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Conserved domains on  [gi|27376314|ref|NP_767843|]
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methyl-accepting chemotaxis protein [Bradyrhizobium diazoefficiens USDA 110]

Protein Classification

methyl-accepting chemotaxis protein (domain architecture ID 11105913)

methyl-accepting chemotaxis protein (MCP) is a bacterial receptor that mediates chemotaxis to diverse signals, responding to changes in the concentration of attractants and repellents in the environment by altering swimming behavior

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MCP_signal super family cl23763
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
484-672 1.86e-34

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.


The actual alignment was detected with superfamily member cd11386:

Pssm-ID: 304920  Cd Length: 200  Bit Score: 130.43  E-value: 1.86e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376314 484 NAVASAAEETSVNVQTVSSgTEQLSSSIAEISRQVVTSAGIAKKAVDEA-GATDATVQSLADSASRISVVVDLIQTIASQ 562
Cdd:cd11386   1 EELSASIEEVAASADQVAE-TSQQAAELAEKGREAAEDAINQMNQIDESvDEAVSAVEELEESSAEIGEIVEVIDDIAEQ 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376314 563 TNLLALNATIEAARAGEAGRGFAVVASEVKSLASQTAKATEEIRTQIASMQDVTTSAVGAIQGIGRII-------GEIND 635
Cdd:cd11386  80 TNLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVeegvelvEETGR 159
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 27376314 636 VTTTIAAAVEEQGAATREIARNIQHAAGGTSEVSSNI 672
Cdd:cd11386 160 AFEEIVASVEEVADGIQEISAATQEQSASTQEIAAAV 196
HAMP pfam00672
HAMP domain;
347-418 2.68e-06

HAMP domain;


:

Pssm-ID: 279063  Cd Length: 69  Bit Score: 45.64  E-value: 2.68e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27376314   347 MLALGALMLVGSALFVWLyVGRNILRRITGLQRAMQSLSAGDLDTEIARTKhnDEIGTMTDTLTVFRDSMVE 418
Cdd:pfam00672   1 LLLVLLIALLLALLLAWL-LARRILRPLRRLAEAARRIASGDLDVPLESGR--DEIGELARAFNQMAERLRE 69
 
Name Accession Description Interval E-value
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
484-672 1.86e-34

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: 130.43  E-value: 1.86e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376314 484 NAVASAAEETSVNVQTVSSgTEQLSSSIAEISRQVVTSAGIAKKAVDEA-GATDATVQSLADSASRISVVVDLIQTIASQ 562
Cdd:cd11386   1 EELSASIEEVAASADQVAE-TSQQAAELAEKGREAAEDAINQMNQIDESvDEAVSAVEELEESSAEIGEIVEVIDDIAEQ 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376314 563 TNLLALNATIEAARAGEAGRGFAVVASEVKSLASQTAKATEEIRTQIASMQDVTTSAVGAIQGIGRII-------GEIND 635
Cdd:cd11386  80 TNLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVeegvelvEETGR 159
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 27376314 636 VTTTIAAAVEEQGAATREIARNIQHAAGGTSEVSSNI 672
Cdd:cd11386 160 AFEEIVASVEEVADGIQEISAATQEQSASTQEIAAAV 196
HAMP pfam00672
HAMP domain;
347-418 2.68e-06

HAMP domain;


Pssm-ID: 279063  Cd Length: 69  Bit Score: 45.64  E-value: 2.68e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27376314   347 MLALGALMLVGSALFVWLyVGRNILRRITGLQRAMQSLSAGDLDTEIARTKhnDEIGTMTDTLTVFRDSMVE 418
Cdd:pfam00672   1 LLLVLLIALLLALLLAWL-LARRILRPLRRLAEAARRIASGDLDVPLESGR--DEIGELARAFNQMAERLRE 69
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
368-421 1.72e-03

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


Pssm-ID: 197640  Cd Length: 53  Bit Score: 37.23  E-value: 1.72e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 27376314    368 RNILRRITGLQRAMQSLSAGDLDTEIArTKHNDEIGTMTDTLTVFRDSMVEARA 421
Cdd:smart00304   1 RRLLRPLRRLAEAAQRIADGDLTVRLP-VDGRDEIGELARAFNEMADRLEETIA 53
IpaC_SipC TIGR02101
type III secretion target, IpaC/SipC family; This model represents a family of proteins ...
449-671 4.59e-03

type III secretion target, IpaC/SipC family; This model represents a family of proteins associated with bacterial type III secretion systems, which are injection machines for virulence factors into host cell cytoplasm. Characterized members of this protein family are known to be secreted and are described as invasins, including IpaC from Shigella flexneri (SP:P18012) and SipC from Salmonella typhimurium (GB:AAA75170.1). Members may be referred to as invasins, pathogenicity island effectors, and cell invasion proteins. [Cellular processes, Pathogenesis]


Pssm-ID: 273972  Cd Length: 317  Bit Score: 38.34  E-value: 4.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376314   449 STVRSALDNLAQSANSMQSTAQSMSTTADQSNAlvnavasaaeetsvnVQTVSSGTEQLSSSIAEISRQVVTSAGIAKKA 528
Cdd:TIGR02101  64 IALRVLMSALNQADRKLSSKLSLLSFDATKSAA---------------ASMVREGKAALSSSIIGSATQVAITGVGAKLQ 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376314   529 V----DEAGATD---ATVQSLADSASRISVVVDLIQT-----IASQTNLLALNATIEAARAGEAGRGFAVVASEVKSLAS 596
Cdd:TIGR02101 129 AkglfKQSGALKknlKPSNKLSAEAAQLKLQLNGQNApklvaDSKRTGVAATKELGETTRHEIDPSNKALSAEHKAQLSQ 208
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27376314   597 QTAKATEEIRTQIASMQDVTTSAvGAIQGIGRIIGEINDVTTTIAAAVEEQGAATREIARNIQHAAGGTSEVSSN 671
Cdd:TIGR02101 209 RVESLQDKIDLHQQTYEQNTLKA-QAMQMIGDLIMRMSAVAGNISGASGQYAATQEEAEQQISQSSSRTASTASN 282
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
370-418 4.63e-03

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: 35.69  E-value: 4.63e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 27376314 370 ILRRITGLQRAMQSLSAGDLDTEIaRTKHNDEIGTMTDTLTVFRDSMVE 418
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGDLDVRL-PVTGRDEIGELARAFNQMAERLRE 48
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
457-710 3.10e-38

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 [Multi-domain]  Cd Length: 262  Bit Score: 142.81  E-value: 3.10e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376314    457 NLAQSANSMQSTAQSMSTTADQSNALVNAVASAAEETSVNVQTVSSGTEQLSSSIAEISRQVVTSAGIAKKAVDEAGATD 536
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376314    537 ATVQSLADSASRISVVVDLIQTIASQTNLLALNATIEAARAGEAGRGFAVVASEVKSLASQTAKATEEIRTQIASMQDVT 616
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEET 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376314    617 TSAVGAIQGIGR-------IIGEINDVTTTIAAAVEEQGAATREIARNIQHAAGGTSEVSSNIVGVSTASAEAGAAASEV 689
Cdd:smart00283 161 NEAVAAMEESSSeveegveLVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240
                          250       260
                   ....*....|....*....|.
gi 27376314    690 LGASDALRREADLLRGEIDAF 710
Cdd:smart00283 241 SAAAEELSGLAEELDELVERF 261
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility, Signal transduction mechanisms];
332-710 7.97e-36

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


Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 139.36  E-value: 7.97e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376314 332 STFQARQEISLATSVMLALGALMLVGSALFVWLYVGRNILRRITGLQRAMQSLSAGDLDTEIARTKhNDEIGTMTDTLTV 411
Cdd:COG0840  46 DAASAEAAALKAVLKFLLISLLVAIIVVLVLAILLLRAILEPISDLLEVVERIAAGDLTKRIDESS-NDEFGQLAKSFNE 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376314 412 FRDSMvearalaseqdkdrvakaeraARIEAKIAEFESTVRSALDNLAQSANSMQSTAQSMSTTADQSNALVNAVASAAE 491
Cdd:COG0840 125 MILNL---------------------RQIIDAVQDNAEALSGASEEIAASATELSARADQQAESLEEVASAIEELSETVK 183
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376314 492 ETSVNVQTVSSGTEQLSSSIAEISRQVVTSAGIAKKAVDEagaTDATVQSLADSASRISVVVDLIQTIASQTNLLALNAT 571
Cdd:COG0840 184 EVAFNAKEAAALASEASQVAEEGGEEVRQAVEQMQEIAEE---LAEVVKKLSESSQEIEEITSVINSIAEQTNLLALNAA 260
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376314 572 IEAARAGEAGRGFAVVASEVKSLASQTAKATEEIRTQIASMQDVTTSAVGAIQGIG-------RIIGEINDVTTTIAAAV 644
Cdd:COG0840 261 IEAARAGEAGRGFAVVADEVRKLAERSADSAKEIGLLIEEIQNEAADAVEHMEESAsevsegvKLVEETGSSLGEIAAAI 340
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27376314 645 EEQGAATREIARNIQHAAGGTSEVSSNIVGVSTASAEAGAAASEVLGASDALRREADLLRGEIDAF 710
Cdd:COG0840 341 EEVSQLISEIAAATEEQTAVLEEINASIEELDDVTQENAAAVEELAAASEELKELAEKLLELVAKF 406
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
502-710 2.67e-24

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 [Multi-domain]  Cd Length: 207  Bit Score: 101.76  E-value: 2.67e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376314   502 SGTEQLSSSIAEISRQVVtsagiaKKAVDEAGATdatVQSLADSASRISVVVDLIQTIASQTNLLALNATIEAARAGEAG 581
Cdd:pfam00015   1 SDLAQLASEEALDEMSQI------GQVVDDAVET---MEELETSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQG 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376314   582 RGFAVVASEVKSLASQTAKATEEIRTQIASMQDVTTSAVGAIQGIGR-------IIGEINDVTTTIAAAVEEQGAATREI 654
Cdd:pfam00015  72 RGFAVVADEVRKLAERSAQAAKEIEALIEEIVKQTNDSTASIQQTRTevevgstIVESTGEALKEIVEAVAEIADIVQEI 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 27376314   655 ARNIQHAAGGTSEVSSNIVGVSTASAEAGAAASEVLGASDALRREADLLRGEIDAF 710
Cdd:pfam00015 152 AAASDEQSAGIDQVNQAVARIDQVTQQNAALVEESAAAAETLEEQAEELTASVAQF 207
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
452-668 5.13e-23

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 102.39  E-value: 5.13e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376314  452 RSALDNLAQSANSMQstaQSMSTTADQSNALVNAVASAAEETSVNVQTVSSGTEQLSSSIAEISRQVVTSAGIAKKAVDE 531
Cdd:PRK15048 244 RSEMGDLAQSVSHMQ---RSLTDTVTHVREGSDAIYAGTREIAAGNTDLSSRTEQQASALEETAASMEQLTATVKQNADN 320
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376314  532 A--------GATDA-------------TVQSLADSASRISVVVDLIQTIASQTNLLALNATIEAARAGEAGRGFAVVASE 590
Cdd:PRK15048 321 ArqasqlaqSASDTaqhggkvvdgvvkTMHEIADSSKKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGE 400
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27376314  591 VKSLASQTAKATEEIRTQIA-SMQDVTTSAVgAIQGIGRIIGEINDVTTTIAAAVEEQGAATREIARNIQHAAGGTSEV 668
Cdd:PRK15048 401 VRNLASRSAQAAKEIKALIEdSVSRVDTGSV-LVESAGETMNNIVNAVTRVTDIMGEIASASDEQSRGIDQVALAVSEM 478
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
92-430 4.15e-12

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


Pssm-ID: 274362 [Multi-domain]  Cd Length: 968  Bit Score: 68.27  E-value: 4.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376314    92 AQSEDALNERTKKLRELQEQTQQKLNEIIELGGDKAVVSGLSETMKSINEAAQSLAKAARERLdiaALHDKQYdalRSAQ 171
Cdd:TIGR02956  69 VDDERQRQAIGKKLTLQSETLLHSLKALGELPFNEDLLARLEVLVKDIIDTLAQLGLSVGERI---TLQAQLQ---QLSR 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376314   172 GAFVGAASPAMLdAQTRVN--AILGSANLS-AEDATEAAQ--TVGQLGNVVASGNLAAADMSAALSANTSdKLDDIQKEF 246
Cdd:TIGR02956 143 ELSEAAQEISEL-SQSQVAnaSTIALANVSgIYDLIESGKndQVYQALDDLIEVDLDLAERLNELRLLAL-RVLNTIDDT 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376314   247 KTAQG-----RLRSNL-----------DLLSDNQGNKMLRATAEKLlalgTGKTGVFNLREKELDSIDYGQTILDETRKL 310
Cdd:TIGR02956 221 KTSQDlahinQLDEEFnrlvmilsrrvQSIEDPTRSNQLKDLLVTL----NKTPKLFKLLRQLSQILQKQQRLQQANLEQ 296
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376314   311 NVGLGISVQQLVDGVQKETNASTFQARQEISLATSVMLALGALMLVGSALFVWLYVGRNILRRITGLQRAMQSLSAGDLD 390
Cdd:TIGR02956 297 FTQLNTTVSQLVNAQNQRTEAAVSDLLMTLSVAQFGLLITGMLGLVILVFIMWRVVYRSVILRLNQHTQALLRLALGDLD 376
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 27376314   391 TEIArTKHNDEIGTMTDTLTVFRDSMVEARALASEQDKDR 430
Cdd:TIGR02956 377 ISLD-ARGDDELAHMGRAIEAFRDTAAHNLKLQADERQVA 415
 
Name Accession Description Interval E-value
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
484-672 1.86e-34

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: 130.43  E-value: 1.86e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376314 484 NAVASAAEETSVNVQTVSSgTEQLSSSIAEISRQVVTSAGIAKKAVDEA-GATDATVQSLADSASRISVVVDLIQTIASQ 562
Cdd:cd11386   1 EELSASIEEVAASADQVAE-TSQQAAELAEKGREAAEDAINQMNQIDESvDEAVSAVEELEESSAEIGEIVEVIDDIAEQ 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376314 563 TNLLALNATIEAARAGEAGRGFAVVASEVKSLASQTAKATEEIRTQIASMQDVTTSAVGAIQGIGRII-------GEIND 635
Cdd:cd11386  80 TNLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVeegvelvEETGR 159
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 27376314 636 VTTTIAAAVEEQGAATREIARNIQHAAGGTSEVSSNI 672
Cdd:cd11386 160 AFEEIVASVEEVADGIQEISAATQEQSASTQEIAAAV 196
HAMP pfam00672
HAMP domain;
347-418 2.68e-06

HAMP domain;


Pssm-ID: 279063  Cd Length: 69  Bit Score: 45.64  E-value: 2.68e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27376314   347 MLALGALMLVGSALFVWLyVGRNILRRITGLQRAMQSLSAGDLDTEIARTKhnDEIGTMTDTLTVFRDSMVE 418
Cdd:pfam00672   1 LLLVLLIALLLALLLAWL-LARRILRPLRRLAEAARRIASGDLDVPLESGR--DEIGELARAFNQMAERLRE 69
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
368-421 1.72e-03

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


Pssm-ID: 197640  Cd Length: 53  Bit Score: 37.23  E-value: 1.72e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 27376314    368 RNILRRITGLQRAMQSLSAGDLDTEIArTKHNDEIGTMTDTLTVFRDSMVEARA 421
Cdd:smart00304   1 RRLLRPLRRLAEAAQRIADGDLTVRLP-VDGRDEIGELARAFNEMADRLEETIA 53
IpaC_SipC TIGR02101
type III secretion target, IpaC/SipC family; This model represents a family of proteins ...
449-671 4.59e-03

type III secretion target, IpaC/SipC family; This model represents a family of proteins associated with bacterial type III secretion systems, which are injection machines for virulence factors into host cell cytoplasm. Characterized members of this protein family are known to be secreted and are described as invasins, including IpaC from Shigella flexneri (SP:P18012) and SipC from Salmonella typhimurium (GB:AAA75170.1). Members may be referred to as invasins, pathogenicity island effectors, and cell invasion proteins. [Cellular processes, Pathogenesis]


Pssm-ID: 273972  Cd Length: 317  Bit Score: 38.34  E-value: 4.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376314   449 STVRSALDNLAQSANSMQSTAQSMSTTADQSNAlvnavasaaeetsvnVQTVSSGTEQLSSSIAEISRQVVTSAGIAKKA 528
Cdd:TIGR02101  64 IALRVLMSALNQADRKLSSKLSLLSFDATKSAA---------------ASMVREGKAALSSSIIGSATQVAITGVGAKLQ 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376314   529 V----DEAGATD---ATVQSLADSASRISVVVDLIQT-----IASQTNLLALNATIEAARAGEAGRGFAVVASEVKSLAS 596
Cdd:TIGR02101 129 AkglfKQSGALKknlKPSNKLSAEAAQLKLQLNGQNApklvaDSKRTGVAATKELGETTRHEIDPSNKALSAEHKAQLSQ 208
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27376314   597 QTAKATEEIRTQIASMQDVTTSAvGAIQGIGRIIGEINDVTTTIAAAVEEQGAATREIARNIQHAAGGTSEVSSN 671
Cdd:TIGR02101 209 RVESLQDKIDLHQQTYEQNTLKA-QAMQMIGDLIMRMSAVAGNISGASGQYAATQEEAEQQISQSSSRTASTASN 282
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
370-418 4.63e-03

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: 35.69  E-value: 4.63e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 27376314 370 ILRRITGLQRAMQSLSAGDLDTEIaRTKHNDEIGTMTDTLTVFRDSMVE 418
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGDLDVRL-PVTGRDEIGELARAFNQMAERLRE 48
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
457-710 3.10e-38

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 [Multi-domain]  Cd Length: 262  Bit Score: 142.81  E-value: 3.10e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376314    457 NLAQSANSMQSTAQSMSTTADQSNALVNAVASAAEETSVNVQTVSSGTEQLSSSIAEISRQVVTSAGIAKKAVDEAGATD 536
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376314    537 ATVQSLADSASRISVVVDLIQTIASQTNLLALNATIEAARAGEAGRGFAVVASEVKSLASQTAKATEEIRTQIASMQDVT 616
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEET 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376314    617 TSAVGAIQGIGR-------IIGEINDVTTTIAAAVEEQGAATREIARNIQHAAGGTSEVSSNIVGVSTASAEAGAAASEV 689
Cdd:smart00283 161 NEAVAAMEESSSeveegveLVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240
                          250       260
                   ....*....|....*....|.
gi 27376314    690 LGASDALRREADLLRGEIDAF 710
Cdd:smart00283 241 SAAAEELSGLAEELDELVERF 261
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility, Signal transduction mechanisms];
332-710 7.97e-36

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


Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 139.36  E-value: 7.97e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376314 332 STFQARQEISLATSVMLALGALMLVGSALFVWLYVGRNILRRITGLQRAMQSLSAGDLDTEIARTKhNDEIGTMTDTLTV 411
Cdd:COG0840  46 DAASAEAAALKAVLKFLLISLLVAIIVVLVLAILLLRAILEPISDLLEVVERIAAGDLTKRIDESS-NDEFGQLAKSFNE 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376314 412 FRDSMvearalaseqdkdrvakaeraARIEAKIAEFESTVRSALDNLAQSANSMQSTAQSMSTTADQSNALVNAVASAAE 491
Cdd:COG0840 125 MILNL---------------------RQIIDAVQDNAEALSGASEEIAASATELSARADQQAESLEEVASAIEELSETVK 183
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376314 492 ETSVNVQTVSSGTEQLSSSIAEISRQVVTSAGIAKKAVDEagaTDATVQSLADSASRISVVVDLIQTIASQTNLLALNAT 571
Cdd:COG0840 184 EVAFNAKEAAALASEASQVAEEGGEEVRQAVEQMQEIAEE---LAEVVKKLSESSQEIEEITSVINSIAEQTNLLALNAA 260
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376314 572 IEAARAGEAGRGFAVVASEVKSLASQTAKATEEIRTQIASMQDVTTSAVGAIQGIG-------RIIGEINDVTTTIAAAV 644
Cdd:COG0840 261 IEAARAGEAGRGFAVVADEVRKLAERSADSAKEIGLLIEEIQNEAADAVEHMEESAsevsegvKLVEETGSSLGEIAAAI 340
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27376314 645 EEQGAATREIARNIQHAAGGTSEVSSNIVGVSTASAEAGAAASEVLGASDALRREADLLRGEIDAF 710
Cdd:COG0840 341 EEVSQLISEIAAATEEQTAVLEEINASIEELDDVTQENAAAVEELAAASEELKELAEKLLELVAKF 406
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
502-710 2.67e-24

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 [Multi-domain]  Cd Length: 207  Bit Score: 101.76  E-value: 2.67e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376314   502 SGTEQLSSSIAEISRQVVtsagiaKKAVDEAGATdatVQSLADSASRISVVVDLIQTIASQTNLLALNATIEAARAGEAG 581
Cdd:pfam00015   1 SDLAQLASEEALDEMSQI------GQVVDDAVET---MEELETSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQG 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376314   582 RGFAVVASEVKSLASQTAKATEEIRTQIASMQDVTTSAVGAIQGIGR-------IIGEINDVTTTIAAAVEEQGAATREI 654
Cdd:pfam00015  72 RGFAVVADEVRKLAERSAQAAKEIEALIEEIVKQTNDSTASIQQTRTevevgstIVESTGEALKEIVEAVAEIADIVQEI 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 27376314   655 ARNIQHAAGGTSEVSSNIVGVSTASAEAGAAASEVLGASDALRREADLLRGEIDAF 710
Cdd:pfam00015 152 AAASDEQSAGIDQVNQAVARIDQVTQQNAALVEESAAAAETLEEQAEELTASVAQF 207
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
452-668 5.13e-23

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 102.39  E-value: 5.13e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376314  452 RSALDNLAQSANSMQstaQSMSTTADQSNALVNAVASAAEETSVNVQTVSSGTEQLSSSIAEISRQVVTSAGIAKKAVDE 531
Cdd:PRK15048 244 RSEMGDLAQSVSHMQ---RSLTDTVTHVREGSDAIYAGTREIAAGNTDLSSRTEQQASALEETAASMEQLTATVKQNADN 320
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376314  532 A--------GATDA-------------TVQSLADSASRISVVVDLIQTIASQTNLLALNATIEAARAGEAGRGFAVVASE 590
Cdd:PRK15048 321 ArqasqlaqSASDTaqhggkvvdgvvkTMHEIADSSKKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGE 400
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27376314  591 VKSLASQTAKATEEIRTQIA-SMQDVTTSAVgAIQGIGRIIGEINDVTTTIAAAVEEQGAATREIARNIQHAAGGTSEV 668
Cdd:PRK15048 401 VRNLASRSAQAAKEIKALIEdSVSRVDTGSV-LVESAGETMNNIVNAVTRVTDIMGEIASASDEQSRGIDQVALAVSEM 478
PRK09793 PRK09793
methyl-accepting protein IV; Provisional
443-658 1.07e-22

methyl-accepting protein IV; Provisional


Pssm-ID: 182079 [Multi-domain]  Cd Length: 533  Bit Score: 101.30  E-value: 1.07e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376314  443 KIAEFESTVRSALDNLAQSANSMQSTAQSMSTTADQSNALVNAVASAAEETSVNVQTVSSGTEQLSSSI---AEISRQVV 519
Cdd:PRK09793 244 EITAIFASLKTMQQALRGTVSDVRKGSQEMHIGIAEIVAGNNDLSSRTEQQAASLAQTAASMEQLTATVgqnADNARQAS 323
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376314  520 ----TSAGIAKKAVDEAGATDATVQSLADSASRISVVVDLIQTIASQTNLLALNATIEAARAGEAGRGFAVVASEVKSLA 595
Cdd:PRK09793 324 elakNAATTAQAGGVQVSTMTHTMQEIATSSQKIGDIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLA 403
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376314  596 SQTAKATEEIR-------TQIASMQDVTTSAVGAIQGIGRIIGEINDVTTTIAAAVEEQGAATREIARNI 658
Cdd:PRK09793 404 SRSAQAAKEIKglieesvNRVQQGSKLVNNAAATMTDIVSSVTRVNDIMGEIASASEEQRRGIEQVAQAV 473
PRK15041 PRK15041
methyl-accepting chemotaxis protein I; Provisional
458-668 6.87e-22

methyl-accepting chemotaxis protein I; Provisional


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 98.87  E-value: 6.87e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376314  458 LAQSANSMQStaQSMSTTADQSNAlVNAVASAAEETSVNVQTVSSGTEQLSSSI-----------------AEISRQVVT 520
Cdd:PRK15041 252 LAESLRHMQG--ELMRTVGDVRNG-ANAIYSGASEIATGNNDLSSRTEQQAASLeetaasmeqltatvkqnAENARQASH 328
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376314  521 SAGIAKKAVDEAG-ATDATVQSLAD---SASRISVVVDLIQTIASQTNLLALNATIEAARAGEAGRGFAVVASEVKSLAS 596
Cdd:PRK15041 329 LALSASETAQRGGkVVDNVVQTMRDistSSQKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQ 408
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27376314  597 QTAKATEEIRTQIASMQDVTTSAVGAIQGIGRIIGEINDVTTTIAAAVEEQGAATREIARNIQHAAGGTSEV 668
Cdd:PRK15041 409 RSAQAAREIKSLIEDSVGKVDVGSTLVESAGETMAEIVSAVTRVTDIMGEIASASDEQSRGIDQVGLAVAEM 480
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
92-430 4.15e-12

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


Pssm-ID: 274362 [Multi-domain]  Cd Length: 968  Bit Score: 68.27  E-value: 4.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376314    92 AQSEDALNERTKKLRELQEQTQQKLNEIIELGGDKAVVSGLSETMKSINEAAQSLAKAARERLdiaALHDKQYdalRSAQ 171
Cdd:TIGR02956  69 VDDERQRQAIGKKLTLQSETLLHSLKALGELPFNEDLLARLEVLVKDIIDTLAQLGLSVGERI---TLQAQLQ---QLSR 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376314   172 GAFVGAASPAMLdAQTRVN--AILGSANLS-AEDATEAAQ--TVGQLGNVVASGNLAAADMSAALSANTSdKLDDIQKEF 246
Cdd:TIGR02956 143 ELSEAAQEISEL-SQSQVAnaSTIALANVSgIYDLIESGKndQVYQALDDLIEVDLDLAERLNELRLLAL-RVLNTIDDT 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376314   247 KTAQG-----RLRSNL-----------DLLSDNQGNKMLRATAEKLlalgTGKTGVFNLREKELDSIDYGQTILDETRKL 310
Cdd:TIGR02956 221 KTSQDlahinQLDEEFnrlvmilsrrvQSIEDPTRSNQLKDLLVTL----NKTPKLFKLLRQLSQILQKQQRLQQANLEQ 296
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376314   311 NVGLGISVQQLVDGVQKETNASTFQARQEISLATSVMLALGALMLVGSALFVWLYVGRNILRRITGLQRAMQSLSAGDLD 390
Cdd:TIGR02956 297 FTQLNTTVSQLVNAQNQRTEAAVSDLLMTLSVAQFGLLITGMLGLVILVFIMWRVVYRSVILRLNQHTQALLRLALGDLD 376
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 27376314   391 TEIArTKHNDEIGTMTDTLTVFRDSMVEARALASEQDKDR 430
Cdd:TIGR02956 377 ISLD-ARGDDELAHMGRAIEAFRDTAAHNLKLQADERQVA 415
valS PRK14900
valyl-tRNA synthetase; Provisional
386-543 5.84e-04

valyl-tRNA synthetase; Provisional


Pssm-ID: 237855 [Multi-domain]  Cd Length: 1052  Bit Score: 41.90  E-value: 5.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376314   386 AGDLDTEIARTKHNDEIGTMTDTLTVFRDSMVEARALAS------EQDKDRVAK-AERAARIEAKIA-----EFESTVRS 453
Cdd:PRK14900  835 AGVIDLAAETARVDKEIGKVDQDLAVLERKLQNPSFVQNappavvEKDRARAEElREKRGKLEAHRAmlsgsEANSARRD 914
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376314   454 ALDNL-----AQSANSMQSTAQSMSTTADQSNALVNAVASAAEETSVNVQtvsSGTEQLSSSIAEISRQVV-----TSAG 523
Cdd:PRK14900  915 TMEIQneqkpTQDGPAAEAQPAQENTVVESAEKAVAAVSEAAQQAATAVA---SGIEKVAEAVRKTVRRSVkkaaaTRAA 991
                         170       180
                  ....*....|....*....|
gi 27376314   524 IAKKAVDEAGATDATVQSLA 543
Cdd:PRK14900  992 MKKKVAKKAPAKKAAAKKAA 1011
NtrY COG5000
Signal transduction histidine kinase involved in nitrogen fixation and metabolism regulation ...
337-439 1.34e-03

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


Pssm-ID: 227333 [Multi-domain]  Cd Length: 712  Bit Score: 40.52  E-value: 1.34e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376314 337 RQEISLATSVMLALGALMLVGSALFVWLYVGRNILRRITGLQRAMQSLSAGDLDTEIARTKHNDEIGTMTDTLTVfrdsM 416
Cdd:COG5000 272 RDGLQIAFALLYLSTALLVLLAAIWTAIAFARRIVRPIRKLIEAADEVADGDLDVQVPVRRVDEDVGRLSKAFNK----M 347
                        90       100
                ....*....|....*....|...
gi 27376314 417 VEarALASEQDKDRVAKAERAAR 439
Cdd:COG5000 348 TE--QLSSQQEALERAKDALEQR 368
YkyA pfam10368
Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein ...
91-174 2.77e-03

Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein signal and a hydrolase domain. It is similar to cell wall binding proteins and might also be recognizable by a host immune defence system. It is thus likely to belong to pathways important for pathogenicity.


Pssm-ID: 287354 [Multi-domain]  Cd Length: 202  Bit Score: 38.40  E-value: 2.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376314    91 AAQSEDALNERTKKLRELQEQTQQKLNEIIELGGDKavvsglsetMKSINEAAQSLAKAARERLDiaaLHDKQYDALRSA 170
Cdd:pfam10368  26 AVKQEKPFVEQQKKLQELEEKEQELYEQIIELGKED---------FDEIKKLADEAIENAEEREK---LLEKEKESIEKS 93

                  ....
gi 27376314   171 QGAF 174
Cdd:pfam10368  94 KEEF 97
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
238-446 3.94e-03

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 39.12  E-value: 3.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376314  238 KLDDIQKEFKTAQGRLRSNLDLLSDNQ---GNKMLRATAEKLLALGTGKTGVFNLREKELDSIDYGQTILDETRKLNVGL 314
Cdd:PRK11466 221 GLEQIQKNAPTLEKQLNNAVKILQRRQiriEDPGVRAQVATTLTTVSQYSDLLALYQQDSEISNHLQTLAQNNIAQFAQF 300
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376314  315 GISVQQLVDGVQKETNASTFQARQEISLATSVMLALGALMLVGSALFVWLYVGRNILRRITGLQRAMQSLSAGDLDTEIA 394
Cdd:PRK11466 301 SSEVSQLVDTIELRNQHGLAHLEKASARGQYSLLLLGMVSLCALILILWRVVYRSVTRPLAEQTQALQRLLDGDIDSPFP 380
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27376314  395 RTKHNDEIGTMTDTLTVFRDS---MVEARALASEQDKDRVAKAE------RAARIEAKIAE 446
Cdd:PRK11466 381 ETAGVRELDTIGRLMDAFRSNvhaLNRHREQLAAQVKARTAELQelviehRQARAEAEKAS 441
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
418-554 5.23e-03

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 [Multi-domain]  Cd Length: 262  Bit Score: 38.04  E-value: 5.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376314    418 EARALASEQdkdrvakAERAARIEAKIAEFESTVRSALDNLAQSansmQSTAQSMSTTADQSNALVNAVASAAEETSVNV 497
Cdd:smart00283 134 EVRKLAERS-------AESAKEIESLIKEIQEETNEAVAAMEES----SSEVEEGVELVEETGDALEEIVDSVEEIADLV 202
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 27376314    498 QTVSSGTEQLSSSIAEISRQVVTSAGIAKKAVDEAGATDATVQSLADSASRISVVVD 554
Cdd:smart00283 203 QEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEISAAAEELSGLAEELDELVE 259
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.15
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.
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