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Conserved domains on  [gi|91788330|ref|YP_549282|]
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methyl-accepting chemotaxis sensory transducer [Polaromonas sp. JS666]

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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. ...
197-244 5.00e-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: 49.94  E-value: 5.00e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 91788330 197 VTRPLEKLREGIAIVGAGNLDHRLAITAKDEIGSLSRAFDEMTEKLKA 244
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGDLDVRLPVTGRDEIGELARAFNQMAERLRE 48
MCP_signal super family cl21547
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
325-519 2.58e-38

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: 206779  Cd Length: 200  Bit Score: 139.68  E-value: 2.58e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91788330 325 TAQVASQKARLVSDSAQKAAQSSQNGRKSTEDVGAGMTRIRQQMEAIAASMTRLSEQSRAIGRIMASVEDLAAQSNLLAV 404
Cdd:cd11386   6 SIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQTNLLAL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91788330 405 NAAIEAARAGEHGKGFGVVAQEVKSLAEQSRQATTQVRTILGDIQKATIAAVLATEQGSKAVEAGSRQTEVAGESIQALA 484
Cdd:cd11386  86 NAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRAFEEIV 165
                       170       180       190
                ....*....|....*....|....*....|....*
gi 91788330 485 GSVTEAVQAATQIAASSQQQLAGVDQVAGAMESIR 519
Cdd:cd11386 166 ASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction ...
143-555 1.38e-39

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


:

Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 148.60  E-value: 1.38e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91788330 143 MNKAQAMISGALSLSDRSRTGVLDAQQRTSAAVVTFGGVVVFVIAATLFLALGSVTRPLEKLREGIAIVGAGNLDHRLAI 222
Cdd:COG0840  30 IDELGKLLLSLNLILDDAASAEAAALKAVLKFLLISLLVAIIVVLVLAILLLRAILEPISDLLEVVERIAAGDLTKRIDE 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91788330 223 TAKDEIGSLSRAFDEMTEKLKATtvsrdelgqgnavlqaevaerkrveenlrllMQETQEIVNVLSSFSSEIVASTTQLA 302
Cdd:COG0840 110 SSNDEFGQLAKSFNEMILNLRQI-------------------------------IDAVQDNAEALSGASEEIAASATELS 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91788330 303 ASASQSAAAVTETTTTVEEVRQTAQVASQKARLVSDSAQKAAQSSQNGRKSTEDVGAGMTRIRqqmEAIAASMTRLSEQS 382
Cdd:COG0840 159 ARADQQAESLEEVASAIEELSETVKEVAFNAKEAAALASEASQVAEEGGEEVRQAVEQMQEIA---EELAEVVKKLSESS 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91788330 383 RAIGRIMASVEDLAAQSNLLAVNAAIEAARAGEHGKGFGVVAQEVKSLAEQSRQATTQVRTILGDIQKATIAAVLATEQG 462
Cdd:COG0840 236 QEIEEITSVINSIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSADSAKEIGLLIEEIQNEAADAVEHMEES 315
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91788330 463 SKAVEAGSRQTEVAGESIQALAGSVTEAVQAATQIAASSQQQLAGVDQVAGAMESIRQASTQNVASARQLEVAARNLDEL 542
Cdd:COG0840 316 ASEVSEGVKLVEETGSSLGEIAAAIEEVSQLISEIAAATEEQTAVLEEINASIEELDDVTQENAAAVEELAAASEELKEL 395
                       410
                ....*....|...
gi 91788330 543 GQRLKQMAERYKV 555
Cdd:COG0840 396 AEKLLELVAKFKL 408
 
Name Accession Description Interval E-value
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
197-244 5.00e-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: 49.94  E-value: 5.00e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 91788330 197 VTRPLEKLREGIAIVGAGNLDHRLAITAKDEIGSLSRAFDEMTEKLKA 244
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGDLDVRLPVTGRDEIGELARAFNQMAERLRE 48
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
325-519 2.58e-38

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: 139.68  E-value: 2.58e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91788330 325 TAQVASQKARLVSDSAQKAAQSSQNGRKSTEDVGAGMTRIRQQMEAIAASMTRLSEQSRAIGRIMASVEDLAAQSNLLAV 404
Cdd:cd11386   6 SIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQTNLLAL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91788330 405 NAAIEAARAGEHGKGFGVVAQEVKSLAEQSRQATTQVRTILGDIQKATIAAVLATEQGSKAVEAGSRQTEVAGESIQALA 484
Cdd:cd11386  86 NAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRAFEEIV 165
                       170       180       190
                ....*....|....*....|....*....|....*
gi 91788330 485 GSVTEAVQAATQIAASSQQQLAGVDQVAGAMESIR 519
Cdd:cd11386 166 ASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
196-245 1.31e-07

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


Pssm-ID: 197640  Cd Length: 53  Bit Score: 48.78  E-value: 1.31e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 91788330    196 SVTRPLEKLREGIAIVGAGNLDHRLAITAKDEIGSLSRAFDEMTEKLKAT 245
Cdd:smart00304   2 RLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRLEET 51
HAMP pfam00672
HAMP domain;
186-244 2.29e-07

HAMP domain;


Pssm-ID: 250044  Cd Length: 70  Bit Score: 48.38  E-value: 2.29e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 91788330   186 IAATLFLALGSVTRPLEKLREGIAIVGAGNLDHRLAITAKDEIGSLSRAFDEMTEKLKA 244
Cdd:pfam00672  12 LLLLAWLLARRLLRPLRRLAEAARRIASGDLDDRVPVSGPDEIGELARAFNQMADRLRE 70
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction ...
143-555 1.38e-39

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


Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 148.60  E-value: 1.38e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91788330 143 MNKAQAMISGALSLSDRSRTGVLDAQQRTSAAVVTFGGVVVFVIAATLFLALGSVTRPLEKLREGIAIVGAGNLDHRLAI 222
Cdd:COG0840  30 IDELGKLLLSLNLILDDAASAEAAALKAVLKFLLISLLVAIIVVLVLAILLLRAILEPISDLLEVVERIAAGDLTKRIDE 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91788330 223 TAKDEIGSLSRAFDEMTEKLKATtvsrdelgqgnavlqaevaerkrveenlrllMQETQEIVNVLSSFSSEIVASTTQLA 302
Cdd:COG0840 110 SSNDEFGQLAKSFNEMILNLRQI-------------------------------IDAVQDNAEALSGASEEIAASATELS 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91788330 303 ASASQSAAAVTETTTTVEEVRQTAQVASQKARLVSDSAQKAAQSSQNGRKSTEDVGAGMTRIRqqmEAIAASMTRLSEQS 382
Cdd:COG0840 159 ARADQQAESLEEVASAIEELSETVKEVAFNAKEAAALASEASQVAEEGGEEVRQAVEQMQEIA---EELAEVVKKLSESS 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91788330 383 RAIGRIMASVEDLAAQSNLLAVNAAIEAARAGEHGKGFGVVAQEVKSLAEQSRQATTQVRTILGDIQKATIAAVLATEQG 462
Cdd:COG0840 236 QEIEEITSVINSIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSADSAKEIGLLIEEIQNEAADAVEHMEES 315
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91788330 463 SKAVEAGSRQTEVAGESIQALAGSVTEAVQAATQIAASSQQQLAGVDQVAGAMESIRQASTQNVASARQLEVAARNLDEL 542
Cdd:COG0840 316 ASEVSEGVKLVEETGSSLGEIAAAIEEVSQLISEIAAATEEQTAVLEEINASIEELDDVTQENAAAVEELAAASEELKEL 395
                       410
                ....*....|...
gi 91788330 543 GQRLKQMAERYKV 555
Cdd:COG0840 396 AEKLLELVAKFKL 408
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
336-554 4.63e-41

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: 149.36  E-value: 4.63e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91788330    336 VSDSAQKAAQSSQNGRKSTEDVGAGMTRIRQQMEAIAASMTRLSEQSRAIGRIMASVEDLAAQSNLLAVNAAIEAARAGE 415
Cdd:smart00283  44 IAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAVSAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGE 123
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91788330    416 HGKGFGVVAQEVKSLAEQSRQATTQVRTILGDIQKATIAAVLATEQGSKAVEAGSRQTEVAGESIQALAGSVTEAVQAAT 495
Cdd:smart00283 124 AGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEETNEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQ 203
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 91788330    496 QIAASSQQQLAGVDQVAGAMESIRQASTQNVASARQLEVAARNLDELGQRLKQMAERYK 554
Cdd:smart00283 204 EIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEISAAAEELSGLAEELDELVERFK 262
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
344-555 3.12e-35

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: 131.41  E-value: 3.12e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91788330   344 AQSSQNGRKSTEDVGAGMTRIRQQMEAIAASMTRLSEQSRAIGRIMASVEDLAAQSNLLAVNAAIEAARAGEHGKGFGVV 423
Cdd:pfam00015   1 AQASDLAQLASEEALDEMSQIGQVVDDAVETMEELETSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91788330   424 AQEVKSLAEQSRQATTQVRTILGDIQKATIAAVLATEQGSKAVEAGSRQTEVAGESIQALAGSVTEAVQAATQIAASSQQ 503
Cdd:pfam00015  81 ADEVRKLAERSAQAAKEIEALIEEIVKQTNDSTASIQQTRTEVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDE 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 91788330   504 QLAGVDQVAGAMESIRQASTQNVASARQLEVAARNLDELGQRLKQMAERYKV 555
Cdd:pfam00015 161 QSAGIDQVNQAVARIDQVTQQNAALVEESAAAAETLEEQAEELTASVAQFRI 212
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
200-555 2.68e-27

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 114.72  E-value: 2.68e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91788330  200 PLEKLREGIAIVGAGNLDHRLAITAKDEIGSLSRAFDEMTEKLKATtvsrdelgqgnavlqaevaerkrveenlrllMQE 279
Cdd:PRK15048 219 PLAKIIAHIREIAGGNLANTLTIDGRSEMGDLAQSVSHMQRSLTDT-------------------------------VTH 267
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91788330  280 TQEIVNVLSSFSSEIVASTTQLAASASQSAAAVTETTTTVEEVRQTAQVASQKARLVSDSAQKAAQSSQNGRKSTEDVga 359
Cdd:PRK15048 268 VREGSDAIYAGTREIAAGNTDLSSRTEQQASALEETAASMEQLTATVKQNADNARQASQLAQSASDTAQHGGKVVDGV-- 345
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91788330  360 gmtrirqqmeaiAASMTRLSEQSRAIGRIMASVEDLAAQSNLLAVNAAIEAARAGEHGKGFGVVAQEVKSLAEQSRQATT 439
Cdd:PRK15048 346 ------------VKTMHEIADSSKKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAK 413
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91788330  440 QVRTILGDiqkatiaavlateqGSKAVEAGSRQTEVAGESIQALAGSVTEAVQAATQIAASSQQQLAGVDQVAGAMESIR 519
Cdd:PRK15048 414 EIKALIED--------------SVSRVDTGSVLVESAGETMNNIVNAVTRVTDIMGEIASASDEQSRGIDQVALAVSEMD 479
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 91788330  520 QASTQNVASARQLEVAARNLDELGQRLKQMAERYKV 555
Cdd:PRK15048 480 RVTQQNASLVQESAAAAAALEEQASRLTQAVSAFRL 515
 
Name Accession Description Interval E-value
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
197-244 5.00e-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: 49.94  E-value: 5.00e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 91788330 197 VTRPLEKLREGIAIVGAGNLDHRLAITAKDEIGSLSRAFDEMTEKLKA 244
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGDLDVRLPVTGRDEIGELARAFNQMAERLRE 48
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
325-519 2.58e-38

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: 139.68  E-value: 2.58e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91788330 325 TAQVASQKARLVSDSAQKAAQSSQNGRKSTEDVGAGMTRIRQQMEAIAASMTRLSEQSRAIGRIMASVEDLAAQSNLLAV 404
Cdd:cd11386   6 SIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQTNLLAL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91788330 405 NAAIEAARAGEHGKGFGVVAQEVKSLAEQSRQATTQVRTILGDIQKATIAAVLATEQGSKAVEAGSRQTEVAGESIQALA 484
Cdd:cd11386  86 NAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRAFEEIV 165
                       170       180       190
                ....*....|....*....|....*....|....*
gi 91788330 485 GSVTEAVQAATQIAASSQQQLAGVDQVAGAMESIR 519
Cdd:cd11386 166 ASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
196-245 1.31e-07

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


Pssm-ID: 197640  Cd Length: 53  Bit Score: 48.78  E-value: 1.31e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 91788330    196 SVTRPLEKLREGIAIVGAGNLDHRLAITAKDEIGSLSRAFDEMTEKLKAT 245
Cdd:smart00304   2 RLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRLEET 51
HAMP pfam00672
HAMP domain;
186-244 2.29e-07

HAMP domain;


Pssm-ID: 250044  Cd Length: 70  Bit Score: 48.38  E-value: 2.29e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 91788330   186 IAATLFLALGSVTRPLEKLREGIAIVGAGNLDHRLAITAKDEIGSLSRAFDEMTEKLKA 244
Cdd:pfam00672  12 LLLLAWLLARRLLRPLRRLAEAARRIASGDLDDRVPVSGPDEIGELARAFNQMADRLRE 70
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction ...
143-555 1.38e-39

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


Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 148.60  E-value: 1.38e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91788330 143 MNKAQAMISGALSLSDRSRTGVLDAQQRTSAAVVTFGGVVVFVIAATLFLALGSVTRPLEKLREGIAIVGAGNLDHRLAI 222
Cdd:COG0840  30 IDELGKLLLSLNLILDDAASAEAAALKAVLKFLLISLLVAIIVVLVLAILLLRAILEPISDLLEVVERIAAGDLTKRIDE 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91788330 223 TAKDEIGSLSRAFDEMTEKLKATtvsrdelgqgnavlqaevaerkrveenlrllMQETQEIVNVLSSFSSEIVASTTQLA 302
Cdd:COG0840 110 SSNDEFGQLAKSFNEMILNLRQI-------------------------------IDAVQDNAEALSGASEEIAASATELS 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91788330 303 ASASQSAAAVTETTTTVEEVRQTAQVASQKARLVSDSAQKAAQSSQNGRKSTEDVGAGMTRIRqqmEAIAASMTRLSEQS 382
Cdd:COG0840 159 ARADQQAESLEEVASAIEELSETVKEVAFNAKEAAALASEASQVAEEGGEEVRQAVEQMQEIA---EELAEVVKKLSESS 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91788330 383 RAIGRIMASVEDLAAQSNLLAVNAAIEAARAGEHGKGFGVVAQEVKSLAEQSRQATTQVRTILGDIQKATIAAVLATEQG 462
Cdd:COG0840 236 QEIEEITSVINSIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSADSAKEIGLLIEEIQNEAADAVEHMEES 315
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91788330 463 SKAVEAGSRQTEVAGESIQALAGSVTEAVQAATQIAASSQQQLAGVDQVAGAMESIRQASTQNVASARQLEVAARNLDEL 542
Cdd:COG0840 316 ASEVSEGVKLVEETGSSLGEIAAAIEEVSQLISEIAAATEEQTAVLEEINASIEELDDVTQENAAAVEELAAASEELKEL 395
                       410
                ....*....|...
gi 91788330 543 GQRLKQMAERYKV 555
Cdd:COG0840 396 AEKLLELVAKFKL 408
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
336-554 4.63e-41

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: 149.36  E-value: 4.63e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91788330    336 VSDSAQKAAQSSQNGRKSTEDVGAGMTRIRQQMEAIAASMTRLSEQSRAIGRIMASVEDLAAQSNLLAVNAAIEAARAGE 415
Cdd:smart00283  44 IAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAVSAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGE 123
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91788330    416 HGKGFGVVAQEVKSLAEQSRQATTQVRTILGDIQKATIAAVLATEQGSKAVEAGSRQTEVAGESIQALAGSVTEAVQAAT 495
Cdd:smart00283 124 AGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEETNEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQ 203
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 91788330    496 QIAASSQQQLAGVDQVAGAMESIRQASTQNVASARQLEVAARNLDELGQRLKQMAERYK 554
Cdd:smart00283 204 EIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEISAAAEELSGLAEELDELVERFK 262
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
344-555 3.12e-35

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: 131.41  E-value: 3.12e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91788330   344 AQSSQNGRKSTEDVGAGMTRIRQQMEAIAASMTRLSEQSRAIGRIMASVEDLAAQSNLLAVNAAIEAARAGEHGKGFGVV 423
Cdd:pfam00015   1 AQASDLAQLASEEALDEMSQIGQVVDDAVETMEELETSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91788330   424 AQEVKSLAEQSRQATTQVRTILGDIQKATIAAVLATEQGSKAVEAGSRQTEVAGESIQALAGSVTEAVQAATQIAASSQQ 503
Cdd:pfam00015  81 ADEVRKLAERSAQAAKEIEALIEEIVKQTNDSTASIQQTRTEVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDE 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 91788330   504 QLAGVDQVAGAMESIRQASTQNVASARQLEVAARNLDELGQRLKQMAERYKV 555
Cdd:pfam00015 161 QSAGIDQVNQAVARIDQVTQQNAALVEESAAAAETLEEQAEELTASVAQFRI 212
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
200-555 2.68e-27

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 114.72  E-value: 2.68e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91788330  200 PLEKLREGIAIVGAGNLDHRLAITAKDEIGSLSRAFDEMTEKLKATtvsrdelgqgnavlqaevaerkrveenlrllMQE 279
Cdd:PRK15048 219 PLAKIIAHIREIAGGNLANTLTIDGRSEMGDLAQSVSHMQRSLTDT-------------------------------VTH 267
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91788330  280 TQEIVNVLSSFSSEIVASTTQLAASASQSAAAVTETTTTVEEVRQTAQVASQKARLVSDSAQKAAQSSQNGRKSTEDVga 359
Cdd:PRK15048 268 VREGSDAIYAGTREIAAGNTDLSSRTEQQASALEETAASMEQLTATVKQNADNARQASQLAQSASDTAQHGGKVVDGV-- 345
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91788330  360 gmtrirqqmeaiAASMTRLSEQSRAIGRIMASVEDLAAQSNLLAVNAAIEAARAGEHGKGFGVVAQEVKSLAEQSRQATT 439
Cdd:PRK15048 346 ------------VKTMHEIADSSKKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAK 413
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91788330  440 QVRTILGDiqkatiaavlateqGSKAVEAGSRQTEVAGESIQALAGSVTEAVQAATQIAASSQQQLAGVDQVAGAMESIR 519
Cdd:PRK15048 414 EIKALIED--------------SVSRVDTGSVLVESAGETMNNIVNAVTRVTDIMGEIASASDEQSRGIDQVALAVSEMD 479
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 91788330  520 QASTQNVASARQLEVAARNLDELGQRLKQMAERYKV 555
Cdd:PRK15048 480 RVTQQNASLVQESAAAAAALEEQASRLTQAVSAFRL 515
PRK15041 PRK15041
methyl-accepting chemotaxis protein I; Provisional
186-555 5.45e-26

methyl-accepting chemotaxis protein I; Provisional


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 110.81  E-value: 5.45e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91788330  186 IAATLFLALGSVTRPLEKLREGIAIVGAGNLDHRLAITAKDEIGSLSRAFDEMTEKLKATtvsrdelgqgnavlqaevae 265
Cdd:PRK15041 207 IFAVWFGIKASLVAPMNRLIDSIRHIAGGDLVKPIEVDGSNEMGQLAESLRHMQGELMRT-------------------- 266
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91788330  266 rkrveenlrllMQETQEIVNVLSSFSSEIVASTTQLAASASQSAAAVTETTTTVEEVRQTAQVASQKARLVSDSAQKAAQ 345
Cdd:PRK15041 267 -----------VGDVRNGANAIYSGASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVKQNAENARQASHLALSASE 335
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91788330  346 SSQNGRKSTEDVgagmtriRQQMEAIAASmtrlseqSRAIGRIMASVEDLAAQSNLLAVNAAIEAARAGEHGKGFGVVAQ 425
Cdd:PRK15041 336 TAQRGGKVVDNV-------VQTMRDISTS-------SQKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAG 401
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91788330  426 EVKSLAEQSRQATTQVRTILgdiqkatiaavlatEQGSKAVEAGSRQTEVAGESIQALAGSVTEAVQAATQIAASSQQQL 505
Cdd:PRK15041 402 EVRNLAQRSAQAAREIKSLI--------------EDSVGKVDVGSTLVESAGETMAEIVSAVTRVTDIMGEIASASDEQS 467
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 91788330  506 AGVDQVAGAMESIRQASTQNVASARQLEVAARNLDELGQRLKQMAERYKV 555
Cdd:PRK15041 468 RGIDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAVFRI 517
PRK09793 PRK09793
methyl-accepting protein IV; Provisional
186-555 6.15e-23

methyl-accepting protein IV; Provisional


Pssm-ID: 182079 [Multi-domain]  Cd Length: 533  Bit Score: 101.30  E-value: 6.15e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91788330  186 IAATLFLALGSVTRPLEKLREGIAIVGAGNLDHRLAITAKDEIGSLSRAFDEMTEKLKATTvsrDELGQGNAVLQAEVae 265
Cdd:PRK09793 203 ISSALWWTRKMIVQPLAIIGSHFDSIAAGNLARPIAVYGRNEITAIFASLKTMQQALRGTV---SDVRKGSQEMHIGI-- 277
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91788330  266 rkrveenlrllmqetqeivnvlssfsSEIVASTTQLAASASQSAAAVTETTTTVEEVRQTAQVASQKARLVSDSAQKAAQ 345
Cdd:PRK09793 278 --------------------------AEIVAGNNDLSSRTEQQAASLAQTAASMEQLTATVGQNADNARQASELAKNAAT 331
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91788330  346 SSQNGrkstedvGAGMTRIRQQMEAIAASmtrlseqSRAIGRIMASVEDLAAQSNLLAVNAAIEAARAGEHGKGFGVVAQ 425
Cdd:PRK09793 332 TAQAG-------GVQVSTMTHTMQEIATS-------SQKIGDIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAG 397
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91788330  426 EVKSLAEQSRQATTQVRTILgdiqkatiaavlatEQGSKAVEAGSRQTEVAGESIQALAGSVTEAVQAATQIAASSQQQL 505
Cdd:PRK09793 398 EVRNLASRSAQAAKEIKGLI--------------EESVNRVQQGSKLVNNAAATMTDIVSSVTRVNDIMGEIASASEEQR 463
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 91788330  506 AGVDQVAGAMESIRQASTQNvasARQLEVAARNLDELGQRLKQMAERYKV 555
Cdd:PRK09793 464 RGIEQVAQAVSQMDQVTQQN---ASLVEEAAVATEQLANQADHLSSRVAV 510
NarQ COG3850
Signal transduction histidine kinase, nitrate/nitrite-specific [Signal transduction mechanisms]
187-283 1.43e-05

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


Pssm-ID: 226368 [Multi-domain]  Cd Length: 574  Bit Score: 46.19  E-value: 1.43e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91788330 187 AATLFLALGSVTRPLEKLREGIAIVGAGNLDHRLAITAKDEIGSLSRAFDEMTEklkattvsrdELGQGNAVLQAEVAER 266
Cdd:COG3850 165 VFTIYWLRRRVVRPLNQLTSAAQRIGRRQFDQRPTDTGRNELGLLGRAFNQMSG----------ELKKLYADLEQRVEEK 234
                        90       100
                ....*....|....*....|.
gi 91788330 267 KR----VEENLRLLMQETQEI 283
Cdd:COG3850 235 TRdleqKNQRLSFLYQSSRRL 255
NtrY COG5000
Signal transduction histidine kinase involved in nitrogen fixation and metabolism regulation ...
196-268 1.03e-03

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


Pssm-ID: 227333 [Multi-domain]  Cd Length: 712  Bit Score: 40.52  E-value: 1.03e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 91788330 196 SVTRPLEKLREGIAIVGAGNLDHRLAITAKDE-IGSLSRAFDEMTEKLKAttvsrdelgQGNAVLQAEVAERKR 268
Cdd:COG5000 304 RIVRPIRKLIEAADEVADGDLDVQVPVRRVDEdVGRLSKAFNKMTEQLSS---------QQEALERAKDALEQR 368
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.12
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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