|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10935 |
PRK10935 |
nitrate/nitrite two-component system sensor histidine kinase NarQ; |
1-560 |
0e+00 |
|
nitrate/nitrite two-component system sensor histidine kinase NarQ;
Pssm-ID: 236800 [Multi-domain] Cd Length: 565 Bit Score: 843.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 1 MLVKRSVTGSLAKALFCIVILSVISTGLALTTVAGSLRDAEAVNIAGSLRMQSYRLAYDLTRQAAGLDQHLQQYQHSLQA 80
Cdd:PRK10935 1 MMVKRSVTSSIARAMLLIILLSSLTTGFALLTLASSLRDAEAINIAGSLRMQSYRLAYDLQSGSPQLNAHLREFEQSLHS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 81 PALQKLDRFYVPADVREKYLSLQQTWQRLARQIQAGQSADYQANVAGYVNQIDHFVLALQRYSELKLAIVATISVVGYIA 160
Cdd:PRK10935 81 PALKNLNRWYVPEDVKDRYALLIARWLEMKSYLEQGDSRWYQANIANYVDQIDLFVLALQHFAERKLILLAAISLLGLIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 161 IIGLVLFCIRFMRRQVVAPLKHLVDASQRVQQRDFHHPQLDVALPNELGVLSQAFAAMSDDLAKLYQSLELKVQEKTQRL 240
Cdd:PRK10935 161 ILTLVFFTVRFTRRQVVAPLNQLVTASQQIEKGQFDHIPLDTTLPNELGLLAKAFNQMSSELHKLYRSLEASVEEKTRKL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 241 QQANETLEVLYNCSQALSVRQIGRQAFEQVLHIVRQSEQLLCIRLNVADSlSEWQLTSGTPSPTQAWQRLTIVQDGKPLG 320
Cdd:PRK10935 241 TQANRSLEVLYQCSQALNASQIDVHCFRHILQIVRDHEGLDYLELEVGEN-EHWRISEGQPNPELPWQILPLTMEDTVLG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 321 ELCWQHQDQPPHPHLMQSVANMLSRGVYFNRAQKQHMQFLLMDERATIARELHDSLAQALSFLRIQLTLLKRTLAGGSPQ 400
Cdd:PRK10935 320 YLHWQASLPCPDEPLMNNVAQMLGRGLYFNQAQKQQQQLLLMEERATIARELHDSLAQVLSYLKIQLTLLKRSLDEDNAK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 401 AQEIINDFDRALADAYRQLRELLTTFRLNIQEADLNAALHQLLAPLKVLTGARIQLHCRLSSQALDAQQQVHALQIVREA 480
Cdd:PRK10935 400 AQSIIAEFDQALSDAYRQLRELLTTFRLTIQEANLGSALEEMLDQLRNQTDAKITLDCRLPSQALDAQQQVHLLQIIREA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 481 VVNAIKHADAREIVIRCEVTTGGDNAISIVDDGCGIASLSEPEGHYGLTIMSERAARLGGTLLIQRGNPKGTEVRLTFPP 560
Cdd:PRK10935 480 TLNAIKHANASEIAVSCVTNPDGEHTVSIRDDGIGIGELKEPEGHYGLNIMQERAERLGGTLTISQPPGGGTTVSLTFPS 559
|
|
| PRK10600 |
PRK10600 |
nitrate/nitrite two-component system sensor histidine kinase NarX; |
40-560 |
3.67e-89 |
|
nitrate/nitrite two-component system sensor histidine kinase NarX;
Pssm-ID: 182581 [Multi-domain] Cd Length: 569 Bit Score: 285.80 E-value: 3.67e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 40 AEAVNIAGSLRMQSYRLAydltrQAAGLDQHLQQYQHSLQAPALQ-KLDRFYVPADVREKYLSLQQTWQ-RLARQI-QAG 116
Cdd:PRK10600 15 AHAINKAGSLRMQSYRLL-----AAVPLSEKDKPLLKEMEQTAFSpELQRAAERDGQLAQLQALQDYWRnELKPALqQAQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 117 QSADYQANVAGYVNQIDHFVLALQRYSELKLAIVATISVVGYIAIIGLVLFCIRFMRRQVVAPLKHLVDASQRVQQRDFH 196
Cdd:PRK10600 90 NPEDVAADVAQFVAGLDALVSAFDHTTEMRIETVVLVHRVFAVFMALLLVFTIIWLRRRLLQPWRQLLSMANAVSHRDFT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 197 HpqlDVALP--NELGVLSQAFAAMSDDLAKLYQSLELKVQEKTQRLQQANETLEVLYNCSqalsvRQIGRQA--FEQVLH 272
Cdd:PRK10600 170 Q---RANISgrDEMAMLGTALNNMSAELAESYAVLEQRVQEKTAGLEQKNQILSFLWQAN-----RRLHSRAplCERLSP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 273 IVRQSEQLLCIR--------LNVADSLSEWQLTSGTPSPTQAWQR-----LTIVQDGKPLgelCWQHQDQ---------- 329
Cdd:PRK10600 242 VLNGLQNLTLLRdielrvyeTDDEENHQEFTCQSDMTCDDKGCQLcprgvLPVGDRGTTL---KWRLSDKhgqygillat 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 330 -PPHPHL---MQSVANML----SRGVYFNRAQKQHMQFLLMDERATIARELHDSLAQALSFLRIQLTLLKRTLAGGSPQA 401
Cdd:PRK10600 319 lPQGRHLshdQQQLVDTLveqlTATLALERQQERQQQLIVMEERATIARELHDSIAQSLSCMKMQVSCLQMQGDALPESS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 402 QEIINDFDRALADAYRQLRELLTTFRLNIQEADLNAALHQLLAPLKVLTGARIQLHCRLSSQALDAQQQVHALQIVREAV 481
Cdd:PRK10600 399 RELLSQIRNELNASWRQLRELLTTFRLQLTEPGLRPALEASCEEFSARFGFPVKLDYQLPPRLVPSHQAIHLLQIAREAL 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503579960 482 VNAIKHADAREIVIRCeVTTGGDNAISIVDDGCGIASLSEPEGHYGLTIMSERAARLGGTLLIQRGNPKGTEVRLTFPP 560
Cdd:PRK10600 479 SNALKHAQASEVVVTV-AQNQNQVKLSVQDNGCGVPENAERSNHYGLIIMRDRAQSLRGDCRVRRRESGGTEVVVTFIP 556
|
|
| NarQ_sensor |
cd22899 |
ligand binding sensor domain of NarQ, and related chemoreceptors; The periplasmic ligand ... |
34-149 |
9.11e-59 |
|
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: 191.19 E-value: 9.11e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 34 AGSLRDAEAVNIAGSLRMQSYRLAYDLTRQAAGLDQHLQQYQHSLQAPALQKLDRFYVPADVREKYLSLQQTWQRLARQI 113
Cdd:cd22899 1 ASSLSDAEAINVAGSLRMQSYRLAYDLESESPLLEQHIAQYEQSLHSPALQSLDRWYVPDEVKQRYQQLLARWQEMKQYL 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 503579960 114 QAGQSADYQANVAGYVNQIDHFVLALQRYSELKLAI 149
Cdd:cd22899 81 LQGDPASYLQQVASYVDQIDQFVLALQHFAERKLRL 116
|
|
| ComP |
COG4585 |
Signal transduction histidine kinase ComP [Signal transduction mechanisms]; |
351-559 |
1.44e-45 |
|
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
Pssm-ID: 443642 [Multi-domain] Cd Length: 252 Bit Score: 160.94 E-value: 1.44e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 351 RAQKQHMQFLLMDERATIARELHDSLAQALSFLRIQLTLLKRTLAGGSPQAQEIINDFDRALADAYRQLRELLTTFR-LN 429
Cdd:COG4585 40 RELAARAEEAREEERRRIARELHDGVGQSLSAIKLQLEAARRLLDADPEAAREELEEIRELAREALAELRRLVRGLRpPA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 430 IQEADLNAALHQLLAPLKVLTGARIQLHCRLSSQALDAQQQVHALQIVREAVVNAIKHADAREIVIRCEVtTGGDNAISI 509
Cdd:COG4585 120 LDDLGLAAALEELAERLLRAAGIRVELDVDGDPDRLPPEVELALYRIVQEALTNALKHAGATRVTVTLEV-DDGELTLTV 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 503579960 510 VDDGCGIASLSEPEGHYGLTIMSERAARLGGTLLIQRGNPKGTEVRLTFP 559
Cdd:COG4585 199 RDDGVGFDPEAAPGGGLGLRGMRERAEALGGTLTIGSAPGGGTRVRATLP 248
|
|
| HATPase_UhpB-NarQ-NarX-like |
cd16917 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
473-559 |
1.69e-24 |
|
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: 97.24 E-value: 1.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 473 ALQIVREAVVNAIKHADAREIVIRCEVTTGGDNaISIVDDGCGI-ASLSEPEGHYGLTIMSERAARLGGTLLIQRGNPKG 551
Cdd:cd16917 1 LYRIVQEALTNALKHAGASRVRVTLSYTADELT-LTVVDDGVGFdGPAPPGGGGFGLLGMRERAELLGGTLTIGSRPGGG 79
|
....*...
gi 503579960 552 TEVRLTFP 559
Cdd:cd16917 80 TRVTARLP 87
|
|
| NarX_NarQ_sensor |
cd19408 |
ligand binding sensor domain of NarX and NarQ, and related chemoreceptors; The periplasmic ... |
39-148 |
2.99e-24 |
|
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: 98.08 E-value: 2.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 39 DAEAVNIAGSLRMQSYRLAYDLTRQAAG----LDQHLQQYQHSLQAPALQKLDRFYVPADVREKYLSLQQTWQR------ 108
Cdd:cd19408 6 DAAAINLAGSLRMQSYRLASLLLQAALEpaeqLAQLIDEFEQRLNSPALTRALPRDSDHPLRQAYQAVLQHWQQelrpal 85
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 503579960 109 LARQIQAGQSADYQANVAGYVNQIDHFVLALQRYSELKLA 148
Cdd:cd19408 86 EAAASGAADREAYLAEVDEFVAQIDQLVKLLQQDTEAKIR 125
|
|
| UhpB |
COG3851 |
Signal transduction histidine kinase UhpB, glucose-6-phosphate specific [Signal transduction ... |
363-559 |
1.55e-20 |
|
Signal transduction histidine kinase UhpB, glucose-6-phosphate specific [Signal transduction mechanisms];
Pssm-ID: 443060 [Multi-domain] Cd Length: 493 Bit Score: 94.69 E-value: 1.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 363 DERATIARELHDSLAQALSFLRIQLTLLKRTLAGGSPQ--AQEIindfdRALAD-AYRQLRELLTTFR-LNIQEADLNAA 438
Cdd:COG3851 291 SERREIARELHDEIGQNITAIRTQASILKRLAPQPEIEqsAQSI-----ESLALrIYDTTRRLLDRLRpAVLDELGLEEA 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 439 LHQLLAPLKV-LTGARIQLHCRLSSQALDAQQQVHALQIVREAVVNAIKHADAREIVIRceVTTGGDNAI-SIVDDGCGI 516
Cdd:COG3851 366 LRELPRELAFeEPGISCQLDLRGDPSLLDDTLQLTLYRLVQEALTNILKHAEASQIRIS--LSQDKRLLSlEIRDDGIGL 443
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 503579960 517 ASlSEPEGHYGLTIMSERAARLGGTLLIQRGnPKGTEVRLTFP 559
Cdd:COG3851 444 PP-ELRAKGFGLRGMRERVRALGGDFRLSSA-PKGTRLSVLLP 484
|
|
| NtrY |
COG5000 |
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
143-559 |
1.72e-17 |
|
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: 85.01 E-value: 1.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 143 SELKLAIVATISVVGYIAIIGLVLFCIRFMRRqVVAPLKHLVDASQRVQQRDFhHPQLDVALPNELGVLSQAFAAMSDDL 222
Cdd:COG5000 1 SGLQILFLLLLLLIALLLLLLALWLALLLARR-LTRPLRRLAEATRAVAAGDL-SVRLPVTGDDEIGELARAFNRMTDQL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 223 AKLYQSLElkvqektqRLQQANETleVLYNCSQA-LSVRQIGR-----QAFEQVLHIVRQSeqllCIRLNVADSLSEWQL 296
Cdd:COG5000 79 KEQREELE--------ERRRYLET--ILENLPAGvIVLDADGRitlanPAAERLLGIPLEE----LIGKPLEELLPELDL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 297 TSG-TPSPTQAWQRLTIVQDGKPLgelcwqhqdqpphpHLMQSVANMLSRG--VYFnraqkQHMQFLLMDER-------- 365
Cdd:COG5000 145 AELlREALERGWQEEIELTRDGRR--------------TLLVRASPLRDDGyvIVF-----DDITELLRAERlaawgela 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 366 ATIARELHDSLAqalsflRIQLT--LLKRTLAGGSPQAQEiinDFDRALADAYRQ---LRELLTTFR-------LNIQEA 433
Cdd:COG5000 206 RRIAHEIKNPLT------PIQLSaeRLRRKLADKLEEDRE---DLERALDTIIRQvdrLKRIVDEFLdfarlpePQLEPV 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 434 DLNAALHQLLAPLKV-LTGARIQLHCRLSSQAL----DAQQ--QV-HALqivreaVVNAIKHADAR-EIVIRCEVtTGGD 504
Cdd:COG5000 277 DLNELLREVLALYEPaLKEKDIRLELDLDPDLPevlaDRDQleQVlINL------LKNAIEAIEEGgEIEVSTRR-EDGR 349
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503579960 505 NAISIVDDGCGIAS-----LSEP------EGH-YGLTIMSERAARLGGTLLIQRGNPKGTEVRLTFP 559
Cdd:COG5000 350 VRIEVSDNGPGIPEevlerIFEPffttkpKGTgLGLAIVKKIVEEHGGTIELESRPGGGTTFTIRLP 416
|
|
| PRK11644 |
PRK11644 |
signal transduction histidine-protein kinase/phosphatase UhpB; |
335-559 |
7.92e-16 |
|
signal transduction histidine-protein kinase/phosphatase UhpB;
Pssm-ID: 236945 [Multi-domain] Cd Length: 495 Bit Score: 80.02 E-value: 7.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 335 LMQSVANMLSRgvyfNRAQKQhmQFLLMDE--RATIARELHDSLAQALSFLRIQLTLLKR--TLAGGSPQAQEIINDFDR 410
Cdd:PRK11644 276 LNQSLQKELAR----NRHLAE--RLLETEEsvRRDVARELHDEIGQTITAIRTQAGIIKRlaADNASVKQSAQLIEQLSL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 411 ALADAYRQLRELLTTFRLNiqEADLNAALHQLLAPLKVL-TGARIQLHCRLSSQALDAQQQVHALQIVREAVVNAIKHAD 489
Cdd:PRK11644 350 GVYDTVRRLLGRLRPRQLD--DLTLEQAIRSLMREMELEdRGIVSHLDWRIDESALSETQRVTLFRVCQEGLNNIVKHAD 427
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503579960 490 AREIVIrcEVTTGGDNAI-SIVDDGCGIASLSEPEGhYGLTIMSERAARLGGTLLIQRGNpkGTEVRLTFP 559
Cdd:PRK11644 428 ASAVTL--QGWQQDERLMlVIEDDGSGLPPGSGQQG-FGLRGMRERVTALGGTLTISCTH--GTRLSVSLP 493
|
|
| HATPase_c |
pfam02518 |
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ... |
470-559 |
5.09e-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: 71.25 E-value: 5.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 470 QVHALQIVREAVVNAIKHA-DAREIVIRceVTTGGDNAISIVDDGCGI--------------ASLSEPEGH-YGLTIMSE 533
Cdd:pfam02518 3 ELRLRQVLSNLLDNALKHAaKAGEITVT--LSEGGELTLTVEDNGIGIppedlprifepfstADKRGGGGTgLGLSIVRK 80
|
90 100
....*....|....*....|....*.
gi 503579960 534 RAARLGGTLLIQRGNPKGTEVRLTFP 559
Cdd:pfam02518 81 LVELLGGTITVESEPGGGTTVTLTLP 106
|
|
| HATPase_c |
smart00387 |
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases. |
475-560 |
9.76e-15 |
|
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
Pssm-ID: 214643 [Multi-domain] Cd Length: 111 Bit Score: 70.37 E-value: 9.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 475 QIVREAVVNAIKHADAR-EIVIRCEvTTGGDNAISIVDDGCGIA----------------SLSEPEGH-YGLTIMSERAA 536
Cdd:smart00387 8 QVLSNLLDNAIKYTPEGgRITVTLE-RDGDHVEITVEDNGPGIPpedlekifepffrtdkRSRKIGGTgLGLSIVKKLVE 86
|
90 100
....*....|....*....|....
gi 503579960 537 RLGGTLLIQRGNPKGTEVRLTFPP 560
Cdd:smart00387 87 LHGGEISVESEPGGGTTFTITLPL 110
|
|
| PilJ |
pfam13675 |
Type IV pili methyl-accepting chemotaxis transducer N-term; This domain is found on many type ... |
32-126 |
7.93e-14 |
|
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: 67.89 E-value: 7.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 32 TVAGSLRDAEAVNIAGSLRMQSYRLAYDLTRQAAG----------LDQHLQQYQHSLQAPAL-QKLDRFYVPA-DVREKY 99
Cdd:pfam13675 2 TLWQSEGDAAAINAAGSLRMQSQRLAKSVLLALAGnydlaeafadLEESIDQFDRTLAALALgDLARGLFVPAgAIRAQL 81
|
90 100 110
....*....|....*....|....*....|.
gi 503579960 100 LSLQQTWQRLARQ----IQAGQSADYQANVA 126
Cdd:pfam13675 82 EAVQPLWERLRKPaeavLAQQDTLAYLAAVL 112
|
|
| HisKA_3 |
pfam07730 |
Histidine kinase; This is the dimerization and phosphoacceptor domain of a sub-family of ... |
364-427 |
1.27e-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: 65.72 E-value: 1.27e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503579960 364 ERATIARELHDSLAQALSFLRIQLTLLKRTLAGGSPQAQEIINDFDRALADAYRQLRELLTTFR 427
Cdd:pfam07730 1 ERNRIARELHDSVGQSLTAIKLQLELARRLLDRDPEEAREQLDAIRELAREALQELRRLLGDLR 64
|
|
| COG3920 |
COG3920 |
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ... |
351-559 |
3.11e-13 |
|
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction mechanisms];
Pssm-ID: 443125 [Multi-domain] Cd Length: 495 Bit Score: 72.25 E-value: 3.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 351 RAQKQHMQFLLMDERATIARELH----DSLAQALSFLRIQLtllkRTLagGSPQAQEIINDFD---RALADAYRQLREll 423
Cdd:COG3920 281 RKRAEEELEASLEEKELLLRELHhrvkNNLQVVSSLLRLQA----RRA--DDPEAREALEESQnriQALALVHELLYQ-- 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 424 ttfRLNIQEADLNAALHQLLAPLK-VLTGARIQLHCRLSSQALDAQQQVH-ALqIVREAVVNAIKHA--DAREIVIRCEV 499
Cdd:COG3920 353 ---SEDWEGVDLRDYLRELLEPLRdSYGGRGIRIELDGPDVELPADAAVPlGL-ILNELVTNALKHAflSGEGGRIRVSW 428
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503579960 500 TTGGDNA-ISIVDDGCGIASLSEPEGH--YGLTIMSERAARLGGTllIQRGNPKGTEVRLTFP 559
Cdd:COG3920 429 RREDGRLrLTVSDNGVGLPEDVDPPARkgLGLRLIRALVRQLGGT--LELDRPEGTRVRITFP 489
|
|
| NarX_sensor |
cd22900 |
ligand binding sensor domain of NarX, and related chemoreceptors; The periplasmic ligand ... |
40-151 |
7.85e-13 |
|
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: 65.28 E-value: 7.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 40 AEAVNIAGSLRMQSYRL--AYDLTRQAAGLDQHLQQYQHSLQapalqkLDRFYVPADVREKYLSLQQTWQ-RLARQI-QA 115
Cdd:cd22900 7 AHAINKAGSLRMQSYRLlaAVPLNPQDQALLDELEQTLSSPE------LQRAARREGLQSQLQALQQYWQqQLKPALlAA 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 503579960 116 GQSADYQANVAGYVNQIDHFVLALQRYSELKLAIVA 151
Cdd:cd22900 81 KNPEDARAEVAAFVAQLDQLVSQIDQKTEQRLSLIS 116
|
|
| BaeS |
COG0642 |
Signal transduction histidine kinase [Signal transduction mechanisms]; |
256-559 |
1.52e-09 |
|
Signal transduction histidine kinase [Signal transduction mechanisms];
Pssm-ID: 440407 [Multi-domain] Cd Length: 328 Bit Score: 59.54 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 256 ALSVRQIGRQAFEQVLHIVRQSEQLLCIRLNVADSLSEWQLTSGTPSPTQAWQRLTIVQDGKPLGELCWQHQDQPPHPHL 335
Cdd:COG0642 10 LLLLLLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLLLLLLLLLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 336 MQSVANMLSRGVYFNRAQKQHMQFLlmderATIArelHDsLAQALSFLRIQLTLLKRTLaggSPQAQEIINDFDRALADA 415
Cdd:COG0642 90 LLLLLLLLALLLLLEEANEAKSRFL-----ANVS---HE-LRTPLTAIRGYLELLLEEL---DEEQREYLETILRSADRL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 416 YRQLRELLT-------TFRLNIQEADLNAALHQLLAPLKVLTGAR-IQLHCRLSSQALDAQQQVHAL-QIVREAVVNAIK 486
Cdd:COG0642 158 LRLINDLLDlsrleagKLELEPEPVDLAELLEEVVELFRPLAEEKgIELELDLPDDLPTVRGDPDRLrQVLLNLLSNAIK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 487 HADA-REIVIRCEVTtGGDNAISIVDDGCGIAS-----LSEP------EGHY-----GLTIMSERAARLGGTLLIQRGNP 549
Cdd:COG0642 238 YTPEgGTVTVSVRRE-GDRVRISVEDTGPGIPPedlerIFEPffrtdpSRRGggtglGLAIVKRIVELHGGTIEVESEPG 316
|
330
....*....|
gi 503579960 550 KGTEVRLTFP 559
Cdd:COG0642 317 KGTTFTVTLP 326
|
|
| RsbW |
COG2172 |
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms]; |
452-559 |
3.64e-09 |
|
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
Pssm-ID: 441775 [Multi-domain] Cd Length: 127 Bit Score: 54.92 E-value: 3.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 452 ARIQLHCRLSSQALDAQQQVHALQIVREAVVNAIKHADAR----EIVIRCEVTtggDNAISIV--DDGCGIASL------ 519
Cdd:COG2172 14 ARRAVRALLRELGLDEDDADDLVLAVSEAVTNAVRHAYGGdpdgPVEVELELD---PDGLEIEvrDEGPGFDPEdlpdpy 90
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 503579960 520 -SEPEGHYGLTIMSERAARLGgtllIQRGnPKGTEVRLTFP 559
Cdd:COG2172 91 sTLAEGGRGLFLIRRLMDEVE----YESD-PGGTTVRLVKR 126
|
|
| KdpD |
COG2205 |
K+-sensing histidine kinase KdpD [Signal transduction mechanisms]; |
380-559 |
8.65e-09 |
|
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
Pssm-ID: 441807 [Multi-domain] Cd Length: 239 Bit Score: 56.45 E-value: 8.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 380 LSFLRIQLTLLKRTLAGGSPQAQEIINDFDRALADAYRQLRELLT-------TFRLNIQEADLNAALHQLLAPLKVLTGA 452
Cdd:COG2205 31 LTSILGAAELLLDEEDLSPEERRELLEIIRESAERLLRLIEDLLDlsrlesgKLSLELEPVDLAELLEEAVEELRPLAEE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 453 RiqlHCRLSSQALDAQQQVHA-----LQIVREAVVNAIKHADA-REIVIRCEVTtGGDNAISIVDDGCGI---------- 516
Cdd:COG2205 111 K---GIRLELDLPPELPLVYAdpellEQVLANLLDNAIKYSPPgGTITISARRE-GDGVRISVSDNGPGIpeeelerife 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 503579960 517 ----ASLSEPEGHYG--LTIMSERAARLGGTLLIQRGNPKGTEVRLTFP 559
Cdd:COG2205 187 rfyrGDNSRGEGGTGlgLAIVKRIVEAHGGTIWVESEPGGGTTFTVTLP 235
|
|
| NarQ |
COG3850 |
Signal transduction histidine kinase NarQ, nitrate/nitrite-specific [Signal transduction ... |
42-281 |
5.39e-07 |
|
Signal transduction histidine kinase NarQ, nitrate/nitrite-specific [Signal transduction mechanisms];
Pssm-ID: 443059 [Multi-domain] Cd Length: 448 Bit Score: 52.19 E-value: 5.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 42 AVNIAGSLRMQSYRLAYDLTRQAAGLDQHLQQYQHSLQAPALQKLDRFYVPADVREKYLSLQQTWQRLARQIQAGQSADY 121
Cdd:COG3850 8 ALALLRLLLALLALLLLALLLLSLLALLLLLERTLLRLLSLLASAGLLAALLAALLLLLSLGLLALLLALLLLLLLLLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 122 QANVAGYVNQIDHFVLALQRYSELKLAIVATISVVGYIAIIGLVLFCIRFMRRQVVAPLKHLVDASQRVQQRDFHHpQLD 201
Cdd:COG3850 88 ALLSLLLLLLLLLLLLLLLLLLLLAAAINRKLALLRLLLALLLALLLAYLLRRRIVRPLRRLTQAAERIARGDFDA-RVP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 202 VALPNELGVLSQAFAAMSDDLAKLYQSLELKVQEKTQRLQQANETLEVLYNCSQALSVRQIGRQAFEQVLHIVRQSEQLL 281
Cdd:COG3850 167 VSGRDELGTLARAFNRMADELQELYAELEEEEELEAELELLALLDELLLLAALLLLLALLLALLLAALLAALLLLLLLQD 246
|
|
| COG4191 |
COG4191 |
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ... |
366-559 |
1.99e-06 |
|
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal transduction mechanisms];
Pssm-ID: 443345 [Multi-domain] Cd Length: 361 Bit Score: 50.18 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 366 ATIArelHDsLAQALSFLRIQLTLLKRTLAGgSPQAQEIINDFDRALADAYR------QLRELLTTFRLNIQEADLNAAL 439
Cdd:COG4191 147 AGIA---HE-INNPLAAILGNAELLRRRLED-EPDPEELREALERILEGAERaaeivrSLRAFSRRDEEEREPVDLNELI 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 440 HQLLAPLKV-LTGARIQLHCRLSSQALDAQqqVHALQIvREAVVN-------AIKHADAREIVIRCEVttGGDNA-ISIV 510
Cdd:COG4191 222 DEALELLRPrLKARGIEVELDLPPDLPPVL--GDPGQL-EQVLLNllinaidAMEEGEGGRITISTRR--EGDYVvISVR 296
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503579960 511 DDGCGIAS-----LSEP------EGH---YGLTIMSERAARLGGTLLIQRGNPKGTEVRLTFP 559
Cdd:COG4191 297 DNGPGIPPevlerIFEPffttkpVGKgtgLGLSISYGIVEKHGGRIEVESEPGGGTTFTITLP 359
|
|
| HAMP |
pfam00672 |
HAMP domain; |
171-222 |
2.70e-06 |
|
HAMP domain;
Pssm-ID: 459898 [Multi-domain] Cd Length: 53 Bit Score: 44.54 E-value: 2.70e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 503579960 171 FMRRQVVAPLKHLVDASQRVQQRDFHHPqLDVALPNELGVLSQAFAAMSDDL 222
Cdd:pfam00672 1 LLARRILRPLRRLAEAARRIASGDLDVR-LPVSGRDEIGELARAFNQMAERL 51
|
|
| CitA |
COG3290 |
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ... |
412-559 |
3.10e-06 |
|
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction mechanisms];
Pssm-ID: 442519 [Multi-domain] Cd Length: 389 Bit Score: 49.46 E-value: 3.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 412 LADAYRQLRELLTTFRLNIQEADLNAALHQLLAplkVLTGARIQLHCRLSSQALDAQQQVHAL-QIVREAVVNAIKHA-- 488
Cdd:COG3290 223 IDEISEELQELIDSLLSRIGNPVLAALLLGKAA---RARERGIDLTIDIDSDLPDLPLSDTDLvTILGNLLDNAIEAVek 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 489 -DAREIVIRCEVT-TGGDNAISIVDDGCGIA------------SLSEPEGH-YGLTIMSERAARLGGTLLIQRGNPKGTE 553
Cdd:COG3290 300 lPEEERRVELSIRdDGDELVIEVEDSGPGIPeellekifergfSTKLGEGRgLGLALVKQIVEKYGGTIEVESEEGEGTV 379
|
....*.
gi 503579960 554 VRLTFP 559
Cdd:COG3290 380 FTVRLP 385
|
|
| HAMP |
cd06225 |
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; ... |
177-222 |
4.65e-06 |
|
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the 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: 43.59 E-value: 4.65e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 503579960 177 VAPLKHLVDASQRVQQRDFHHPqLDVALPNELGVLSQAFAAMSDDL 222
Cdd:cd06225 1 TRPLRRLTEAARRIAEGDLDVR-VPVRSKDEIGELARAFNQMAERL 45
|
|
| HATPase_EL346-LOV-HK-like |
cd16951 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
476-559 |
1.09e-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: 45.10 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 476 IVREAVVNAIKHA-DARE---IVIRCEVTTGGDNaISIVDDGCGIASLSEP--EGHYGLTIM-SERAARLGGTLLIQRGN 548
Cdd:cd16951 43 VVNELLQNALKHAfSDREggtITIRSVVDGDYLR-ITVIDDGVGLPQDEDWpnKGSLGLQIVrSLVEGELKAFLEVQSAE 121
|
90
....*....|.
gi 503579960 549 pKGTEVRLTFP 559
Cdd:cd16951 122 -NGTRVNIDIP 131
|
|
| WalK |
COG5002 |
Sensor histidine kinase WalK [Signal transduction mechanisms]; |
380-559 |
1.16e-05 |
|
Sensor histidine kinase WalK [Signal transduction mechanisms];
Pssm-ID: 444026 [Multi-domain] Cd Length: 390 Bit Score: 47.62 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 380 LSFLRIQLTLLKRTLAGGSPQAQEIIndfDRALADAYRQLR---ELLT-------TFRLNIQEADLNAALHQLLAPLKVL 449
Cdd:COG5002 180 LTSIRGYLELLLDGAADDPEERREYL---EIILEEAERLSRlvnDLLDlsrlesgELKLEKEPVDLAELLEEVVEELRPL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 450 TGAR-IQLHCRLSSQALdaqqQVHA-----LQIVREAVVNAIKHADA-REIVIRCEvTTGGDNAISIVDDGCGIA----- 517
Cdd:COG5002 257 AEEKgIELELDLPEDPL----LVLGdpdrlEQVLTNLLDNAIKYTPEgGTITVSLR-EEDDQVRISVRDTGIGIPeedlp 331
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 503579960 518 -----------SLSEPEGHY--GLTIMSERAARLGGTLLIQRGNPKGTEVRLTFP 559
Cdd:COG5002 332 riferfyrvdkSRSRETGGTglGLAIVKHIVEAHGGRIWVESEPGKGTTFTITLP 386
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
18-248 |
3.40e-05 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 46.55 E-value: 3.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 18 IVILSVISTGLALTTVAGSLRDAEAVNIAGSLRMQSYRLAYDLTRQAAGLDQHLQQYQHSLQAPALQKLDRFYVPADVRE 97
Cdd:COG0840 50 SLLALLLLLLLLALALLLVLLALLLLLALVVLLALLLALLLLLLALLALALAALALLAALAALLALLELLLAALLAALAI 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 98 KYLSLQQTWQRLARQIQAGQSADYQANVAGYVNQIDHFVLALQRYSELKLAIVATISVVGYIAIIGLVLfcIRFMRRQVV 177
Cdd:COG0840 130 ALLALAALLALAALALALLALALLAAAAAAAAALAALLEAAALALAAAALALALLAAALLALVALAIIL--ALLLSRSIT 207
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503579960 178 APLKHLVDASQRVQQRDFHHpQLDVALPNELGVLSQAFAAMSDDLaklyQSLELKVQEKTQRLQQANETLE 248
Cdd:COG0840 208 RPLRELLEVLERIAEGDLTV-RIDVDSKDEIGQLADAFNRMIENL----RELVGQVRESAEQVASASEELA 273
|
|
| HATPase_RsbW-like |
cd16936 |
Histidine kinase-like ATPase domain of RsbW, an anti sigma-B factor and serine-protein kinase ... |
476-558 |
4.97e-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: 42.26 E-value: 4.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 476 IVREAVVNAIKHA--DAREIVIRCEVTTGGDNA-ISIVDDGCGIA-------SLSEPEGHYGLTIMSERAARLGgtllIQ 545
Cdd:cd16936 4 AVSEAVTNAVRHAyrHDGPGPVRLELDLDPDRLrVEVTDSGPGFDplrpadpDAGLREGGRGLALIRALMDEVG----YR 79
|
90
....*....|...
gi 503579960 546 RGnPKGTEVRLTF 558
Cdd:cd16936 80 RT-PGGKTVWLEL 91
|
|
| YesM |
COG2972 |
Sensor histidine kinase YesM [Signal transduction mechanisms]; |
121-559 |
7.31e-05 |
|
Sensor histidine kinase YesM [Signal transduction mechanisms];
Pssm-ID: 442211 [Multi-domain] Cd Length: 445 Bit Score: 45.39 E-value: 7.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 121 YQANVAGYVNQIDHFVLALQRYSELKLAIVATISVVGYIAIIGLVL--FCIRFMRRQVVAPLKHLVDASQRVQQRDFHhp 198
Cdd:COG2972 124 LLLIILLLLSLLGWTLVSLIPKSELFRGLFSLRRLILLIILLLLLLalLLSYLLSRSITRPIKRLKKAMKKVEKGDLV-- 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 199 QLDVALPNELGVLSQAFAAMSDDLAKLyqslelkvQEKTQRLQQANETLEVLYNCSQalsvrqigrqafeqvlhivrqse 278
Cdd:COG2972 202 RLEVSGNDEIGILARSFNEMVERIKEL--------IEEVYELELEKKEAELKALQAQ----------------------- 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 279 qllcIRlnvadslsewqltsgtpsptqawqrltivqdgkplgelcwqhqdqpphPHLMQsvaNMLSRgvyfnraqkqhMQ 358
Cdd:COG2972 251 ----IN------------------------------------------------PHFLF---NTLNS-----------IR 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 359 FLLMDERATIARELHDSLAQalsFLRIQLTLLKRTlaggSPQAQEIindfdrALADAYrqlrellttfrLNIQeadlnaa 438
Cdd:COG2972 265 WLAELEDPEEAEEMLEALSK---LLRYSLSKGDEL----VTLEEEL------ELIKSY-----------LEIQ------- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 439 lhqllaplKVLTGARIQLHCRLSSQALDAQQQVHALQIVREavvNAIKHA-----DAREIVIRCEVTtGGDNAISIVDDG 513
Cdd:COG2972 314 --------KLRFGDRLEVEIEIDEELLDLLIPKLILQPLVE---NAIEHGiepkeGGGTIRISIRKE-GDRLVITVEDNG 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 514 CGI-----------ASLSEPEGHYGLTIMSERAARL---GGTLLIQRGNPKGTEVRLTFP 559
Cdd:COG2972 382 VGMpeekleklleeLSSKGEGRGIGLRNVRERLKLYygeEYGLEIESEPGEGTTVTIRIP 441
|
|
| LytS |
COG3275 |
Sensor histidine kinase, LytS/YehU family [Signal transduction mechanisms]; |
483-559 |
9.69e-05 |
|
Sensor histidine kinase, LytS/YehU family [Signal transduction mechanisms];
Pssm-ID: 442506 [Multi-domain] Cd Length: 352 Bit Score: 44.86 E-value: 9.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 483 NAIKHADAR-----EIVIRCEVtTGGDNAISIVDDGCGI-ASLSEPEGHYGLTIMSERAARLGG---TLLIQRGNPKGTE 553
Cdd:COG3275 264 NAIKHGISSkegggTISISIEV-EGDRLVIEVENNGVGIqPKKKKKGSGIGLKNVRERLELLYGdkySLEIESTDGGGTK 342
|
....*.
gi 503579960 554 VRLTFP 559
Cdd:COG3275 343 VTLKIP 348
|
|
| HAMP |
smart00304 |
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain; |
174-227 |
1.77e-04 |
|
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
Pssm-ID: 197640 [Multi-domain] Cd Length: 53 Bit Score: 39.54 E-value: 1.77e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 503579960 174 RQVVAPLKHLVDASQRVQQRDFHHPqLDVALPNELGVLSQAFAAMSDDLAKLYQ 227
Cdd:smart00304 1 RRLLRPLRRLAEAAQRIADGDLTVR-LPVDGRDEIGELARAFNEMADRLEETIA 53
|
|
| HAMP |
COG2770 |
HAMP domain [Signal transduction mechanisms]; |
18-493 |
3.99e-04 |
|
HAMP domain [Signal transduction mechanisms];
Pssm-ID: 442051 [Multi-domain] Cd Length: 631 Bit Score: 43.18 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 18 IVILSVISTGLALTTVAGSLRDAEAVNIAGSLRMQSYRLAYDLTRQAAGLDQHLQQYQHSLQAPALQKLDRFYVPADVRE 97
Cdd:COG2770 78 LLLLLSLVALAALLLALLLLLLLALLLLLAALLLLLLLAALALLLLLLLLLAALLALLLALALLALLLGLAAARLLLAAL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 98 KYLSLQQTWQRLARQIQAGQSADYQANVAGYVNQIDHFVLALQRYSELKLAIVATISVVGYIAIIGLVLFCIRFMRRQVV 177
Cdd:COG2770 158 LALAAALALALGAGELLLLADLAAAIAALLAALLLLLLGGLLLVVLLEAALAALLLLLLLALLALLLALLLALLLARRIT 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 178 APLKHLVDASQRVQQRDFHHPqLDVALPNELGVLSQAFAAMSDDLAKLYQSLELKVQEKTQRLQQANETLEVLYNCSQAL 257
Cdd:COG2770 238 RPLRRLAEAARRIAAGDLDVR-IPVSRKDEIGELARAFNRMADSLRESIEEAEEEEELAEAELARLLEALLELLLALLLL 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 258 SVRQIgRQAFEQVLHIVRQSEQLLCIRLNVADSLSEWQLTSGTPSPTQAWQRLTIVQDGKPLGELCWQHQDQPPHPHLMQ 337
Cdd:COG2770 317 LLALL-LLAAAALLLELLLLLLLALLLLLLLAADLLLALALAALLLLLALELLLEAELLVLLALEALALEAELAAVLALL 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 338 SVANMLSRGVYFNRAQKQHMQFLLMDERATIARELHDSLAQALSFLRIQLTLLKRTLAGGSPQAQEIINDFDRALADAYR 417
Cdd:COG2770 396 AALAAALLLLELALEELVLALLALALLALAAAAAAAEAAAAALELAAAAIAAAAAAEAEGGLAELEAEELVAAAEALLLL 475
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503579960 418 QLRELLTTFRLNIQEADLNAALHQLLAPLKVLTGARIQLHCRLSSQALDAQQQVHALQIVREAVVNAIKHADAREI 493
Cdd:COG2770 476 AALLLLAALGALELLLLEEEEEAGAAAEELAEELLLLEGLLLLLLLEAEALEVAEELLELEEAALLLAAAAELAAL 551
|
|
| KinA |
COG5805 |
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ... |
475-559 |
1.43e-03 |
|
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: 41.26 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 475 QIvREAVVNAIKHA-----DAREIVIRCEvTTGGDNAISIVDDGCGI-----ASLSEP-----EGHYGLTIM-SER-AAR 537
Cdd:COG5805 395 QI-KQVFINLIKNAieampNGGTITIHTE-EEDNSVIIRVIDEGIGIpeerlKKLGEPffttkEKGTGLGLMvSYKiIEN 472
|
90 100
....*....|....*....|..
gi 503579960 538 LGGTLLIQRGNPKGTEVRLTFP 559
Cdd:COG5805 473 HNGTIDIDSKVGKGTTFTITLP 494
|
|
| HATPase_MutL-MLH-PMS-like |
cd16926 |
Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, ... |
476-516 |
3.02e-03 |
|
Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, human MutL homologs (MLH/ PMS), and related domains; This family includes the histidine kinase-like ATPase (HATPase) domains of Escherichia coli MutL, human MLH1 (mutL homolog 1), human PMS1 (PMS1 homolog 1, mismatch repair system component), human MLH3 (mutL homolog 3), and human PMS2 (PMS1 homolog 2, mismatch repair system component). MutL homologs (MLH/PMS) participate in MMR (DNA mismatch repair), and in addition have role(s) in DNA damage signaling and suppression of homologous recombination (recombination between partially homologous parental DNAs). The primary role of MutL in MMR is to mediate protein-protein interactions during mismatch recognition and strand removal; a ternary complex is formed between MutS, MutL, and the mismatched DNA, which activates the MutH endonuclease.
Pssm-ID: 340403 [Multi-domain] Cd Length: 188 Bit Score: 38.96 E-value: 3.02e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 503579960 476 IVREAVVNAIKhADAREIVIrcEVTTGGDNAISIVDDGCGI 516
Cdd:cd16926 17 VVKELVENSID-AGATRIDV--EIEEGGLKLIRVTDNGSGI 54
|
|
| mutl |
TIGR00585 |
DNA mismatch repair protein MutL; All proteins in this family for which the functions are ... |
476-516 |
3.46e-03 |
|
DNA mismatch repair protein MutL; All proteins in this family for which the functions are known are involved in the process of generalized mismatch repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273155 [Multi-domain] Cd Length: 312 Bit Score: 39.55 E-value: 3.46e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 503579960 476 IVREAVVNAIKhADAREIVIrcEVTTGGDNAISIVDDGCGI 516
Cdd:TIGR00585 26 VVKELVENSLD-AGATRIDV--EIEEGGLKLIEVSDNGSGI 63
|
|
| PRK15347 |
PRK15347 |
two component system sensor kinase; |
160-243 |
5.57e-03 |
|
two component system sensor kinase;
Pssm-ID: 237951 [Multi-domain] Cd Length: 921 Bit Score: 39.63 E-value: 5.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 160 AIIGLVLFCIRF---MRRQVVAPLKHLVDASQRVQQrdfhhPQLDVALP----NELGVLSQAFAAMSDDLAKLYQSLELK 232
Cdd:PRK15347 302 ALLILVLLTSVLfllLRRYLAKPLWRFVDIINKTGP-----AALEPRLPenrlDELGSIAKAYNQLLDTLNEQYDTLENK 376
|
90
....*....|.
gi 503579960 233 VQEKTQRLQQA 243
Cdd:PRK15347 377 VAERTQALAEA 387
|
|
| PRK11100 |
PRK11100 |
sensory histidine kinase CreC; Provisional |
431-559 |
6.22e-03 |
|
sensory histidine kinase CreC; Provisional
Pssm-ID: 236846 [Multi-domain] Cd Length: 475 Bit Score: 39.44 E-value: 6.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503579960 431 QEADLNAALHQLLAPLKV-LTGARIQLHCRLSSQALDAQQQvhalqIVREAVVNAIKHA-----DAREIVIRCEvTTGGD 504
Cdd:PRK11100 327 EPVALAALLEELVEAREAqAAAKGITLRLRPDDARVLGDPF-----LLRQALGNLLDNAidfspEGGTITLSAE-VDGEQ 400
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503579960 505 NAISIVDDGCGIA------------SLSEPEGH-----YGLTIMSERAARLGGTLLIQRGNPKGTEVRLTFP 559
Cdd:PRK11100 401 VALSVEDQGPGIPdyalpriferfySLPRPANGrkstgLGLAFVREVARLHGGEVTLRNRPEGGVLATLTLP 472
|
|
| |
