFRDNAVNFDKLQAEQLEAKAQSEAEKRRAFAALADNFEASIREVVT 394
Cdd:COG2268 300 IQEEKAQAEQEVQHAKALEAremrVGLIERQKETELEPQERSYFINAAQRQAQEEAKAAANIAEAIGAQAEAAVETARET 379
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284 395 TVSAAAVEMEHTARSMSAIVEQSR--EQTRTVSSASALASENVQTVAAAAEELSSSMTEISRRLAHATEVVGKAASdGRQ 472
Cdd:COG2268 380 EEAERAEQAALVAAAEAAEQEQVEiaVRAEAAKAEAEAQAAEIKAEAEAIREKGKAEAEAKRALAEAIQVLGDAAA-AEL 458
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27382284 473 SNARVQSLADAAQKIGDVVSFINGIagqtnllALNATIEAARAGEAGRGFA-VVASEVKALATQTAKATE----EIGAQV 547
Cdd:COG2268 459 FKALVQALPEVAEEAAQPMKNIDSE-------KVRVIGGANGGSTAGKVNAgGLGLLLMALLEALKKTTGvdvaESLLNE 531
                       250
                ....*....|....*
gi 27382284 548 TAVQGETTGAVDGIQ 562
Cdd:COG2268 532 LSGNGNSSAALSELD 546
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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