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Conserved domains on  [gi|86160313|ref|YP_467098|]
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methyl-accepting chemotaxis sensory transducer [Anaeromyxobacter dehalogenans 2CP-C]

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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. ...
214-261 5.76e-08

Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established.


:

Pssm-ID: 100122  Cd Length: 48  Bit Score: 49.94  E-value: 5.76e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 86160313 214 ITVPLRATVVHAERIARGDLREEVEVTGRDEIGQLEQAMQAMTEKLAE 261
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGDLDVRLPVTGRDEIGELARAFNQMAERLRE 48
MCP_signal super family cl21547
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
293-477 5.30e-38

Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis proteins (MCPs or chemotaxis receptors) are an integral part of the transmembrane protein complex that controls bacterial chemotaxis, together with the histidine kinase CheA, the receptor-coupling protein CheW, receptor-modification enzymes, and localized phosphatases. MCPs contain a four helix trans membrane region, an N-terminal periplasmic ligand binding domain, and a C-terminal HAMP domain followed by a cytoplasmic signaling domain. This C-terminal signaling domain dimerizes into a four-helix bundle and interacts with CheA through the adaptor protein CheW.


The actual alignment was detected with superfamily member cd11386:

Pssm-ID: 206779  Cd Length: 200  Bit Score: 138.52  E-value: 5.30e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313 293 EQAASVEETTSSLEEMSASITQNAENSRQTEAVALEGARNAQESGEAVRRSVEAMRTIAEK-------ISIIEEIAYQTN 365
Cdd:cd11386   2 ELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESsaeigeiVEVIDDIAEQTN 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313 366 LLALNAAIEAARAGEHGRGFAVVATEVRKLAERAQKSAGEIGALAGS-------SVEVAERSGALLAELVPAIRKTSDLV 438
Cdd:cd11386  82 LLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEiqeqteeAVEAMEETSEEVEEGVELVEETGRAF 161
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 86160313 439 QEVAAASREQSTGVRQVTKAMGVVDQVTQRNASAAEELS 477
Cdd:cd11386 162 EEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction ...
144-499 1.91e-59

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


:

Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 204.45  E-value: 1.91e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313 144 VRATDLQQLISARADLQGAWQRLAGLETERVREAAGAAQADAAVVRLWIYAGLTLAGTLVILASVTLTRSITVPLRATVV 223
Cdd:COG0840  14 LAAGEADAGLLKLKKLIDELGKLLLSLNLILDDAASAEAAALKAVLKFLLISLLVAIIVVLVLAILLLRAILEPISDLLE 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313 224 HAERIARGDLREEVEVTGRDEIGQLEQAMQAMTEKLAEVIGEVRGSTDALTSASQQLSATAQNVSQGTGEQAASVEETTS 303
Cdd:COG0840  94 VVERIAAGDLTKRIDESSNDEFGQLAKSFNEMILNLRQIIDAVQDNAEALSGASEEIAASATELSARADQQAESLEEVAS 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313 304 SLEEMSASITQNAENSRQTEAVALEGARNAQESGEAVRRSVEAMRTIAEK------------------ISIIEEIAYQTN 365
Cdd:COG0840 174 AIEELSETVKEVAFNAKEAAALASEASQVAEEGGEEVRQAVEQMQEIAEElaevvkklsessqeieeiTSVINSIAEQTN 253
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313 366 LLALNAAIEAARAGEHGRGFAVVATEVRKLAERAQKSAGEIGAL---------------------AGSSVEVAERSGALL 424
Cdd:COG0840 254 LLALNAAIEAARAGEAGRGFAVVADEVRKLAERSADSAKEIGLLieeiqneaadavehmeesaseVSEGVKLVEETGSSL 333
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 86160313 425 AELVPAIRKTSDLVQEVAAASREQSTGVRQVTKAMGVVDQVTQRNASAAEELSSTAEEMSSQAEALQQLVAFFRV 499
Cdd:COG0840 334 GEIAAAIEEVSQLISEIAAATEEQTAVLEEINASIEELDDVTQENAAAVEELAAASEELKELAEKLLELVAKFKL 408
 
Name Accession Description Interval E-value
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
214-261 5.76e-08

Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established.


Pssm-ID: 100122  Cd Length: 48  Bit Score: 49.94  E-value: 5.76e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 86160313 214 ITVPLRATVVHAERIARGDLREEVEVTGRDEIGQLEQAMQAMTEKLAE 261
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGDLDVRLPVTGRDEIGELARAFNQMAERLRE 48
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
293-477 5.30e-38

Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis proteins (MCPs or chemotaxis receptors) are an integral part of the transmembrane protein complex that controls bacterial chemotaxis, together with the histidine kinase CheA, the receptor-coupling protein CheW, receptor-modification enzymes, and localized phosphatases. MCPs contain a four helix trans membrane region, an N-terminal periplasmic ligand binding domain, and a C-terminal HAMP domain followed by a cytoplasmic signaling domain. This C-terminal signaling domain dimerizes into a four-helix bundle and interacts with CheA through the adaptor protein CheW.


Pssm-ID: 206779  Cd Length: 200  Bit Score: 138.52  E-value: 5.30e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313 293 EQAASVEETTSSLEEMSASITQNAENSRQTEAVALEGARNAQESGEAVRRSVEAMRTIAEK-------ISIIEEIAYQTN 365
Cdd:cd11386   2 ELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESsaeigeiVEVIDDIAEQTN 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313 366 LLALNAAIEAARAGEHGRGFAVVATEVRKLAERAQKSAGEIGALAGS-------SVEVAERSGALLAELVPAIRKTSDLV 438
Cdd:cd11386  82 LLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEiqeqteeAVEAMEETSEEVEEGVELVEETGRAF 161
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 86160313 439 QEVAAASREQSTGVRQVTKAMGVVDQVTQRNASAAEELS 477
Cdd:cd11386 162 EEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
HAMP pfam00672
HAMP domain;
192-261 4.54e-09

HAMP domain;


Pssm-ID: 250044  Cd Length: 70  Bit Score: 53.39  E-value: 4.54e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313   192 IYAGLTLAGTLVILASVTLTRSITVPLRATVVHAERIARGDLREEVEVTGRDEIGQLEQAMQAMTEKLAE 261
Cdd:pfam00672   1 LLLVLLIALLLLLLLAWLLARRLLRPLRRLAEAARRIASGDLDDRVPVSGPDEIGELARAFNQMADRLRE 70
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
212-264 5.97e-08

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


Pssm-ID: 197640  Cd Length: 53  Bit Score: 49.94  E-value: 5.97e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 86160313    212 RSITVPLRATVVHAERIARGDLREEVEVTGRDEIGQLEQAMQAMTEKLAEVIG 264
Cdd:smart00304   1 RRLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRLEETIA 53
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction ...
144-499 1.91e-59

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


Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 204.45  E-value: 1.91e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313 144 VRATDLQQLISARADLQGAWQRLAGLETERVREAAGAAQADAAVVRLWIYAGLTLAGTLVILASVTLTRSITVPLRATVV 223
Cdd:COG0840  14 LAAGEADAGLLKLKKLIDELGKLLLSLNLILDDAASAEAAALKAVLKFLLISLLVAIIVVLVLAILLLRAILEPISDLLE 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313 224 HAERIARGDLREEVEVTGRDEIGQLEQAMQAMTEKLAEVIGEVRGSTDALTSASQQLSATAQNVSQGTGEQAASVEETTS 303
Cdd:COG0840  94 VVERIAAGDLTKRIDESSNDEFGQLAKSFNEMILNLRQIIDAVQDNAEALSGASEEIAASATELSARADQQAESLEEVAS 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313 304 SLEEMSASITQNAENSRQTEAVALEGARNAQESGEAVRRSVEAMRTIAEK------------------ISIIEEIAYQTN 365
Cdd:COG0840 174 AIEELSETVKEVAFNAKEAAALASEASQVAEEGGEEVRQAVEQMQEIAEElaevvkklsessqeieeiTSVINSIAEQTN 253
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313 366 LLALNAAIEAARAGEHGRGFAVVATEVRKLAERAQKSAGEIGAL---------------------AGSSVEVAERSGALL 424
Cdd:COG0840 254 LLALNAAIEAARAGEAGRGFAVVADEVRKLAERSADSAKEIGLLieeiqneaadavehmeesaseVSEGVKLVEETGSSL 333
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 86160313 425 AELVPAIRKTSDLVQEVAAASREQSTGVRQVTKAMGVVDQVTQRNASAAEELSSTAEEMSSQAEALQQLVAFFRV 499
Cdd:COG0840 334 GEIAAAIEEVSQLISEIAAATEEQTAVLEEINASIEELDDVTQENAAAVEELAAASEELKELAEKLLELVAKFKL 408
PRK15041 PRK15041
methyl-accepting chemotaxis protein I; Provisional
190-518 1.64e-68

methyl-accepting chemotaxis protein I; Provisional


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 232.54  E-value: 1.64e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313  190 LWIYAGLTLAGTLVILAS-VTLTRSITVPLRATVVHAERIARGDLREEVEVTGRDEIGQLEQAMQAMTEKLAEVIGEVRG 268
Cdd:PRK15041 193 MWILVGVMIVVLAVIFAVwFGIKASLVAPMNRLIDSIRHIAGGDLVKPIEVDGSNEMGQLAESLRHMQGELMRTVGDVRN 272
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313  269 STDALTSASQQLSATAQNVSQGTGEQAASVEETTSSLEEMSASITQNAENSRQTEAVALEGARNAQESGEAVRRSVEAMR 348
Cdd:PRK15041 273 GANAIYSGASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQTMR 352
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313  349 -------TIAEKISIIEEIAYQTNLLALNAAIEAARAGEHGRGFAVVATEVRKLAERAQKSAGEIGALAGSSVE------ 415
Cdd:PRK15041 353 distssqKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGkvdvgs 432
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313  416 -VAERSGALLAELVPAIRKTSDLVQEVAAASREQSTGVRQVTKAMGVVDQVTQRNASAAEELSSTAEEMSSQAEALQQLV 494
Cdd:PRK15041 433 tLVESAGETMAEIVSAVTRVTDIMGEIASASDEQSRGIDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRLTEAV 512
                        330       340
                 ....*....|....*....|....
gi 86160313  495 AFFRVREVHAPARPRPPLAAPRLP 518
Cdd:PRK15041 513 AVFRIQQQQQQQRETSAVVKTVTP 536
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
265-498 1.64e-48

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: 170.16  E-value: 1.64e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313    265 EVRGSTDALTSASQQLSATAQNVSQGTGEQAASVEETTSSLEEMSASITQNAENSRQTEAVALEGARNAQESGEAVRRSV 344
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313    345 EAMRTIAEK-------ISIIEEIAYQTNLLALNAAIEAARAGEHGRGFAVVATEVRKLAERAQKSAGEIGALAG------ 411
Cdd:smart00283  81 SAVEELEESsdeigeiVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKeiqeet 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313    412 ---------------SSVEVAERSGALLAELVPAIRKTSDLVQEVAAASREQSTGVRQVTKAMGVVDQVTQRNASAAEEL 476
Cdd:smart00283 161 neavaameessseveEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240
                          250       260
                   ....*....|....*....|..
gi 86160313    477 SSTAEEMSSQAEALQQLVAFFR 498
Cdd:smart00283 241 SAAAEELSGLAEELDELVERFK 262
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
329-499 6.86e-35

Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to transduce the signal to CheA since it is highly conserved in very diverse MCPs.


Pssm-ID: 249510 [Multi-domain]  Cd Length: 213  Bit Score: 130.26  E-value: 6.86e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313   329 GARNAQESGEAVRRSVEAMRTIAEKISIIEEIAYQTNLLALNAAIEAARAGEHGRGFAVVATEVRKLAERAQKSAGEIGA 408
Cdd:pfam00015  21 IGQVVDDAVETMEELETSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLAERSAQAAKEIEA 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313   409 LAGSSV---------------------EVAERSGALLAELVPAIRKTSDLVQEVAAASREQSTGVRQVTKAMGVVDQVTQ 467
Cdd:pfam00015 101 LIEEIVkqtndstasiqqtrtevevgsTIVESTGEALKEIVDAVAEIADIVQEIAAASDEQSAGIDQVNQAVARIDQVTQ 180
                         170       180       190
                  ....*....|....*....|....*....|..
gi 86160313   468 RNASAAEELSSTAEEMSSQAEALQQLVAFFRV 499
Cdd:pfam00015 181 QNAALVEESAAAAETLEEQAEELTASVAQFRI 212
PTZ00121 PTZ00121
MAEBL; Provisional
240-492 5.51e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 57.84  E-value: 5.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313   240 TGRDEIGQLEQAMQAMTEKlaevIGEVRGSTDALTSASQqlSATAQNVSQGtgEQAASVEETTSSLEEMSASITQNAENS 319
Cdd:PTZ00121 1092 ATEEAFGKAEEAKKTETGK----AEEARKAEEAKKKAED--ARKAEEARKA--EDARKAEEARKAEDAKRVEIARKAEDA 1163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313   320 RQTE-AVALEGARNAQES--GEAVRRSVEAMRtiAEKISIIEEIAYQTNLlalnAAIEAARAGEHGRGFAVV--ATEVRK 394
Cdd:PTZ00121 1164 RKAEeARKAEDAKKAEAArkAEEVRKAEELRK--AEDARKAEAARKAEEE----RKAEEARKAEDAKKAEAVkkAEEAKK 1237
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313   395 LAERAQKSAGEIGALAGSSVE------VAERSGALLAElvpAIRKTSDL--VQEVAAASR-EQSTGVRQVTKAMGVVDQv 465
Cdd:PTZ00121 1238 DAEEAKKAEEERNNEEIRKFEearmahFARRQAAIKAE---EARKADELkkAEEKKKADEaKKAEEKKKADEAKKKAEE- 1313
                         250       260
                  ....*....|....*....|....*..
gi 86160313   466 tqrnASAAEELSSTAEEMSSQAEALQQ 492
Cdd:PTZ00121 1314 ----AKKADEAKKKAEEAKKKADAAKK 1336
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
228-495 2.53e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins].


Pssm-ID: 233757 [Multi-domain]  Cd Length: 1179  Bit Score: 42.74  E-value: 2.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313    228 IARGDLREEVEVTGRD-EIGQLEQAMQAMTEKLAE---VIGEVRGSTDALTSASQQLSATAQNVSQ---GTGEQAASVEE 300
Cdd:TIGR02168  661 ITGGSAKTNSSILERRrEIEELEEKIEELEEKIAElekALAELRKELEELEEELEQLRKELEELSRqisALRKDLARLEA 740
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313    301 TTSSLEEMSASIT---QNAENSRQTEAVALEGARNAQESGEAVRRSVEA-MRTIAEKISIIEEI--AYQTNLLALNAAIE 374
Cdd:TIGR02168  741 EVEQLEERIAQLSkelTELEAEIEELEERLEEAEEELAEAEAEIEELEAqIEQLKEELKALREAldELRAELTLLNEEAA 820
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313    375 AARAGEHGRGFAVVATEVRklAERAQKSAGEIGALAGSSVEVAERSGALLAELVPAIRKTSDLVQEVAAASREQSTGVRQ 454
Cdd:TIGR02168  821 NLRERLESLERRIAATERR--LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEE 898
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 86160313    455 VTKAMGVVDQVTQRNASAAEELSSTAEEMSSQAEALQQLVA 495
Cdd:TIGR02168  899 LSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRID 939
 
Name Accession Description Interval E-value
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
214-261 5.76e-08

Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established.


Pssm-ID: 100122  Cd Length: 48  Bit Score: 49.94  E-value: 5.76e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 86160313 214 ITVPLRATVVHAERIARGDLREEVEVTGRDEIGQLEQAMQAMTEKLAE 261
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGDLDVRLPVTGRDEIGELARAFNQMAERLRE 48
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
293-477 5.30e-38

Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis proteins (MCPs or chemotaxis receptors) are an integral part of the transmembrane protein complex that controls bacterial chemotaxis, together with the histidine kinase CheA, the receptor-coupling protein CheW, receptor-modification enzymes, and localized phosphatases. MCPs contain a four helix trans membrane region, an N-terminal periplasmic ligand binding domain, and a C-terminal HAMP domain followed by a cytoplasmic signaling domain. This C-terminal signaling domain dimerizes into a four-helix bundle and interacts with CheA through the adaptor protein CheW.


Pssm-ID: 206779  Cd Length: 200  Bit Score: 138.52  E-value: 5.30e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313 293 EQAASVEETTSSLEEMSASITQNAENSRQTEAVALEGARNAQESGEAVRRSVEAMRTIAEK-------ISIIEEIAYQTN 365
Cdd:cd11386   2 ELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESsaeigeiVEVIDDIAEQTN 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313 366 LLALNAAIEAARAGEHGRGFAVVATEVRKLAERAQKSAGEIGALAGS-------SVEVAERSGALLAELVPAIRKTSDLV 438
Cdd:cd11386  82 LLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEiqeqteeAVEAMEETSEEVEEGVELVEETGRAF 161
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 86160313 439 QEVAAASREQSTGVRQVTKAMGVVDQVTQRNASAAEELS 477
Cdd:cd11386 162 EEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
HAMP pfam00672
HAMP domain;
192-261 4.54e-09

HAMP domain;


Pssm-ID: 250044  Cd Length: 70  Bit Score: 53.39  E-value: 4.54e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313   192 IYAGLTLAGTLVILASVTLTRSITVPLRATVVHAERIARGDLREEVEVTGRDEIGQLEQAMQAMTEKLAE 261
Cdd:pfam00672   1 LLLVLLIALLLLLLLAWLLARRLLRPLRRLAEAARRIASGDLDDRVPVSGPDEIGELARAFNQMADRLRE 70
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
212-264 5.97e-08

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


Pssm-ID: 197640  Cd Length: 53  Bit Score: 49.94  E-value: 5.97e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 86160313    212 RSITVPLRATVVHAERIARGDLREEVEVTGRDEIGQLEQAMQAMTEKLAEVIG 264
Cdd:smart00304   1 RRLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRLEETIA 53
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction ...
144-499 1.91e-59

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


Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 204.45  E-value: 1.91e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313 144 VRATDLQQLISARADLQGAWQRLAGLETERVREAAGAAQADAAVVRLWIYAGLTLAGTLVILASVTLTRSITVPLRATVV 223
Cdd:COG0840  14 LAAGEADAGLLKLKKLIDELGKLLLSLNLILDDAASAEAAALKAVLKFLLISLLVAIIVVLVLAILLLRAILEPISDLLE 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313 224 HAERIARGDLREEVEVTGRDEIGQLEQAMQAMTEKLAEVIGEVRGSTDALTSASQQLSATAQNVSQGTGEQAASVEETTS 303
Cdd:COG0840  94 VVERIAAGDLTKRIDESSNDEFGQLAKSFNEMILNLRQIIDAVQDNAEALSGASEEIAASATELSARADQQAESLEEVAS 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313 304 SLEEMSASITQNAENSRQTEAVALEGARNAQESGEAVRRSVEAMRTIAEK------------------ISIIEEIAYQTN 365
Cdd:COG0840 174 AIEELSETVKEVAFNAKEAAALASEASQVAEEGGEEVRQAVEQMQEIAEElaevvkklsessqeieeiTSVINSIAEQTN 253
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313 366 LLALNAAIEAARAGEHGRGFAVVATEVRKLAERAQKSAGEIGAL---------------------AGSSVEVAERSGALL 424
Cdd:COG0840 254 LLALNAAIEAARAGEAGRGFAVVADEVRKLAERSADSAKEIGLLieeiqneaadavehmeesaseVSEGVKLVEETGSSL 333
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 86160313 425 AELVPAIRKTSDLVQEVAAASREQSTGVRQVTKAMGVVDQVTQRNASAAEELSSTAEEMSSQAEALQQLVAFFRV 499
Cdd:COG0840 334 GEIAAAIEEVSQLISEIAAATEEQTAVLEEINASIEELDDVTQENAAAVEELAAASEELKELAEKLLELVAKFKL 408
PRK15041 PRK15041
methyl-accepting chemotaxis protein I; Provisional
190-518 1.64e-68

methyl-accepting chemotaxis protein I; Provisional


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 232.54  E-value: 1.64e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313  190 LWIYAGLTLAGTLVILAS-VTLTRSITVPLRATVVHAERIARGDLREEVEVTGRDEIGQLEQAMQAMTEKLAEVIGEVRG 268
Cdd:PRK15041 193 MWILVGVMIVVLAVIFAVwFGIKASLVAPMNRLIDSIRHIAGGDLVKPIEVDGSNEMGQLAESLRHMQGELMRTVGDVRN 272
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313  269 STDALTSASQQLSATAQNVSQGTGEQAASVEETTSSLEEMSASITQNAENSRQTEAVALEGARNAQESGEAVRRSVEAMR 348
Cdd:PRK15041 273 GANAIYSGASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQTMR 352
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313  349 -------TIAEKISIIEEIAYQTNLLALNAAIEAARAGEHGRGFAVVATEVRKLAERAQKSAGEIGALAGSSVE------ 415
Cdd:PRK15041 353 distssqKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGkvdvgs 432
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313  416 -VAERSGALLAELVPAIRKTSDLVQEVAAASREQSTGVRQVTKAMGVVDQVTQRNASAAEELSSTAEEMSSQAEALQQLV 494
Cdd:PRK15041 433 tLVESAGETMAEIVSAVTRVTDIMGEIASASDEQSRGIDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRLTEAV 512
                        330       340
                 ....*....|....*....|....
gi 86160313  495 AFFRVREVHAPARPRPPLAAPRLP 518
Cdd:PRK15041 513 AVFRIQQQQQQQRETSAVVKTVTP 536
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
191-519 3.63e-62

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 215.26  E-value: 3.63e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313  191 WIYAGLTLAGTLVILAS-VTLTRSITVPLRATVVHAERIARGDLREEVEVTGRDEIGQLEQAMQAMTEKLAEVIGEVRGS 269
Cdd:PRK15048 192 WQLAVIALVVVLILLVAwYGIRRMLLTPLAKIIAHIREIAGGNLANTLTIDGRSEMGDLAQSVSHMQRSLTDTVTHVREG 271
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313  270 TDALTSASQQLSATAQNVSQGTGEQAASVEETTSSLEEMSASITQNAENSRQTEAVALEGARNAQESGEAVRRSVEAM-- 347
Cdd:PRK15048 272 SDAIYAGTREIAAGNTDLSSRTEQQASALEETAASMEQLTATVKQNADNARQASQLAQSASDTAQHGGKVVDGVVKTMhe 351
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313  348 -----RTIAEKISIIEEIAYQTNLLALNAAIEAARAGEHGRGFAVVATEVRKLAERAQKSAGEIGALAGSSVE------- 415
Cdd:PRK15048 352 iadssKKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKALIEDSVSrvdtgsv 431
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313  416 VAERSGALLAELVPAIRKTSDLVQEVAAASREQSTGVRQVTKAMGVVDQVTQRNASAAEELSSTAEEMSSQAEALQQLVA 495
Cdd:PRK15048 432 LVESAGETMNNIVNAVTRVTDIMGEIASASDEQSRGIDQVALAVSEMDRVTQQNASLVQESAAAAAALEEQASRLTQAVS 511
                        330       340
                 ....*....|....*....|....*..
gi 86160313  496 FFRVRE---VHAPARPRPPLAAPRLPQ 519
Cdd:PRK15048 512 AFRLAAsplTNKPQTPSRPASEQPPAQ 538
PRK09793 PRK09793
methyl-accepting protein IV; Provisional
162-515 1.78e-59

methyl-accepting protein IV; Provisional


Pssm-ID: 182079 [Multi-domain]  Cd Length: 533  Bit Score: 207.62  E-value: 1.78e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313  162 AWQrlagLETERVREAAGAAQADAAVVRLWIYAGLTLAGTLVILASVTLTRSITV-PLRATVVHAERIARGDLREEVEVT 240
Cdd:PRK09793 165 AWQ----LEINHVLEAASAQSQRNYQISALVFISMIIVAAIYISSALWWTRKMIVqPLAIIGSHFDSIAAGNLARPIAVY 240
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313  241 GRDEIGQLEQAMQAMTEKLAEVIGEVRGSTDALTSASQQLSATAQNVSQGTGEQAASVEETTSSLEEMSASITQNAENSR 320
Cdd:PRK09793 241 GRNEITAIFASLKTMQQALRGTVSDVRKGSQEMHIGIAEIVAGNNDLSSRTEQQAASLAQTAASMEQLTATVGQNADNAR 320
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313  321 QTEAVALEGARNAQESGEAVRRSVEAMRTIAEK-------ISIIEEIAYQTNLLALNAAIEAARAGEHGRGFAVVATEVR 393
Cdd:PRK09793 321 QASELAKNAATTAQAGGVQVSTMTHTMQEIATSsqkigdiISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVR 400
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313  394 KLAERAQKSAGEIGALAGSSVEVAERSGAL-------LAELVPAIRKTSDLVQEVAAASREQSTGVRQVTKAMGVVDQVT 466
Cdd:PRK09793 401 NLASRSAQAAKEIKGLIEESVNRVQQGSKLvnnaaatMTDIVSSVTRVNDIMGEIASASEEQRRGIEQVAQAVSQMDQVT 480
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 86160313  467 QRNASAAEELSSTAEEMSSQAEALQQLVAFFRVRE-VHAPARPRPPLAAP 515
Cdd:PRK09793 481 QQNASLVEEAAVATEQLANQADHLSSRVAVFTLEEhEVARHESAQLQIAP 530
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
265-498 1.64e-48

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: 170.16  E-value: 1.64e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313    265 EVRGSTDALTSASQQLSATAQNVSQGTGEQAASVEETTSSLEEMSASITQNAENSRQTEAVALEGARNAQESGEAVRRSV 344
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313    345 EAMRTIAEK-------ISIIEEIAYQTNLLALNAAIEAARAGEHGRGFAVVATEVRKLAERAQKSAGEIGALAG------ 411
Cdd:smart00283  81 SAVEELEESsdeigeiVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKeiqeet 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313    412 ---------------SSVEVAERSGALLAELVPAIRKTSDLVQEVAAASREQSTGVRQVTKAMGVVDQVTQRNASAAEEL 476
Cdd:smart00283 161 neavaameessseveEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240
                          250       260
                   ....*....|....*....|..
gi 86160313    477 SSTAEEMSSQAEALQQLVAFFR 498
Cdd:smart00283 241 SAAAEELSGLAEELDELVERFK 262
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
329-499 6.86e-35

Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to transduce the signal to CheA since it is highly conserved in very diverse MCPs.


Pssm-ID: 249510 [Multi-domain]  Cd Length: 213  Bit Score: 130.26  E-value: 6.86e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313   329 GARNAQESGEAVRRSVEAMRTIAEKISIIEEIAYQTNLLALNAAIEAARAGEHGRGFAVVATEVRKLAERAQKSAGEIGA 408
Cdd:pfam00015  21 IGQVVDDAVETMEELETSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLAERSAQAAKEIEA 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313   409 LAGSSV---------------------EVAERSGALLAELVPAIRKTSDLVQEVAAASREQSTGVRQVTKAMGVVDQVTQ 467
Cdd:pfam00015 101 LIEEIVkqtndstasiqqtrtevevgsTIVESTGEALKEIVDAVAEIADIVQEIAAASDEQSAGIDQVNQAVARIDQVTQ 180
                         170       180       190
                  ....*....|....*....|....*....|..
gi 86160313   468 RNASAAEELSSTAEEMSSQAEALQQLVAFFRV 499
Cdd:pfam00015 181 QNAALVEESAAAAETLEEQAEELTASVAQFRI 212
PTZ00121 PTZ00121
MAEBL; Provisional
240-492 5.51e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 57.84  E-value: 5.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313   240 TGRDEIGQLEQAMQAMTEKlaevIGEVRGSTDALTSASQqlSATAQNVSQGtgEQAASVEETTSSLEEMSASITQNAENS 319
Cdd:PTZ00121 1092 ATEEAFGKAEEAKKTETGK----AEEARKAEEAKKKAED--ARKAEEARKA--EDARKAEEARKAEDAKRVEIARKAEDA 1163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313   320 RQTE-AVALEGARNAQES--GEAVRRSVEAMRtiAEKISIIEEIAYQTNLlalnAAIEAARAGEHGRGFAVV--ATEVRK 394
Cdd:PTZ00121 1164 RKAEeARKAEDAKKAEAArkAEEVRKAEELRK--AEDARKAEAARKAEEE----RKAEEARKAEDAKKAEAVkkAEEAKK 1237
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313   395 LAERAQKSAGEIGALAGSSVE------VAERSGALLAElvpAIRKTSDL--VQEVAAASR-EQSTGVRQVTKAMGVVDQv 465
Cdd:PTZ00121 1238 DAEEAKKAEEERNNEEIRKFEearmahFARRQAAIKAE---EARKADELkkAEEKKKADEaKKAEEKKKADEAKKKAEE- 1313
                         250       260
                  ....*....|....*....|....*..
gi 86160313   466 tqrnASAAEELSSTAEEMSSQAEALQQ 492
Cdd:PTZ00121 1314 ----AKKADEAKKKAEEAKKKADAAKK 1336
Smc COG1196
Chromosome segregation ATPases [Cell division and chromosome partitioning]
242-493 5.44e-05

Chromosome segregation ATPases [Cell division and chromosome partitioning]


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 44.71  E-value: 5.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313  242 RDEIGQLEQAMQAMTEKLAEVIGEVRGSTDALTSASQQLSAtAQNVSQGTGEQAASVEETTSSLEEMsasitqnAENSRQ 321
Cdd:COG1196  245 EEELSRLEEELEELQEELEEAEKEIEELKSELEELREELEE-LQEELLELKEEIEELEGEISLLRER-------LEELEN 316
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313  322 TEAVALEGARNAQESGEAVRRSVEAMRTIAEKISiiEEIAYQTNLLALNAAIEAARAGEHGRGFAVVATEVRKLAERAQK 401
Cdd:COG1196  317 ELEELEERLEELKEKIEALKEELEERETLLEELE--QLLAELEEAKEELEEKLSALLEELEELFEALREELAELEAELAE 394
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313  402 SAGEIGALAGSSVEVAERSGALLAELVPAIRKTSDLVQEVAAASREQSTGVRQVTKAMGVVDQVTQRNASAAEELSSTAE 481
Cdd:COG1196  395 IRNELEELKREIESLEERLERLSERLEDLKEELKELEAELEELQTELEELNEELEELEEQLEELRDRLKELERELAELQE 474
                        250
                 ....*....|..
gi 86160313  482 EMSSQAEALQQL 493
Cdd:COG1196  475 ELQRLEKELSSL 486
NarQ COG3850
Signal transduction histidine kinase, nitrate/nitrite-specific [Signal transduction mechanisms]
189-282 1.40e-04

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


Pssm-ID: 226368 [Multi-domain]  Cd Length: 574  Bit Score: 43.10  E-value: 1.40e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313 189 RLWIYAGLTLAGTLVILASVTLT-----RSITVPLRATVVHAERIARGDLREEVEVTGRDEIGQLEQAMQAMTEKLAEVI 263
Cdd:COG3850 145 KTILLVLVQLAGMLLILLLVVFTiywlrRRVVRPLNQLTSAAQRIGRRQFDQRPTDTGRNELGLLGRAFNQMSGELKKLY 224
                        90       100
                ....*....|....*....|...
gi 86160313 264 GEVRGS----TDALTSASQQLSA 282
Cdd:COG3850 225 ADLEQRveekTRDLEQKNQRLSF 247
NtrY COG5000
Signal transduction histidine kinase involved in nitrogen fixation and metabolism regulation ...
192-290 1.48e-04

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


Pssm-ID: 227333 [Multi-domain]  Cd Length: 712  Bit Score: 43.22  E-value: 1.48e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313 192 IYAGL-TLAGTLVILASVTL----TRSITVPLRATVVHAERIARGDLREEVEVTGRDE-IGQLEQAMQAMTEKLAEVIGE 265
Cdd:COG5000 278 AFALLyLSTALLVLLAAIWTaiafARRIVRPIRKLIEAADEVADGDLDVQVPVRRVDEdVGRLSKAFNKMTEQLSSQQEA 357
                        90       100
                ....*....|....*....|....*
gi 86160313 266 VRGSTDALTSASQQLSATAQNVSQG 290
Cdd:COG5000 358 LERAKDALEQRRRFLEAVLSGLTAG 382
PRK10549 PRK10549
signal transduction histidine-protein kinase BaeS; Provisional
191-250 1.78e-04

signal transduction histidine-protein kinase BaeS; Provisional


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 42.70  E-value: 1.78e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313  191 WIYAGLTLagTLVILASVTLTRSITVPLRATVVHAERIARGDLREEVEVTGRDEIGQLEQ 250
Cdd:PRK10549 167 WLIVALST--LLAALATFLLARGLLAPVKRLVEGTHKLAAGDFTTRVTPTSRDELGRLAQ 224
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
228-495 2.53e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins].


Pssm-ID: 233757 [Multi-domain]  Cd Length: 1179  Bit Score: 42.74  E-value: 2.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313    228 IARGDLREEVEVTGRD-EIGQLEQAMQAMTEKLAE---VIGEVRGSTDALTSASQQLSATAQNVSQ---GTGEQAASVEE 300
Cdd:TIGR02168  661 ITGGSAKTNSSILERRrEIEELEEKIEELEEKIAElekALAELRKELEELEEELEQLRKELEELSRqisALRKDLARLEA 740
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313    301 TTSSLEEMSASIT---QNAENSRQTEAVALEGARNAQESGEAVRRSVEA-MRTIAEKISIIEEI--AYQTNLLALNAAIE 374
Cdd:TIGR02168  741 EVEQLEERIAQLSkelTELEAEIEELEERLEEAEEELAEAEAEIEELEAqIEQLKEELKALREAldELRAELTLLNEEAA 820
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313    375 AARAGEHGRGFAVVATEVRklAERAQKSAGEIGALAGSSVEVAERSGALLAELVPAIRKTSDLVQEVAAASREQSTGVRQ 454
Cdd:TIGR02168  821 NLRERLESLERRIAATERR--LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEE 898
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 86160313    455 VTKAMGVVDQVTQRNASAAEELSSTAEEMSSQAEALQQLVA 495
Cdd:TIGR02168  899 LSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRID 939
VicK COG5002
Signal transduction histidine kinase [Signal transduction mechanisms]
192-261 2.71e-03

Signal transduction histidine kinase [Signal transduction mechanisms]


Pssm-ID: 227335 [Multi-domain]  Cd Length: 459  Bit Score: 38.95  E-value: 2.71e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313 192 IYAGLTLAGTLVILASVTLTRSITVPLRATVVHAERIARGDLREEVEVTGRDEIGQLEQAMQAMTEKLAE 261
Cdd:COG5002  32 LISGTLIALIITALLGILLARTITKPITDMRKQAVDMARGNYSRKVKVYGTDEIGELADSFNDLTKRVQE 101
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
240-342 4.02e-03

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: 38.04  E-value: 4.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313    240 TGRDEIGQLEQAMQAMTEKLAEVIGEVRGSTDAL---TSASQQLSATAQNVSQGTGEQAASVEETTSSLEEMSASITQNA 316
Cdd:smart00283 155 EIQEETNEAVAAMEESSSEVEEGVELVEETGDALeeiVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETA 234
                           90       100
                   ....*....|....*....|....*.
gi 86160313    317 ENSRQTEAVALEGARNAQESGEAVRR 342
Cdd:smart00283 235 AMSEEISAAAEELSGLAEELDELVER 260
PRK10600 PRK10600
nitrate/nitrite sensor protein NarX; Provisional
192-261 4.52e-03

nitrate/nitrite sensor protein NarX; Provisional


Pssm-ID: 182581 [Multi-domain]  Cd Length: 569  Bit Score: 38.50  E-value: 4.52e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313  192 IYAGLTLagTLVILASVTLTRSITVPLRATVVHAERIARGDLREEVEVTGRDEIGQLEQAMQAMTEKLAE 261
Cdd:PRK10600 129 VFAVFMA--LLLVFTIIWLRRRLLQPWRQLLSMANAVSHRDFTQRANISGRDEMAMLGTALNNMSAELAE 196
COG1511 COG1511
Predicted membrane protein [Function unknown]
250-496 4.60e-03

Predicted membrane protein [Function unknown]


Pssm-ID: 224428 [Multi-domain]  Cd Length: 780  Bit Score: 38.26  E-value: 4.60e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313 250 QAMQAMTEKLAEVIGEVRGSTDALTSASQQLSATAQNVSQGTGEQAASVE------ETTSSLEEMSASITQNAENSRQTE 323
Cdd:COG1511 251 GELKQGAEQLNEGIGEFSSGLSELNSGVQDLAAGVPQLNQGISALAAGLSlpdslgDQFSSLQEALTQIAQGLKQKTSSS 330
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313 324 AVALEGARNAQESGEAVRRSVEAMRTIAEKI---------SIIEEIAYQTNLLALNA-AIEAARAGEHGRGFAVVatevr 393
Cdd:COG1511 331 LEAAQGSLSSLQSMLALSKSLDLTAEGATVDalgapdgvqWLDESQKTLATLSELLStGIDGVSEGLDALEQASA----- 405
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313 394 KLAERAQKSAGEIGALAGSSVEVAERSGALLAELVPAIRKT--SDLVQEVAAASREQSTGVRQVTKAMGVVD-----QVT 466
Cdd:COG1511 406 QLAKSLAKLKTAVAQIAASIAQLLPGASEVLKTLKSKGLDKllNQLNGALAKGSNALVQGLSDANDSFRSITsaqlkAGL 485
                       250       260       270
                ....*....|....*....|....*....|
gi 86160313 467 QRNASAAEELSSTAEEMSSQAEALQQLVAF 496
Cdd:COG1511 486 NTLADGSNDLSSLGPGLGQLADGSKLLADG 515
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
212-331 5.63e-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: 234070 [Multi-domain]  Cd Length: 968  Bit Score: 38.22  E-value: 5.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86160313   212 RSITVPLRATVVHAERIARGDLREEVEVTGRDEIGQLEQAMQAMTEKlaevigevrgstdalTSASQQLSATAQNVSQGT 291
Cdd:TIGR02956 354 RSVILRLNQHTQALLRLALGDLDISLDARGDDELAHMGRAIEAFRDT---------------AAHNLKLQADERQVAQEL 418
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 86160313   292 GEQAASVEET----TSSLEEMSASITQNAENSRQTEAVALEGAR 331
Cdd:TIGR02956 419 QEHKESLEQLvaqrTQELAETNERLNAEVKNHAKARAEAEEANR 462
 
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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