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Conserved domains on  [gi|91783810|ref|YP_559016|]
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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 ...
291-482 3.50e-53

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: 181.67  E-value: 3.50e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810 291 EEQASALQQTASSMEELTGTVRQNADNARQASSLAANASEIANKGSAVVDKVVGTMGDINQSSARIADIISIIEGIAFQT 370
Cdd:cd11386   1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810 371 NILALNAAVEAARAGEDGRGFAVVAGEVRSLAQRSSAAAKEIKELIDTSVERVQSGSALVDEAGRTMTDIIGAVQRVTDI 450
Cdd:cd11386  81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160
                       170       180       190
                ....*....|....*....|....*....|..
gi 91783810 451 MGEIAAASEEQSGGIDQVARAVTQMDEVTQQN 482
Cdd:cd11386 161 FEEIVASVEEVADGIQEISAATQEQSASTQEI 192
Tar_Tsr_LBD cd00181
ligand binding domain of Tar- and Tsr-related chemoreceptors; E.coli Tar (taxis to aspartate ...
66-170 4.83e-06

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.


:

Pssm-ID: 206638  Cd Length: 129  Bit Score: 45.10  E-value: 4.83e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810  66 RLALDRAA--FMIGTP--EAAPTLERARGMRATSDMWWKQYMDLPREPDEDR-LAQDVVSRREALHQQLDAFAATIAAND 140
Cdd:cd00181  21 RNTLNRAAirLLLGDPdaSAAELLDRAKASLAAADKAFAAFKALPKLTGEERaLAAELEASYQAYHDALQELIAALQKGD 100
                        90       100       110
                ....*....|....*....|....*....|
gi 91783810 141 QAKLVDgAKRLQVAYNDLANADDALRKYQF 170
Cdd:cd00181 101 AIDAFL-DQPTQGLQDAFEEAYDAYLNYLN 129
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
213-260 2.40e-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: 39.54  E-value: 2.40e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 91783810 213 IARPLDAALGYFDAISAGDLRRPVIVTSRDEMGRLLEGIARMQRSLTD 260
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGDLDVRLPVTGRDEIGELARAFNQMAERLRE 48
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction ...
133-512 1.81e-68

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


:

Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 229.49  E-value: 1.81e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810 133 AATIAANDQAKLVDGAKRLQVAYNDLANADDALRKYQFTSAKEGYDAAESSFELfrlisggALLIGVLAAAISYLALSRA 212
Cdd:COG0840  11 LIELAAGEADAGLLKLKKLIDELGKLLLSLNLILDDAASAEAAALKAVLKFLLI-------SLLVAIIVVLVLAILLLRA 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810 213 IARPLDAALGYFDAISAGDLRRPVIVTSRDEMGRLLEGIARMQRSLTDTVRSVRSGSESIATATRQIAAGNIDLSSRTEE 292
Cdd:COG0840  84 ILEPISDLLEVVERIAAGDLTKRIDESSNDEFGQLAKSFNEMILNLRQIIDAVQDNAEALSGASEEIAASATELSARADQ 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810 293 QASALQQTASSMEELTGTVRQNADNARQASSLAANASEIANKGSAVVDKVVGTMGDIN-----------QSSARIADIIS 361
Cdd:COG0840 164 QAESLEEVASAIEELSETVKEVAFNAKEAAALASEASQVAEEGGEEVRQAVEQMQEIAeelaevvkklsESSQEIEEITS 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810 362 IIEGIAFQTNILALNAAVEAARAGEDGRGFAVVAGEVRSLAQRSSAAAKEIKELIDT--------------SVERVQSGS 427
Cdd:COG0840 244 VINSIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSADSAKEIGLLIEEiqneaadavehmeeSASEVSEGV 323
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810 428 ALVDEAGRTMTDIIGAVQRVTDIMGEIAAASEEQSGGIDQVARAVTQMDEVTQQNAALVEEAAAAASSLEDQAGKLRHAV 507
Cdd:COG0840 324 KLVEETGSSLGEIAAAIEEVSQLISEIAAATEEQTAVLEEINASIEELDDVTQENAAAVEELAAASEELKELAEKLLELV 403

                ....*
gi 91783810 508 AVFQL 512
Cdd:COG0840 404 AKFKL 408
 
Name Accession Description Interval E-value
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
291-482 3.50e-53

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: 181.67  E-value: 3.50e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810 291 EEQASALQQTASSMEELTGTVRQNADNARQASSLAANASEIANKGSAVVDKVVGTMGDINQSSARIADIISIIEGIAFQT 370
Cdd:cd11386   1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810 371 NILALNAAVEAARAGEDGRGFAVVAGEVRSLAQRSSAAAKEIKELIDTSVERVQSGSALVDEAGRTMTDIIGAVQRVTDI 450
Cdd:cd11386  81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160
                       170       180       190
                ....*....|....*....|....*....|..
gi 91783810 451 MGEIAAASEEQSGGIDQVARAVTQMDEVTQQN 482
Cdd:cd11386 161 FEEIVASVEEVADGIQEISAATQEQSASTQEI 192
Tar_Tsr_LBD cd00181
ligand binding domain of Tar- and Tsr-related chemoreceptors; E.coli Tar (taxis to aspartate ...
66-170 4.83e-06

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.


Pssm-ID: 206638  Cd Length: 129  Bit Score: 45.10  E-value: 4.83e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810  66 RLALDRAA--FMIGTP--EAAPTLERARGMRATSDMWWKQYMDLPREPDEDR-LAQDVVSRREALHQQLDAFAATIAAND 140
Cdd:cd00181  21 RNTLNRAAirLLLGDPdaSAAELLDRAKASLAAADKAFAAFKALPKLTGEERaLAAELEASYQAYHDALQELIAALQKGD 100
                        90       100       110
                ....*....|....*....|....*....|
gi 91783810 141 QAKLVDgAKRLQVAYNDLANADDALRKYQF 170
Cdd:cd00181 101 AIDAFL-DQPTQGLQDAFEEAYDAYLNYLN 129
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
213-260 2.40e-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: 39.54  E-value: 2.40e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 91783810 213 IARPLDAALGYFDAISAGDLRRPVIVTSRDEMGRLLEGIARMQRSLTD 260
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGDLDVRLPVTGRDEIGELARAFNQMAERLRE 48
TarH pfam02203
Tar ligand binding domain homologue;
27-165 4.13e-22

Tar ligand binding domain homologue;


Pssm-ID: 251153  Cd Length: 146  Bit Score: 93.20  E-value: 4.13e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810    27 GVFGLFGMSRSNHALSDTFTNAMPSAVDIGNAELYAARERLALDRAAFMIGTPEAAPTLERARGMRATSDMWWKQYMDLP 106
Cdd:pfam02203   1 GGLGLSGLQSANDALDEVYTNSLQQQAALADAWVLLLQARLTLDRAALLPDAPDAAELLDRARESLAQSEKAWKAYLALP 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 91783810   107 REPDED-RLAQDVVSRREA-LHQQLDAFAATIAANDQAKLVD-GAKRLQVAYNDLANADDAL 165
Cdd:pfam02203  81 KSAPEEeALADELKAKYKQyLQDGLDPLAAALRAGDLDAFFDqPTQKMQPLFNALTRAWYAQ 142
HAMP pfam00672
HAMP domain;
191-260 4.01e-07

HAMP domain;


Pssm-ID: 250044  Cd Length: 70  Bit Score: 48.00  E-value: 4.01e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810   191 SGGALLIGVLAAAISYLALSRAIARPLDAALGYFDAISAGDLRRPVIVTSRDEMGRLLEGIARMQRSLTD 260
Cdd:pfam00672   1 LLLVLLIALLLLLLLAWLLARRLLRPLRRLAEAARRIASGDLDDRVPVSGPDEIGELARAFNQMADRLRE 70
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
211-263 4.49e-06

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


Pssm-ID: 197640  Cd Length: 53  Bit Score: 44.55  E-value: 4.49e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 91783810    211 RAIARPLDAALGYFDAISAGDLRRPVIVTSRDEMGRLLEGIARMQRSLTDTVR 263
Cdd:smart00304   1 RRLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRLEETIA 53
ResE COG2770
FOG: HAMP domain [Signal transduction mechanisms]
190-258 3.77e-03

FOG: HAMP domain [Signal transduction mechanisms]


Pssm-ID: 225359  Cd Length: 83  Bit Score: 36.20  E-value: 3.77e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 91783810 190 ISGGALLIGVLAAAISYLALSRAIARPLDAALGYFDAISAGDLRRPVIVTSRDEMGRLLEGIARMQRSL 258
Cdd:COG2770   7 IFGLLVLALVLILAVLLLAAARRVTRPLRRLADLAQNLALGDLSAEIPQPMLDEIGELAKAFNRMRDSL 75
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction ...
133-512 1.81e-68

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


Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 229.49  E-value: 1.81e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810 133 AATIAANDQAKLVDGAKRLQVAYNDLANADDALRKYQFTSAKEGYDAAESSFELfrlisggALLIGVLAAAISYLALSRA 212
Cdd:COG0840  11 LIELAAGEADAGLLKLKKLIDELGKLLLSLNLILDDAASAEAAALKAVLKFLLI-------SLLVAIIVVLVLAILLLRA 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810 213 IARPLDAALGYFDAISAGDLRRPVIVTSRDEMGRLLEGIARMQRSLTDTVRSVRSGSESIATATRQIAAGNIDLSSRTEE 292
Cdd:COG0840  84 ILEPISDLLEVVERIAAGDLTKRIDESSNDEFGQLAKSFNEMILNLRQIIDAVQDNAEALSGASEEIAASATELSARADQ 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810 293 QASALQQTASSMEELTGTVRQNADNARQASSLAANASEIANKGSAVVDKVVGTMGDIN-----------QSSARIADIIS 361
Cdd:COG0840 164 QAESLEEVASAIEELSETVKEVAFNAKEAAALASEASQVAEEGGEEVRQAVEQMQEIAeelaevvkklsESSQEIEEITS 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810 362 IIEGIAFQTNILALNAAVEAARAGEDGRGFAVVAGEVRSLAQRSSAAAKEIKELIDT--------------SVERVQSGS 427
Cdd:COG0840 244 VINSIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSADSAKEIGLLIEEiqneaadavehmeeSASEVSEGV 323
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810 428 ALVDEAGRTMTDIIGAVQRVTDIMGEIAAASEEQSGGIDQVARAVTQMDEVTQQNAALVEEAAAAASSLEDQAGKLRHAV 507
Cdd:COG0840 324 KLVEETGSSLGEIAAAIEEVSQLISEIAAATEEQTAVLEEINASIEELDDVTQENAAAVEELAAASEELKELAEKLLELV 403

                ....*
gi 91783810 508 AVFQL 512
Cdd:COG0840 404 AKFKL 408
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
162-512 4.52e-119

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 367.02  E-value: 4.52e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810  162 DDALRKYQFTSAKEGYDAAESSFELFRLIS---GGALLIGVLAAAISYLALSRAIARPLDAALGYFDAISAGDLRRPVIV 238
Cdd:PRK15048 162 GEAFAQYALSSEKLYRDIVTDNADDYRFAQwqlAVIALVVVLILLVAWYGIRRMLLTPLAKIIAHIREIAGGNLANTLTI 241
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810  239 TSRDEMGRLLEGIARMQRSLTDTVRSVRSGSESIATATRQIAAGNIDLSSRTEEQASALQQTASSMEELTGTVRQNADNA 318
Cdd:PRK15048 242 DGRSEMGDLAQSVSHMQRSLTDTVTHVREGSDAIYAGTREIAAGNTDLSSRTEQQASALEETAASMEQLTATVKQNADNA 321
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810  319 RQASSLAANASEIANKGSAVVDKVVGTMGDINQSSARIADIISIIEGIAFQTNILALNAAVEAARAGEDGRGFAVVAGEV 398
Cdd:PRK15048 322 RQASQLAQSASDTAQHGGKVVDGVVKTMHEIADSSKKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEV 401
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810  399 RSLAQRSSAAAKEIKELIDTSVERVQSGSALVDEAGRTMTDIIGAVQRVTDIMGEIAAASEEQSGGIDQVARAVTQMDEV 478
Cdd:PRK15048 402 RNLASRSAQAAKEIKALIEDSVSRVDTGSVLVESAGETMNNIVNAVTRVTDIMGEIASASDEQSRGIDQVALAVSEMDRV 481
                        330       340       350
                 ....*....|....*....|....*....|....
gi 91783810  479 TQQNAALVEEAAAAASSLEDQAGKLRHAVAVFQL 512
Cdd:PRK15048 482 TQQNASLVQESAAAAAALEEQASRLTQAVSAFRL 515
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
265-511 7.40e-62

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: 207.14  E-value: 7.40e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810    265 VRSGSESIATATRQIAAGNIDLSSRTEEQASALQQTASSMEELTGTVRQNADNARQASSLAANASEIANKGSAVVDKVVG 344
Cdd:smart00283   2 VSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAVS 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810    345 TMGDINQSSARIADIISIIEGIAFQTNILALNAAVEAARAGEDGRGFAVVAGEVRSLAQRSSAAAKEIKELIDT------ 418
Cdd:smart00283  82 AVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEiqeetn 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810    419 --------SVERVQSGSALVDEAGRTMTDIIGAVQRVTDIMGEIAAASEEQSGGIDQVARAVTQMDEVTQQNAALVEEAA 490
Cdd:smart00283 162 eavaameeSSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEIS 241
                          250       260
                   ....*....|....*....|.
gi 91783810    491 AAASSLEDQAGKLRHAVAVFQ 511
Cdd:smart00283 242 AAAEELSGLAEELDELVERFK 262
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
312-513 5.25e-54

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: 184.19  E-value: 5.25e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810   312 RQNADNARQASSlaaNASEIANKGSAVVDKVVGTMGDINQSSARIADIISIIEGIAFQTNILALNAAVEAARAGEDGRGF 391
Cdd:pfam00015   1 AQASDLAQLASE---EALDEMSQIGQVVDDAVETMEELETSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810   392 AVVAGEVRSLAQRSSAAAKEIKELIDTSV--------------ERVQSGSALVDEAGRTMTDIIGAVQRVTDIMGEIAAA 457
Cdd:pfam00015  78 AVVADEVRKLAERSAQAAKEIEALIEEIVkqtndstasiqqtrTEVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAA 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 91783810   458 SEEQSGGIDQVARAVTQMDEVTQQNAALVEEAAAAASSLEDQAGKLRHAVAVFQLE 513
Cdd:pfam00015 158 SDEQSAGIDQVNQAVARIDQVTQQNAALVEESAAAAETLEEQAEELTASVAQFRIK 213
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
248-477 1.95e-03

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: 40.04  E-value: 1.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810    248 LEGIARMQRSLTDTVRSVRSGSESIataTRQIAAGNIDLSSRTEEQASALQQTASSMEELTgtvrqnaDNARQASSLAAN 327
Cdd:TIGR02168  700 LAELRKELEELEEELEQLRKELEEL---SRQISALRKDLARLEAEVEQLEERIAQLSKELT-------ELEAEIEELEER 769
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810    328 ASEIANKGSAVVDKVVGTMGDINQSSARIADIISIIEgiafqtnilALNAAVEAARagedgRGFAVVAGEVRSLAQRSSA 407
Cdd:TIGR02168  770 LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALD---------ELRAELTLLN-----EEAANLRERLESLERRIAA 835
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 91783810    408 AAKEIKELIDTSV---ERVQSGSALVDEAGRTMTDIIGAVQRVTDIMGEIAAASEEQSGGIDQVARAVTQMDE 477
Cdd:TIGR02168  836 TERRLEDLEEQIEelsEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
 
Name Accession Description Interval E-value
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
291-482 3.50e-53

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: 181.67  E-value: 3.50e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810 291 EEQASALQQTASSMEELTGTVRQNADNARQASSLAANASEIANKGSAVVDKVVGTMGDINQSSARIADIISIIEGIAFQT 370
Cdd:cd11386   1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810 371 NILALNAAVEAARAGEDGRGFAVVAGEVRSLAQRSSAAAKEIKELIDTSVERVQSGSALVDEAGRTMTDIIGAVQRVTDI 450
Cdd:cd11386  81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160
                       170       180       190
                ....*....|....*....|....*....|..
gi 91783810 451 MGEIAAASEEQSGGIDQVARAVTQMDEVTQQN 482
Cdd:cd11386 161 FEEIVASVEEVADGIQEISAATQEQSASTQEI 192
Tar_Tsr_LBD cd00181
ligand binding domain of Tar- and Tsr-related chemoreceptors; E.coli Tar (taxis to aspartate ...
66-170 4.83e-06

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.


Pssm-ID: 206638  Cd Length: 129  Bit Score: 45.10  E-value: 4.83e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810  66 RLALDRAA--FMIGTP--EAAPTLERARGMRATSDMWWKQYMDLPREPDEDR-LAQDVVSRREALHQQLDAFAATIAAND 140
Cdd:cd00181  21 RNTLNRAAirLLLGDPdaSAAELLDRAKASLAAADKAFAAFKALPKLTGEERaLAAELEASYQAYHDALQELIAALQKGD 100
                        90       100       110
                ....*....|....*....|....*....|
gi 91783810 141 QAKLVDgAKRLQVAYNDLANADDALRKYQF 170
Cdd:cd00181 101 AIDAFL-DQPTQGLQDAFEEAYDAYLNYLN 129
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
213-260 2.40e-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: 39.54  E-value: 2.40e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 91783810 213 IARPLDAALGYFDAISAGDLRRPVIVTSRDEMGRLLEGIARMQRSLTD 260
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGDLDVRLPVTGRDEIGELARAFNQMAERLRE 48
TarH pfam02203
Tar ligand binding domain homologue;
27-165 4.13e-22

Tar ligand binding domain homologue;


Pssm-ID: 251153  Cd Length: 146  Bit Score: 93.20  E-value: 4.13e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810    27 GVFGLFGMSRSNHALSDTFTNAMPSAVDIGNAELYAARERLALDRAAFMIGTPEAAPTLERARGMRATSDMWWKQYMDLP 106
Cdd:pfam02203   1 GGLGLSGLQSANDALDEVYTNSLQQQAALADAWVLLLQARLTLDRAALLPDAPDAAELLDRARESLAQSEKAWKAYLALP 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 91783810   107 REPDED-RLAQDVVSRREA-LHQQLDAFAATIAANDQAKLVD-GAKRLQVAYNDLANADDAL 165
Cdd:pfam02203  81 KSAPEEeALADELKAKYKQyLQDGLDPLAAALRAGDLDAFFDqPTQKMQPLFNALTRAWYAQ 142
4HB_MCP_1 pfam12729
Four helix bundle sensory module for signal transduction; This family is a four helix bundle ...
6-184 1.98e-09

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: 56.08  E-value: 1.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810     6 ITIKARIGLTMAFLAALLVAIGVFGLFGMSRSNHALSDTFTNAMPSAVDIGNAELYAARERLALDRaafMIGTPEAAPTL 85
Cdd:pfam12729   2 LKIRTKLILLFLLLALLLIIVGIVGLYSLKKINKNSETMYEDRLLPIKWLGEIRSNLREIRANLLE---LILTTDPAERD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810    86 ERARGM---RATSDMWWKQYMDLPREPDEDRLAQDVVSRREALHQQLDAFAATIAANDQaklvDGAKRLQ-----VAYND 157
Cdd:pfam12729  79 ELLKDIeelRAEIDKLLKKYEKTILTEEEKKLFNEFKEQLKAYRKVRNKVLDLAKAGKN----DEAYALYltelePARDA 154
                         170       180
                  ....*....|....*....|....*..
gi 91783810   158 LANADDALRKYQFTSAKEGYDAAESSF 184
Cdd:pfam12729 155 VIEALDELIDYNLKVAKEAYEDNKASY 181
HAMP pfam00672
HAMP domain;
191-260 4.01e-07

HAMP domain;


Pssm-ID: 250044  Cd Length: 70  Bit Score: 48.00  E-value: 4.01e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810   191 SGGALLIGVLAAAISYLALSRAIARPLDAALGYFDAISAGDLRRPVIVTSRDEMGRLLEGIARMQRSLTD 260
Cdd:pfam00672   1 LLLVLLIALLLLLLLAWLLARRLLRPLRRLAEAARRIASGDLDDRVPVSGPDEIGELARAFNQMADRLRE 70
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
211-263 4.49e-06

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


Pssm-ID: 197640  Cd Length: 53  Bit Score: 44.55  E-value: 4.49e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 91783810    211 RAIARPLDAALGYFDAISAGDLRRPVIVTSRDEMGRLLEGIARMQRSLTDTVR 263
Cdd:smart00304   1 RRLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRLEETIA 53
ResE COG2770
FOG: HAMP domain [Signal transduction mechanisms]
190-258 3.77e-03

FOG: HAMP domain [Signal transduction mechanisms]


Pssm-ID: 225359  Cd Length: 83  Bit Score: 36.20  E-value: 3.77e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 91783810 190 ISGGALLIGVLAAAISYLALSRAIARPLDAALGYFDAISAGDLRRPVIVTSRDEMGRLLEGIARMQRSL 258
Cdd:COG2770   7 IFGLLVLALVLILAVLLLAAARRVTRPLRRLADLAQNLALGDLSAEIPQPMLDEIGELAKAFNRMRDSL 75
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction ...
133-512 1.81e-68

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


Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 229.49  E-value: 1.81e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810 133 AATIAANDQAKLVDGAKRLQVAYNDLANADDALRKYQFTSAKEGYDAAESSFELfrlisggALLIGVLAAAISYLALSRA 212
Cdd:COG0840  11 LIELAAGEADAGLLKLKKLIDELGKLLLSLNLILDDAASAEAAALKAVLKFLLI-------SLLVAIIVVLVLAILLLRA 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810 213 IARPLDAALGYFDAISAGDLRRPVIVTSRDEMGRLLEGIARMQRSLTDTVRSVRSGSESIATATRQIAAGNIDLSSRTEE 292
Cdd:COG0840  84 ILEPISDLLEVVERIAAGDLTKRIDESSNDEFGQLAKSFNEMILNLRQIIDAVQDNAEALSGASEEIAASATELSARADQ 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810 293 QASALQQTASSMEELTGTVRQNADNARQASSLAANASEIANKGSAVVDKVVGTMGDIN-----------QSSARIADIIS 361
Cdd:COG0840 164 QAESLEEVASAIEELSETVKEVAFNAKEAAALASEASQVAEEGGEEVRQAVEQMQEIAeelaevvkklsESSQEIEEITS 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810 362 IIEGIAFQTNILALNAAVEAARAGEDGRGFAVVAGEVRSLAQRSSAAAKEIKELIDT--------------SVERVQSGS 427
Cdd:COG0840 244 VINSIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSADSAKEIGLLIEEiqneaadavehmeeSASEVSEGV 323
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810 428 ALVDEAGRTMTDIIGAVQRVTDIMGEIAAASEEQSGGIDQVARAVTQMDEVTQQNAALVEEAAAAASSLEDQAGKLRHAV 507
Cdd:COG0840 324 KLVEETGSSLGEIAAAIEEVSQLISEIAAATEEQTAVLEEINASIEELDDVTQENAAAVEELAAASEELKELAEKLLELV 403

                ....*
gi 91783810 508 AVFQL 512
Cdd:COG0840 404 AKFKL 408
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
162-512 4.52e-119

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 367.02  E-value: 4.52e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810  162 DDALRKYQFTSAKEGYDAAESSFELFRLIS---GGALLIGVLAAAISYLALSRAIARPLDAALGYFDAISAGDLRRPVIV 238
Cdd:PRK15048 162 GEAFAQYALSSEKLYRDIVTDNADDYRFAQwqlAVIALVVVLILLVAWYGIRRMLLTPLAKIIAHIREIAGGNLANTLTI 241
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810  239 TSRDEMGRLLEGIARMQRSLTDTVRSVRSGSESIATATRQIAAGNIDLSSRTEEQASALQQTASSMEELTGTVRQNADNA 318
Cdd:PRK15048 242 DGRSEMGDLAQSVSHMQRSLTDTVTHVREGSDAIYAGTREIAAGNTDLSSRTEQQASALEETAASMEQLTATVKQNADNA 321
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810  319 RQASSLAANASEIANKGSAVVDKVVGTMGDINQSSARIADIISIIEGIAFQTNILALNAAVEAARAGEDGRGFAVVAGEV 398
Cdd:PRK15048 322 RQASQLAQSASDTAQHGGKVVDGVVKTMHEIADSSKKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEV 401
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810  399 RSLAQRSSAAAKEIKELIDTSVERVQSGSALVDEAGRTMTDIIGAVQRVTDIMGEIAAASEEQSGGIDQVARAVTQMDEV 478
Cdd:PRK15048 402 RNLASRSAQAAKEIKALIEDSVSRVDTGSVLVESAGETMNNIVNAVTRVTDIMGEIASASDEQSRGIDQVALAVSEMDRV 481
                        330       340       350
                 ....*....|....*....|....*....|....
gi 91783810  479 TQQNAALVEEAAAAASSLEDQAGKLRHAVAVFQL 512
Cdd:PRK15048 482 TQQNASLVQESAAAAAALEEQASRLTQAVSAFRL 515
PRK15041 PRK15041
methyl-accepting chemotaxis protein I; Provisional
99-514 1.08e-110

methyl-accepting chemotaxis protein I; Provisional


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 345.40  E-value: 1.08e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810   99 WKQYMDLPREPDE-DRLAQDVVSRREALHQQLDAFAATIAANDQAKLVDGAKR-----LQVAYNDLANADDALRKYQFTS 172
Cdd:PRK15041 105 WADYEALPRDPRQsTAAAAEIKRNYDIYHNALAELIQLLGAGKINEFFDQPTQgyqdgFEKQYVAYMEQNDRLYDIAVSD 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810  173 AKEGYDAAessfeLFRLISggaLLIGVLAAAIS-YLALSRAIARPLDAALGYFDAISAGDLRRPVIVTSRDEMGRLLEGI 251
Cdd:PRK15041 185 NNASYSQA-----MWILVG---VMIVVLAVIFAvWFGIKASLVAPMNRLIDSIRHIAGGDLVKPIEVDGSNEMGQLAESL 256
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810  252 ARMQRSLTDTVRSVRSGSESIATATRQIAAGNIDLSSRTEEQASALQQTASSMEELTGTVRQNADNARQASSLAANASEI 331
Cdd:PRK15041 257 RHMQGELMRTVGDVRNGANAIYSGASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVKQNAENARQASHLALSASET 336
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810  332 ANKGSAVVDKVVGTMGDINQSSARIADIISIIEGIAFQTNILALNAAVEAARAGEDGRGFAVVAGEVRSLAQRSSAAAKE 411
Cdd:PRK15041 337 AQRGGKVVDNVVQTMRDISTSSQKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAARE 416
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810  412 IKELIDTSVERVQSGSALVDEAGRTMTDIIGAVQRVTDIMGEIAAASEEQSGGIDQVARAVTQMDEVTQQNAALVEEAAA 491
Cdd:PRK15041 417 IKSLIEDSVGKVDVGSTLVESAGETMAEIVSAVTRVTDIMGEIASASDEQSRGIDQVGLAVAEMDRVTQQNAALVEESAA 496
                        410       420
                 ....*....|....*....|...
gi 91783810  492 AASSLEDQAGKLRHAVAVFQLEE 514
Cdd:PRK15041 497 AAAALEEQASRLTEAVAVFRIQQ 519
PRK09793 PRK09793
methyl-accepting protein IV; Provisional
112-514 5.23e-107

methyl-accepting protein IV; Provisional


Pssm-ID: 182079 [Multi-domain]  Cd Length: 533  Bit Score: 335.12  E-value: 5.23e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810  112 DRLAQDVVSRREALHQ---QLDAFAATIAANDQAKLVDGA--KRLQVAYNDLANADDALRKYQ---FTSA--KEGYDAAE 181
Cdd:PRK09793  81 DDIKTLMTTARASLTQsttLFKSFMAMTAGNEHVRALQKEteKSFARWHNDLEHQATWLESNQlsdFLTApvQGSQNAFD 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810  182 SSFELFRL------------------ISGGALLIGVLAAAI----SYLALSRAIARPLDAALGYFDAISAGDLRRPVIVT 239
Cdd:PRK09793 161 VNFEAWQLeinhvleaasaqsqrnyqISALVFISMIIVAAIyissALWWTRKMIVQPLAIIGSHFDSIAAGNLARPIAVY 240
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810  240 SRDEMGRLLEGIARMQRSLTDTVRSVRSGSESIATATRQIAAGNIDLSSRTEEQASALQQTASSMEELTGTVRQNADNAR 319
Cdd:PRK09793 241 GRNEITAIFASLKTMQQALRGTVSDVRKGSQEMHIGIAEIVAGNNDLSSRTEQQAASLAQTAASMEQLTATVGQNADNAR 320
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810  320 QASSLAANASEIANKGSAVVDKVVGTMGDINQSSARIADIISIIEGIAFQTNILALNAAVEAARAGEDGRGFAVVAGEVR 399
Cdd:PRK09793 321 QASELAKNAATTAQAGGVQVSTMTHTMQEIATSSQKIGDIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVR 400
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810  400 SLAQRSSAAAKEIKELIDTSVERVQSGSALVDEAGRTMTDIIGAVQRVTDIMGEIAAASEEQSGGIDQVARAVTQMDEVT 479
Cdd:PRK09793 401 NLASRSAQAAKEIKGLIEESVNRVQQGSKLVNNAAATMTDIVSSVTRVNDIMGEIASASEEQRRGIEQVAQAVSQMDQVT 480
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 91783810  480 QQNAALVEEAAAAASSLEDQAGKLRHAVAVFQLEE 514
Cdd:PRK09793 481 QQNASLVEEAAVATEQLANQADHLSSRVAVFTLEE 515
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
265-511 7.40e-62

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: 207.14  E-value: 7.40e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810    265 VRSGSESIATATRQIAAGNIDLSSRTEEQASALQQTASSMEELTGTVRQNADNARQASSLAANASEIANKGSAVVDKVVG 344
Cdd:smart00283   2 VSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAVS 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810    345 TMGDINQSSARIADIISIIEGIAFQTNILALNAAVEAARAGEDGRGFAVVAGEVRSLAQRSSAAAKEIKELIDT------ 418
Cdd:smart00283  82 AVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEiqeetn 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810    419 --------SVERVQSGSALVDEAGRTMTDIIGAVQRVTDIMGEIAAASEEQSGGIDQVARAVTQMDEVTQQNAALVEEAA 490
Cdd:smart00283 162 eavaameeSSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEIS 241
                          250       260
                   ....*....|....*....|.
gi 91783810    491 AAASSLEDQAGKLRHAVAVFQ 511
Cdd:smart00283 242 AAAEELSGLAEELDELVERFK 262
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
312-513 5.25e-54

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: 184.19  E-value: 5.25e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810   312 RQNADNARQASSlaaNASEIANKGSAVVDKVVGTMGDINQSSARIADIISIIEGIAFQTNILALNAAVEAARAGEDGRGF 391
Cdd:pfam00015   1 AQASDLAQLASE---EALDEMSQIGQVVDDAVETMEELETSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810   392 AVVAGEVRSLAQRSSAAAKEIKELIDTSV--------------ERVQSGSALVDEAGRTMTDIIGAVQRVTDIMGEIAAA 457
Cdd:pfam00015  78 AVVADEVRKLAERSAQAAKEIEALIEEIVkqtndstasiqqtrTEVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAA 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 91783810   458 SEEQSGGIDQVARAVTQMDEVTQQNAALVEEAAAAASSLEDQAGKLRHAVAVFQLE 513
Cdd:pfam00015 158 SDEQSAGIDQVNQAVARIDQVTQQNAALVEESAAAAETLEEQAEELTASVAQFRIK 213
NarQ COG3850
Signal transduction histidine kinase, nitrate/nitrite-specific [Signal transduction mechanisms]
179-313 8.23e-04

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


Pssm-ID: 226368 [Multi-domain]  Cd Length: 574  Bit Score: 40.79  E-value: 8.23e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810 179 AAESSFELFRLISG-GALLIGVLAAAISYLaLSRAIARPLDAALGYFDAISAGDLRRPVIVTSRDEMGRLLEGIARMQRS 257
Cdd:COG3850 141 FAERKTILLVLVQLaGMLLILLLVVFTIYW-LRRRVVRPLNQLTSAAQRIGRRQFDQRPTDTGRNELGLLGRAFNQMSGE 219
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 91783810 258 LTDTVRsvrsgsesiatatrqiaagniDLSSRTEEQASALQQTASSMEELTGTVRQ 313
Cdd:COG3850 220 LKKLYA---------------------DLEQRVEEKTRDLEQKNQRLSFLYQSSRR 254
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
248-477 1.95e-03

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: 40.04  E-value: 1.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810    248 LEGIARMQRSLTDTVRSVRSGSESIataTRQIAAGNIDLSSRTEEQASALQQTASSMEELTgtvrqnaDNARQASSLAAN 327
Cdd:TIGR02168  700 LAELRKELEELEEELEQLRKELEEL---SRQISALRKDLARLEAEVEQLEERIAQLSKELT-------ELEAEIEELEER 769
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810    328 ASEIANKGSAVVDKVVGTMGDINQSSARIADIISIIEgiafqtnilALNAAVEAARagedgRGFAVVAGEVRSLAQRSSA 407
Cdd:TIGR02168  770 LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALD---------ELRAELTLLN-----EEAANLRERLESLERRIAA 835
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 91783810    408 AAKEIKELIDTSV---ERVQSGSALVDEAGRTMTDIIGAVQRVTDIMGEIAAASEEQSGGIDQVARAVTQMDE 477
Cdd:TIGR02168  836 TERRLEDLEEQIEelsEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
259-341 5.28e-03

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: 37.42  E-value: 5.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810   259 TDTVRSVRSGSESIATATRQIAAGNIDLSSRTEEQASALQQTASSMEELTGTVRQNADNARQASSLAANASEIANKGSAV 338
Cdd:pfam00015 127 STIVESTGEALKEIVDAVAEIADIVQEIAAASDEQSAGIDQVNQAVARIDQVTQQNAALVEESAAAAETLEEQAEELTAS 206

                  ...
gi 91783810   339 VDK 341
Cdd:pfam00015 207 VAQ 209
NtrY COG5000
Signal transduction histidine kinase involved in nitrogen fixation and metabolism regulation ...
47-281 6.46e-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: 38.21  E-value: 6.46e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810  47 NAMPSAVDignaeLYAARERLALDRAAF--MIGTPEAAPTLERARGMRATSDMWWKQYMDLPR---EPDEDRL----AQD 117
Cdd:COG5000 141 TALSMAID-----LNRARELLGLDPAGFtdLLNTEAAGRALLEAALLRADGRIVAQSYLDFDFpfpAPPEDSIkkadLGK 215
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810 118 VVSRREALHQQLDAFAATIAANDQAKLVDGAKRLQVAyNDLANADDALRKYQftSAKEGYDAAESSFELFRLisgGALLI 197
Cdd:COG5000 216 PVLIEPDNTNIRGALIKLKEIEDVYLYVVRPVDPKVA-EHADLTEGAAAEYR--ELEAGRDGLQIAFALLYL---STALL 289
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91783810 198 GVLAAAISYLALSRAIARPLDAALGYFDAISAGDLRRPVIVTSRDE-MGRLLEGIARMQRSLTDTVRSVRSGSESIATAT 276
Cdd:COG5000 290 VLLAAIWTAIAFARRIVRPIRKLIEAADEVADGDLDVQVPVRRVDEdVGRLSKAFNKMTEQLSSQQEALERAKDALEQRR 369

                ....*
gi 91783810 277 RQIAA 281
Cdd:COG5000 370 RFLEA 374
 
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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