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Conserved domains on  [gi|27376040|ref|NP_767569|]
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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
MCPsignal super family cl28165
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
310-539 6.96e-40

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.


The actual alignment was detected with superfamily member smart00283:

Pssm-ID: 332985  Cd Length: 262  Bit Score: 147.05  E-value: 6.96e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040    310 VERAVSSLSEIARSLSSESQAVAAASTQALGSSQTVSAAAEELSVSIREIAGQVARTSTVTRSAVAGREQAR-------S 382
Cdd:smart00283   2 VSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIRevveeavS 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040    383 TIQALAGSVKKIAEVSDLIGGIAGQTNLLALNATIEAARAGEAGRGFAVVAAEVKSLSDQTAKSTEEIGRLIAEIQASTQ 462
Cdd:smart00283  82 AVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEETN 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040    463 AAV---------------------DAVETMGGHIVEIDGVASSVAAAMEQQDAATREIARSISESASAAKEVSAKIGNVS 521
Cdd:smart00283 162 EAVaameessseveegvelveetgDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEIS 241
                          250
                   ....*....|....*...
gi 27376040    522 RDAASVNERAAEVRQAIA 539
Cdd:smart00283 242 AAAEELSGLAEELDELVE 259
PRK15347 super family cl28304
two component system sensor kinase SsrA; Provisional
163-357 9.77e-09

two component system sensor kinase SsrA; Provisional


The actual alignment was detected with superfamily member TIGR02956:

Pssm-ID: 333124  Cd Length: 968  Bit Score: 58.25  E-value: 9.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040   163 IDSIVESANKQNAdmeklAAERDSTMLyillgVSAAVLAFVAAGLLGVAL-----------GVVRPIVRMTDTMQRLATG 231
Cdd:TIGR02956 304 VSQLVNAQNQRTE-----AAVSDLLMT-----LSVAQFGLLITGMLGLVIlvfimwrvvyrSVILRLNQHTQALLRLALG 373
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040   232 DLaaDIPF-AHRQDEVGSMAGALVVFKQAAAENSRLREEQLQKEQEAALAKRgalhQMAETVERETgrsvdtasaasqgv 310
Cdd:TIGR02956 374 DL--DISLdARGDDELAHMGRAIEAFRDTAAHNLKLQADERQVAQELQEHKE----SLEQLVAQRT-------------- 433
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 27376040   311 eravSSLSEIARSLSSESQAVAAASTQALGSSQTVSAAAEELSVSIR 357
Cdd:TIGR02956 434 ----QELAETNERLNAEVKNHAKARAEAEEANRAKSAFLATMSHEIR 476
 
Name Accession Description Interval E-value
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
310-539 6.96e-40

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: 147.05  E-value: 6.96e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040    310 VERAVSSLSEIARSLSSESQAVAAASTQALGSSQTVSAAAEELSVSIREIAGQVARTSTVTRSAVAGREQAR-------S 382
Cdd:smart00283   2 VSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIRevveeavS 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040    383 TIQALAGSVKKIAEVSDLIGGIAGQTNLLALNATIEAARAGEAGRGFAVVAAEVKSLSDQTAKSTEEIGRLIAEIQASTQ 462
Cdd:smart00283  82 AVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEETN 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040    463 AAV---------------------DAVETMGGHIVEIDGVASSVAAAMEQQDAATREIARSISESASAAKEVSAKIGNVS 521
Cdd:smart00283 162 EAVaameessseveegvelveetgDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEIS 241
                          250
                   ....*....|....*...
gi 27376040    522 RDAASVNERAAEVRQAIA 539
Cdd:smart00283 242 AAAEELSGLAEELDELVE 259
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
322-522 1.88e-35

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: 132.75  E-value: 1.88e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040 322 RSLSSESQAVAAASTQALGSSQTVSAAAEELSVSIREIAGQVARTSTVTrsavagrEQARSTIQALAGSVKKIAEVSDLI 401
Cdd:cd11386   1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESV-------DEAVSAVEELEESSAEIGEIVEVI 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040 402 GGIAGQTNLLALNATIEAARAGEAGRGFAVVAAEVKSLSDQTAKSTEEIGRLIAEIQASTQAAVDAVETMGGHIVEIDGV 481
Cdd:cd11386  74 DDIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVEL 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 27376040 482 ASSVAAAMEQQDAATREIARSISESASAAKEVSAKIGNVSR 522
Cdd:cd11386 154 VEETGRAFEEIVASVEEVADGIQEISAATQEQSASTQEIAA 194
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility, Signal transduction mechanisms];
144-548 8.89e-34

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


Pssm-ID: 223910  Cd Length: 408  Bit Score: 132.81  E-value: 8.89e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040 144 AAEGAYAQLKDAYTAHRAVIDSIVESANKQNADMEKLAAERDSTMLYILLGVSAAVLAFVAAGLLGVALGVVRPIVRMTD 223
Cdd:COG0840  14 LAAGEADAGLLKLKKLIDELGKLLLSLNLILDDAASAEAAALKAVLKFLLISLLVAIIVVLVLAILLLRAILEPISDLLE 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040 224 TMQRLATGDLAADIPFaHRQDEVGSMAgalvvfkqaaaensrlreEQLQKEQEAALAKRGALHQMAETVERETGRSVDTA 303
Cdd:COG0840  94 VVERIAAGDLTKRIDE-SSNDEFGQLA------------------KSFNEMILNLRQIIDAVQDNAEALSGASEEIAASA 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040 304 SAASQGVERAVSSLSEIARS---LSSESQAVAAASTQALGSSQTVSAAAEELSVSIREIAGQVARTStvtrsavagrEQA 380
Cdd:COG0840 155 TELSARADQQAESLEEVASAieeLSETVKEVAFNAKEAAALASEASQVAEEGGEEVRQAVEQMQEIA----------EEL 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040 381 RSTIQALAGSVKKIAEVSDLIGGIAGQTNLLALNATIEAARAGEAGRGFAVVAAEVKSLSDQTAKSTEEIGRLIAEIQAS 460
Cdd:COG0840 225 AEVVKKLSESSQEIEEITSVINSIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSADSAKEIGLLIEEIQNE 304
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040 461 TQAAVDAVETMGGHIVEIDGVASSVAAAMEQQDAATREIARSISESASAAKEVSAKIGNVSRDAASVNERAAEVRQAIAG 540
Cdd:COG0840 305 AADAVEHMEESASEVSEGVKLVEETGSSLGEIAAAIEEVSQLISEIAAATEEQTAVLEEINASIEELDDVTQENAAAVEE 384

                ....*...
gi 27376040 541 MASNLEQL 548
Cdd:COG0840 385 LAAASEEL 392
PRK15041 PRK15041
methyl-accepting chemotaxis protein I; Provisional
186-563 8.52e-29

methyl-accepting chemotaxis protein I; Provisional


Pssm-ID: 185001  Cd Length: 554  Bit Score: 120.44  E-value: 8.52e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040  186 STMLYILLGVSAAVLAFVAAGLLGVALGVVRPIVRMTDTMQRLATGDLAADIPfAHRQDEVGsmagalvvfkqaaaensr 265
Cdd:PRK15041 190 SQAMWILVGVMIVVLAVIFAVWFGIKASLVAPMNRLIDSIRHIAGGDLVKPIE-VDGSNEMG------------------ 250
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040  266 lreeqlqkeqeaalakrgalhQMAETVERETGRSVDTASAASQGVERAVSSLSEIA---RSLSSESQAVAAastqalgSS 342
Cdd:PRK15041 251 ---------------------QLAESLRHMQGELMRTVGDVRNGANAIYSGASEIAtgnNDLSSRTEQQAA-------SL 302
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040  343 QTVSAAAEELSVSIREIAGQVARTSTVTRSAVAGREQAR-------STIQALAGSVKKIAEVSDLIGGIAGQTNLLALNA 415
Cdd:PRK15041 303 EETAASMEQLTATVKQNAENARQASHLALSASETAQRGGkvvdnvvQTMRDISTSSQKIADIISVIDGIAFQTNILALNA 382
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040  416 TIEAARAGEAGRGFAVVAAEVKSLSDQTAKSTEEIGRLIAEIQASTQAAVDAVETMGGHIVEIDGVASSVAAAMEQQDAA 495
Cdd:PRK15041 383 AVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLVESAGETMAEIVSAVTRVTDIMGEIASA 462
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27376040  496 TREIARSISESASAAKEV-------SAKIGNVSRDAASVNERAAEVRQAIAGMASNLEQLRSVVVRTVRDSTAAA 563
Cdd:PRK15041 463 SDEQSRGIDQVGLAVAEMdrvtqqnAALVEESAAAAAALEEQASRLTEAVAVFRIQQQQQQQRETSAVVKTVTPA 537
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
378-540 9.22e-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  Cd Length: 207  Bit Score: 100.21  E-value: 9.22e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040   378 EQARSTIQALAGSVKKIAEVSDLIGGIAGQTNLLALNATIEAARAGEAGRGFAVVAAEVKSLSDQTAKSTEEIGRLIAEI 457
Cdd:pfam00015  23 DDAVETMEELETSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLAERSAQAAKEIEALIEEI 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040   458 QASTQAAV---------------------DAVETMGGHIVEIDGVASSVAAAMEQQDAATREIARSISESASAAKEVSAK 516
Cdd:pfam00015 103 VKQTNDSTasiqqtrtevevgstivestgEALKEIVEAVAEIADIVQEIAAASDEQSAGIDQVNQAVARIDQVTQQNAAL 182
                         170       180
                  ....*....|....*....|....
gi 27376040   517 IGNVSRDAASVNERAAEVRQAIAG 540
Cdd:pfam00015 183 VEESAAAAETLEEQAEELTASVAQ 206
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
163-357 9.77e-09

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: 58.25  E-value: 9.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040   163 IDSIVESANKQNAdmeklAAERDSTMLyillgVSAAVLAFVAAGLLGVAL-----------GVVRPIVRMTDTMQRLATG 231
Cdd:TIGR02956 304 VSQLVNAQNQRTE-----AAVSDLLMT-----LSVAQFGLLITGMLGLVIlvfimwrvvyrSVILRLNQHTQALLRLALG 373
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040   232 DLaaDIPF-AHRQDEVGSMAGALVVFKQAAAENSRLREEQLQKEQEAALAKRgalhQMAETVERETgrsvdtasaasqgv 310
Cdd:TIGR02956 374 DL--DISLdARGDDELAHMGRAIEAFRDTAAHNLKLQADERQVAQELQEHKE----SLEQLVAQRT-------------- 433
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 27376040   311 eravSSLSEIARSLSSESQAVAAASTQALGSSQTVSAAAEELSVSIR 357
Cdd:TIGR02956 434 ----QELAETNERLNAEVKNHAKARAEAEEANRAKSAFLATMSHEIR 476
NtrY COG5000
Signal transduction histidine kinase involved in nitrogen fixation and metabolism regulation ...
160-282 7.04e-06

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


Pssm-ID: 227333  Cd Length: 712  Bit Score: 48.61  E-value: 7.04e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040 160 RAVIDSIVESA---NKQNADMEKLAAERDS-TMLYILLGVSAAVLAFVAAGLLGVALG--VVRPIVRMTDTMQRLATGDL 233
Cdd:COG5000 245 RPVDPKVAEHAdltEGAAAEYRELEAGRDGlQIAFALLYLSTALLVLLAAIWTAIAFArrIVRPIRKLIEAADEVADGDL 324
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 27376040 234 AADIPFAHRQDEVGSMAGAlvvFKQAAAENSRLREEQLQKEQEAALAKR 282
Cdd:COG5000 325 DVQVPVRRVDEDVGRLSKA---FNKMTEQLSSQQEALERAKDALEQRRR 370
HAMP pfam00672
HAMP domain;
192-253 8.88e-06

HAMP domain;


Pssm-ID: 307012  Cd Length: 69  Bit Score: 44.87  E-value: 8.88e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27376040   192 LLGVSAAVLAFVAAGLLGVALGVVRPIVRMTDTMQRLATGDLaaDIPFAHRQDEVGSMAGAL 253
Cdd:pfam00672   1 LLLVLLIALLLALLLAWLLARRILRPLRRLAEAARRIASGDL--DVPLESGRDEIGELARAF 60
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
267-549 4.20e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008  Cd Length: 1179  Bit Score: 43.12  E-value: 4.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040    267 REEQLQKEQEAALAKRGALHQMAETVEREtgrsvdtasaaSQGVERAVSSLSEIARSLSSESQAVAAASTQAlgssqtvS 346
Cdd:TIGR02168  692 KIAELEKALAELRKELEELEEELEQLRKE-----------LEELSRQISALRKDLARLEAEVEQLEERIAQL-------S 753
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040    347 AAAEELSVSIREIAGQVARTSTVTRSAVAGREQARSTIQALAGSVKKIAEVSDLIGGIAGQTNLLALNATIEAA----RA 422
Cdd:TIGR02168  754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLEslerRI 833
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040    423 GEAGRGFAVVAAEVKSLSDQTAKSTEEIGRL---IAEIQASTQAAVDAVETMGGHIVEIDGVASSVAAAMEQQDAATREI 499
Cdd:TIGR02168  834 AATERRLEDLEEQIEELSEDIESLAAEIEELeelIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL 913
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 27376040    500 ARSISESASAAKEVSAKIGNVSRDAASVNERAAEVRQAIAGMASNLEQLR 549
Cdd:TIGR02168  914 RRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKI 963
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
214-253 5.05e-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: 39.54  E-value: 5.05e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 27376040 214 VVRPIVRMTDTMQRLATGDLAADIPFaHRQDEVGSMAGAL 253
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGDLDVRLPV-TGRDEIGELARAF 39
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
214-253 3.05e-03

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


Pssm-ID: 197640  Cd Length: 53  Bit Score: 37.23  E-value: 3.05e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 27376040    214 VVRPIVRMTDTMQRLATGDLAADIPfAHRQDEVGSMAGAL 253
Cdd:smart00304   3 LLRPLRRLAEAAQRIADGDLTVRLP-VDGRDEIGELARAF 41
 
Name Accession Description Interval E-value
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
310-539 6.96e-40

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: 147.05  E-value: 6.96e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040    310 VERAVSSLSEIARSLSSESQAVAAASTQALGSSQTVSAAAEELSVSIREIAGQVARTSTVTRSAVAGREQAR-------S 382
Cdd:smart00283   2 VSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIRevveeavS 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040    383 TIQALAGSVKKIAEVSDLIGGIAGQTNLLALNATIEAARAGEAGRGFAVVAAEVKSLSDQTAKSTEEIGRLIAEIQASTQ 462
Cdd:smart00283  82 AVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEETN 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040    463 AAV---------------------DAVETMGGHIVEIDGVASSVAAAMEQQDAATREIARSISESASAAKEVSAKIGNVS 521
Cdd:smart00283 162 EAVaameessseveegvelveetgDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEIS 241
                          250
                   ....*....|....*...
gi 27376040    522 RDAASVNERAAEVRQAIA 539
Cdd:smart00283 242 AAAEELSGLAEELDELVE 259
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
322-522 1.88e-35

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: 132.75  E-value: 1.88e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040 322 RSLSSESQAVAAASTQALGSSQTVSAAAEELSVSIREIAGQVARTSTVTrsavagrEQARSTIQALAGSVKKIAEVSDLI 401
Cdd:cd11386   1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESV-------DEAVSAVEELEESSAEIGEIVEVI 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040 402 GGIAGQTNLLALNATIEAARAGEAGRGFAVVAAEVKSLSDQTAKSTEEIGRLIAEIQASTQAAVDAVETMGGHIVEIDGV 481
Cdd:cd11386  74 DDIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVEL 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 27376040 482 ASSVAAAMEQQDAATREIARSISESASAAKEVSAKIGNVSR 522
Cdd:cd11386 154 VEETGRAFEEIVASVEEVADGIQEISAATQEQSASTQEIAA 194
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility, Signal transduction mechanisms];
144-548 8.89e-34

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


Pssm-ID: 223910  Cd Length: 408  Bit Score: 132.81  E-value: 8.89e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040 144 AAEGAYAQLKDAYTAHRAVIDSIVESANKQNADMEKLAAERDSTMLYILLGVSAAVLAFVAAGLLGVALGVVRPIVRMTD 223
Cdd:COG0840  14 LAAGEADAGLLKLKKLIDELGKLLLSLNLILDDAASAEAAALKAVLKFLLISLLVAIIVVLVLAILLLRAILEPISDLLE 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040 224 TMQRLATGDLAADIPFaHRQDEVGSMAgalvvfkqaaaensrlreEQLQKEQEAALAKRGALHQMAETVERETGRSVDTA 303
Cdd:COG0840  94 VVERIAAGDLTKRIDE-SSNDEFGQLA------------------KSFNEMILNLRQIIDAVQDNAEALSGASEEIAASA 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040 304 SAASQGVERAVSSLSEIARS---LSSESQAVAAASTQALGSSQTVSAAAEELSVSIREIAGQVARTStvtrsavagrEQA 380
Cdd:COG0840 155 TELSARADQQAESLEEVASAieeLSETVKEVAFNAKEAAALASEASQVAEEGGEEVRQAVEQMQEIA----------EEL 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040 381 RSTIQALAGSVKKIAEVSDLIGGIAGQTNLLALNATIEAARAGEAGRGFAVVAAEVKSLSDQTAKSTEEIGRLIAEIQAS 460
Cdd:COG0840 225 AEVVKKLSESSQEIEEITSVINSIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSADSAKEIGLLIEEIQNE 304
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040 461 TQAAVDAVETMGGHIVEIDGVASSVAAAMEQQDAATREIARSISESASAAKEVSAKIGNVSRDAASVNERAAEVRQAIAG 540
Cdd:COG0840 305 AADAVEHMEESASEVSEGVKLVEETGSSLGEIAAAIEEVSQLISEIAAATEEQTAVLEEINASIEELDDVTQENAAAVEE 384

                ....*...
gi 27376040 541 MASNLEQL 548
Cdd:COG0840 385 LAAASEEL 392
PRK15041 PRK15041
methyl-accepting chemotaxis protein I; Provisional
186-563 8.52e-29

methyl-accepting chemotaxis protein I; Provisional


Pssm-ID: 185001  Cd Length: 554  Bit Score: 120.44  E-value: 8.52e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040  186 STMLYILLGVSAAVLAFVAAGLLGVALGVVRPIVRMTDTMQRLATGDLAADIPfAHRQDEVGsmagalvvfkqaaaensr 265
Cdd:PRK15041 190 SQAMWILVGVMIVVLAVIFAVWFGIKASLVAPMNRLIDSIRHIAGGDLVKPIE-VDGSNEMG------------------ 250
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040  266 lreeqlqkeqeaalakrgalhQMAETVERETGRSVDTASAASQGVERAVSSLSEIA---RSLSSESQAVAAastqalgSS 342
Cdd:PRK15041 251 ---------------------QLAESLRHMQGELMRTVGDVRNGANAIYSGASEIAtgnNDLSSRTEQQAA-------SL 302
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040  343 QTVSAAAEELSVSIREIAGQVARTSTVTRSAVAGREQAR-------STIQALAGSVKKIAEVSDLIGGIAGQTNLLALNA 415
Cdd:PRK15041 303 EETAASMEQLTATVKQNAENARQASHLALSASETAQRGGkvvdnvvQTMRDISTSSQKIADIISVIDGIAFQTNILALNA 382
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040  416 TIEAARAGEAGRGFAVVAAEVKSLSDQTAKSTEEIGRLIAEIQASTQAAVDAVETMGGHIVEIDGVASSVAAAMEQQDAA 495
Cdd:PRK15041 383 AVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLVESAGETMAEIVSAVTRVTDIMGEIASA 462
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27376040  496 TREIARSISESASAAKEV-------SAKIGNVSRDAASVNERAAEVRQAIAGMASNLEQLRSVVVRTVRDSTAAA 563
Cdd:PRK15041 463 SDEQSRGIDQVGLAVAEMdrvtqqnAALVEESAAAAAALEEQASRLTEAVAVFRIQQQQQQQRETSAVVKTVTPA 537
PRK09793 PRK09793
methyl-accepting protein IV; Provisional
118-551 1.74e-25

methyl-accepting protein IV; Provisional


Pssm-ID: 182079  Cd Length: 533  Bit Score: 110.16  E-value: 1.74e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040  118 SDAEVQKFWkVLSDQLLPALkaknSAAAEGAYAQLKDAYTAHRAVIDSIVESANKQNADMEKLAAerdstMLYILLGVSA 197
Cdd:PRK09793 130 NDLEHQATW-LESNQLSDFL----TAPVQGSQNAFDVNFEAWQLEINHVLEAASAQSQRNYQISA-----LVFISMIIVA 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040  198 AVLafVAAGLLGVALGVVRPIVRMTDTMQRLATGDLAADIPfAHRQDEVGSMAGALVVFKQAaaensrLREeqlqkeqea 277
Cdd:PRK09793 200 AIY--ISSALWWTRKMIVQPLAIIGSHFDSIAAGNLARPIA-VYGRNEITAIFASLKTMQQA------LRG--------- 261
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040  278 alakrgalhqmaetveretgrsvdTASAASQGVERAVSSLSEIA---RSLSSESQAVAAASTQALGSSQTVSAAAEELSV 354
Cdd:PRK09793 262 ------------------------TVSDVRKGSQEMHIGIAEIVagnNDLSSRTEQQAASLAQTAASMEQLTATVGQNAD 317
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040  355 SIREIAGQVARTSTVTRSAVAGREQARSTIQALAGSVKKIAEVSDLIGGIAGQTNLLALNATIEAARAGEAGRGFAVVAA 434
Cdd:PRK09793 318 NARQASELAKNAATTAQAGGVQVSTMTHTMQEIATSSQKIGDIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAG 397
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040  435 EVKSLSDQTAKSTEEIGRLIAEIQASTQAAVDAVETMGGHIVEIDGVASSVAAAMEQQDAATREIARSISESASAAkevs 514
Cdd:PRK09793 398 EVRNLASRSAQAAKEIKGLIEESVNRVQQGSKLVNNAAATMTDIVSSVTRVNDIMGEIASASEEQRRGIEQVAQAV---- 473
                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 27376040  515 AKIGNVSRDAASVNERAAEVRQAIAGMASNLEQLRSV 551
Cdd:PRK09793 474 SQMDQVTQQNASLVEEAAVATEQLANQADHLSSRVAV 510
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
279-547 7.63e-25

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008  Cd Length: 553  Bit Score: 108.56  E-value: 7.63e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040  279 LAKRGALHQMAETVERETGRSVDTASAASQGVERAVSSLSEIA---RSLSSESQAVAAASTQALGSSQTVSAAAEELSVS 355
Cdd:PRK15048 241 IDGRSEMGDLAQSVSHMQRSLTDTVTHVREGSDAIYAGTREIAagnTDLSSRTEQQASALEETAASMEQLTATVKQNADN 320
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040  356 IREIAGQVARTSTVTRSAVAGREQARSTIQALAGSVKKIAEVSDLIGGIAGQTNLLALNATIEAARAGEAGRGFAVVAAE 435
Cdd:PRK15048 321 ARQASQLAQSASDTAQHGGKVVDGVVKTMHEIADSSKKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGE 400
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040  436 VKSLSDQTAKSTEEIGRLIAEIQASTQAAVDAVETMGGHIVEIDGVASSVAAAMEQQDAATREIARSISESASAAKEVSa 515
Cdd:PRK15048 401 VRNLASRSAQAAKEIKALIEDSVSRVDTGSVLVESAGETMNNIVNAVTRVTDIMGEIASASDEQSRGIDQVALAVSEMD- 479
                        250       260       270
                 ....*....|....*....|....*....|..
gi 27376040  516 kigNVSRDAASVNERAAEVRQAIAGMASNLEQ 547
Cdd:PRK15048 480 ---RVTQQNASLVQESAAAAAALEEQASRLTQ 508
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
378-540 9.22e-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  Cd Length: 207  Bit Score: 100.21  E-value: 9.22e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040   378 EQARSTIQALAGSVKKIAEVSDLIGGIAGQTNLLALNATIEAARAGEAGRGFAVVAAEVKSLSDQTAKSTEEIGRLIAEI 457
Cdd:pfam00015  23 DDAVETMEELETSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLAERSAQAAKEIEALIEEI 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040   458 QASTQAAV---------------------DAVETMGGHIVEIDGVASSVAAAMEQQDAATREIARSISESASAAKEVSAK 516
Cdd:pfam00015 103 VKQTNDSTasiqqtrtevevgstivestgEALKEIVEAVAEIADIVQEIAAASDEQSAGIDQVNQAVARIDQVTQQNAAL 182
                         170       180
                  ....*....|....*....|....
gi 27376040   517 IGNVSRDAASVNERAAEVRQAIAG 540
Cdd:pfam00015 183 VEESAAAAETLEEQAEELTASVAQ 206
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
163-357 9.77e-09

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: 58.25  E-value: 9.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040   163 IDSIVESANKQNAdmeklAAERDSTMLyillgVSAAVLAFVAAGLLGVAL-----------GVVRPIVRMTDTMQRLATG 231
Cdd:TIGR02956 304 VSQLVNAQNQRTE-----AAVSDLLMT-----LSVAQFGLLITGMLGLVIlvfimwrvvyrSVILRLNQHTQALLRLALG 373
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040   232 DLaaDIPF-AHRQDEVGSMAGALVVFKQAAAENSRLREEQLQKEQEAALAKRgalhQMAETVERETgrsvdtasaasqgv 310
Cdd:TIGR02956 374 DL--DISLdARGDDELAHMGRAIEAFRDTAAHNLKLQADERQVAQELQEHKE----SLEQLVAQRT-------------- 433
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 27376040   311 eravSSLSEIARSLSSESQAVAAASTQALGSSQTVSAAAEELSVSIR 357
Cdd:TIGR02956 434 ----QELAETNERLNAEVKNHAKARAEAEEANRAKSAFLATMSHEIR 476
NtrY COG5000
Signal transduction histidine kinase involved in nitrogen fixation and metabolism regulation ...
160-282 7.04e-06

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


Pssm-ID: 227333  Cd Length: 712  Bit Score: 48.61  E-value: 7.04e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040 160 RAVIDSIVESA---NKQNADMEKLAAERDS-TMLYILLGVSAAVLAFVAAGLLGVALG--VVRPIVRMTDTMQRLATGDL 233
Cdd:COG5000 245 RPVDPKVAEHAdltEGAAAEYRELEAGRDGlQIAFALLYLSTALLVLLAAIWTAIAFArrIVRPIRKLIEAADEVADGDL 324
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 27376040 234 AADIPFAHRQDEVGSMAGAlvvFKQAAAENSRLREEQLQKEQEAALAKR 282
Cdd:COG5000 325 DVQVPVRRVDEDVGRLSKA---FNKMTEQLSSQQEALERAKDALEQRRR 370
HAMP pfam00672
HAMP domain;
192-253 8.88e-06

HAMP domain;


Pssm-ID: 307012  Cd Length: 69  Bit Score: 44.87  E-value: 8.88e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27376040   192 LLGVSAAVLAFVAAGLLGVALGVVRPIVRMTDTMQRLATGDLaaDIPFAHRQDEVGSMAGAL 253
Cdd:pfam00672   1 LLLVLLIALLLALLLAWLLARRILRPLRRLAEAARRIASGDL--DVPLESGRDEIGELARAF 60
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
267-549 4.20e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008  Cd Length: 1179  Bit Score: 43.12  E-value: 4.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040    267 REEQLQKEQEAALAKRGALHQMAETVEREtgrsvdtasaaSQGVERAVSSLSEIARSLSSESQAVAAASTQAlgssqtvS 346
Cdd:TIGR02168  692 KIAELEKALAELRKELEELEEELEQLRKE-----------LEELSRQISALRKDLARLEAEVEQLEERIAQL-------S 753
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040    347 AAAEELSVSIREIAGQVARTSTVTRSAVAGREQARSTIQALAGSVKKIAEVSDLIGGIAGQTNLLALNATIEAA----RA 422
Cdd:TIGR02168  754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLEslerRI 833
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040    423 GEAGRGFAVVAAEVKSLSDQTAKSTEEIGRL---IAEIQASTQAAVDAVETMGGHIVEIDGVASSVAAAMEQQDAATREI 499
Cdd:TIGR02168  834 AATERRLEDLEEQIEELSEDIESLAAEIEELeelIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL 913
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 27376040    500 ARSISESASAAKEVSAKIGNVSRDAASVNERAAEVRQAIAGMASNLEQLR 549
Cdd:TIGR02168  914 RRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKI 963
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
214-253 5.05e-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: 39.54  E-value: 5.05e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 27376040 214 VVRPIVRMTDTMQRLATGDLAADIPFaHRQDEVGSMAGAL 253
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGDLDVRLPV-TGRDEIGELARAF 39
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility, Signal transduction mechanisms];
343-558 1.07e-03

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


Pssm-ID: 223910  Cd Length: 408  Bit Score: 41.51  E-value: 1.07e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040 343 QTVSAAAEELSVSIREIAGQVARTSTVTRSAVAGREQARSTIQALAGSVKKIAEVSDLIGGIAGQTNLLALNATIEAArA 422
Cdd:COG0840  10 ELIELAAGEADAGLLKLKKLIDELGKLLLSLNLILDDAASAEAAALKAVLKFLLISLLVAIIVVLVLAILLLRAILEP-I 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040 423 GEAGRGFAVVAA------EVKSLSDQTAKSTEEIGRLIAEIQASTQAAVDAVETMGGHIVEIDGVASSVAAAMEQQDAAT 496
Cdd:COG0840  89 SDLLEVVERIAAgdltkrIDESSNDEFGQLAKSFNEMILNLRQIIDAVQDNAEALSGASEEIAASATELSARADQQAESL 168
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27376040 497 REIARSISESASAAKEVSAKIGNVSRDAASVNERAAEVRQAIAGMASNLEQLRSVVVRTVRD 558
Cdd:COG0840 169 EEVASAIEELSETVKEVAFNAKEAAALASEASQVAEEGGEEVRQAVEQMQEIAEELAEVVKK 230
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
287-396 2.39e-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  Cd Length: 262  Bit Score: 39.96  E-value: 2.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040    287 QMAETVERETGRSVDTASAASQGVERAVSSLSEIARSLssesQAVAAASTQALGSSQTVSAAAEELSVSIREIAGQVART 366
Cdd:smart00283 151 SLIKEIQEETNEAVAAMEESSSEVEEGVELVEETGDAL----EEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEI 226
                           90       100       110
                   ....*....|....*....|....*....|
gi 27376040    367 STVTRSAVAGREQARSTIQALAGSVKKIAE 396
Cdd:smart00283 227 AQVTQETAAMSEEISAAAEELSGLAEELDE 256
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
214-253 3.05e-03

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


Pssm-ID: 197640  Cd Length: 53  Bit Score: 37.23  E-value: 3.05e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 27376040    214 VVRPIVRMTDTMQRLATGDLAADIPfAHRQDEVGSMAGAL 253
Cdd:smart00304   3 LLRPLRRLAEAAQRIADGDLTVRLP-VDGRDEIGELARAF 41
MlaD COG1463
ABC-type transporter Mla maintaining outer membrane lipid asymmetry, periplasmic component ...
434-555 4.66e-03

ABC-type transporter Mla maintaining outer membrane lipid asymmetry, periplasmic component MlaD [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 224380  Cd Length: 359  Bit Score: 39.37  E-value: 4.66e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040 434 AEVKSLSDQTAKSTEEIGRLIAEIQASTQAAVDAVETMGGHIVEI----DGVASSVAAAMEQQDAATREIARSISESASA 509
Cdd:COG1463 158 DRLNAILNEAAAALAGTGPQLNALLDNLAQFTDALNARDGDIGALianlNQLLDSLAAASDQLDRLLDNLATLTAALAAR 237
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 27376040 510 AKEVSAKIGNVSRDAASVNERAAEVRQAIAGMASNLEQLRSVVVRT 555
Cdd:COG1463 238 RDALDDALAALSALAATVNDLLAENRPNLNQALANLRPLATLLVDY 283
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
247-549 7.69e-03

Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 224117  Cd Length: 1163  Bit Score: 38.93  E-value: 7.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040  247 GSMAGALVVFKQAAAENSRLREEQLQ-KEQEAALAKrgalhqmAETVERETGRSVDTASAASQGVERAVSSLSEIARSLS 325
Cdd:COG1196  650 GSITGGSRNKRSSLAQKRELKELEEElAELEAQLEK-------LEEELKSLKNELRSLEDLLEELRRQLEELERQLEELK 722
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040  326 SESQAVAAASTQALGSSQTVSAAAEELSVSIREIAGQVARTSTVTRSAVAGREQARSTIQALAGSVKKIAEvsdliggia 405
Cdd:COG1196  723 RELAALEEELEQLQSRLEELEEELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQE--------- 793
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27376040  406 gqtNLLALNATIEAARAgeagrgfavvaaEVKSLSDQTAKSTEEIGRLIAEIQASTQAavdavetmgghIVEIDGVASSV 485
Cdd:COG1196  794 ---ELEELEEELEEAER------------RLDALERELESLEQRRERLEQEIEELEEE-----------IEELEEKLDEL 847
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27376040  486 AAAMEQQDAATREIARSISESASAAKEVSAKIGNVSRDAASVNERAAEVRQAIAGMASNLEQLR 549
Cdd:COG1196  848 EEELEELEKELEELKEELEELEAEKEELEDELKELEEEKEELEEELRELESELAELKEEIEKLR 911
 
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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