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Conserved domains on  [gi|46578760|ref|YP_009568|]
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methyl-accepting chemotaxis protein [Desulfovibrio vulgaris str. Hildenborough]

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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. ...
269-316 6.08e-06

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: 44.16  E-value: 6.08e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 46578760 269 IVRPLAAATHAATRITAGELDITLDTSGRDEAATLQRALADMVTTLRD 316
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGDLDVRLPVTGRDEIGELARAFNQMAERLRE 48
MCP_signal super family cl21547
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
404-602 4.04e-43

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: 153.93  E-value: 4.04e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46578760 404 QMNATVLDVAHSAAGAAEQTALTRDKAREGVDSVKATLDAMQSLDTVATGLADDMRKLDAQSAAIDKVVNVINDIADQTN 483
Cdd:cd11386   2 ELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQTN 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46578760 484 LLALNAAIEAARAGEAGRGFAVVADEVRKLAEKTMQATGEVGITVRNIQTLTRSNVASMEDALKAIRAAAERSGQSAATL 563
Cdd:cd11386  82 LLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRAF 161
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 46578760 564 GEILRMTDAAAAQVQAIAAAAEEQSAASEQITRSIAEID 602
Cdd:cd11386 162 EEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
Cache_2 smart01049
Cache is an extracellular domain that is predicted to have a role in small-molecule ...
86-173 1.18e-13

Cache is an extracellular domain that is predicted to have a role in small-molecule recognition in a wide range of proteins; Members include the animal dihydropyridine-sensitive voltage-gated Ca2+ channel; alpha-2delta subunit, and various bacterial chemotaxis receptors. The name Cache comes from CAlcium channels and CHEmotaxis receptors. This domain consists of an N-terminal part with three predicted strands and an alpha-helix, and a C-terminal part with a strand dyad followed by a relatively unstructured region. The N-terminal portion of the (unpermuted) Cache domain contains three predicted strands that could form a sheet analogous to that present in the core of the PAS domain structure. Cache domains are particularly widespread in bacteria, with Vibrio cholerae. The animal calcium channel alpha-2delta subunits might have acquired a part of their extracellular domains from a bacterial source. The Cache domain appears to have arisen from the GAF-PAS fold despite their divergent functions.


:

Pssm-ID: 214995  Cd Length: 91  Bit Score: 67.67  E-value: 1.18e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46578760     86 LLDEQKNRIQSITHSTALSLEVLTARVQ----TDEEKLAIIADAIEKARFesDNSGYFFVYTGT-VNAAHPTQKQLIGKD 160
Cdd:smart01049   1 LLEERKAELKNLVEIAVSIVEAYYAQAAagklTEEEAQAQAKAALRALRY--GGDGYFFVYDSDgVMLMHPAKPELEGKN 78
                           90
                   ....*....|...
gi 46578760    161 LGNTTDREGVYYV 173
Cdd:smart01049  79 LSDLKDPNGKYLF 91
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
378-634 7.82e-51

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


:

Pssm-ID: 214599 [Multi-domain]  Cd Length: 262  Bit Score: 177.48  E-value: 7.82e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46578760    378 AALSGSINSGSGIQLQRVGETATAMSQMNATVLDVAHSAAGAAEQTALTRDKAREGVDSVKATLDAMQSLDTVATGLADD 457
Cdd:smart00283   3 SEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAVSA 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46578760    458 MRKLDAQSAAIDKVVNVINDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAEKTMQATGEVGITVRNIQTLTRS 537
Cdd:smart00283  83 VEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEETNE 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46578760    538 NVASMEDALKAIRAAAERSGQSAATLGEILRMTDAAAAQVQAIAAAAEEQSAASEQITRSIAEIDAVARDNGSLLSEADT 617
Cdd:smart00283 163 AVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEISA 242
                          250
                   ....*....|....*..
gi 46578760    618 AIRGIEDKTGILRGLMA 634
Cdd:smart00283 243 AAEELSGLAEELDELVE 259
 
Name Accession Description Interval E-value
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
269-316 6.08e-06

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: 44.16  E-value: 6.08e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 46578760 269 IVRPLAAATHAATRITAGELDITLDTSGRDEAATLQRALADMVTTLRD 316
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGDLDVRLPVTGRDEIGELARAFNQMAERLRE 48
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
404-602 4.04e-43

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: 153.93  E-value: 4.04e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46578760 404 QMNATVLDVAHSAAGAAEQTALTRDKAREGVDSVKATLDAMQSLDTVATGLADDMRKLDAQSAAIDKVVNVINDIADQTN 483
Cdd:cd11386   2 ELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQTN 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46578760 484 LLALNAAIEAARAGEAGRGFAVVADEVRKLAEKTMQATGEVGITVRNIQTLTRSNVASMEDALKAIRAAAERSGQSAATL 563
Cdd:cd11386  82 LLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRAF 161
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 46578760 564 GEILRMTDAAAAQVQAIAAAAEEQSAASEQITRSIAEID 602
Cdd:cd11386 162 EEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
Cache_2 smart01049
Cache is an extracellular domain that is predicted to have a role in small-molecule ...
86-173 1.18e-13

Cache is an extracellular domain that is predicted to have a role in small-molecule recognition in a wide range of proteins; Members include the animal dihydropyridine-sensitive voltage-gated Ca2+ channel; alpha-2delta subunit, and various bacterial chemotaxis receptors. The name Cache comes from CAlcium channels and CHEmotaxis receptors. This domain consists of an N-terminal part with three predicted strands and an alpha-helix, and a C-terminal part with a strand dyad followed by a relatively unstructured region. The N-terminal portion of the (unpermuted) Cache domain contains three predicted strands that could form a sheet analogous to that present in the core of the PAS domain structure. Cache domains are particularly widespread in bacteria, with Vibrio cholerae. The animal calcium channel alpha-2delta subunits might have acquired a part of their extracellular domains from a bacterial source. The Cache domain appears to have arisen from the GAF-PAS fold despite their divergent functions.


Pssm-ID: 214995  Cd Length: 91  Bit Score: 67.67  E-value: 1.18e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46578760     86 LLDEQKNRIQSITHSTALSLEVLTARVQ----TDEEKLAIIADAIEKARFesDNSGYFFVYTGT-VNAAHPTQKQLIGKD 160
Cdd:smart01049   1 LLEERKAELKNLVEIAVSIVEAYYAQAAagklTEEEAQAQAKAALRALRY--GGDGYFFVYDSDgVMLMHPAKPELEGKN 78
                           90
                   ....*....|...
gi 46578760    161 LGNTTDREGVYYV 173
Cdd:smart01049  79 LSDLKDPNGKYLF 91
Cache_2 pfam08269
Cache domain;
86-174 1.40e-08

Cache domain;


Pssm-ID: 254697  Cd Length: 95  Bit Score: 52.69  E-value: 1.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46578760    86 LLDEQKNRIQSITHSTALSLEVLTARVQ----TDEEKLAIIADAIEKARFESDnsGYFFVY-TGTVNAAHPTQKQLIGKD 160
Cdd:pfam08269   4 LIEERKAELKAVVESALSIIKEYYQQAQkgklTREEAQAQAKALLRALRYDGD--GYFFAYdSNGTNVMHPIKPELVGKN 81
                          90
                  ....*....|....
gi 46578760   161 LGNTTDREGVYYVR 174
Cdd:pfam08269  82 LSNLKDPNGNNVFV 95
HAMP pfam00672
HAMP domain;
261-316 1.83e-06

HAMP domain;


Pssm-ID: 250044  Cd Length: 70  Bit Score: 46.07  E-value: 1.83e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 46578760   261 AAMALTRSIVRPLAAATHAATRITAGELDITLDTSGRDEAATLQRALADMVTTLRD 316
Cdd:pfam00672  15 LAWLLARRLLRPLRRLAEAARRIASGDLDDRVPVSGPDEIGELARAFNQMADRLRE 70
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
267-316 6.71e-06

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


Pssm-ID: 197640  Cd Length: 53  Bit Score: 44.16  E-value: 6.71e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 46578760    267 RSIVRPLAAATHAATRITAGELDITLDTSGRDEAATLQRALADMVTTLRD 316
Cdd:smart00304   1 RRLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRLEE 50
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
378-634 7.82e-51

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


Pssm-ID: 214599 [Multi-domain]  Cd Length: 262  Bit Score: 177.48  E-value: 7.82e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46578760    378 AALSGSINSGSGIQLQRVGETATAMSQMNATVLDVAHSAAGAAEQTALTRDKAREGVDSVKATLDAMQSLDTVATGLADD 457
Cdd:smart00283   3 SEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAVSA 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46578760    458 MRKLDAQSAAIDKVVNVINDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAEKTMQATGEVGITVRNIQTLTRS 537
Cdd:smart00283  83 VEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEETNE 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46578760    538 NVASMEDALKAIRAAAERSGQSAATLGEILRMTDAAAAQVQAIAAAAEEQSAASEQITRSIAEIDAVARDNGSLLSEADT 617
Cdd:smart00283 163 AVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEISA 242
                          250
                   ....*....|....*..
gi 46578760    618 AIRGIEDKTGILRGLMA 634
Cdd:smart00283 243 AAEELSGLAEELDELVE 259
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction ...
261-637 2.68e-45

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


Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 165.93  E-value: 2.68e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46578760 261 AAMALTRSIVRPLAAATHAATRITAGELDITLDTSGRDEAATLQRALADMVTTLRDnfaalhakeaeaqrqtqsaleaaa 340
Cdd:COG0840  76 LAILLLRAILEPISDLLEVVERIAAGDLTKRIDESSNDEFGQLAKSFNEMILNLRQ------------------------ 131
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46578760 341 rademarvalasregmssTAVRLGEVTTDLDTDSHRLAALSGSINSGSGIQLQRVGETATAMSQMNATVLDVAHSAAGAA 420
Cdd:COG0840 132 ------------------IIDAVQDNAEALSGASEEIAASATELSARADQQAESLEEVASAIEELSETVKEVAFNAKEAA 193
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46578760 421 EQTALTRDKAREGVDSVKATLDAMQSldtVATGLADDMRKLDAQSAAIDKVVNVINDIADQTNLLALNAAIEAARAGEAG 500
Cdd:COG0840 194 ALASEASQVAEEGGEEVRQAVEQMQE---IAEELAEVVKKLSESSQEIEEITSVINSIAEQTNLLALNAAIEAARAGEAG 270
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46578760 501 RGFAVVADEVRKLAEKTMQATGEVGITVRNIQTLTRSNVASMEDALKAIRAAAERSGQSAATLGEILRMTDAAAAQVQAI 580
Cdd:COG0840 271 RGFAVVADEVRKLAERSADSAKEIGLLIEEIQNEAADAVEHMEESASEVSEGVKLVEETGSSLGEIAAAIEEVSQLISEI 350
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 46578760 581 AAAAEEQSAASEQITRSIAEIDAVARDNGSLLSEADTAIRGIEDKTGILRGLMADLN 637
Cdd:COG0840 351 AAATEEQTAVLEEINASIEELDDVTQENAAAVEELAAASEELKELAEKLLELVAKFK 407
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
433-634 1.61e-34

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: 130.26  E-value: 1.61e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46578760   433 GVDSVKATLDAMQSLDTVATGLADDMRKLDAQSAAIDKVVNVINDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRK 512
Cdd:pfam00015   7 AQLASEEALDEMSQIGQVVDDAVETMEELETSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46578760   513 LAEKTMQATGEVGITVRNIQTLTRSNVASMEDALKAIRAAAERSGQSAATLGEILRMTDAAAAQVQAIAAAAEEQSAASE 592
Cdd:pfam00015  87 LAERSAQAAKEIEALIEEIVKQTNDSTASIQQTRTEVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDEQSAGID 166
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 46578760   593 QITRSIAEIDAVARDNGSLLSEADTAIRGIEDKTGILRGLMA 634
Cdd:pfam00015 167 QVNQAVARIDQVTQQNAALVEESAAAAETLEEQAEELTASVA 208
PRK15041 PRK15041
methyl-accepting chemotaxis protein I; Provisional
342-629 1.45e-23

methyl-accepting chemotaxis protein I; Provisional


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 103.88  E-value: 1.45e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46578760  342 ADEMARVALASREGMSSTAVRLGEVTTDLD---TDSHRLAALSGSINSGSGIQLQRVGETATAMSQMNATVLDVAHSAAG 418
Cdd:PRK15041 246 SNEMGQLAESLRHMQGELMRTVGDVRNGANaiySGASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVKQNAENARQ 325
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46578760  419 AAEQTALTRDKAREG---VDSVKATldamqsldtvatgladdMRKLDAQSAAIDKVVNVINDIADQTNLLALNAAIEAAR 495
Cdd:PRK15041 326 ASHLALSASETAQRGgkvVDNVVQT-----------------MRDISTSSQKIADIISVIDGIAFQTNILALNAAVEAAR 388
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46578760  496 AGEAGRGFAVVADEVRKLAEKTMQATgevgitvRNIQTLTRSNVASMEDALKAIRAAAErsgqsaaTLGEILRMTDAAAA 575
Cdd:PRK15041 389 AGEQGRGFAVVAGEVRNLAQRSAQAA-------REIKSLIEDSVGKVDVGSTLVESAGE-------TMAEIVSAVTRVTD 454
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 46578760  576 QVQAIAAAAEEQSAASEQITRSIAEIDAVARDNGSLLSEADTAIRGIEDKTGIL 629
Cdd:PRK15041 455 IMGEIASASDEQSRGIDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRL 508
COG4564 COG4564
Signal transduction histidine kinase [Signal transduction mechanisms]
44-233 2.67e-14

Signal transduction histidine kinase [Signal transduction mechanisms]


Pssm-ID: 226930 [Multi-domain]  Cd Length: 459  Bit Score: 74.09  E-value: 2.67e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46578760  44 SIATRMTALFTVMALCIVCIVAAFYGTIARVTAAGVSTSQTMLLDEQK---NRIQSITHSTALSLEvltarvQTDEEKLA 120
Cdd:COG4564  11 ALLPLLIAILSITAIITHQSKTLAQREIEIFEANMLEAKETELLNLVNlalSAIRLVYNNAGPSDE------AAKQEVKA 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46578760 121 IIADAiekaRFESDnsGYFFVY--TGTvNAAHPTQKQLIGKDLGNTTDREGVYYVRELARVAASGGGFVTFVFPKPGKGD 198
Cdd:COG4564  85 ILTNL----DYGSD--GYFFVYdyQGT-NLVHPRQPELVGQNLWQLTDPRGDRVIQALIAKAQEGGGLHQYLWEKPSSHE 157
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 46578760 199 L-SKLGYAEAIPGTRYWIGTGIYIDNIDAARETLHA 233
Cdd:COG4564 158 TvDKLSYAAGLDKWEWMIGTGLYLDDVSAETAAAQA 193
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
267-336 2.34e-06

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


Pssm-ID: 234070 [Multi-domain]  Cd Length: 968  Bit Score: 49.39  E-value: 2.34e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46578760   267 RSIVRPLAAATHAATRITAGELDITLDTSGRDEAATLQRALAdmvtTLRDNfAALHAKEAEAQRQTQSAL 336
Cdd:TIGR02956 354 RSVILRLNQHTQALLRLALGDLDISLDARGDDELAHMGRAIE----AFRDT-AAHNLKLQADERQVAQEL 418
 
Name Accession Description Interval E-value
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
269-316 6.08e-06

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: 44.16  E-value: 6.08e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 46578760 269 IVRPLAAATHAATRITAGELDITLDTSGRDEAATLQRALADMVTTLRD 316
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGDLDVRLPVTGRDEIGELARAFNQMAERLRE 48
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
404-602 4.04e-43

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: 153.93  E-value: 4.04e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46578760 404 QMNATVLDVAHSAAGAAEQTALTRDKAREGVDSVKATLDAMQSLDTVATGLADDMRKLDAQSAAIDKVVNVINDIADQTN 483
Cdd:cd11386   2 ELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQTN 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46578760 484 LLALNAAIEAARAGEAGRGFAVVADEVRKLAEKTMQATGEVGITVRNIQTLTRSNVASMEDALKAIRAAAERSGQSAATL 563
Cdd:cd11386  82 LLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRAF 161
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 46578760 564 GEILRMTDAAAAQVQAIAAAAEEQSAASEQITRSIAEID 602
Cdd:cd11386 162 EEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
Cache_2 smart01049
Cache is an extracellular domain that is predicted to have a role in small-molecule ...
86-173 1.18e-13

Cache is an extracellular domain that is predicted to have a role in small-molecule recognition in a wide range of proteins; Members include the animal dihydropyridine-sensitive voltage-gated Ca2+ channel; alpha-2delta subunit, and various bacterial chemotaxis receptors. The name Cache comes from CAlcium channels and CHEmotaxis receptors. This domain consists of an N-terminal part with three predicted strands and an alpha-helix, and a C-terminal part with a strand dyad followed by a relatively unstructured region. The N-terminal portion of the (unpermuted) Cache domain contains three predicted strands that could form a sheet analogous to that present in the core of the PAS domain structure. Cache domains are particularly widespread in bacteria, with Vibrio cholerae. The animal calcium channel alpha-2delta subunits might have acquired a part of their extracellular domains from a bacterial source. The Cache domain appears to have arisen from the GAF-PAS fold despite their divergent functions.


Pssm-ID: 214995  Cd Length: 91  Bit Score: 67.67  E-value: 1.18e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46578760     86 LLDEQKNRIQSITHSTALSLEVLTARVQ----TDEEKLAIIADAIEKARFesDNSGYFFVYTGT-VNAAHPTQKQLIGKD 160
Cdd:smart01049   1 LLEERKAELKNLVEIAVSIVEAYYAQAAagklTEEEAQAQAKAALRALRY--GGDGYFFVYDSDgVMLMHPAKPELEGKN 78
                           90
                   ....*....|...
gi 46578760    161 LGNTTDREGVYYV 173
Cdd:smart01049  79 LSDLKDPNGKYLF 91
Cache_2 pfam08269
Cache domain;
86-174 1.40e-08

Cache domain;


Pssm-ID: 254697  Cd Length: 95  Bit Score: 52.69  E-value: 1.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46578760    86 LLDEQKNRIQSITHSTALSLEVLTARVQ----TDEEKLAIIADAIEKARFESDnsGYFFVY-TGTVNAAHPTQKQLIGKD 160
Cdd:pfam08269   4 LIEERKAELKAVVESALSIIKEYYQQAQkgklTREEAQAQAKALLRALRYDGD--GYFFAYdSNGTNVMHPIKPELVGKN 81
                          90
                  ....*....|....
gi 46578760   161 LGNTTDREGVYYVR 174
Cdd:pfam08269  82 LSNLKDPNGNNVFV 95
HAMP pfam00672
HAMP domain;
261-316 1.83e-06

HAMP domain;


Pssm-ID: 250044  Cd Length: 70  Bit Score: 46.07  E-value: 1.83e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 46578760   261 AAMALTRSIVRPLAAATHAATRITAGELDITLDTSGRDEAATLQRALADMVTTLRD 316
Cdd:pfam00672  15 LAWLLARRLLRPLRRLAEAARRIASGDLDDRVPVSGPDEIGELARAFNQMADRLRE 70
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
267-316 6.71e-06

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


Pssm-ID: 197640  Cd Length: 53  Bit Score: 44.16  E-value: 6.71e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 46578760    267 RSIVRPLAAATHAATRITAGELDITLDTSGRDEAATLQRALADMVTTLRD 316
Cdd:smart00304   1 RRLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRLEE 50
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
378-634 7.82e-51

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


Pssm-ID: 214599 [Multi-domain]  Cd Length: 262  Bit Score: 177.48  E-value: 7.82e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46578760    378 AALSGSINSGSGIQLQRVGETATAMSQMNATVLDVAHSAAGAAEQTALTRDKAREGVDSVKATLDAMQSLDTVATGLADD 457
Cdd:smart00283   3 SEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAVSA 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46578760    458 MRKLDAQSAAIDKVVNVINDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAEKTMQATGEVGITVRNIQTLTRS 537
Cdd:smart00283  83 VEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEETNE 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46578760    538 NVASMEDALKAIRAAAERSGQSAATLGEILRMTDAAAAQVQAIAAAAEEQSAASEQITRSIAEIDAVARDNGSLLSEADT 617
Cdd:smart00283 163 AVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEISA 242
                          250
                   ....*....|....*..
gi 46578760    618 AIRGIEDKTGILRGLMA 634
Cdd:smart00283 243 AAEELSGLAEELDELVE 259
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction ...
261-637 2.68e-45

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


Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 165.93  E-value: 2.68e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46578760 261 AAMALTRSIVRPLAAATHAATRITAGELDITLDTSGRDEAATLQRALADMVTTLRDnfaalhakeaeaqrqtqsaleaaa 340
Cdd:COG0840  76 LAILLLRAILEPISDLLEVVERIAAGDLTKRIDESSNDEFGQLAKSFNEMILNLRQ------------------------ 131
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46578760 341 rademarvalasregmssTAVRLGEVTTDLDTDSHRLAALSGSINSGSGIQLQRVGETATAMSQMNATVLDVAHSAAGAA 420
Cdd:COG0840 132 ------------------IIDAVQDNAEALSGASEEIAASATELSARADQQAESLEEVASAIEELSETVKEVAFNAKEAA 193
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46578760 421 EQTALTRDKAREGVDSVKATLDAMQSldtVATGLADDMRKLDAQSAAIDKVVNVINDIADQTNLLALNAAIEAARAGEAG 500
Cdd:COG0840 194 ALASEASQVAEEGGEEVRQAVEQMQE---IAEELAEVVKKLSESSQEIEEITSVINSIAEQTNLLALNAAIEAARAGEAG 270
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46578760 501 RGFAVVADEVRKLAEKTMQATGEVGITVRNIQTLTRSNVASMEDALKAIRAAAERSGQSAATLGEILRMTDAAAAQVQAI 580
Cdd:COG0840 271 RGFAVVADEVRKLAERSADSAKEIGLLIEEIQNEAADAVEHMEESASEVSEGVKLVEETGSSLGEIAAAIEEVSQLISEI 350
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 46578760 581 AAAAEEQSAASEQITRSIAEIDAVARDNGSLLSEADTAIRGIEDKTGILRGLMADLN 637
Cdd:COG0840 351 AAATEEQTAVLEEINASIEELDDVTQENAAAVEELAAASEELKELAEKLLELVAKFK 407
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
433-634 1.61e-34

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: 130.26  E-value: 1.61e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46578760   433 GVDSVKATLDAMQSLDTVATGLADDMRKLDAQSAAIDKVVNVINDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRK 512
Cdd:pfam00015   7 AQLASEEALDEMSQIGQVVDDAVETMEELETSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46578760   513 LAEKTMQATGEVGITVRNIQTLTRSNVASMEDALKAIRAAAERSGQSAATLGEILRMTDAAAAQVQAIAAAAEEQSAASE 592
Cdd:pfam00015  87 LAERSAQAAKEIEALIEEIVKQTNDSTASIQQTRTEVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDEQSAGID 166
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 46578760   593 QITRSIAEIDAVARDNGSLLSEADTAIRGIEDKTGILRGLMA 634
Cdd:pfam00015 167 QVNQAVARIDQVTQQNAALVEESAAAAETLEEQAEELTASVA 208
PRK15041 PRK15041
methyl-accepting chemotaxis protein I; Provisional
342-629 1.45e-23

methyl-accepting chemotaxis protein I; Provisional


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 103.88  E-value: 1.45e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46578760  342 ADEMARVALASREGMSSTAVRLGEVTTDLD---TDSHRLAALSGSINSGSGIQLQRVGETATAMSQMNATVLDVAHSAAG 418
Cdd:PRK15041 246 SNEMGQLAESLRHMQGELMRTVGDVRNGANaiySGASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVKQNAENARQ 325
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46578760  419 AAEQTALTRDKAREG---VDSVKATldamqsldtvatgladdMRKLDAQSAAIDKVVNVINDIADQTNLLALNAAIEAAR 495
Cdd:PRK15041 326 ASHLALSASETAQRGgkvVDNVVQT-----------------MRDISTSSQKIADIISVIDGIAFQTNILALNAAVEAAR 388
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46578760  496 AGEAGRGFAVVADEVRKLAEKTMQATgevgitvRNIQTLTRSNVASMEDALKAIRAAAErsgqsaaTLGEILRMTDAAAA 575
Cdd:PRK15041 389 AGEQGRGFAVVAGEVRNLAQRSAQAA-------REIKSLIEDSVGKVDVGSTLVESAGE-------TMAEIVSAVTRVTD 454
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 46578760  576 QVQAIAAAAEEQSAASEQITRSIAEIDAVARDNGSLLSEADTAIRGIEDKTGIL 629
Cdd:PRK15041 455 IMGEIASASDEQSRGIDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRL 508
PRK09793 PRK09793
methyl-accepting protein IV; Provisional
377-637 4.87e-23

methyl-accepting protein IV; Provisional


Pssm-ID: 182079 [Multi-domain]  Cd Length: 533  Bit Score: 102.07  E-value: 4.87e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46578760  377 LAALSGSINSGSGIQLQRVGETATAMSQMNATV---LDVAHSAAGAAEQTALTrdkAREGVDSvkatldamqsldtvATG 453
Cdd:PRK09793 280 IVAGNNDLSSRTEQQAASLAQTAASMEQLTATVgqnADNARQASELAKNAATT---AQAGGVQ--------------VST 342
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46578760  454 LADDMRKLDAQSAAIDKVVNVINDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAEKTMQATGEVGITVrniqt 533
Cdd:PRK09793 343 MTHTMQEIATSSQKIGDIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKGLI----- 417
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46578760  534 ltrsnvasmEDALKAIRAAAERSGQSAATLGEILRMTDAAAAQVQAIAAAAEEQSAASEQITRSIAEIDAVARDNGSLLS 613
Cdd:PRK09793 418 ---------EESVNRVQQGSKLVNNAAATMTDIVSSVTRVNDIMGEIASASEEQRRGIEQVAQAVSQMDQVTQQNASLVE 488
                        250       260
                 ....*....|....*....|....
gi 46578760  614 EADTAIRGIEDKTGILRGLMADLN 637
Cdd:PRK09793 489 EAAVATEQLANQADHLSSRVAVFT 512
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
267-629 4.96e-23

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 102.01  E-value: 4.96e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46578760  267 RSIVRPLAAATHAATRITAGELDITLDTSGRDEAATLQRALADMVTTLRDNFAALhakeaeaqRQTQSALEAAARADEMA 346
Cdd:PRK15048 214 RMLLTPLAKIIAHIREIAGGNLANTLTIDGRSEMGDLAQSVSHMQRSLTDTVTHV--------REGSDAIYAGTREIAAG 285
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46578760  347 RVALASREGMSSTAVRlgevttdldtdshrlaalsgsinsgsgiqlqrvgETATAMSQMNATVLDVAHSAAGAAEQTALT 426
Cdd:PRK15048 286 NTDLSSRTEQQASALE----------------------------------ETAASMEQLTATVKQNADNARQASQLAQSA 331
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46578760  427 RDKAREGvdsvkatldamqslDTVATGLADDMRKLDAQSAAIDKVVNVINDIADQTNLLALNAAIEAARAGEAGRGFAVV 506
Cdd:PRK15048 332 SDTAQHG--------------GKVVDGVVKTMHEIADSSKKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVV 397
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46578760  507 ADEVRKLAEKTMQATGEVGI----TVRNIQT---LTRSNVASMEDALKAIRAAAERSGQSAATLGEILRMTDaaaaqvqa 579
Cdd:PRK15048 398 AGEVRNLASRSAQAAKEIKAliedSVSRVDTgsvLVESAGETMNNIVNAVTRVTDIMGEIASASDEQSRGID-------- 469
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 46578760  580 iaaaaeeqsaaseQITRSIAEIDAVARDNGSLLSEADTAIRGIEDKTGIL 629
Cdd:PRK15048 470 -------------QVALAVSEMDRVTQQNASLVQESAAAAAALEEQASRL 506
COG4564 COG4564
Signal transduction histidine kinase [Signal transduction mechanisms]
44-233 2.67e-14

Signal transduction histidine kinase [Signal transduction mechanisms]


Pssm-ID: 226930 [Multi-domain]  Cd Length: 459  Bit Score: 74.09  E-value: 2.67e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46578760  44 SIATRMTALFTVMALCIVCIVAAFYGTIARVTAAGVSTSQTMLLDEQK---NRIQSITHSTALSLEvltarvQTDEEKLA 120
Cdd:COG4564  11 ALLPLLIAILSITAIITHQSKTLAQREIEIFEANMLEAKETELLNLVNlalSAIRLVYNNAGPSDE------AAKQEVKA 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46578760 121 IIADAiekaRFESDnsGYFFVY--TGTvNAAHPTQKQLIGKDLGNTTDREGVYYVRELARVAASGGGFVTFVFPKPGKGD 198
Cdd:COG4564  85 ILTNL----DYGSD--GYFFVYdyQGT-NLVHPRQPELVGQNLWQLTDPRGDRVIQALIAKAQEGGGLHQYLWEKPSSHE 157
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 46578760 199 L-SKLGYAEAIPGTRYWIGTGIYIDNIDAARETLHA 233
Cdd:COG4564 158 TvDKLSYAAGLDKWEWMIGTGLYLDDVSAETAAAQA 193
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
267-336 2.34e-06

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


Pssm-ID: 234070 [Multi-domain]  Cd Length: 968  Bit Score: 49.39  E-value: 2.34e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46578760   267 RSIVRPLAAATHAATRITAGELDITLDTSGRDEAATLQRALAdmvtTLRDNfAALHAKEAEAQRQTQSAL 336
Cdd:TIGR02956 354 RSVILRLNQHTQALLRLALGDLDISLDARGDDELAHMGRAIE----AFRDT-AAHNLKLQADERQVAQEL 418
NarQ COG3850
Signal transduction histidine kinase, nitrate/nitrite-specific [Signal transduction mechanisms]
265-334 4.25e-04

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


Pssm-ID: 226368 [Multi-domain]  Cd Length: 574  Bit Score: 41.95  E-value: 4.25e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46578760 265 LTRSIVRPLAAATHAATRITAGELDITLDTSGRDEAATLQRALADMVTTLRDNFAALhakEAEAQRQTQS 334
Cdd:COG3850 171 LRRRVVRPLNQLTSAAQRIGRRQFDQRPTDTGRNELGLLGRAFNQMSGELKKLYADL---EQRVEEKTRD 237
NtrY COG5000
Signal transduction histidine kinase involved in nitrogen fixation and metabolism regulation ...
262-330 1.25e-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: 1.25e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46578760 262 AMALTRSIVRPLAAATHAATRITAGELDITLDTSGRDE-AATLQRALADMVTTLRDNFAAL-HAKEAEAQR 330
Cdd:COG5000 298 AIAFARRIVRPIRKLIEAADEVADGDLDVQVPVRRVDEdVGRLSKAFNKMTEQLSSQQEALeRAKDALEQR 368
TIGR02680 TIGR02680
TIGR02680 family protein; Members of this protein family belong to a conserved gene four-gene ...
274-432 2.02e-03

TIGR02680 family protein; Members of this protein family belong to a conserved gene four-gene neighborhood found sporadically in a phylogenetically broad range of bacteria: Nocardia farcinica, Symbiobacterium thermophilum, and Streptomyces avermitilis (Actinobacteria), Geobacillus kaustophilus (Firmicutes), Azoarcus sp. EbN1 and Ralstonia solanacearum (Betaproteobacteria). Proteins in this family average over 1400 amino acids in length [Hypothetical proteins, Conserved].


Pssm-ID: 233973 [Multi-domain]  Cd Length: 1353  Bit Score: 40.18  E-value: 2.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46578760    274 AAATHAATRITAGELDITLDTSGrDEAATLQRALAdMVTTLRDNFAAL-------------HAKEAEAQRQTQSALEAAA 340
Cdd:TIGR02680  733 AAARERARLRRIAELDARLAAVD-DELAELARELR-ALGARQRALADElagapsdrslraaHRRAAEAERQAESAERELA 810
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46578760    341 RADEMARVALASREGMSSTAVRLGEvTTDLDTDSHRLAALsgsinsgsGIQLQRVGETATAMSQMNATVLDVAHSAAGAA 420
Cdd:TIGR02680  811 RAARKAAAAAAAWKQARRELERDAA-DLDLPTDPDALEAV--------GLALKRFGDHLHTLEVAVRELRHAATRAAEQR 881
                          170
                   ....*....|..
gi 46578760    421 EQTALTRDKARE 432
Cdd:TIGR02680  882 ARAARAESDARE 893
 
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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