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Conserved domains on  [gi|107026920|ref|YP_624431|]
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methyl-accepting chemotaxis sensory transducer [Burkholderia cenocepacia AU 1054]

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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. ...
229-276 1.55e-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: 45.70  E-value: 1.55e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 107026920 229 VTVPMARLVEVHDVMRTGNLTHRLDLRRRDEFGTLETGFNRMADELTE 276
Cdd:cd06225    1 ILRPLRRLAEAAQRIAAGDLDVRLPVTGRDEIGELARAFNQMAERLRE 48
MCP_signal super family cl19050
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
321-520 1.75e-36

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: 267403  Cd Length: 200  Bit Score: 134.29  E-value: 1.75e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920 321 REIFATSRDLLRTMNEVAGVAEQSATLAGVSQSGLTRMGETMRSVMDAAGSVNAKLAILNEKALNINQVVATITKVADQT 400
Cdd:cd11386    1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920 401 NLLSLNAAIEAEKAGEYGRGFAVVATEIRRLADQTAVATYDIEQTVKEIQSAVSAGVMGMDKFSEEVRRGMLDVQQVGGQ 480
Cdd:cd11386   81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 107026920 481 LSQIIAEVQTLAPRFQMVNEGMQTQANGAEQITQALSQLS 520
Cdd:cd11386  161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
Tar_Tsr_LBD super family cl00144
ligand binding domain of Tar- and Tsr-related chemoreceptors; E.coli Tar (taxis to aspartate ...
21-192 2.42e-19

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: 85.74  E-value: 2.42e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920   21 RLTLGNRILLSFGVLFVLMLVTAGVSYERLRAINAEAVSIERDSLPGVYLASSLRAAVNETFVMLQQAtFVETDPDAVQR 100
Cdd:pfam12729   1 NLKIRTKLILLFLLLALLLIIVGIVGLYSLKKINKNSETMYEDRLLPIKWLGEIRSNLREIRANLLEL-ILTTDPAERDE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920  101 DLAKIADATKQVESLSVDYQASIFRDDDRARFATFRGAYDRYLPLLTDAVQRHR-GSRDEAIAAYAK-VLPGWAEVVQDA 178
Cdd:pfam12729  80 LLKDIEELRAEIDKLLKKYEKTILTEEEKKLFNEFKEQLKAYRKVRNKVLDLAKaGKNDEAYALYLTeLEPARDAVIEAL 159
                         170
                  ....*....|....
gi 107026920  179 NIMVQENRKFADQS 192
Cdd:pfam12729 160 DELIDYNLKVAKEA 173
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction ...
144-556 3.53e-59

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


:

Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 203.68  E-value: 3.53e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920 144 PLLTDAVQRHRGSRDEAIAAYAKVLPGWAEVVQDANIMVQenrkfaDQSARVIRESVQDAEVVLVGALTIMLLSALgLGY 223
Cdd:COG0840    6 PLNLELIELAAGEADAGLLKLKKLIDELGKLLLSLNLILD------DAASAEAAALKAVLKFLLISLLVAIIVVLV-LAI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920 224 MLYRSVTVPMARLVEVHDVMRTGNLTHRLDLRRRDEFGTLETGFNRMADELTELVARAQQSSMQVTTSVAEIAATSREQQ 303
Cdd:COG0840   79 LLLRAILEPISDLLEVVERIAAGDLTKRIDESSNDEFGQLAKSFNEMILNLRQIIDAVQDNAEALSGASEEIAASATELS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920 304 ATANETAATTTEIGATSREIFATSRDLLRTMNEVAGVAEQSATLAgvsQSGLTRMGETMRSVMDAAGSVNAKLAILNEKA 383
Cdd:COG0840  159 ARADQQAESLEEVASAIEELSETVKEVAFNAKEAAALASEASQVA---EEGGEEVRQAVEQMQEIAEELAEVVKKLSESS 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920 384 LNINQVVATITKVADQTNLLSLNAAIEAEKAGEYGRGFAVVATEIRRLADQTAVATYDIEQTVKEIQSAVSAGVMGMDKF 463
Cdd:COG0840  236 QEIEEITSVINSIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSADSAKEIGLLIEEIQNEAADAVEHMEES 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920 464 SEEVRRGMLDVQQVGGQLSQIIAEVQTLAPRFQMVNEGMQTQANGAEQITQALSQLSEAAQQTAESLRQSSQAIDDLTLV 543
Cdd:COG0840  316 ASEVSEGVKLVEETGSSLGEIAAAIEEVSQLISEIAAATEEQTAVLEEINASIEELDDVTQENAAAVEELAAASEELKEL 395
                        410
                 ....*....|...
gi 107026920 544 ANQLRTSVSRFKV 556
Cdd:COG0840  396 AEKLLELVAKFKL 408
 
Name Accession Description Interval E-value
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
229-276 1.55e-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: 45.70  E-value: 1.55e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 107026920 229 VTVPMARLVEVHDVMRTGNLTHRLDLRRRDEFGTLETGFNRMADELTE 276
Cdd:cd06225    1 ILRPLRRLAEAAQRIAAGDLDVRLPVTGRDEIGELARAFNQMAERLRE 48
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
321-520 1.75e-36

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: 134.29  E-value: 1.75e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920 321 REIFATSRDLLRTMNEVAGVAEQSATLAGVSQSGLTRMGETMRSVMDAAGSVNAKLAILNEKALNINQVVATITKVADQT 400
Cdd:cd11386    1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920 401 NLLSLNAAIEAEKAGEYGRGFAVVATEIRRLADQTAVATYDIEQTVKEIQSAVSAGVMGMDKFSEEVRRGMLDVQQVGGQ 480
Cdd:cd11386   81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 107026920 481 LSQIIAEVQTLAPRFQMVNEGMQTQANGAEQITQALSQLS 520
Cdd:cd11386  161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
4HB_MCP_1 pfam12729
Four helix bundle sensory module for signal transduction; This family is a four helix bundle ...
21-192 2.42e-19

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: 85.74  E-value: 2.42e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920   21 RLTLGNRILLSFGVLFVLMLVTAGVSYERLRAINAEAVSIERDSLPGVYLASSLRAAVNETFVMLQQAtFVETDPDAVQR 100
Cdd:pfam12729   1 NLKIRTKLILLFLLLALLLIIVGIVGLYSLKKINKNSETMYEDRLLPIKWLGEIRSNLREIRANLLEL-ILTTDPAERDE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920  101 DLAKIADATKQVESLSVDYQASIFRDDDRARFATFRGAYDRYLPLLTDAVQRHR-GSRDEAIAAYAK-VLPGWAEVVQDA 178
Cdd:pfam12729  80 LLKDIEELRAEIDKLLKKYEKTILTEEEKKLFNEFKEQLKAYRKVRNKVLDLAKaGKNDEAYALYLTeLEPARDAVIEAL 159
                         170
                  ....*....|....
gi 107026920  179 NIMVQENRKFADQS 192
Cdd:pfam12729 160 DELIDYNLKVAKEA 173
HAMP pfam00672
HAMP domain;
207-276 2.42e-09

HAMP domain;


Pssm-ID: 250044  Cd Length: 70  Bit Score: 54.16  E-value: 2.42e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920  207 LVGALTIMLLSALGLGYMLYRSVTVPMARLVEVHDVMRTGNLTHRLDLRRRDEFGTLETGFNRMADELTE 276
Cdd:pfam00672   1 LLLVLLIALLLLLLLAWLLARRLLRPLRRLAEAARRIASGDLDDRVPVSGPDEIGELARAFNQMADRLRE 70
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
227-279 1.04e-07

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


Pssm-ID: 197640  Cd Length: 53  Bit Score: 49.17  E-value: 1.04e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 107026920   227 RSVTVPMARLVEVHDVMRTGNLTHRLDLRRRDEFGTLETGFNRMADELTELVA 279
Cdd:smart00304   1 RRLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRLEETIA 53
ResE COG2770
FOG: HAMP domain [Signal transduction mechanisms]
210-274 2.90e-03

FOG: HAMP domain [Signal transduction mechanisms]


Pssm-ID: 225359  Cd Length: 83  Bit Score: 36.20  E-value: 2.90e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 107026920 210 ALTIMLLSALGLGYMLYRSVTVPMARLVEVHDVMRTGNLTHRLDLRRRDEFGTLETGFNRMADEL 274
Cdd:COG2770   11 LVLALVLILAVLLLAAARRVTRPLRRLADLAQNLALGDLSAEIPQPMLDEIGELAKAFNRMRDSL 75
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction ...
144-556 3.53e-59

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


Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 203.68  E-value: 3.53e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920 144 PLLTDAVQRHRGSRDEAIAAYAKVLPGWAEVVQDANIMVQenrkfaDQSARVIRESVQDAEVVLVGALTIMLLSALgLGY 223
Cdd:COG0840    6 PLNLELIELAAGEADAGLLKLKKLIDELGKLLLSLNLILD------DAASAEAAALKAVLKFLLISLLVAIIVVLV-LAI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920 224 MLYRSVTVPMARLVEVHDVMRTGNLTHRLDLRRRDEFGTLETGFNRMADELTELVARAQQSSMQVTTSVAEIAATSREQQ 303
Cdd:COG0840   79 LLLRAILEPISDLLEVVERIAAGDLTKRIDESSNDEFGQLAKSFNEMILNLRQIIDAVQDNAEALSGASEEIAASATELS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920 304 ATANETAATTTEIGATSREIFATSRDLLRTMNEVAGVAEQSATLAgvsQSGLTRMGETMRSVMDAAGSVNAKLAILNEKA 383
Cdd:COG0840  159 ARADQQAESLEEVASAIEELSETVKEVAFNAKEAAALASEASQVA---EEGGEEVRQAVEQMQEIAEELAEVVKKLSESS 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920 384 LNINQVVATITKVADQTNLLSLNAAIEAEKAGEYGRGFAVVATEIRRLADQTAVATYDIEQTVKEIQSAVSAGVMGMDKF 463
Cdd:COG0840  236 QEIEEITSVINSIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSADSAKEIGLLIEEIQNEAADAVEHMEES 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920 464 SEEVRRGMLDVQQVGGQLSQIIAEVQTLAPRFQMVNEGMQTQANGAEQITQALSQLSEAAQQTAESLRQSSQAIDDLTLV 543
Cdd:COG0840  316 ASEVSEGVKLVEETGSSLGEIAAAIEEVSQLISEIAAATEEQTAVLEEINASIEELDDVTQENAAAVEELAAASEELKEL 395
                        410
                 ....*....|...
gi 107026920 544 ANQLRTSVSRFKV 556
Cdd:COG0840  396 AEKLLELVAKFKL 408
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
287-555 4.12e-45

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: 160.91  E-value: 4.12e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920   287 QVTTSVAEIAATSREQQATANETAATTTEIGATSREIFATsrdllrtMNEVAGVAEQSATLAGVSQSGLTRMGETMRSVM 366
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAAN-------ADEIAATAQSAAEAAEEGREAVEDAITAMDQIR 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920   367 DAAGSVNAKLAILNEKALNINQVVATITKVADQTNLLSLNAAIEAEKAGEYGRGFAVVATEIRRLADQTAVATYDIEQTV 446
Cdd:smart00283  74 EVVEEAVSAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLI 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920   447 KEIQSAVSAGVMGMDKFSEEVRRGMLDVQQVGGQLSQIIAEVQTLAPRFQMVNEGMQTQANGAEQITQALSQLSEAAQQT 526
Cdd:smart00283 154 KEIQEETNEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQET 233
                          250       260
                   ....*....|....*....|....*....
gi 107026920   527 AESLRQSSQAIDDLTLVANQLRTSVSRFK 555
Cdd:smart00283 234 AAMSEEISAAAEELSGLAEELDELVERFK 262
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
351-556 5.13e-31

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: 5.13e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920  351 SQSGLTRMGETMRSVMDAAGSVNAklaiLNEKALNINQVVATITKVADQTNLLSLNAAIEAEKAGEYGRGFAVVATEIRR 430
Cdd:pfam00015  11 SEEALDEMSQIGQVVDDAVETMEE----LETSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920  431 LADQTAVATYDIEQTVKEIQSAVSAGVMGMDKFSEEVRRGMLDVQQVGGQLSQIIAEVQTLAPRFQMVNEGMQTQANGAE 510
Cdd:pfam00015  87 LAERSAQAAKEIEALIEEIVKQTNDSTASIQQTRTEVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDEQSAGID 166
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 107026920  511 QITQALSQLSEAAQQTAESLRQSSQAIDDLTLVANQLRTSVSRFKV 556
Cdd:pfam00015 167 QVNQAVARIDQVTQQNAALVEESAAAAETLEEQAEELTASVAQFRI 212
PRK09793 PRK09793
methyl-accepting protein IV; Provisional
183-557 1.10e-28

methyl-accepting protein IV; Provisional


Pssm-ID: 182079 [Multi-domain]  Cd Length: 533  Bit Score: 118.64  E-value: 1.10e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920 183 QENRKFADQSARVIRESVQDAEVVLVgalTIMLLSALGLGYMLY---RSVTVPMARLVEVHDVMRTGNLTHRLDLRRRDE 259
Cdd:PRK09793 168 LEINHVLEAASAQSQRNYQISALVFI---SMIIVAAIYISSALWwtrKMIVQPLAIIGSHFDSIAAGNLARPIAVYGRNE 244
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920 260 FGTLETGFNRMADELTELVARAQQSSMQVTTSVAEIAATSREQQATANETAATTTEIGATSREIFATSRDLLRTMNEVAG 339
Cdd:PRK09793 245 ITAIFASLKTMQQALRGTVSDVRKGSQEMHIGIAEIVAGNNDLSSRTEQQAASLAQTAASMEQLTATVGQNADNARQASE 324
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920 340 VAEQSATLAGVSQSGLTRMGETMRSVmdAAGSvnaklailnekaLNINQVVATITKVADQTNLLSLNAAIEAEKAGEYGR 419
Cdd:PRK09793 325 LAKNAATTAQAGGVQVSTMTHTMQEI--ATSS------------QKIGDIISVIDGIAFQTNILALNAAVEAARAGEQGR 390
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920 420 GFAVVATEIRRLADQTAVATYDIEQTVKEIQSAVSAGvmgmDKFSEEVRRGMLDVQQVGGQLSQIIAEVQTLAprfqmvn 499
Cdd:PRK09793 391 GFAVVAGEVRNLASRSAQAAKEIKGLIEESVNRVQQG----SKLVNNAAATMTDIVSSVTRVNDIMGEIASAS------- 459
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 107026920 500 egmQTQANGAEQITQALSQLSEAAQQTAESLRQSSQAIDDLTLVANQLRTSVSRFKVD 557
Cdd:PRK09793 460 ---EEQRRGIEQVAQAVSQMDQVTQQNASLVEEAAVATEQLANQADHLSSRVAVFTLE 514
 
Name Accession Description Interval E-value
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
229-276 1.55e-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: 45.70  E-value: 1.55e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 107026920 229 VTVPMARLVEVHDVMRTGNLTHRLDLRRRDEFGTLETGFNRMADELTE 276
Cdd:cd06225    1 ILRPLRRLAEAAQRIAAGDLDVRLPVTGRDEIGELARAFNQMAERLRE 48
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
321-520 1.75e-36

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: 134.29  E-value: 1.75e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920 321 REIFATSRDLLRTMNEVAGVAEQSATLAGVSQSGLTRMGETMRSVMDAAGSVNAKLAILNEKALNINQVVATITKVADQT 400
Cdd:cd11386    1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920 401 NLLSLNAAIEAEKAGEYGRGFAVVATEIRRLADQTAVATYDIEQTVKEIQSAVSAGVMGMDKFSEEVRRGMLDVQQVGGQ 480
Cdd:cd11386   81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 107026920 481 LSQIIAEVQTLAPRFQMVNEGMQTQANGAEQITQALSQLS 520
Cdd:cd11386  161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
4HB_MCP_1 pfam12729
Four helix bundle sensory module for signal transduction; This family is a four helix bundle ...
21-192 2.42e-19

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: 85.74  E-value: 2.42e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920   21 RLTLGNRILLSFGVLFVLMLVTAGVSYERLRAINAEAVSIERDSLPGVYLASSLRAAVNETFVMLQQAtFVETDPDAVQR 100
Cdd:pfam12729   1 NLKIRTKLILLFLLLALLLIIVGIVGLYSLKKINKNSETMYEDRLLPIKWLGEIRSNLREIRANLLEL-ILTTDPAERDE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920  101 DLAKIADATKQVESLSVDYQASIFRDDDRARFATFRGAYDRYLPLLTDAVQRHR-GSRDEAIAAYAK-VLPGWAEVVQDA 178
Cdd:pfam12729  80 LLKDIEELRAEIDKLLKKYEKTILTEEEKKLFNEFKEQLKAYRKVRNKVLDLAKaGKNDEAYALYLTeLEPARDAVIEAL 159
                         170
                  ....*....|....
gi 107026920  179 NIMVQENRKFADQS 192
Cdd:pfam12729 160 DELIDYNLKVAKEA 173
HAMP pfam00672
HAMP domain;
207-276 2.42e-09

HAMP domain;


Pssm-ID: 250044  Cd Length: 70  Bit Score: 54.16  E-value: 2.42e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920  207 LVGALTIMLLSALGLGYMLYRSVTVPMARLVEVHDVMRTGNLTHRLDLRRRDEFGTLETGFNRMADELTE 276
Cdd:pfam00672   1 LLLVLLIALLLLLLLAWLLARRLLRPLRRLAEAARRIASGDLDDRVPVSGPDEIGELARAFNQMADRLRE 70
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
227-279 1.04e-07

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


Pssm-ID: 197640  Cd Length: 53  Bit Score: 49.17  E-value: 1.04e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 107026920   227 RSVTVPMARLVEVHDVMRTGNLTHRLDLRRRDEFGTLETGFNRMADELTELVA 279
Cdd:smart00304   1 RRLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRLEETIA 53
ResE COG2770
FOG: HAMP domain [Signal transduction mechanisms]
210-274 2.90e-03

FOG: HAMP domain [Signal transduction mechanisms]


Pssm-ID: 225359  Cd Length: 83  Bit Score: 36.20  E-value: 2.90e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 107026920 210 ALTIMLLSALGLGYMLYRSVTVPMARLVEVHDVMRTGNLTHRLDLRRRDEFGTLETGFNRMADEL 274
Cdd:COG2770   11 LVLALVLILAVLLLAAARRVTRPLRRLADLAQNLALGDLSAEIPQPMLDEIGELAKAFNRMRDSL 75
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction ...
144-556 3.53e-59

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


Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 203.68  E-value: 3.53e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920 144 PLLTDAVQRHRGSRDEAIAAYAKVLPGWAEVVQDANIMVQenrkfaDQSARVIRESVQDAEVVLVGALTIMLLSALgLGY 223
Cdd:COG0840    6 PLNLELIELAAGEADAGLLKLKKLIDELGKLLLSLNLILD------DAASAEAAALKAVLKFLLISLLVAIIVVLV-LAI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920 224 MLYRSVTVPMARLVEVHDVMRTGNLTHRLDLRRRDEFGTLETGFNRMADELTELVARAQQSSMQVTTSVAEIAATSREQQ 303
Cdd:COG0840   79 LLLRAILEPISDLLEVVERIAAGDLTKRIDESSNDEFGQLAKSFNEMILNLRQIIDAVQDNAEALSGASEEIAASATELS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920 304 ATANETAATTTEIGATSREIFATSRDLLRTMNEVAGVAEQSATLAgvsQSGLTRMGETMRSVMDAAGSVNAKLAILNEKA 383
Cdd:COG0840  159 ARADQQAESLEEVASAIEELSETVKEVAFNAKEAAALASEASQVA---EEGGEEVRQAVEQMQEIAEELAEVVKKLSESS 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920 384 LNINQVVATITKVADQTNLLSLNAAIEAEKAGEYGRGFAVVATEIRRLADQTAVATYDIEQTVKEIQSAVSAGVMGMDKF 463
Cdd:COG0840  236 QEIEEITSVINSIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSADSAKEIGLLIEEIQNEAADAVEHMEES 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920 464 SEEVRRGMLDVQQVGGQLSQIIAEVQTLAPRFQMVNEGMQTQANGAEQITQALSQLSEAAQQTAESLRQSSQAIDDLTLV 543
Cdd:COG0840  316 ASEVSEGVKLVEETGSSLGEIAAAIEEVSQLISEIAAATEEQTAVLEEINASIEELDDVTQENAAAVEELAAASEELKEL 395
                        410
                 ....*....|...
gi 107026920 544 ANQLRTSVSRFKV 556
Cdd:COG0840  396 AEKLLELVAKFKL 408
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
287-555 4.12e-45

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: 160.91  E-value: 4.12e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920   287 QVTTSVAEIAATSREQQATANETAATTTEIGATSREIFATsrdllrtMNEVAGVAEQSATLAGVSQSGLTRMGETMRSVM 366
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAAN-------ADEIAATAQSAAEAAEEGREAVEDAITAMDQIR 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920   367 DAAGSVNAKLAILNEKALNINQVVATITKVADQTNLLSLNAAIEAEKAGEYGRGFAVVATEIRRLADQTAVATYDIEQTV 446
Cdd:smart00283  74 EVVEEAVSAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLI 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920   447 KEIQSAVSAGVMGMDKFSEEVRRGMLDVQQVGGQLSQIIAEVQTLAPRFQMVNEGMQTQANGAEQITQALSQLSEAAQQT 526
Cdd:smart00283 154 KEIQEETNEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQET 233
                          250       260
                   ....*....|....*....|....*....
gi 107026920   527 AESLRQSSQAIDDLTLVANQLRTSVSRFK 555
Cdd:smart00283 234 AAMSEEISAAAEELSGLAEELDELVERFK 262
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
351-556 5.13e-31

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: 5.13e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920  351 SQSGLTRMGETMRSVMDAAGSVNAklaiLNEKALNINQVVATITKVADQTNLLSLNAAIEAEKAGEYGRGFAVVATEIRR 430
Cdd:pfam00015  11 SEEALDEMSQIGQVVDDAVETMEE----LETSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920  431 LADQTAVATYDIEQTVKEIQSAVSAGVMGMDKFSEEVRRGMLDVQQVGGQLSQIIAEVQTLAPRFQMVNEGMQTQANGAE 510
Cdd:pfam00015  87 LAERSAQAAKEIEALIEEIVKQTNDSTASIQQTRTEVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDEQSAGID 166
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 107026920  511 QITQALSQLSEAAQQTAESLRQSSQAIDDLTLVANQLRTSVSRFKV 556
Cdd:pfam00015 167 QVNQAVARIDQVTQQNAALVEESAAAAETLEEQAEELTASVAQFRI 212
PRK09793 PRK09793
methyl-accepting protein IV; Provisional
183-557 1.10e-28

methyl-accepting protein IV; Provisional


Pssm-ID: 182079 [Multi-domain]  Cd Length: 533  Bit Score: 118.64  E-value: 1.10e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920 183 QENRKFADQSARVIRESVQDAEVVLVgalTIMLLSALGLGYMLY---RSVTVPMARLVEVHDVMRTGNLTHRLDLRRRDE 259
Cdd:PRK09793 168 LEINHVLEAASAQSQRNYQISALVFI---SMIIVAAIYISSALWwtrKMIVQPLAIIGSHFDSIAAGNLARPIAVYGRNE 244
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920 260 FGTLETGFNRMADELTELVARAQQSSMQVTTSVAEIAATSREQQATANETAATTTEIGATSREIFATSRDLLRTMNEVAG 339
Cdd:PRK09793 245 ITAIFASLKTMQQALRGTVSDVRKGSQEMHIGIAEIVAGNNDLSSRTEQQAASLAQTAASMEQLTATVGQNADNARQASE 324
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920 340 VAEQSATLAGVSQSGLTRMGETMRSVmdAAGSvnaklailnekaLNINQVVATITKVADQTNLLSLNAAIEAEKAGEYGR 419
Cdd:PRK09793 325 LAKNAATTAQAGGVQVSTMTHTMQEI--ATSS------------QKIGDIISVIDGIAFQTNILALNAAVEAARAGEQGR 390
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920 420 GFAVVATEIRRLADQTAVATYDIEQTVKEIQSAVSAGvmgmDKFSEEVRRGMLDVQQVGGQLSQIIAEVQTLAprfqmvn 499
Cdd:PRK09793 391 GFAVVAGEVRNLASRSAQAAKEIKGLIEESVNRVQQG----SKLVNNAAATMTDIVSSVTRVNDIMGEIASAS------- 459
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 107026920 500 egmQTQANGAEQITQALSQLSEAAQQTAESLRQSSQAIDDLTLVANQLRTSVSRFKVD 557
Cdd:PRK09793 460 ---EEQRRGIEQVAQAVSQMDQVTQQNASLVEEAAVATEQLANQADHLSSRVAVFTLE 514
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
206-558 4.74e-26

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 110.87  E-value: 4.74e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920 206 VLVGALTIMLLSALglgYMLYRSVTVPMARLVEVHDVMRTGNLTHRLDLRRRDEFGTLETGFNRMADELTELVARAQQSS 285
Cdd:PRK15048 196 VIALVVVLILLVAW---YGIRRMLLTPLAKIIAHIREIAGGNLANTLTIDGRSEMGDLAQSVSHMQRSLTDTVTHVREGS 272
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920 286 MQVTTSVAEIAATSREQQATANETAATTTEIGATSREIFATSR---DLLRTMNEVAGVAEQSATLAGVSQSGLTRmgeTM 362
Cdd:PRK15048 273 DAIYAGTREIAAGNTDLSSRTEQQASALEETAASMEQLTATVKqnaDNARQASQLAQSASDTAQHGGKVVDGVVK---TM 349
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920 363 RSVMDAAGsvnaklailnekalNINQVVATITKVADQTNLLSLNAAIEAEKAGEYGRGFAVVATEIRRLADQTAvatydi 442
Cdd:PRK15048 350 HEIADSSK--------------KIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSA------ 409
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920 443 eQTVKEIQSAVSAGVMGMDKfseevrrGMLDVQQVGGQLSQIIAEVQTLAPRFQMVNEGMQTQANGAEQITQALSQLSEA 522
Cdd:PRK15048 410 -QAAKEIKALIEDSVSRVDT-------GSVLVESAGETMNNIVNAVTRVTDIMGEIASASDEQSRGIDQVALAVSEMDRV 481
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 107026920 523 AQQTAESLRQSSQAIDDLTLVANQLRTSVSRFKVDA 558
Cdd:PRK15048 482 TQQNASLVQESAAAAAALEEQASRLTQAVSAFRLAA 517
PRK15041 PRK15041
methyl-accepting chemotaxis protein I; Provisional
182-556 2.35e-25

methyl-accepting chemotaxis protein I; Provisional


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 108.89  E-value: 2.35e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920 182 VQENRKFADQSARVIRESVQDAEVVLVGALTIMLLSALGLGYMLYRSVTVPMARLVEVHDVMRTGNLTHRLDLRRRDEFG 261
Cdd:PRK15041 171 MEQNDRLYDIAVSDNNASYSQAMWILVGVMIVVLAVIFAVWFGIKASLVAPMNRLIDSIRHIAGGDLVKPIEVDGSNEMG 250
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920 262 TLETGFNRMADELTELVARAQQSSMQVTTSVAEIAA-----TSREQQAtanetaattteiGATSREIFATSRDLLRTMNE 336
Cdd:PRK15041 251 QLAESLRHMQGELMRTVGDVRNGANAIYSGASEIATgnndlSSRTEQQ------------AASLEETAASMEQLTATVKQ 318
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920 337 VAGVAEQSATLA----GVSQSGLTRMGETMRSVMDAAGSvnaklailnekALNINQVVATITKVADQTNLLSLNAAIEAE 412
Cdd:PRK15041 319 NAENARQASHLAlsasETAQRGGKVVDNVVQTMRDISTS-----------SQKIADIISVIDGIAFQTNILALNAAVEAA 387
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920 413 KAGEYGRGFAVVATEIRRLADQTAvatydieQTVKEIQSAVSAGVmgmdkfsEEVRRGMLDVQQVGGQLSQIIAEVQTLA 492
Cdd:PRK15041 388 RAGEQGRGFAVVAGEVRNLAQRSA-------QAAREIKSLIEDSV-------GKVDVGSTLVESAGETMAEIVSAVTRVT 453
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 107026920 493 PRFQMVNEGMQTQANGAEQITQALSQLSEAAQQTAESLRQSSQAIDDLTLVANQLRTSVSRFKV 556
Cdd:PRK15041 454 DIMGEIASASDEQSRGIDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAVFRI 517
NarQ COG3850
Signal transduction histidine kinase, nitrate/nitrite-specific [Signal transduction mechanisms]
157-284 4.20e-08

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


Pssm-ID: 226368 [Multi-domain]  Cd Length: 574  Bit Score: 54.66  E-value: 4.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920 157 RDEAIAAYAKVLPGWaevVQDANIMVQENRKFADQsaRVIResvqdaeVVLVGaLTIMLLSALGLGYMLY---RSVTVPM 233
Cdd:COG3850  113 LQGDRRPYQADLADF---VAQIDQFVLALQRFAER--KTIL-------LVLVQ-LAGMLLILLLVVFTIYwlrRRVVRPL 179
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 107026920 234 ARLVEVHDVMRTGNLTHRLDLRRRDEFGTLETGFNRMADELTELVARAQQS 284
Cdd:COG3850  180 NQLTSAAQRIGRRQFDQRPTDTGRNELGLLGRAFNQMSGELKKLYADLEQR 230
NtrY COG5000
Signal transduction histidine kinase involved in nitrogen fixation and metabolism regulation ...
207-277 1.60e-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: 46.30  E-value: 1.60e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 107026920 207 LVGALTIMLLSALGLGYMLYRSVTVPMARLVEVHDVMRTGNLTHRLDLRRRDEF-GTLETGFNRMADELTEL 277
Cdd:COG5000  283 YLSTALLVLLAAIWTAIAFARRIVRPIRKLIEAADEVADGDLDVQVPVRRVDEDvGRLSKAFNKMTEQLSSQ 354
PRK10549 PRK10549
signal transduction histidine-protein kinase BaeS; Provisional
207-274 5.04e-04

signal transduction histidine-protein kinase BaeS; Provisional


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 41.16  E-value: 5.04e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 107026920 207 LVGALTiMLLSALgLGYMLYRSVTVPMARLVEVHDVMRTGNLTHRLDLRRRDEFGTLETGFNRMADEL 274
Cdd:PRK10549 168 LIVALS-TLLAAL-ATFLLARGLLAPVKRLVEGTHKLAAGDFTTRVTPTSRDELGRLAQDFNQLASTL 233
PRK10600 PRK10600
nitrate/nitrite sensor protein NarX; Provisional
205-283 1.91e-03

nitrate/nitrite sensor protein NarX; Provisional


Pssm-ID: 182581 [Multi-domain]  Cd Length: 569  Bit Score: 39.65  E-value: 1.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920 205 VVLVGALTI--MLLSALGLGYMLYRSVTVPMARLVEVHDVMRTGNLTHRLDLRRRDEFGTLETGFNRMADELTELVARAQ 282
Cdd:PRK10600 123 VVLVHRVFAvfMALLLVFTIIWLRRRLLQPWRQLLSMANAVSHRDFTQRANISGRDEMAMLGTALNNMSAELAESYAVLE 202

                 .
gi 107026920 283 Q 283
Cdd:PRK10600 203 Q 203
COG1511 COG1511
Predicted membrane protein [Function unknown]
326-541 3.21e-03

Predicted membrane protein [Function unknown]


Pssm-ID: 224428 [Multi-domain]  Cd Length: 780  Bit Score: 39.03  E-value: 3.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920 326 TSRDLLRTMNEVAGVAEQSATLAGVSQSGLTRMGETMRSVMDAAGSVNAKLAILNEkalNINQVVATITKVADQTNLLSL 405
Cdd:COG1511  165 TKVVAFPTIYDLGGGVKGAADGAEKLKDGTDEASNGNKKLSDLLNTLNNSSATFSD---GLNALTSGLTTLTDGLNQLDS 241
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920 406 NAAIEAEKAGEygrgfavvateirrladqtavatydieqtVKEIQSAVSAGVMGMDKFSEEVRRGMLDVQQVGGQLSQII 485
Cdd:COG1511  242 GLGTLAAGIGE-----------------------------LKQGAEQLNEGIGEFSSGLSELNSGVQDLAAGVPQLNQGI 292
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 107026920 486 AEVQTLAPRFQMVNEGMQTQANGAEQITQALSQLSEAAQQTAESLRQSSQAIDDLT 541
Cdd:COG1511  293 SALAAGLSLPDSLGDQFSSLQEALTQIAQGLKQKTSSSLEAAQGSLSSLQSMLALS 348
PRK15347 PRK15347
two component system sensor kinase SsrA; Provisional
210-276 4.07e-03

two component system sensor kinase SsrA; Provisional


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 38.47  E-value: 4.07e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 107026920 210 ALTIMLLSALGLGYMLYRSVTVPMARLVEVHDVMRTGNLTHRLDLRRRDEFGTLETGFNRMADELTE 276
Cdd:PRK15347 302 ALLILVLLTSVLFLLLRRYLAKPLWRFVDIINKTGPAALEPRLPENRLDELGSIAKAYNQLLDTLNE 368
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
212-289 6.05e-03

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 37.91  E-value: 6.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920 212 TIMLLSALGL----GYMLYRSVTVPMARLVEVHDVMRTGNLTHRLDLRRRDEFGTLETGFNRMADELTELVARAQQSSMQ 287
Cdd:PRK11107 181 FLMLLLGIGLallfAFRLMRDVTGPIRNMVNTVDRIRRGQLDSRVEGNMLGELDMLKNGINAMAMSLSAYHEEMQQNIDQ 260

                 ..
gi 107026920 288 VT 289
Cdd:PRK11107 261 AT 262
COG1511 COG1511
Predicted membrane protein [Function unknown]
267-549 6.60e-03

Predicted membrane protein [Function unknown]


Pssm-ID: 224428 [Multi-domain]  Cd Length: 780  Bit Score: 37.87  E-value: 6.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920 267 FNRMADELTELVARAQQSSMQVTTSVAEIAATSREQQATANETAATTTEIGATSREIFATSRDLLRTMNEVAGVAEQSAT 346
Cdd:COG1511  267 FSSGLSELNSGVQDLAAGVPQLNQGISALAAGLSLPDSLGDQFSSLQEALTQIAQGLKQKTSSSLEAAQGSLSSLQSMLA 346
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920 347 LAGVSQSGLTRMGETMRSVMDAAGSVNAKLAILNEKALNINQVVATITKVADQtnlLSLNAAIEAEKAGEYGRGFAVVAT 426
Cdd:COG1511  347 LSKSLDLTAEGATVDALGAPDGVQWLDESQKTLATLSELLSTGIDGVSEGLDA---LEQASAQLAKSLAKLKTAVAQIAA 423
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 107026920 427 EIRRLAD-----QTAVATYDIEQTVKEIQSAVSAG----VMGMDKFSEEVRR--------GMLDVQQVGGQLSQIIAEVQ 489
Cdd:COG1511  424 SIAQLLPgasevLKTLKSKGLDKLLNQLNGALAKGsnalVQGLSDANDSFRSitsaqlkaGLNTLADGSNDLSSLGPGLG 503
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 107026920 490 TLAPRFQMVNEGMQTQANGAEQITQALSQLSEAAQQTAESLRQSSQAIDDLT-------LVANQLRT 549
Cdd:COG1511  504 QLADGSKLLADGLSELNTGSAQLRDGLGELSDGLTELADSLQDAADQLSLANdsdkqasFIANPVEL 570
 
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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