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Conserved domains on  [gi|27377458|ref|NP_768987|]
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sensory transducer protein [Bradyrhizobium diazoefficiens USDA 110]

Protein classification: methyl-accepting chemotaxis protein (MCP) is a bacterial receptor that mediates chemotaxis to diverse signals, responding to changes in the concentration of attractants and repellents in the environment by altering swimming behavior

Graphical summary

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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. ...
208-255 6.97e-06

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


:

Pssm-ID: 100122  Cd Length: 48  Bit Score: 43.78  E-value: 6.97e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 27377458 208 ISRALAQAVGLADAVAIGDLSRKIESSSNDEIGDLIKSLNAMTVNLNA 255
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGDLDVRLPVTGRDEIGELARAFNQMAERLRE 48
MCP_signal super family cl21547
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
304-510 2.60e-32

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: 123.50  E-value: 2.60e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458 304 QNVSAGSQELSASAEQLSqgateqassaeeasssmeemaSNVKQNADNANQTEKIAAQSAKDAEASGAAVGRAVNAM--- 380
Cdd:cd11386   1 EELSASIEEVAASADQVA---------------------ETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVeel 59
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458 381 ----QTIAEKITIVQEIARQTDLLALNAAVEAARAGEHGKGFAVVASEVRKLAERSQAAAAEIGTL-------STETVKV 449
Cdd:cd11386  60 eessAEIGEIVEVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELieeiqeqTEEAVEA 139
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27377458 450 AQEAGNMLAKLVPDIKKTAELVEEITAACREQDVGSAQINQAIQQLDKVGQQNASASEQVS 510
Cdd:cd11386 140 MEETSEEVEEGVELVEETGRAFEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
Tar_Tsr_LBD super family cl00144
ligand binding domain of Tar- and Tsr-related chemoreceptors; E.coli Tar (taxis to aspartate ...
2-183 3.72e-07

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: 49.15  E-value: 3.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458     2 RFTVKAKLASAFGVVILLSMIAGAVGYVKLSDMVGTTETLVS-RAGRMEKAAELKEGILFLVRAEKNSILAATDAEYDQF 80
Cdd:pfam12729   1 NLKIRTKLILLFLLLALLLIIVGIVGLYSLKKINKNSETMYEdRLLPIKWLGEIRSNLREIRANLLELILTTDPAERDEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458    81 VADLAKNREALVKSKDEIHAAAS-EGGKKLMESFSTAFAKLSAYQDETVRLAKS-DKPKALDrsmhdgrKVVADALEAAD 158
Cdd:pfam12729  81 LKDIEELRAEIDKLLKKYEKTILtEEEKKLFNEFKEQLKAYRKVRNKVLDLAKAgKNDEAYA-------LYLTELEPARD 153
                         170       180
                  ....*....|....*....|....*
gi 27377458   159 GYIKNVKKNMAEQAEQSKQDGARAE 183
Cdd:pfam12729 154 AVIEALDELIDYNLKVAKEAYEDNK 178
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility, Signal transduction mechanisms];
152-532 2.17e-42

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


:

Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 157.46  E-value: 2.17e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458 152 DALEAADGYIKNVKKNMAEQAEQSKQDGARAEMLLMSLVIASLLIAAVAATWIALNISRALAQAVGLADAVAIGDLSRKI 231
Cdd:COG0840  28 KLIDELGKLLLSLNLILDDAASAEAAALKAVLKFLLISLLVAIIVVLVLAILLLRAILEPISDLLEVVERIAAGDLTKRI 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458 232 ESSSNDEIGDLIKSLNamtvnlnataavaneiaqgnlmveakpqsdkdtlglaleRMVEKLRQIVSEALTAAQNVSAGSQ 311
Cdd:COG0840 108 DESSNDEFGQLAKSFN---------------------------------------EMILNLRQIIDAVQDNAEALSGASE 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458 312 ELSASAEQLSQGATEQASSAEEASSSMEEMASNVKQNADNANQTEKIAAQSAKDAEASGAAVGRAVNAMQTIAEK----- 386
Cdd:COG0840 149 EIAASATELSARADQQAESLEEVASAIEELSETVKEVAFNAKEAAALASEASQVAEEGGEEVRQAVEQMQEIAEElaevv 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458 387 -------------ITIVQEIARQTDLLALNAAVEAARAGEHGKGFAVVASEVRKLAERSQAAAAEIGTL----------- 442
Cdd:COG0840 229 kklsessqeieeiTSVINSIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSADSAKEIGLLieeiqneaada 308
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458 443 ----------STETVKVAQEAGNMLAKLVPDIKKTAELVEEITAACREQDVGSAQINQAIQQLDKVGQQNASASEQVSST 512
Cdd:COG0840 309 vehmeesaseVSEGVKLVEETGSSLGEIAAAIEEVSQLISEIAAATEEQTAVLEEINASIEELDDVTQENAAAVEELAAA 388
                       410       420
                ....*....|....*....|
gi 27377458 513 SEELASQAEQLQSTIAYFRI 532
Cdd:COG0840 389 SEELKELAEKLLELVAKFKL 408
 
Name Accession Description Interval E-value
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
208-255 6.97e-06

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


Pssm-ID: 100122  Cd Length: 48  Bit Score: 43.78  E-value: 6.97e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 27377458 208 ISRALAQAVGLADAVAIGDLSRKIESSSNDEIGDLIKSLNAMTVNLNA 255
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGDLDVRLPVTGRDEIGELARAFNQMAERLRE 48
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
304-510 2.60e-32

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: 123.50  E-value: 2.60e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458 304 QNVSAGSQELSASAEQLSqgateqassaeeasssmeemaSNVKQNADNANQTEKIAAQSAKDAEASGAAVGRAVNAM--- 380
Cdd:cd11386   1 EELSASIEEVAASADQVA---------------------ETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVeel 59
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458 381 ----QTIAEKITIVQEIARQTDLLALNAAVEAARAGEHGKGFAVVASEVRKLAERSQAAAAEIGTL-------STETVKV 449
Cdd:cd11386  60 eessAEIGEIVEVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELieeiqeqTEEAVEA 139
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27377458 450 AQEAGNMLAKLVPDIKKTAELVEEITAACREQDVGSAQINQAIQQLDKVGQQNASASEQVS 510
Cdd:cd11386 140 MEETSEEVEEGVELVEETGRAFEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
HAMP pfam00672
HAMP domain;
186-255 3.57e-09

HAMP domain;


Pssm-ID: 250044  Cd Length: 70  Bit Score: 53.77  E-value: 3.57e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458   186 LMSLVIASLLIAAVAATWIALNISRALAQAVGLADAVAIGDLSRKIESSSNDEIGDLIKSLNAMTVNLNA 255
Cdd:pfam00672   1 LLLVLLIALLLLLLLAWLLARRLLRPLRRLAEAARRIASGDLDDRVPVSGPDEIGELARAFNQMADRLRE 70
4HB_MCP_1 pfam12729
Four helix bundle sensory module for signal transduction; This family is a four helix bundle ...
2-183 3.72e-07

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: 49.15  E-value: 3.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458     2 RFTVKAKLASAFGVVILLSMIAGAVGYVKLSDMVGTTETLVS-RAGRMEKAAELKEGILFLVRAEKNSILAATDAEYDQF 80
Cdd:pfam12729   1 NLKIRTKLILLFLLLALLLIIVGIVGLYSLKKINKNSETMYEdRLLPIKWLGEIRSNLREIRANLLELILTTDPAERDEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458    81 VADLAKNREALVKSKDEIHAAAS-EGGKKLMESFSTAFAKLSAYQDETVRLAKS-DKPKALDrsmhdgrKVVADALEAAD 158
Cdd:pfam12729  81 LKDIEELRAEIDKLLKKYEKTILtEEEKKLFNEFKEQLKAYRKVRNKVLDLAKAgKNDEAYA-------LYLTELEPARD 153
                         170       180
                  ....*....|....*....|....*
gi 27377458   159 GYIKNVKKNMAEQAEQSKQDGARAE 183
Cdd:pfam12729 154 AVIEALDELIDYNLKVAKEAYEDNK 178
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
207-258 2.55e-06

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


Pssm-ID: 197640  Cd Length: 53  Bit Score: 45.32  E-value: 2.55e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 27377458    207 NISRALAQAVGLADAVAIGDLSRKIESSSNDEIGDLIKSLNAMTVNLNATAA 258
Cdd:smart00304   2 RLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRLEETIA 53
HAMP COG2770
HAMP domain [Signal transduction mechanisms];
189-254 5.24e-03

HAMP domain [Signal transduction mechanisms];


Pssm-ID: 225359  Cd Length: 83  Bit Score: 35.43  E-value: 5.24e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27377458 189 LVIASLLIAAVAATWIALNISRALAQAVGLADAVAIGDLSRKIESSSNDEIGDLIKSLNAMTVNLN 254
Cdd:COG2770  11 LVLALVLILAVLLLAAARRVTRPLRRLADLAQNLALGDLSAEIPQPMLDEIGELAKAFNRMRDSLQ 76
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility, Signal transduction mechanisms];
152-532 2.17e-42

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


Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 157.46  E-value: 2.17e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458 152 DALEAADGYIKNVKKNMAEQAEQSKQDGARAEMLLMSLVIASLLIAAVAATWIALNISRALAQAVGLADAVAIGDLSRKI 231
Cdd:COG0840  28 KLIDELGKLLLSLNLILDDAASAEAAALKAVLKFLLISLLVAIIVVLVLAILLLRAILEPISDLLEVVERIAAGDLTKRI 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458 232 ESSSNDEIGDLIKSLNamtvnlnataavaneiaqgnlmveakpqsdkdtlglaleRMVEKLRQIVSEALTAAQNVSAGSQ 311
Cdd:COG0840 108 DESSNDEFGQLAKSFN---------------------------------------EMILNLRQIIDAVQDNAEALSGASE 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458 312 ELSASAEQLSQGATEQASSAEEASSSMEEMASNVKQNADNANQTEKIAAQSAKDAEASGAAVGRAVNAMQTIAEK----- 386
Cdd:COG0840 149 EIAASATELSARADQQAESLEEVASAIEELSETVKEVAFNAKEAAALASEASQVAEEGGEEVRQAVEQMQEIAEElaevv 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458 387 -------------ITIVQEIARQTDLLALNAAVEAARAGEHGKGFAVVASEVRKLAERSQAAAAEIGTL----------- 442
Cdd:COG0840 229 kklsessqeieeiTSVINSIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSADSAKEIGLLieeiqneaada 308
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458 443 ----------STETVKVAQEAGNMLAKLVPDIKKTAELVEEITAACREQDVGSAQINQAIQQLDKVGQQNASASEQVSST 512
Cdd:COG0840 309 vehmeesaseVSEGVKLVEETGSSLGEIAAAIEEVSQLISEIAAATEEQTAVLEEINASIEELDDVTQENAAAVEELAAA 388
                       410       420
                ....*....|....*....|
gi 27377458 513 SEELASQAEQLQSTIAYFRI 532
Cdd:COG0840 389 SEELKELAEKLLELVAKFKL 408
PRK09793 PRK09793
methyl-accepting protein IV; Provisional
162-534 1.70e-44

methyl-accepting protein IV; Provisional


Pssm-ID: 182079 [Multi-domain]  Cd Length: 533  Bit Score: 165.63  E-value: 1.70e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458  162 KNVKKNMAEQAEQSKQDGARAEMLLMSLVIASLLIAAVAATWIALNISRALAQAVGLADAVAIGDLSRKIESSSNDEIGD 241
Cdd:PRK09793 168 LEINHVLEAASAQSQRNYQISALVFISMIIVAAIYISSALWWTRKMIVQPLAIIGSHFDSIAAGNLARPIAVYGRNEITA 247
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458  242 LIKSLNAMTVNLNATaavaneiaqgnlmveakpqsdkdtlglalermVEKLRQIVSEALTAAQNVSAGSQELSASAEQls 321
Cdd:PRK09793 248 IFASLKTMQQALRGT--------------------------------VSDVRKGSQEMHIGIAEIVAGNNDLSSRTEQ-- 293
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458  322 qgateQASSAEEASSSMEEMASNVKQNADNANQTEKIAAQSAKDAEASGAAVGRAVNAMQTIAEK-------ITIVQEIA 394
Cdd:PRK09793 294 -----QAASLAQTAASMEQLTATVGQNADNARQASELAKNAATTAQAGGVQVSTMTHTMQEIATSsqkigdiISVIDGIA 368
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458  395 RQTDLLALNAAVEAARAGEHGKGFAVVASEVRKLAERSQAAAAEIGTLSTETVKVAQE-------AGNMLAKLVPDIKKT 467
Cdd:PRK09793 369 FQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKGLIEESVNRVQQgsklvnnAAATMTDIVSSVTRV 448
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27377458  468 AELVEEITAACREQDVGSAQINQAIQQLDKVGQQNASASEQVSSTSEELASQAEQLQSTIAYFRIEQ 534
Cdd:PRK09793 449 NDIMGEIASASEEQRRGIEQVAQAVSQMDQVTQQNASLVEEAAVATEQLANQADHLSSRVAVFTLEE 515
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
301-531 2.83e-41

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: 150.13  E-value: 2.83e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458    301 TAAQNVSAGSQELSASAEQLSQGATEQASSAEEASSSMEEMASNVKQNADNANQTEKIAAQSAKDAEASGAAVGRAVNAM 380
Cdd:smart00283   4 EAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAVSAV 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458    381 QTIAEK-------ITIVQEIARQTDLLALNAAVEAARAGEHGKGFAVVASEVRKLAERSQAAAAEIGTL----------- 442
Cdd:smart00283  84 EELEESsdeigeiVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLikeiqeetnea 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458    443 ----------STETVKVAQEAGNMLAKLVPDIKKTAELVEEITAACREQDVGSAQINQAIQQLDKVGQQNASASEQVSST 512
Cdd:smart00283 164 vaameessseVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEISAA 243
                          250
                   ....*....|....*....
gi 27377458    513 SEELASQAEQLQSTIAYFR 531
Cdd:smart00283 244 AEELSGLAEELDELVERFK 262
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
347-533 1.03e-30

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: 119.47  E-value: 1.03e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458   347 QNADNANQTEKIAAQSAKDAEASGAAVGRAVNAMQTIAEKIT----IVQEIARQTDLLALNAAVEAARAGEHGKGFAVVA 422
Cdd:pfam00015   2 QASDLAQLASEEALDEMSQIGQVVDDAVETMEELETSSKKISdiisVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458   423 SEVRKLAERSQAAAAEIGTLSTETVK---------------------VAQEAGNMLAKLVPDIKKTAELVEEITAACREQ 481
Cdd:pfam00015  82 DEVRKLAERSAQAAKEIEALIEEIVKqtndstasiqqtrtevevgstIVESTGEALKEIVDAVAEIADIVQEIAAASDEQ 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 27377458   482 DVGSAQINQAIQQLDKVGQQNASASEQVSSTSEELASQAEQLQSTIAYFRIE 533
Cdd:pfam00015 162 SAGIDQVNQAVARIDQVTQQNAALVEESAAAAETLEEQAEELTASVAQFRIK 213
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
284-523 1.76e-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: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.04  E-value: 1.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458    284 ALERMVEKLRQIVSEALTAAQNVSAGSQELsASAEQLSQGATEQASSAEEASSSMEEMASNVKQNADNANQTEKIAAQSA 363
Cdd:TIGR02168  706 ELEELEEELEQLRKELEELSRQISALRKDL-ARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI 784
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458    364 KDAEASgaaVGRAVNAMQTIAEKITIVQEIARQTDLLALNAAVEAA----RAGEHGKGFAVVASEVRKLAERSQAAAAEI 439
Cdd:TIGR02168  785 EELEAQ---IEQLKEELKALREALDELRAELTLLNEEAANLRERLEslerRIAATERRLEDLEEQIEELSEDIESLAAEI 861
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458    440 GTLSTETVKVAQEAGNMLAKLVPDIKKTAELVEEITAACREQDVGSAQINQAIQQLDKVGQQNASASEQVSSTSEELASQ 519
Cdd:TIGR02168  862 EELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL 941

                   ....
gi 27377458    520 AEQL 523
Cdd:TIGR02168  942 QERL 945
valS PRK14900
valyl-tRNA synthetase; Provisional
467-580 7.69e-03

valyl-tRNA synthetase; Provisional


Pssm-ID: 237855 [Multi-domain]  Cd Length: 1052  Bit Score: 38.05  E-value: 7.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458   467 TAELVEEITAACREQDVGSAQINQAIQQLDKVGqqnaSASEQVSSTSEELASQAEQLQSTIAYFRIEQGGKGRAAAPIDR 546
Cdd:PRK14900  911 ARRDTMEIQNEQKPTQDGPAAEAQPAQENTVVE----SAEKAVAAVSEAAQQAATAVASGIEKVAEAVRKTVRRSVKKAA 986
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 27377458   547 AVNQLRAKAAT--MAAVERPARKPPAKPARAMKVAG 580
Cdd:PRK14900  987 ATRAAMKKKVAkkAPAKKAAAKKAAAKKAAAKKKVA 1022
 
Name Accession Description Interval E-value
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
208-255 6.97e-06

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


Pssm-ID: 100122  Cd Length: 48  Bit Score: 43.78  E-value: 6.97e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 27377458 208 ISRALAQAVGLADAVAIGDLSRKIESSSNDEIGDLIKSLNAMTVNLNA 255
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGDLDVRLPVTGRDEIGELARAFNQMAERLRE 48
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
304-510 2.60e-32

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: 123.50  E-value: 2.60e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458 304 QNVSAGSQELSASAEQLSqgateqassaeeasssmeemaSNVKQNADNANQTEKIAAQSAKDAEASGAAVGRAVNAM--- 380
Cdd:cd11386   1 EELSASIEEVAASADQVA---------------------ETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVeel 59
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458 381 ----QTIAEKITIVQEIARQTDLLALNAAVEAARAGEHGKGFAVVASEVRKLAERSQAAAAEIGTL-------STETVKV 449
Cdd:cd11386  60 eessAEIGEIVEVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELieeiqeqTEEAVEA 139
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27377458 450 AQEAGNMLAKLVPDIKKTAELVEEITAACREQDVGSAQINQAIQQLDKVGQQNASASEQVS 510
Cdd:cd11386 140 MEETSEEVEEGVELVEETGRAFEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
HAMP pfam00672
HAMP domain;
186-255 3.57e-09

HAMP domain;


Pssm-ID: 250044  Cd Length: 70  Bit Score: 53.77  E-value: 3.57e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458   186 LMSLVIASLLIAAVAATWIALNISRALAQAVGLADAVAIGDLSRKIESSSNDEIGDLIKSLNAMTVNLNA 255
Cdd:pfam00672   1 LLLVLLIALLLLLLLAWLLARRLLRPLRRLAEAARRIASGDLDDRVPVSGPDEIGELARAFNQMADRLRE 70
4HB_MCP_1 pfam12729
Four helix bundle sensory module for signal transduction; This family is a four helix bundle ...
2-183 3.72e-07

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: 49.15  E-value: 3.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458     2 RFTVKAKLASAFGVVILLSMIAGAVGYVKLSDMVGTTETLVS-RAGRMEKAAELKEGILFLVRAEKNSILAATDAEYDQF 80
Cdd:pfam12729   1 NLKIRTKLILLFLLLALLLIIVGIVGLYSLKKINKNSETMYEdRLLPIKWLGEIRSNLREIRANLLELILTTDPAERDEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458    81 VADLAKNREALVKSKDEIHAAAS-EGGKKLMESFSTAFAKLSAYQDETVRLAKS-DKPKALDrsmhdgrKVVADALEAAD 158
Cdd:pfam12729  81 LKDIEELRAEIDKLLKKYEKTILtEEEKKLFNEFKEQLKAYRKVRNKVLDLAKAgKNDEAYA-------LYLTELEPARD 153
                         170       180
                  ....*....|....*....|....*
gi 27377458   159 GYIKNVKKNMAEQAEQSKQDGARAE 183
Cdd:pfam12729 154 AVIEALDELIDYNLKVAKEAYEDNK 178
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
207-258 2.55e-06

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


Pssm-ID: 197640  Cd Length: 53  Bit Score: 45.32  E-value: 2.55e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 27377458    207 NISRALAQAVGLADAVAIGDLSRKIESSSNDEIGDLIKSLNAMTVNLNATAA 258
Cdd:smart00304   2 RLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRLEETIA 53
HAMP COG2770
HAMP domain [Signal transduction mechanisms];
189-254 5.24e-03

HAMP domain [Signal transduction mechanisms];


Pssm-ID: 225359  Cd Length: 83  Bit Score: 35.43  E-value: 5.24e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27377458 189 LVIASLLIAAVAATWIALNISRALAQAVGLADAVAIGDLSRKIESSSNDEIGDLIKSLNAMTVNLN 254
Cdd:COG2770  11 LVLALVLILAVLLLAAARRVTRPLRRLADLAQNLALGDLSAEIPQPMLDEIGELAKAFNRMRDSLQ 76
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility, Signal transduction mechanisms];
152-532 2.17e-42

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


Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 157.46  E-value: 2.17e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458 152 DALEAADGYIKNVKKNMAEQAEQSKQDGARAEMLLMSLVIASLLIAAVAATWIALNISRALAQAVGLADAVAIGDLSRKI 231
Cdd:COG0840  28 KLIDELGKLLLSLNLILDDAASAEAAALKAVLKFLLISLLVAIIVVLVLAILLLRAILEPISDLLEVVERIAAGDLTKRI 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458 232 ESSSNDEIGDLIKSLNamtvnlnataavaneiaqgnlmveakpqsdkdtlglaleRMVEKLRQIVSEALTAAQNVSAGSQ 311
Cdd:COG0840 108 DESSNDEFGQLAKSFN---------------------------------------EMILNLRQIIDAVQDNAEALSGASE 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458 312 ELSASAEQLSQGATEQASSAEEASSSMEEMASNVKQNADNANQTEKIAAQSAKDAEASGAAVGRAVNAMQTIAEK----- 386
Cdd:COG0840 149 EIAASATELSARADQQAESLEEVASAIEELSETVKEVAFNAKEAAALASEASQVAEEGGEEVRQAVEQMQEIAEElaevv 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458 387 -------------ITIVQEIARQTDLLALNAAVEAARAGEHGKGFAVVASEVRKLAERSQAAAAEIGTL----------- 442
Cdd:COG0840 229 kklsessqeieeiTSVINSIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSADSAKEIGLLieeiqneaada 308
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458 443 ----------STETVKVAQEAGNMLAKLVPDIKKTAELVEEITAACREQDVGSAQINQAIQQLDKVGQQNASASEQVSST 512
Cdd:COG0840 309 vehmeesaseVSEGVKLVEETGSSLGEIAAAIEEVSQLISEIAAATEEQTAVLEEINASIEELDDVTQENAAAVEELAAA 388
                       410       420
                ....*....|....*....|
gi 27377458 513 SEELASQAEQLQSTIAYFRI 532
Cdd:COG0840 389 SEELKELAEKLLELVAKFKL 408
PRK09793 PRK09793
methyl-accepting protein IV; Provisional
162-534 1.70e-44

methyl-accepting protein IV; Provisional


Pssm-ID: 182079 [Multi-domain]  Cd Length: 533  Bit Score: 165.63  E-value: 1.70e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458  162 KNVKKNMAEQAEQSKQDGARAEMLLMSLVIASLLIAAVAATWIALNISRALAQAVGLADAVAIGDLSRKIESSSNDEIGD 241
Cdd:PRK09793 168 LEINHVLEAASAQSQRNYQISALVFISMIIVAAIYISSALWWTRKMIVQPLAIIGSHFDSIAAGNLARPIAVYGRNEITA 247
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458  242 LIKSLNAMTVNLNATaavaneiaqgnlmveakpqsdkdtlglalermVEKLRQIVSEALTAAQNVSAGSQELSASAEQls 321
Cdd:PRK09793 248 IFASLKTMQQALRGT--------------------------------VSDVRKGSQEMHIGIAEIVAGNNDLSSRTEQ-- 293
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458  322 qgateQASSAEEASSSMEEMASNVKQNADNANQTEKIAAQSAKDAEASGAAVGRAVNAMQTIAEK-------ITIVQEIA 394
Cdd:PRK09793 294 -----QAASLAQTAASMEQLTATVGQNADNARQASELAKNAATTAQAGGVQVSTMTHTMQEIATSsqkigdiISVIDGIA 368
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458  395 RQTDLLALNAAVEAARAGEHGKGFAVVASEVRKLAERSQAAAAEIGTLSTETVKVAQE-------AGNMLAKLVPDIKKT 467
Cdd:PRK09793 369 FQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKGLIEESVNRVQQgsklvnnAAATMTDIVSSVTRV 448
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27377458  468 AELVEEITAACREQDVGSAQINQAIQQLDKVGQQNASASEQVSSTSEELASQAEQLQSTIAYFRIEQ 534
Cdd:PRK09793 449 NDIMGEIASASEEQRRGIEQVAQAVSQMDQVTQQNASLVEEAAVATEQLANQADHLSSRVAVFTLEE 515
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
301-531 2.83e-41

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: 150.13  E-value: 2.83e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458    301 TAAQNVSAGSQELSASAEQLSQGATEQASSAEEASSSMEEMASNVKQNADNANQTEKIAAQSAKDAEASGAAVGRAVNAM 380
Cdd:smart00283   4 EAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAVSAV 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458    381 QTIAEK-------ITIVQEIARQTDLLALNAAVEAARAGEHGKGFAVVASEVRKLAERSQAAAAEIGTL----------- 442
Cdd:smart00283  84 EELEESsdeigeiVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLikeiqeetnea 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458    443 ----------STETVKVAQEAGNMLAKLVPDIKKTAELVEEITAACREQDVGSAQINQAIQQLDKVGQQNASASEQVSST 512
Cdd:smart00283 164 vaameessseVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEISAA 243
                          250
                   ....*....|....*....
gi 27377458    513 SEELASQAEQLQSTIAYFR 531
Cdd:smart00283 244 AEELSGLAEELDELVERFK 262
PRK15041 PRK15041
methyl-accepting chemotaxis protein I; Provisional
173-559 4.73e-41

methyl-accepting chemotaxis protein I; Provisional


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 155.50  E-value: 4.73e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458  173 EQSKQDGARAEMLLMSLVIASLLIAAVAATWIALNISRALAQAVGLADAVAIGDLSRKIESSSNDEIGDLIKSLNAMtvn 252
Cdd:PRK15041 183 SDNNASYSQAMWILVGVMIVVLAVIFAVWFGIKASLVAPMNRLIDSIRHIAGGDLVKPIEVDGSNEMGQLAESLRHM--- 259
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458  253 lnataavaneiaQGNLMveakpqsdkdtlglaleRMVEKLRQIVSEALTAAQNVSAGSQELSASAEQlsqgateQASSAE 332
Cdd:PRK15041 260 ------------QGELM-----------------RTVGDVRNGANAIYSGASEIATGNNDLSSRTEQ-------QAASLE 303
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458  333 EASSSMEEMASNVKQNADNANQTEKIAAQSAKDAEASGAAVGRAVNAM-------QTIAEKITIVQEIARQTDLLALNAA 405
Cdd:PRK15041 304 ETAASMEQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQTMrdistssQKIADIISVIDGIAFQTNILALNAA 383
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458  406 VEAARAGEHGKGFAVVASEVRKLAERSQAAAAEIGTLSTETVK-------VAQEAGNMLAKLVPDIKKTAELVEEITAAC 478
Cdd:PRK15041 384 VEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGkvdvgstLVESAGETMAEIVSAVTRVTDIMGEIASAS 463
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458  479 REQDVGSAQINQAIQQLDKVGQQNASASEQVSSTSEELASQAEQLQSTIAYFRIEQGG-KGRAAAPIDRAVNQLRAKAAT 557
Cdd:PRK15041 464 DEQSRGIDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAVFRIQQQQqQQRETSAVVKTVTPATPRKMA 543

                 ..
gi 27377458  558 MA 559
Cdd:PRK15041 544 VA 545
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
155-566 1.54e-39

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 150.93  E-value: 1.54e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458  155 EAADGYIKNVKKNMAEQAEQSKQDGARAEMLLMSLVIASLLIAAVAATWIALNISRALAQAVGLADAVAIGDLSRKIESS 234
Cdd:PRK15048 163 EAFAQYALSSEKLYRDIVTDNADDYRFAQWQLAVIALVVVLILLVAWYGIRRMLLTPLAKIIAHIREIAGGNLANTLTID 242
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458  235 SNDEIGDLIKSLNAMTVNLNATaavaneiaqgnlmveakpqsdkdtlglalermVEKLRQIVSEALTAAQNVSAGSQELS 314
Cdd:PRK15048 243 GRSEMGDLAQSVSHMQRSLTDT--------------------------------VTHVREGSDAIYAGTREIAAGNTDLS 290
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458  315 ASAEQlsqgateQASSAEEASSSMEEMASNVKQNADNANQTEKIAAQSAKDAEASGAAVGRAVNAMQTIAEK-------I 387
Cdd:PRK15048 291 SRTEQ-------QASALEETAASMEQLTATVKQNADNARQASQLAQSASDTAQHGGKVVDGVVKTMHEIADSskkiadiI 363
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458  388 TIVQEIARQTDLLALNAAVEAARAGEHGKGFAVVASEVRKLAERSQAAAAEIGTLSTETVK-------VAQEAGNMLAKL 460
Cdd:PRK15048 364 SVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKALIEDSVSrvdtgsvLVESAGETMNNI 443
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458  461 VPDIKKTAELVEEITAACREQDVGSAQINQAIQQLDKVGQQNASASEQVSSTSEELASQAEQLQSTIAYFRIeqggkgrA 540
Cdd:PRK15048 444 VNAVTRVTDIMGEIASASDEQSRGIDQVALAVSEMDRVTQQNASLVQESAAAAAALEEQASRLTQAVSAFRL-------A 516
                        410       420
                 ....*....|....*....|....*.
gi 27377458  541 AAPIDRAVNQLRAKAATMAAVERPAR 566
Cdd:PRK15048 517 ASPLTNKPQTPSRPASEQPPAQPRLR 542
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
347-533 1.03e-30

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: 119.47  E-value: 1.03e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458   347 QNADNANQTEKIAAQSAKDAEASGAAVGRAVNAMQTIAEKIT----IVQEIARQTDLLALNAAVEAARAGEHGKGFAVVA 422
Cdd:pfam00015   2 QASDLAQLASEEALDEMSQIGQVVDDAVETMEELETSSKKISdiisVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458   423 SEVRKLAERSQAAAAEIGTLSTETVK---------------------VAQEAGNMLAKLVPDIKKTAELVEEITAACREQ 481
Cdd:pfam00015  82 DEVRKLAERSAQAAKEIEALIEEIVKqtndstasiqqtrtevevgstIVESTGEALKEIVDAVAEIADIVQEIAAASDEQ 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 27377458   482 DVGSAQINQAIQQLDKVGQQNASASEQVSSTSEELASQAEQLQSTIAYFRIE 533
Cdd:pfam00015 162 SAGIDQVNQAVARIDQVTQQNAALVEESAAAAETLEEQAEELTASVAQFRIK 213
NtrY COG5000
Signal transduction histidine kinase involved in nitrogen fixation and metabolism regulation ...
150-253 7.22e-05

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


Pssm-ID: 227333 [Multi-domain]  Cd Length: 712  Bit Score: 44.37  E-value: 7.22e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458 150 VADALEAadgyiknVKKNMAEQAEQSK-QDGARAEMLLMSLVIAslLIAAVAATWIAL----NISRALAQAVGLADAVAI 224
Cdd:COG5000 251 VAEHADL-------TEGAAAEYRELEAgRDGLQIAFALLYLSTA--LLVLLAAIWTAIafarRIVRPIRKLIEAADEVAD 321
                        90       100       110
                ....*....|....*....|....*....|
gi 27377458 225 GDLSRKIESSSNDE-IGDLIKSLNAMTVNL 253
Cdd:COG5000 322 GDLDVQVPVRRVDEdVGRLSKAFNKMTEQL 351
YhgE COG1511
Uncharacterized membrane protein YhgE, phage infection protein (PIP) family [Function unknown]; ...
214-525 1.74e-04

Uncharacterized membrane protein YhgE, phage infection protein (PIP) family [Function unknown];


Pssm-ID: 224428 [Multi-domain]  Cd Length: 780  Bit Score: 43.26  E-value: 1.74e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458 214 QAVGLADAVAIGDLSRKIESSSnDEIGDLIKSLNAMTVNLNATAAVANEIAQGNLMVEAKPQSDKDTLGLALERMVEKLR 293
Cdd:COG1511 159 ELTETYTKVVAFPTIYDLGGGV-KGAADGAEKLKDGTDEASNGNKKLSDLLNTLNNSSATFSDGLNALTSGLTTLTDGLN 237
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458 294 QIVSEALTaaqnVSAGSQELSASAEQLSQGATEQASSAEEASSSMEEMASNVKQ--------------------NADNAN 353
Cdd:COG1511 238 QLDSGLGT----LAAGIGELKQGAEQLNEGIGEFSSGLSELNSGVQDLAAGVPQlnqgisalaaglslpdslgdQFSSLQ 313
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458 354 QTEKIAAQSAKDA-EASGAAVGRAVNAMQTIAekitivqEIARQTDLLALNAAVEAARAGEHGKGFAVVASEVRKLAERS 432
Cdd:COG1511 314 EALTQIAQGLKQKtSSSLEAAQGSLSSLQSML-------ALSKSLDLTAEGATVDALGAPDGVQWLDESQKTLATLSELL 386
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458 433 QAAAAEIGTL-------STETVKVAQEAGNMLAKLVPDIKKTAELVEEITAACREQdvGSAQINQAIQQLDKVGQQNAS- 504
Cdd:COG1511 387 STGIDGVSEGldaleqaSAQLAKSLAKLKTAVAQIAASIAQLLPGASEVLKTLKSK--GLDKLLNQLNGALAKGSNALVq 464
                       330       340       350
                ....*....|....*....|....*....|...
gi 27377458 505 ------------ASEQVSSTSEELASQAEQLQS 525
Cdd:COG1511 465 glsdandsfrsiTSAQLKAGLNTLADGSNDLSS 497
PTZ00121 PTZ00121
MAEBL; Provisional
271-522 1.44e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458   271 EAKPQSDKDTLGLALERMVEKLRQivSEALTAAQNVSAGSQELSASAEQLSQGATEQASSAEEASSSMEEMASNVKQNAD 350
Cdd:PTZ00121 1448 EAKKKAEEAKKAEEAKKKAEEAKK--ADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKAD 1525
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458   351 NANQTE-KIAAQSAKDAEASGAA--VGRAVNAMQtiAEKITIVQEIARQTD--LLALNAAVEAARAGEHGKGFAVVASEV 425
Cdd:PTZ00121 1526 EAKKAEeAKKADEAKKAEEKKKAdeLKKAEELKK--AEEKKKAEEAKKAEEdkNMALRKAEEAKKAEEARIEEVMKLYEE 1603
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458   426 RKLAERSQAAAAEIGTLSTETVKVAQEAGNMLAKLVPDIKKTAELVEEITAACREQDVGSAQINQAIQQLDKVGQQNASA 505
Cdd:PTZ00121 1604 EKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKA 1683
                         250
                  ....*....|....*..
gi 27377458   506 SEQVSSTSEELASQAEQ 522
Cdd:PTZ00121 1684 EEDEKKAAEALKKEAEE 1700
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
284-523 1.76e-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: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.04  E-value: 1.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458    284 ALERMVEKLRQIVSEALTAAQNVSAGSQELsASAEQLSQGATEQASSAEEASSSMEEMASNVKQNADNANQTEKIAAQSA 363
Cdd:TIGR02168  706 ELEELEEELEQLRKELEELSRQISALRKDL-ARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI 784
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458    364 KDAEASgaaVGRAVNAMQTIAEKITIVQEIARQTDLLALNAAVEAA----RAGEHGKGFAVVASEVRKLAERSQAAAAEI 439
Cdd:TIGR02168  785 EELEAQ---IEQLKEELKALREALDELRAELTLLNEEAANLRERLEslerRIAATERRLEDLEEQIEELSEDIESLAAEI 861
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458    440 GTLSTETVKVAQEAGNMLAKLVPDIKKTAELVEEITAACREQDVGSAQINQAIQQLDKVGQQNASASEQVSSTSEELASQ 519
Cdd:TIGR02168  862 EELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL 941

                   ....
gi 27377458    520 AEQL 523
Cdd:TIGR02168  942 QERL 945
PTZ00121 PTZ00121
MAEBL; Provisional
82-524 5.66e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.58  E-value: 5.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458    82 ADLAKNREALVKSKDEIHAAASEGGKKLMESFSTAFAKLSAYQDETVRLAKSDKPKALDRSMHDGRKVVADALEAadgyi 161
Cdd:PTZ00121 1311 AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKK----- 1385
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458   162 KNVKKNMAEQAEQ-SKQDGARAEMLLMSlviASLLIAAVAATWIALNISRALAQAVGLADAVAIGDLSRKIESSSNDEig 240
Cdd:PTZ00121 1386 KAEEKKKADEAKKkAEEDKKKADELKKA---AAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAE-- 1460
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458   241 dlikslnamtvNLNATAAVANEIAQGNLMVEAKPQSDKdtlglaLERMVEKLRQIVSEALTAAQNVSAGSQ----ELSAS 316
Cdd:PTZ00121 1461 -----------EAKKKAEEAKKADEAKKKAEEAKKADE------AKKKAEEAKKKADEAKKAAEAKKKADEakkaEEAKK 1523
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458   317 AEQLSQgATEQASSAEEASSSMEEMASNVKQNADNANQTEKIAAQSAKDAEASGAAVGRAVNAMQTIAEKItiVQEIARQ 396
Cdd:PTZ00121 1524 ADEAKK-AEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAR--IEEVMKL 1600
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458   397 TDLLALNAAVEAARAGEHGKGFAVV--ASEVRKLAERSQAAAAEiGTLSTETVKVAQEAGNM----LAKLVPDIKKTAEL 470
Cdd:PTZ00121 1601 YEEEKKMKAEEAKKAEEAKIKAEELkkAEEEKKKVEQLKKKEAE-EKKKAEELKKAEEENKIkaaeEAKKAEEDKKKAEE 1679
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 27377458   471 V---EEITAACREQDVGSAQINQAIQQLDKVGQQNASASEQVSSTSEELASQAEQLQ 524
Cdd:PTZ00121 1680 AkkaEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAK 1736
valS PRK14900
valyl-tRNA synthetase; Provisional
467-580 7.69e-03

valyl-tRNA synthetase; Provisional


Pssm-ID: 237855 [Multi-domain]  Cd Length: 1052  Bit Score: 38.05  E-value: 7.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377458   467 TAELVEEITAACREQDVGSAQINQAIQQLDKVGqqnaSASEQVSSTSEELASQAEQLQSTIAYFRIEQGGKGRAAAPIDR 546
Cdd:PRK14900  911 ARRDTMEIQNEQKPTQDGPAAEAQPAQENTVVE----SAEKAVAAVSEAAQQAATAVASGIEKVAEAVRKTVRRSVKKAA 986
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 27377458   547 AVNQLRAKAAT--MAAVERPARKPPAKPARAMKVAG 580
Cdd:PRK14900  987 ATRAAMKKKVAkkAPAKKAAAKKAAAKKAAAKKKVA 1022
 
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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