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Conserved domains on  [gi|39996405|ref|NP_952356|]
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methyl-accepting chemotaxis sensory transducer, class 34H [Geobacter sulfurreducens PCA]

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List of domain hits

Name Accession Description Interval E-value
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
209-256 5.57e-08

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: 49.56  E-value: 5.57e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 39996405 209 LVRPLRDAVATVDRLATGDLSVAVEAKGTDEIGRLLAAMGNMVSKLRE 256
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGDLDVRLPVTGRDEIGELARAFNQMAERLRE 48
MCP_signal super family cl19050
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
299-472 2.27e-42

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: 267403  Cd Length: 200  Bit Score: 150.47  E-value: 2.27e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996405 299 NMEEMSGSIRHTADNAVQTEKIAGKSAADAREGGEAVAETVSAMKVIAGKIA-------IIEEIARQTNLLALNAAIEAA 371
Cdd:cd11386  13 SADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAeigeiveVIDDIAEQTNLLALNAAIEAA 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996405 372 RAGEHGKGFAVVASEVRKLAERSQKAAGEIGEL-------SASSVRIAEKAGEMLARMIPDIQRTAELVQEISAACKEQD 444
Cdd:cd11386  93 RAGEAGRGFAVVADEVRKLAEESAEAAKEIEELieeiqeqTEEAVEAMEETSEEVEEGVELVEETGRAFEEIVASVEEVA 172
                       170       180
                ....*....|....*....|....*...
gi 39996405 445 SGADQINRAIQQLDNVIQQNASTSEEMA 472
Cdd:cd11386 173 DGIQEISAATQEQSASTQEIAAAVEEIA 200
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
261-492 1.11e-51

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: 177.86  E-value: 1.11e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996405    261 VKSASDNVAAGARELSVSAEEMSEGATEQAAAAEQASGNMEEMSGSIRHTADNAVQTEKIAGKSAADAREGGEAVAETVS 340
Cdd:smart00283   2 VSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAVS 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996405    341 AMKVIAGK-------IAIIEEIARQTNLLALNAAIEAARAGEHGKGFAVVASEVRKLAERSQKAAGEIGEL--------- 404
Cdd:smart00283  82 AVEELEESsdeigeiVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLikeiqeetn 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996405    405 ------------SASSVRIAEKAGEMLARMIPDIQRTAELVQEISAACKEQDSGADQINRAIQQLDNVIQQNASTSEEMA 472
Cdd:smart00283 162 eavaameessseVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEIS 241
                          250       260
                   ....*....|....*....|
gi 39996405    473 STSEELASQAEQLQATIAFF 492
Cdd:smart00283 242 AAAEELSGLAEELDELVERF 261
 
Name Accession Description Interval E-value
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
209-256 5.57e-08

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: 49.56  E-value: 5.57e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 39996405 209 LVRPLRDAVATVDRLATGDLSVAVEAKGTDEIGRLLAAMGNMVSKLRE 256
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGDLDVRLPVTGRDEIGELARAFNQMAERLRE 48
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
299-472 2.27e-42

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: 150.47  E-value: 2.27e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996405 299 NMEEMSGSIRHTADNAVQTEKIAGKSAADAREGGEAVAETVSAMKVIAGKIA-------IIEEIARQTNLLALNAAIEAA 371
Cdd:cd11386  13 SADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAeigeiveVIDDIAEQTNLLALNAAIEAA 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996405 372 RAGEHGKGFAVVASEVRKLAERSQKAAGEIGEL-------SASSVRIAEKAGEMLARMIPDIQRTAELVQEISAACKEQD 444
Cdd:cd11386  93 RAGEAGRGFAVVADEVRKLAEESAEAAKEIEELieeiqeqTEEAVEAMEETSEEVEEGVELVEETGRAFEEIVASVEEVA 172
                       170       180
                ....*....|....*....|....*...
gi 39996405 445 SGADQINRAIQQLDNVIQQNASTSEEMA 472
Cdd:cd11386 173 DGIQEISAATQEQSASTQEIAAAVEEIA 200
HAMP pfam00672
HAMP domain;
187-256 1.88e-10

HAMP domain;


Pssm-ID: 250044  Cd Length: 70  Bit Score: 57.24  E-value: 1.88e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996405   187 IVGSAVGTVLLACLVAGFVSGRLVRPLRDAVATVDRLATGDLSVAVEAKGTDEIGRLLAAMGNMVSKLRE 256
Cdd:pfam00672   1 LLLVLLIALLLLLLLAWLLARRLLRPLRRLAEAARRIASGDLDDRVPVSGPDEIGELARAFNQMADRLRE 70
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
208-259 2.70e-08

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


Pssm-ID: 197640  Cd Length: 53  Bit Score: 50.71  E-value: 2.70e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 39996405    208 RLVRPLRDAVATVDRLATGDLSVAVEAKGTDEIGRLLAAMGNMVSKLREVVT 259
Cdd:smart00304   2 RLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRLEETIA 53
FlxA pfam14282
FlxA-like protein; This family includes FlxA from Escherichia coli. The expression of FlxA is ...
437-490 8.70e-03

FlxA-like protein; This family includes FlxA from Escherichia coli. The expression of FlxA is regulated by the FliA sigma factor, a transcription factor specific for class 3 flagellar operons. However FlxA is not required for flagellar function or formation.


Pssm-ID: 258463  Cd Length: 106  Bit Score: 34.70  E-value: 8.70e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 39996405   437 SAACKEQDSGADQINRAIQQLDNVIQQNASTSEEMASTSEELASQAEQLQATIA 490
Cdd:pfam14282   8 TSSSASSGSSDSQIKSLQKQIQSLTKQLKELSSSEDLTAEEKQKQQQLIQQQIQ 61
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
261-492 1.11e-51

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: 177.86  E-value: 1.11e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996405    261 VKSASDNVAAGARELSVSAEEMSEGATEQAAAAEQASGNMEEMSGSIRHTADNAVQTEKIAGKSAADAREGGEAVAETVS 340
Cdd:smart00283   2 VSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAVS 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996405    341 AMKVIAGK-------IAIIEEIARQTNLLALNAAIEAARAGEHGKGFAVVASEVRKLAERSQKAAGEIGEL--------- 404
Cdd:smart00283  82 AVEELEESsdeigeiVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLikeiqeetn 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996405    405 ------------SASSVRIAEKAGEMLARMIPDIQRTAELVQEISAACKEQDSGADQINRAIQQLDNVIQQNASTSEEMA 472
Cdd:smart00283 162 eavaameessseVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEIS 241
                          250       260
                   ....*....|....*....|
gi 39996405    473 STSEELASQAEQLQATIAFF 492
Cdd:smart00283 242 AAAEELSGLAEELDELVERF 261
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction ...
190-494 1.70e-61

Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction mechanisms]


Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 208.31  E-value: 1.70e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996405 190 SAVGTVLLACLVAGFVSGRLVRPLRDAVATVDRLATGDLSVAVEAKGTDEIGRLLAAMGNMVSKLREVVTSVKSASDNVA 269
Cdd:COG0840  65 SLLVAIIVVLVLAILLLRAILEPISDLLEVVERIAAGDLTKRIDESSNDEFGQLAKSFNEMILNLRQIIDAVQDNAEALS 144
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996405 270 AGARELSVSAEEMSEGATEQAAAAEQASGNMEEMSGSIRHTADNAVQTEKIAGKSAADAREGGEAVAETVSAM------- 342
Cdd:COG0840 145 GASEEIAASATELSARADQQAESLEEVASAIEELSETVKEVAFNAKEAAALASEASQVAEEGGEEVRQAVEQMqeiaeel 224
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996405 343 -----------KVIAGKIAIIEEIARQTNLLALNAAIEAARAGEHGKGFAVVASEVRKLAERSQKAAGEIGEL------- 404
Cdd:COG0840 225 aevvkklsessQEIEEITSVINSIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSADSAKEIGLLieeiqne 304
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996405 405 --------------SASSVRIAEKAGEMLARMIPDIQRTAELVQEISAACKEQDSGADQINRAIQQLDNVIQQNASTSEE 470
Cdd:COG0840 305 aadavehmeesaseVSEGVKLVEETGSSLGEIAAAIEEVSQLISEIAAATEEQTAVLEEINASIEELDDVTQENAAAVEE 384
                       330       340
                ....*....|....*....|....
gi 39996405 471 MASTSEELASQAEQLQATIAFFNI 494
Cdd:COG0840 385 LAAASEELKELAEKLLELVAKFKL 408
PRK15041 PRK15041
methyl-accepting chemotaxis protein I; Provisional
179-494 5.31e-56

methyl-accepting chemotaxis protein I; Provisional


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 197.10  E-value: 5.31e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996405  179 SYDRLKLIIVGsaVGTVLLACLVAGF--VSGRLVRPLRDAVATVDRLATGDLSVAVEAKGTDEIGRLLAAMGNMVSKLRE 256
Cdd:PRK15041 188 SYSQAMWILVG--VMIVVLAVIFAVWfgIKASLVAPMNRLIDSIRHIAGGDLVKPIEVDGSNEMGQLAESLRHMQGELMR 265
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996405  257 VVTSVKSASDNVAAGARELSVSAEEMSEGATEQAAAAEQASGNMEEMSGSIRHTADNAVQTEKIAGKSAADAREGGEAVA 336
Cdd:PRK15041 266 TVGDVRNGANAIYSGASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVKQNAENARQASHLALSASETAQRGGKVVD 345
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996405  337 ETVSAMKVIAGK-------IAIIEEIARQTNLLALNAAIEAARAGEHGKGFAVVASEVRKLAERSQKAAGEIGELSASSV 409
Cdd:PRK15041 346 NVVQTMRDISTSsqkiadiISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSV 425
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996405  410 -------RIAEKAGEMLARMIPDIQRTAELVQEISAACKEQDSGADQINRAIQQLDNVIQQNASTSEEMASTSEELASQA 482
Cdd:PRK15041 426 gkvdvgsTLVESAGETMAEIVSAVTRVTDIMGEIASASDEQSRGIDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQA 505
                        330
                 ....*....|..
gi 39996405  483 EQLQATIAFFNI 494
Cdd:PRK15041 506 SRLTEAVAVFRI 517
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
308-494 8.57e-43

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: 249510 [Multi-domain]  Cd Length: 213  Bit Score: 151.83  E-value: 8.57e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996405   308 RHTADNAVQTEKIAgksAADAREGGEAVAETVSAMKVIAGK-------IAIIEEIARQTNLLALNAAIEAARAGEHGKGF 380
Cdd:pfam00015   1 AQASDLAQLASEEA---LDEMSQIGQVVDDAVETMEELETSskkisdiISVIDEIAFQTNLLALNAAIEAARAGEQGRGF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996405   381 AVVASEVRKLAERSQKAAGEIGELSASSVR---------------------IAEKAGEMLARMIPDIQRTAELVQEISAA 439
Cdd:pfam00015  78 AVVADEVRKLAERSAQAAKEIEALIEEIVKqtndstasiqqtrtevevgstIVESTGEALKEIVDAVAEIADIVQEIAAA 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 39996405   440 CKEQDSGADQINRAIQQLDNVIQQNASTSEEMASTSEELASQAEQLQATIAFFNI 494
Cdd:pfam00015 158 SDEQSAGIDQVNQAVARIDQVTQQNAALVEESAAAAETLEEQAEELTASVAQFRI 212
NtrY COG5000
Signal transduction histidine kinase involved in nitrogen fixation and metabolism regulation ...
181-275 2.78e-07

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


Pssm-ID: 227333 [Multi-domain]  Cd Length: 712  Bit Score: 51.69  E-value: 2.78e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996405 181 DRLKLIIVGSAVGTVLLACLVA----GFVSGRLVRPLRDAVATVDRLATGDLSVAVEA-KGTDEIGRLLAAMGNMVSKLR 255
Cdd:COG5000 273 DGLQIAFALLYLSTALLVLLAAiwtaIAFARRIVRPIRKLIEAADEVADGDLDVQVPVrRVDEDVGRLSKAFNKMTEQLS 352
                        90       100
                ....*....|....*....|
gi 39996405 256 EVVTSVKSASDNVAAGAREL 275
Cdd:COG5000 353 SQQEALERAKDALEQRRRFL 372
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
170-284 6.45e-06

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: 234070 [Multi-domain]  Cd Length: 968  Bit Score: 47.47  E-value: 6.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996405   170 GVKKSEFFESYDRLKLIIVGsAVGTVLLACLVAGFVSGRLVRPLRDAVATVDRLATGDLSVAVEAKGTDEigrlLAAMGN 249
Cdd:TIGR02956 318 AVSDLLMTLSVAQFGLLITG-MLGLVILVFIMWRVVYRSVILRLNQHTQALLRLALGDLDISLDARGDDE----LAHMGR 392
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 39996405   250 MVSKLREVVTSVKSASDNVAAGARELSVSAEEMSE 284
Cdd:TIGR02956 393 AIEAFRDTAAHNLKLQADERQVAQELQEHKESLEQ 427
PRK10549 PRK10549
signal transduction histidine-protein kinase BaeS; Provisional
186-243 1.33e-05

signal transduction histidine-protein kinase BaeS; Provisional


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 46.16  E-value: 1.33e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 39996405  186 IIVGSavgTVLLACLVAGFVSGRLVRPLRDAVATVDRLATGDLSVAVEAKGTDEIGRL 243
Cdd:PRK10549 168 LIVAL---STLLAALATFLLARGLLAPVKRLVEGTHKLAAGDFTTRVTPTSRDELGRL 222
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
336-493 7.75e-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: 233757 [Multi-domain]  Cd Length: 1179  Bit Score: 40.81  E-value: 7.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996405    336 AETVSAMKVIAGKIAIIEE--IARQTNLLALNAAIEAARAGEHG---------KGFAVVASEVRKLAERSQKAAGEIGEL 404
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKalAELRKELEELEEELEQLRKELEElsrqisalrKDLARLEAEVEQLEERIAQLSKELTEL 759
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996405    405 SASSVRIA---EKAGEMLARMIPDIQRTAELVQEISAACKEQDSGAD-------QINRAIQQLDNVIQQNASTSEEMAST 474
Cdd:TIGR02168  760 EAEIEELEerlEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDelraeltLLNEEAANLRERLESLERRIAATERR 839
                          170
                   ....*....|....*....
gi 39996405    475 SEELASQAEQLQATIAFFN 493
Cdd:TIGR02168  840 LEDLEEQIEELSEDIESLA 858
 
Name Accession Description Interval E-value
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
209-256 5.57e-08

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: 49.56  E-value: 5.57e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 39996405 209 LVRPLRDAVATVDRLATGDLSVAVEAKGTDEIGRLLAAMGNMVSKLRE 256
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGDLDVRLPVTGRDEIGELARAFNQMAERLRE 48
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
299-472 2.27e-42

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: 150.47  E-value: 2.27e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996405 299 NMEEMSGSIRHTADNAVQTEKIAGKSAADAREGGEAVAETVSAMKVIAGKIA-------IIEEIARQTNLLALNAAIEAA 371
Cdd:cd11386  13 SADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAeigeiveVIDDIAEQTNLLALNAAIEAA 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996405 372 RAGEHGKGFAVVASEVRKLAERSQKAAGEIGEL-------SASSVRIAEKAGEMLARMIPDIQRTAELVQEISAACKEQD 444
Cdd:cd11386  93 RAGEAGRGFAVVADEVRKLAEESAEAAKEIEELieeiqeqTEEAVEAMEETSEEVEEGVELVEETGRAFEEIVASVEEVA 172
                       170       180
                ....*....|....*....|....*...
gi 39996405 445 SGADQINRAIQQLDNVIQQNASTSEEMA 472
Cdd:cd11386 173 DGIQEISAATQEQSASTQEIAAAVEEIA 200
HAMP pfam00672
HAMP domain;
187-256 1.88e-10

HAMP domain;


Pssm-ID: 250044  Cd Length: 70  Bit Score: 57.24  E-value: 1.88e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996405   187 IVGSAVGTVLLACLVAGFVSGRLVRPLRDAVATVDRLATGDLSVAVEAKGTDEIGRLLAAMGNMVSKLRE 256
Cdd:pfam00672   1 LLLVLLIALLLLLLLAWLLARRLLRPLRRLAEAARRIASGDLDDRVPVSGPDEIGELARAFNQMADRLRE 70
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
208-259 2.70e-08

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


Pssm-ID: 197640  Cd Length: 53  Bit Score: 50.71  E-value: 2.70e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 39996405    208 RLVRPLRDAVATVDRLATGDLSVAVEAKGTDEIGRLLAAMGNMVSKLREVVT 259
Cdd:smart00304   2 RLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRLEETIA 53
FlxA pfam14282
FlxA-like protein; This family includes FlxA from Escherichia coli. The expression of FlxA is ...
437-490 8.70e-03

FlxA-like protein; This family includes FlxA from Escherichia coli. The expression of FlxA is regulated by the FliA sigma factor, a transcription factor specific for class 3 flagellar operons. However FlxA is not required for flagellar function or formation.


Pssm-ID: 258463  Cd Length: 106  Bit Score: 34.70  E-value: 8.70e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 39996405   437 SAACKEQDSGADQINRAIQQLDNVIQQNASTSEEMASTSEELASQAEQLQATIA 490
Cdd:pfam14282   8 TSSSASSGSSDSQIKSLQKQIQSLTKQLKELSSSEDLTAEEKQKQQQLIQQQIQ 61
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
261-492 1.11e-51

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: 177.86  E-value: 1.11e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996405    261 VKSASDNVAAGARELSVSAEEMSEGATEQAAAAEQASGNMEEMSGSIRHTADNAVQTEKIAGKSAADAREGGEAVAETVS 340
Cdd:smart00283   2 VSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAVS 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996405    341 AMKVIAGK-------IAIIEEIARQTNLLALNAAIEAARAGEHGKGFAVVASEVRKLAERSQKAAGEIGEL--------- 404
Cdd:smart00283  82 AVEELEESsdeigeiVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLikeiqeetn 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996405    405 ------------SASSVRIAEKAGEMLARMIPDIQRTAELVQEISAACKEQDSGADQINRAIQQLDNVIQQNASTSEEMA 472
Cdd:smart00283 162 eavaameessseVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEIS 241
                          250       260
                   ....*....|....*....|
gi 39996405    473 STSEELASQAEQLQATIAFF 492
Cdd:smart00283 242 AAAEELSGLAEELDELVERF 261
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction ...
190-494 1.70e-61

Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction mechanisms]


Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 208.31  E-value: 1.70e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996405 190 SAVGTVLLACLVAGFVSGRLVRPLRDAVATVDRLATGDLSVAVEAKGTDEIGRLLAAMGNMVSKLREVVTSVKSASDNVA 269
Cdd:COG0840  65 SLLVAIIVVLVLAILLLRAILEPISDLLEVVERIAAGDLTKRIDESSNDEFGQLAKSFNEMILNLRQIIDAVQDNAEALS 144
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996405 270 AGARELSVSAEEMSEGATEQAAAAEQASGNMEEMSGSIRHTADNAVQTEKIAGKSAADAREGGEAVAETVSAM------- 342
Cdd:COG0840 145 GASEEIAASATELSARADQQAESLEEVASAIEELSETVKEVAFNAKEAAALASEASQVAEEGGEEVRQAVEQMqeiaeel 224
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996405 343 -----------KVIAGKIAIIEEIARQTNLLALNAAIEAARAGEHGKGFAVVASEVRKLAERSQKAAGEIGEL------- 404
Cdd:COG0840 225 aevvkklsessQEIEEITSVINSIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSADSAKEIGLLieeiqne 304
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996405 405 --------------SASSVRIAEKAGEMLARMIPDIQRTAELVQEISAACKEQDSGADQINRAIQQLDNVIQQNASTSEE 470
Cdd:COG0840 305 aadavehmeesaseVSEGVKLVEETGSSLGEIAAAIEEVSQLISEIAAATEEQTAVLEEINASIEELDDVTQENAAAVEE 384
                       330       340
                ....*....|....*....|....
gi 39996405 471 MASTSEELASQAEQLQATIAFFNI 494
Cdd:COG0840 385 LAAASEELKELAEKLLELVAKFKL 408
PRK15041 PRK15041
methyl-accepting chemotaxis protein I; Provisional
179-494 5.31e-56

methyl-accepting chemotaxis protein I; Provisional


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 197.10  E-value: 5.31e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996405  179 SYDRLKLIIVGsaVGTVLLACLVAGF--VSGRLVRPLRDAVATVDRLATGDLSVAVEAKGTDEIGRLLAAMGNMVSKLRE 256
Cdd:PRK15041 188 SYSQAMWILVG--VMIVVLAVIFAVWfgIKASLVAPMNRLIDSIRHIAGGDLVKPIEVDGSNEMGQLAESLRHMQGELMR 265
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996405  257 VVTSVKSASDNVAAGARELSVSAEEMSEGATEQAAAAEQASGNMEEMSGSIRHTADNAVQTEKIAGKSAADAREGGEAVA 336
Cdd:PRK15041 266 TVGDVRNGANAIYSGASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVKQNAENARQASHLALSASETAQRGGKVVD 345
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996405  337 ETVSAMKVIAGK-------IAIIEEIARQTNLLALNAAIEAARAGEHGKGFAVVASEVRKLAERSQKAAGEIGELSASSV 409
Cdd:PRK15041 346 NVVQTMRDISTSsqkiadiISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSV 425
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996405  410 -------RIAEKAGEMLARMIPDIQRTAELVQEISAACKEQDSGADQINRAIQQLDNVIQQNASTSEEMASTSEELASQA 482
Cdd:PRK15041 426 gkvdvgsTLVESAGETMAEIVSAVTRVTDIMGEIASASDEQSRGIDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQA 505
                        330
                 ....*....|..
gi 39996405  483 EQLQATIAFFNI 494
Cdd:PRK15041 506 SRLTEAVAVFRI 517
PRK09793 PRK09793
methyl-accepting protein IV; Provisional
179-494 4.06e-55

methyl-accepting protein IV; Provisional


Pssm-ID: 182079 [Multi-domain]  Cd Length: 533  Bit Score: 194.13  E-value: 4.06e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996405  179 SYDRLKLIIVGSAVGTVLLACLVAGFVSGRLVRPLRDAVATVDRLATGDLSVAVEAKGTDEIGRLLAAMGNMVSKLREVV 258
Cdd:PRK09793 184 NYQISALVFISMIIVAAIYISSALWWTRKMIVQPLAIIGSHFDSIAAGNLARPIAVYGRNEITAIFASLKTMQQALRGTV 263
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996405  259 TSVKSASDNVAAGARELSVSAEEMSEGATEQAAAAEQASGNMEEMSGSIRHTADNAVQTEKIAGKSAADAREGGEAVAET 338
Cdd:PRK09793 264 SDVRKGSQEMHIGIAEIVAGNNDLSSRTEQQAASLAQTAASMEQLTATVGQNADNARQASELAKNAATTAQAGGVQVSTM 343
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996405  339 VSAMKVIAGK-------IAIIEEIARQTNLLALNAAIEAARAGEHGKGFAVVASEVRKLAERSQKAAGEIGELSASSV-- 409
Cdd:PRK09793 344 THTMQEIATSsqkigdiISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKGLIEESVnr 423
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996405  410 -----RIAEKAGEMLARMIPDIQRTAELVQEISAACKEQDSGADQINRAIQQLDNVIQQNASTSEEMASTSEELASQAEQ 484
Cdd:PRK09793 424 vqqgsKLVNNAAATMTDIVSSVTRVNDIMGEIASASEEQRRGIEQVAQAVSQMDQVTQQNASLVEEAAVATEQLANQADH 503
                        330
                 ....*....|
gi 39996405  485 LQATIAFFNI 494
Cdd:PRK09793 504 LSSRVAVFTL 513
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
209-494 1.09e-54

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 193.30  E-value: 1.09e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996405  209 LVRPLRDAVATVDRLATGDLSVAVEAKGTDEIGRLLAAMGNMVSKLREVVTSVKSASDNVAAGARELSVSAEEMSEGATE 288
Cdd:PRK15048 216 LLTPLAKIIAHIREIAGGNLANTLTIDGRSEMGDLAQSVSHMQRSLTDTVTHVREGSDAIYAGTREIAAGNTDLSSRTEQ 295
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996405  289 QAAAAEQASGNMEEMSGSIRHTADNAVQTEKIAGKSAADAREGGEAVAETVSAM-------KVIAGKIAIIEEIARQTNL 361
Cdd:PRK15048 296 QASALEETAASMEQLTATVKQNADNARQASQLAQSASDTAQHGGKVVDGVVKTMheiadssKKIADIISVIDGIAFQTNI 375
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996405  362 LALNAAIEAARAGEHGKGFAVVASEVRKLAERSQKAAGEIGELSASSVR-------IAEKAGEMLARMIPDIQRTAELVQ 434
Cdd:PRK15048 376 LALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKALIEDSVSrvdtgsvLVESAGETMNNIVNAVTRVTDIMG 455
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996405  435 EISAACKEQDSGADQINRAIQQLDNVIQQNASTSEEMASTSEELASQAEQLQATIAFFNI 494
Cdd:PRK15048 456 EIASASDEQSRGIDQVALAVSEMDRVTQQNASLVQESAAAAAALEEQASRLTQAVSAFRL 515
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
308-494 8.57e-43

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: 249510 [Multi-domain]  Cd Length: 213  Bit Score: 151.83  E-value: 8.57e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996405   308 RHTADNAVQTEKIAgksAADAREGGEAVAETVSAMKVIAGK-------IAIIEEIARQTNLLALNAAIEAARAGEHGKGF 380
Cdd:pfam00015   1 AQASDLAQLASEEA---LDEMSQIGQVVDDAVETMEELETSskkisdiISVIDEIAFQTNLLALNAAIEAARAGEQGRGF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996405   381 AVVASEVRKLAERSQKAAGEIGELSASSVR---------------------IAEKAGEMLARMIPDIQRTAELVQEISAA 439
Cdd:pfam00015  78 AVVADEVRKLAERSAQAAKEIEALIEEIVKqtndstasiqqtrtevevgstIVESTGEALKEIVDAVAEIADIVQEIAAA 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 39996405   440 CKEQDSGADQINRAIQQLDNVIQQNASTSEEMASTSEELASQAEQLQATIAFFNI 494
Cdd:pfam00015 158 SDEQSAGIDQVNQAVARIDQVTQQNAALVEESAAAAETLEEQAEELTASVAQFRI 212
NtrY COG5000
Signal transduction histidine kinase involved in nitrogen fixation and metabolism regulation ...
181-275 2.78e-07

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


Pssm-ID: 227333 [Multi-domain]  Cd Length: 712  Bit Score: 51.69  E-value: 2.78e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996405 181 DRLKLIIVGSAVGTVLLACLVA----GFVSGRLVRPLRDAVATVDRLATGDLSVAVEA-KGTDEIGRLLAAMGNMVSKLR 255
Cdd:COG5000 273 DGLQIAFALLYLSTALLVLLAAiwtaIAFARRIVRPIRKLIEAADEVADGDLDVQVPVrRVDEDVGRLSKAFNKMTEQLS 352
                        90       100
                ....*....|....*....|
gi 39996405 256 EVVTSVKSASDNVAAGAREL 275
Cdd:COG5000 353 SQQEALERAKDALEQRRRFL 372
VicK COG5002
Signal transduction histidine kinase [Signal transduction mechanisms]
161-285 4.07e-06

Signal transduction histidine kinase [Signal transduction mechanisms]


Pssm-ID: 227335 [Multi-domain]  Cd Length: 459  Bit Score: 47.81  E-value: 4.07e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996405 161 GAIIGVLYVGVK-KSEFFESYDRLKLIIVGSAVGTVLLACLVAgFVSGRLVRPLRDAVATVDRLATGDLSVAVEAKGTDE 239
Cdd:COG5002   6 KKVIGAIYIEASiEDVYNQMNFINNILISGTLIALIITALLGI-LLARTITKPITDMRKQAVDMARGNYSRKVKVYGTDE 84
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 39996405 240 IGRLLAAMGNMVSKLREvvtsvksASDNVAAGARELSVSAEEMSEG 285
Cdd:COG5002  85 IGELADSFNDLTKRVQE-------AQANTEQERRKLDSVLAYMTDG 123
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
170-284 6.45e-06

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: 234070 [Multi-domain]  Cd Length: 968  Bit Score: 47.47  E-value: 6.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996405   170 GVKKSEFFESYDRLKLIIVGsAVGTVLLACLVAGFVSGRLVRPLRDAVATVDRLATGDLSVAVEAKGTDEigrlLAAMGN 249
Cdd:TIGR02956 318 AVSDLLMTLSVAQFGLLITG-MLGLVILVFIMWRVVYRSVILRLNQHTQALLRLALGDLDISLDARGDDE----LAHMGR 392
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 39996405   250 MVSKLREVVTSVKSASDNVAAGARELSVSAEEMSE 284
Cdd:TIGR02956 393 AIEAFRDTAAHNLKLQADERQVAQELQEHKESLEQ 427
PRK10549 PRK10549
signal transduction histidine-protein kinase BaeS; Provisional
186-243 1.33e-05

signal transduction histidine-protein kinase BaeS; Provisional


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 46.16  E-value: 1.33e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 39996405  186 IIVGSavgTVLLACLVAGFVSGRLVRPLRDAVATVDRLATGDLSVAVEAKGTDEIGRL 243
Cdd:PRK10549 168 LIVAL---STLLAALATFLLARGLLAPVKRLVEGTHKLAAGDFTTRVTPTSRDELGRL 222
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
155-254 8.82e-05

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 43.29  E-value: 8.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996405  155 PLRDaSGAIIGVLYVGVKKSEFFESYDRLKLIIVGSAVGTVLLACLVAGFVSGRLVRPLRDAVATVDRLATGDlSVAVEA 234
Cdd:PRK11100 153 PIRD-GGRIIGVLSVGKPNSSMAPFIKRSERRILWAGALLLGIALLIGAGVVWWLNRSIRRLTRYADAVTEGK-PVPLPK 230
                         90       100
                 ....*....|....*....|
gi 39996405  235 KGTDEIGRLLAAMGNMVSKL 254
Cdd:PRK11100 231 LGSSELRELAQALESMRVKL 250
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
336-493 7.75e-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: 233757 [Multi-domain]  Cd Length: 1179  Bit Score: 40.81  E-value: 7.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996405    336 AETVSAMKVIAGKIAIIEE--IARQTNLLALNAAIEAARAGEHG---------KGFAVVASEVRKLAERSQKAAGEIGEL 404
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKalAELRKELEELEEELEQLRKELEElsrqisalrKDLARLEAEVEQLEERIAQLSKELTEL 759
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996405    405 SASSVRIA---EKAGEMLARMIPDIQRTAELVQEISAACKEQDSGAD-------QINRAIQQLDNVIQQNASTSEEMAST 474
Cdd:TIGR02168  760 EAEIEELEerlEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDelraeltLLNEEAANLRERLESLERRIAATERR 839
                          170
                   ....*....|....*....
gi 39996405    475 SEELASQAEQLQATIAFFN 493
Cdd:TIGR02168  840 LEDLEEQIEELSEDIESLA 858
COG4372 COG4372
Uncharacterized protein conserved in bacteria with the myosin-like domain [Function unknown]
314-487 9.30e-04

Uncharacterized protein conserved in bacteria with the myosin-like domain [Function unknown]


Pssm-ID: 226809 [Multi-domain]  Cd Length: 499  Bit Score: 40.39  E-value: 9.30e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996405 314 AVQTEKIAGKSAAD-AREGGEAVAETVSAMKviAGKIAIIEEIARQT----NLLALNAAIEAARAGEHGKGFAVVASEvR 388
Cdd:COG4372  99 AAETEREAARSELQkARQEREAVRQELAAAR--QNLAKAQQELARLTkqaqDLQTRLKTLAEQRRQLEAQAQSLQASQ-K 175
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996405 389 KLAERSQKAAGEIGELSASSVRIAEKAGEMLARMIPDIQRTAEL------VQEISAACKEQDSGADQINRAIQQLDNVIQ 462
Cdd:COG4372 176 QLQASATQLKSQVLDLKLRSAQIEQEAQNLATRANAAQARTEELarraaaAQQTAQAIQQRDAQISQKAQQIAARAEQIR 255
                       170       180
                ....*....|....*....|....*
gi 39996405 463 QNASTSEEMASTSEELASQAEQLQA 487
Cdd:COG4372 256 ERERQLQRLETAQARLEQEVAQLEA 280
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.11
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • 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 et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • 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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