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Conserved domains on  [gi|77389852|gb|ABA81036.1|]
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methyl-accepting chemotaxis protein [Rhodobacter sphaeroides 2.4.1]

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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. ...
212-259 4.05e-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: 4.05e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 77389852 212 IGRGLRRALALTRRVAAGDLTEGEEVKGRDEIADLLGASNRMLEKLRE 259
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGDLDVRLPVTGRDEIGELARAFNQMAERLRE 48
MCP_signal super family cl21547
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
290-470 1.10e-24

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: 101.16  E-value: 1.10e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389852 290 EEQASATVEASAAVEQMVGNITQSESNAGVTAQIAGSSADDARRCGVAVAEAVRSMQEIAER-------IGVVREIARQT 362
Cdd:cd11386   1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESsaeigeiVEVIDDIAEQT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389852 363 DLLALNAAVEAARAGEQGRGFAVVAAEVRRLAERSAEAAAEISTLSAGTARAAAGAGEMIDRLVPEIERTSELVTD---- 438
Cdd:cd11386  81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEEtgra 160
                       170       180       190
                ....*....|....*....|....*....|....*
gi 77389852 439 ---ISVASRELSEGARQVSLAIDALDRVTQQTDAA 470
Cdd:cd11386 161 feeIVASVEEVADGIQEISAATQEQSASTQEIAAA 195
Tar_Tsr_LBD super family cl00144
ligand binding domain of Tar- and Tsr-related chemoreceptors; E.coli Tar (taxis to aspartate ...
4-182 2.40e-04

ligand binding domain of Tar- and Tsr-related chemoreceptors; E.coli Tar (taxis to aspartate and repellents) and Tsr (taxis to serine and repellents) are homologous chemoreceptors that have a high specificity for aspartate and serine, respectively. Both are homodimeric receptors and contain an N-terminal periplasmic ligand binding domain, a transmembrane region, a HAMP domain and a C-terminal cytosolic signaling domain.


The actual alignment was detected with superfamily member pfam12729:

Pssm-ID: 260214  Cd Length: 181  Bit Score: 40.67  E-value: 2.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389852     4 TIRTKLAAAFTVVFVMAGLAVALALVQLGRVDQRMTEVIDEHVQEVVLAQRLSIGQYRVMASIRAHLLDRDSDSAIQIET 83
Cdd:pfam12729   3 KIRTKLILLFLLLALLLIIVGIVGLYSLKKINKNSETMYEDRLLPIKWLGEIRSNLREIRANLLELILTTDPAERDELLK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389852    84 SVQEGRMIQRRALRALRDRPQDAATADLLIRYNDLRKQIQRVNNRAMILSLGGNPQGAAAFLREAGAAGLERSLEGLsED 163
Cdd:pfam12729  83 DIEELRAEIDKLLKKYEKTILTEEEKKLFNEFKEQLKAYRKVRNKVLDLAKAGKNDEAYALYLTELEPARDAVIEAL-DE 161
                         170
                  ....*....|....*....
gi 77389852   164 LVTHKLELLEREKAEANAE 182
Cdd:pfam12729 162 LIDYNLKVAKEAYEDNKAS 180
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
263-496 3.31e-31

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: 120.85  E-value: 3.31e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389852    263 EVSGTARDVAAASGRMATAAGQLKSGTEEQASATVEASAAVEQMVGNITQSESNAGVTAQIAGSSADDARRCGVAVAEAV 342
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389852    343 RSMQEIAER-------IGVVREIARQTDLLALNAAVEAARAGEQGRGFAVVAAEVRRLAERSAEAAAEISTLSAGTARAA 415
Cdd:smart00283  81 SAVEELEESsdeigeiVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEET 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389852    416 AGAGEMIDRLVPEIERTSELVTD---------------------ISVASRELSEGARQVSLAIDALDRVTQQTDAASKLL 474
Cdd:smart00283 161 NEAVAAMEESSSEVEEGVELVEEtgdaleeivdsveeiadlvqeIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240
                          250       260
                   ....*....|....*....|..
gi 77389852    475 DEDAEDLAARARRLLTSATYFR 496
Cdd:smart00283 241 SAAAEELSGLAEELDELVERFK 262
 
Name Accession Description Interval E-value
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
212-259 4.05e-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: 4.05e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 77389852 212 IGRGLRRALALTRRVAAGDLTEGEEVKGRDEIADLLGASNRMLEKLRE 259
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGDLDVRLPVTGRDEIGELARAFNQMAERLRE 48
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
290-470 1.10e-24

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: 101.16  E-value: 1.10e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389852 290 EEQASATVEASAAVEQMVGNITQSESNAGVTAQIAGSSADDARRCGVAVAEAVRSMQEIAER-------IGVVREIARQT 362
Cdd:cd11386   1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESsaeigeiVEVIDDIAEQT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389852 363 DLLALNAAVEAARAGEQGRGFAVVAAEVRRLAERSAEAAAEISTLSAGTARAAAGAGEMIDRLVPEIERTSELVTD---- 438
Cdd:cd11386  81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEEtgra 160
                       170       180       190
                ....*....|....*....|....*....|....*
gi 77389852 439 ---ISVASRELSEGARQVSLAIDALDRVTQQTDAA 470
Cdd:cd11386 161 feeIVASVEEVADGIQEISAATQEQSASTQEIAAA 195
HAMP pfam00672
HAMP domain;
192-259 7.94e-07

HAMP domain;


Pssm-ID: 250044  Cd Length: 70  Bit Score: 46.84  E-value: 7.94e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 77389852   192 LIGALSAVVGSAAAIWITLSIGRGLRRALALTRRVAAGDLTEGEEVKGRDEIADLLGASNRMLEKLRE 259
Cdd:pfam00672   3 LVLLIALLLLLLLAWLLARRLLRPLRRLAEAARRIASGDLDDRVPVSGPDEIGELARAFNQMADRLRE 70
4HB_MCP_1 pfam12729
Four helix bundle sensory module for signal transduction; This family is a four helix bundle ...
4-182 2.40e-04

Four helix bundle sensory module for signal transduction; This family is a four helix bundle that operates as a ubiquitous sensory module in prokaryotic signal-transduction. The 4HB_MCP is always found between two predicted transmembrane helices indicating that it detects only extracellular signals. In many cases the domain is associated with a cytoplasmic HAMP domain suggesting that most proteins carrying the bundle might share the mechanism of transmembrane signalling which is well-characterized in E coli chemoreceptors.


Pssm-ID: 193205  Cd Length: 181  Bit Score: 40.67  E-value: 2.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389852     4 TIRTKLAAAFTVVFVMAGLAVALALVQLGRVDQRMTEVIDEHVQEVVLAQRLSIGQYRVMASIRAHLLDRDSDSAIQIET 83
Cdd:pfam12729   3 KIRTKLILLFLLLALLLIIVGIVGLYSLKKINKNSETMYEDRLLPIKWLGEIRSNLREIRANLLELILTTDPAERDELLK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389852    84 SVQEGRMIQRRALRALRDRPQDAATADLLIRYNDLRKQIQRVNNRAMILSLGGNPQGAAAFLREAGAAGLERSLEGLsED 163
Cdd:pfam12729  83 DIEELRAEIDKLLKKYEKTILTEEEKKLFNEFKEQLKAYRKVRNKVLDLAKAGKNDEAYALYLTELEPARDAVIEAL-DE 161
                         170
                  ....*....|....*....
gi 77389852   164 LVTHKLELLEREKAEANAE 182
Cdd:pfam12729 162 LIDYNLKVAKEAYEDNKAS 180
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
211-262 3.18e-03

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


Pssm-ID: 197640  Cd Length: 53  Bit Score: 35.69  E-value: 3.18e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 77389852    211 SIGRGLRRALALTRRVAAGDLTEGEEVKGRDEIADLLGASNRMLEKLREVMD 262
Cdd:smart00304   2 RLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRLEETIA 53
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
263-496 3.31e-31

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: 120.85  E-value: 3.31e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389852    263 EVSGTARDVAAASGRMATAAGQLKSGTEEQASATVEASAAVEQMVGNITQSESNAGVTAQIAGSSADDARRCGVAVAEAV 342
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389852    343 RSMQEIAER-------IGVVREIARQTDLLALNAAVEAARAGEQGRGFAVVAAEVRRLAERSAEAAAEISTLSAGTARAA 415
Cdd:smart00283  81 SAVEELEESsdeigeiVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEET 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389852    416 AGAGEMIDRLVPEIERTSELVTD---------------------ISVASRELSEGARQVSLAIDALDRVTQQTDAASKLL 474
Cdd:smart00283 161 NEAVAAMEESSSEVEEGVELVEEtgdaleeivdsveeiadlvqeIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240
                          250       260
                   ....*....|....*....|..
gi 77389852    475 DEDAEDLAARARRLLTSATYFR 496
Cdd:smart00283 241 SAAAEELSGLAEELDELVERFK 262
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
216-496 5.33e-43

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 160.56  E-value: 5.33e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389852  216 LRRALALTRRVAAGDLTEGEEVKGRDEIADLLGASNRMLEKLREVMDEVSGTARDVAAASGRMATAAGQLKSGTEEQASA 295
Cdd:PRK15048 220 LAKIIAHIREIAGGNLANTLTIDGRSEMGDLAQSVSHMQRSLTDTVTHVREGSDAIYAGTREIAAGNTDLSSRTEQQASA 299
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389852  296 TVEASAAVEQMVGNITQSESNAGVTAQIAGSSADDARRCGVAVAEAVRSMQEIAER-------IGVVREIARQTDLLALN 368
Cdd:PRK15048 300 LEETAASMEQLTATVKQNADNARQASQLAQSASDTAQHGGKVVDGVVKTMHEIADSskkiadiISVIDGIAFQTNILALN 379
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389852  369 AAVEAARAGEQGRGFAVVAAEVRRLAERSAEAAAEISTLSAGTARA-------AAGAGEMIDRLVPEIERTSELVTDISV 441
Cdd:PRK15048 380 AAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKALIEDSVSRvdtgsvlVESAGETMNNIVNAVTRVTDIMGEIAS 459
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 77389852  442 ASRELSEGARQVSLAIDALDRVTQQTDAASKLLDEDAEDLAARARRLLTSATYFR 496
Cdd:PRK15048 460 ASDEQSRGIDQVALAVSEMDRVTQQNASLVQESAAAAAALEEQASRLTQAVSAFR 514
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility, Signal transduction mechanisms];
171-497 2.05e-39

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


Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 147.83  E-value: 2.05e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389852 171 LLEREKAEANAEGRSVLALVMLIGALSAVVGSAAAIWITLSIGRGLRRALALTRRVAAGDLTEGEEVKGRDEIADLLGAS 250
Cdd:COG0840  43 ILDDAASAEAAALKAVLKFLLISLLVAIIVVLVLAILLLRAILEPISDLLEVVERIAAGDLTKRIDESSNDEFGQLAKSF 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389852 251 NRMLEKLREVMDEVSGTARDVAAASGRMATAAGQLKSGTEEQASATVEASAAVEQMVGNITQSESNAGVTAQIAGSSADD 330
Cdd:COG0840 123 NEMILNLRQIIDAVQDNAEALSGASEEIAASATELSARADQQAESLEEVASAIEELSETVKEVAFNAKEAAALASEASQV 202
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389852 331 ARRCGVAVAEAVRSMQEIAER------------------IGVVREIARQTDLLALNAAVEAARAGEQGRGFAVVAAEVRR 392
Cdd:COG0840 203 AEEGGEEVRQAVEQMQEIAEElaevvkklsessqeieeiTSVINSIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRK 282
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389852 393 LAERSAEAAAEISTL---------------------SAGTARAAAGAGEMIDRLVPEIERTSELVTDISVASRELSEGAR 451
Cdd:COG0840 283 LAERSADSAKEIGLLieeiqneaadavehmeesaseVSEGVKLVEETGSSLGEIAAAIEEVSQLISEIAAATEEQTAVLE 362
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 77389852 452 QVSLAIDALDRVTQQTDAASKLLDEDAEDLAARARRLLTSATYFRT 497
Cdd:COG0840 363 EINASIEELDDVTQENAAAVEELAAASEELKELAEKLLELVAKFKL 408
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
321-496 1.74e-21

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: 92.51  E-value: 1.74e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389852   321 AQIAGSSADD-ARRCGVAVAEAVRSMQEIAER-------IGVVREIARQTDLLALNAAVEAARAGEQGRGFAVVAAEVRR 392
Cdd:pfam00015   7 AQLASEEALDeMSQIGQVVDDAVETMEELETSskkisdiISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389852   393 LAERSAEAAAEISTLSAGTARAAAGAGEMIDRLVPEIERTSELV---------------------TDISVASRELSEGAR 451
Cdd:pfam00015  87 LAERSAQAAKEIEALIEEIVKQTNDSTASIQQTRTEVEVGSTIVestgealkeivdavaeiadivQEIAAASDEQSAGID 166
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 77389852   452 QVSLAIDALDRVTQQTDAASKLLDEDAEDLAARARRLLTSATYFR 496
Cdd:pfam00015 167 QVNQAVARIDQVTQQNAALVEESAAAAETLEEQAEELTASVAQFR 211
NtrY COG5000
Signal transduction histidine kinase involved in nitrogen fixation and metabolism regulation ...
188-264 6.54e-03

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


Pssm-ID: 227333 [Multi-domain]  Cd Length: 712  Bit Score: 37.83  E-value: 6.54e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389852 188 ALVMLIGALSAVVgsaAAIWITLSIGRGLRRALAL----TRRVAAGDLTEGEEVKGRDE-IADLLGASNRMLEKLREVMD 262
Cdd:COG5000 280 ALLYLSTALLVLL---AAIWTAIAFARRIVRPIRKlieaADEVADGDLDVQVPVRRVDEdVGRLSKAFNKMTEQLSSQQE 356

                ..
gi 77389852 263 EV 264
Cdd:COG5000 357 AL 358
TIGR02680 TIGR02680
TIGR02680 family protein; Members of this protein family belong to a conserved gene four-gene ...
218-488 7.14e-03

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


Pssm-ID: 274256 [Multi-domain]  Cd Length: 1353  Bit Score: 37.86  E-value: 7.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389852    218 RALALTRRVAAGDLtegeEVKGRDEIADLLGASNRML-EKLREVMDEVSG--TARDVAAASGRMATAAGQLKSGTEEQAS 294
Cdd:TIGR02680  736 RERARLRRIAELDA----RLAAVDDELAELARELRALgARQRALADELAGapSDRSLRAAHRRAAEAERQAESAERELAR 811
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389852    295 ATVEASAAVEQMVGNITQSESNAGVTA--------QIAGSSADDARRCGVAVAEAVRSMQEIAERIGVVREIARQTDLLA 366
Cdd:TIGR02680  812 AARKAAAAAAAWKQARRELERDAADLDlptdpdalEAVGLALKRFGDHLHTLEVAVRELRHAATRAAEQRARAARAESDA 891
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389852    367 LNAAVEAARAGEQGRGFAVVAAEVRRlaersaeaaaeistlsagtaraaaGAGEMIDRLVPEIERTSELVTDIsvaSREL 446
Cdd:TIGR02680  892 REAAEDAAEARAEAEEASLRLRTLEE------------------------SVGAMVDEIRARLAETRAALASG---GREL 944
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 77389852    447 SEGARQVSLAIDALDRVTQQTDAASKLLDEDAEDLAARARRL 488
Cdd:TIGR02680  945 PRLAEALATAEEARGRAEEKRAEADATLDERAEARDHAIGQL 986
 
Name Accession Description Interval E-value
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
212-259 4.05e-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: 4.05e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 77389852 212 IGRGLRRALALTRRVAAGDLTEGEEVKGRDEIADLLGASNRMLEKLRE 259
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGDLDVRLPVTGRDEIGELARAFNQMAERLRE 48
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
290-470 1.10e-24

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: 101.16  E-value: 1.10e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389852 290 EEQASATVEASAAVEQMVGNITQSESNAGVTAQIAGSSADDARRCGVAVAEAVRSMQEIAER-------IGVVREIARQT 362
Cdd:cd11386   1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESsaeigeiVEVIDDIAEQT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389852 363 DLLALNAAVEAARAGEQGRGFAVVAAEVRRLAERSAEAAAEISTLSAGTARAAAGAGEMIDRLVPEIERTSELVTD---- 438
Cdd:cd11386  81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEEtgra 160
                       170       180       190
                ....*....|....*....|....*....|....*
gi 77389852 439 ---ISVASRELSEGARQVSLAIDALDRVTQQTDAA 470
Cdd:cd11386 161 feeIVASVEEVADGIQEISAATQEQSASTQEIAAA 195
HAMP pfam00672
HAMP domain;
192-259 7.94e-07

HAMP domain;


Pssm-ID: 250044  Cd Length: 70  Bit Score: 46.84  E-value: 7.94e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 77389852   192 LIGALSAVVGSAAAIWITLSIGRGLRRALALTRRVAAGDLTEGEEVKGRDEIADLLGASNRMLEKLRE 259
Cdd:pfam00672   3 LVLLIALLLLLLLAWLLARRLLRPLRRLAEAARRIASGDLDDRVPVSGPDEIGELARAFNQMADRLRE 70
4HB_MCP_1 pfam12729
Four helix bundle sensory module for signal transduction; This family is a four helix bundle ...
4-182 2.40e-04

Four helix bundle sensory module for signal transduction; This family is a four helix bundle that operates as a ubiquitous sensory module in prokaryotic signal-transduction. The 4HB_MCP is always found between two predicted transmembrane helices indicating that it detects only extracellular signals. In many cases the domain is associated with a cytoplasmic HAMP domain suggesting that most proteins carrying the bundle might share the mechanism of transmembrane signalling which is well-characterized in E coli chemoreceptors.


Pssm-ID: 193205  Cd Length: 181  Bit Score: 40.67  E-value: 2.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389852     4 TIRTKLAAAFTVVFVMAGLAVALALVQLGRVDQRMTEVIDEHVQEVVLAQRLSIGQYRVMASIRAHLLDRDSDSAIQIET 83
Cdd:pfam12729   3 KIRTKLILLFLLLALLLIIVGIVGLYSLKKINKNSETMYEDRLLPIKWLGEIRSNLREIRANLLELILTTDPAERDELLK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389852    84 SVQEGRMIQRRALRALRDRPQDAATADLLIRYNDLRKQIQRVNNRAMILSLGGNPQGAAAFLREAGAAGLERSLEGLsED 163
Cdd:pfam12729  83 DIEELRAEIDKLLKKYEKTILTEEEKKLFNEFKEQLKAYRKVRNKVLDLAKAGKNDEAYALYLTELEPARDAVIEAL-DE 161
                         170
                  ....*....|....*....
gi 77389852   164 LVTHKLELLEREKAEANAE 182
Cdd:pfam12729 162 LIDYNLKVAKEAYEDNKAS 180
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
211-262 3.18e-03

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


Pssm-ID: 197640  Cd Length: 53  Bit Score: 35.69  E-value: 3.18e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 77389852    211 SIGRGLRRALALTRRVAAGDLTEGEEVKGRDEIADLLGASNRMLEKLREVMD 262
Cdd:smart00304   2 RLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRLEETIA 53
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
263-496 3.31e-31

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: 120.85  E-value: 3.31e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389852    263 EVSGTARDVAAASGRMATAAGQLKSGTEEQASATVEASAAVEQMVGNITQSESNAGVTAQIAGSSADDARRCGVAVAEAV 342
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389852    343 RSMQEIAER-------IGVVREIARQTDLLALNAAVEAARAGEQGRGFAVVAAEVRRLAERSAEAAAEISTLSAGTARAA 415
Cdd:smart00283  81 SAVEELEESsdeigeiVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEET 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389852    416 AGAGEMIDRLVPEIERTSELVTD---------------------ISVASRELSEGARQVSLAIDALDRVTQQTDAASKLL 474
Cdd:smart00283 161 NEAVAAMEESSSEVEEGVELVEEtgdaleeivdsveeiadlvqeIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240
                          250       260
                   ....*....|....*....|..
gi 77389852    475 DEDAEDLAARARRLLTSATYFR 496
Cdd:smart00283 241 SAAAEELSGLAEELDELVERFK 262
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
216-496 5.33e-43

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 160.56  E-value: 5.33e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389852  216 LRRALALTRRVAAGDLTEGEEVKGRDEIADLLGASNRMLEKLREVMDEVSGTARDVAAASGRMATAAGQLKSGTEEQASA 295
Cdd:PRK15048 220 LAKIIAHIREIAGGNLANTLTIDGRSEMGDLAQSVSHMQRSLTDTVTHVREGSDAIYAGTREIAAGNTDLSSRTEQQASA 299
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389852  296 TVEASAAVEQMVGNITQSESNAGVTAQIAGSSADDARRCGVAVAEAVRSMQEIAER-------IGVVREIARQTDLLALN 368
Cdd:PRK15048 300 LEETAASMEQLTATVKQNADNARQASQLAQSASDTAQHGGKVVDGVVKTMHEIADSskkiadiISVIDGIAFQTNILALN 379
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389852  369 AAVEAARAGEQGRGFAVVAAEVRRLAERSAEAAAEISTLSAGTARA-------AAGAGEMIDRLVPEIERTSELVTDISV 441
Cdd:PRK15048 380 AAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKALIEDSVSRvdtgsvlVESAGETMNNIVNAVTRVTDIMGEIAS 459
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 77389852  442 ASRELSEGARQVSLAIDALDRVTQQTDAASKLLDEDAEDLAARARRLLTSATYFR 496
Cdd:PRK15048 460 ASDEQSRGIDQVALAVSEMDRVTQQNASLVQESAAAAAALEEQASRLTQAVSAFR 514
PRK15041 PRK15041
methyl-accepting chemotaxis protein I; Provisional
188-496 1.29e-41

methyl-accepting chemotaxis protein I; Provisional


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 156.27  E-value: 1.29e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389852  188 ALVMLIGALSAVVGSAAAIW--ITLSIGRGLRRALALTRRVAAGDLTEGEEVKGRDEIADLLGASNRMLEKLREVMDEVS 265
Cdd:PRK15041 192 AMWILVGVMIVVLAVIFAVWfgIKASLVAPMNRLIDSIRHIAGGDLVKPIEVDGSNEMGQLAESLRHMQGELMRTVGDVR 271
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389852  266 GTARDVAAASGRMATAAGQLKSGTEEQASATVEASAAVEQMVGNITQSESNAGVTAQIAGSSADDARRCGVAVAEAVRSM 345
Cdd:PRK15041 272 NGANAIYSGASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQTM 351
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389852  346 -------QEIAERIGVVREIARQTDLLALNAAVEAARAGEQGRGFAVVAAEVRRLAERSAEAAAEISTL-------SAGT 411
Cdd:PRK15041 352 rdistssQKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLiedsvgkVDVG 431
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389852  412 ARAAAGAGEMIDRLVPEIERTSELVTDISVASRELSEGARQVSLAIDALDRVTQQTDAaskLLDEDAEDLAA---RARRL 488
Cdd:PRK15041 432 STLVESAGETMAEIVSAVTRVTDIMGEIASASDEQSRGIDQVGLAVAEMDRVTQQNAA---LVEESAAAAAAleeQASRL 508

                 ....*...
gi 77389852  489 LTSATYFR 496
Cdd:PRK15041 509 TEAVAVFR 516
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility, Signal transduction mechanisms];
171-497 2.05e-39

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


Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 147.83  E-value: 2.05e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389852 171 LLEREKAEANAEGRSVLALVMLIGALSAVVGSAAAIWITLSIGRGLRRALALTRRVAAGDLTEGEEVKGRDEIADLLGAS 250
Cdd:COG0840  43 ILDDAASAEAAALKAVLKFLLISLLVAIIVVLVLAILLLRAILEPISDLLEVVERIAAGDLTKRIDESSNDEFGQLAKSF 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389852 251 NRMLEKLREVMDEVSGTARDVAAASGRMATAAGQLKSGTEEQASATVEASAAVEQMVGNITQSESNAGVTAQIAGSSADD 330
Cdd:COG0840 123 NEMILNLRQIIDAVQDNAEALSGASEEIAASATELSARADQQAESLEEVASAIEELSETVKEVAFNAKEAAALASEASQV 202
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389852 331 ARRCGVAVAEAVRSMQEIAER------------------IGVVREIARQTDLLALNAAVEAARAGEQGRGFAVVAAEVRR 392
Cdd:COG0840 203 AEEGGEEVRQAVEQMQEIAEElaevvkklsessqeieeiTSVINSIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRK 282
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389852 393 LAERSAEAAAEISTL---------------------SAGTARAAAGAGEMIDRLVPEIERTSELVTDISVASRELSEGAR 451
Cdd:COG0840 283 LAERSADSAKEIGLLieeiqneaadavehmeesaseVSEGVKLVEETGSSLGEIAAAIEEVSQLISEIAAATEEQTAVLE 362
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 77389852 452 QVSLAIDALDRVTQQTDAASKLLDEDAEDLAARARRLLTSATYFRT 497
Cdd:COG0840 363 EINASIEELDDVTQENAAAVEELAAASEELKELAEKLLELVAKFKL 408
PRK09793 PRK09793
methyl-accepting protein IV; Provisional
175-496 5.71e-37

methyl-accepting protein IV; Provisional


Pssm-ID: 182079 [Multi-domain]  Cd Length: 533  Bit Score: 142.13  E-value: 5.71e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389852  175 EKAEANAEGRSVLALVMLIgaLSAVVGSAAAIWITLSIGRGLRRALALTRRVAAGDLTEGEEVKGRDEIADLLGASNRML 254
Cdd:PRK09793 179 AQSQRNYQISALVFISMII--VAAIYISSALWWTRKMIVQPLAIIGSHFDSIAAGNLARPIAVYGRNEITAIFASLKTMQ 256
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389852  255 EKLREVMDEVSGTARDVAAASGRMATAAGQLKSGTEEQASATVEASAAVEQMVGNITQSESNAGVTAQIAGSSADDARRC 334
Cdd:PRK09793 257 QALRGTVSDVRKGSQEMHIGIAEIVAGNNDLSSRTEQQAASLAQTAASMEQLTATVGQNADNARQASELAKNAATTAQAG 336
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389852  335 GVAVAEAVRSMQEIA-------ERIGVVREIARQTDLLALNAAVEAARAGEQGRGFAVVAAEVRRLAERSAEAAAEISTL 407
Cdd:PRK09793 337 GVQVSTMTHTMQEIAtssqkigDIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKGL 416
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389852  408 SAGTARAAAGAGEMID-------RLVPEIERTSELVTDISVASRELSEGARQVSLAIDALDRVTQQTDAASKLLDEDAED 480
Cdd:PRK09793 417 IEESVNRVQQGSKLVNnaaatmtDIVSSVTRVNDIMGEIASASEEQRRGIEQVAQAVSQMDQVTQQNASLVEEAAVATEQ 496
                        330
                 ....*....|....*.
gi 77389852  481 LAARARRLLTSATYFR 496
Cdd:PRK09793 497 LANQADHLSSRVAVFT 512
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
321-496 1.74e-21

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: 92.51  E-value: 1.74e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389852   321 AQIAGSSADD-ARRCGVAVAEAVRSMQEIAER-------IGVVREIARQTDLLALNAAVEAARAGEQGRGFAVVAAEVRR 392
Cdd:pfam00015   7 AQLASEEALDeMSQIGQVVDDAVETMEELETSskkisdiISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389852   393 LAERSAEAAAEISTLSAGTARAAAGAGEMIDRLVPEIERTSELV---------------------TDISVASRELSEGAR 451
Cdd:pfam00015  87 LAERSAQAAKEIEALIEEIVKQTNDSTASIQQTRTEVEVGSTIVestgealkeivdavaeiadivQEIAAASDEQSAGID 166
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 77389852   452 QVSLAIDALDRVTQQTDAASKLLDEDAEDLAARARRLLTSATYFR 496
Cdd:pfam00015 167 QVNQAVARIDQVTQQNAALVEESAAAAETLEEQAEELTASVAQFR 211
NtrY COG5000
Signal transduction histidine kinase involved in nitrogen fixation and metabolism regulation ...
188-264 6.54e-03

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


Pssm-ID: 227333 [Multi-domain]  Cd Length: 712  Bit Score: 37.83  E-value: 6.54e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389852 188 ALVMLIGALSAVVgsaAAIWITLSIGRGLRRALAL----TRRVAAGDLTEGEEVKGRDE-IADLLGASNRMLEKLREVMD 262
Cdd:COG5000 280 ALLYLSTALLVLL---AAIWTAIAFARRIVRPIRKlieaADEVADGDLDVQVPVRRVDEdVGRLSKAFNKMTEQLSSQQE 356

                ..
gi 77389852 263 EV 264
Cdd:COG5000 357 AL 358
TIGR02680 TIGR02680
TIGR02680 family protein; Members of this protein family belong to a conserved gene four-gene ...
218-488 7.14e-03

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


Pssm-ID: 274256 [Multi-domain]  Cd Length: 1353  Bit Score: 37.86  E-value: 7.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389852    218 RALALTRRVAAGDLtegeEVKGRDEIADLLGASNRML-EKLREVMDEVSG--TARDVAAASGRMATAAGQLKSGTEEQAS 294
Cdd:TIGR02680  736 RERARLRRIAELDA----RLAAVDDELAELARELRALgARQRALADELAGapSDRSLRAAHRRAAEAERQAESAERELAR 811
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389852    295 ATVEASAAVEQMVGNITQSESNAGVTA--------QIAGSSADDARRCGVAVAEAVRSMQEIAERIGVVREIARQTDLLA 366
Cdd:TIGR02680  812 AARKAAAAAAAWKQARRELERDAADLDlptdpdalEAVGLALKRFGDHLHTLEVAVRELRHAATRAAEQRARAARAESDA 891
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389852    367 LNAAVEAARAGEQGRGFAVVAAEVRRlaersaeaaaeistlsagtaraaaGAGEMIDRLVPEIERTSELVTDIsvaSREL 446
Cdd:TIGR02680  892 REAAEDAAEARAEAEEASLRLRTLEE------------------------SVGAMVDEIRARLAETRAALASG---GREL 944
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 77389852    447 SEGARQVSLAIDALDRVTQQTDAASKLLDEDAEDLAARARRL 488
Cdd:TIGR02680  945 PRLAEALATAEEARGRAEEKRAEADATLDERAEARDHAIGQL 986
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.14
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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