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Conserved domains on  [gi|91777198|ref|YP_552406|]
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methyl-accepting chemotaxis sensory transducer [Burkholderia xenovorans LB400]

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List of domain hits

Name Accession Description Interval E-value
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
448-643 3.08e-56

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: 190.91  E-value: 3.08e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91777198 448 QASSLEETAASMEEITSTVQQNADHAAQANTLVTRAADAALEGGRAVERVVSTMGEISRSSQKIAEITSVIEGIAFQTNI 527
Cdd:cd11386   3 LSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQTNL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91777198 528 LALNAAVEAARAGEHGKGFAVVASEVRALAQRSAASVKEIEGLIATSTATVQSGFRIAEEASSTMQGIVQQVGEVRAIMG 607
Cdd:cd11386  83 LALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRAFE 162
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 91777198 608 EISVASREQSGGIEQVNLAVTQIGEATQQNATIVGE 643
Cdd:cd11386 163 EIVASVEEVADGIQEISAATQEQSASTQEIAAAVEE 198
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
365-407 6.66e-04

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: 38.38  E-value: 6.66e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 91777198 365 VSRPLEEAAKASERFASGDLSVRVANGanaRADEIGRLMQSID 407
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGDLDVRLPVT---GRDEIGELARAFN 40
Cache_1 super family cl03691
Cache domain;
199-266 6.49e-05

Cache domain;


The actual alignment was detected with superfamily member pfam02743:

Pssm-ID: 251508  Cd Length: 80  Bit Score: 41.48  E-value: 6.49e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 91777198   199 GKRLITQYRPITDAsGRVIGALFVGVNVDKeiqsVEDGIRNLKIGDTGYYFVVDASkgadrGKLIVHP 266
Cdd:pfam02743  11 GDLVITIAQPVYDN-GDLLGVIGLDVPLED----LLKITKSIKLGKTGYAFIIDNN-----GKVLAHP 68
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
419-666 2.33e-67

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: 223.32  E-value: 2.33e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91777198    419 QVRNASADMSHGTGKIATGSGHIAARIATQASSLEETAASMEEITSTVQQNADHAAQANTLVTRAADAALEGGRAVERVV 498
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91777198    499 STMGEISRSSQKIAEITSVIEGIAFQTNILALNAAVEAARAGEHGKGFAVVASEVRALAQRSAASVKEIEGLIAT----- 573
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEiqeet 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91777198    574 ---------STATVQSGFRIAEEASSTMQGIVQQVGEVRAIMGEISVASREQSGGIEQVNLAVTQIGEATQQNATIVGEA 644
Cdd:smart00283 161 neavaameeSSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240
                          250       260
                   ....*....|....*....|..
gi 91777198    645 ELAAAELRDQAARLAQVVSVFK 666
Cdd:smart00283 241 SAAAEELSGLAEELDELVERFK 262
 
Name Accession Description Interval E-value
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
448-643 3.08e-56

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: 190.91  E-value: 3.08e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91777198 448 QASSLEETAASMEEITSTVQQNADHAAQANTLVTRAADAALEGGRAVERVVSTMGEISRSSQKIAEITSVIEGIAFQTNI 527
Cdd:cd11386   3 LSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQTNL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91777198 528 LALNAAVEAARAGEHGKGFAVVASEVRALAQRSAASVKEIEGLIATSTATVQSGFRIAEEASSTMQGIVQQVGEVRAIMG 607
Cdd:cd11386  83 LALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRAFE 162
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 91777198 608 EISVASREQSGGIEQVNLAVTQIGEATQQNATIVGE 643
Cdd:cd11386 163 EIVASVEEVADGIQEISAATQEQSASTQEIAAAVEE 198
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
365-407 6.66e-04

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: 38.38  E-value: 6.66e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 91777198 365 VSRPLEEAAKASERFASGDLSVRVANGanaRADEIGRLMQSID 407
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGDLDVRLPVT---GRDEIGELARAFN 40
HAMP pfam00672
HAMP domain;
343-407 1.54e-06

HAMP domain;


Pssm-ID: 250044  Cd Length: 70  Bit Score: 46.45  E-value: 1.54e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 91777198   343 LLLGFILVGVFAVVFLIAVRRLVSRPLEEAAKASERFASGDLSVRVANGanaRADEIGRLMQSID 407
Cdd:pfam00672   1 LLLVLLIALLLLLLLAWLLARRLLRPLRRLAEAARRIASGDLDDRVPVS---GPDEIGELARAFN 62
Cache_1 pfam02743
Cache domain;
199-266 6.49e-05

Cache domain;


Pssm-ID: 251508  Cd Length: 80  Bit Score: 41.48  E-value: 6.49e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 91777198   199 GKRLITQYRPITDAsGRVIGALFVGVNVDKeiqsVEDGIRNLKIGDTGYYFVVDASkgadrGKLIVHP 266
Cdd:pfam02743  11 GDLVITIAQPVYDN-GDLLGVIGLDVPLED----LLKITKSIKLGKTGYAFIIDNN-----GKVLAHP 68
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
363-418 2.32e-04

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


Pssm-ID: 197640  Cd Length: 53  Bit Score: 39.54  E-value: 2.32e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 91777198    363 RLVSRPLEEAAKASERFASGDLSVRVANGanaRADEIGRLMQSIDGIGEGLARIVS 418
Cdd:smart00304   1 RRLLRPLRRLAEAAQRIADGDLTVRLPVD---GRDEIGELARAFNEMADRLEETIA 53
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
419-666 2.33e-67

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: 223.32  E-value: 2.33e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91777198    419 QVRNASADMSHGTGKIATGSGHIAARIATQASSLEETAASMEEITSTVQQNADHAAQANTLVTRAADAALEGGRAVERVV 498
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91777198    499 STMGEISRSSQKIAEITSVIEGIAFQTNILALNAAVEAARAGEHGKGFAVVASEVRALAQRSAASVKEIEGLIAT----- 573
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEiqeet 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91777198    574 ---------STATVQSGFRIAEEASSTMQGIVQQVGEVRAIMGEISVASREQSGGIEQVNLAVTQIGEATQQNATIVGEA 644
Cdd:smart00283 161 neavaameeSSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240
                          250       260
                   ....*....|....*....|..
gi 91777198    645 ELAAAELRDQAARLAQVVSVFK 666
Cdd:smart00283 241 SAAAEELSGLAEELDELVERFK 262
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
344-670 9.29e-93

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 300.38  E-value: 9.29e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91777198  344 LLGFILVGVFAVVFLiAVRRLVSRPLEEAAKASERFASGDLSVRVA-NGANaradEIGRLMQSIDGIGEGLARIVSQVRN 422
Cdd:PRK15048 196 VIALVVVLILLVAWY-GIRRMLLTPLAKIIAHIREIAGGNLANTLTiDGRS----EMGDLAQSVSHMQRSLTDTVTHVRE 270
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91777198  423 ASADMSHGTGKIATGSGHIAARIATQASSLEETAASMEEITSTVQQNADHAAQANTLVTRAADAALEGGRAVERVVSTMG 502
Cdd:PRK15048 271 GSDAIYAGTREIAAGNTDLSSRTEQQASALEETAASMEQLTATVKQNADNARQASQLAQSASDTAQHGGKVVDGVVKTMH 350
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91777198  503 EISRSSQKIAEITSVIEGIAFQTNILALNAAVEAARAGEHGKGFAVVASEVRALAQRSAASVKEIEGLIATSTATVQSGF 582
Cdd:PRK15048 351 EIADSSKKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKALIEDSVSRVDTGS 430
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91777198  583 RIAEEASSTMQGIVQQVGEVRAIMGEISVASREQSGGIEQVNLAVTQIGEATQQNATIVGEAELAAAELRDQAARLAQVV 662
Cdd:PRK15048 431 VLVESAGETMNNIVNAVTRVTDIMGEIASASDEQSRGIDQVALAVSEMDRVTQQNASLVQESAAAAAALEEQASRLTQAV 510

                 ....*...
gi 91777198  663 SVFKLESG 670
Cdd:PRK15048 511 SAFRLAAS 518
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction ...
330-667 3.41e-70

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


Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 236.04  E-value: 3.41e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91777198 330 EVMADVVATRNEFLLLGFILVGVFAVVFLIAVRRLVSRPLEEAAKASERFASGDLSVRVANganARADEIGRLMQSIDGI 409
Cdd:COG0840  49 SAEAAALKAVLKFLLISLLVAIIVVLVLAILLLRAILEPISDLLEVVERIAAGDLTKRIDE---SSNDEFGQLAKSFNEM 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91777198 410 GEGLARIVSQVRNASADMSHGTGKIATGSGHIAARIATQASSLEETAASMEEITSTVQQNADHAAQANTLVTRAADAALE 489
Cdd:COG0840 126 ILNLRQIIDAVQDNAEALSGASEEIAASATELSARADQQAESLEEVASAIEELSETVKEVAFNAKEAAALASEASQVAEE 205
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91777198 490 GGRAVERVVSTMGEI-----------SRSSQKIAEITSVIEGIAFQTNILALNAAVEAARAGEHGKGFAVVASEVRALAQ 558
Cdd:COG0840 206 GGEEVRQAVEQMQEIaeelaevvkklSESSQEIEEITSVINSIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAE 285
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91777198 559 RSAASVKEIEGLIAT--------------STATVQSGFRIAEEASSTMQGIVQQVGEVRAIMGEISVASREQSGGIEQVN 624
Cdd:COG0840 286 RSADSAKEIGLLIEEiqneaadavehmeeSASEVSEGVKLVEETGSSLGEIAAAIEEVSQLISEIAAATEEQTAVLEEIN 365
                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
gi 91777198 625 LAVTQIGEATQQNATIVGEAELAAAELRDQAARLAQVVSVFKL 667
Cdd:COG0840 366 ASIEELDDVTQENAAAVEELAAASEELKELAEKLLELVAKFKL 408
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
474-668 5.09e-57

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


Pssm-ID: 249510 [Multi-domain]  Cd Length: 213  Bit Score: 193.43  E-value: 5.09e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91777198   474 AQANTLVTRAADAALE----GGRAVERVVSTMGEISRSSQKIAEITSVIEGIAFQTNILALNAAVEAARAGEHGKGFAVV 549
Cdd:pfam00015   1 AQASDLAQLASEEALDemsqIGQVVDDAVETMEELETSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91777198   550 ASEVRALAQRSAASVKEIEGLIATSTA--------------TVQSGFRIAEEASSTMQGIVQQVGEVRAIMGEISVASRE 615
Cdd:pfam00015  81 ADEVRKLAERSAQAAKEIEALIEEIVKqtndstasiqqtrtEVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDE 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 91777198   616 QSGGIEQVNLAVTQIGEATQQNATIVGEAELAAAELRDQAARLAQVVSVFKLE 668
Cdd:pfam00015 161 QSAGIDQVNQAVARIDQVTQQNAALVEESAAAAETLEEQAEELTASVAQFRIK 213
NtrY COG5000
Signal transduction histidine kinase involved in nitrogen fixation and metabolism regulation ...
342-426 1.10e-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: 43.99  E-value: 1.10e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91777198 342 FLLLGFILVGVF-AVVFLIAVRRLVSRPLEEAAKASERFASGDLSVRVAngANARADEIGRLMQSIDGIGEGLARIVSQV 420
Cdd:COG5000 281 LLYLSTALLVLLaAIWTAIAFARRIVRPIRKLIEAADEVADGDLDVQVP--VRRVDEDVGRLSKAFNKMTEQLSSQQEAL 358

                ....*.
gi 91777198 421 RNASAD 426
Cdd:COG5000 359 ERAKDA 364
PRK10549 PRK10549
signal transduction histidine-protein kinase BaeS; Provisional
348-429 5.43e-03

signal transduction histidine-protein kinase BaeS; Provisional


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 38.46  E-value: 5.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91777198  348 ILVGvFAVVFLIAVRRLVSR----PLEEAAKASERFASGDLSVRVAngANARaDEIGRLMQSIDGIGEGLARIVSQVRNA 423
Cdd:PRK10549 168 LIVA-LSTLLAALATFLLARgllaPVKRLVEGTHKLAAGDFTTRVT--PTSR-DELGRLAQDFNQLASTLEKNEQMRRDF 243

                 ....*.
gi 91777198  424 SADMSH 429
Cdd:PRK10549 244 MADISH 249
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
353-482 8.30e-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: 37.27  E-value: 8.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91777198    353 FAVVfliA--VRRLVSRPLEEA----AKASERFASGDLSVRVANGANARADE----IGRLMQSIDGIGEGLARIVSQVRN 422
Cdd:smart00283 128 FAVV---AdeVRKLAERSAESAkeieSLIKEIQEETNEAVAAMEESSSEVEEgvelVEETGDALEEIVDSVEEIADLVQE 204
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 91777198    423 asadMSHGTGKIATGSGHIAARIATQASSLEETAASMEEITSTVQQNADHAAQANTLVTR 482
Cdd:smart00283 205 ----IAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEISAAAEELSGLAEELDELVER 260
 
Name Accession Description Interval E-value
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
448-643 3.08e-56

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: 190.91  E-value: 3.08e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91777198 448 QASSLEETAASMEEITSTVQQNADHAAQANTLVTRAADAALEGGRAVERVVSTMGEISRSSQKIAEITSVIEGIAFQTNI 527
Cdd:cd11386   3 LSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQTNL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91777198 528 LALNAAVEAARAGEHGKGFAVVASEVRALAQRSAASVKEIEGLIATSTATVQSGFRIAEEASSTMQGIVQQVGEVRAIMG 607
Cdd:cd11386  83 LALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRAFE 162
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 91777198 608 EISVASREQSGGIEQVNLAVTQIGEATQQNATIVGE 643
Cdd:cd11386 163 EIVASVEEVADGIQEISAATQEQSASTQEIAAAVEE 198
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
365-407 6.66e-04

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: 38.38  E-value: 6.66e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 91777198 365 VSRPLEEAAKASERFASGDLSVRVANGanaRADEIGRLMQSID 407
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGDLDVRLPVT---GRDEIGELARAFN 40
HAMP pfam00672
HAMP domain;
343-407 1.54e-06

HAMP domain;


Pssm-ID: 250044  Cd Length: 70  Bit Score: 46.45  E-value: 1.54e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 91777198   343 LLLGFILVGVFAVVFLIAVRRLVSRPLEEAAKASERFASGDLSVRVANGanaRADEIGRLMQSID 407
Cdd:pfam00672   1 LLLVLLIALLLLLLLAWLLARRLLRPLRRLAEAARRIASGDLDDRVPVS---GPDEIGELARAFN 62
Cache_1 pfam02743
Cache domain;
199-266 6.49e-05

Cache domain;


Pssm-ID: 251508  Cd Length: 80  Bit Score: 41.48  E-value: 6.49e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 91777198   199 GKRLITQYRPITDAsGRVIGALFVGVNVDKeiqsVEDGIRNLKIGDTGYYFVVDASkgadrGKLIVHP 266
Cdd:pfam02743  11 GDLVITIAQPVYDN-GDLLGVIGLDVPLED----LLKITKSIKLGKTGYAFIIDNN-----GKVLAHP 68
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
363-418 2.32e-04

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


Pssm-ID: 197640  Cd Length: 53  Bit Score: 39.54  E-value: 2.32e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 91777198    363 RLVSRPLEEAAKASERFASGDLSVRVANGanaRADEIGRLMQSIDGIGEGLARIVS 418
Cdd:smart00304   1 RRLLRPLRRLAEAAQRIADGDLTVRLPVD---GRDEIGELARAFNEMADRLEETIA 53
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
419-666 2.33e-67

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: 223.32  E-value: 2.33e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91777198    419 QVRNASADMSHGTGKIATGSGHIAARIATQASSLEETAASMEEITSTVQQNADHAAQANTLVTRAADAALEGGRAVERVV 498
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91777198    499 STMGEISRSSQKIAEITSVIEGIAFQTNILALNAAVEAARAGEHGKGFAVVASEVRALAQRSAASVKEIEGLIAT----- 573
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEiqeet 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91777198    574 ---------STATVQSGFRIAEEASSTMQGIVQQVGEVRAIMGEISVASREQSGGIEQVNLAVTQIGEATQQNATIVGEA 644
Cdd:smart00283 161 neavaameeSSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240
                          250       260
                   ....*....|....*....|..
gi 91777198    645 ELAAAELRDQAARLAQVVSVFK 666
Cdd:smart00283 241 SAAAEELSGLAEELDELVERFK 262
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
344-670 9.29e-93

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 300.38  E-value: 9.29e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91777198  344 LLGFILVGVFAVVFLiAVRRLVSRPLEEAAKASERFASGDLSVRVA-NGANaradEIGRLMQSIDGIGEGLARIVSQVRN 422
Cdd:PRK15048 196 VIALVVVLILLVAWY-GIRRMLLTPLAKIIAHIREIAGGNLANTLTiDGRS----EMGDLAQSVSHMQRSLTDTVTHVRE 270
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91777198  423 ASADMSHGTGKIATGSGHIAARIATQASSLEETAASMEEITSTVQQNADHAAQANTLVTRAADAALEGGRAVERVVSTMG 502
Cdd:PRK15048 271 GSDAIYAGTREIAAGNTDLSSRTEQQASALEETAASMEQLTATVKQNADNARQASQLAQSASDTAQHGGKVVDGVVKTMH 350
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91777198  503 EISRSSQKIAEITSVIEGIAFQTNILALNAAVEAARAGEHGKGFAVVASEVRALAQRSAASVKEIEGLIATSTATVQSGF 582
Cdd:PRK15048 351 EIADSSKKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKALIEDSVSRVDTGS 430
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91777198  583 RIAEEASSTMQGIVQQVGEVRAIMGEISVASREQSGGIEQVNLAVTQIGEATQQNATIVGEAELAAAELRDQAARLAQVV 662
Cdd:PRK15048 431 VLVESAGETMNNIVNAVTRVTDIMGEIASASDEQSRGIDQVALAVSEMDRVTQQNASLVQESAAAAAALEEQASRLTQAV 510

                 ....*...
gi 91777198  663 SVFKLESG 670
Cdd:PRK15048 511 SAFRLAAS 518
PRK15041 PRK15041
methyl-accepting chemotaxis protein I; Provisional
347-672 2.55e-89

methyl-accepting chemotaxis protein I; Provisional


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 291.47  E-value: 2.55e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91777198  347 FILVGVFAVVFLIAV------RRLVSRPLEEAAKASERFASGDLSVRV-ANGANaradEIGRLMQSIDGIGEGLARIVSQ 419
Cdd:PRK15041 194 WILVGVMIVVLAVIFavwfgiKASLVAPMNRLIDSIRHIAGGDLVKPIeVDGSN----EMGQLAESLRHMQGELMRTVGD 269
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91777198  420 VRNASADMSHGTGKIATGSGHIAARIATQASSLEETAASMEEITSTVQQNADHAAQANTLVTRAADAALEGGRAVERVVS 499
Cdd:PRK15041 270 VRNGANAIYSGASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQ 349
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91777198  500 TMGEISRSSQKIAEITSVIEGIAFQTNILALNAAVEAARAGEHGKGFAVVASEVRALAQRSAASVKEIEGLIATSTATVQ 579
Cdd:PRK15041 350 TMRDISTSSQKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVD 429
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91777198  580 SGFRIAEEASSTMQGIVQQVGEVRAIMGEISVASREQSGGIEQVNLAVTQIGEATQQNATIVGEAELAAAELRDQAARLA 659
Cdd:PRK15041 430 VGSTLVESAGETMAEIVSAVTRVTDIMGEIASASDEQSRGIDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRLT 509
                        330
                 ....*....|...
gi 91777198  660 QVVSVFKLESGRD 672
Cdd:PRK15041 510 EAVAVFRIQQQQQ 522
PRK09793 PRK09793
methyl-accepting protein IV; Provisional
348-668 1.20e-83

methyl-accepting protein IV; Provisional


Pssm-ID: 182079 [Multi-domain]  Cd Length: 533  Bit Score: 275.80  E-value: 1.20e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91777198  348 ILVGVFAVVFLIAVRRLVSRPLEEAAKASERFASGDLSVRVA-NGANaradEIGRLMQSIDGIGEGLARIVSQVRNASAD 426
Cdd:PRK09793 197 IVAAIYISSALWWTRKMIVQPLAIIGSHFDSIAAGNLARPIAvYGRN----EITAIFASLKTMQQALRGTVSDVRKGSQE 272
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91777198  427 MSHGTGKIATGSGHIAARIATQASSLEETAASMEEITSTVQQNADHAAQANTLVTRAADAALEGGRAVERVVSTMGEISR 506
Cdd:PRK09793 273 MHIGIAEIVAGNNDLSSRTEQQAASLAQTAASMEQLTATVGQNADNARQASELAKNAATTAQAGGVQVSTMTHTMQEIAT 352
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91777198  507 SSQKIAEITSVIEGIAFQTNILALNAAVEAARAGEHGKGFAVVASEVRALAQRSAASVKEIEGLIATSTATVQSGFRIAE 586
Cdd:PRK09793 353 SSQKIGDIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKGLIEESVNRVQQGSKLVN 432
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91777198  587 EASSTMQGIVQQVGEVRAIMGEISVASREQSGGIEQVNLAVTQIGEATQQNATIVGEAELAAAELRDQAARLAQVVSVFK 666
Cdd:PRK09793 433 NAAATMTDIVSSVTRVNDIMGEIASASEEQRRGIEQVAQAVSQMDQVTQQNASLVEEAAVATEQLANQADHLSSRVAVFT 512

                 ..
gi 91777198  667 LE 668
Cdd:PRK09793 513 LE 514
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction ...
330-667 3.41e-70

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


Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 236.04  E-value: 3.41e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91777198 330 EVMADVVATRNEFLLLGFILVGVFAVVFLIAVRRLVSRPLEEAAKASERFASGDLSVRVANganARADEIGRLMQSIDGI 409
Cdd:COG0840  49 SAEAAALKAVLKFLLISLLVAIIVVLVLAILLLRAILEPISDLLEVVERIAAGDLTKRIDE---SSNDEFGQLAKSFNEM 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91777198 410 GEGLARIVSQVRNASADMSHGTGKIATGSGHIAARIATQASSLEETAASMEEITSTVQQNADHAAQANTLVTRAADAALE 489
Cdd:COG0840 126 ILNLRQIIDAVQDNAEALSGASEEIAASATELSARADQQAESLEEVASAIEELSETVKEVAFNAKEAAALASEASQVAEE 205
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91777198 490 GGRAVERVVSTMGEI-----------SRSSQKIAEITSVIEGIAFQTNILALNAAVEAARAGEHGKGFAVVASEVRALAQ 558
Cdd:COG0840 206 GGEEVRQAVEQMQEIaeelaevvkklSESSQEIEEITSVINSIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAE 285
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91777198 559 RSAASVKEIEGLIAT--------------STATVQSGFRIAEEASSTMQGIVQQVGEVRAIMGEISVASREQSGGIEQVN 624
Cdd:COG0840 286 RSADSAKEIGLLIEEiqneaadavehmeeSASEVSEGVKLVEETGSSLGEIAAAIEEVSQLISEIAAATEEQTAVLEEIN 365
                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
gi 91777198 625 LAVTQIGEATQQNATIVGEAELAAAELRDQAARLAQVVSVFKL 667
Cdd:COG0840 366 ASIEELDDVTQENAAAVEELAAASEELKELAEKLLELVAKFKL 408
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
474-668 5.09e-57

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


Pssm-ID: 249510 [Multi-domain]  Cd Length: 213  Bit Score: 193.43  E-value: 5.09e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91777198   474 AQANTLVTRAADAALE----GGRAVERVVSTMGEISRSSQKIAEITSVIEGIAFQTNILALNAAVEAARAGEHGKGFAVV 549
Cdd:pfam00015   1 AQASDLAQLASEEALDemsqIGQVVDDAVETMEELETSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91777198   550 ASEVRALAQRSAASVKEIEGLIATSTA--------------TVQSGFRIAEEASSTMQGIVQQVGEVRAIMGEISVASRE 615
Cdd:pfam00015  81 ADEVRKLAERSAQAAKEIEALIEEIVKqtndstasiqqtrtEVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDE 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 91777198   616 QSGGIEQVNLAVTQIGEATQQNATIVGEAELAAAELRDQAARLAQVVSVFKLE 668
Cdd:pfam00015 161 QSAGIDQVNQAVARIDQVTQQNAALVEESAAAAETLEEQAEELTASVAQFRIK 213
NtrY COG5000
Signal transduction histidine kinase involved in nitrogen fixation and metabolism regulation ...
342-426 1.10e-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: 43.99  E-value: 1.10e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91777198 342 FLLLGFILVGVF-AVVFLIAVRRLVSRPLEEAAKASERFASGDLSVRVAngANARADEIGRLMQSIDGIGEGLARIVSQV 420
Cdd:COG5000 281 LLYLSTALLVLLaAIWTAIAFARRIVRPIRKLIEAADEVADGDLDVQVP--VRRVDEDVGRLSKAFNKMTEQLSSQQEAL 358

                ....*.
gi 91777198 421 RNASAD 426
Cdd:COG5000 359 ERAKDA 364
EspB pfam05802
Enterobacterial EspB protein; EspB is a type-III-secreted pore-forming protein of ...
392-520 1.90e-03

Enterobacterial EspB protein; EspB is a type-III-secreted pore-forming protein of enteropathogenic Escherichia coli (EPEC) which is essential for EPEC pathogenesis. EspB is also found in Citrobacter rodentium.


Pssm-ID: 114524 [Multi-domain]  Cd Length: 317  Bit Score: 39.67  E-value: 1.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91777198   392 ANARADEIGRLMQSIDGIGEGLARIVSQVRNASaDMSHGTGKIATGSGHIAARIATQA--SSLEETAASMEEITSTVQQN 469
Cdd:pfam05802  95 AAATAALVGGAISSVLGILGSFAAINSATKGAS-DIAQKATSASSKAVNAASEVATKAlvKATESVADAAEEASSTMQQA 173
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 91777198   470 ------------------ADHAAQANTLVTRAADAALEGGRAvERVVSTMGEISRSSQKIAeITSVIEG 520
Cdd:pfam05802 174 matatkaasrtsgvaddvATSAQKASQVAEEAADAAQKASRL-SRFTAAVDKITGSTAFVA-VTSLAEG 240
PRK10549 PRK10549
signal transduction histidine-protein kinase BaeS; Provisional
348-429 5.43e-03

signal transduction histidine-protein kinase BaeS; Provisional


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 38.46  E-value: 5.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91777198  348 ILVGvFAVVFLIAVRRLVSR----PLEEAAKASERFASGDLSVRVAngANARaDEIGRLMQSIDGIGEGLARIVSQVRNA 423
Cdd:PRK10549 168 LIVA-LSTLLAALATFLLARgllaPVKRLVEGTHKLAAGDFTTRVT--PTSR-DELGRLAQDFNQLASTLEKNEQMRRDF 243

                 ....*.
gi 91777198  424 SADMSH 429
Cdd:PRK10549 244 MADISH 249
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
353-482 8.30e-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: 37.27  E-value: 8.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91777198    353 FAVVfliA--VRRLVSRPLEEA----AKASERFASGDLSVRVANGANARADE----IGRLMQSIDGIGEGLARIVSQVRN 422
Cdd:smart00283 128 FAVV---AdeVRKLAERSAESAkeieSLIKEIQEETNEAVAAMEESSSEVEEgvelVEETGDALEEIVDSVEEIADLVQE 204
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 91777198    423 asadMSHGTGKIATGSGHIAARIATQASSLEETAASMEEITSTVQQNADHAAQANTLVTR 482
Cdd:smart00283 205 ----IAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEISAAAEELSGLAEELDELVER 260
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.11
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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