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Conserved domains on  [gi|505191104|ref|WP_015378206|]
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MULTISPECIES: nitrate/nitrite two-component system sensor histidine kinase NarX [Serratia]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK10600 super family cl32542
nitrate/nitrite two-component system sensor histidine kinase NarX;
29-591 0e+00

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


The actual alignment was detected with superfamily member PRK10600:

Pssm-ID: 182581 [Multi-domain]  Cd Length: 569  Bit Score: 876.69  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104  29 MGISAWMSQSIQGNAHAINKAGSLRMQSYRLLAQVPLDERHEALIRELERDENSPDLQRSVEQEGLTQPFDTLRDYWQQT 108
Cdd:PRK10600   1 MAVSGWLVQGVQGSAHAINKAGSLRMQSYRLLAAVPLSEKDKPLLKEMEQTAFSPELQRAAERDGQLAQLQALQDYWRNE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 109 LQPRLRSAQRPADAAPQVAHFVQLLDKLVSDIDRQTERRLLMVTLVQAGFIALTLLLLIGTTCYLRRRLLHPWRQLVEMA 188
Cdd:PRK10600  81 LKPALQQAQNPEDVAADVAQFVAGLDALVSAFDHTTEMRIETVVLVHRVFAVFMALLLVFTIIWLRRRLLQPWRQLLSMA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 189 LAVGRGDFSRRFAQRGHqDEMASLGGALNTMSDELSATYSGLEQRVAEKTADLQQKNQMLSFLYRASRLLHASEPLCSRL 268
Cdd:PRK10600 161 NAVSHRDFTQRANISGR-DEMAMLGTALNNMSAELAESYAVLEQRVQEKTAGLEQKNQILSFLWQANRRLHSRAPLCERL 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 269 TPLLNQLQILTPLRAIQVRLYENDSREPLLQLSGNQPLrpeHCHNPVCSACLHDSDRQHPDNPSLSWSLSDKLGDYGVIV 348
Cdd:PRK10600 240 SPVLNGLQNLTLLRDIELRVYETDDEENHQEFTCQSDM---TCDDKGCQLCPRGVLPVGDRGTTLKWRLSDKHGQYGILL 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 349 AQHAPQQPLNDEHRQLVNTLVEQLTSVLAIERQVDHQQQLMLMEERAAIARELHDSIAQSLSCLKMQIACLQMQGETLSS 428
Cdd:PRK10600 317 ATLPQGRHLSHDQQQLVDTLVEQLTATLALERQQERQQQLIVMEERATIARELHDSIAQSLSCMKMQVSCLQMQGDALPE 396
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 429 ASQALVQQMREELNGAYRQLRELLTTFRLQLTEPGLLAALQSTVAEFNPKLGLNISLDYQLGPRTVPAYQAIHLLQIARE 508
Cdd:PRK10600 397 SSRELLSQIRNELNASWRQLRELLTTFRLQLTEPGLRPALEASCEEFSARFGFPVKLDYQLPPRLVPSHQAIHLLQIARE 476
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 509 ALSNILKHAAASEVSIQVINKRGEVTLSVCDNGRGLPAETSRPDHYGLIIMRDRAKSLHGRCDILPRSGGGTEVRVSFTP 588
Cdd:PRK10600 477 ALSNALKHAQASEVVVTVAQNQNQVKLSVQDNGCGVPENAERSNHYGLIIMRDRAQSLRGDCRVRRRESGGTEVVVTFIP 556

                 ...
gi 505191104 589 DNH 591
Cdd:PRK10600 557 EKT 559
 
Name Accession Description Interval E-value
PRK10600 PRK10600
nitrate/nitrite two-component system sensor histidine kinase NarX;
29-591 0e+00

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


Pssm-ID: 182581 [Multi-domain]  Cd Length: 569  Bit Score: 876.69  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104  29 MGISAWMSQSIQGNAHAINKAGSLRMQSYRLLAQVPLDERHEALIRELERDENSPDLQRSVEQEGLTQPFDTLRDYWQQT 108
Cdd:PRK10600   1 MAVSGWLVQGVQGSAHAINKAGSLRMQSYRLLAAVPLSEKDKPLLKEMEQTAFSPELQRAAERDGQLAQLQALQDYWRNE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 109 LQPRLRSAQRPADAAPQVAHFVQLLDKLVSDIDRQTERRLLMVTLVQAGFIALTLLLLIGTTCYLRRRLLHPWRQLVEMA 188
Cdd:PRK10600  81 LKPALQQAQNPEDVAADVAQFVAGLDALVSAFDHTTEMRIETVVLVHRVFAVFMALLLVFTIIWLRRRLLQPWRQLLSMA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 189 LAVGRGDFSRRFAQRGHqDEMASLGGALNTMSDELSATYSGLEQRVAEKTADLQQKNQMLSFLYRASRLLHASEPLCSRL 268
Cdd:PRK10600 161 NAVSHRDFTQRANISGR-DEMAMLGTALNNMSAELAESYAVLEQRVQEKTAGLEQKNQILSFLWQANRRLHSRAPLCERL 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 269 TPLLNQLQILTPLRAIQVRLYENDSREPLLQLSGNQPLrpeHCHNPVCSACLHDSDRQHPDNPSLSWSLSDKLGDYGVIV 348
Cdd:PRK10600 240 SPVLNGLQNLTLLRDIELRVYETDDEENHQEFTCQSDM---TCDDKGCQLCPRGVLPVGDRGTTLKWRLSDKHGQYGILL 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 349 AQHAPQQPLNDEHRQLVNTLVEQLTSVLAIERQVDHQQQLMLMEERAAIARELHDSIAQSLSCLKMQIACLQMQGETLSS 428
Cdd:PRK10600 317 ATLPQGRHLSHDQQQLVDTLVEQLTATLALERQQERQQQLIVMEERATIARELHDSIAQSLSCMKMQVSCLQMQGDALPE 396
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 429 ASQALVQQMREELNGAYRQLRELLTTFRLQLTEPGLLAALQSTVAEFNPKLGLNISLDYQLGPRTVPAYQAIHLLQIARE 508
Cdd:PRK10600 397 SSRELLSQIRNELNASWRQLRELLTTFRLQLTEPGLRPALEASCEEFSARFGFPVKLDYQLPPRLVPSHQAIHLLQIARE 476
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 509 ALSNILKHAAASEVSIQVINKRGEVTLSVCDNGRGLPAETSRPDHYGLIIMRDRAKSLHGRCDILPRSGGGTEVRVSFTP 588
Cdd:PRK10600 477 ALSNALKHAQASEVVVTVAQNQNQVKLSVQDNGCGVPENAERSNHYGLIIMRDRAQSLRGDCRVRRRESGGTEVVVTFIP 556

                 ...
gi 505191104 589 DNH 591
Cdd:PRK10600 557 EKT 559
NarX_sensor cd22900
ligand binding sensor domain of NarX, and related chemoreceptors; The periplasmic ligand ...
37-152 7.27e-53

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: 176.21  E-value: 7.27e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104  37 QSIQGNAHAINKAGSLRMQSYRLLAQVPLDERHEALIRELERDENSPDLQRSVEQEGLTQPFDTLRDYWQQTLQPRLRSA 116
Cdd:cd22900    1 NSIQGNAHAINKAGSLRMQSYRLLAAVPLNPQDQALLDELEQTLSSPELQRAARREGLQSQLQALQQYWQQQLKPALLAA 80
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 505191104 117 QRPADAAPQVAHFVQLLDKLVSDIDRQTERRLLMVT 152
Cdd:cd22900   81 KNPEDARAEVAAFVAQLDQLVSQIDQKTEQRLSLIS 116
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
364-586 1.86e-52

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 180.20  E-value: 1.86e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 364 LVNTLVEQLTSVLAIERQVDHQQQLMLMEERAAIARELHDSIAQSLSCLKMQIACLQMQGETLSSASQALVQQMREELNG 443
Cdd:COG4585   24 LVLLRARRAERAAELERELAARAEEAREEERRRIARELHDGVGQSLSAIKLQLEAARRLLDADPEAAREELEEIRELARE 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 444 AYRQLRELLTTFR-LQLTEPGLLAALQSTVAEFNPKLGLNISLDYQLGPRTVPAYQAIHLLQIAREALSNILKHAAASEV 522
Cdd:COG4585  104 ALAELRRLVRGLRpPALDDLGLAAALEELAERLLRAAGIRVELDVDGDPDRLPPEVELALYRIVQEALTNALKHAGATRV 183
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505191104 523 SIQVINKRGEVTLSVCDNGRGLPAETSRPDHYGLIIMRDRAKSLHGRCDILPRSGGGTEVRVSF 586
Cdd:COG4585  184 TVTLEVDDGELTLTVRDDGVGFDPEAAPGGGLGLRGMRERAEALGGTLTIGSAPGGGTRVRATL 247
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
499-586 2.06e-13

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 66.52  E-value: 2.06e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104   499 AIHLLQIAREALSNILKHA-AASEVSIQVINKRGEVTLSVCDNGRGLPAE----------TSRPDHY-------GLIIMR 560
Cdd:smart00387   3 PDRLRQVLSNLLDNAIKYTpEGGRITVTLERDGDHVEITVEDNGPGIPPEdlekifepffRTDKRSRkiggtglGLSIVK 82
                           90       100
                   ....*....|....*....|....*.
gi 505191104   561 DRAKSLHGRCDILPRSGGGTEVRVSF 586
Cdd:smart00387  83 KLVELHGGEISVESEPGGGTTFTITL 108
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
499-586 2.66e-13

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: 66.24  E-value: 2.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104  499 AIHLLQIAREALSNILKHAA-ASEVSIqVINKRGEVTLSVCDNGRGLPAET--------SRPDH-------YGLIIMRDR 562
Cdd:pfam02518   3 ELRLRQVLSNLLDNALKHAAkAGEITV-TLSEGGELTLTVEDNGIGIPPEDlprifepfSTADKrggggtgLGLSIVRKL 81
                          90       100
                  ....*....|....*....|....
gi 505191104  563 AKSLHGRCDILPRSGGGTEVRVSF 586
Cdd:pfam02518  82 VELLGGTITVESEPGGGTTVTLTL 105
 
Name Accession Description Interval E-value
PRK10600 PRK10600
nitrate/nitrite two-component system sensor histidine kinase NarX;
29-591 0e+00

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


Pssm-ID: 182581 [Multi-domain]  Cd Length: 569  Bit Score: 876.69  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104  29 MGISAWMSQSIQGNAHAINKAGSLRMQSYRLLAQVPLDERHEALIRELERDENSPDLQRSVEQEGLTQPFDTLRDYWQQT 108
Cdd:PRK10600   1 MAVSGWLVQGVQGSAHAINKAGSLRMQSYRLLAAVPLSEKDKPLLKEMEQTAFSPELQRAAERDGQLAQLQALQDYWRNE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 109 LQPRLRSAQRPADAAPQVAHFVQLLDKLVSDIDRQTERRLLMVTLVQAGFIALTLLLLIGTTCYLRRRLLHPWRQLVEMA 188
Cdd:PRK10600  81 LKPALQQAQNPEDVAADVAQFVAGLDALVSAFDHTTEMRIETVVLVHRVFAVFMALLLVFTIIWLRRRLLQPWRQLLSMA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 189 LAVGRGDFSRRFAQRGHqDEMASLGGALNTMSDELSATYSGLEQRVAEKTADLQQKNQMLSFLYRASRLLHASEPLCSRL 268
Cdd:PRK10600 161 NAVSHRDFTQRANISGR-DEMAMLGTALNNMSAELAESYAVLEQRVQEKTAGLEQKNQILSFLWQANRRLHSRAPLCERL 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 269 TPLLNQLQILTPLRAIQVRLYENDSREPLLQLSGNQPLrpeHCHNPVCSACLHDSDRQHPDNPSLSWSLSDKLGDYGVIV 348
Cdd:PRK10600 240 SPVLNGLQNLTLLRDIELRVYETDDEENHQEFTCQSDM---TCDDKGCQLCPRGVLPVGDRGTTLKWRLSDKHGQYGILL 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 349 AQHAPQQPLNDEHRQLVNTLVEQLTSVLAIERQVDHQQQLMLMEERAAIARELHDSIAQSLSCLKMQIACLQMQGETLSS 428
Cdd:PRK10600 317 ATLPQGRHLSHDQQQLVDTLVEQLTATLALERQQERQQQLIVMEERATIARELHDSIAQSLSCMKMQVSCLQMQGDALPE 396
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 429 ASQALVQQMREELNGAYRQLRELLTTFRLQLTEPGLLAALQSTVAEFNPKLGLNISLDYQLGPRTVPAYQAIHLLQIARE 508
Cdd:PRK10600 397 SSRELLSQIRNELNASWRQLRELLTTFRLQLTEPGLRPALEASCEEFSARFGFPVKLDYQLPPRLVPSHQAIHLLQIARE 476
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 509 ALSNILKHAAASEVSIQVINKRGEVTLSVCDNGRGLPAETSRPDHYGLIIMRDRAKSLHGRCDILPRSGGGTEVRVSFTP 588
Cdd:PRK10600 477 ALSNALKHAQASEVVVTVAQNQNQVKLSVQDNGCGVPENAERSNHYGLIIMRDRAQSLRGDCRVRRRESGGTEVVVTFIP 556

                 ...
gi 505191104 589 DNH 591
Cdd:PRK10600 557 EKT 559
PRK10935 PRK10935
nitrate/nitrite two-component system sensor histidine kinase NarQ;
9-588 3.52e-111

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


Pssm-ID: 236800 [Multi-domain]  Cd Length: 565  Bit Score: 343.76  E-value: 3.52e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104   9 SIVNQVALLMLLSGILGVAGMGIsawMSQSIqGNAHAINKAGSLRMQSYRLL--AQVPLDErHEALIRELERDENSPDLQ 86
Cdd:PRK10935  10 SIARAMLLIILLSSLTTGFALLT---LASSL-RDAEAINIAGSLRMQSYRLAydLQSGSPQ-LNAHLREFEQSLHSPALK 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104  87 RS----VEQEgLTQPFDTLRDYWQqTLQPRLRSAQRPADAApQVAHFVQLLDKLVSDIDRQTERRLLMVTLVQ-AGFIAL 161
Cdd:PRK10935  85 NLnrwyVPED-VKDRYALLIARWL-EMKSYLEQGDSRWYQA-NIANYVDQIDLFVLALQHFAERKLILLAAISlLGLILI 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 162 TLLLLIGTTcYLRRRLLHPWRQLVEMALAVGRGDFSRRFAQRGHQDEMASLGGALNTMSDELSATYSGLEQRVAEKTADL 241
Cdd:PRK10935 162 LTLVFFTVR-FTRRQVVAPLNQLVTASQQIEKGQFDHIPLDTTLPNELGLLAKAFNQMSSELHKLYRSLEASVEEKTRKL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 242 QQKNQMLSFLYRASRLLHASEPLCSRLTPLLNQLQILTPLRAIQVRLYENdsrePLLQLSGNQPlrpehchnpvcsaclh 321
Cdd:PRK10935 241 TQANRSLEVLYQCSQALNASQIDVHCFRHILQIVRDHEGLDYLELEVGEN----EHWRISEGQP---------------- 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 322 dsdrqhpdNPSLSWSLSD-KLGD--YGVIVAQHAPQQPlndeHRQLVNTLVEQLTSVLAIERQVDHQQQLMLMEERAAIA 398
Cdd:PRK10935 301 --------NPELPWQILPlTMEDtvLGYLHWQASLPCP----DEPLMNNVAQMLGRGLYFNQAQKQQQQLLLMEERATIA 368
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 399 RELHDSIAQSLSCLKMQIACLQMQGETLSSASQALVQQMREELNGAYRQLRELLTTFRLQLTEPGLLAALQSTVAEFNPK 478
Cdd:PRK10935 369 RELHDSLAQVLSYLKIQLTLLKRSLDEDNAKAQSIIAEFDQALSDAYRQLRELLTTFRLTIQEANLGSALEEMLDQLRNQ 448
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 479 LGLNISLDYQLGPRTVPAYQAIHLLQIAREALSNILKHAAASEVSIQ-VINKRGEVTLSVCDNGRGLPAETSRPDHYGLI 557
Cdd:PRK10935 449 TDAKITLDCRLPSQALDAQQQVHLLQIIREATLNAIKHANASEIAVScVTNPDGEHTVSIRDDGIGIGELKEPEGHYGLN 528
                        570       580       590
                 ....*....|....*....|....*....|.
gi 505191104 558 IMRDRAKSLHGRCDILPRSGGGTEVRVSFTP 588
Cdd:PRK10935 529 IMQERAERLGGTLTISQPPGGGTTVSLTFPS 559
NarX_sensor cd22900
ligand binding sensor domain of NarX, and related chemoreceptors; The periplasmic ligand ...
37-152 7.27e-53

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: 176.21  E-value: 7.27e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104  37 QSIQGNAHAINKAGSLRMQSYRLLAQVPLDERHEALIRELERDENSPDLQRSVEQEGLTQPFDTLRDYWQQTLQPRLRSA 116
Cdd:cd22900    1 NSIQGNAHAINKAGSLRMQSYRLLAAVPLNPQDQALLDELEQTLSSPELQRAARREGLQSQLQALQQYWQQQLKPALLAA 80
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 505191104 117 QRPADAAPQVAHFVQLLDKLVSDIDRQTERRLLMVT 152
Cdd:cd22900   81 KNPEDARAEVAAFVAQLDQLVSQIDQKTEQRLSLIS 116
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
364-586 1.86e-52

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 180.20  E-value: 1.86e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 364 LVNTLVEQLTSVLAIERQVDHQQQLMLMEERAAIARELHDSIAQSLSCLKMQIACLQMQGETLSSASQALVQQMREELNG 443
Cdd:COG4585   24 LVLLRARRAERAAELERELAARAEEAREEERRRIARELHDGVGQSLSAIKLQLEAARRLLDADPEAAREELEEIRELARE 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 444 AYRQLRELLTTFR-LQLTEPGLLAALQSTVAEFNPKLGLNISLDYQLGPRTVPAYQAIHLLQIAREALSNILKHAAASEV 522
Cdd:COG4585  104 ALAELRRLVRGLRpPALDDLGLAAALEELAERLLRAAGIRVELDVDGDPDRLPPEVELALYRIVQEALTNALKHAGATRV 183
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505191104 523 SIQVINKRGEVTLSVCDNGRGLPAETSRPDHYGLIIMRDRAKSLHGRCDILPRSGGGTEVRVSF 586
Cdd:COG4585  184 TVTLEVDDGELTLTVRDDGVGFDPEAAPGGGLGLRGMRERAEALGGTLTIGSAPGGGTRVRATL 247
HATPase_UhpB-NarQ-NarX-like cd16917
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
502-586 9.94e-27

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: 103.79  E-value: 9.94e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 502 LLQIAREALSNILKHAAASEVSIQVINKRGEVTLSVCDNGRGLPAETSRPD-HYGLIIMRDRAKSLHGRCDILPRSGGGT 580
Cdd:cd16917    1 LYRIVQEALTNALKHAGASRVRVTLSYTADELTLTVVDDGVGFDGPAPPGGgGFGLLGMRERAELLGGTLTIGSRPGGGT 80

                 ....*.
gi 505191104 581 EVRVSF 586
Cdd:cd16917   81 RVTARL 86
NarX_NarQ_sensor cd19408
ligand binding sensor domain of NarX and NarQ, and related chemoreceptors; The periplasmic ...
37-150 8.67e-26

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: 102.32  E-value: 8.67e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104  37 QSIQGNAHAINKAGSLRMQSYRLLAQVPLDERH-----EALIRELERDENSPDLQRSVEQEG---LTQPFDTLRDYWQQT 108
Cdd:cd19408    1 ESTEGDAAAINLAGSLRMQSYRLASLLLQAALEpaeqlAQLIDEFEQRLNSPALTRALPRDSdhpLRQAYQAVLQHWQQE 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 505191104 109 LQPRL----RSAQRPADAAPQVAHFVQLLDKLVSDIDRQTERRLLM 150
Cdd:cd19408   81 LRPALeaaaSGAADREAYLAEVDEFVAQIDQLVKLLQQDTEAKIRL 126
UhpB COG3851
Signal transduction histidine kinase UhpB, glucose-6-phosphate specific [Signal transduction ...
355-587 1.57e-25

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


Pssm-ID: 443060 [Multi-domain]  Cd Length: 493  Bit Score: 110.10  E-value: 1.57e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 355 QPLNDEHRQLVNTLVEQLtsVLAierqvdhqQQLMLMEE--RAAIARELHDSIAQSLSCLKMQIACLQMQGETLSSASQA 432
Cdd:COG3851  262 QRQRQLNQQLEQELRENR--ALA--------RQLVSAEEseRREIARELHDEIGQNITAIRTQASILKRLAPQPEIEQSA 331
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 433 lvQQMREELNGAYRQLRELLTTFR-LQLTEPGLLAALQSTVAEF-NPKLGLNISLDYQLGPRTVPAYQAIHLLQIAREAL 510
Cdd:COG3851  332 --QSIESLALRIYDTTRRLLDRLRpAVLDELGLEEALRELPRELaFEEPGISCQLDLRGDPSLLDDTLQLTLYRLVQEAL 409
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505191104 511 SNILKHAAASEVSIQVINKRGEVTLSVCDNGRGLPAETSRPdHYGLIIMRDRAKSLHGRCDILPRsGGGTEVRVSFT 587
Cdd:COG3851  410 TNILKHAEASQIRISLSQDKRLLSLEIRDDGIGLPPELRAK-GFGLRGMRERVRALGGDFRLSSA-PKGTRLSVLLP 484
PRK11644 PRK11644
signal transduction histidine-protein kinase/phosphatase UhpB;
355-585 1.45e-19

signal transduction histidine-protein kinase/phosphatase UhpB;


Pssm-ID: 236945 [Multi-domain]  Cd Length: 495  Bit Score: 91.96  E-value: 1.45e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 355 QPLNDE-HRQLVNTLVEQLTSVL---AIERQVDHQQQLML--------------MEE--RAAIARELHDSIAQSLSCLKM 414
Cdd:PRK11644 243 QTWHDHpVDLLLSLLAQSLTGLLlgaGIQRQRELNQSLQKelarnrhlaerlleTEEsvRRDVARELHDEIGQTITAIRT 322
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 415 QIACLQmqgeTLSSASQALVQ--QMREELN-GAYRQLRELLTTFR-LQLTEPGLLAALQSTVAEFNPK-LGLNISLDYQL 489
Cdd:PRK11644 323 QAGIIK----RLAADNASVKQsaQLIEQLSlGVYDTVRRLLGRLRpRQLDDLTLEQAIRSLMREMELEdRGIVSHLDWRI 398
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 490 GPRTVPAYQAIHLLQIAREALSNILKHAAASEVSIQVINKRGEVTLSVCDNGRGLPAETSRPDhYGLIIMRDRAKSLHGR 569
Cdd:PRK11644 399 DESALSETQRVTLFRVCQEGLNNIVKHADASAVTLQGWQQDERLMLVIEDDGSGLPPGSGQQG-FGLRGMRERVTALGGT 477
                        250
                 ....*....|....*.
gi 505191104 570 CDIlpRSGGGTEVRVS 585
Cdd:PRK11644 478 LTI--SCTHGTRLSVS 491
NarQ_sensor cd22899
ligand binding sensor domain of NarQ, and related chemoreceptors; The periplasmic ligand ...
40-150 1.02e-15

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: 73.32  E-value: 1.02e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104  40 QGNAHAINKAGSLRMQSYRLL----AQVPLDERHealIRELERDENSPDLQRSVEQ---EGLTQPFDTLRDYWQQtLQPR 112
Cdd:cd22899    4 LSDAEAINVAGSLRMQSYRLAydleSESPLLEQH---IAQYEQSLHSPALQSLDRWyvpDEVKQRYQQLLARWQE-MKQY 79
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 505191104 113 LRSaQRPADAAPQVAHFVQLLDKLVSDIDRQTERRLLM 150
Cdd:cd22899   80 LLQ-GDPASYLQQVASYVDQIDQFVLALQHFAERKLRL 116
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
499-586 2.06e-13

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 66.52  E-value: 2.06e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104   499 AIHLLQIAREALSNILKHA-AASEVSIQVINKRGEVTLSVCDNGRGLPAE----------TSRPDHY-------GLIIMR 560
Cdd:smart00387   3 PDRLRQVLSNLLDNAIKYTpEGGRITVTLERDGDHVEITVEDNGPGIPPEdlekifepffRTDKRSRkiggtglGLSIVK 82
                           90       100
                   ....*....|....*....|....*.
gi 505191104   561 DRAKSLHGRCDILPRSGGGTEVRVSF 586
Cdd:smart00387  83 KLVELHGGEISVESEPGGGTTFTITL 108
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
499-586 2.66e-13

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: 66.24  E-value: 2.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104  499 AIHLLQIAREALSNILKHAA-ASEVSIqVINKRGEVTLSVCDNGRGLPAET--------SRPDH-------YGLIIMRDR 562
Cdd:pfam02518   3 ELRLRQVLSNLLDNALKHAAkAGEITV-TLSEGGELTLTVEDNGIGIPPEDlprifepfSTADKrggggtgLGLSIVRKL 81
                          90       100
                  ....*....|....*....|....
gi 505191104  563 AKSLHGRCDILPRSGGGTEVRVSF 586
Cdd:pfam02518  82 VELLGGTITVESEPGGGTTVTLTL 105
HisKA_3 pfam07730
Histidine kinase; This is the dimerization and phosphoacceptor domain of a sub-family of ...
393-456 5.35e-13

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: 64.18  E-value: 5.35e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505191104  393 ERAAIARELHDSIAQSLSCLKMQIACLQMQGETLSSASQALVQQMREELNGAYRQLRELLTTFR 456
Cdd:pfam07730   1 ERNRIARELHDSVGQSLTAIKLQLELARRLLDRDPEEAREQLDAIRELAREALQELRRLLGDLR 64
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
172-586 7.68e-12

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: 67.68  E-value: 7.68e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 172 YLRRRLLHPWRQLVEMALAVGRGDFSRRFAQRGhQDEMASLGGALNTMSDELSATYSGLEQRVAEKTADLQQKNQMLSFL 251
Cdd:COG5000   28 LLARRLTRPLRRLAEATRAVAAGDLSVRLPVTG-DDEIGELARAFNRMTDQLKEQREELEERRRYLETILENLPAGVIVL 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 252 YRASRLLHAseplcsrltpllnqlqiltplraiqvrlyeNDSREPLLQLSGNQPLrpehchnpvcsaclhdsdRQHPDNP 331
Cdd:COG5000  107 DADGRITLA------------------------------NPAAERLLGIPLEELI------------------GKPLEEL 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 332 SLSWSLSDKLGDYGVIVAQHAPQQPLNDEHRQLVNTLVEQLTSVLAIERQVdhqQQLMLMEERAAI---AREL-HD---- 403
Cdd:COG5000  139 LPELDLAELLREALERGWQEEIELTRDGRRTLLVRASPLRDDGYVIVFDDI---TELLRAERLAAWgelARRIaHEiknp 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 404 --SIAQSLSCLKMQIA-CLQMQGETLSSASQALVQQMREelngayrqLRELLTTFR-------LQLTEPGLLAALQSTVA 473
Cdd:COG5000  216 ltPIQLSAERLRRKLAdKLEEDREDLERALDTIIRQVDR--------LKRIVDEFLdfarlpePQLEPVDLNELLREVLA 287
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 474 EFNPKL-GLNISLDYQLGPRTVPAY-------QAIH-LLQIAREALSNilkhaaASEVSIQVINKRGEVTLSVCDNGRGL 544
Cdd:COG5000  288 LYEPALkEKDIRLELDLDPDLPEVLadrdqleQVLInLLKNAIEAIEE------GGEIEVSTRREDGRVRIEVSDNGPGI 361
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 505191104 545 PAE----------TSRPDHYGL---I---IMRDraksLHGRCDILPRSGGGTEVRVSF 586
Cdd:COG5000  362 PEEvlerifepffTTKPKGTGLglaIvkkIVEE----HGGTIELESRPGGGTTFTIRL 415
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
377-586 5.15e-10

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 59.92  E-value: 5.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 377 AIERQVDHQQQLMLMEER--AAIARELHdsiaQSLSCLKMQIACLQMQGETLSSASQALVQQMREELNGAYRQLRELLT- 453
Cdd:COG2205    1 ELEEALEELEELERLKSEflANVSHELR----TPLTSILGAAELLLDEEDLSPEERRELLEIIRESAERLLRLIEDLLDl 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 454 ------TFRLQLTEPGLLAALQSTVAEFNPKL-GLNISLDYQLGPRTVPAYQAIHLL-QIAREALSNILKHA-AASEVSI 524
Cdd:COG2205   77 srlesgKLSLELEPVDLAELLEEAVEELRPLAeEKGIRLELDLPPELPLVYADPELLeQVLANLLDNAIKYSpPGGTITI 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505191104 525 QVINKRGEVTLSVCDNGRGLPAE-----------TSRPDHY-----GLIIMRDRAKSLHGRCDILPRSGGGTEVRVSF 586
Cdd:COG2205  157 SARREGDGVRISVSDNGPGIPEEeleriferfyrGDNSRGEggtglGLAIVKRIVEAHGGTIWVESEPGGGTTFTVTL 234
COG3920 COG3920
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...
379-592 6.08e-10

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


Pssm-ID: 443125 [Multi-domain]  Cd Length: 495  Bit Score: 61.84  E-value: 6.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 379 ERQVDHQQQLMLMEERAAIARELHD------SIAQSLsclkmqiacLQMQGETLSSASqalVQQMREELNG-------AY 445
Cdd:COG3920  280 ERKRAEEELEASLEEKELLLRELHHrvknnlQVVSSL---------LRLQARRADDPE---AREALEESQNriqalalVH 347
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 446 RQLRELLTTFRLQLTE--PGLLAALQSTVAEFNpklglnISLDYQLGPRTVPAYQAIHLLQIAREALSNILKHAAAS--- 520
Cdd:COG3920  348 ELLYQSEDWEGVDLRDylRELLEPLRDSYGGRG------IRIELDGPDVELPADAAVPLGLILNELVTNALKHAFLSgeg 421
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505191104 521 -EVSIQVINKRGEVTLSVCDNGRGLPAETSRPDH--YGLIIMRDRAKSLHGRCDIlpRSGGGTEVRVSFTPDNHA 592
Cdd:COG3920  422 gRIRVSWRREDGRLRLTVSDNGVGLPEDVDPPARkgLGLRLIRALVRQLGGTLEL--DRPEGTRVRITFPLAELA 494
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
175-228 6.17e-08

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


Pssm-ID: 197640 [Multi-domain]  Cd Length: 53  Bit Score: 49.17  E-value: 6.17e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 505191104   175 RRLLHPWRQLVEMALAVGRGDFSRRFAQRGhQDEMASLGGALNTMSDELSATYS 228
Cdd:smart00304   1 RRLLRPLRRLAEAAQRIADGDLTVRLPVDG-RDEIGELARAFNEMADRLEETIA 53
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
419-586 7.35e-08

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 54.53  E-value: 7.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 419 LQMQGETLSSASQALVQQMREELNGAYRQLRELLTTFRLQLTEPG-------LLAALQSTVAEFNPKL---GLNISLDYQ 488
Cdd:COG0642  132 LELLLEELDEEQREYLETILRSADRLLRLINDLLDLSRLEAGKLElepepvdLAELLEEVVELFRPLAeekGIELELDLP 211
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 489 LGPRTVPAYqAIHLLQIAREALSNILKHAAA-SEVSIQVINKRGEVTLSVCDNGRGLPAE-----------TSRPDHY-- 554
Cdd:COG0642  212 DDLPTVRGD-PDRLRQVLLNLLSNAIKYTPEgGTVTVSVRREGDRVRISVEDTGPGIPPEdlerifepffrTDPSRRGgg 290
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 505191104 555 ---GLIIMRDRAKSLHGRCDILPRSGGGTEVRVSF 586
Cdd:COG0642  291 tglGLAIVKRIVELHGGTIEVESEPGKGTTFTVTL 325
HAMP pfam00672
HAMP domain;
173-225 7.77e-08

HAMP domain;


Pssm-ID: 459898 [Multi-domain]  Cd Length: 53  Bit Score: 49.16  E-value: 7.77e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 505191104  173 LRRRLLHPWRQLVEMALAVGRGDFSRRFAQRGhQDEMASLGGALNTMSDELSA 225
Cdd:pfam00672   2 LARRILRPLRRLAEAARRIASGDLDVRLPVSG-RDEIGELARAFNQMAERLRE 53
PilJ pfam13675
Type IV pili methyl-accepting chemotaxis transducer N-term; This domain is found on many type ...
34-127 1.69e-07

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: 49.78  E-value: 1.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104   34 WMSQSIQGNAHAINKAGSLRMQSYRLLAQVPLderheALIRELERDENSPDLQRSVEQ---------------------E 92
Cdd:pfam13675   1 WTLWQSEGDAAAINAAGSLRMQSQRLAKSVLL-----ALAGNYDLAEAFADLEESIDQfdrtlaalalgdlarglfvpaG 75
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 505191104   93 GLTQPFDTLRDYWQQTLQPRLRSAQRPADAAPQVA 127
Cdd:pfam13675  76 AIRAQLEAVQPLWERLRKPAEAVLAQQDTLAYLAA 110
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; ...
178-223 4.92e-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: 46.28  E-value: 4.92e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 505191104 178 LHPWRQLVEMALAVGRGDFSRRFAQRGHqDEMASLGGALNTMSDEL 223
Cdd:cd06225    1 TRPLRRLTEAARRIAEGDLDVRVPVRSK-DEIGELARAFNQMAERL 45
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
1-249 1.27e-06

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


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 51.17  E-value: 1.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104   1 MKRLLAPLSIVNQVALLMLLSGILGVAGMGISAWMSQSIQGNAHAINKAGSLRMQSYRLLAQVPLDERHEALIRELERDE 80
Cdd:COG0840   30 LILLALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVVLLALLLALLLLLLALLALALAALALLAAL 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104  81 NSPDLQRSVEQEGLTQPFDTLRDYWQQTLQPRLRSAQRPADAAPQVAHFVQLLDKLVSDIDRQTERRLLMVTLVQAGFIA 160
Cdd:COG0840  110 AALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAAALAALLEAAALALAAAALALALLAAALL 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 161 LTLLLLIGTTCYLRRRLLHPWRQLVEMALAVGRGDFSRRFAQRGhQDEMASLGGALNTMSDELSATYSGLEQ---RVAEK 237
Cdd:COG0840  190 ALVALAIILALLLSRSITRPLRELLEVLERIAEGDLTVRIDVDS-KDEIGQLADAFNRMIENLRELVGQVREsaeQVASA 268
                        250
                 ....*....|..
gi 505191104 238 TADLQQKNQMLS 249
Cdd:COG0840  269 SEELAASAEELA 280
HATPase_NtrY-like cd16944
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
507-586 1.92e-06

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Azorhizobium caulinodans NtrY; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs) such as Azorhizobium caulinodans ORS571 NtrY of the NtrY-NtrX TCS, which is involved in nitrogen fixation and metabolism. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and a HAMP sensor domain; some also have PAS sensor domains.


Pssm-ID: 340420 [Multi-domain]  Cd Length: 108  Bit Score: 46.76  E-value: 1.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 507 REALSNILKHAAAS---------EVSIQV-INKRGEVTLSVCDNGRGLPAE----------TSRPDHYGL------IIMR 560
Cdd:cd16944    6 SQVLTNILKNAAEAiegrpsdvgEVRIRVeADQDGRIVLIVCDNGKGFPREmrhratepyvTTRPKGTGLglaivkKIME 85
                         90       100
                 ....*....|....*....|....*.
gi 505191104 561 DRAkslhGRCDILPRSGGGTEVRVSF 586
Cdd:cd16944   86 EHG----GRISLSNREAGGACIRIIL 107
NarQ COG3850
Signal transduction histidine kinase NarQ, nitrate/nitrite-specific [Signal transduction ...
39-474 2.77e-06

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


Pssm-ID: 443059 [Multi-domain]  Cd Length: 448  Bit Score: 50.27  E-value: 2.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104  39 IQGNAHAINKAGSLRMQSYRLLAQVPLDERHEALIRELERDENSPDLQRSVEQEGLTQPFDTLRDYWQQTLQPRLRSAQR 118
Cdd:COG3850    4 LLLLALALLRLLLALLALLLLALLLLSLLALLLLLERTLLRLLSLLASAGLLAALLAALLLLLSLGLLALLLALLLLLLL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 119 PADAAPQVAHFVQLLDKLVSDIDRQTERRLLMVTLVQAGFIALTLLLLIGTTCYLRRRLLHPWRQLVEMALAVGRGDFSR 198
Cdd:COG3850   84 LLLAALLSLLLLLLLLLLLLLLLLLLLLAAAINRKLALLRLLLALLLALLLAYLLRRRIVRPLRRLTQAAERIARGDFDA 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 199 RFAQRGhQDEMASLGGALNTMSDELSATYSGLEQ-RVAEKTADLQQKNQMLSFLYRASRLLHASEPLCSRLTPLLNQLQI 277
Cdd:COG3850  164 RVPVSG-RDELGTLARAFNRMADELQELYAELEEeEELEAELELLALLDELLLLAALLLLLALLLALLLAALLAALLLLL 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 278 LTPLRAIQVRLYENDSREPLLQLSGNQPLRPEHCHNPVCSACLHDSDRQHPDNPSLSWSLSDKLGDYGVIVAQHAPQQPL 357
Cdd:COG3850  243 LLQDALAESELLALNILAGLLELLLALLLLLLASALLLLELELLALLLELVELLALAAAEEALLLLVELAALLLLLLLQA 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 358 NDEHRQLVNTLVEQLTSVLAIERQVDHQQQLMLMEERAAIARELHDSIAQSLSCLKMQIACLQMQGETLSSASQALVQQM 437
Cdd:COG3850  323 IANASLLLIALASVVAALLELASILALQAALEAAAAGAALAAAAAAAGLARALAQAGADAAEALGLLAEASEGAAGQGAG 402
                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 505191104 438 REELNGAYRQLRELLTTFRLQLTEPGLLAALQSTVAE 474
Cdd:COG3850  403 LVDVEGGVAGEGGLVVLIVSIIAGGEAIARGEALAAR 439
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
409-586 9.33e-06

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 48.40  E-value: 9.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 409 LSCLKMQIACLQMQGETLSSASQALVQQMREELNGAYRQLRELLT-------TFRLQLTEPGLLAALQSTVAEFNPKL-- 479
Cdd:COG5002  180 LTSIRGYLELLLDGAADDPEERREYLEIILEEAERLSRLVNDLLDlsrlesgELKLEKEPVDLAELLEEVVEELRPLAee 259
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 480 -GLNISLDYQLGPRTVPAyQAIHLLQIAREALSNILKHAAA-SEVSIQVINKRGEVTLSVCDNGRGLPAE---------- 547
Cdd:COG5002  260 kGIELELDLPEDPLLVLG-DPDRLEQVLTNLLDNAIKYTPEgGTITVSLREEDDQVRISVRDTGIGIPEEdlpriferfy 338
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 505191104 548 ---TSRPDHY-----GLIIMRDRAKSLHGRCDILPRSGGGTEVRVSF 586
Cdd:COG5002  339 rvdKSRSRETggtglGLAIVKHIVEAHGGRIWVESEPGKGTTFTITL 385
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
461-586 1.38e-05

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


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 44.90  E-value: 1.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 461 EPGLLAALQSTVAEFNPKLGLnisldyqlgprtvPAYQAIHLLQIAREALSNILKHA----AASEVSIQVINKRGEVTLS 536
Cdd:COG2172    7 DLEDLGLARRAVRALLRELGL-------------DEDDADDLVLAVSEAVTNAVRHAyggdPDGPVEVELELDPDGLEIE 73
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 505191104 537 VCDNGRGL-------PAETSRPDHYGLIIMRDRAKSLHGRcdilpRSGGGTEVRVSF 586
Cdd:COG2172   74 VRDEGPGFdpedlpdPYSTLAEGGRGLFLIRRLMDEVEYE-----SDPGGTTVRLVK 125
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
359-586 1.55e-05

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 47.49  E-value: 1.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 359 DEHRQLVNTLVEQLTSVLAIERQVDHQQQLMLMEER--------AAIArelHDsIAQSLSCLKMQIACLQMQGETLSSAS 430
Cdd:COG4191  103 AEENAELEELERDITELERAEEELRELQEQLVQSEKlaalgelaAGIA---HE-INNPLAAILGNAELLRRRLEDEPDPE 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 431 QA--LVQQMREELNGAYRQLRELLTTFRLQLTEPGLL---AALQSTVAEFNPKLG-LNISLDYQLGPRTVPAY------- 497
Cdd:COG4191  179 ELreALERILEGAERAAEIVRSLRAFSRRDEEEREPVdlnELIDEALELLRPRLKaRGIEVELDLPPDLPPVLgdpgqle 258
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 498 QAI-HLLQIAREALsnilKHAAASEVSIQVINKRGEVTLSVCDNGRGLPAE----------TSRPDHY----GLIIMRDR 562
Cdd:COG4191  259 QVLlNLLINAIDAM----EEGEGGRITISTRREGDYVVISVRDNGPGIPPEvlerifepffTTKPVGKgtglGLSISYGI 334
                        250       260
                 ....*....|....*....|....
gi 505191104 563 AKSLHGRCDILPRSGGGTEVRVSF 586
Cdd:COG4191  335 VEKHGGRIEVESEPGGGTTFTITL 358
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
521-585 3.54e-05

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Rhizobium meliloti FixL, and Rhodobacter capsulatus DctS; includes hybrid sensor histidine kinase similar to Pseudomonas mendocina TmoS; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs), such as Pseudomonas mendocina TmoS HK of the TmoS-TmoT TCS, which controls the expression of the toluene-4-monooxygenase pathway, Rhizobium meliloti FixL HK of the FixL-FixJ TCS, which regulates the expression of the genes related to nitrogen fixation in the root nodule in response to O(2) levels, and Rhodobacter capsulatus DctS of the DctS-DctR TCS, which controls synthesis of the high-affinity C4-dicarboxylate transport system. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and PAS sensor domain(s); many are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340397 [Multi-domain]  Cd Length: 104  Bit Score: 43.15  E-value: 3.54e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505191104 521 EVSIQV-INKRGEVTLSVCDNGRGLPAE----------TSRPDHYG--LIIMRDRAKSLHGRCDILPRSGGGTEVRVS 585
Cdd:cd16920   25 ELTIRTsPADDRAVTISVKDTGPGIAEEvagqlfdpfyTTKSEGLGmgLSICRSIIEAHGGRLSVESPAGGGATFQFT 102
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
355-586 5.24e-05

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 45.61  E-value: 5.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 355 QPLNDEHRQLVNTLV-EQLTSVLAIERQVDHQQQLMLMEERAA-IArelHD------SIAQSLSCLKMQIAclqmqgetl 426
Cdd:COG3852   98 SPLRDAEGEGGVLLVlRDITERKRLERELRRAEKLAAVGELAAgLA---HEirnpltGIRGAAQLLERELP--------- 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 427 SSASQALVQQMREELNGAYRQLRELLTTFRLQLTEPGLL---AALQSTVAEFNPKLGLNISLDYQLGPRTVPAY------ 497
Cdd:COG3852  166 DDELREYTQLIIEEADRLNNLVDRLLSFSRPRPPEREPVnlhEVLERVLELLRAEAPKNIRIVRDYDPSLPEVLgdpdql 245
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 498 -QAI-HLLQIAREALSN----ILKHAAASEVSIQVINKRGEVTLSVCDNGRGLPAE----------TSRPDHYGL----- 556
Cdd:COG3852  246 iQVLlNLVRNAAEAMPEggtiTIRTRVERQVTLGGLRPRLYVRIEVIDNGPGIPEEildrifepffTTKEKGTGLglaiv 325
                        250       260       270
                 ....*....|....*....|....*....|..
gi 505191104 557 --IImrdraKSLHGRCDILPRSGGGTEVRVSF 586
Cdd:COG3852  326 qkIV-----EQHGGTIEVESEPGKGTTFRIYL 352
HATPase_EL346-LOV-HK-like cd16951
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
468-586 8.36e-05

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: 42.79  E-value: 8.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 468 LQSTVAEFNPKLGLNISLDYQLGPrtVPAYQAIHLLQIAREALSNILKHA---AAS---EVSIQVINKRGEVTlsVCDNG 541
Cdd:cd16951    8 IASAINAIHAVGDIRINITGDTGP--VSSEVATAIGLVVNELLQNALKHAfsdREGgtiTIRSVVDGDYLRIT--VIDDG 83
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 505191104 542 RGLPAETS--RPDHYGLIIMRDRAKSLHGRCDILPRSGGGTEVRVSF 586
Cdd:cd16951   84 VGLPQDEDwpNKGSLGLQIVRSLVEGELKAFLEVQSAENGTRVNIDI 130
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
435-586 1.57e-04

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 44.45  E-value: 1.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 435 QQMREELNGAYRQLRELLTTFRLQLTEPGLLAALQSTVAEFNPK-LGLNISLDYQLGPRTVPAYqaiHLLQIAREALSNI 513
Cdd:COG3290  217 DEALEYIDEISEELQELIDSLLSRIGNPVLAALLLGKAARARERgIDLTIDIDSDLPDLPLSDT---DLVTILGNLLDNA 293
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 514 LKHAAASE-----VSIQVINKRGEVTLSVCDNGRGLPAE----------TSRPDH---YGLIIMRDRAKSLHGRCDILPR 575
Cdd:COG3290  294 IEAVEKLPeeerrVELSIRDDGDELVIEVEDSGPGIPEEllekifergfSTKLGEgrgLGLALVKQIVEKYGGTIEVESE 373
                        170
                 ....*....|.
gi 505191104 576 SGGGTEVRVSF 586
Cdd:COG3290  374 EGEGTVFTVRL 384
HATPase_RsbW-like cd16936
Histidine kinase-like ATPase domain of RsbW, an anti sigma-B factor and serine-protein kinase ...
508-586 5.16e-04

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: 39.17  E-value: 5.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 508 EALSNILKHAAASEVSIQVI----NKRGEVTLSVCDNGRGLPAETSR-PDH------YGLIIMRDRAKSLHGRcdilpRS 576
Cdd:cd16936    7 EAVTNAVRHAYRHDGPGPVRleldLDPDRLRVEVTDSGPGFDPLRPAdPDAglreggRGLALIRALMDEVGYR-----RT 81
                         90
                 ....*....|
gi 505191104 577 GGGTEVRVSF 586
Cdd:cd16936   82 PGGKTVWLEL 91
PRK13560 PRK13560
hypothetical protein; Provisional
379-586 2.02e-03

hypothetical protein; Provisional


Pssm-ID: 106506 [Multi-domain]  Cd Length: 807  Bit Score: 41.20  E-value: 2.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 379 ERQVDHQQQLMLMEERAAIARELHDSIAQSL----SCLKMQIACLQMQG-ETLSSASQALVQQMREELNGAYRQLrellt 453
Cdd:PRK13560 590 ERKHAEEKIKAALTEKEVLLKEIHHRVKNNLqiisSLLDLQAEKLHDEEaKCAFAESQDRICAMALAHEKLYQSE----- 664
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104 454 tfrlQLTEPGLLAALQSTVAEFNPKLGLN---ISLDYQLGPRTVPAYQAIHLLQIAREALSNILKHA----AASEVSIQV 526
Cdd:PRK13560 665 ----DLADIDFLDYIESLTAHLKNSFAIDfgrIDCKIDADDGCLDIDKAIPCGLIISELLSNALKHAfpdgAAGNIKVEI 740
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505191104 527 INKR-GEVTLSVCDNGRGLPA--ETSRPDHYGLIIMRDRAKSLHGrcDILPRSGGGTEVRVSF 586
Cdd:PRK13560 741 REQGdGMVNLCVADDGIGLPAgfDFRAAETLGLQLVCALVKQLDG--EIALDSRGGARFNIRF 801
HATPase_LytS-like cd16957
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
494-547 3.29e-03

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis LytS and Staphylococcus aureus LytS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Bacillus subtilis LytS, a HK of the two-component system (TCS) LytS-LytR needed for growth on pyruvate, and Staphylococcus aureus LytS-LytR TCS involved in the adaptation of S. aureus to cationic antimicrobial peptides. Proteins having this HATPase domain also contain a histidine kinase domain (His-kinase), and a GAF sensor domain; most contain a DUF3816 domain.


Pssm-ID: 340433 [Multi-domain]  Cd Length: 106  Bit Score: 37.40  E-value: 3.29e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 505191104 494 VPAYqaihLLQIAREalsNILKHAAAS-----EVSIQVINKRGEVTLSVCDNGRGLPAE 547
Cdd:cd16957    1 VPPF----ALQVLVE---NAIRHAFPKrkennEVRVVVKKDQHKVHVSVSDNGQGIPEE 52
HATPase_c_2 pfam13581
Histidine kinase-like ATPase domain;
461-586 3.65e-03

Histidine kinase-like ATPase domain;


Pssm-ID: 433327 [Multi-domain]  Cd Length: 127  Bit Score: 37.65  E-value: 3.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104  461 EPGLLAALQSTVAEFNPKLGLnisldyqlgprtvPAYQAIHLLQIAREALSNILKHA----AASEVSIQVINKRGEVTLS 536
Cdd:pfam13581   4 DPEQLRAARRVLEAVLRRAGL-------------PEELLDEVELAVGEACTNAVEHAyregPEGPVEVRLTSDGGGLVVT 70
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505191104  537 VCDNGRGLPAETSRPDH------------YGLIIMRdrakSLHGRCDIlPRSGGGTEVRVSF 586
Cdd:pfam13581  71 VADSGPPFDPLTLPPPDleepdedrkeggRGLALIR----GLMDDVEY-TRGGEGNTVRMRK 127
chemoreceptor_sensor cd00181
4-helix bundle ligand binding sensor domain of chemoreceptors such as Tar or Tsr; The ligand ...
37-145 4.17e-03

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: 37.49  E-value: 4.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505191104  37 QSIQGNAHAINKAGSLRMQSYRLLAQVPL---DERHEALIRELERDENSPDLQRSVEQEGLTQP------FDTLRDYWQQ 107
Cdd:cd00181    1 QEIRQQASAISSLESLVLQARVTLRAEALtgvEELGDALIRALKQTAAVLAQFRALTRDPPEAEaeildkVQDYQKALAA 80
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 505191104 108 TLQprLRSAQRPADAAPQVAHFVQLLDKLVSDIDRQTE 145
Cdd:cd00181   81 LIP--ALLERGAESALFDQSEAQGGLELLLSLLQQLTA 116
 
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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