NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|73537566|ref|YP_297933|]
View 

methyl-accepting chemotaxis sensory transducer [Ralstonia eutropha JMP134]

Graphical summary

show options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
290-481 2.59e-50

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: 172.42  E-value: 2.59e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73537566 290 EEQASSLQQTAASMEELTSIVRQNADNAKQASALAVNASEIAAKGGDVADKVAETMEEINGASKKVVDIIAVIEGIAFQT 369
Cdd:cd11386   1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73537566 370 NILALNAAVEAARAGEQGRGFAVVAGEVRSLAQRSATAAKEIKALIGDSVDRVEKGSTLVAQSGQTMLEIVEAVRRVTDI 449
Cdd:cd11386  81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160
                       170       180       190
                ....*....|....*....|....*....|..
gi 73537566 450 MGEISAASAEQSAGIEQVNQAVTQMDSVTQQN 481
Cdd:cd11386 161 FEEIVASVEEVADGIQEISAATQEQSASTQEI 192
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
212-257 4.38e-05

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: 41.47  E-value: 4.38e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 73537566 212 IIRPLGHAVDIARTVASGDLTSDIRVDSQDETGQLLHALSEMNTNI 257
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGDLDVRLPVTGRDEIGELARAFNQMAERL 46
Tar_Tsr_LBD super family cl00144
ligand binding domain of Tar- and Tsr-related chemoreceptors; E.coli Tar (taxis to aspartate ...
3-183 8.09e-13

ligand binding domain of Tar- and Tsr-related chemoreceptors; E.coli Tar (taxis to aspartate and repellents) and Tsr (taxis to serine and repellents) are homologous chemoreceptors that have a high specificity for aspartate and serine, respectively. Both are homodimeric receptors and contain an N-terminal periplasmic ligand binding domain, a transmembrane region, a HAMP domain and a C-terminal cytosolic signaling domain.


The actual alignment was detected with superfamily member pfam12729:

Pssm-ID: 260214  Cd Length: 181  Bit Score: 66.09  E-value: 8.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73537566     3 NFGIGVRLGIGFGVVLVLCALMSAFGIMRLQQVAERTHDMMQqpltkERLVS-DWYRLMHTSVRRTTAVAK----SADPS 77
Cdd:pfam12729   1 NLKIRTKLILLFLLLALLLIIVGIVGLYSLKKINKNSETMYE-----DRLLPiKWLGEIRSNLREIRANLLelilTTDPA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73537566    78 LGAFFAKETKASLEGIAALRDKMQPMLTSEAEKAAFAKILQVREPYNASRDKITKLKQEGLTEEANAVLEKEFVPAGDAY 157
Cdd:pfam12729  76 ERDELLKDIEELRAEIDKLLKKYEKTILTEEEKKLFNEFKEQLKAYRKVRNKVLDLAKAGKNDEAYALYLTELEPARDAV 155
                         170       180
                  ....*....|....*....|....*.
gi 73537566   158 LAEIQKLLDIQRTSIDATAAEINTIY 183
Cdd:pfam12729 156 IEALDELIDYNLKVAKEAYEDNKASY 181
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction ...
150-511 6.72e-70

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


:

Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 231.42  E-value: 6.72e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73537566 150 FVPAGDAYLAEIQKLLDIQRTSIDATAAEINTIYVNARNSLILLGVLVLAIGVGFAVWLTRGIIRPLGHAVDIARTVASG 229
Cdd:COG0840  22 GLLKLKKLIDELGKLLLSLNLILDDAASAEAAALKAVLKFLLISLLVAIIVVLVLAILLLRAILEPISDLLEVVERIAAG 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73537566 230 DLTSDIRVDSQDETGQLLHALSEMNTNILHIVRDVRTGTEAIASGTSQIAVGNTDLSQRTEEQASSLQQTAASMEELTSI 309
Cdd:COG0840 102 DLTKRIDESSNDEFGQLAKSFNEMILNLRQIIDAVQDNAEALSGASEEIAASATELSARADQQAESLEEVASAIEELSET 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73537566 310 VRQNADNAKQASALAVNASEIAAKGGDVADKVAETMEEINGA-----------SKKVVDIIAVIEGIAFQTNILALNAAV 378
Cdd:COG0840 182 VKEVAFNAKEAAALASEASQVAEEGGEEVRQAVEQMQEIAEElaevvkklsesSQEIEEITSVINSIAEQTNLLALNAAI 261
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73537566 379 EAARAGEQGRGFAVVAGEVRSLAQRSATAAKEIKALIGD--------------SVDRVEKGSTLVAQSGQTMLEIVEAVR 444
Cdd:COG0840 262 EAARAGEAGRGFAVVADEVRKLAERSADSAKEIGLLIEEiqneaadavehmeeSASEVSEGVKLVEETGSSLGEIAAAIE 341
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 73537566 445 RVTDIMGEISAASAEQSAGIEQVNQAVTQMDSVTQQNAALVEEAAAAAGSLEEQAQRLKQAVATFRI 511
Cdd:COG0840 342 EVSQLISEIAAATEEQTAVLEEINASIEELDDVTQENAAAVEELAAASEELKELAEKLLELVAKFKL 408
 
Name Accession Description Interval E-value
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
290-481 2.59e-50

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: 172.42  E-value: 2.59e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73537566 290 EEQASSLQQTAASMEELTSIVRQNADNAKQASALAVNASEIAAKGGDVADKVAETMEEINGASKKVVDIIAVIEGIAFQT 369
Cdd:cd11386   1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73537566 370 NILALNAAVEAARAGEQGRGFAVVAGEVRSLAQRSATAAKEIKALIGDSVDRVEKGSTLVAQSGQTMLEIVEAVRRVTDI 449
Cdd:cd11386  81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160
                       170       180       190
                ....*....|....*....|....*....|..
gi 73537566 450 MGEISAASAEQSAGIEQVNQAVTQMDSVTQQN 481
Cdd:cd11386 161 FEEIVASVEEVADGIQEISAATQEQSASTQEI 192
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
212-257 4.38e-05

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: 41.47  E-value: 4.38e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 73537566 212 IIRPLGHAVDIARTVASGDLTSDIRVDSQDETGQLLHALSEMNTNI 257
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGDLDVRLPVTGRDEIGELARAFNQMAERL 46
4HB_MCP_1 pfam12729
Four helix bundle sensory module for signal transduction; This family is a four helix bundle ...
3-183 8.09e-13

Four helix bundle sensory module for signal transduction; This family is a four helix bundle that operates as a ubiquitous sensory module in prokaryotic signal-transduction. The 4HB_MCP is always found between two predicted transmembrane helices indicating that it detects only extracellular signals. In many cases the domain is associated with a cytoplasmic HAMP domain suggesting that most proteins carrying the bundle might share the mechanism of transmembrane signalling which is well-characterized in E coli chemoreceptors.


Pssm-ID: 193205  Cd Length: 181  Bit Score: 66.09  E-value: 8.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73537566     3 NFGIGVRLGIGFGVVLVLCALMSAFGIMRLQQVAERTHDMMQqpltkERLVS-DWYRLMHTSVRRTTAVAK----SADPS 77
Cdd:pfam12729   1 NLKIRTKLILLFLLLALLLIIVGIVGLYSLKKINKNSETMYE-----DRLLPiKWLGEIRSNLREIRANLLelilTTDPA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73537566    78 LGAFFAKETKASLEGIAALRDKMQPMLTSEAEKAAFAKILQVREPYNASRDKITKLKQEGLTEEANAVLEKEFVPAGDAY 157
Cdd:pfam12729  76 ERDELLKDIEELRAEIDKLLKKYEKTILTEEEKKLFNEFKEQLKAYRKVRNKVLDLAKAGKNDEAYALYLTELEPARDAV 155
                         170       180
                  ....*....|....*....|....*.
gi 73537566   158 LAEIQKLLDIQRTSIDATAAEINTIY 183
Cdd:pfam12729 156 IEALDELIDYNLKVAKEAYEDNKASY 181
HAMP pfam00672
HAMP domain;
190-253 5.53e-08

HAMP domain;


Pssm-ID: 250044  Cd Length: 70  Bit Score: 50.31  E-value: 5.53e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 73537566   190 LILLGVLVLAIGVGFAVWLTRGIIRPLGHAVDIARTVASGDLTSDIRVDSQDETGQLLHALSEM 253
Cdd:pfam00672   1 LLLVLLIALLLLLLLAWLLARRLLRPLRRLAEAARRIASGDLDDRVPVSGPDEIGELARAFNQM 64
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
210-262 3.51e-05

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


Pssm-ID: 197640  Cd Length: 53  Bit Score: 41.46  E-value: 3.51e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 73537566    210 RGIIRPLGHAVDIARTVASGDLTSDIRVDSQDETGQLLHALSEMNTNILHIVR 262
Cdd:smart00304   1 RRLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRLEETIA 53
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction ...
150-511 6.72e-70

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


Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 231.42  E-value: 6.72e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73537566 150 FVPAGDAYLAEIQKLLDIQRTSIDATAAEINTIYVNARNSLILLGVLVLAIGVGFAVWLTRGIIRPLGHAVDIARTVASG 229
Cdd:COG0840  22 GLLKLKKLIDELGKLLLSLNLILDDAASAEAAALKAVLKFLLISLLVAIIVVLVLAILLLRAILEPISDLLEVVERIAAG 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73537566 230 DLTSDIRVDSQDETGQLLHALSEMNTNILHIVRDVRTGTEAIASGTSQIAVGNTDLSQRTEEQASSLQQTAASMEELTSI 309
Cdd:COG0840 102 DLTKRIDESSNDEFGQLAKSFNEMILNLRQIIDAVQDNAEALSGASEEIAASATELSARADQQAESLEEVASAIEELSET 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73537566 310 VRQNADNAKQASALAVNASEIAAKGGDVADKVAETMEEINGA-----------SKKVVDIIAVIEGIAFQTNILALNAAV 378
Cdd:COG0840 182 VKEVAFNAKEAAALASEASQVAEEGGEEVRQAVEQMQEIAEElaevvkklsesSQEIEEITSVINSIAEQTNLLALNAAI 261
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73537566 379 EAARAGEQGRGFAVVAGEVRSLAQRSATAAKEIKALIGD--------------SVDRVEKGSTLVAQSGQTMLEIVEAVR 444
Cdd:COG0840 262 EAARAGEAGRGFAVVADEVRKLAERSADSAKEIGLLIEEiqneaadavehmeeSASEVSEGVKLVEETGSSLGEIAAAIE 341
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 73537566 445 RVTDIMGEISAASAEQSAGIEQVNQAVTQMDSVTQQNAALVEEAAAAAGSLEEQAQRLKQAVATFRI 511
Cdd:COG0840 342 EVSQLISEIAAATEEQTAVLEEINASIEELDDVTQENAAAVEELAAASEELKELAEKLLELVAKFKL 408
PRK15041 PRK15041
methyl-accepting chemotaxis protein I; Provisional
146-511 1.02e-121

methyl-accepting chemotaxis protein I; Provisional


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 370.82  E-value: 1.02e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73537566  146 LEKEFVpagdAYLAEIQKLLDIqrtsidaTAAEINTIYVNArnSLILLGVLVLAIGVGFAVWL--TRGIIRPLGHAVDIA 223
Cdd:PRK15041 163 FEKQYV----AYMEQNDRLYDI-------AVSDNNASYSQA--MWILVGVMIVVLAVIFAVWFgiKASLVAPMNRLIDSI 229
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73537566  224 RTVASGDLTSDIRVDSQDETGQLLHALSEMNTNILHIVRDVRTGTEAIASGTSQIAVGNTDLSQRTEEQASSLQQTAASM 303
Cdd:PRK15041 230 RHIAGGDLVKPIEVDGSNEMGQLAESLRHMQGELMRTVGDVRNGANAIYSGASEIATGNNDLSSRTEQQAASLEETAASM 309
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73537566  304 EELTSIVRQNADNAKQASALAVNASEIAAKGGDVADKVAETMEEINGASKKVVDIIAVIEGIAFQTNILALNAAVEAARA 383
Cdd:PRK15041 310 EQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQTMRDISTSSQKIADIISVIDGIAFQTNILALNAAVEAARA 389
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73537566  384 GEQGRGFAVVAGEVRSLAQRSATAAKEIKALIGDSVDRVEKGSTLVAQSGQTMLEIVEAVRRVTDIMGEISAASAEQSAG 463
Cdd:PRK15041 390 GEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLVESAGETMAEIVSAVTRVTDIMGEIASASDEQSRG 469
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 73537566  464 IEQVNQAVTQMDSVTQQNAALVEEAAAAAGSLEEQAQRLKQAVATFRI 511
Cdd:PRK15041 470 IDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAVFRI 517
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
263-510 7.13e-63

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: 207.91  E-value: 7.13e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73537566    263 DVRTGTEAIASGTSQIAVGNTDLSQRTEEQASSLQQTAASMEELTSIVRQNADNAKQASALAVNASEIAAKGGDVADKVA 342
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73537566    343 ETMEEINGASKKVVDIIAVIEGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRSLAQRSATAAKEIKALIGD----- 417
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEiqeet 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73537566    418 ---------SVDRVEKGSTLVAQSGQTMLEIVEAVRRVTDIMGEISAASAEQSAGIEQVNQAVTQMDSVTQQNAALVEEA 488
Cdd:smart00283 161 neavaameeSSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240
                          250       260
                   ....*....|....*....|..
gi 73537566    489 AAAAGSLEEQAQRLKQAVATFR 510
Cdd:smart00283 241 SAAAEELSGLAEELDELVERFK 262
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
319-511 6.99e-57

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: 190.35  E-value: 6.99e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73537566   319 QASALAVNASEIAA----KGGDVADKVAETMEEINGASKKVVDIIAVIEGIAFQTNILALNAAVEAARAGEQGRGFAVVA 394
Cdd:pfam00015   2 QASDLAQLASEEALdemsQIGQVVDDAVETMEELETSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73537566   395 GEVRSLAQRSATAAKEIKALIGDSV--------------DRVEKGSTLVAQSGQTMLEIVEAVRRVTDIMGEISAASAEQ 460
Cdd:pfam00015  82 DEVRKLAERSAQAAKEIEALIEEIVkqtndstasiqqtrTEVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDEQ 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 73537566   461 SAGIEQVNQAVTQMDSVTQQNAALVEEAAAAAGSLEEQAQRLKQAVATFRI 511
Cdd:pfam00015 162 SAGIDQVNQAVARIDQVTQQNAALVEESAAAAETLEEQAEELTASVAQFRI 212
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
160-329 4.79e-04

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: 41.69  E-value: 4.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73537566   160 EIQKLLDIQRTSIDATAAEINTIYVNARNSLILLGVLVLAIgVGFAVW--LTRGIIRPLGHAVDIARTVASGDLTSDIRV 237
Cdd:TIGR02956 303 TVSQLVNAQNQRTEAAVSDLLMTLSVAQFGLLITGMLGLVI-LVFIMWrvVYRSVILRLNQHTQALLRLALGDLDISLDA 381
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73537566   238 DSQDETGQLLHALSemntnilhIVRDVRTGTEAIASGTSQIAvgnTDLSQRTEEQASSLQQTAASMEELTSIVRQNADNA 317
Cdd:TIGR02956 382 RGDDELAHMGRAIE--------AFRDTAAHNLKLQADERQVA---QELQEHKESLEQLVAQRTQELAETNERLNAEVKNH 450
                         170
                  ....*....|..
gi 73537566   318 KQASALAVNASE 329
Cdd:TIGR02956 451 AKARAEAEEANR 462
 
Name Accession Description Interval E-value
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
290-481 2.59e-50

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: 172.42  E-value: 2.59e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73537566 290 EEQASSLQQTAASMEELTSIVRQNADNAKQASALAVNASEIAAKGGDVADKVAETMEEINGASKKVVDIIAVIEGIAFQT 369
Cdd:cd11386   1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73537566 370 NILALNAAVEAARAGEQGRGFAVVAGEVRSLAQRSATAAKEIKALIGDSVDRVEKGSTLVAQSGQTMLEIVEAVRRVTDI 449
Cdd:cd11386  81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160
                       170       180       190
                ....*....|....*....|....*....|..
gi 73537566 450 MGEISAASAEQSAGIEQVNQAVTQMDSVTQQN 481
Cdd:cd11386 161 FEEIVASVEEVADGIQEISAATQEQSASTQEI 192
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
212-257 4.38e-05

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: 41.47  E-value: 4.38e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 73537566 212 IIRPLGHAVDIARTVASGDLTSDIRVDSQDETGQLLHALSEMNTNI 257
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGDLDVRLPVTGRDEIGELARAFNQMAERL 46
4HB_MCP_1 pfam12729
Four helix bundle sensory module for signal transduction; This family is a four helix bundle ...
3-183 8.09e-13

Four helix bundle sensory module for signal transduction; This family is a four helix bundle that operates as a ubiquitous sensory module in prokaryotic signal-transduction. The 4HB_MCP is always found between two predicted transmembrane helices indicating that it detects only extracellular signals. In many cases the domain is associated with a cytoplasmic HAMP domain suggesting that most proteins carrying the bundle might share the mechanism of transmembrane signalling which is well-characterized in E coli chemoreceptors.


Pssm-ID: 193205  Cd Length: 181  Bit Score: 66.09  E-value: 8.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73537566     3 NFGIGVRLGIGFGVVLVLCALMSAFGIMRLQQVAERTHDMMQqpltkERLVS-DWYRLMHTSVRRTTAVAK----SADPS 77
Cdd:pfam12729   1 NLKIRTKLILLFLLLALLLIIVGIVGLYSLKKINKNSETMYE-----DRLLPiKWLGEIRSNLREIRANLLelilTTDPA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73537566    78 LGAFFAKETKASLEGIAALRDKMQPMLTSEAEKAAFAKILQVREPYNASRDKITKLKQEGLTEEANAVLEKEFVPAGDAY 157
Cdd:pfam12729  76 ERDELLKDIEELRAEIDKLLKKYEKTILTEEEKKLFNEFKEQLKAYRKVRNKVLDLAKAGKNDEAYALYLTELEPARDAV 155
                         170       180
                  ....*....|....*....|....*.
gi 73537566   158 LAEIQKLLDIQRTSIDATAAEINTIY 183
Cdd:pfam12729 156 IEALDELIDYNLKVAKEAYEDNKASY 181
HAMP pfam00672
HAMP domain;
190-253 5.53e-08

HAMP domain;


Pssm-ID: 250044  Cd Length: 70  Bit Score: 50.31  E-value: 5.53e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 73537566   190 LILLGVLVLAIGVGFAVWLTRGIIRPLGHAVDIARTVASGDLTSDIRVDSQDETGQLLHALSEM 253
Cdd:pfam00672   1 LLLVLLIALLLLLLLAWLLARRLLRPLRRLAEAARRIASGDLDDRVPVSGPDEIGELARAFNQM 64
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
210-262 3.51e-05

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


Pssm-ID: 197640  Cd Length: 53  Bit Score: 41.46  E-value: 3.51e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 73537566    210 RGIIRPLGHAVDIARTVASGDLTSDIRVDSQDETGQLLHALSEMNTNILHIVR 262
Cdd:smart00304   1 RRLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRLEETIA 53
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction ...
150-511 6.72e-70

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


Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 231.42  E-value: 6.72e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73537566 150 FVPAGDAYLAEIQKLLDIQRTSIDATAAEINTIYVNARNSLILLGVLVLAIGVGFAVWLTRGIIRPLGHAVDIARTVASG 229
Cdd:COG0840  22 GLLKLKKLIDELGKLLLSLNLILDDAASAEAAALKAVLKFLLISLLVAIIVVLVLAILLLRAILEPISDLLEVVERIAAG 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73537566 230 DLTSDIRVDSQDETGQLLHALSEMNTNILHIVRDVRTGTEAIASGTSQIAVGNTDLSQRTEEQASSLQQTAASMEELTSI 309
Cdd:COG0840 102 DLTKRIDESSNDEFGQLAKSFNEMILNLRQIIDAVQDNAEALSGASEEIAASATELSARADQQAESLEEVASAIEELSET 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73537566 310 VRQNADNAKQASALAVNASEIAAKGGDVADKVAETMEEINGA-----------SKKVVDIIAVIEGIAFQTNILALNAAV 378
Cdd:COG0840 182 VKEVAFNAKEAAALASEASQVAEEGGEEVRQAVEQMQEIAEElaevvkklsesSQEIEEITSVINSIAEQTNLLALNAAI 261
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73537566 379 EAARAGEQGRGFAVVAGEVRSLAQRSATAAKEIKALIGD--------------SVDRVEKGSTLVAQSGQTMLEIVEAVR 444
Cdd:COG0840 262 EAARAGEAGRGFAVVADEVRKLAERSADSAKEIGLLIEEiqneaadavehmeeSASEVSEGVKLVEETGSSLGEIAAAIE 341
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 73537566 445 RVTDIMGEISAASAEQSAGIEQVNQAVTQMDSVTQQNAALVEEAAAAAGSLEEQAQRLKQAVATFRI 511
Cdd:COG0840 342 EVSQLISEIAAATEEQTAVLEEINASIEELDDVTQENAAAVEELAAASEELKELAEKLLELVAKFKL 408
PRK15041 PRK15041
methyl-accepting chemotaxis protein I; Provisional
146-511 1.02e-121

methyl-accepting chemotaxis protein I; Provisional


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 370.82  E-value: 1.02e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73537566  146 LEKEFVpagdAYLAEIQKLLDIqrtsidaTAAEINTIYVNArnSLILLGVLVLAIGVGFAVWL--TRGIIRPLGHAVDIA 223
Cdd:PRK15041 163 FEKQYV----AYMEQNDRLYDI-------AVSDNNASYSQA--MWILVGVMIVVLAVIFAVWFgiKASLVAPMNRLIDSI 229
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73537566  224 RTVASGDLTSDIRVDSQDETGQLLHALSEMNTNILHIVRDVRTGTEAIASGTSQIAVGNTDLSQRTEEQASSLQQTAASM 303
Cdd:PRK15041 230 RHIAGGDLVKPIEVDGSNEMGQLAESLRHMQGELMRTVGDVRNGANAIYSGASEIATGNNDLSSRTEQQAASLEETAASM 309
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73537566  304 EELTSIVRQNADNAKQASALAVNASEIAAKGGDVADKVAETMEEINGASKKVVDIIAVIEGIAFQTNILALNAAVEAARA 383
Cdd:PRK15041 310 EQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQTMRDISTSSQKIADIISVIDGIAFQTNILALNAAVEAARA 389
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73537566  384 GEQGRGFAVVAGEVRSLAQRSATAAKEIKALIGDSVDRVEKGSTLVAQSGQTMLEIVEAVRRVTDIMGEISAASAEQSAG 463
Cdd:PRK15041 390 GEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLVESAGETMAEIVSAVTRVTDIMGEIASASDEQSRG 469
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 73537566  464 IEQVNQAVTQMDSVTQQNAALVEEAAAAAGSLEEQAQRLKQAVATFRI 511
Cdd:PRK15041 470 IDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAVFRI 517
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
166-513 1.89e-117

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 359.70  E-value: 1.89e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73537566  166 DIQRTSIDATAAEintiYVNARNSLILLGVLVLAIGVGFAVWLTRGIIRPLGHAVDIARTVASGDLTSDIRVDSQDETGQ 245
Cdd:PRK15048 174 KLYRDIVTDNADD----YRFAQWQLAVIALVVVLILLVAWYGIRRMLLTPLAKIIAHIREIAGGNLANTLTIDGRSEMGD 249
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73537566  246 LLHALSEMNTNILHIVRDVRTGTEAIASGTSQIAVGNTDLSQRTEEQASSLQQTAASMEELTSIVRQNADNAKQASALAV 325
Cdd:PRK15048 250 LAQSVSHMQRSLTDTVTHVREGSDAIYAGTREIAAGNTDLSSRTEQQASALEETAASMEQLTATVKQNADNARQASQLAQ 329
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73537566  326 NASEIAAKGGDVADKVAETMEEINGASKKVVDIIAVIEGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRSLAQRSA 405
Cdd:PRK15048 330 SASDTAQHGGKVVDGVVKTMHEIADSSKKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSA 409
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73537566  406 TAAKEIKALIGDSVDRVEKGSTLVAQSGQTMLEIVEAVRRVTDIMGEISAASAEQSAGIEQVNQAVTQMDSVTQQNAALV 485
Cdd:PRK15048 410 QAAKEIKALIEDSVSRVDTGSVLVESAGETMNNIVNAVTRVTDIMGEIASASDEQSRGIDQVALAVSEMDRVTQQNASLV 489
                        330       340
                 ....*....|....*....|....*...
gi 73537566  486 EEAAAAAGSLEEQAQRLKQAVATFRIAA 513
Cdd:PRK15048 490 QESAAAAAALEEQASRLTQAVSAFRLAA 517
PRK09793 PRK09793
methyl-accepting protein IV; Provisional
195-511 3.49e-100

methyl-accepting protein IV; Provisional


Pssm-ID: 182079 [Multi-domain]  Cd Length: 533  Bit Score: 314.32  E-value: 3.49e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73537566  195 VLVLAIGVGFAVWLTRG-IIRPLGHAVDIARTVASGDLTSDIRVDSQDETGQLLHALSEMNTNILHIVRDVRTGTEAIAS 273
Cdd:PRK09793 196 IIVAAIYISSALWWTRKmIVQPLAIIGSHFDSIAAGNLARPIAVYGRNEITAIFASLKTMQQALRGTVSDVRKGSQEMHI 275
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73537566  274 GTSQIAVGNTDLSQRTEEQASSLQQTAASMEELTSIVRQNADNAKQASALAVNASEIAAKGGDVADKVAETMEEINGASK 353
Cdd:PRK09793 276 GIAEIVAGNNDLSSRTEQQAASLAQTAASMEQLTATVGQNADNARQASELAKNAATTAQAGGVQVSTMTHTMQEIATSSQ 355
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73537566  354 KVVDIIAVIEGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRSLAQRSATAAKEIKALIGDSVDRVEKGSTLVAQSG 433
Cdd:PRK09793 356 KIGDIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKGLIEESVNRVQQGSKLVNNAA 435
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 73537566  434 QTMLEIVEAVRRVTDIMGEISAASAEQSAGIEQVNQAVTQMDSVTQQNAALVEEAAAAAGSLEEQAQRLKQAVATFRI 511
Cdd:PRK09793 436 ATMTDIVSSVTRVNDIMGEIASASEEQRRGIEQVAQAVSQMDQVTQQNASLVEEAAVATEQLANQADHLSSRVAVFTL 513
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
263-510 7.13e-63

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: 207.91  E-value: 7.13e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73537566    263 DVRTGTEAIASGTSQIAVGNTDLSQRTEEQASSLQQTAASMEELTSIVRQNADNAKQASALAVNASEIAAKGGDVADKVA 342
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73537566    343 ETMEEINGASKKVVDIIAVIEGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRSLAQRSATAAKEIKALIGD----- 417
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEiqeet 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73537566    418 ---------SVDRVEKGSTLVAQSGQTMLEIVEAVRRVTDIMGEISAASAEQSAGIEQVNQAVTQMDSVTQQNAALVEEA 488
Cdd:smart00283 161 neavaameeSSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240
                          250       260
                   ....*....|....*....|..
gi 73537566    489 AAAAGSLEEQAQRLKQAVATFR 510
Cdd:smart00283 241 SAAAEELSGLAEELDELVERFK 262
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
319-511 6.99e-57

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: 190.35  E-value: 6.99e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73537566   319 QASALAVNASEIAA----KGGDVADKVAETMEEINGASKKVVDIIAVIEGIAFQTNILALNAAVEAARAGEQGRGFAVVA 394
Cdd:pfam00015   2 QASDLAQLASEEALdemsQIGQVVDDAVETMEELETSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73537566   395 GEVRSLAQRSATAAKEIKALIGDSV--------------DRVEKGSTLVAQSGQTMLEIVEAVRRVTDIMGEISAASAEQ 460
Cdd:pfam00015  82 DEVRKLAERSAQAAKEIEALIEEIVkqtndstasiqqtrTEVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDEQ 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 73537566   461 SAGIEQVNQAVTQMDSVTQQNAALVEEAAAAAGSLEEQAQRLKQAVATFRI 511
Cdd:pfam00015 162 SAGIDQVNQAVARIDQVTQQNAALVEESAAAAETLEEQAEELTASVAQFRI 212
NarQ COG3850
Signal transduction histidine kinase, nitrate/nitrite-specific [Signal transduction mechanisms]
93-312 8.71e-06

Signal transduction histidine kinase, nitrate/nitrite-specific [Signal transduction mechanisms]


Pssm-ID: 226368 [Multi-domain]  Cd Length: 574  Bit Score: 46.96  E-value: 8.71e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73537566  93 IAALRDKMQPMLTSEAEKAAfakiLQVREPyNASRDKITKLKQEgLTEEANAVLEKEFVPAGDAYLAEIQKLLDIQRTSI 172
Cdd:COG3850  65 LDAHVALFQTSLHSPALRAL----LPWRVP-LAVKTQYQQLIAY-WRNMLKPLLLQGDRRPYQADLADFVAQIDQFVLAL 138
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73537566 173 DATAaEINTIYVNARNSLILLGVLVLAIGVGFavWLTRGIIRPLGHAVDIARTVASGDLTSDIRVDSQDETGQLLHALSE 252
Cdd:COG3850 139 QRFA-ERKTILLVLVQLAGMLLILLLVVFTIY--WLRRRVVRPLNQLTSAAQRIGRRQFDQRPTDTGRNELGLLGRAFNQ 215
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 73537566 253 MNTNiLHIVRDvrtgteaiasgtsqiavgntDLSQRTEEQASSLQQTAASMEELTSIVRQ 312
Cdd:COG3850 216 MSGE-LKKLYA--------------------DLEQRVEEKTRDLEQKNQRLSFLYQSSRR 254
PRK10600 PRK10600
nitrate/nitrite sensor protein NarX; Provisional
189-298 6.96e-05

nitrate/nitrite sensor protein NarX; Provisional


Pssm-ID: 182581 [Multi-domain]  Cd Length: 569  Bit Score: 43.89  E-value: 6.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73537566  189 SLILLGVLVLAIgvgfaVWLTRGIIRPLGHAVDIARTVASGDLTSDIRVDSQDETGQLLHALSEMNTnilhivrdvrtgt 268
Cdd:PRK10600 131 AVFMALLLVFTI-----IWLRRRLLQPWRQLLSMANAVSHRDFTQRANISGRDEMAMLGTALNNMSA------------- 192
                         90       100       110
                 ....*....|....*....|....*....|
gi 73537566  269 eaiasgtsQIAVGNTDLSQRTEEQASSLQQ 298
Cdd:PRK10600 193 --------ELAESYAVLEQRVQEKTAGLEQ 214
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
240-343 1.50e-04

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


Pssm-ID: 214599 [Multi-domain]  Cd Length: 262  Bit Score: 42.27  E-value: 1.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73537566    240 QDETGQLLHALSEMNTNILHIVRDVRTGTEA---IASGTSQIAVGNTDLSQRTEEQASSLQQTAASMEELTSIVRQNADN 316
Cdd:smart00283 157 QEETNEAVAAMEESSSEVEEGVELVEETGDAleeIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAM 236
                           90       100
                   ....*....|....*....|....*..
gi 73537566    317 AKQASAlavNASEIAAKGGDVADKVAE 343
Cdd:smart00283 237 SEEISA---AAEELSGLAEELDELVER 260
NtrY COG5000
Signal transduction histidine kinase involved in nitrogen fixation and metabolism regulation ...
189-412 4.75e-04

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


Pssm-ID: 227333 [Multi-domain]  Cd Length: 712  Bit Score: 41.29  E-value: 4.75e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73537566 189 SLILLGVLVLAIGVGFAVWLTRGIIRPLGHAVDIARTVASGDLTSDIRVDSQDE-TGQLLHALSEMntnilhivrdvrtg 267
Cdd:COG5000 282 LYLSTALLVLLAAIWTAIAFARRIVRPIRKLIEAADEVADGDLDVQVPVRRVDEdVGRLSKAFNKM-------------- 347
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73537566 268 TEAIASGTSQIAVGNTDLSQRTEEQASSLQQTAASMEELTSIVRQNADNAKQASALAVNASE-IAAKGGDVADKVAETME 346
Cdd:COG5000 348 TEQLSSQQEALERAKDALEQRRRFLEAVLSGLTAGVIGFDNRGCITTVNPSAEQILGKPFDQlLGQSLSAIAPELEEVFA 427
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 73537566 347 EINGASKKVVDiiaVIEGIAFQTNILALNaaVEAAR-AGEQGRGFAVVAGEVRSL--AQRSAT-------AAKEIK 412
Cdd:COG5000 428 EAGAAARTDKR---VEVKLAREGEERTLN--VQATRePEDNGNGYVVTFDDITDLviAQRSAAwgdvarrIAHEIK 498
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
160-329 4.79e-04

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: 41.69  E-value: 4.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73537566   160 EIQKLLDIQRTSIDATAAEINTIYVNARNSLILLGVLVLAIgVGFAVW--LTRGIIRPLGHAVDIARTVASGDLTSDIRV 237
Cdd:TIGR02956 303 TVSQLVNAQNQRTEAAVSDLLMTLSVAQFGLLITGMLGLVI-LVFIMWrvVYRSVILRLNQHTQALLRLALGDLDISLDA 381
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73537566   238 DSQDETGQLLHALSemntnilhIVRDVRTGTEAIASGTSQIAvgnTDLSQRTEEQASSLQQTAASMEELTSIVRQNADNA 317
Cdd:TIGR02956 382 RGDDELAHMGRAIE--------AFRDTAAHNLKLQADERQVA---QELQEHKESLEQLVAQRTQELAETNERLNAEVKNH 450
                         170
                  ....*....|..
gi 73537566   318 KQASALAVNASE 329
Cdd:TIGR02956 451 AKARAEAEEANR 462
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH