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Conserved domains on  [gi|446840827|ref|WP_000918083|]
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MULTISPECIES: nitrate/nitrite two-component system sensor histidine kinase NarX [Enterobacteriaceae]

Protein Classification

nitrate/nitrite two-component system sensor histidine kinase NarX( domain architecture ID 11484817)

nitrate/nitrite two-component system sensor histidine kinase NarX acts as a sensor for nitrate/nitrite and transduces signal of nitrite/nitrate availability

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK10600 PRK10600
nitrate/nitrite two-component system sensor histidine kinase NarX;
30-598 0e+00

nitrate/nitrite two-component system sensor histidine kinase NarX;


:

Pssm-ID: 182581 [Multi-domain]  Cd Length: 569  Bit Score: 1100.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827  30 MAVSGWLVQGVQGSAHAINKAGSLRMQSYRLLAAVPLSEKDKPLIKEMEQTAFSAELTRAAERDGQLAQLQGLQDYWRNE 109
Cdd:PRK10600   1 MAVSGWLVQGVQGSAHAINKAGSLRMQSYRLLAAVPLSEKDKPLLKEMEQTAFSPELQRAAERDGQLAQLQALQDYWRNE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 110 LIPTLMRAQNRETVSADVSQFVAGLDQLVSGFDRTTEMRIETVVLVHRVMAVFMALLLVFTIIWLRARLLQPWRQLLAMA 189
Cdd:PRK10600  81 LKPALQQAQNPEDVAADVAQFVAGLDALVSAFDHTTEMRIETVVLVHRVFAVFMALLLVFTIIWLRRRLLQPWRQLLSMA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 190 SAVSHRDFTQRANISGRNEMAMLGTALNNMSAELAESYAVLEQRVQEKTAGLEHKNQILSFLWQANRRLHSRAPLCERLS 269
Cdd:PRK10600 161 NAVSHRDFTQRANISGRDEMAMLGTALNNMSAELAESYAVLEQRVQEKTAGLEQKNQILSFLWQANRRLHSRAPLCERLS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 270 PVLNGLQNLTLLRDIELRVYDTDDEENHQEFTCQPDMTCDDKGCQLCPRGVLPVGDRGTTLKWRLADSHTQYGILLATLP 349
Cdd:PRK10600 241 PVLNGLQNLTLLRDIELRVYETDDEENHQEFTCQSDMTCDDKGCQLCPRGVLPVGDRGTTLKWRLSDKHGQYGILLATLP 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 350 QGRHLSHDQQQLVDTLVEQLTATLALDRHQERQQQLIVMEERATIARELHDSIAQSLSCMKMQVSCLQMQGDALPESSRE 429
Cdd:PRK10600 321 QGRHLSHDQQQLVDTLVEQLTATLALERQQERQQQLIVMEERATIARELHDSIAQSLSCMKMQVSCLQMQGDALPESSRE 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 430 LLSQIRNELNASWAQLRELLTTFRLQLTEPGLRPALEASCEEYSAKFGFPVKLDYQLPPRLVPSHQAIHLLQIAREALSN 509
Cdd:PRK10600 401 LLSQIRNELNASWRQLRELLTTFRLQLTEPGLRPALEASCEEFSARFGFPVKLDYQLPPRLVPSHQAIHLLQIAREALSN 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 510 ALKHSQASEVVVTVAQNDNQVKLTVQDNGCGVPENAIRSNHYGMIIMRDRAQSLRGDCRVRRRESGGTEVVVTFIPEKTF 589
Cdd:PRK10600 481 ALKHAQASEVVVTVAQNQNQVKLSVQDNGCGVPENAERSNHYGLIIMRDRAQSLRGDCRVRRRESGGTEVVVTFIPEKTF 560

                 ....*....
gi 446840827 590 TDVQGDTHE 598
Cdd:PRK10600 561 TDVQGDTHE 569
 
Name Accession Description Interval E-value
PRK10600 PRK10600
nitrate/nitrite two-component system sensor histidine kinase NarX;
30-598 0e+00

nitrate/nitrite two-component system sensor histidine kinase NarX;


Pssm-ID: 182581 [Multi-domain]  Cd Length: 569  Bit Score: 1100.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827  30 MAVSGWLVQGVQGSAHAINKAGSLRMQSYRLLAAVPLSEKDKPLIKEMEQTAFSAELTRAAERDGQLAQLQGLQDYWRNE 109
Cdd:PRK10600   1 MAVSGWLVQGVQGSAHAINKAGSLRMQSYRLLAAVPLSEKDKPLLKEMEQTAFSPELQRAAERDGQLAQLQALQDYWRNE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 110 LIPTLMRAQNRETVSADVSQFVAGLDQLVSGFDRTTEMRIETVVLVHRVMAVFMALLLVFTIIWLRARLLQPWRQLLAMA 189
Cdd:PRK10600  81 LKPALQQAQNPEDVAADVAQFVAGLDALVSAFDHTTEMRIETVVLVHRVFAVFMALLLVFTIIWLRRRLLQPWRQLLSMA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 190 SAVSHRDFTQRANISGRNEMAMLGTALNNMSAELAESYAVLEQRVQEKTAGLEHKNQILSFLWQANRRLHSRAPLCERLS 269
Cdd:PRK10600 161 NAVSHRDFTQRANISGRDEMAMLGTALNNMSAELAESYAVLEQRVQEKTAGLEQKNQILSFLWQANRRLHSRAPLCERLS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 270 PVLNGLQNLTLLRDIELRVYDTDDEENHQEFTCQPDMTCDDKGCQLCPRGVLPVGDRGTTLKWRLADSHTQYGILLATLP 349
Cdd:PRK10600 241 PVLNGLQNLTLLRDIELRVYETDDEENHQEFTCQSDMTCDDKGCQLCPRGVLPVGDRGTTLKWRLSDKHGQYGILLATLP 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 350 QGRHLSHDQQQLVDTLVEQLTATLALDRHQERQQQLIVMEERATIARELHDSIAQSLSCMKMQVSCLQMQGDALPESSRE 429
Cdd:PRK10600 321 QGRHLSHDQQQLVDTLVEQLTATLALERQQERQQQLIVMEERATIARELHDSIAQSLSCMKMQVSCLQMQGDALPESSRE 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 430 LLSQIRNELNASWAQLRELLTTFRLQLTEPGLRPALEASCEEYSAKFGFPVKLDYQLPPRLVPSHQAIHLLQIAREALSN 509
Cdd:PRK10600 401 LLSQIRNELNASWRQLRELLTTFRLQLTEPGLRPALEASCEEFSARFGFPVKLDYQLPPRLVPSHQAIHLLQIAREALSN 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 510 ALKHSQASEVVVTVAQNDNQVKLTVQDNGCGVPENAIRSNHYGMIIMRDRAQSLRGDCRVRRRESGGTEVVVTFIPEKTF 589
Cdd:PRK10600 481 ALKHAQASEVVVTVAQNQNQVKLSVQDNGCGVPENAERSNHYGLIIMRDRAQSLRGDCRVRRRESGGTEVVVTFIPEKTF 560

                 ....*....
gi 446840827 590 TDVQGDTHE 598
Cdd:PRK10600 561 TDVQGDTHE 569
NarX_sensor cd22900
ligand binding sensor domain of NarX, and related chemoreceptors; The periplasmic ligand ...
38-152 7.37e-57

ligand binding sensor domain of NarX, and related chemoreceptors; The periplasmic ligand binding sensor domain of NarX is a histidine kinase receptor that responds to nitrate and nitrite to effect regulation of anaerobic respiration in various bacteria and similar proteins. It forms a homodimer and binds to ligands such as nitrate via the dimerization interface, a feature that appears to be conserved in this domain superfamily. NarX-NarL sensor-response regulator pair controls Escherichia coli gene expression in response to nitrate and nitrite. NarX has been shown to exhibit a clear kinetic preference for NarL over NarP, the sensor response partner of NarQ.


Pssm-ID: 438632 [Multi-domain]  Cd Length: 116  Bit Score: 187.00  E-value: 7.37e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827  38 QGVQGSAHAINKAGSLRMQSYRLLAAVPLSEKDKPLIKEMEQTAFSAELTRAAERDGQLAQLQGLQDYWRNELIPTLMRA 117
Cdd:cd22900    1 NSIQGNAHAINKAGSLRMQSYRLLAAVPLNPQDQALLDELEQTLSSPELQRAARREGLQSQLQALQQYWQQQLKPALLAA 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446840827 118 QNRETVSADVSQFVAGLDQLVSGFDRTTEMRIETV 152
Cdd:cd22900   81 KNPEDARAEVAAFVAQLDQLVSQIDQKTEQRLSLI 115
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
361-583 4.09e-55

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 187.13  E-value: 4.09e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 361 LVDTLVEQLTATLALDRHQERQQQLIVMEERATIARELHDSIAQSLSCMKMQVSCLQMQGDALPESSRELLSQIRNELNA 440
Cdd:COG4585   24 LVLLRARRAERAAELERELAARAEEAREEERRRIARELHDGVGQSLSAIKLQLEAARRLLDADPEAAREELEEIRELARE 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 441 SWAQLRELLTTFR-LQLTEPGLRPALEASCEEYSAKFGFPVKLDYQLPPRLVPSHQAIHLLQIAREALSNALKHSQASEV 519
Cdd:COG4585  104 ALAELRRLVRGLRpPALDDLGLAAALEELAERLLRAAGIRVELDVDGDPDRLPPEVELALYRIVQEALTNALKHAGATRV 183
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446840827 520 VVTVAQNDNQVKLTVQDNGCGVPENAIRSNHYGMIIMRDRAQSLRGDCRVRRRESGGTEVVVTF 583
Cdd:COG4585  184 TVTLEVDDGELTLTVRDDGVGFDPEAAPGGGLGLRGMRERAEALGGTLTIGSAPGGGTRVRATL 247
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
496-583 1.81e-16

Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 75.38  E-value: 1.81e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827   496 AIHLLQIAREALSNALKHSQA-SEVVVTVAQNDNQVKLTVQDNGCGVPEN-----------------AIRSNHYGMIIMR 557
Cdd:smart00387   3 PDRLRQVLSNLLDNAIKYTPEgGRITVTLERDGDHVEITVEDNGPGIPPEdlekifepffrtdkrsrKIGGTGLGLSIVK 82
                           90       100
                   ....*....|....*....|....*.
gi 446840827   558 DRAQSLRGDCRVRRRESGGTEVVVTF 583
Cdd:smart00387  83 KLVELHGGEISVESEPGGGTTFTITL 108
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
496-583 1.88e-15

Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.


Pssm-ID: 460579 [Multi-domain]  Cd Length: 109  Bit Score: 72.40  E-value: 1.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827  496 AIHLLQIAREALSNALKHS-QASEVVVTVaQNDNQVKLTVQDNGCGVPENAI---------------RSNHYGMIIMRDR 559
Cdd:pfam02518   3 ELRLRQVLSNLLDNALKHAaKAGEITVTL-SEGGELTLTVEDNGIGIPPEDLprifepfstadkrggGGTGLGLSIVRKL 81
                          90       100
                  ....*....|....*....|....
gi 446840827  560 AQSLRGDCRVRRRESGGTEVVVTF 583
Cdd:pfam02518  82 VELLGGTITVESEPGGGTTVTLTL 105
 
Name Accession Description Interval E-value
PRK10600 PRK10600
nitrate/nitrite two-component system sensor histidine kinase NarX;
30-598 0e+00

nitrate/nitrite two-component system sensor histidine kinase NarX;


Pssm-ID: 182581 [Multi-domain]  Cd Length: 569  Bit Score: 1100.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827  30 MAVSGWLVQGVQGSAHAINKAGSLRMQSYRLLAAVPLSEKDKPLIKEMEQTAFSAELTRAAERDGQLAQLQGLQDYWRNE 109
Cdd:PRK10600   1 MAVSGWLVQGVQGSAHAINKAGSLRMQSYRLLAAVPLSEKDKPLLKEMEQTAFSPELQRAAERDGQLAQLQALQDYWRNE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 110 LIPTLMRAQNRETVSADVSQFVAGLDQLVSGFDRTTEMRIETVVLVHRVMAVFMALLLVFTIIWLRARLLQPWRQLLAMA 189
Cdd:PRK10600  81 LKPALQQAQNPEDVAADVAQFVAGLDALVSAFDHTTEMRIETVVLVHRVFAVFMALLLVFTIIWLRRRLLQPWRQLLSMA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 190 SAVSHRDFTQRANISGRNEMAMLGTALNNMSAELAESYAVLEQRVQEKTAGLEHKNQILSFLWQANRRLHSRAPLCERLS 269
Cdd:PRK10600 161 NAVSHRDFTQRANISGRDEMAMLGTALNNMSAELAESYAVLEQRVQEKTAGLEQKNQILSFLWQANRRLHSRAPLCERLS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 270 PVLNGLQNLTLLRDIELRVYDTDDEENHQEFTCQPDMTCDDKGCQLCPRGVLPVGDRGTTLKWRLADSHTQYGILLATLP 349
Cdd:PRK10600 241 PVLNGLQNLTLLRDIELRVYETDDEENHQEFTCQSDMTCDDKGCQLCPRGVLPVGDRGTTLKWRLSDKHGQYGILLATLP 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 350 QGRHLSHDQQQLVDTLVEQLTATLALDRHQERQQQLIVMEERATIARELHDSIAQSLSCMKMQVSCLQMQGDALPESSRE 429
Cdd:PRK10600 321 QGRHLSHDQQQLVDTLVEQLTATLALERQQERQQQLIVMEERATIARELHDSIAQSLSCMKMQVSCLQMQGDALPESSRE 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 430 LLSQIRNELNASWAQLRELLTTFRLQLTEPGLRPALEASCEEYSAKFGFPVKLDYQLPPRLVPSHQAIHLLQIAREALSN 509
Cdd:PRK10600 401 LLSQIRNELNASWRQLRELLTTFRLQLTEPGLRPALEASCEEFSARFGFPVKLDYQLPPRLVPSHQAIHLLQIAREALSN 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 510 ALKHSQASEVVVTVAQNDNQVKLTVQDNGCGVPENAIRSNHYGMIIMRDRAQSLRGDCRVRRRESGGTEVVVTFIPEKTF 589
Cdd:PRK10600 481 ALKHAQASEVVVTVAQNQNQVKLSVQDNGCGVPENAERSNHYGLIIMRDRAQSLRGDCRVRRRESGGTEVVVTFIPEKTF 560

                 ....*....
gi 446840827 590 TDVQGDTHE 598
Cdd:PRK10600 561 TDVQGDTHE 569
PRK10935 PRK10935
nitrate/nitrite two-component system sensor histidine kinase NarQ;
17-588 3.11e-101

nitrate/nitrite two-component system sensor histidine kinase NarQ;


Pssm-ID: 236800 [Multi-domain]  Cd Length: 565  Bit Score: 318.34  E-value: 3.11e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827  17 LIVLLS---TAIGLAGMAVSgwlvqgvQGSAHAINKAGSLRMQSYRLL-----AAVPLSEKdkplIKEMEQTAFSAELTR 88
Cdd:PRK10935  17 LIILLSsltTGFALLTLASS-------LRDAEAINIAGSLRMQSYRLAydlqsGSPQLNAH----LREFEQSLHSPALKN 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827  89 -------AAERDgqlaQLQGLQDYWrnELIPTLMRAQNRETVSADVSQFVAGLDQLVSGFDRTTEMRIETVVLVHRVMAV 161
Cdd:PRK10935  86 lnrwyvpEDVKD----RYALLIARW--LEMKSYLEQGDSRWYQANIANYVDQIDLFVLALQHFAERKLILLAAISLLGLI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 162 FMALLLVFTIIWLRARLLQPWRQLLAMASAVSHRDF-TQRANISGRNEMAMLGTALNNMSAELAESYAVLEQRVQEKTAG 240
Cdd:PRK10935 160 LILTLVFFTVRFTRRQVVAPLNQLVTASQQIEKGQFdHIPLDTTLPNELGLLAKAFNQMSSELHKLYRSLEASVEEKTRK 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 241 LEHKNQILSFLWQANRRLHSRAPLCERLSPVLNGLQNLTLLRDIELRVYDtDDEENHQEFTcqpdmTCDDKGCQLCPrgv 320
Cdd:PRK10935 240 LTQANRSLEVLYQCSQALNASQIDVHCFRHILQIVRDHEGLDYLELEVGE-NEHWRISEGQ-----PNPELPWQILP--- 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 321 lpvgdrgttlkwrLADSHTQYGILL--ATLPqgrhlsHDQQQLVDTLVEQLTATLALDRHQERQQQLIVMEERATIAREL 398
Cdd:PRK10935 311 -------------LTMEDTVLGYLHwqASLP------CPDEPLMNNVAQMLGRGLYFNQAQKQQQQLLLMEERATIAREL 371
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 399 HDSIAQSLSCMKMQVSCLQMQGDALPESSRELLSQIRNELNASWAQLRELLTTFRLQLTEPGLRPALEASCEEYSAKFGF 478
Cdd:PRK10935 372 HDSLAQVLSYLKIQLTLLKRSLDEDNAKAQSIIAEFDQALSDAYRQLRELLTTFRLTIQEANLGSALEEMLDQLRNQTDA 451
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 479 PVKLDYQLPPRLVPSHQAIHLLQIAREALSNALKHSQASEVVVTVAQN-DNQVKLTVQDNGCGVPENAIRSNHYGMIIMR 557
Cdd:PRK10935 452 KITLDCRLPSQALDAQQQVHLLQIIREATLNAIKHANASEIAVSCVTNpDGEHTVSIRDDGIGIGELKEPEGHYGLNIMQ 531
                        570       580       590
                 ....*....|....*....|....*....|.
gi 446840827 558 DRAQSLRGDCRVRRRESGGTEVVVTFIPEKT 588
Cdd:PRK10935 532 ERAERLGGTLTISQPPGGGTTVSLTFPSQQE 562
NarX_sensor cd22900
ligand binding sensor domain of NarX, and related chemoreceptors; The periplasmic ligand ...
38-152 7.37e-57

ligand binding sensor domain of NarX, and related chemoreceptors; The periplasmic ligand binding sensor domain of NarX is a histidine kinase receptor that responds to nitrate and nitrite to effect regulation of anaerobic respiration in various bacteria and similar proteins. It forms a homodimer and binds to ligands such as nitrate via the dimerization interface, a feature that appears to be conserved in this domain superfamily. NarX-NarL sensor-response regulator pair controls Escherichia coli gene expression in response to nitrate and nitrite. NarX has been shown to exhibit a clear kinetic preference for NarL over NarP, the sensor response partner of NarQ.


Pssm-ID: 438632 [Multi-domain]  Cd Length: 116  Bit Score: 187.00  E-value: 7.37e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827  38 QGVQGSAHAINKAGSLRMQSYRLLAAVPLSEKDKPLIKEMEQTAFSAELTRAAERDGQLAQLQGLQDYWRNELIPTLMRA 117
Cdd:cd22900    1 NSIQGNAHAINKAGSLRMQSYRLLAAVPLNPQDQALLDELEQTLSSPELQRAARREGLQSQLQALQQYWQQQLKPALLAA 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446840827 118 QNRETVSADVSQFVAGLDQLVSGFDRTTEMRIETV 152
Cdd:cd22900   81 KNPEDARAEVAAFVAQLDQLVSQIDQKTEQRLSLI 115
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
361-583 4.09e-55

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 187.13  E-value: 4.09e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 361 LVDTLVEQLTATLALDRHQERQQQLIVMEERATIARELHDSIAQSLSCMKMQVSCLQMQGDALPESSRELLSQIRNELNA 440
Cdd:COG4585   24 LVLLRARRAERAAELERELAARAEEAREEERRRIARELHDGVGQSLSAIKLQLEAARRLLDADPEAAREELEEIRELARE 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 441 SWAQLRELLTTFR-LQLTEPGLRPALEASCEEYSAKFGFPVKLDYQLPPRLVPSHQAIHLLQIAREALSNALKHSQASEV 519
Cdd:COG4585  104 ALAELRRLVRGLRpPALDDLGLAAALEELAERLLRAAGIRVELDVDGDPDRLPPEVELALYRIVQEALTNALKHAGATRV 183
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446840827 520 VVTVAQNDNQVKLTVQDNGCGVPENAIRSNHYGMIIMRDRAQSLRGDCRVRRRESGGTEVVVTF 583
Cdd:COG4585  184 TVTLEVDDGELTLTVRDDGVGFDPEAAPGGGLGLRGMRERAEALGGTLTIGSAPGGGTRVRATL 247
HATPase_UhpB-NarQ-NarX-like cd16917
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
499-583 7.60e-28

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli UhpB, NarQ and NarX, and Bacillus subtilis YdfH, YhcY and YfiJ; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs) such as Escherichia coli UhpB, a HK of the UhpB-UhpA TCS, NarQ and NarX, HKs of the NarQ-NarP and NarX-NarL TCSs, respectively, and Bacillus YdfH, YhcY and YfiJ HKs, of the YdfH-YdfI, YhcY-YhcZ and YfiJ-YfiK TCSs, respectively. In addition, it includes Bacillus YxjM, ComP, LiaS and DesK, HKs of the YxjM-YxjML, ComP-ComA, LiaS-LiaR, DesR-DesK TCSs, respectively. Proteins having this HATPase domain have a histidine kinase dimerization and phosphoacceptor domain; some have accessory domains such as GAF, HAMP, PAS and MASE sensor domains.


Pssm-ID: 340394 [Multi-domain]  Cd Length: 87  Bit Score: 106.87  E-value: 7.60e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 499 LLQIAREALSNALKHSQASEVVVTVAQNDNQVKLTVQDNGCG-VPENAIRSNHYGMIIMRDRAQSLRGDCRVRRRESGGT 577
Cdd:cd16917    1 LYRIVQEALTNALKHAGASRVRVTLSYTADELTLTVVDDGVGfDGPAPPGGGGFGLLGMRERAELLGGTLTIGSRPGGGT 80

                 ....*.
gi 446840827 578 EVVVTF 583
Cdd:cd16917   81 RVTARL 86
NarX_NarQ_sensor cd19408
ligand binding sensor domain of NarX and NarQ, and related chemoreceptors; The periplasmic ...
41-151 5.03e-27

ligand binding sensor domain of NarX and NarQ, and related chemoreceptors; The periplasmic ligand binding sensor domain of NarX and NarQ is a histidine kinase receptor that responds to nitrate and nitrite to effect regulation of anaerobic respiration in various bacteria and similar proteins. It forms a homodimer and binds to ligands such as nitrate via the dimerization interface, a feature that appears to be conserved in this domain superfamily. NarX-NarL sensor-response regulator pair, along with NarQ-NarP, control Escherichia coli gene expression in response to nitrate and nitrite. NarX has been shown to exhibit a clear kinetic preference for NarL over NarP, whereas NarQ exhibits a relatively slight kinetic preference for NarL. There is asymmetry in the Nar cross-regulation network with NarQ shown to interact similarly with both response regulators, while NarX interacts preferentially with NarL.


Pssm-ID: 438626 [Multi-domain]  Cd Length: 126  Bit Score: 105.79  E-value: 5.03e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827  41 QGSAHAINKAGSLRMQSYRLLAAVPLSEKDKP-----LIKEMEQTAFSAELTRAAERDGQ---LAQLQGLQDYWRNELIP 112
Cdd:cd19408    4 EGDAAAINLAGSLRMQSYRLASLLLQAALEPAeqlaqLIDEFEQRLNSPALTRALPRDSDhplRQAYQAVLQHWQQELRP 83
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 446840827 113 TLMRA----QNRETVSADVSQFVAGLDQLVSGFDRTTEMRIET 151
Cdd:cd19408   84 ALEAAasgaADREAYLAEVDEFVAQIDQLVKLLQQDTEAKIRL 126
UhpB COG3851
Signal transduction histidine kinase UhpB, glucose-6-phosphate specific [Signal transduction ...
368-583 8.27e-26

Signal transduction histidine kinase UhpB, glucose-6-phosphate specific [Signal transduction mechanisms];


Pssm-ID: 443060 [Multi-domain]  Cd Length: 493  Bit Score: 111.25  E-value: 8.27e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 368 QLTATLALDRHQERQ--QQLIVMEE--RATIARELHDSIAQSLSCMKMQVSCLQMQGDAlpESSRELLSQIRNELNASWA 443
Cdd:COG3851  266 QLNQQLEQELRENRAlaRQLVSAEEseRREIARELHDEIGQNITAIRTQASILKRLAPQ--PEIEQSAQSIESLALRIYD 343
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 444 QLRELLTTFR-LQLTEPGLRPALEASCEEYS-AKFGFPVKLDYQLPPRLVPSHQAIHLLQIAREALSNALKHSQASEVVV 521
Cdd:COG3851  344 TTRRLLDRLRpAVLDELGLEEALRELPRELAfEEPGISCQLDLRGDPSLLDDTLQLTLYRLVQEALTNILKHAEASQIRI 423
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446840827 522 TVAQNDNQVKLTVQDNGCGVPENAiRSNHYGMIIMRDRAQSLRGDCRVRRRESgGTEVVVTF 583
Cdd:COG3851  424 SLSQDKRLLSLEIRDDGIGLPPEL-RAKGFGLRGMRERVRALGGDFRLSSAPK-GTRLSVLL 483
PRK11644 PRK11644
signal transduction histidine-protein kinase/phosphatase UhpB;
365-582 7.18e-19

signal transduction histidine-protein kinase/phosphatase UhpB;


Pssm-ID: 236945 [Multi-domain]  Cd Length: 495  Bit Score: 90.04  E-value: 7.18e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 365 LVEQLTATLAldRHQERQQQLIVMEE--RATIARELHDSIAQSLSCMKMQVSCLQMQGDALPESSR-----ELLSqirne 437
Cdd:PRK11644 276 LNQSLQKELA--RNRHLAERLLETEEsvRRDVARELHDEIGQTITAIRTQAGIIKRLAADNASVKQsaqliEQLS----- 348
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 438 LNAsWAQLRELLTTFR-LQLTEPGLRPALEASCEEYS-AKFGFPVKLDYQLPPRLVPSHQAIHLLQIAREALSNALKHSQ 515
Cdd:PRK11644 349 LGV-YDTVRRLLGRLRpRQLDDLTLEQAIRSLMREMElEDRGIVSHLDWRIDESALSETQRVTLFRVCQEGLNNIVKHAD 427
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446840827 516 ASEVVVTVAQNDNQVKLTVQDNGCGVPENAIrSNHYGMIIMRDRAQSLRGdcRVRRRESGGTEVVVT 582
Cdd:PRK11644 428 ASAVTLQGWQQDERLMLVIEDDGSGLPPGSG-QQGFGLRGMRERVTALGG--TLTISCTHGTRLSVS 491
chemoreceptor_sensor cd00181
4-helix bundle ligand binding sensor domain of chemoreceptors such as Tar or Tsr; The ligand ...
38-149 1.07e-18

4-helix bundle ligand binding sensor domain of chemoreceptors such as Tar or Tsr; The ligand binding sensor domain of chemoreceptors and related sensor histidine kinases forms homodimers and binds to ligands via the dimerization interface, a feature that appears to be conserved in this domain superfamily. This family includes ligand binding sensor domain of several chemoreceptors, such as Escherichia coli Tar, Tsr, NarQ, NarX, Pseudomonas aeruginosa KinB, Rhodopseudomonas palustris histidine kinase HK9 chemoreceptors, Comamonas testosteroni CNB-2 MCP2201 and Anaeromyxobacter dehalogenans histidine kinase Adeh_2942, among others.


Pssm-ID: 438624 [Multi-domain]  Cd Length: 119  Bit Score: 82.18  E-value: 1.07e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827  38 QGVQGSAHAINKAGSLRMQSYRLLAAVPLS---EKDKPLIKEMEQTAFSAELTRAAERD------GQLAQLQGLQDYWRn 108
Cdd:cd00181    1 QEIRQQASAISSLESLVLQARVTLRAEALTgveELGDALIRALKQTAAVLAQFRALTRDppeaeaEILDKVQDYQKALA- 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 446840827 109 ELIPTLMRaQNRETVSADVSQFVAGLDQLVSGFDRTTEMRI 149
Cdd:cd00181   80 ALIPALLE-RGAESALFDQSEAQGGLELLLSLLQQLTAAGI 119
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
496-583 1.81e-16

Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 75.38  E-value: 1.81e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827   496 AIHLLQIAREALSNALKHSQA-SEVVVTVAQNDNQVKLTVQDNGCGVPEN-----------------AIRSNHYGMIIMR 557
Cdd:smart00387   3 PDRLRQVLSNLLDNAIKYTPEgGRITVTLERDGDHVEITVEDNGPGIPPEdlekifepffrtdkrsrKIGGTGLGLSIVK 82
                           90       100
                   ....*....|....*....|....*.
gi 446840827   558 DRAQSLRGDCRVRRRESGGTEVVVTF 583
Cdd:smart00387  83 KLVELHGGEISVESEPGGGTTFTITL 108
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
496-583 1.88e-15

Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.


Pssm-ID: 460579 [Multi-domain]  Cd Length: 109  Bit Score: 72.40  E-value: 1.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827  496 AIHLLQIAREALSNALKHS-QASEVVVTVaQNDNQVKLTVQDNGCGVPENAI---------------RSNHYGMIIMRDR 559
Cdd:pfam02518   3 ELRLRQVLSNLLDNALKHAaKAGEITVTL-SEGGELTLTVEDNGIGIPPEDLprifepfstadkrggGGTGLGLSIVRKL 81
                          90       100
                  ....*....|....*....|....
gi 446840827  560 AQSLRGDCRVRRRESGGTEVVVTF 583
Cdd:pfam02518  82 VELLGGTITVESEPGGGTTVTLTL 105
HisKA_3 pfam07730
Histidine kinase; This is the dimerization and phosphoacceptor domain of a sub-family of ...
390-453 3.21e-15

Histidine kinase; This is the dimerization and phosphoacceptor domain of a sub-family of histidine kinases. It shares sequence similarity with pfam00512 and pfam07536.


Pssm-ID: 429624 [Multi-domain]  Cd Length: 68  Bit Score: 70.34  E-value: 3.21e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446840827  390 ERATIARELHDSIAQSLSCMKMQVSCLQMQGDALPESSRELLSQIRNELNASWAQLRELLTTFR 453
Cdd:pfam07730   1 ERNRIARELHDSVGQSLTAIKLQLELARRLLDRDPEEAREQLDAIRELAREALQELRRLLGDLR 64
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
151-583 8.43e-15

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


Pssm-ID: 444024 [Multi-domain]  Cd Length: 422  Bit Score: 76.54  E-value: 8.43e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 151 TVVLVHRVMAVFMALLLVFTIIWLRARLLQPWRQLLAMASAVSHRDFTQRANISGRNEMAMLGTALNNMSAELAESYAVL 230
Cdd:COG5000    6 LFLLLLLLIALLLLLLALWLALLLARRLTRPLRRLAEATRAVAAGDLSVRLPVTGDDEIGELARAFNRMTDQLKEQREEL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 231 EQRVQEKTAGLEHKNQ-ILSFlwQANRRLHSRAPLCERLSpvlnglqNLTLLRDIELRVYDTDDEENHQEFTCQPDMTCD 309
Cdd:COG5000   86 EERRRYLETILENLPAgVIVL--DADGRITLANPAAERLL-------GIPLEELIGKPLEELLPELDLAELLREALERGW 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 310 DKGCQLCPRGVLPVGDRGTTLKWRladshtqyGILLatlpqgrhlshdqqqlvdtLVEQLTATLaldrhqeRQQQLIVME 389
Cdd:COG5000  157 QEEIELTRDGRRTLLVRASPLRDD--------GYVI-------------------VFDDITELL-------RAERLAAWG 202
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 390 EratIAREL-HD------SIAQSLSCMKMQvscLQMQGDALPESSRELLSQIRNELNAswaqLRELLTTFR-------LQ 455
Cdd:COG5000  203 E---LARRIaHEiknpltPIQLSAERLRRK---LADKLEEDREDLERALDTIIRQVDR----LKRIVDEFLdfarlpePQ 272
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 456 LTEPGLRPALEASCEEYSAKFGFP-VKLDYQLPPRLVPS-------HQAIH-LLQIAREALsnalkhSQASEVVVTVAQN 526
Cdd:COG5000  273 LEPVDLNELLREVLALYEPALKEKdIRLELDLDPDLPEVladrdqlEQVLInLLKNAIEAI------EEGGEIEVSTRRE 346
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 527 DNQVKLTVQDNGCGVPEnAIRSN----HY---------GMIIMRDRAQSLRGDCRVRRRESGGTEVVVTF 583
Cdd:COG5000  347 DGRVRIEVSDNGPGIPE-EVLERifepFFttkpkgtglGLAIVKKIVEEHGGTIELESRPGGGTTFTIRL 415
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
374-583 2.43e-13

K+-sensing histidine kinase KdpD [Signal transduction mechanisms];


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 69.94  E-value: 2.43e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 374 ALDRHQERQQQLIVMEER--ATIARELHdsiaQSLSCMKMQVSCLQMQGDALPESSRELLSQIRNELNaswaQLRELLTT 451
Cdd:COG2205    1 ELEEALEELEELERLKSEflANVSHELR----TPLTSILGAAELLLDEEDLSPEERRELLEIIRESAE----RLLRLIED 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 452 F-----------RLQLTEPGLRPALEASCEEYSAKF-GFPVKLDYQLPPRLVPSHQAIHLL-QIAREALSNALKHSQA-S 517
Cdd:COG2205   73 LldlsrlesgklSLELEPVDLAELLEEAVEELRPLAeEKGIRLELDLPPELPLVYADPELLeQVLANLLDNAIKYSPPgG 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 518 EVVVTVAQNDNQVKLTVQDNGCGVPENAI-----------RSNHY-----GMIIMRDRAQSLRGDCRVRRRESGGTEVVV 581
Cdd:COG2205  153 TITISARREGDGVRISVSDNGPGIPEEELeriferfyrgdNSRGEggtglGLAIVKRIVEAHGGTIWVESEPGGGTTFTV 232

                 ..
gi 446840827 582 TF 583
Cdd:COG2205  233 TL 234
COG3920 COG3920
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...
84-583 4.34e-13

Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction mechanisms];


Pssm-ID: 443125 [Multi-domain]  Cd Length: 495  Bit Score: 71.86  E-value: 4.34e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827  84 AELTRAAERDGQLAQLQGLQDYWRNELIPTLMRAQNRETVSADVSQFVAGLDQLVSGFDRTTEMRIETVVLVHRVMAVFM 163
Cdd:COG3920    1 LLLALLLLLLLALAALLLLAALLLLAAALLLALLALLLLALLLLALLLASALLALLALSAAALAAALAVALAAAVGAAAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 164 ALLLVFTIIWLRARLLQPWRQLLAMASAVSHRDFTQRANISGRNEMAMLGTALNNMSAELAESYAVLEQRVQEKTAGLEH 243
Cdd:COG3920   81 LLALLVLLLLLLLAAAALALALLLAALAGLLLLAALLLLRLVALLAALALLALLLLLLLLLAILALAELAVALAELAAAL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 244 KNQILSFLWQANRRLHSRAPLCERLSPVLNGLQNLTLLRDIELRVYDTDDEENHQEFTcqpdmtcddkgcqLCPRGVLPV 323
Cdd:COG3920  161 LLLAEELAALRLAAAALLLLLAALLDLGLALAALAAAALLALLLALELLLALLLLLLL-------------LLALLLVLL 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 324 GDRGTTLKWRLADSHTQYGILLATLPQGRHLSHDQQQLVDTLVEQLTATLALDRHQERQQQLIVMEERATIARELHD--- 400
Cdd:COG3920  228 AALLRLRAAVLEELERRRRARGLGRLLLLLLLLLLLLRALLLLAAGIRLVITERKRAEEELEASLEEKELLLRELHHrvk 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 401 ---SIAQSLscmkmqvscLQMQGDALP-ESSRELLSQIRNELNASwAQLRELLTTfRLQLTEPGLRPALEASCEEYSAKF 476
Cdd:COG3920  308 nnlQVVSSL---------LRLQARRADdPEAREALEESQNRIQAL-ALVHELLYQ-SEDWEGVDLRDYLRELLEPLRDSY 376
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 477 G-FPVKLDYQLPPRLVPSHQAIHLLQIAREALSNALKHSQAS----EVVVTVAQNDNQVKLTVQDNGCGVPENAI--RSN 549
Cdd:COG3920  377 GgRGIRIELDGPDVELPADAAVPLGLILNELVTNALKHAFLSgeggRIRVSWRREDGRLRLTVSDNGVGLPEDVDppARK 456
                        490       500       510
                 ....*....|....*....|....*....|....
gi 446840827 550 HYGMIIMRDRAQSLRGdcRVRRRESGGTEVVVTF 583
Cdd:COG3920  457 GLGLRLIRALVRQLGG--TLELDRPEGTRVRITF 488
NarQ COG3850
Signal transduction histidine kinase NarQ, nitrate/nitrite-specific [Signal transduction ...
41-400 1.08e-11

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


Pssm-ID: 443059 [Multi-domain]  Cd Length: 448  Bit Score: 67.22  E-value: 1.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827  41 QGSAHAINKAGSLRMQSYRLLAAVPLSEKDKPLIKEMEQTAFSAELTRAAERDGQLAQLQGLQDYWRNELIPTLMRAQNR 120
Cdd:COG3850    5 LLLALALLRLLLALLALLLLALLLLSLLALLLLLERTLLRLLSLLASAGLLAALLAALLLLLSLGLLALLLALLLLLLLL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 121 ETVSADVSQFVAGLDQLVSGFDRTTEMRIETVVLVHRVMAVFMALLLVFTIIWLRARLLQPWRQLLAMASAVSHRDFTQR 200
Cdd:COG3850   85 LLAALLSLLLLLLLLLLLLLLLLLLLLAAAINRKLALLRLLLALLLALLLAYLLRRRIVRPLRRLTQAAERIARGDFDAR 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 201 ANISGRNEMAMLGTALNNMSAELAESYAVLEQRVQEKTAGLEHKNQILSFLWQANRRLHSRAPLCERLSPVLNGLQNLTL 280
Cdd:COG3850  165 VPVSGRDELGTLARAFNRMADELQELYAELEEEEELEAELELLALLDELLLLAALLLLLALLLALLLAALLAALLLLLLL 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 281 LRDIELRVYDTDDEENHQEFTCQPDMTCDDKGCQLCPRGVLPVGDRGTTLKWRLADSHTQYGILLATLPQGRHLSHDQQQ 360
Cdd:COG3850  245 QDALAESELLALNILAGLLELLLALLLLLLASALLLLELELLALLLELVELLALAAAEEALLLLVELAALLLLLLLQAIA 324
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 446840827 361 LVDTLVEQLTATLALDRHQERQQQLIVMEERATIARELHD 400
Cdd:COG3850  325 NASLLLIALASVVAALLELASILALQAALEAAAAGAALAA 364
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
329-583 2.61e-09

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 59.15  E-value: 2.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 329 TLKWRLADSHTQYGILLATLPQGRHLSHDQQQLVDTLVEQLTATLALDRHQERQQQLIvmeerATIArelHDsIAQSLSC 408
Cdd:COG0642   57 ALLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLLLLEEANEAKSRFL-----ANVS---HE-LRTPLTA 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 409 MKMQvscLQMQGDALPESSRELLSQIRNELNASWAQLRELLTTFRLQLTEPGLRPA-------LEASCEEYSAKFGFP-V 480
Cdd:COG0642  128 IRGY---LELLLEELDEEQREYLETILRSADRLLRLINDLLDLSRLEAGKLELEPEpvdlaelLEEVVELFRPLAEEKgI 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 481 KLDYQLPPRLVPSH-QAIHLLQIAREALSNALKHSQA-SEVVVTVAQNDNQVKLTVQDNGCGVPE--------------N 544
Cdd:COG0642  205 ELELDLPDDLPTVRgDPDRLRQVLLNLLSNAIKYTPEgGTVTVSVRREGDRVRISVEDTGPGIPPedlerifepffrtdP 284
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 446840827 545 AIRSNHYGM--IIMRDRAQSLRGDCRVRRRESGGTEVVVTF 583
Cdd:COG0642  285 SRRGGGTGLglAIVKRIVELHGGTIEVESEPGKGTTFTVTL 325
NarQ_sensor cd22899
ligand binding sensor domain of NarQ, and related chemoreceptors; The periplasmic ligand ...
44-138 7.40e-09

ligand binding sensor domain of NarQ, and related chemoreceptors; The periplasmic ligand binding sensor domain of NarQ is a histidine kinase receptor that responds to nitrate and nitrite to effect regulation of anaerobic respiration in various bacteria and similar proteins. It forms a homodimer and binds to ligands such as nitrate via the dimerization interface, a feature that appears to be conserved in this domain superfamily. NarQ-NarP sensor-response regulator pair controls Escherichia coli gene expression in response to nitrate and nitrite. NarQ has been shown to interact equally with NarP and NarL response regulators; NarL is the sensor response partner of NarX.


Pssm-ID: 438631 [Multi-domain]  Cd Length: 116  Bit Score: 53.68  E-value: 7.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827  44 AHAINKAGSLRMQSYRLLAAVplsEKDKPL----IKEMEQTAFSAELTRAaerDGQL------AQLQGLQDYWRnELIPT 113
Cdd:cd22899    7 AEAINVAGSLRMQSYRLAYDL---ESESPLleqhIAQYEQSLHSPALQSL---DRWYvpdevkQRYQQLLARWQ-EMKQY 79
                         90       100
                 ....*....|....*....|....*
gi 446840827 114 LmRAQNRETVSADVSQFVAGLDQLV 138
Cdd:cd22899   80 L-LQGDPASYLQQVASYVDQIDQFV 103
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
406-577 7.43e-09

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 58.03  E-value: 7.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 406 LSCMKMQVSCLQMQGDALPESSRELLSQIRNELNASWAQLRELLTTFRLQLTEPGLRPA-------LEASCEEYSAKFG- 477
Cdd:COG5002  180 LTSIRGYLELLLDGAADDPEERREYLEIILEEAERLSRLVNDLLDLSRLESGELKLEKEpvdlaelLEEVVEELRPLAEe 259
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 478 FPVKLDYQLPPRLVPSH-QAIHLLQIAREALSNALKHSQA-SEVVVTVAQNDNQVKLTVQDNGCGVPENAIrsNH----- 550
Cdd:COG5002  260 KGIELELDLPEDPLLVLgDPDRLEQVLTNLLDNAIKYTPEgGTITVSLREEDDQVRISVRDTGIGIPEEDL--PRiferf 337
                        170       180
                 ....*....|....*....|....*..
gi 446840827 551 YgmiimrdraqslRGDcRVRRRESGGT 577
Cdd:COG5002  338 Y------------RVD-KSRSRETGGT 351
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
177-228 3.32e-08

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


Pssm-ID: 197640 [Multi-domain]  Cd Length: 53  Bit Score: 49.94  E-value: 3.32e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 446840827   177 RLLQPWRQLLAMASAVSHRDFTQRANISGRNEMAMLGTALNNMSAELAESYA 228
Cdd:smart00304   2 RLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRLEETIA 53
HAMP pfam00672
HAMP domain;
173-225 6.62e-08

HAMP domain;


Pssm-ID: 459898 [Multi-domain]  Cd Length: 53  Bit Score: 49.16  E-value: 6.62e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 446840827  173 WLRARLLQPWRQLLAMASAVSHRDFTQRANISGRNEMAMLGTALNNMSAELAE 225
Cdd:pfam00672   1 LLARRILRPLRRLAEAARRIASGDLDVRLPVSGRDEIGELARAFNQMAERLRE 53
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; ...
179-223 1.45e-07

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 Af1503 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: 381743 [Multi-domain]  Cd Length: 45  Bit Score: 47.82  E-value: 1.45e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 446840827 179 LQPWRQLLAMASAVSHRDFTQRANISGRNEMAMLGTALNNMSAEL 223
Cdd:cd06225    1 TRPLRRLTEAARRIAEGDLDVRVPVRSKDEIGELARAFNQMAERL 45
HATPase_EL346-LOV-HK-like cd16951
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
491-583 2.16e-07

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Erythrobacter litoralis blue light-activated histidine kinase 2; This domain family includes the histidine kinase-like ATPase (HATPase) domain of blue light-activated histidine kinase 2 of Erythrobacter litoralis (EL346). Signaling commonly occurs within HK dimers, however EL346 functions as a monomer. Also included in this family are the HATPase domains of ethanolamine utilization sensory transduction histidine kinase (EutW), whereby regulation of ethanolamine, a carbon and nitrogen source for gut bacteria, results in autophosphorylation and subsequent phosphoryl transfer to a response regulator (EutV) containing an RNA-binding domain. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some have an accessory PAS sensor domain, while some have an N-terminal histidine kinase domain.


Pssm-ID: 340427 [Multi-domain]  Cd Length: 131  Bit Score: 50.11  E-value: 2.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 491 VPSHQAIHLLQIAREALSNALKH--SQASEVVVTV-AQNDN-QVKLTVQDNGCGVPE--NAIRSNHYGMIIMRDRAQSLR 564
Cdd:cd16951   32 VSSEVATAIGLVVNELLQNALKHafSDREGGTITIrSVVDGdYLRITVIDDGVGLPQdeDWPNKGSLGLQIVRSLVEGEL 111
                         90
                 ....*....|....*....
gi 446840827 565 GDCRVRRRESGGTEVVVTF 583
Cdd:cd16951  112 KAFLEVQSAENGTRVNIDI 130
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
9-225 3.78e-07

Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 53.10  E-value: 3.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827   9 LTLVNQVALIVLLSTAIGLAGMAVSGWLVQGVQGSAHAINKAGSLRMQSYRLLAAVPLSEKDKPLIKEMEQTAFSAELTR 88
Cdd:COG0840   34 ALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVVLLALLLALLLLLLALLALALAALALLAALAALL 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827  89 AAERDGQLAQLQGLQDYWRNELIPTLMRAQNRETVSADVSQFVAGLDQLVSGFDRTTEMRIETVVLVHRVMAVFMALLLV 168
Cdd:COG0840  114 ALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAAALAALLEAAALALAAAALALALLAAALLALVA 193
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 169 FTII---WLRARLLQPWRQLLAMASAVSHRDFTQRANISGRNEMAMLGTALNNMSAELAE 225
Cdd:COG0840  194 LAIIlalLLSRSITRPLRELLEVLERIAEGDLTVRIDVDSKDEIGQLADAFNRMIENLRE 253
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
491-583 1.23e-06

Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 47.99  E-value: 1.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 491 VPSHQAIHLLQIAREALSNALKHSQAS----EVVVTVAQNDNQVKLTVQDNGCGVPENAI-------RSNHYGMIIMRdr 559
Cdd:COG2172   27 LDEDDADDLVLAVSEAVTNAVRHAYGGdpdgPVEVELELDPDGLEIEVRDEGPGFDPEDLpdpystlAEGGRGLFLIR-- 104
                         90       100
                 ....*....|....*....|....
gi 446840827 560 aqSLRGDCRVRRREsGGTEVVVTF 583
Cdd:COG2172  105 --RLMDEVEYESDP-GGTTVRLVK 125
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
480-583 6.68e-06

Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction mechanisms];


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 48.69  E-value: 6.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 480 VKLDYQLPPRLVPSHqaiHLLQIAREALSNALKHSQASE-----VVVTVAQNDNQVKLTVQDNGCGVPENAIRS------ 548
Cdd:COG3290  266 IDIDSDLPDLPLSDT---DLVTILGNLLDNAIEAVEKLPeeerrVELSIRDDGDELVIEVEDSGPGIPEELLEKifergf 342
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 446840827 549 ------NH-YGMIIMRDRAQSLRGDCRVRRRESGGTEVVVTF 583
Cdd:COG3290  343 stklgeGRgLGLALVKQIVEKYGGTIEVESEEGEGTVFTVRL 384
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
374-547 7.03e-06

Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal transduction mechanisms];


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 48.64  E-value: 7.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 374 ALDRHQERQQQLIVMEERATIArEL-----HDsIAQSLSCMKMQVSCLQ--MQGDALPESSRELLSQIRNELNASWAQLR 446
Cdd:COG4191  122 AEEELRELQEQLVQSEKLAALG-ELaagiaHE-INNPLAAILGNAELLRrrLEDEPDPEELREALERILEGAERAAEIVR 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 447 ELLTTFRLQLTEPG---LRPALEASCEEYSAKFG-FPVKLDYQLPPRLVPSH-------QAI-HLLQIAREALsnalKHS 514
Cdd:COG4191  200 SLRAFSRRDEEEREpvdLNELIDEALELLRPRLKaRGIEVELDLPPDLPPVLgdpgqleQVLlNLLINAIDAM----EEG 275
                        170       180       190
                 ....*....|....*....|....*....|...
gi 446840827 515 QASEVVVTVAQNDNQVKLTVQDNGCGVPENAIR 547
Cdd:COG4191  276 EGGRITISTRREGDYVVISVRDNGPGIPPEVLE 308
HATPase_RsbW-like cd16936
Histidine kinase-like ATPase domain of RsbW, an anti sigma-B factor and serine-protein kinase ...
505-583 1.44e-05

Histidine kinase-like ATPase domain of RsbW, an anti sigma-B factor and serine-protein kinase involved in regulating sigma-B during stress in Bacilli, and related domains; This family includes histidine kinase-like ATPase (HATPase) domain of RsbW, an anti sigma-B factor as well as a serine-protein kinase involved in regulating sigma-B during stress in Bacilli. The alternative sigma factor sigma-B is an important regulator of the general stress response of Bacillus cereus and B. subtilis. RsbW is an anti-sigma factor while RsbV is an anti-sigma factor antagonist (anti-anti-sigma factor). RsbW can also act as a kinase on RsbV. In a partner-switching mechanism, RsbW, RsbV, and sigma-B participate as follows: in non-stressed cells, sigma-B is present in an inactive form complexed with RsbW; in this form, sigma-B is unable to bind to RNA polymerase. Under stress, RsbV binds to RsbW, forming an RsbV-RsbW complex, and sigma-B is released to bind to RNA polymerase. RsbW may then act as a kinase on RsbV, phosphorylating a serine residue; RsbW is then released to bind to sigma-B, hence blocking its ability to bind RNA polymerase. A phosphatase then dephosphorylates RsbV so that it can again form a complex with RsbW, leading to the release of sigma-B.


Pssm-ID: 340413 [Multi-domain]  Cd Length: 91  Bit Score: 43.80  E-value: 1.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 505 EALSNALKHSQAS----EVVVTVAQNDNQVKLTVQDNGCGV-------PENAIRSNHYGMIIMRdraqSLRGDCRVRRRE 573
Cdd:cd16936    7 EAVTNAVRHAYRHdgpgPVRLELDLDPDRLRVEVTDSGPGFdplrpadPDAGLREGGRGLALIR----ALMDEVGYRRTP 82
                         90
                 ....*....|
gi 446840827 574 sGGTEVVVTF 583
Cdd:cd16936   83 -GGKTVWLEL 91
PilJ pfam13675
Type IV pili methyl-accepting chemotaxis transducer N-term; This domain is found on many type ...
35-110 2.10e-05

Type IV pili methyl-accepting chemotaxis transducer N-term; This domain is found on many type IV pili methyl-accepting chemotaxis transducer proteins where there is also a HAMP signature towards the C-terminus. It is a monomodular four-helix bundle and recognizes nitrate and nitrite (Matilla et al. FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 433397 [Multi-domain]  Cd Length: 112  Bit Score: 44.00  E-value: 2.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827   35 WLVQGVQGSAHAINKAGSLRMQSYRL----LAAVPLSEKDKPLIKEMEQTAFSAELTRAAERDGQL------------AQ 98
Cdd:pfam13675   1 WTLWQSEGDAAAINAAGSLRMQSQRLaksvLLALAGNYDLAEAFADLEESIDQFDRTLAALALGDLarglfvpagairAQ 80
                          90
                  ....*....|..
gi 446840827   99 LQGLQDYWRNEL 110
Cdd:pfam13675  81 LEAVQPLWERLR 92
HATPase_PhoQ-like cd16954
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
507-583 2.54e-05

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli PhoQ and Providencia stuartii AarG; This family includes histidine kinase-like ATPase (HATPase) domain of two-component sensor histidine kinases similar to Escherichia coli PhoQ and Providencia stuartii AarG. PhoQ is the histidine kinase (HK) of the PhoP-PhoQ two-component regulatory system (TCS), which responds to the levels of Mg2+ and Ca2+, controls virulence, mediates the adaptation to Mg2+-limiting environments, and regulates numerous cellular activities. Providencia stuartii AarG is a putative sensor kinase which controls the expression of the 2'-N-acetyltransferase and an intrinsic multiple antibiotic resistance (Mar) response in Providencia stuartii. The AarG product is similar to PhoQ in that it is able to restore wild-type levels of resistance to a Salmonella typhimurium phoQ mutant. However, the expression of the 2'-N-acetyltransferase gene and of aarP (a gene encoding a transcriptional activator of 2'-N-acetyltransferase) are not significantly affected by the levels of Mg2+ or Ca2+. Most proteins in this group contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some have an accessory HAMP sensor domain, and some have an intracellular membrane -interaction PhoQ sensor domain.


Pssm-ID: 340430 [Multi-domain]  Cd Length: 135  Bit Score: 44.16  E-value: 2.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 507 LSNALKHSQaSEVVVTVAQNDNQVKLTVQDNGCGVPENAI-------------RSNH-YGMIIMRDRAQSLRGDCRVRRR 572
Cdd:cd16954   46 LDNACKWCL-EFVEVTARQTDGGLHLIVDDDGPGVPESQRskifqrgqrldeqRPGQgLGLAIAKEIVEQYGGELSLSDS 124
                         90
                 ....*....|.
gi 446840827 573 ESGGTEVVVTF 583
Cdd:cd16954  125 PLGGARFEVVF 135
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
482-583 3.93e-05

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 46.55  E-value: 3.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 482 LDYQLPPRLvpshqaihlLQIAREalsNALKHS-----QASEVVVTVAQNDNQVKLTVQDNGCGVPENAI---------- 546
Cdd:COG2972  332 LDLLIPKLI---------LQPLVE---NAIEHGiepkeGGGTIRISIRKEGDRLVITVEDNGVGMPEEKLeklleelssk 399
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 446840827 547 -RSNHYGMIIMRDRAQSLRGD---CRVRRRESGGTEVVVTF 583
Cdd:COG2972  400 gEGRGIGLRNVRERLKLYYGEeygLEIESEPGEGTTVTIRI 440
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
418-583 4.00e-05

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 46.38  E-value: 4.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 418 MQGDALPESSRELLSQIRNE-----------LN-ASWAQLRELLTTFRLQLtEPGLRPALEASCEEYSAKfgfPVKLDYQ 485
Cdd:PRK11100 281 LQEDPPPEDRARFTGNILTQsarlqqlidrlLElARLEQRQELEVLEPVAL-AALLEELVEAREAQAAAK---GITLRLR 356
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 486 LPPRLVPS-----HQAIHLLqiareaLSNALKHS-QASEVVVTVAQNDNQVKLTVQDNGCGVPENAI------------- 546
Cdd:PRK11100 357 PDDARVLGdpfllRQALGNL------LDNAIDFSpEGGTITLSAEVDGEQVALSVEDQGPGIPDYALpriferfyslprp 430
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 446840827 547 ----RSNHYGMIIMRDRAQSLRGDCRVRRRESGGTEVVVTF 583
Cdd:PRK11100 431 angrKSTGLGLAFVREVARLHGGEVTLRNRPEGGVLATLTL 471
HAMP COG2770
HAMP domain [Signal transduction mechanisms];
9-467 5.59e-05

HAMP domain [Signal transduction mechanisms];


Pssm-ID: 442051 [Multi-domain]  Cd Length: 631  Bit Score: 46.26  E-value: 5.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827   9 LTLVNQVALIVLLSTAIGLAGMAVSGWLVQGVQGSAHAINKAGSLRMQSYRLLAAVPLSEKDKPLIKEMEQTAFSAELTR 88
Cdd:COG2770   72 AAALLLLLLLLSLVALAALLLALLLLLLLALLLLLAALLLLLLLAALALLLLLLLLLAALLALLLALALLALLLGLAAAR 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827  89 AAERDGQLAQLQGLQDYWRNELIPTLMRAQNRETVSADVSQFVAGLdQLVSGFDRTTEMRIETVVLVhrvmAVFMALLLV 168
Cdd:COG2770  152 LLLAALLALAAALALALGAGELLLLADLAAAIAALLAALLLLLLGG-LLLVVLLEAALAALLLLLLL----ALLALLLAL 226
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 169 FTIIWLRARLLQPWRQLLAMASAVSHRDFTQRANISGRNEMAMLGTALNNMSAELAESYAVLEQRVQEKTAGLEHKNQIL 248
Cdd:COG2770  227 LLALLLARRITRPLRRLAEAARRIAAGDLDVRIPVSRKDEIGELARAFNRMADSLRESIEEAEEEEELAEAELARLLEAL 306
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 249 SFLWQANRRLHSRAPLCERLSPVLNGLQNLTLLRDIELRVYDTDDEENHQEFTCQPDMTCDDKGCQLCPRGVLPVGDRGT 328
Cdd:COG2770  307 LELLLALLLLLLALLLLAAAALLLELLLLLLLALLLLLLLAADLLLALALAALLLLLALELLLEAELLVLLALEALALEA 386
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 329 TLKWRLADSHTQYGILLATLPQGRHLSHDQQQLVDTLVEQLTATLALDRHQERQQQLIVMEERATIARELHDSIAQSLSC 408
Cdd:COG2770  387 ELAAVLALLAALAAALLLLELALEELVLALLALALLALAAAAAAAEAAAAALELAAAAIAAAAAAEAEGGLAELEAEELV 466
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446840827 409 MKMQVSCLQMQGDALPESSRELLSQIRNELNASWAQLRELLTTFRLQLTEPGLRPALEA 467
Cdd:COG2770  467 AAAEALLLLAALLLLAALGALELLLLEEEEEAGAAAEELAEELLLLEGLLLLLLLEAEA 525
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
499-543 5.86e-05

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis BceS, YxdK, and Bacillus thuringiensis YvcQ; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Bacillus subtilis BceS and Bacillus thuringiensis YvcQ, the HKs of the two-component regulatory system (TCSs) BceS-BceR and YvcQ-YvcP, repsectively, which are both involved in regulating bacitracin resistance. It also includes the HATPase domain of YxdK, the HK of YxdK-YxdJ TCS involved in sensing antimicrobial compounds.


Pssm-ID: 340424 [Multi-domain]  Cd Length: 109  Bit Score: 42.66  E-value: 5.86e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 446840827 499 LLQIAREALSNALKHS-QASEVVVTVAQNDNQVKLTVQDNGCGVPE 543
Cdd:cd16948    6 LSFIIGQIVSNALKYSkQGGKIEIYSETNEQGVVLSIKDFGIGIPE 51
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
499-546 4.90e-04

Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid sensor histidine kinases, similar to Escherichia coli EvgS, ArcB, TorS, BarA, RcsC; This family contains the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinases (HKs), including the following Escherichia coli HKs: EvgS, a HK of the EvgS-EvgA two-component system (TCS) that confers acid resistance; ArcB, a HK of the ArcB-ArcA TCS that modulates the expression of numerous genes in response to respiratory growth conditions; TorS, a HK of the TorS-TorR TCS which is involved in the anaerobic utilization of trimethylamine-N-oxide; BarA, a HK of the BarA-UvrY TCS involved in the regulation of carbon metabolism; and RcsC, a HK of the RcsB-RcsC TCS which regulates the expression of the capsule operon and of the cell division gene ftsZ. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), with most having accessory sensor domain(s) such as GAF, PAS and CHASE; many are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340399 [Multi-domain]  Cd Length: 110  Bit Score: 39.78  E-value: 4.90e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446840827 499 LLQIAREALSNALKHSQASEVVVTVA-----QNDNQVKLTVQDNGCGVPENAI 546
Cdd:cd16922    1 LRQILLNLLGNAIKFTEEGEVTLRVSleeeeEDGVQLRFSVEDTGIGIPEEQQ 53
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
497-546 5.75e-04

Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444507 [Multi-domain]  Cd Length: 496  Bit Score: 42.80  E-value: 5.75e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 446840827 497 IHLLQIAREALSNAlkhsqaSEVVVTVAQNDNQVKLTVQDNGCGVPENAI 546
Cdd:COG5805  401 INLIKNAIEAMPNG------GTITIHTEEEDNSVIIRVIDEGIGIPEERL 444
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
507-577 6.40e-04

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli CpxA; This family includes the histidine kinase-like ATPase (HATPase) domains of two-component sensor histidine kinase (HKs) similar to Escherichia coli CpxA, HK of the CpxA-CpxR two-component regulatory system (TCS) which may function in acid stress and in cell wall stability. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and a HAMP sensor domain; some also contain a CpxA family periplasmic domain.


Pssm-ID: 340425 [Multi-domain]  Cd Length: 104  Bit Score: 39.62  E-value: 6.40e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446840827 507 LSNALKHSQaSEVVVTVAQNDNQVKLTVQDNGCGVPENAIRSnhygmiIMRD--RAQSlrgdcrVRRRESGGT 577
Cdd:cd16949    9 LRNALRYSP-SKILLDISQDGDQWTITITDDGPGVPEDQLEQ------IFLPfyRVDS------ARDRESGGT 68
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
158-228 6.84e-04

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 42.69  E-value: 6.84e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446840827 158 VMAVFMALLLVFTIIWLRARLLQPWRQLLAMASAVSHRDFTQRANISGRNEMAMLGTALNNMSAELAESYA 228
Cdd:PRK15048 196 VIALVVVLILLVAWYGIRRMLLTPLAKIIAHIREIAGGNLANTLTIDGRSEMGDLAQSVSHMQRSLTDTVT 266
cpxA PRK09470
envelope stress sensor histidine kinase CpxA;
509-577 1.26e-03

envelope stress sensor histidine kinase CpxA;


Pssm-ID: 236532 [Multi-domain]  Cd Length: 461  Bit Score: 41.46  E-value: 1.26e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446840827 509 NALKHSQaSEVVVTVAQNDNQVKLTVQDNGCGVPEnairsnhygmiimRDRAQSLRGDCRV---RRRESGGT 577
Cdd:PRK09470 364 NALRYSH-TKIEVAFSVDKDGLTITVDDDGPGVPE-------------EEREQIFRPFYRVdeaRDRESGGT 421
PRK13560 PRK13560
hypothetical protein; Provisional
495-583 1.29e-03

hypothetical protein; Provisional


Pssm-ID: 106506 [Multi-domain]  Cd Length: 807  Bit Score: 41.97  E-value: 1.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 495 QAIHLLQIAREALSNALKH----SQASEVVVTVA-QNDNQVKLTVQDNGCGVPENA--IRSNHYGMIIMRDRAQSLRGDC 567
Cdd:PRK13560 708 KAIPCGLIISELLSNALKHafpdGAAGNIKVEIReQGDGMVNLCVADDGIGLPAGFdfRAAETLGLQLVCALVKQLDGEI 787
                         90
                 ....*....|....*.
gi 446840827 568 RVRRResGGTEVVVTF 583
Cdd:PRK13560 788 ALDSR--GGARFNIRF 801
PRK15347 PRK15347
two component system sensor kinase;
160-286 1.46e-03

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 41.55  E-value: 1.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 160 AVFMALLLVFTIIW-LRARLLQPWRQLLAMASAVSHRDFTQRANISGRNEMAMLGTALNNMSAELAESYAVLEQRVQEKT 238
Cdd:PRK15347 302 ALLILVLLTSVLFLlLRRYLAKPLWRFVDIINKTGPAALEPRLPENRLDELGSIAKAYNQLLDTLNEQYDTLENKVAERT 381
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446840827 239 AGLEHKNQILSflwQANRR--LHSRAPLCERLSPvLNG-LQNLTLLRDIEL 286
Cdd:PRK15347 382 QALAEAKQRAE---QANKRksEHLTTISHEIRTP-LNGvLGALELLQNTPL 428
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
365-543 3.10e-03

Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 40.21  E-value: 3.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 365 LVEQLTATLALDRHQERQQQLIVMEEratIAREL-HD------SIAQSLSCMKMQVSclqmqgdalPESSRELLSQIRNE 437
Cdd:COG3852  112 VLRDITERKRLERELRRAEKLAAVGE---LAAGLaHEirnpltGIRGAAQLLERELP---------DDELREYTQLIIEE 179
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 438 LNaswaQLRELLTTFrLQLTEPG--------LRPALEASCEEYSAKFGFPVKLDYQLPPRLVPS-------HQAI-HLLQ 501
Cdd:COG3852  180 AD----RLNNLVDRL-LSFSRPRpperepvnLHEVLERVLELLRAEAPKNIRIVRDYDPSLPEVlgdpdqlIQVLlNLVR 254
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 446840827 502 IAREALSNA----LKHSQASEVVVTVAQNDNQVKLTVQDNGCGVPE 543
Cdd:COG3852  255 NAAEAMPEGgtitIRTRVERQVTLGGLRPRLYVRIEVIDNGPGIPE 300
HATPase_TopVIB-like cd16933
Histidine kinase-like ATPase domain of type IIB topoisomerase, Topo VI, subunit B; This family ...
499-546 6.59e-03

Histidine kinase-like ATPase domain of type IIB topoisomerase, Topo VI, subunit B; This family includes the histidine kinase-like ATPase (HATPase) domain of the B subunit of topoisomerase VI (Topo VIB). Topo VI is a heterotetrameric complex composed of two TopVIA and two TopVIB subunits and is categorized as a type II B DNA topoisomerase. It is found in archaea and also in plants. Type II enzymes cleave both strands of a DNA duplex and pass a second duplex through the resulting break in an ATP-dependent mechanism. DNA cleavage by Topo VI generates two-nucleotide 5'-protruding ends.


Pssm-ID: 340410 [Multi-domain]  Cd Length: 203  Bit Score: 38.10  E-value: 6.59e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446840827 499 LLQIAREALSNAL----KHSQASEVVVTVAQNDNQ-VKLTVQDNGCGVPENAI 546
Cdd:cd16933   20 LYTTVRELVENSLdateEAGILPDIKVEIEEIGKDhYKVIVEDNGPGIPEEQI 72
HATPase_CreC-like cd16945
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
504-576 7.67e-03

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli CreC; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Escherichia coli CreC of the CreC-CreB two-component regulatory system (TCS) involved in catabolic regulation. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and accessory sensory domain(s) such as HAMP, CACHE or PAS.


Pssm-ID: 340421 [Multi-domain]  Cd Length: 106  Bit Score: 36.28  E-value: 7.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446840827 504 REALSNALKH-----SQASEVVVTVAQNDNQVKLTVQDNGCGVPENAI-----------------RSNHYGMIIMRDRAQ 561
Cdd:cd16945    6 RQAINNLLDNaidfsPEGGLIALQLEADTEGIELLVFDEGSGIPDYALnrvferfyslprphsgqKSTGLGLAFVQEVAQ 85
                         90
                 ....*....|....*
gi 446840827 562 SLRGDCRVRRRESGG 576
Cdd:cd16945   86 LHGGRITLRNRPDGV 100
PRK15347 PRK15347
two component system sensor kinase;
496-541 7.86e-03

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 39.24  E-value: 7.86e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 446840827 496 AIHLLQIAREALSNALKHSQASEVVVTVAQNDNQVKLTVQDNGCGV 541
Cdd:PRK15347 511 SLRLRQILVNLLGNAVKFTETGGIRLRVKRHEQQLCFTVEDTGCGI 556
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
507-543 9.22e-03

Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal transduction mechanisms];


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 39.00  E-value: 9.22e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 446840827 507 LSNALKHSQASE---VVVTVAQNDNQVKLTVQDNGCGVPE 543
Cdd:COG4251  403 ISNAIKYSRPGEpprIEIGAEREGGEWVFSVRDNGIGIDP 442
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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