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Conserved domains on  [gi|39996402|ref|NP_952353|]
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methyl-accepting chemotaxis sensory transducer, class 34H [Geobacter sulfurreducens PCA]

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
213-259 7.21e-07

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: 46.47  E-value: 7.21e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 39996402 213 ITRPLDKAVSVSNELAEGNLTVTIEATSKDETGQLLAAMHNMVEKLK 259
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGDLDVRLPVTGRDEIGELARAFNQMAERLR 47
MCP_signal super family cl21547
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
304-476 2.84e-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: 206779  Cd Length: 200  Bit Score: 150.85  E-value: 2.84e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996402 304 MEQMSSNIRQNADNATQTEKIALKSATDAREGGKAVAGTVSAM-------KEIASKISIIEEIARQTNLLALNAAIEAAR 376
Cdd:cd11386  14 ADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVeeleessAEIGEIVEVIDDIAEQTNLLALNAAIEAAR 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996402 377 AGEHGKGFAVVAAEVRKLAERSQKAAGEISEL-------SASSVQVAEEAGEMLTRIVPDIQRTAELVQEISAACKEQDT 449
Cdd:cd11386  94 AGEAGRGFAVVADEVRKLAEESAEAAKEIEELieeiqeqTEEAVEAMEETSEEVEEGVELVEETGRAFEEIVASVEEVAD 173
                       170       180
                ....*....|....*....|....*..
gi 39996402 450 GAEQINKAIQQLDQVIQQNASASEEMA 476
Cdd:cd11386 174 GIQEISAATQEQSASTQEIAAAVEEIA 200
Tar_Tsr_LBD super family cl00144
ligand binding domain of Tar- and Tsr-related chemoreceptors; E.coli Tar (taxis to aspartate ...
31-184 1.22e-11

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: 63.01  E-value: 1.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996402    31 INGMKEINSKLDRILKVNYGKIKNANEVSMVVGDLMGKINEIML-KDVNERPAIKQEIEKLRSDYRSALERLEQLEQTDQ 109
Cdd:pfam12729  27 LYSLKKINKNSETMYEDRLLPIKWLGEIRSNLREIRANLLELILtTDPAERDELLKDIEELRAEIDKLLKKYEKTILTEE 106
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 39996402   110 GKQLIAGAKSAIDNAKKANNDIIELSLAGKTDQALIVYNKEGAPLSQKIVTAFKNIVKYQEERMELRYAEALKAY 184
Cdd:pfam12729 107 EKKLFNEFKEQLKAYRKVRNKVLDLAKAGKNDEAYALYLTELEPARDAVIEALDELIDYNLKVAKEAYEDNKASY 181
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility, Signal transduction mechanisms];
161-498 5.45e-54

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


:

Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 189.82  E-value: 5.45e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996402 161 AFKNIVKYQEERMELRYAEALKAYGTSRAVALGVAFCAAIIGILISLFATRSITRPLDKAVSVSNELAEGNLTVTIEATS 240
Cdd:COG0840  32 ELGKLLLSLNLILDDAASAEAAALKAVLKFLLISLLVAIIVVLVLAILLLRAILEPISDLLEVVERIAAGDLTKRIDESS 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996402 241 KDETGQLLAAMHNMVEKLKGVVADVKSAADNVAAGSQELSSSSEEMSQGATEQAAAAEEASSSMEQMSSNIRQNADNATQ 320
Cdd:COG0840 112 NDEFGQLAKSFNEMILNLRQIIDAVQDNAEALSGASEEIAASATELSARADQQAESLEEVASAIEELSETVKEVAFNAKE 191
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996402 321 TEKIALKSATDAREGGKAVAGTVSAM------------------KEIASKISIIEEIARQTNLLALNAAIEAARAGEHGK 382
Cdd:COG0840 192 AAALASEASQVAEEGGEEVRQAVEQMqeiaeelaevvkklsessQEIEEITSVINSIAEQTNLLALNAAIEAARAGEAGR 271
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996402 383 GFAVVAAEVRKLAERSQKAAGEISEL---------------------SASSVQVAEEAGEMLTRIVPDIQRTAELVQEIS 441
Cdd:COG0840 272 GFAVVADEVRKLAERSADSAKEIGLLieeiqneaadavehmeesaseVSEGVKLVEETGSSLGEIAAAIEEVSQLISEIA 351
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 39996402 442 AACKEQDTGAEQINKAIQQLDQVIQQNASASEEMASTSEELASQAEQLQATISFFRT 498
Cdd:COG0840 352 AATEEQTAVLEEINASIEELDDVTQENAAAVEELAAASEELKELAEKLLELVAKFKL 408
 
Name Accession Description Interval E-value
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
213-259 7.21e-07

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: 46.47  E-value: 7.21e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 39996402 213 ITRPLDKAVSVSNELAEGNLTVTIEATSKDETGQLLAAMHNMVEKLK 259
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGDLDVRLPVTGRDEIGELARAFNQMAERLR 47
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
304-476 2.84e-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: 150.85  E-value: 2.84e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996402 304 MEQMSSNIRQNADNATQTEKIALKSATDAREGGKAVAGTVSAM-------KEIASKISIIEEIARQTNLLALNAAIEAAR 376
Cdd:cd11386  14 ADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVeeleessAEIGEIVEVIDDIAEQTNLLALNAAIEAAR 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996402 377 AGEHGKGFAVVAAEVRKLAERSQKAAGEISEL-------SASSVQVAEEAGEMLTRIVPDIQRTAELVQEISAACKEQDT 449
Cdd:cd11386  94 AGEAGRGFAVVADEVRKLAEESAEAAKEIEELieeiqeqTEEAVEAMEETSEEVEEGVELVEETGRAFEEIVASVEEVAD 173
                       170       180
                ....*....|....*....|....*..
gi 39996402 450 GAEQINKAIQQLDQVIQQNASASEEMA 476
Cdd:cd11386 174 GIQEISAATQEQSASTQEIAAAVEEIA 200
4HB_MCP_1 pfam12729
Four helix bundle sensory module for signal transduction; This family is a four helix bundle ...
31-184 1.22e-11

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: 63.01  E-value: 1.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996402    31 INGMKEINSKLDRILKVNYGKIKNANEVSMVVGDLMGKINEIML-KDVNERPAIKQEIEKLRSDYRSALERLEQLEQTDQ 109
Cdd:pfam12729  27 LYSLKKINKNSETMYEDRLLPIKWLGEIRSNLREIRANLLELILtTDPAERDELLKDIEELRAEIDKLLKKYEKTILTEE 106
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 39996402   110 GKQLIAGAKSAIDNAKKANNDIIELSLAGKTDQALIVYNKEGAPLSQKIVTAFKNIVKYQEERMELRYAEALKAY 184
Cdd:pfam12729 107 EKKLFNEFKEQLKAYRKVRNKVLDLAKAGKNDEAYALYLTELEPARDAVIEALDELIDYNLKVAKEAYEDNKASY 181
HAMP pfam00672
HAMP domain;
192-259 4.16e-10

HAMP domain;


Pssm-ID: 250044  Cd Length: 70  Bit Score: 56.47  E-value: 4.16e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 39996402   192 LGVAFCAAIIGILISLFATRSITRPLDKAVSVSNELAEGNLTVTIEATSKDETGQLLAAMHNMVEKLK 259
Cdd:pfam00672   2 LLVLLIALLLLLLLAWLLARRLLRPLRRLAEAARRIASGDLDDRVPVSGPDEIGELARAFNQMADRLR 69
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
211-263 2.74e-08

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


Pssm-ID: 197640  Cd Length: 53  Bit Score: 50.71  E-value: 2.74e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 39996402    211 RSITRPLDKAVSVSNELAEGNLTVTIEATSKDETGQLLAAMHNMVEKLKGVVA 263
Cdd:smart00304   1 RRLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRLEETIA 53
HAMP COG2770
HAMP domain [Signal transduction mechanisms];
199-260 7.68e-04

HAMP domain [Signal transduction mechanisms];


Pssm-ID: 225359  Cd Length: 83  Bit Score: 38.13  E-value: 7.68e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 39996402 199 AIIGILISLFATRSITRPLDKAVSVSNELAEGNLTVTIEATSKDETGQLLAAMHNMVEKLKG 260
Cdd:COG2770  16 VLILAVLLLAAARRVTRPLRRLADLAQNLALGDLSAEIPQPMLDEIGELAKAFNRMRDSLQR 77
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility, Signal transduction mechanisms];
161-498 5.45e-54

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


Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 189.82  E-value: 5.45e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996402 161 AFKNIVKYQEERMELRYAEALKAYGTSRAVALGVAFCAAIIGILISLFATRSITRPLDKAVSVSNELAEGNLTVTIEATS 240
Cdd:COG0840  32 ELGKLLLSLNLILDDAASAEAAALKAVLKFLLISLLVAIIVVLVLAILLLRAILEPISDLLEVVERIAAGDLTKRIDESS 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996402 241 KDETGQLLAAMHNMVEKLKGVVADVKSAADNVAAGSQELSSSSEEMSQGATEQAAAAEEASSSMEQMSSNIRQNADNATQ 320
Cdd:COG0840 112 NDEFGQLAKSFNEMILNLRQIIDAVQDNAEALSGASEEIAASATELSARADQQAESLEEVASAIEELSETVKEVAFNAKE 191
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996402 321 TEKIALKSATDAREGGKAVAGTVSAM------------------KEIASKISIIEEIARQTNLLALNAAIEAARAGEHGK 382
Cdd:COG0840 192 AAALASEASQVAEEGGEEVRQAVEQMqeiaeelaevvkklsessQEIEEITSVINSIAEQTNLLALNAAIEAARAGEAGR 271
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996402 383 GFAVVAAEVRKLAERSQKAAGEISEL---------------------SASSVQVAEEAGEMLTRIVPDIQRTAELVQEIS 441
Cdd:COG0840 272 GFAVVADEVRKLAERSADSAKEIGLLieeiqneaadavehmeesaseVSEGVKLVEETGSSLGEIAAAIEEVSQLISEIA 351
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 39996402 442 AACKEQDTGAEQINKAIQQLDQVIQQNASASEEMASTSEELASQAEQLQATISFFRT 498
Cdd:COG0840 352 AATEEQTAVLEEINASIEELDDVTQENAAAVEELAAASEELKELAEKLLELVAKFKL 408
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
160-520 2.18e-57

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 202.54  E-value: 2.18e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996402  160 TAFKNIVKYQEERMELRYAEALKAYGTSRAVALGVAFCAAIIGILISLFATRSITRPLDKAVSVSNELAEGNLTVTIEAT 239
Cdd:PRK15048 163 EAFAQYALSSEKLYRDIVTDNADDYRFAQWQLAVIALVVVLILLVAWYGIRRMLLTPLAKIIAHIREIAGGNLANTLTID 242
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996402  240 SKDETGQLLAAMHNMVEKLKGVVADVKSAADNVAAGSQELSSSSEEMSQGATEQAAAAEEASSSMEQMSSNIRQNADNAT 319
Cdd:PRK15048 243 GRSEMGDLAQSVSHMQRSLTDTVTHVREGSDAIYAGTREIAAGNTDLSSRTEQQASALEETAASMEQLTATVKQNADNAR 322
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996402  320 QTEKIALKSATDAREGGKAVAGTVSAMKEIA--SK-----ISIIEEIARQTNLLALNAAIEAARAGEHGKGFAVVAAEVR 392
Cdd:PRK15048 323 QASQLAQSASDTAQHGGKVVDGVVKTMHEIAdsSKkiadiISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVR 402
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996402  393 KLAERSQKAAGEISELSASSVQ-------VAEEAGEMLTRIVPDIQRTAELVQEISAACKEQDTGAEQINKAIQQLDQVI 465
Cdd:PRK15048 403 NLASRSAQAAKEIKALIEDSVSrvdtgsvLVESAGETMNNIVNAVTRVTDIMGEIASASDEQSRGIDQVALAVSEMDRVT 482
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 39996402  466 QQNASASEEMASTSEELASQAEQLQATISFFR------TDDRGASSRSAVHRPVAKKKAAI 520
Cdd:PRK15048 483 QQNASLVQESAAAAAALEEQASRLTQAVSAFRlaasplTNKPQTPSRPASEQPPAQPRLRI 543
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
304-497 5.14e-50

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: 174.40  E-value: 5.14e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996402    304 MEQMSSNIRQNADNATQTEKIALKSATDAREGGKAVAGTVSAMKEIASK-------ISIIEEIARQTNLLALNAAIEAAR 376
Cdd:smart00283  41 ADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAVSAVEELEESsdeigeiVSVIDDIADQTNLLALNAAIEAAR 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996402    377 AGEHGKGFAVVAAEVRKLAERSQKAAGEISEL---------------------SASSVQVAEEAGEMLTRIVPDIQRTAE 435
Cdd:smart00283 121 AGEAGRGFAVVADEVRKLAERSAESAKEIESLikeiqeetneavaameessseVEEGVELVEETGDALEEIVDSVEEIAD 200
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 39996402    436 LVQEISAACKEQDTGAEQINKAIQQLDQVIQQNASASEEMASTSEELASQAEQLQATISFFR 497
Cdd:smart00283 201 LVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEISAAAEELSGLAEELDELVERFK 262
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
312-497 5.61e-42

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: 150.29  E-value: 5.61e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996402   312 RQNADNATQTEKIALksaTDAREGGKAVAGTVSAMKEIASK-------ISIIEEIARQTNLLALNAAIEAARAGEHGKGF 384
Cdd:pfam00015   1 AQASDLAQLASEEAL---DEMSQIGQVVDDAVETMEELETSskkisdiISVIDEIAFQTNLLALNAAIEAARAGEQGRGF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996402   385 AVVAAEVRKLAERSQKAAGEISELSASSVQ---------------------VAEEAGEMLTRIVPDIQRTAELVQEISAA 443
Cdd:pfam00015  78 AVVADEVRKLAERSAQAAKEIEALIEEIVKqtndstasiqqtrtevevgstIVESTGEALKEIVDAVAEIADIVQEIAAA 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 39996402   444 CKEQDTGAEQINKAIQQLDQVIQQNASASEEMASTSEELASQAEQLQATISFFR 497
Cdd:pfam00015 158 SDEQSAGIDQVNQAVARIDQVTQQNAALVEESAAAAETLEEQAEELTASVAQFR 211
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
85-251 9.59e-03

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


Pssm-ID: 274362 [Multi-domain]  Cd Length: 968  Bit Score: 37.45  E-value: 9.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996402    85 QEIEKLRSDYRSALERLEQLEQTDQGKQLIAGAKSAIDNAKKANNDIIELSLAGKTDQALIVYNKEGAPLSQKIVTAFKN 164
Cdd:TIGR02956 227 AHINQLDEEFNRLVMILSRRVQSIEDPTRSNQLKDLLVTLNKTPKLFKLLRQLSQILQKQQRLQQANLEQFTQLNTTVSQ 306
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996402   165 IVKYQEERMELRYAEALKAYGTSRA--VALGV-AFCaaIIGILISLFATRSITRPLDKAVSVSNELAEGNLTVTIEATSK 241
Cdd:TIGR02956 307 LVNAQNQRTEAAVSDLLMTLSVAQFglLITGMlGLV--ILVFIMWRVVYRSVILRLNQHTQALLRLALGDLDISLDARGD 384
                         170
                  ....*....|
gi 39996402   242 DETGQLLAAM 251
Cdd:TIGR02956 385 DELAHMGRAI 394
 
Name Accession Description Interval E-value
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
213-259 7.21e-07

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: 46.47  E-value: 7.21e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 39996402 213 ITRPLDKAVSVSNELAEGNLTVTIEATSKDETGQLLAAMHNMVEKLK 259
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGDLDVRLPVTGRDEIGELARAFNQMAERLR 47
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
304-476 2.84e-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: 150.85  E-value: 2.84e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996402 304 MEQMSSNIRQNADNATQTEKIALKSATDAREGGKAVAGTVSAM-------KEIASKISIIEEIARQTNLLALNAAIEAAR 376
Cdd:cd11386  14 ADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVeeleessAEIGEIVEVIDDIAEQTNLLALNAAIEAAR 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996402 377 AGEHGKGFAVVAAEVRKLAERSQKAAGEISEL-------SASSVQVAEEAGEMLTRIVPDIQRTAELVQEISAACKEQDT 449
Cdd:cd11386  94 AGEAGRGFAVVADEVRKLAEESAEAAKEIEELieeiqeqTEEAVEAMEETSEEVEEGVELVEETGRAFEEIVASVEEVAD 173
                       170       180
                ....*....|....*....|....*..
gi 39996402 450 GAEQINKAIQQLDQVIQQNASASEEMA 476
Cdd:cd11386 174 GIQEISAATQEQSASTQEIAAAVEEIA 200
4HB_MCP_1 pfam12729
Four helix bundle sensory module for signal transduction; This family is a four helix bundle ...
31-184 1.22e-11

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: 63.01  E-value: 1.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996402    31 INGMKEINSKLDRILKVNYGKIKNANEVSMVVGDLMGKINEIML-KDVNERPAIKQEIEKLRSDYRSALERLEQLEQTDQ 109
Cdd:pfam12729  27 LYSLKKINKNSETMYEDRLLPIKWLGEIRSNLREIRANLLELILtTDPAERDELLKDIEELRAEIDKLLKKYEKTILTEE 106
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 39996402   110 GKQLIAGAKSAIDNAKKANNDIIELSLAGKTDQALIVYNKEGAPLSQKIVTAFKNIVKYQEERMELRYAEALKAY 184
Cdd:pfam12729 107 EKKLFNEFKEQLKAYRKVRNKVLDLAKAGKNDEAYALYLTELEPARDAVIEALDELIDYNLKVAKEAYEDNKASY 181
HAMP pfam00672
HAMP domain;
192-259 4.16e-10

HAMP domain;


Pssm-ID: 250044  Cd Length: 70  Bit Score: 56.47  E-value: 4.16e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 39996402   192 LGVAFCAAIIGILISLFATRSITRPLDKAVSVSNELAEGNLTVTIEATSKDETGQLLAAMHNMVEKLK 259
Cdd:pfam00672   2 LLVLLIALLLLLLLAWLLARRLLRPLRRLAEAARRIASGDLDDRVPVSGPDEIGELARAFNQMADRLR 69
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
211-263 2.74e-08

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


Pssm-ID: 197640  Cd Length: 53  Bit Score: 50.71  E-value: 2.74e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 39996402    211 RSITRPLDKAVSVSNELAEGNLTVTIEATSKDETGQLLAAMHNMVEKLKGVVA 263
Cdd:smart00304   1 RRLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRLEETIA 53
HAMP COG2770
HAMP domain [Signal transduction mechanisms];
199-260 7.68e-04

HAMP domain [Signal transduction mechanisms];


Pssm-ID: 225359  Cd Length: 83  Bit Score: 38.13  E-value: 7.68e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 39996402 199 AIIGILISLFATRSITRPLDKAVSVSNELAEGNLTVTIEATSKDETGQLLAAMHNMVEKLKG 260
Cdd:COG2770  16 VLILAVLLLAAARRVTRPLRRLADLAQNLALGDLSAEIPQPMLDEIGELAKAFNRMRDSLQR 77
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility, Signal transduction mechanisms];
161-498 5.45e-54

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


Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 189.82  E-value: 5.45e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996402 161 AFKNIVKYQEERMELRYAEALKAYGTSRAVALGVAFCAAIIGILISLFATRSITRPLDKAVSVSNELAEGNLTVTIEATS 240
Cdd:COG0840  32 ELGKLLLSLNLILDDAASAEAAALKAVLKFLLISLLVAIIVVLVLAILLLRAILEPISDLLEVVERIAAGDLTKRIDESS 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996402 241 KDETGQLLAAMHNMVEKLKGVVADVKSAADNVAAGSQELSSSSEEMSQGATEQAAAAEEASSSMEQMSSNIRQNADNATQ 320
Cdd:COG0840 112 NDEFGQLAKSFNEMILNLRQIIDAVQDNAEALSGASEEIAASATELSARADQQAESLEEVASAIEELSETVKEVAFNAKE 191
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996402 321 TEKIALKSATDAREGGKAVAGTVSAM------------------KEIASKISIIEEIARQTNLLALNAAIEAARAGEHGK 382
Cdd:COG0840 192 AAALASEASQVAEEGGEEVRQAVEQMqeiaeelaevvkklsessQEIEEITSVINSIAEQTNLLALNAAIEAARAGEAGR 271
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996402 383 GFAVVAAEVRKLAERSQKAAGEISEL---------------------SASSVQVAEEAGEMLTRIVPDIQRTAELVQEIS 441
Cdd:COG0840 272 GFAVVADEVRKLAERSADSAKEIGLLieeiqneaadavehmeesaseVSEGVKLVEETGSSLGEIAAAIEEVSQLISEIA 351
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 39996402 442 AACKEQDTGAEQINKAIQQLDQVIQQNASASEEMASTSEELASQAEQLQATISFFRT 498
Cdd:COG0840 352 AATEEQTAVLEEINASIEELDDVTQENAAAVEELAAASEELKELAEKLLELVAKFKL 408
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
160-520 2.18e-57

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 202.54  E-value: 2.18e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996402  160 TAFKNIVKYQEERMELRYAEALKAYGTSRAVALGVAFCAAIIGILISLFATRSITRPLDKAVSVSNELAEGNLTVTIEAT 239
Cdd:PRK15048 163 EAFAQYALSSEKLYRDIVTDNADDYRFAQWQLAVIALVVVLILLVAWYGIRRMLLTPLAKIIAHIREIAGGNLANTLTID 242
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996402  240 SKDETGQLLAAMHNMVEKLKGVVADVKSAADNVAAGSQELSSSSEEMSQGATEQAAAAEEASSSMEQMSSNIRQNADNAT 319
Cdd:PRK15048 243 GRSEMGDLAQSVSHMQRSLTDTVTHVREGSDAIYAGTREIAAGNTDLSSRTEQQASALEETAASMEQLTATVKQNADNAR 322
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996402  320 QTEKIALKSATDAREGGKAVAGTVSAMKEIA--SK-----ISIIEEIARQTNLLALNAAIEAARAGEHGKGFAVVAAEVR 392
Cdd:PRK15048 323 QASQLAQSASDTAQHGGKVVDGVVKTMHEIAdsSKkiadiISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVR 402
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996402  393 KLAERSQKAAGEISELSASSVQ-------VAEEAGEMLTRIVPDIQRTAELVQEISAACKEQDTGAEQINKAIQQLDQVI 465
Cdd:PRK15048 403 NLASRSAQAAKEIKALIEDSVSrvdtgsvLVESAGETMNNIVNAVTRVTDIMGEIASASDEQSRGIDQVALAVSEMDRVT 482
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 39996402  466 QQNASASEEMASTSEELASQAEQLQATISFFR------TDDRGASSRSAVHRPVAKKKAAI 520
Cdd:PRK15048 483 QQNASLVQESAAAAAALEEQASRLTQAVSAFRlaasplTNKPQTPSRPASEQPPAQPRLRI 543
PRK15041 PRK15041
methyl-accepting chemotaxis protein I; Provisional
187-520 3.16e-55

methyl-accepting chemotaxis protein I; Provisional


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 196.33  E-value: 3.16e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996402  187 SRAVALGVAFCAAIIGILISLF--ATRSITRPLDKAVSVSNELAEGNLTVTIEATSKDETGQLLAAMHNMVEKLKGVVAD 264
Cdd:PRK15041 190 SQAMWILVGVMIVVLAVIFAVWfgIKASLVAPMNRLIDSIRHIAGGDLVKPIEVDGSNEMGQLAESLRHMQGELMRTVGD 269
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996402  265 VKSAADNVAAGSQELSSSSEEMSQGATEQAAAAEEASSSMEQMSSNIRQNADNATQTEKIALKSATDAREGGKAVAGTVS 344
Cdd:PRK15041 270 VRNGANAIYSGASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQ 349
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996402  345 AMKEIASK-------ISIIEEIARQTNLLALNAAIEAARAGEHGKGFAVVAAEVRKLAERSQKAAGEISELSASSVQ--- 414
Cdd:PRK15041 350 TMRDISTSsqkiadiISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGkvd 429
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996402  415 ----VAEEAGEMLTRIVPDIQRTAELVQEISAACKEQDTGAEQINKAIQQLDQVIQQNASASEEMASTSEELASQAEQLQ 490
Cdd:PRK15041 430 vgstLVESAGETMAEIVSAVTRVTDIMGEIASASDEQSRGIDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRLT 509
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 39996402  491 ATISFFRTDD-----RGASSRSAVHRPVAKKKAAI 520
Cdd:PRK15041 510 EAVAVFRIQQqqqqqRETSAVVKTVTPATPRKMAV 544
PRK09793 PRK09793
methyl-accepting protein IV; Provisional
178-501 2.10e-54

methyl-accepting protein IV; Provisional


Pssm-ID: 182079 [Multi-domain]  Cd Length: 533  Bit Score: 193.75  E-value: 2.10e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996402  178 AEALKAYGTSRAVALGVAFCAAIIGILISLFATRSITRPLDKAVSVSNELAEGNLTVTIEATSKDETGQLLAAMHNMVEK 257
Cdd:PRK09793 179 AQSQRNYQISALVFISMIIVAAIYISSALWWTRKMIVQPLAIIGSHFDSIAAGNLARPIAVYGRNEITAIFASLKTMQQA 258
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996402  258 LKGVVADVKSAADNVAAGSQELSSSSEEMSQGATEQAAAAEEASSSMEQMSSNIRQNADNATQTEKIALKSATDAREGGK 337
Cdd:PRK09793 259 LRGTVSDVRKGSQEMHIGIAEIVAGNNDLSSRTEQQAASLAQTAASMEQLTATVGQNADNARQASELAKNAATTAQAGGV 338
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996402  338 AVAGTVSAMKEIASK-------ISIIEEIARQTNLLALNAAIEAARAGEHGKGFAVVAAEVRKLAERSQKAAGEISELSA 410
Cdd:PRK09793 339 QVSTMTHTMQEIATSsqkigdiISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKGLIE 418
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996402  411 SSV-------QVAEEAGEMLTRIVPDIQRTAELVQEISAACKEQDTGAEQINKAIQQLDQVIQQNASASEEMASTSEELA 483
Cdd:PRK09793 419 ESVnrvqqgsKLVNNAAATMTDIVSSVTRVNDIMGEIASASEEQRRGIEQVAQAVSQMDQVTQQNASLVEEAAVATEQLA 498
                        330
                 ....*....|....*...
gi 39996402  484 SQAEQLQATISFFRTDDR 501
Cdd:PRK09793 499 NQADHLSSRVAVFTLEEH 516
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
304-497 5.14e-50

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: 174.40  E-value: 5.14e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996402    304 MEQMSSNIRQNADNATQTEKIALKSATDAREGGKAVAGTVSAMKEIASK-------ISIIEEIARQTNLLALNAAIEAAR 376
Cdd:smart00283  41 ADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAVSAVEELEESsdeigeiVSVIDDIADQTNLLALNAAIEAAR 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996402    377 AGEHGKGFAVVAAEVRKLAERSQKAAGEISEL---------------------SASSVQVAEEAGEMLTRIVPDIQRTAE 435
Cdd:smart00283 121 AGEAGRGFAVVADEVRKLAERSAESAKEIESLikeiqeetneavaameessseVEEGVELVEETGDALEEIVDSVEEIAD 200
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 39996402    436 LVQEISAACKEQDTGAEQINKAIQQLDQVIQQNASASEEMASTSEELASQAEQLQATISFFR 497
Cdd:smart00283 201 LVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEISAAAEELSGLAEELDELVERFK 262
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
312-497 5.61e-42

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: 150.29  E-value: 5.61e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996402   312 RQNADNATQTEKIALksaTDAREGGKAVAGTVSAMKEIASK-------ISIIEEIARQTNLLALNAAIEAARAGEHGKGF 384
Cdd:pfam00015   1 AQASDLAQLASEEAL---DEMSQIGQVVDDAVETMEELETSskkisdiISVIDEIAFQTNLLALNAAIEAARAGEQGRGF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996402   385 AVVAAEVRKLAERSQKAAGEISELSASSVQ---------------------VAEEAGEMLTRIVPDIQRTAELVQEISAA 443
Cdd:pfam00015  78 AVVADEVRKLAERSAQAAKEIEALIEEIVKqtndstasiqqtrtevevgstIVESTGEALKEIVDAVAEIADIVQEIAAA 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 39996402   444 CKEQDTGAEQINKAIQQLDQVIQQNASASEEMASTSEELASQAEQLQATISFFR 497
Cdd:pfam00015 158 SDEQSAGIDQVNQAVARIDQVTQQNAALVEESAAAAETLEEQAEELTASVAQFR 211
NtrY COG5000
Signal transduction histidine kinase involved in nitrogen fixation and metabolism regulation ...
192-270 2.35e-05

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


Pssm-ID: 227333 [Multi-domain]  Cd Length: 712  Bit Score: 45.92  E-value: 2.35e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996402 192 LGVAFCAAIIGILISLFATRSITRPLDKAVSVSNELAEGNLTVTIEATSKDE-TGQLLAAMHNMVEKLKGVVADVKSAAD 270
Cdd:COG5000 284 LSTALLVLLAAIWTAIAFARRIVRPIRKLIEAADEVADGDLDVQVPVRRVDEdVGRLSKAFNKMTEQLSSQQEALERAKD 363
COG4372 COG4372
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
304-490 4.77e-04

Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 226809 [Multi-domain]  Cd Length: 499  Bit Score: 41.55  E-value: 4.77e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996402 304 MEQMSSNIRQNADNATQTEKiALKSATDAREGGKAVAGTVSAMKEIAskisiiEEIARQTNLLALNAAIEAARAGEHGKG 383
Cdd:COG4372  76 LDDIRPQLRALRTELGTAQG-EKRAAETEREAARSELQKARQEREAV------RQELAAARQNLAKAQQELARLTKQAQD 148
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996402 384 ----FAVVAAEVRKLAERSQKAAGEISELSASSVQVAEEAGEMLTRIVP------DIQRTAELVQEISAACKEQDTGAEQ 453
Cdd:COG4372 149 lqtrLKTLAEQRRQLEAQAQSLQASQKQLQASATQLKSQVLDLKLRSAQieqeaqNLATRANAAQARTEELARRAAAAQQ 228
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 39996402 454 INKAIQQLDQVIQQNAsasEEMASTSEELASQAEQLQ 490
Cdd:COG4372 229 TAQAIQQRDAQISQKA---QQIAARAEQIRERERQLQ 262
NarQ COG3850
Signal transduction histidine kinase, nitrate/nitrite-specific [Signal transduction mechanisms] ...
198-268 1.85e-03

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


Pssm-ID: 226368 [Multi-domain]  Cd Length: 574  Bit Score: 39.64  E-value: 1.85e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 39996402 198 AAIIGILISLFAT-----RSITRPLDKAVSVSNELAEGNLTVTIEATSKDETGQLLAAMHNMVEKLKGVVADVKSA 268
Cdd:COG3850 155 AGMLLILLLVVFTiywlrRRVVRPLNQLTSAAQRIGRRQFDQRPTDTGRNELGLLGRAFNQMSGELKKLYADLEQR 230
COG4372 COG4372
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
387-491 2.90e-03

Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 226809 [Multi-domain]  Cd Length: 499  Bit Score: 38.85  E-value: 2.90e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996402 387 VAAEVRKLAERSQKAAGEISELSASSVQVAEEAGEMLTRIVPDIQRTAEL------VQEISAACKEQDTGAEQINKAIQQ 460
Cdd:COG4372 170 LQASQKQLQASATQLKSQVLDLKLRSAQIEQEAQNLATRANAAQARTEELarraaaAQQTAQAIQQRDAQISQKAQQIAA 249
                        90       100       110
                ....*....|....*....|....*....|.
gi 39996402 461 LDQVIQQNASASEEMASTSEELASQAEQLQA 491
Cdd:COG4372 250 RAEQIRERERQLQRLETAQARLEQEVAQLEA 280
PRK10549 PRK10549
signal transduction histidine-protein kinase BaeS; Provisional
194-247 3.23e-03

signal transduction histidine-protein kinase BaeS; Provisional


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 38.85  E-value: 3.23e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 39996402  194 VAFcAAIIGILISLFATRSITRPLDKAVSVSNELAEGNLTVTIEATSKDETGQL 247
Cdd:PRK10549 170 VAL-STLLAALATFLLARGLLAPVKRLVEGTHKLAAGDFTTRVTPTSRDELGRL 222
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
85-251 9.59e-03

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


Pssm-ID: 274362 [Multi-domain]  Cd Length: 968  Bit Score: 37.45  E-value: 9.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996402    85 QEIEKLRSDYRSALERLEQLEQTDQGKQLIAGAKSAIDNAKKANNDIIELSLAGKTDQALIVYNKEGAPLSQKIVTAFKN 164
Cdd:TIGR02956 227 AHINQLDEEFNRLVMILSRRVQSIEDPTRSNQLKDLLVTLNKTPKLFKLLRQLSQILQKQQRLQQANLEQFTQLNTTVSQ 306
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996402   165 IVKYQEERMELRYAEALKAYGTSRA--VALGV-AFCaaIIGILISLFATRSITRPLDKAVSVSNELAEGNLTVTIEATSK 241
Cdd:TIGR02956 307 LVNAQNQRTEAAVSDLLMTLSVAQFglLITGMlGLV--ILVFIMWRVVYRSVILRLNQHTQALLRLALGDLDISLDARGD 384
                         170
                  ....*....|
gi 39996402   242 DETGQLLAAM 251
Cdd:TIGR02956 385 DELAHMGRAI 394
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.14
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A 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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