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Conserved domains on  [gi|83575008|gb|ABC21559|]
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chemotaxis sensory transducer [Rhodospirillum rubrum ATCC 11170]

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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. ...
220-267 7.07e-04

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


:

Pssm-ID: 100122  Cd Length: 48  Bit Score: 38.00  E-value: 7.07e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 83575008 220 IRPLKRLTASMLRLAEGDLGVDLPVaRGRDEVGEIIGAVAVFKRNAQE 267
Cdd:cd06225   2 LRPLRRLAEAAQRIAAGDLDVRLPV-TGRDEIGELARAFNQMAERLRE 48
MCP_signal super family cl19050
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
345-532 6.65e-30

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: 116.18  E-value: 6.65e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008 345 SNAETVAGAAEEMTASIREILRQMDNTTALTAQAARTGQTAETTVASLQAAVERIGEVATLIGTIAGQTNLLALNATIES 424
Cdd:cd11386  12 ASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQTNLLALNAAIEA 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008 425 ARAGDAGKGFAVVAQEVKNLANQTGRSTEEITRQIAEVQSATRAAAEAVKAMigdirtiDQVSASVASAVREQDQATAEI 504
Cdd:cd11386  92 ARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEET-------SEEVEEGVELVEETGRAFEEI 164
                       170       180
                ....*....|....*....|....*...
gi 83575008 505 ARSVAETAAASSEVTERIDDVAREADAN 532
Cdd:cd11386 165 VASVEEVADGIQEISAATQEQSASTQEI 192
Tar_Tsr_LBD super family cl00144
ligand binding domain of Tar- and Tsr-related chemoreceptors; E.coli Tar (taxis to aspartate ...
6-191 2.01e-13

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: 68.41  E-value: 2.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008     6 DTKIGTRLLIGFGGMLVMTVILAVFGIHRVNEISHSLDVINEVNSVKQRYAINFRGSVHDRAIALRDVTLVTSAGDADAV 85
Cdd:pfam12729   1 NLKIRTKLILLFLLLALLLIIVGIVGLYSLKKINKNSETMYEDRLLPIKWLGEIRSNLREIRANLLELILTTDPAERDEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008    86 VATIDKLAgdyQRSAELMDRMfaERNDIGAEERTILGQIKQTESRTMPLVKTVIDRRRAGDLEGARALLMAEARPAFVEW 165
Cdd:pfam12729  81 LKDIEELR---AEIDKLLKKY--EKTILTEEEKKLFNEFKEQLKAYRKVRNKVLDLAKAGKNDEAYALYLTELEPARDAV 155
                         170       180
                  ....*....|....*....|....*.
gi 83575008   166 LERINRFIDLQENANQVIAERTRAVA 191
Cdd:pfam12729 156 IEALDELIDYNLKVAKEAYEDNKASY 181
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
307-557 2.53e-33

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: 127.40  E-value: 2.53e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008    307 EVARRTSRLNASAEDMATSAQTVSASSDSVSTSARKALSNAETVAGAAEEMTASIREILRQMDNTTALTAQAARTGQTAE 386
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008    387 TTVASLQAAVERIGEVATLIGTIAGQTNLLALNATIESARAGDAGKGFAVVAQEVKNLANQTGRSTEEITRQIAEVQSAT 466
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEET 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008    467 RAAAEA-------VKAMIGDIRTIDQVSASVASAVREQDQATAEIARSVAETAAASSEVTERIDDVAREADANGLRAQAV 539
Cdd:smart00283 161 NEAVAAmeessseVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240
                          250
                   ....*....|....*...
gi 83575008    540 KEIGRDVDHSIEALRQTL 557
Cdd:smart00283 241 SAAAEELSGLAEELDELV 258
 
Name Accession Description Interval E-value
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
220-267 7.07e-04

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


Pssm-ID: 100122  Cd Length: 48  Bit Score: 38.00  E-value: 7.07e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 83575008 220 IRPLKRLTASMLRLAEGDLGVDLPVaRGRDEVGEIIGAVAVFKRNAQE 267
Cdd:cd06225   2 LRPLRRLAEAAQRIAAGDLDVRLPV-TGRDEIGELARAFNQMAERLRE 48
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
345-532 6.65e-30

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: 116.18  E-value: 6.65e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008 345 SNAETVAGAAEEMTASIREILRQMDNTTALTAQAARTGQTAETTVASLQAAVERIGEVATLIGTIAGQTNLLALNATIES 424
Cdd:cd11386  12 ASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQTNLLALNAAIEA 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008 425 ARAGDAGKGFAVVAQEVKNLANQTGRSTEEITRQIAEVQSATRAAAEAVKAMigdirtiDQVSASVASAVREQDQATAEI 504
Cdd:cd11386  92 ARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEET-------SEEVEEGVELVEETGRAFEEI 164
                       170       180
                ....*....|....*....|....*...
gi 83575008 505 ARSVAETAAASSEVTERIDDVAREADAN 532
Cdd:cd11386 165 VASVEEVADGIQEISAATQEQSASTQEI 192
4HB_MCP_1 pfam12729
Four helix bundle sensory module for signal transduction; This family is a four helix bundle ...
6-191 2.01e-13

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: 68.41  E-value: 2.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008     6 DTKIGTRLLIGFGGMLVMTVILAVFGIHRVNEISHSLDVINEVNSVKQRYAINFRGSVHDRAIALRDVTLVTSAGDADAV 85
Cdd:pfam12729   1 NLKIRTKLILLFLLLALLLIIVGIVGLYSLKKINKNSETMYEDRLLPIKWLGEIRSNLREIRANLLELILTTDPAERDEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008    86 VATIDKLAgdyQRSAELMDRMfaERNDIGAEERTILGQIKQTESRTMPLVKTVIDRRRAGDLEGARALLMAEARPAFVEW 165
Cdd:pfam12729  81 LKDIEELR---AEIDKLLKKY--EKTILTEEEKKLFNEFKEQLKAYRKVRNKVLDLAKAGKNDEAYALYLTELEPARDAV 155
                         170       180
                  ....*....|....*....|....*.
gi 83575008   166 LERINRFIDLQENANQVIAERTRAVA 191
Cdd:pfam12729 156 IEALDELIDYNLKVAKEAYEDNKASY 181
HAMP pfam00672
HAMP domain;
198-258 2.71e-06

HAMP domain;


Pssm-ID: 250044  Cd Length: 70  Bit Score: 45.30  E-value: 2.71e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 83575008   198 MIGLCALVLVVGVALAWWTIGSI-RPLKRLTASMLRLAEGDLGVDLPVaRGRDEVGEIIGAV 258
Cdd:pfam00672   1 LLLVLLIALLLLLLLAWLLARRLlRPLRRLAEAARRIASGDLDDRVPV-SGPDEIGELARAF 61
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
220-270 2.65e-03

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


Pssm-ID: 197640  Cd Length: 53  Bit Score: 36.07  E-value: 2.65e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 83575008    220 IRPLKRLTASMLRLAEGDLGVDLPVaRGRDEVGEIIGAVAVFKRNAQEAAE 270
Cdd:smart00304   4 LRPLRRLAEAAQRIADGDLTVRLPV-DGRDEIGELARAFNEMADRLEETIA 53
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
307-557 2.53e-33

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: 127.40  E-value: 2.53e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008    307 EVARRTSRLNASAEDMATSAQTVSASSDSVSTSARKALSNAETVAGAAEEMTASIREILRQMDNTTALTAQAARTGQTAE 386
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008    387 TTVASLQAAVERIGEVATLIGTIAGQTNLLALNATIESARAGDAGKGFAVVAQEVKNLANQTGRSTEEITRQIAEVQSAT 466
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEET 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008    467 RAAAEA-------VKAMIGDIRTIDQVSASVASAVREQDQATAEIARSVAETAAASSEVTERIDDVAREADANGLRAQAV 539
Cdd:smart00283 161 NEAVAAmeessseVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240
                          250
                   ....*....|....*...
gi 83575008    540 KEIGRDVDHSIEALRQTL 557
Cdd:smart00283 241 SAAAEELSGLAEELDELV 258
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction ...
135-557 2.32e-32

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


Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 127.80  E-value: 2.32e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008 135 VKTVIDRRRAGDLEGARALLMAEARPAFVEWLERINRFIDLQENANQVIAERTRAVARGFAERMIGLCALVLVVGVALAW 214
Cdd:COG0840   3 LEAPLNLELIELAAGEADAGLLKLKKLIDELGKLLLSLNLILDDAASAEAAALKAVLKFLLISLLVAIIVVLVLAILLLR 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008 215 WTIgsiRPLKRLTASMLRLAEGDLGVDLPVaRGRDEVGEIIGAVAVFKRNAQEA-AELRAEQAAMAERSErqkrealgam 293
Cdd:COG0840  83 AIL---EPISDLLEVVERIAAGDLTKRIDE-SSNDEFGQLAKSFNEMILNLRQIiDAVQDNAEALSGASE---------- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008 294 aatverETAQVVDEVARRTSRLNASAEDMATSAQTVSASSDSVSTSARKALSNAETVAGAAEEMTASIREILRQMDNTTa 373
Cdd:COG0840 149 ------EIAASATELSARADQQAESLEEVASAIEELSETVKEVAFNAKEAAALASEASQVAEEGGEEVRQAVEQMQEIA- 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008 374 ltaqaartgQTAETTVASLQAAVERIGEVATLIGTIAGQTNLLALNATIESARAGDAGKGFAVVAQEVKNLANQTGRSTE 453
Cdd:COG0840 222 ---------EELAEVVKKLSESSQEIEEITSVINSIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSADSAK 292
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008 454 EITRQIAEVQSATRAAAEAVKAM-------IGDIRTIDQVSASVASAVREQDQATAEIARSVAETAAASSEVTERIDDVA 526
Cdd:COG0840 293 EIGLLIEEIQNEAADAVEHMEESasevsegVKLVEETGSSLGEIAAAIEEVSQLISEIAAATEEQTAVLEEINASIEELD 372
                       410       420       430
                ....*....|....*....|....*....|.
gi 83575008 527 READANGLRAQAVKEIGRDVDHSIEALRQTL 557
Cdd:COG0840 373 DVTQENAAAVEELAAASEELKELAEKLLELV 403
PRK09793 PRK09793
methyl-accepting protein IV; Provisional
162-544 1.03e-21

methyl-accepting protein IV; Provisional


Pssm-ID: 182079 [Multi-domain]  Cd Length: 533  Bit Score: 97.45  E-value: 1.03e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008  162 FVEWLERINRFIDLQENANQVIAERTRAVargFAErMIGLCALVlvVGVALAWWTIGSIRPLKRLTASMLRLAEGDLGVD 241
Cdd:PRK09793 163 FEAWQLEINHVLEAASAQSQRNYQISALV---FIS-MIIVAAIY--ISSALWWTRKMIVQPLAIIGSHFDSIAAGNLARP 236
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008  242 LPVaRGRDEVGEIIgavavfkrnaqeaAELRAEQAAMAErSERQKREALGAMAATVEretaqvvdEVARRTSRLNASAED 321
Cdd:PRK09793 237 IAV-YGRNEITAIF-------------ASLKTMQQALRG-TVSDVRKGSQEMHIGIA--------EIVAGNNDLSSRTEQ 293
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008  322 MATSAqtvsassdsvstsarkalsnAETvAGAAEEMTASIREILRQMDNTTALTAQAARTGQ-------TAETTVASLQA 394
Cdd:PRK09793 294 QAASL--------------------AQT-AASMEQLTATVGQNADNARQASELAKNAATTAQaggvqvsTMTHTMQEIAT 352
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008  395 AVERIGEVATLIGTIAGQTNLLALNATIESARAGDAGKGFAVVAQEVKNLANQTGRSTEEITRQIAE----VQSATRAAA 470
Cdd:PRK09793 353 SSQKIGDIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKGLIEEsvnrVQQGSKLVN 432
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008  471 EAVKAMIGDIRTIDQV--------SAS---------VASAVREQDQATAEIARSVAETAAASSEVTERIDDVAREADANG 533
Cdd:PRK09793 433 NAAATMTDIVSSVTRVndimgeiaSASeeqrrgieqVAQAVSQMDQVTQQNASLVEEAAVATEQLANQADHLSSRVAVFT 512
                        410
                 ....*....|...
gi 83575008  534 LRAQ--AVKEIGR 544
Cdd:PRK09793 513 LEEHevARHESAQ 525
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
375-527 4.13e-20

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: 88.66  E-value: 4.13e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008   375 TAQAARTGQTAETTVASLQAAVERIGEVATLIGTIAGQTNLLALNATIESARAGDAGKGFAVVAQEVKNLANQTGRSTEE 454
Cdd:pfam00015  18 MSQIGQVVDDAVETMEELETSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLAERSAQAAKE 97
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 83575008   455 ITRQIAEVQSATRAAAEAVKAMIGDIRTIDQVSASVASAVREQDQATAEIARSVAETAAASSEVTERIDDVAR 527
Cdd:pfam00015  98 IEALIEEIVKQTNDSTASIQQTRTEVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDEQSAGIDQVNQ 170
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
198-319 4.11e-09

TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the torCAD operon that encodes the pterin molybdenum cofactor-containing enzyme trimethylamine-N-oxide (TMAO) reductase (TorA), a cognate chaperone (TorD), and a penta-haem cytochrome (TorC). TorS works together with the inducer-binding protein TorT and the response regulator TorR. TorS contains histidine kinase ATPase (pfam02518), HAMP (pfam00672), phosphoacceptor (pfam00512), and phosphotransfer (pfam01627) domains and a response regulator receiver domain (pfam00072) [Signal transduction, Two-component systems].


Pssm-ID: 234070 [Multi-domain]  Cd Length: 968  Bit Score: 58.25  E-value: 4.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008   198 MIGLCALVLVVgvalaWWTI--GSIRPLKRLTASMLRLAEGDLGVDLPvARGRDEVGEIIGAVAVFKRNAQEAAELRAEQ 275
Cdd:TIGR02956 338 MLGLVILVFIM-----WRVVyrSVILRLNQHTQALLRLALGDLDISLD-ARGDDELAHMGRAIEAFRDTAAHNLKLQADE 411
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 83575008   276 aAMAERSERQKREALgamaatvERETAQVVDEVARRTSRLNASA 319
Cdd:TIGR02956 412 -RQVAQELQEHKESL-------EQLVAQRTQELAETNERLNAEV 447
PTZ00121 PTZ00121
MAEBL; Provisional
262-554 6.70e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 6.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008   262 KRNAQEAAElRAEQAAMAERSERQKREALGAMAATVERETAQVVDEV-------------ARRTSRLNASAEDMATSAQT 328
Cdd:PTZ00121 1443 AKKADEAKK-KAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAkkkaeeakkkadeAKKAAEAKKKADEAKKAEEA 1521
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008   329 VSASSDSVSTSARKA--LSNAETVAGAAEEMTAsiREILRQMDNTTALTAQAARTGQTAETTVASL--QAAVERIGEVAT 404
Cdd:PTZ00121 1522 KKADEAKKAEEAKKAdeAKKAEEKKKADELKKA--EELKKAEEKKKAEEAKKAEEDKNMALRKAEEakKAEEARIEEVMK 1599
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008   405 LIGTIAGQTNLLALNATIESARAGDAGKgfavvAQEVKNLANQTGRSTEEITRQIAEVQSA-----TRAAAEAVKAMiGD 479
Cdd:PTZ00121 1600 LYEEEKKMKAEEAKKAEEAKIKAEELKK-----AEEEKKKVEQLKKKEAEEKKKAEELKKAeeenkIKAAEEAKKAE-ED 1673
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 83575008   480 IRTIDQVSASVASAVR--EQDQATAEIARSVAETAAASSEVTERIDDVAREADANGLRAQAVKEIGRDVDHSIEALR 554
Cdd:PTZ00121 1674 KKKAEEAKKAEEDEKKaaEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAK 1750
NtrY COG5000
Signal transduction histidine kinase involved in nitrogen fixation and metabolism regulation ...
194-322 7.38e-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: 7.38e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008 194 FAERMIGLCALVLVVGVALAWWTIGSI-RPLKRLTASMLRLAEGDLGVDLPVARGRDEVGEIIGAVAVFKRNAQEAAELR 272
Cdd:COG5000 279 FALLYLSTALLVLLAAIWTAIAFARRIvRPIRKLIEAADEVADGDLDVQVPVRRVDEDVGRLSKAFNKMTEQLSSQQEAL 358
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 83575008 273 AEQAAMAERSERQKREALGAMAATVeretaqVVDEVARRTSRLNASAEDM 322
Cdd:COG5000 359 ERAKDALEQRRRFLEAVLSGLTAGV------IGFDNRGCITTVNPSAEQI 402
 
Name Accession Description Interval E-value
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
220-267 7.07e-04

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


Pssm-ID: 100122  Cd Length: 48  Bit Score: 38.00  E-value: 7.07e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 83575008 220 IRPLKRLTASMLRLAEGDLGVDLPVaRGRDEVGEIIGAVAVFKRNAQE 267
Cdd:cd06225   2 LRPLRRLAEAAQRIAAGDLDVRLPV-TGRDEIGELARAFNQMAERLRE 48
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
345-532 6.65e-30

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: 116.18  E-value: 6.65e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008 345 SNAETVAGAAEEMTASIREILRQMDNTTALTAQAARTGQTAETTVASLQAAVERIGEVATLIGTIAGQTNLLALNATIES 424
Cdd:cd11386  12 ASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQTNLLALNAAIEA 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008 425 ARAGDAGKGFAVVAQEVKNLANQTGRSTEEITRQIAEVQSATRAAAEAVKAMigdirtiDQVSASVASAVREQDQATAEI 504
Cdd:cd11386  92 ARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEET-------SEEVEEGVELVEETGRAFEEI 164
                       170       180
                ....*....|....*....|....*...
gi 83575008 505 ARSVAETAAASSEVTERIDDVAREADAN 532
Cdd:cd11386 165 VASVEEVADGIQEISAATQEQSASTQEI 192
4HB_MCP_1 pfam12729
Four helix bundle sensory module for signal transduction; This family is a four helix bundle ...
6-191 2.01e-13

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: 68.41  E-value: 2.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008     6 DTKIGTRLLIGFGGMLVMTVILAVFGIHRVNEISHSLDVINEVNSVKQRYAINFRGSVHDRAIALRDVTLVTSAGDADAV 85
Cdd:pfam12729   1 NLKIRTKLILLFLLLALLLIIVGIVGLYSLKKINKNSETMYEDRLLPIKWLGEIRSNLREIRANLLELILTTDPAERDEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008    86 VATIDKLAgdyQRSAELMDRMfaERNDIGAEERTILGQIKQTESRTMPLVKTVIDRRRAGDLEGARALLMAEARPAFVEW 165
Cdd:pfam12729  81 LKDIEELR---AEIDKLLKKY--EKTILTEEEKKLFNEFKEQLKAYRKVRNKVLDLAKAGKNDEAYALYLTELEPARDAV 155
                         170       180
                  ....*....|....*....|....*.
gi 83575008   166 LERINRFIDLQENANQVIAERTRAVA 191
Cdd:pfam12729 156 IEALDELIDYNLKVAKEAYEDNKASY 181
HAMP pfam00672
HAMP domain;
198-258 2.71e-06

HAMP domain;


Pssm-ID: 250044  Cd Length: 70  Bit Score: 45.30  E-value: 2.71e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 83575008   198 MIGLCALVLVVGVALAWWTIGSI-RPLKRLTASMLRLAEGDLGVDLPVaRGRDEVGEIIGAV 258
Cdd:pfam00672   1 LLLVLLIALLLLLLLAWLLARRLlRPLRRLAEAARRIASGDLDDRVPV-SGPDEIGELARAF 61
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
220-270 2.65e-03

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


Pssm-ID: 197640  Cd Length: 53  Bit Score: 36.07  E-value: 2.65e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 83575008    220 IRPLKRLTASMLRLAEGDLGVDLPVaRGRDEVGEIIGAVAVFKRNAQEAAE 270
Cdd:smart00304   4 LRPLRRLAEAAQRIADGDLTVRLPV-DGRDEIGELARAFNEMADRLEETIA 53
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
307-557 2.53e-33

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: 127.40  E-value: 2.53e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008    307 EVARRTSRLNASAEDMATSAQTVSASSDSVSTSARKALSNAETVAGAAEEMTASIREILRQMDNTTALTAQAARTGQTAE 386
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008    387 TTVASLQAAVERIGEVATLIGTIAGQTNLLALNATIESARAGDAGKGFAVVAQEVKNLANQTGRSTEEITRQIAEVQSAT 466
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEET 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008    467 RAAAEA-------VKAMIGDIRTIDQVSASVASAVREQDQATAEIARSVAETAAASSEVTERIDDVAREADANGLRAQAV 539
Cdd:smart00283 161 NEAVAAmeessseVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240
                          250
                   ....*....|....*...
gi 83575008    540 KEIGRDVDHSIEALRQTL 557
Cdd:smart00283 241 SAAAEELSGLAEELDELV 258
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction ...
135-557 2.32e-32

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


Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 127.80  E-value: 2.32e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008 135 VKTVIDRRRAGDLEGARALLMAEARPAFVEWLERINRFIDLQENANQVIAERTRAVARGFAERMIGLCALVLVVGVALAW 214
Cdd:COG0840   3 LEAPLNLELIELAAGEADAGLLKLKKLIDELGKLLLSLNLILDDAASAEAAALKAVLKFLLISLLVAIIVVLVLAILLLR 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008 215 WTIgsiRPLKRLTASMLRLAEGDLGVDLPVaRGRDEVGEIIGAVAVFKRNAQEA-AELRAEQAAMAERSErqkrealgam 293
Cdd:COG0840  83 AIL---EPISDLLEVVERIAAGDLTKRIDE-SSNDEFGQLAKSFNEMILNLRQIiDAVQDNAEALSGASE---------- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008 294 aatverETAQVVDEVARRTSRLNASAEDMATSAQTVSASSDSVSTSARKALSNAETVAGAAEEMTASIREILRQMDNTTa 373
Cdd:COG0840 149 ------EIAASATELSARADQQAESLEEVASAIEELSETVKEVAFNAKEAAALASEASQVAEEGGEEVRQAVEQMQEIA- 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008 374 ltaqaartgQTAETTVASLQAAVERIGEVATLIGTIAGQTNLLALNATIESARAGDAGKGFAVVAQEVKNLANQTGRSTE 453
Cdd:COG0840 222 ---------EELAEVVKKLSESSQEIEEITSVINSIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSADSAK 292
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008 454 EITRQIAEVQSATRAAAEAVKAM-------IGDIRTIDQVSASVASAVREQDQATAEIARSVAETAAASSEVTERIDDVA 526
Cdd:COG0840 293 EIGLLIEEIQNEAADAVEHMEESasevsegVKLVEETGSSLGEIAAAIEEVSQLISEIAAATEEQTAVLEEINASIEELD 372
                       410       420       430
                ....*....|....*....|....*....|.
gi 83575008 527 READANGLRAQAVKEIGRDVDHSIEALRQTL 557
Cdd:COG0840 373 DVTQENAAAVEELAAASEELKELAEKLLELV 403
PRK09793 PRK09793
methyl-accepting protein IV; Provisional
162-544 1.03e-21

methyl-accepting protein IV; Provisional


Pssm-ID: 182079 [Multi-domain]  Cd Length: 533  Bit Score: 97.45  E-value: 1.03e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008  162 FVEWLERINRFIDLQENANQVIAERTRAVargFAErMIGLCALVlvVGVALAWWTIGSIRPLKRLTASMLRLAEGDLGVD 241
Cdd:PRK09793 163 FEAWQLEINHVLEAASAQSQRNYQISALV---FIS-MIIVAAIY--ISSALWWTRKMIVQPLAIIGSHFDSIAAGNLARP 236
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008  242 LPVaRGRDEVGEIIgavavfkrnaqeaAELRAEQAAMAErSERQKREALGAMAATVEretaqvvdEVARRTSRLNASAED 321
Cdd:PRK09793 237 IAV-YGRNEITAIF-------------ASLKTMQQALRG-TVSDVRKGSQEMHIGIA--------EIVAGNNDLSSRTEQ 293
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008  322 MATSAqtvsassdsvstsarkalsnAETvAGAAEEMTASIREILRQMDNTTALTAQAARTGQ-------TAETTVASLQA 394
Cdd:PRK09793 294 QAASL--------------------AQT-AASMEQLTATVGQNADNARQASELAKNAATTAQaggvqvsTMTHTMQEIAT 352
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008  395 AVERIGEVATLIGTIAGQTNLLALNATIESARAGDAGKGFAVVAQEVKNLANQTGRSTEEITRQIAE----VQSATRAAA 470
Cdd:PRK09793 353 SSQKIGDIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKGLIEEsvnrVQQGSKLVN 432
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008  471 EAVKAMIGDIRTIDQV--------SAS---------VASAVREQDQATAEIARSVAETAAASSEVTERIDDVAREADANG 533
Cdd:PRK09793 433 NAAATMTDIVSSVTRVndimgeiaSASeeqrrgieqVAQAVSQMDQVTQQNASLVEEAAVATEQLANQADHLSSRVAVFT 512
                        410
                 ....*....|...
gi 83575008  534 LRAQ--AVKEIGR 544
Cdd:PRK09793 513 LEEHevARHESAQ 525
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
194-539 1.57e-21

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 97.00  E-value: 1.57e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008  194 FAERMIGLCALVLVVGVALAWWTIGSI--RPLKRLTASMLRLAEGDLGVDLPVArGRDEVGEIIGAVAVFKRNAQEAAel 271
Cdd:PRK15048 189 FAQWQLAVIALVVVLILLVAWYGIRRMllTPLAKIIAHIREIAGGNLANTLTID-GRSEMGDLAQSVSHMQRSLTDTV-- 265
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008  272 raeqaamaerseRQKREALGAMAATVEretaqvvdEVARRTSRLNASAEDMAtsaqtvsassdsvstsarkalSNAETVA 351
Cdd:PRK15048 266 ------------THVREGSDAIYAGTR--------EIAAGNTDLSSRTEQQA---------------------SALEETA 304
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008  352 GAAEEMTASIREilrQMDNTTALTAQAARTGQTAE----------TTVASLQAAVERIGEVATLIGTIAGQTNLLALNAT 421
Cdd:PRK15048 305 ASMEQLTATVKQ---NADNARQASQLAQSASDTAQhggkvvdgvvKTMHEIADSSKKIADIISVIDGIAFQTNILALNAA 381
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008  422 IESARAGDAGKGFAVVAQEVKNLANQTGRSTEEITRQIAE-----------VQSATRAAAEAVKA------MIGDI---- 480
Cdd:PRK15048 382 VEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKALIEDsvsrvdtgsvlVESAGETMNNIVNAvtrvtdIMGEIasas 461
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 83575008  481 ----RTIDQvsasVASAVREQDQATAEIARSVAETAAASSEVTERIDDVAREADANGLRAQAV 539
Cdd:PRK15048 462 deqsRGIDQ----VALAVSEMDRVTQQNASLVQESAAAAAALEEQASRLTQAVSAFRLAASPL 520
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
375-527 4.13e-20

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: 88.66  E-value: 4.13e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008   375 TAQAARTGQTAETTVASLQAAVERIGEVATLIGTIAGQTNLLALNATIESARAGDAGKGFAVVAQEVKNLANQTGRSTEE 454
Cdd:pfam00015  18 MSQIGQVVDDAVETMEELETSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLAERSAQAAKE 97
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 83575008   455 ITRQIAEVQSATRAAAEAVKAMIGDIRTIDQVSASVASAVREQDQATAEIARSVAETAAASSEVTERIDDVAR 527
Cdd:pfam00015  98 IEALIEEIVKQTNDSTASIQQTRTEVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDEQSAGIDQVNQ 170
PRK15041 PRK15041
methyl-accepting chemotaxis protein I; Provisional
198-521 2.47e-19

methyl-accepting chemotaxis protein I; Provisional


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 90.01  E-value: 2.47e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008  198 MIGLCALVLVVGVALaWWTIGS--IRPLKRLTASMLRLAEGDLGVDLPVaRGRDEVGEIigavavfkrnaqeAAELRAEQ 275
Cdd:PRK15041 196 LVGVMIVVLAVIFAV-WFGIKAslVAPMNRLIDSIRHIAGGDLVKPIEV-DGSNEMGQL-------------AESLRHMQ 260
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008  276 AAMAeRSERQKREALGAMAATVErETAQVVDEVARRTSRLNASAEDMATSaqtvsassdsvstsarkalsnaetvagaAE 355
Cdd:PRK15041 261 GELM-RTVGDVRNGANAIYSGAS-EIATGNNDLSSRTEQQAASLEETAAS----------------------------ME 310
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008  356 EMTASIREILRQMDNTTALTAQAARTGQ-------TAETTVASLQAAVERIGEVATLIGTIAGQTNLLALNATIESARAG 428
Cdd:PRK15041 311 QLTATVKQNAENARQASHLALSASETAQrggkvvdNVVQTMRDISTSSQKIADIISVIDGIAFQTNILALNAAVEAARAG 390
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008  429 DAGKGFAVVAQEVKNLANQTGRSTEEITRQIAE-----------VQSATRAAAEAVKA------MIGDI--------RTI 483
Cdd:PRK15041 391 EQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDsvgkvdvgstlVESAGETMAEIVSAvtrvtdIMGEIasasdeqsRGI 470
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 83575008  484 DQVSASVAsavrEQDQATAEIARSVAETAAASSEVTER 521
Cdd:PRK15041 471 DQVGLAVA----EMDRVTQQNAALVEESAAAAAALEEQ 504
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
198-319 4.11e-09

TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the torCAD operon that encodes the pterin molybdenum cofactor-containing enzyme trimethylamine-N-oxide (TMAO) reductase (TorA), a cognate chaperone (TorD), and a penta-haem cytochrome (TorC). TorS works together with the inducer-binding protein TorT and the response regulator TorR. TorS contains histidine kinase ATPase (pfam02518), HAMP (pfam00672), phosphoacceptor (pfam00512), and phosphotransfer (pfam01627) domains and a response regulator receiver domain (pfam00072) [Signal transduction, Two-component systems].


Pssm-ID: 234070 [Multi-domain]  Cd Length: 968  Bit Score: 58.25  E-value: 4.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008   198 MIGLCALVLVVgvalaWWTI--GSIRPLKRLTASMLRLAEGDLGVDLPvARGRDEVGEIIGAVAVFKRNAQEAAELRAEQ 275
Cdd:TIGR02956 338 MLGLVILVFIM-----WRVVyrSVILRLNQHTQALLRLALGDLDISLD-ARGDDELAHMGRAIEAFRDTAAHNLKLQADE 411
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 83575008   276 aAMAERSERQKREALgamaatvERETAQVVDEVARRTSRLNASA 319
Cdd:TIGR02956 412 -RQVAQELQEHKESL-------EQLVAQRTQELAETNERLNAEV 447
PTZ00121 PTZ00121
MAEBL; Provisional
262-554 6.70e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 6.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008   262 KRNAQEAAElRAEQAAMAERSERQKREALGAMAATVERETAQVVDEV-------------ARRTSRLNASAEDMATSAQT 328
Cdd:PTZ00121 1443 AKKADEAKK-KAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAkkkaeeakkkadeAKKAAEAKKKADEAKKAEEA 1521
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008   329 VSASSDSVSTSARKA--LSNAETVAGAAEEMTAsiREILRQMDNTTALTAQAARTGQTAETTVASL--QAAVERIGEVAT 404
Cdd:PTZ00121 1522 KKADEAKKAEEAKKAdeAKKAEEKKKADELKKA--EELKKAEEKKKAEEAKKAEEDKNMALRKAEEakKAEEARIEEVMK 1599
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008   405 LIGTIAGQTNLLALNATIESARAGDAGKgfavvAQEVKNLANQTGRSTEEITRQIAEVQSA-----TRAAAEAVKAMiGD 479
Cdd:PTZ00121 1600 LYEEEKKMKAEEAKKAEEAKIKAEELKK-----AEEEKKKVEQLKKKEAEEKKKAEELKKAeeenkIKAAEEAKKAE-ED 1673
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 83575008   480 IRTIDQVSASVASAVR--EQDQATAEIARSVAETAAASSEVTERIDDVAREADANGLRAQAVKEIGRDVDHSIEALR 554
Cdd:PTZ00121 1674 KKKAEEAKKAEEDEKKaaEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAK 1750
NtrY COG5000
Signal transduction histidine kinase involved in nitrogen fixation and metabolism regulation ...
194-322 7.38e-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: 7.38e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008 194 FAERMIGLCALVLVVGVALAWWTIGSI-RPLKRLTASMLRLAEGDLGVDLPVARGRDEVGEIIGAVAVFKRNAQEAAELR 272
Cdd:COG5000 279 FALLYLSTALLVLLAAIWTAIAFARRIvRPIRKLIEAADEVADGDLDVQVPVRRVDEDVGRLSKAFNKMTEQLSSQQEAL 358
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 83575008 273 AEQAAMAERSERQKREALGAMAATVeretaqVVDEVARRTSRLNASAEDM 322
Cdd:COG5000 359 ERAKDALEQRRRFLEAVLSGLTAGV------IGFDNRGCITTVNPSAEQI 402
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
265-515 7.23e-03

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 37.62  E-value: 7.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008  265 AQEAAELRAEQA-----AMAERSERQKREALGAMAATVERETAQVVDEVARRTSRLNA--SAEDMATSAQTVSASSDSVS 337
Cdd:PRK05035 440 AIEQEKKKAEEAkarfeARQARLEREKAAREARHKKAAEARAAKDKDAVAAALARVKAkkAAATQPIVIKAGARPDNSAV 519
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008  338 TSARKALSNAETVAGAAEEMTASIRE----ILRQMDNTTALTAQAARTGQTAETTVASLQAAVErigevATLIGTIAGQT 413
Cdd:PRK05035 520 IAAREARKAQARARQAEKQAAAAADPkkaaVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVA-----AAIARAKAKKA 594
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83575008  414 NLLALNATIESARAGDAGKGFAVVAQEVKNLANQTGRSTEEIT-RQIAEVQSATRAAAEAVKAmigDIRTIDQVSASVAS 492
Cdd:PRK05035 595 AQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPeEPVDPRKAAVAAAIARAKA---RKAAQQQANAEPEE 671
                        250       260
                 ....*....|....*....|....
gi 83575008  493 AVREQDQAT-AEIARSVAETAAAS 515
Cdd:PRK05035 672 AEDPKKAAVaAAIARAKAKKAAQQ 695
 
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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