|
Name |
Accession |
Description |
Interval |
E-value |
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
228-571 |
1.62e-68 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 225.50 E-value: 1.62e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 228 ALKERERELRLIVDTVPALIYLVGSDGVPSYMNRRIQDYYGIAFDKLpqvdgaqVRAALEARVHPDDEpaVAAALKHAYA 307
Cdd:COG3852 1 ALRESEELLRAILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEEL-------LGRPLAELFPEDSP--LRELLERALA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 308 TGEPFALR-YRNYTADGVPRWVDGRVQPLRDDTGRVerwyGLVIdvedEVRAQENLRAAQRKLARASQLASLAELSASIA 386
Cdd:COG3852 72 EGQPVTEReVTLRRKDGEERPVDVSVSPLRDAEGEG----GVLL----VLRDITERKRLERELRRAEKLAAVGELAAGLA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 387 HEVRQPLAAVVSNSQacqrwLSSQSLDLGRIRAIMDRIVRDANAAAATVTSVRALYANTATSRVSIDVNAVVEEARLLLA 466
Cdd:COG3852 144 HEIRNPLTGIRGAAQ-----LLERELPDDELREYTQLIIEEADRLNNLVDRLLSFSRPRPPEREPVNLHEVLERVLELLR 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 467 DDLSKAATtFRAELDPDLPPVLADRIQIQQVLVNLVRNAMEAMRAN----IETARVIVVRSRGA--DGQVQVEVADTGSG 540
Cdd:COG3852 219 AEAPKNIR-IVRDYDPSLPEVLGDPDQLIQVLLNLVRNAAEAMPEGgtitIRTRVERQVTLGGLrpRLYVRIEVIDNGPG 297
|
330 340 350
....*....|....*....|....*....|...
gi 1720335109 541 IAEPAL--IFEPLFTTKARGMGLGLAVSRSILE 571
Cdd:COG3852 298 IPEEILdrIFEPFFTTKEKGTGLGLAIVQKIVE 330
|
|
| COG4191 |
COG4191 |
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ... |
258-571 |
1.36e-67 |
|
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal transduction mechanisms];
Pssm-ID: 443345 [Multi-domain] Cd Length: 361 Bit Score: 223.14 E-value: 1.36e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 258 YMNRRIQDYYGIAFDKLPQVDGAQVRAALEARVHPDDEPAVAAALKHAYATGEPFALRYRNYTADGVPRWVDGRVQPLRD 337
Cdd:COG4191 22 LALLLLLLLLLLALLLLLLALLLALLALLLLLLLLLLLLLLELLLLLLALLGGLLRLLLLLGLLLLLLLEALLLLLLAAL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 338 DTGRVERWYGLVIDVEDEVRAQENLRAAQRKLARASQLASLAELSASIAHEVRQPLAAVVSNSQACQRWLSsQSLDLGRI 417
Cdd:COG4191 102 DAEENAELEELERDITELERAEEELRELQEQLVQSEKLAALGELAAGIAHEINNPLAAILGNAELLRRRLE-DEPDPEEL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 418 RAIMDRIVRDANAAAATVTSVRALYANTATSRVSIDVNAVVEEARLLLADDLSKAATTFRAELDPDLPPVLADRIQIQQV 497
Cdd:COG4191 181 REALERILEGAERAAEIVRSLRAFSRRDEEEREPVDLNELIDEALELLRPRLKARGIEVELDLPPDLPPVLGDPGQLEQV 260
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720335109 498 LVNLVRNAMEAMRANIEtaRVIVVRSRGADGQVQVEVADTGSGIAEPAL--IFEPLFTTKA--RGMGLGLAVSRSILE 571
Cdd:COG4191 261 LLNLLINAIDAMEEGEG--GRITISTRREGDYVVISVRDNGPGIPPEVLerIFEPFFTTKPvgKGTGLGLSISYGIVE 336
|
|
| KinA |
COG5805 |
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ... |
113-571 |
4.21e-60 |
|
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: 207.28 E-value: 4.21e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 113 LIDALPTLVWSTDADGTVTFVNQRWRTYTGLSREEAAEGGWIDAVHPEDRDRLLAYWQALRGAGTPGEIEGRlRRADGHY 192
Cdd:COG5805 39 ILENLPDAIIAVNREGKVIYINPAMEKLLGYTSEEIIGKTIFDFLEKEYHYRVKTRIERLQKGYDVVMIEQI-YCKDGEL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 193 RWFLFRGEPFRDAAGAVVQWfgSTTDIHAGRLVREALKERERELRLIVDTVPALIYLVGSDGVPSYMNRRIQDYYGIAFD 272
Cdd:COG5805 118 IYVEVKLFPIYNQNGQAAIL--ALRDITKKKKIEEILQEQEERLQTLIENSPDLICVIDTDGRILFINESIERLFGAPRE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 273 KLpqvdgaqVRAALEARVHPDDEPAVAAALKHAYATGEPFALRYRNYTADGVPRWVDGRVQPLRDDTGRVERWYGLVIDV 352
Cdd:COG5805 196 EL-------IGKNLLELLHPCDKEEFKERIESITEVWQEFIIEREIITKDGRIRYFEAVIVPLIDTDGSVKGILVILRDI 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 353 EDEVRAQENLRaaqrklaRASQLASLAELSASIAHEVRQPLAAV------VSNSQACQRWLSSQSLD-LGRIRAImdriv 425
Cdd:COG5805 269 TEKKEAEELMA-------RSEKLSIAGQLAAGIAHEIRNPLTSIkgflqlLQPGIEDKEEYFDIMLSeLDRIESI----- 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 426 rdanaaaatVTSVRALYANTATSRVSIDVNAVVEEARLLLADDLSKAATTFRAELDPDLPPVLADRIQIQQVLVNLVRNA 505
Cdd:COG5805 337 ---------ISEFLALAKPQAVNKEKENINELIQDVVTLLETEAILHNIQIRLELLDEDPFIYCDENQIKQVFINLIKNA 407
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720335109 506 MEAMraniETARVIVVRSRGADGQVQVEVADTGSGIAEPAL--IFEPLFTTKARGMGLGLAVSRSILE 571
Cdd:COG5805 408 IEAM----PNGGTITIHTEEEDNSVIIRVIDEGIGIPEERLkkLGEPFFTTKEKGTGLGLMVSYKIIE 471
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
118-571 |
8.43e-54 |
|
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 444511 [Multi-domain] Cd Length: 489 Bit Score: 190.19 E-value: 8.43e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 118 PTLVWstDADGTVTFVNQRWRTYTGLSREEAAEGGWIDAVHPEDRDRLLAYWQALRGAGTPGEIEGRLRRADGHYRWFLF 197
Cdd:COG5809 27 AILIL--DLEGKILKVNPAAERIFGYTEDELLGTNILDFLHPDDEKELREILKLLKEGESRDELEFELRHKNGKRLEFSS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 198 RGEPFRDAAGAVVQWFGSTTDIHAGRLVREALKERERELRLIVDTVPALIYLVGSDGVPSYMNRRIQDYYGIAFDKLpqv 277
Cdd:COG5809 105 KLSPIFDQNGDIEGMLAISRDITERKRMEEALRESEEKFRLIFNHSPDGIIVTDLDGRIIYANPAACKLLGISIEEL--- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 278 dgaqVRAALEARVHPDDEPAVAAALKHAYATGEPFALRYRNYTADGVPRWVDGRVQPLrDDTGRVERWYGLVIDVEDEVR 357
Cdd:COG5809 182 ----IGKSILELIHSDDQENVAAFISQLLKDGGIAQGEVRFWTKDGRWRLLEASGAPI-KKNGEVDGIVIIFRDITERKK 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 358 AQENLRAAQrKLARASQLAslaelsASIAHEVRQPLAAVVSNSQACQ-RWLSSQSLDLGRIRAIMDRIvrdanaaAATVT 436
Cdd:COG5809 257 LEELLRKSE-KLSVVGELA------AGIAHEIRNPLTSLKGFIQLLKdTIDEEQKTYLDIMLSELDRI-------ESIIS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 437 SVRALYANTATSRVSIDVNAVVEE-ARLLLADDLSKaATTFRAELDPDLPPVLADRIQIQQVLVNLVRNAMEAMRANIEt 515
Cdd:COG5809 323 EFLVLAKPQAIKYEPKDLNTLIEEvIPLLQPQALLK-NVQIELELEDDIPDILGDENQLKQVFINLLKNAIEAMPEGGN- 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720335109 516 arVIVVRSRGADGQVQVEVADTGSGIAEPAL--IFEPLFTTKARGMGLGLAVSRSILE 571
Cdd:COG5809 401 --ITIETKAEDDDKVVISVTDEGCGIPEERLkkLGEPFYTTKEKGTGLGLMVSYKIIE 456
|
|
| NtrY |
COG5000 |
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
226-571 |
2.79e-53 |
|
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: 187.09 E-value: 2.79e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 226 REALKERERELRLIVDTVPALIYLVGSDGVPSYMNRriqdyygiAFDKLPQVDGAQVRAALEARVHPddEPAVAAALKHA 305
Cdd:COG5000 82 REELEERRRYLETILENLPAGVIVLDADGRITLANP--------AAERLLGIPLEELIGKPLEELLP--ELDLAELLREA 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 306 YATGEPFALRYRNytadGVPRWVDGRVQPLRDDtgrverwyGLVI---DVEDEVRAQEnlraaqrklarasqLASLAELS 382
Cdd:COG5000 152 LERGWQEEIELTR----DGRRTLLVRASPLRDD--------GYVIvfdDITELLRAER--------------LAAWGELA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 383 ASIAHEVRQPLAAVVSNSQACQR-WLSSQSLDLGRIRAIMDRIVRDANAAAATVTSVRALYANTATSRVSIDVNAVVEEA 461
Cdd:COG5000 206 RRIAHEIKNPLTPIQLSAERLRRkLADKLEEDREDLERALDTIIRQVDRLKRIVDEFLDFARLPEPQLEPVDLNELLREV 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 462 RLLLADDLSKAATTFRAELDPDLPPVLADRIQIQQVLVNLVRNAMEAMRANIEtarvIVVRSRGADGQVQVEVADTGSGI 541
Cdd:COG5000 286 LALYEPALKEKDIRLELDLDPDLPEVLADRDQLEQVLINLLKNAIEAIEEGGE----IEVSTRREDGRVRIEVSDNGPGI 361
|
330 340 350
....*....|....*....|....*....|..
gi 1720335109 542 AEPAL--IFEPLFTTKARGMGLGLAVSRSILE 571
Cdd:COG5000 362 PEEVLerIFEPFFTTKPKGTGLGLAIVKKIVE 393
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
101-362 |
1.42e-40 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 147.86 E-value: 1.42e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 101 EQALHAQLYQQQLIDALPTLVWSTDADGTVTFVNQRWRTYTGLSREEAAEGGWIDAVHPEDRDRLLAYWQALRGAGTPGE 180
Cdd:COG2202 4 EALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVWR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 181 IEGRLRRADGHYRWFLFRGEPFRDAAGAVVQWFGSTTDIHAGRLVREALKERERELRLIVDTVPALIYLVGSDGVPSYMN 260
Cdd:COG2202 84 GELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEERLRLLVENAPDGIFVLDLDGRILYVN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 261 RRIQDYYGIAFDKLpqvdgaqVRAALEARVHPDDEPAVAAALKHAYATG-EPFALRYRNYTADGVPRWVDGRVQPLRDDt 339
Cdd:COG2202 164 PAAEELLGYSPEEL-------LGKSLLDLLHPEDRERLLELLRRLLEGGrESYELELRLKDGDGRWVWVEASAVPLRDG- 235
|
250 260
....*....|....*....|...
gi 1720335109 340 GRVERWYGLVIDVEDEVRAQENL 362
Cdd:COG2202 236 GEVIGVLGIVRDITERKRAEEAL 258
|
|
| PRK11360 |
PRK11360 |
two-component system sensor histidine kinase AtoS; |
363-571 |
4.71e-36 |
|
two-component system sensor histidine kinase AtoS;
Pssm-ID: 236901 [Multi-domain] Cd Length: 607 Bit Score: 142.41 E-value: 4.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 363 RAAQRKLARASQLASLAELSASIAHEVRQPLAAV---VSNSQAC------QRWLSSQSLDLGRIRAIMDRIVRDANAAAA 433
Cdd:PRK11360 375 KRLQRRVARQERLAALGELVAGVAHEIRNPLTAIrgyVQIWRQQtsdppsQEYLSVVLREVDRLNKVIDQLLEFSRPRES 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 434 TVTSVralyantatsrvsiDVNAVVEEARLLLADDLSKAATTFRAELDPDLPPVLADRIQIQQVLVNLVRNAMEAMRANI 513
Cdd:PRK11360 455 QWQPV--------------SLNALVEEVLQLFQTAGVQARVDFETELDNELPPIWADPELLKQVLLNILINAVQAISARG 520
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720335109 514 EtarvIVVR-SRGADGQVQVEVADTGSGIAEPAL--IFEPLFTTKARGMGLGLAVSRSILE 571
Cdd:PRK11360 521 K----IRIRtWQYSDGQVAVSIEDNGCGIDPELLkkIFDPFFTTKAKGTGLGLALSQRIIN 577
|
|
| KdpD |
COG2205 |
K+-sensing histidine kinase KdpD [Signal transduction mechanisms]; |
362-571 |
4.62e-34 |
|
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
Pssm-ID: 441807 [Multi-domain] Cd Length: 239 Bit Score: 129.26 E-value: 4.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 362 LRAAQRKLARASQLASlaELSASIAHEVRQPLAAVVSnsqACQRWLSSQSLDLGRIRAIMDRIVRDANAAAATVTSV--- 438
Cdd:COG2205 2 LEEALEELEELERLKS--EFLANVSHELRTPLTSILG---AAELLLDEEDLSPEERRELLEIIRESAERLLRLIEDLldl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 439 -RALYANTATSRVSIDVNAVVEEARLLLADDLSKAATTFRAELDPDLPPVLADRIQIQQVLVNLVRNAMEAMRANIEtar 517
Cdd:COG2205 77 sRLESGKLSLELEPVDLAELLEEAVEELRPLAEEKGIRLELDLPPELPLVYADPELLEQVLANLLDNAIKYSPPGGT--- 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 518 vIVVRSRGADGQVQVEVADTGSGIAEPAL--IFEPLF----TTKARGMGLGLAVSRSILE 571
Cdd:COG2205 154 -ITISARREGDGVRISVSDNGPGIPEEELerIFERFYrgdnSRGEGGTGLGLAIVKRIVE 212
|
|
| BaeS |
COG0642 |
Signal transduction histidine kinase [Signal transduction mechanisms]; |
280-571 |
7.49e-33 |
|
Signal transduction histidine kinase [Signal transduction mechanisms];
Pssm-ID: 440407 [Multi-domain] Cd Length: 328 Bit Score: 128.49 E-value: 7.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 280 AQVRAALEARVHPDDEPAVAAALKHAYATGEPFALRYRNYTADGVPRWVDGRVQPLRDDTGRVERWYGLVIDVEDEVRAQ 359
Cdd:COG0642 13 LLLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 360 ENLRAAQRKLARASQlASLAELSASIAHEVRQPLAAVVSNSQACQRWLSSQsldlgrIRAIMDRIVRDANAAAATVTSVR 439
Cdd:COG0642 93 LLLLLALLLLLEEAN-EAKSRFLANVSHELRTPLTAIRGYLELLLEELDEE------QREYLETILRSADRLLRLINDLL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 440 ALY----ANTATSRVSIDVNAVVEEARLLLADDLSKAATTFRAELDPDLPPVLADRIQIQQVLVNLVRNAMEAMRANiet 515
Cdd:COG0642 166 DLSrleaGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDDLPTVRGDPDRLRQVLLNLLSNAIKYTPEG--- 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720335109 516 aRVIVVRSRGADGQVQVEVADTGSGIAEPAL--IFEPLFTTKA----RGMGLGLAVSRSILE 571
Cdd:COG0642 243 -GTVTVSVRREGDRVRISVEDTGPGIPPEDLerIFEPFFRTDPsrrgGGTGLGLAIVKRIVE 303
|
|
| KinC |
COG5807 |
Sporulation sensor histidine kinase C [Cell cycle control, cell division, chromosome ... |
229-571 |
5.64e-31 |
|
Sporulation sensor histidine kinase C [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 444509 [Multi-domain] Cd Length: 358 Bit Score: 123.74 E-value: 5.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 229 LKERERELRLIVDTVPALIYLVGSDGVPSYMNRRIQDYYGIAFDKLPQVDGAQVRAALEARVHPDDEPAVAAALKHAYAT 308
Cdd:COG5807 22 TEDSEFKFKQLFDSILEFVFFIDSKGEILECNDFAEDLYGLSQNEYIGKTFVEEKCILKDEQLYNKEAFDRIEISYLTKN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 309 GEPFALRYRNYTADGVprwVDGRVQPLRDDTGRVErwyglvidvedevraqenlraAQRKLARASQLASLAELSASIAHE 388
Cdd:COG5807 102 GEFDEIIYPIYYKDGV---ILGLITVYRDITKRKE---------------------AEDKLLRSEKLSVAGELAAGIAHE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 389 VRQPLAAVVSNSQacqrwLSSQSLDLGRIRAIMDRIVRDANAAAATVTSVRALYANTATSRVSIDVNAVVEEARLLLADD 468
Cdd:COG5807 158 IRNPLTSIKGFLQ-----LLQESREDSEREEYFNIIISEIDRINTIITELLVLSKPKKFNFKKLNLNDVLEDVIALLSTE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 469 LSKAATTFRAELDPDLPPVLADRIQIQQVLVNLVRNAMEAMraniETARVIVVRSRGADGQVQVEVADTGSGIAEPAL-- 546
Cdd:COG5807 233 AILKNISIKYDLADDEPVINGDKNQLKQVFINLIKNAIEAM----ETGGNITIKTYVEGDFVVISVKDEGIGIPEEVLek 308
|
330 340
....*....|....*....|....*
gi 1720335109 547 IFEPLFTTKARGMGLGLAVSRSILE 571
Cdd:COG5807 309 IGEPFFTTKEEGTGLGLSICKKIIE 333
|
|
| COG4251 |
COG4251 |
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ... |
94-571 |
2.30e-27 |
|
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal transduction mechanisms];
Pssm-ID: 443393 [Multi-domain] Cd Length: 503 Bit Score: 115.65 E-value: 2.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 94 RAEMAVVEQALHAQLYQQQLIDALPTLVWSTDADGTVTFVNQRWRTYTGLSREEAAEGgwIDAVHPEDRDRLLAYWQALR 173
Cdd:COG4251 1 LLLLALLLLLLLLLLLLLLLLLLLLLVLLLALALLLLLALLVLLLLLIRLLLLLLLSL--LALLLLLLLLLLLLLVLAAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 174 GAGTPGEIEGRLRRADGHYRWFLFRGEPFRDAAGAVVQWFGSTTDIHAGRLVREALKERERELRLIVDTVPALIYLVGSD 253
Cdd:COG4251 79 ALLLLLLLLELALVLLALLLVLLLLLALLLLLALLLLLELLLLLLALLLLLLLLALLLLEELALLRLALALLLLLLLLLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 254 GVPSYMNRRIQDYYGIAFDKLPQVDGAQVRAALEARVHPDDEPAVAAALKHAYATGEPFALRYRNYTADGVPRWVDGRVQ 333
Cdd:COG4251 159 LLLLLLALILALLLAALAELELLLLLLLVLLLLLLLLLLLLLLLLRLLLELLLLLEAELLLSLGGGLGLLLLLLLLLVLL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 334 PLRDDTGRVERWYGLVIDVEDEV-RAQENLRAAQRKLARASQlaSLAELSASIAHEVRQPLAAVVSNSQACQRWLSSQsL 412
Cdd:COG4251 239 LLLILLLLLLILVLELLELRLELeELEEELEERTAELERSNE--ELEQFAYVASHDLREPLRKISGFSQLLEEDYGDK-L 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 413 DlGRIRAIMDRIVRDANAAAATVTSVRALY--ANTATSRVSIDVNAVVEEARLLLADDLSKAATTFRAEldpDLPPVLAD 490
Cdd:COG4251 316 D-EEGREYLERIRDAAERMQALIDDLLAYSrvGRQELEFEPVDLNELLEEVLEDLEPRIEERGAEIEVG---PLPTVRGD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 491 RIQIQQVLVNLVRNAMEAMRANIETarVIVVRSRGADGQVQVEVADTGSGIAEPAL--IFEPLFTTKAR----GMGLGLA 564
Cdd:COG4251 392 PTLLRQVFQNLISNAIKYSRPGEPP--RIEIGAEREGGEWVFSVRDNGIGIDPEYAekIFEIFQRLHSRdeyeGTGIGLA 469
|
....*..
gi 1720335109 565 VSRSILE 571
Cdd:COG4251 470 IVKKIVE 476
|
|
| COG4192 |
COG4192 |
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ... |
352-571 |
3.00e-26 |
|
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal transduction mechanisms];
Pssm-ID: 443346 [Multi-domain] Cd Length: 640 Bit Score: 113.24 E-value: 3.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 352 VEDEVRAQENLRAAQRKLARASQLASLAELSASIAHEVRQPLAAVVSNSQACQRWLSSQSLDlgRIRAIMDRIVRDANAA 431
Cdd:COG4192 407 IEERKRIEKNLRQTQDELIQAAKMAVVGQTMTSLAHELNQPLNAMSMYLFSAKKALEQENYA--QLPTSLDKIEGLIERM 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 432 AATVTSVRALYANTATSRVSIDVNAVVEEARLLLAddlSKAATTFRAELDPDLPPVLADRIQIQQVLVNLVRNAMEAMra 511
Cdd:COG4192 485 DKIIKSLRQFSRKSDTPLQPVDLRQVIEQAWELVE---SRAKPQQITLHIPDDLMVQGDQVLLEQVLVNLLVNALDAV-- 559
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 512 niETARVIVVRSRGADGQVQVEVADTGSGIAEPALIFEPLFTTKARGMGLGLAVSRSILE 571
Cdd:COG4192 560 --ATQPQISVDLLSNAENLRVAISDNGNGWPLVDKLFTPFTTTKEVGLGLGLSICRSIMQ 617
|
|
| WalK |
COG5002 |
Sensor histidine kinase WalK [Signal transduction mechanisms]; |
223-571 |
1.66e-25 |
|
Sensor histidine kinase WalK [Signal transduction mechanisms];
Pssm-ID: 444026 [Multi-domain] Cd Length: 390 Bit Score: 108.49 E-value: 1.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 223 RLVREALKERERELRLIVDTVPALIYLVGSDGVPSYMNRRIQDYYGIAFDKLPQVDGAQVRAALEARVHPDDEPAVAAAL 302
Cdd:COG5002 9 LALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLLLLLLLLLLLLALLLLLLLLLLLLALALLLLAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 303 KHAYATGEPFALRYRNYTADGVPRWVDGRVQPLRDDTGRVERWYGLVIDVEDEVRAQENLRAAQRKLARASQL-ASLAEL 381
Cdd:COG5002 89 LLLLLLLLLLLALLILLLLLALLILLAALLLLLSELLLLLLLLGRLSLRLSALLLGLLLLAAVERDITELERLeQMRREF 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 382 SASIAHEVRQPLAAVVSNSQACQRWLSSqslDLGRIRAIMDRIVRDANAAAATVTSV----RALYANTATSRVSIDVNAV 457
Cdd:COG5002 169 VANVSHELRTPLTSIRGYLELLLDGAAD---DPEERREYLEIILEEAERLSRLVNDLldlsRLESGELKLEKEPVDLAEL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 458 VEEARLLLADDLSKAATTFRAELDPDLPPVLADRIQIQQVLVNLVRNAMEAMRANIEtarvIVVRSRGADGQVQVEVADT 537
Cdd:COG5002 246 LEEVVEELRPLAEEKGIELELDLPEDPLLVLGDPDRLEQVLTNLLDNAIKYTPEGGT----ITVSLREEDDQVRISVRDT 321
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1720335109 538 GSGIAEPAL--IFEPLFTT-KAR-----GMGLGLAVSRSILE 571
Cdd:COG5002 322 GIGIPEEDLprIFERFYRVdKSRsretgGTGLGLAIVKHIVE 363
|
|
| HATPase_TmoS-FixL-DctS-like |
cd16920 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
494-571 |
1.31e-24 |
|
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: 98.24 E-value: 1.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 494 IQQVLVNLVRNAMEAMRANIETARVIVVR-SRGADGQVQVEVADTGSGIAE--PALIFEPLFTTKARGMGLGLAVSRSIL 570
Cdd:cd16920 1 IQQVLINLVRNGIEAMSEGGCERRELTIRtSPADDRAVTISVKDTGPGIAEevAGQLFDPFYTTKSEGLGMGLSICRSII 80
|
.
gi 1720335109 571 E 571
Cdd:cd16920 81 E 81
|
|
| PRK13837 |
PRK13837 |
two-component system VirA-like sensor kinase; |
328-571 |
1.40e-23 |
|
two-component system VirA-like sensor kinase;
Pssm-ID: 237526 [Multi-domain] Cd Length: 828 Bit Score: 105.53 E-value: 1.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 328 VDGRVQPLRDDTGRVERWYGLVIDVEDEVRAQENLRAAQRKLARASQLASLAELSASIAHEVRQPLAAVVSNSQACQRWL 407
Cdd:PRK13837 400 QRYGLRPPAGELQLLELALDCLAHAIERRRLETERDALERRLEHARRLEAVGTLASGIAHNFNNILGAILGYAEMALNKL 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 408 SSQSldlgRIRAIMDRIVRDANAAAATVTSVRALYANTATSRVSIDVNAVVEEARLLLAddlskAATTFRAELDPDLPP- 486
Cdd:PRK13837 480 ARHS----RAARYIDEIISAGARARLIIDQILAFGRKGERNTKPFDLSELVTEIAPLLR-----VSLPPGVELDFDQDQe 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 487 ---VLADRIQIQQVLVNLVRNAMEAMRAN----IETARVIVVRSRG-------ADGQVQVEVADTGSGIAEPAL--IFEP 550
Cdd:PRK13837 551 pavVEGNPAELQQVLMNLCSNAAQAMDGAgrvdISLSRAKLRAPKVlshgvlpPGRYVLLRVSDTGAGIDEAVLphIFEP 630
|
250 260
....*....|....*....|.
gi 1720335109 551 LFTTKARGMGLGLAVSRSILE 571
Cdd:PRK13837 631 FFTTRAGGTGLGLATVHGIVS 651
|
|
| PRK13557 |
PRK13557 |
histidine kinase; Provisional |
292-566 |
1.39e-22 |
|
histidine kinase; Provisional
Pssm-ID: 237425 [Multi-domain] Cd Length: 540 Bit Score: 101.67 E-value: 1.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 292 PDDEPAVAAALKHAYATGEPFALRYRNYTADGVPRWVDGRVQPLRDDTGRVERWYGLVIDVEDEVRAQENLRAAQRklar 371
Cdd:PRK13557 84 PETDRATVAEVRDAIAERREIATEILNYRKDGSSFWNALFVSPVYNDAGDLVYFFGSQLDVSRRRDAEDALRQAQK---- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 372 asqLASLAELSASIAHEVRQPLAAVVSNSQACQRWLSSQSLDLGRIRAIMDRIvRDANAAAATVTsvRALYANTATSRV- 450
Cdd:PRK13557 160 ---MEALGQLTGGIAHDFNNLLQVMSGYLDVIQAALSHPDADRGRMARSVENI-RAAAERAATLT--QQLLAFARKQRLe 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 451 --SIDVNAVVEEARLLLADDLSKAaTTFRAELDPDLPPVLADRIQIQQVLVNLVRNAMEAM----RANIETARVIVVRSR 524
Cdd:PRK13557 234 grVLNLNGLVSGMGELAERTLGDA-VTIETDLAPDLWNCRIDPTQAEVALLNVLINARDAMpeggRVTIRTRNVEIEDED 312
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1720335109 525 GA------DGQ-VQVEVADTGSGIAEPAL--IFEPLFTTKARGMGLGLAVS 566
Cdd:PRK13557 313 LAmyhglpPGRyVSIAVTDTGSGMPPEILarVMDPFFTTKEEGKGTGLGLS 363
|
|
| PRK10364 |
PRK10364 |
two-component system sensor histidine kinase ZraS; |
357-571 |
2.05e-22 |
|
two-component system sensor histidine kinase ZraS;
Pssm-ID: 236674 [Multi-domain] Cd Length: 457 Bit Score: 100.25 E-value: 2.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 357 RAQENLRAAQRKLARASQLASLAELSASIAHEVRQPLAAVvsnsQACQRWLSSQSLDLGRIRAIMDRIVRDANAAAATVT 436
Cdd:PRK10364 216 RYLRSRQLLQDEMKRKEKLVALGHLAAGVAHEIRNPLSSI----KGLAKYFAERAPAGGEAHQLAQVMAKEADRLNRVVS 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 437 SVRALYANTATSRVSIDVNAVVEEARLLLADDLSKAATTFRAELDPDLPPVLADRIQIQQVLVNLVRNAMEAMraniETA 516
Cdd:PRK10364 292 ELLELVKPTHLALQAVDLNDLINHSLQLVSQDANSREIQLRFTANDTLPEIQADPDRLTQVLLNLYLNAIQAI----GQH 367
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720335109 517 RVIVVRSRGADGQVQVEVADTGSGIAEPAL--IFEPLFTTKARGMGLGLAVSRSILE 571
Cdd:PRK10364 368 GVISVTASESGAGVKISVTDSGKGIAADQLeaIFTPYFTTKAEGTGLGLAVVHNIVE 424
|
|
| KinB |
COG5806 |
Sporulation sensor histidine kinase B [Cell cycle control, cell division, chromosome ... |
360-571 |
1.11e-21 |
|
Sporulation sensor histidine kinase B [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 444508 [Multi-domain] Cd Length: 412 Bit Score: 97.63 E-value: 1.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 360 ENLRAAQ---RKLARASQLASLAELSASIAHEVRQPLAAVVSNSQACQrwlSSQSLDLGRIRAI------MDR---IVRD 427
Cdd:COG5806 180 ENLIENIllrKELQRAEKLEVVSELAASIAHEVRNPLTVVRGFIQLLQ---EPELSDEKRKQYIrialeeLDRaeaIITD 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 428 anaaaatvtsvralYANTA----TSRVSIDVNAVVEEARLLladdLSKAATTFRAELDPDLPP---VLADRIQIQQVLVN 500
Cdd:COG5806 257 --------------YLTFAkpqpEKLEKIDVSEELEHVIDV----LSPYANMNNVEIQTELEPglyIEGDRQKLQQCLIN 318
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720335109 501 LVRNAMEAMraniETARVIVVRSRGADGQVQVEVADTGSGIAEPAL--IFEPLFTTKARGMGLGLAVSRSILE 571
Cdd:COG5806 319 IIKNGIEAM----PNGGTLTIDVSIDKNKVIISIKDTGVGMTKEQLerLGEPYFSTKEKGTGLGTMVSYRIIE 387
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
117-219 |
6.34e-19 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.
Pssm-ID: 238075 [Multi-domain] Cd Length: 103 Bit Score: 82.30 E-value: 6.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 117 LPTLVWSTDADGTVTFVNQRWRTYTGLSREEAAEGGWIDAVHPEDRDRLLAYWQALRGAGTPGEIEGRLRRADGHYRWFL 196
Cdd:cd00130 1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVL 80
|
90 100
....*....|....*....|...
gi 1720335109 197 FRGEPFRDAAGAVVQWFGSTTDI 219
Cdd:cd00130 81 VSLTPIRDEGGEVIGLLGVVRDI 103
|
|
| PAS_3 |
pfam08447 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
130-214 |
1.89e-18 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.
Pssm-ID: 430001 [Multi-domain] Cd Length: 89 Bit Score: 80.08 E-value: 1.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 130 VTFVNQRWRTYTGLSREEAAEGG--WIDAVHPEDRDRLL-AYWQALRGaGTPGEIEGRLRRADGHYRWFLFRGEPFRDAA 206
Cdd:pfam08447 1 IIYWSPRFEEILGYTPEELLGKGesWLDLVHPDDRERVReALWEALKG-GEPYSGEYRIRRKDGEYRWVEARARPIRDEN 79
|
....*...
gi 1720335109 207 GAVVQWFG 214
Cdd:pfam08447 80 GKPVRVIG 87
|
|
| PRK13560 |
PRK13560 |
hypothetical protein; Provisional |
86-398 |
3.62e-18 |
|
hypothetical protein; Provisional
Pssm-ID: 106506 [Multi-domain] Cd Length: 807 Bit Score: 88.58 E-value: 3.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 86 IRASTDAMRAEMAVVEQALHAQLYQQqLIDALPTLVWSTDADGTVTFVNQRWRTYTGLSREEAAEGGWIDAVHPEDRDRL 165
Cdd:PRK13560 311 VGAITDISGRRAAERELLEKEDMLRA-IIEAAPIAAIGLDADGNICFVNNNAAERMLGWSAAEVMGKPLPGMDPELNEEF 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 166 LA----YW---------------QALRGAGTPGEIEGRLRRADGHYRWFLFRGEPFRDAAGAVVQWFGSTTDIhagrLVR 226
Cdd:PRK13560 390 WCgdfqEWypdgrpmafdacpmaKTIKGGKIFDGQEVLIEREDDGPADCSAYAEPLHDADGNIIGAIALLVDI----TER 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 227 EALKERERELRLIVDTVPALIY-LVGSDGVPSYMNRRIQDYYGIAFDKLpqVDGAQVRAALearVHPDDEPAVAAALKHA 305
Cdd:PRK13560 466 KQVEEQLLLANLIVENSPLVLFrWKAEEGWPVELVSKNITQFGYEPDEF--ISGKRMFAAI---IHPADLEQVAAEVAEF 540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 306 YATG-EPFALRYRNYTADGVPRWVDGRVQPLRDDTGRVERWYGLVIDVEDEVRAQENLRAAqrklarasqLASLAELSAS 384
Cdd:PRK13560 541 AAQGvDRFEQEYRILGKGGAVCWIDDQSAAERDEEGQISHFEGIVIDISERKHAEEKIKAA---------LTEKEVLLKE 611
|
330
....*....|....
gi 1720335109 385 IAHEVRQPLAAVVS 398
Cdd:PRK13560 612 IHHRVKNNLQIISS 625
|
|
| HATPase_c |
smart00387 |
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases. |
489-571 |
8.43e-18 |
|
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
Pssm-ID: 214643 [Multi-domain] Cd Length: 111 Bit Score: 79.23 E-value: 8.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 489 ADRIQIQQVLVNLVRNAMEAMRANIEtarvIVVRSRGADGQVQVEVADTGSGIAEPAL--IFEPLFTTKAR-----GMGL 561
Cdd:smart00387 1 GDPDRLRQVLSNLLDNAIKYTPEGGR----ITVTLERDGDHVEITVEDNGPGIPPEDLekIFEPFFRTDKRsrkigGTGL 76
|
90
....*....|
gi 1720335109 562 GLAVSRSILE 571
Cdd:smart00387 77 GLSIVKKLVE 86
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
226-379 |
1.06e-16 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 80.07 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 226 REALKERERELRLIVDTVPALIYLVGSDGVPSYMNRRIQDYYGIAFDKLpqvdgaqVRAALEARVHPDDEPAVAAALKHA 305
Cdd:COG2202 3 EEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEEL-------LGKTLRDLLPPEDDDEFLELLRAA 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720335109 306 YATGEPFALRYRNYTADGVPRWVDGRVQPLRDDTGRVERWYGLVIDVEDEVRAQENLRAAQRKLARASQLASLA 379
Cdd:COG2202 76 LAGGGVWRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEERLRLLVENAPDG 149
|
|
| HATPase_HupT_MifS-like |
cd16976 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
494-571 |
2.21e-16 |
|
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Rhodobacter capsulatus HupT and Pseudomonas aeruginosa MifS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Rhodobacter capsulatus HupT of the HupT-HupR two-component regulatory system (TCS), which regulates the synthesis of HupSL, a membrane bound [NiFe]hydrogenase. It also contains the HATPase domain of Pseudomonas aeruginosa MifS, the HK of the MifS-MifR TCS, which may be involved in sensing alpha-ketoglutarate and regulating its transport and subsequent metabolism. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some also have a C-terminal PAS sensor domain.
Pssm-ID: 340435 [Multi-domain] Cd Length: 102 Bit Score: 74.80 E-value: 2.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 494 IQQVLVNLVRNAMEAMrANIETARvIVVRSRGADGQVQVEVADTGSGIAEPAL--IFEPLFTTK--ARGMGLGLAVSRSI 569
Cdd:cd16976 1 IQQVLMNLLQNALDAM-GKVENPR-IRIAARRLGGRLVLVVRDNGPGIAEEHLsrVFDPFFTTKpvGKGTGLGLSISYGI 78
|
..
gi 1720335109 570 LE 571
Cdd:cd16976 79 VE 80
|
|
| glnL |
PRK11073 |
nitrogen regulation protein NR(II); |
322-571 |
2.81e-16 |
|
nitrogen regulation protein NR(II);
Pssm-ID: 182947 [Multi-domain] Cd Length: 348 Bit Score: 80.51 E-value: 2.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 322 DGVPRWVDGRVQPLRDDTGRVErwyglVIDVEDEVR-AQENLRAAQRKLARasqlaslaELSASIAHEVRQPLAAVVSNS 400
Cdd:PRK11073 86 DGRSHILSLTAQRLPEGMILLE-----MAPMDNQRRlSQEQLQHAQQVAAR--------DLVRGLAHEIKNPLGGLRGAA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 401 QACQRWLSSQSL---------DLGRIRAIMDRIvrdanaaaatvtsvraLYANTATSRVSIDVNAVVEEARLLLADDLSK 471
Cdd:PRK11073 153 QLLSKALPDPALteytkviieQADRLRNLVDRL----------------LGPQRPGTHVTESIHKVAERVVQLVSLELPD 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 472 AATTFRaELDPDLPPVLADRIQIQQVLVNLVRNAMEAMRaniETARVIVVRSRGA-----DGQ-----VQVEVADTGSGI 541
Cdd:PRK11073 217 NVRLIR-DYDPSLPELAHDPDQIEQVLLNIVRNALQALG---PEGGTITLRTRTAfqltlHGEryrlaARIDIEDNGPGI 292
|
250 260 270
....*....|....*....|....*....|....
gi 1720335109 542 aePALI----FEPLFTTKARGMGLGLAVSRSILE 571
Cdd:PRK11073 293 --PPHLqdtlFYPMVSGREGGTGLGLSIARNLID 324
|
|
| HATPase_AtoS-like |
cd16943 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
491-570 |
3.11e-16 |
|
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli K-12 AtoS; 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 AtoS, an HK of the AtoS-AtoC TCS. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some have accessory domains such as HAMP or PAS sensor domains or CBS-pair domains.
Pssm-ID: 340419 [Multi-domain] Cd Length: 105 Bit Score: 74.38 E-value: 3.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 491 RIQIQQVLVNLVRNAMEAMRANIEtarvIVVRSRGADGQVQVEVADTGSGIAEPAL--IFEPLFTTK--ARGMGLGLAVS 566
Cdd:cd16943 1 PSQLNQVLLNLLVNAAQAMEGRGR----ITIRTWAHVDQVLIEVEDTGSGIDPEILgrIFDPFFTTKpvGEGTGLGLSLS 76
|
....
gi 1720335109 567 RSIL 570
Cdd:cd16943 77 YRII 80
|
|
| PRK09303 |
PRK09303 |
histidine kinase; |
324-571 |
9.59e-15 |
|
histidine kinase;
Pssm-ID: 236462 [Multi-domain] Cd Length: 380 Bit Score: 76.14 E-value: 9.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 324 VPRW-VDGRV--------QPLRDDTGRVErwyGLVIDVEDEVraqenLRAAQRKLARASQLASLAELSASIAHEVRQPLA 394
Cdd:PRK09303 96 WPRWqQEGATysglgenlQPSEIDSGRYS---QELLQLSDEL-----FVLRQENETLLEQLKFKDRVLAMLAHDLRTPLT 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 395 AVVsnsqacqrwLSSQSLDLGRIRA---------------------IMDRIVRDANAAAATVTSvrALYANtatsRVSID 453
Cdd:PRK09303 168 AAS---------LALETLELGQIDEdtelkpalieqlqdqarrqleEIERLITDLLEVGRTRWE--ALRFN----PQKLD 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 454 VNAVVEEARLLLADDLSKAATTFRAELDPDLPPVLADRIQIQQVLVNLVRNAMEAMRANIETARVIVVRSrgaDGQVQVE 533
Cdd:PRK09303 233 LGSLCQEVILELEKRWLAKSLEIQTDIPSDLPSVYADQERIRQVLLNLLDNAIKYTPEGGTITLSMLHRT---TQKVQVS 309
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1720335109 534 VADTGSGI--AEPALIFEPLFTTK----ARGMGLGLAVSRSILE 571
Cdd:PRK09303 310 ICDTGPGIpeEEQERIFEDRVRLPrdegTEGYGIGLSVCRRIVR 353
|
|
| PAS_3 |
pfam08447 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
258-349 |
1.51e-14 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.
Pssm-ID: 430001 [Multi-domain] Cd Length: 89 Bit Score: 69.29 E-value: 1.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 258 YMNRRIQDYYGIAFDKLPQVdgaqvRAALEARVHPDDEPAVAAALKHAYATGEPFALRYRNYTADGVPRWVDGRVQPLRD 337
Cdd:pfam08447 3 YWSPRFEEILGYTPEELLGK-----GESWLDLVHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRD 77
|
90
....*....|..
gi 1720335109 338 DTGRVERWYGLV 349
Cdd:pfam08447 78 ENGKPVRVIGVA 89
|
|
| CitA |
COG3290 |
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ... |
223-571 |
1.79e-14 |
|
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction mechanisms];
Pssm-ID: 442519 [Multi-domain] Cd Length: 389 Bit Score: 75.27 E-value: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 223 RLVREALKERERELRLIVDTVPALIYLVGSDGVPSYMNRRIQDYYGiafdklpqvdgaqvraaLEARVHPDDEpaVAAAL 302
Cdd:COG3290 73 LKLLEEIARLVEEREAVLESIREGVIAVDRDGRITLINDAARRLLG-----------------LDAIGRPIDE--VLAEV 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 303 KHAYATGEPFALRYRNYTADGVPRWVDGRVQplrddtgrverwyGLVIDVED--EVRAQENlraaqrklaRASQLASLAE 380
Cdd:COG3290 134 LETGERDEEILLNGRVLVVNRVPIRDDGRVV-------------GAVATFRDrtELERLEE---------ELEGVKELAE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 381 LSASIAHEVRQPLAAVVSNsqacqrwlssqsLDLGRIRAIMDRIVRDANAAAATVTSVRALYANTAtsrvsidVNAvvee 460
Cdd:COG3290 192 ALRAQRHDFRNHLHTISGL------------LQLGEYDEALEYIDEISEELQELIDSLLSRIGNPV-------LAA---- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 461 arlLLADDLSKAAT---TFRAELDPDLPPVLADRIQIQQVLVNLVRNAMEAMRANIETARVIVVRSRGADGQVQVEVADT 537
Cdd:COG3290 249 ---LLLGKAARARErgiDLTIDIDSDLPDLPLSDTDLVTILGNLLDNAIEAVEKLPEEERRVELSIRDDGDELVIEVEDS 325
|
330 340 350
....*....|....*....|....*....|....*..
gi 1720335109 538 GSGIAEPAL--IFEPLFTTKAR-GMGLGLAVSRSILE 571
Cdd:COG3290 326 GPGIPEELLekIFERGFSTKLGeGRGLGLALVKQIVE 362
|
|
| HATPase_c |
pfam02518 |
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ... |
489-571 |
1.76e-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: 66.62 E-value: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 489 ADRIQIQQVLVNLVRNAMEAMrANIETARVIVVRsrgaDGQVQVEVADTGSGIAEPAL--IFEPLFTTKAR---GMGLGL 563
Cdd:pfam02518 1 GDELRLRQVLSNLLDNALKHA-AKAGEITVTLSE----GGELTLTVEDNGIGIPPEDLprIFEPFSTADKRgggGTGLGL 75
|
....*...
gi 1720335109 564 AVSRSILE 571
Cdd:pfam02518 76 SIVRKLVE 83
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
111-219 |
6.11e-13 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 395786 [Multi-domain] Cd Length: 113 Bit Score: 65.52 E-value: 6.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 111 QQLIDALPTLVWSTDADGTVTFVNQRWRTYTGLSREEAAEGGWIDAVHPEDRDRLLA-YWQALRGAGTPGEIEGRLRRAD 189
Cdd:pfam00989 4 RAILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAElLRQALLQGEESRGFEVSFRVPD 83
|
90 100 110
....*....|....*....|....*....|
gi 1720335109 190 GHYRWFLFRGEPFRDAAGAVVQWFGSTTDI 219
Cdd:pfam00989 84 GRPRHVEVRASPVRDAGGEILGFLGVLRDI 113
|
|
| HATPase_NtrY-like |
cd16944 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
490-571 |
6.31e-12 |
|
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: 62.17 E-value: 6.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 490 DRIQIQQVLVNLVRNAMEAMRANIETARVIVVRSR-GADGQVQVEVADTGSGIAEPAL--IFEPLFTTKARGMGLGLAVS 566
Cdd:cd16944 1 DTTQISQVLTNILKNAAEAIEGRPSDVGEVRIRVEaDQDGRIVLIVCDNGKGFPREMRhrATEPYVTTRPKGTGLGLAIV 80
|
....*
gi 1720335109 567 RSILE 571
Cdd:cd16944 81 KKIME 85
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
111-172 |
7.08e-12 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.
Pssm-ID: 214512 Cd Length: 67 Bit Score: 60.88 E-value: 7.08e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720335109 111 QQLIDALPTLVWSTDADGTVTFVNQRWRTYTGLSREEAAEGGWIDAVHPEDRDRLLAYWQAL 172
Cdd:smart00091 4 RAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRL 65
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
112-236 |
5.22e-11 |
|
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions]
Pssm-ID: 272971 [Multi-domain] Cd Length: 124 Bit Score: 60.00 E-value: 5.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 112 QLIDALPTLVWSTDADGTVTFVNQRWRTYTGLSREEAAEGGWIDAVHPEDRDRLLAY-WQALRGAGTPGEIEGRLRRADG 190
Cdd:TIGR00229 7 AIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERiERRLEGEPEPVSEERRVRRKDG 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1720335109 191 HYRWFLFRGEPFRdAAGAVVQWFGSTTDIHagrlvreALKEREREL 236
Cdd:TIGR00229 87 SEIWVEVSVSPIR-TNGGELGVVGIVRDIT-------ERKEAEEAL 124
|
|
| HATPase_Glnl-NtrB-like |
cd16918 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
494-569 |
1.26e-10 |
|
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli GlnL (synonyms NtrB and NRII); This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs), similar to Escherichia coli GlnL/NtrB/NRII HK of the two-component regulatory system (TCS) GlnL/GlnG (NtrB-NtrC, or NRII-NRI), which regulates the transcription of genes encoding metabolic enzymes and permeases in response to carbon and nitrogen status in E. coli and related bacteria. Also included in this family are Rhodobacter capsulatus NtrB, Azospirillum brasilense NtrB, Vibrio alginolyticus NtrB, Rhizobium leguminosarum biovar phaseoli NtrB, and Herbaspirillum seropedicae NtrB. Escherichia coli GlnL/NtrB/NRII is both a kinase and a phosphatase, catalyzing the phosphorylation and dephosphorylation of GlnG/NtrC/NRI. The kinase and phosphatase activities of GlnL/NtrB/NRII are regulated by the PII signal transduction protein, which on binding to GlnL/NtrB/NRII, inhibits the kinase activity of GlnL/NtrB/NRII and activates the GlnL/NtrB/NRII phosphatase activity. Proteins having this HATPase domain also have a histidine kinase dimerization and phosphoacceptor domain (HisKA); some also contain PAS sensor domain(s).
Pssm-ID: 340395 [Multi-domain] Cd Length: 109 Bit Score: 58.57 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 494 IQQVLVNLVRNAMEAMRaniETARVIVVRSRgADGQV-----------QVEVADTGSGIAePAL---IFEPLFTTKARGM 559
Cdd:cd16918 1 LIQVFLNLVRNAAQALA---GSGGEIILRTR-TQRQVtlghprhrlalRVSVIDNGPGIP-PDLqdtIFYPMVSGRENGT 75
|
90
....*....|
gi 1720335109 560 GLGLAVSRSI 569
Cdd:cd16918 76 GLGLAIAQNI 85
|
|
| HATPase_CckA-like |
cd16919 |
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ... |
495-566 |
2.81e-10 |
|
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar to Brucella abortus 2308 CckA; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinase (HKs) similar to Brucella abortus 2308 CckA, which is a component of an essential protein phosphorelay that regulates expression of genes required for growth, division, and intracellular survival; phosphoryl transfer initiates from the sensor kinase CckA and proceeds via the ChpT phosphotransferase to two regulatory substrates: the DNA-binding response regulator CtrA and the phospho-receiver protein CpdR. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), a REC signal receiver domain, and some contain PAS or PAS and GAF sensor domain(s).
Pssm-ID: 340396 [Multi-domain] Cd Length: 116 Bit Score: 57.77 E-value: 2.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 495 QQVLVNLVRNAMEAM----RANIETARVIV-------VRSRGADGQVQVEVADTGSGIAEPAL--IFEPLFTTKARGMGL 561
Cdd:cd16919 2 ELAILNLAVNARDAMpeggRLTIETSNQRVdadyalnYRDLIPGNYVCLEVSDTGSGMPAEVLrrAFEPFFTTKEVGKGT 81
|
....*
gi 1720335109 562 GLAVS 566
Cdd:cd16919 82 GLGLS 86
|
|
| HATPase_EvgS-ArcB-TorS-like |
cd16922 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ... |
494-571 |
7.97e-10 |
|
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid sensor histidine kinases, similar to Escherichia coli EvgS, ArcB, TorS, BarA, RcsC; This family contains the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinases (HKs), including the following Escherichia coli HKs: EvgS, a HK of the EvgS-EvgA two-component system (TCS) that confers acid resistance; ArcB, a HK of the ArcB-ArcA TCS that modulates the expression of numerous genes in response to respiratory growth conditions; TorS, a HK of the TorS-TorR TCS which is involved in the anaerobic utilization of trimethylamine-N-oxide; BarA, a HK of the BarA-UvrY TCS involved in the regulation of carbon metabolism; and RcsC, a HK of the RcsB-RcsC TCS which regulates the expression of the capsule operon and of the cell division gene ftsZ. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), with most having accessory sensor domain(s) such as GAF, PAS and CHASE; many are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.
Pssm-ID: 340399 [Multi-domain] Cd Length: 110 Bit Score: 56.35 E-value: 7.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 494 IQQVLVNLVRNAmeamranIE-TAR---VIVVRSRGADG---QVQVEVADTGSGIAEPAL--IFEPL------FTTKARG 558
Cdd:cd16922 1 LRQILLNLLGNA-------IKfTEEgevTLRVSLEEEEEdgvQLRFSVEDTGIGIPEEQQarLFEPFsqadssTTRKYGG 73
|
90
....*....|...
gi 1720335109 559 MGLGLAVSRSILE 571
Cdd:cd16922 74 TGLGLAISKKLVE 86
|
|
| PRK15347 |
PRK15347 |
two component system sensor kinase; |
325-569 |
2.14e-09 |
|
two component system sensor kinase;
Pssm-ID: 237951 [Multi-domain] Cd Length: 921 Bit Score: 60.43 E-value: 2.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 325 PRWVDGRvqplRDDTGRVERWYGLVIDVedeVRAQ-ENL--RAAQR--KLARASQLASLA-----ELSASIAHEVRQPLA 394
Cdd:PRK15347 342 PRLPENR----LDELGSIAKAYNQLLDT---LNEQyDTLenKVAERtqALAEAKQRAEQAnkrksEHLTTISHEIRTPLN 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 395 AVV------SNSQacqrwLSSQSLDLgriraimdrivrdANAAAATVTSVRALYANTAT-SRV-SIDVNAVVEEARLL-L 465
Cdd:PRK15347 415 GVLgalellQNTP-----LTAEQMDL-------------ADTARQCTLSLLAIINNLLDfSRIeSGQMTLSLEETALLpL 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 466 ADD---------LSKAaTTFRAELDPDLPPVLA-DRIQIQQVLVNLVRNAMEAMraniETARvIVVRSRGADGQVQVEVA 535
Cdd:PRK15347 477 LDQamltiqgpaQSKS-LTLRTFVGAHVPLYLHlDSLRLRQILVNLLGNAVKFT----ETGG-IRLRVKRHEQQLCFTVE 550
|
250 260 270
....*....|....*....|....*....|....*...
gi 1720335109 536 DTGSGIAEPAL--IFEPLFTT--KARGMGLGLAVSRSI 569
Cdd:PRK15347 551 DTGCGIDIQQQqqIFTPFYQAdtHSQGTGLGLTIASSL 588
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
127-221 |
1.11e-08 |
|
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 463873 [Multi-domain] Cd Length: 93 Bit Score: 52.46 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 127 DGTVTFVNQRWRTYTGLSREEAaEGGWIDAVHPEDrDRLLAYWQALRGAGTPGEIEGRLRRADGHYRWFLFRGEPFRDAA 206
Cdd:pfam13426 1 DGRIIYVNDAALRLLGYTREEL-LGKSITDLFAEP-EDSERLREALREGKAVREFEVVLYRKDGEPFPVLVSLAPIRDDG 78
|
90
....*....|....*
gi 1720335109 207 GAVVQWFGSTTDIHA 221
Cdd:pfam13426 79 GELVGIIAILRDITE 93
|
|
| PRK11100 |
PRK11100 |
sensory histidine kinase CreC; Provisional |
384-569 |
1.23e-08 |
|
sensory histidine kinase CreC; Provisional
Pssm-ID: 236846 [Multi-domain] Cd Length: 475 Bit Score: 57.55 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 384 SIAHEVRQPLAAVVSNS---------QACQRWLSSQSLDLGRIRAIMDRIVRdanaaAATVTSVRALYAntatsRVSIDV 454
Cdd:PRK11100 262 TLTHELKSPLAAIRGAAellqedpppEDRARFTGNILTQSARLQQLIDRLLE-----LARLEQRQELEV-----LEPVAL 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 455 NAVVEEARLLLADDLSKAATTFRaeLDPDLPPVLADRIQIQQVLVNLVRNAMEAMRANIEtarvIVVRSRGADGQVQVEV 534
Cdd:PRK11100 332 AALLEELVEAREAQAAAKGITLR--LRPDDARVLGDPFLLRQALGNLLDNAIDFSPEGGT----ITLSAEVDGEQVALSV 405
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1720335109 535 ADTGSGIAEPAL--IFEPLFT-----TKARGMGLGLAVSRSI 569
Cdd:PRK11100 406 EDQGPGIPDYALprIFERFYSlprpaNGRKSTGLGLAFVREV 447
|
|
| PRK13560 |
PRK13560 |
hypothetical protein; Provisional |
90-365 |
1.37e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 106506 [Multi-domain] Cd Length: 807 Bit Score: 57.76 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 90 TDAMRAEMAVVEQaLHaqlYQQQLIDALPTLVWSTDADGTVTFVNQRWRTYTGLSREEAAeGGWIDAVHPEDR--DRLLA 167
Cdd:PRK13560 190 TERKRAEERIDEA-LH---FLQQLLDNIADPAFWKDEDAKVFGCNDAACLACGFRREEII-GMSIHDFAPAQPadDYQEA 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 168 YWQALRGAGTPgEIEGRLRRADGHYRWF--LFRGEPFRDAAGAVVQWFGSTTDIHAGRLVREALKERERELRLIVDTVPA 245
Cdd:PRK13560 265 DAAKFDADGSQ-IIEAEFQNKDGRTRPVdvIFNHAEFDDKENHCAGLVGAITDISGRRAAERELLEKEDMLRAIIEAAPI 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 246 LIYLVGSDGVPSYMNRRIQDYY------GIAFDKLPQVDGAQvRAALEARV----HPDDEPAVAAALKHAYAT--GEPF- 312
Cdd:PRK13560 344 AAIGLDADGNICFVNNNAAERMlgwsaaEVMGKPLPGMDPEL-NEEFWCGDfqewYPDGRPMAFDACPMAKTIkgGKIFd 422
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1720335109 313 ALRYRNYTADGVPRWVDGRVQPLRDDTGRVERWYGLVIDVEDEVRAQENLRAA 365
Cdd:PRK13560 423 GQEVLIEREDDGPADCSAYAEPLHDADGNIIGAIALLVDITERKQVEEQLLLA 475
|
|
| PRK11466 |
PRK11466 |
hybrid sensory histidine kinase TorS; Provisional |
363-571 |
2.53e-08 |
|
hybrid sensory histidine kinase TorS; Provisional
Pssm-ID: 236914 [Multi-domain] Cd Length: 914 Bit Score: 56.84 E-value: 2.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 363 RAAQRKLARASQLASlaELSASIAHEVRQPLAAVVSNSQ--ACQRWLSSQSLDLGRIR-------AIMDRIVrDANAAAA 433
Cdd:PRK11466 431 RQARAEAEKASQAKS--AFLAAMSHEIRTPLYGILGTAQllADNPALNAQRDDLRAITdsgesllTILNDIL-DYSAIEA 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 434 TVTSVralyantATSRVSIDVNAVVEEARLLLADDLSKAATTFRAELDPDLPPVL-ADRIQIQQVLVNLVRNAMEAmran 512
Cdd:PRK11466 508 GGKNV-------SVSDEPFEPRPLLESTLQLMSGRVKGRPIRLATDIADDLPTALmGDPRRIRQVITNLLSNALRF---- 576
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720335109 513 ieTAR-VIVVRSRGADGQVQVEVADTGSGI--AEPALIFEPLFTTKAR--GMGLGLAVSRSILE 571
Cdd:PRK11466 577 --TDEgSIVLRSRTDGEQWLVEVEDSGCGIdpAKLAEIFQPFVQVSGKrgGTGLGLTISSRLAQ 638
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
124-357 |
2.73e-08 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 56.99 E-value: 2.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 124 TDADGTVTFVNQRWRTYTGLSREEAAEGGWIDAVHPEDR-------DRLLAywqalrgagtpGEI-----EGRLRRADGH 191
Cdd:PRK09776 299 VGTEGQWLQVNKALCQFLGYSQEELRGLTFQQLTWPEDLnkdlqqvEKLLS-----------GEInsysmEKRYYRRDGE 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 192 YRWFLFRGEPFRDAAGAVVQWFGSTTDIHAGRL---VREALKERereLRLIVDTVPALIYL--VGSDGVpsYMNRRIQDY 266
Cdd:PRK09776 368 VVWALLAVSLVRDTDGTPLYFIAQIEDINELKRteqVNERLMER---ITLANEAGGIGIWEwdLKPNII--SWDKRMFEL 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 267 YGIAFDKLPQVDGAQvraaleARVHPDDEPAVAAALKHAYATGEPFALRYRNYTADGVpRWVDGRVQPLRDDTGRVERWY 346
Cdd:PRK09776 443 YEIPPHIKPTWQVWY------ACLHPEDRQRVEKEIRDALQGRSPFKLEFRIVVKDGV-RHIRALANRVLNKDGEVERLL 515
|
250
....*....|.
gi 1720335109 347 GLVIDVEdEVR 357
Cdd:PRK09776 516 GINMDMT-EVR 525
|
|
| HATPase_DpiB-CitA-like |
cd16915 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
500-571 |
7.57e-08 |
|
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli K-12 DpiB, DcuS, and Bacillus subtilis CitS, DctS, and YufL; This family includes histidine kinase-like ATPase domains of Escherichia coli K-12 DpiB and DcuS, and Bacillus subtilis CitS, DctS and MalK histidine kinases (HKs) all of which are two component transduction systems (TCSs). E. coli K-12 DpiB (also known as CitA) is the histidine kinase (HK) of DpiA-DpiB, a two-component signal transduction system (TCS) required for the expression of citrate-specific fermentation genes and genes involved in plasmid inheritance. E. coli K-12 DcuS (also known as YjdH) is the HK of DcuS-DcuR, a TCS that in the presence of the extracellular C4-dicarboxlates, activates the expression of the genes of anaerobic fumarate respiration and of aerobic C4-dicarboxylate uptake. CitS is the HK of Bacillus subtilis CitS-CitT, a TCS which regulates expression of CitM, the Mg-citrate transporter. Bacillus subtilis DctS forms a tripartite sensor unit (DctS/DctA/DctB) for sensing C4 dicarboxylates. Bacillus subtilis MalK (also known as YfuL) is the HK of MalK-MalR (YufL-YufM) a TCS which regulates the expression of the malate transporters MaeN (YufR) and YflS, and is essential for utilization of malate in minimal medium. Proteins having this DpiB-CitA-like HATPase domain generally have sensor domains such as Cache and PAS, and a histidine kinase A (HisKA)-like SpoOB-type, alpha-helical domain.
Pssm-ID: 340392 [Multi-domain] Cd Length: 104 Bit Score: 50.75 E-value: 7.57e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720335109 500 NLVRNAMEAM-RANIETARVIV-VRSRGADgqVQVEVADTGSGIAEP--ALIFEPLFTTKA-RGMGLGLAVSRSILE 571
Cdd:cd16915 7 NLIDNALDALaATGAPNKQVEVfLRDEGDD--LVIEVRDTGPGIAPElrDKVFERGVSTKGqGERGIGLALVRQSVE 81
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
244-352 |
8.83e-08 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.
Pssm-ID: 238075 [Multi-domain] Cd Length: 103 Bit Score: 50.32 E-value: 8.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 244 PALIYLVGSDGVPSYMNRRIQDYYGIAFDKLPQVDGAQVraalearVHPDDEPAVAAALKHAYATGEPFALRYRNYTADG 323
Cdd:cd00130 2 PDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDL-------IHPEDREELRERLENLLSGGEPVTLEVRLRRKDG 74
|
90 100
....*....|....*....|....*....
gi 1720335109 324 VPRWVDGRVQPLRDDTGRVERWYGLVIDV 352
Cdd:cd00130 75 SVIWVLVSLTPIRDEGGEVIGLLGVVRDI 103
|
|
| PRK11086 |
PRK11086 |
sensory histidine kinase DcuS; Provisional |
497-571 |
6.79e-07 |
|
sensory histidine kinase DcuS; Provisional
Pssm-ID: 236839 [Multi-domain] Cd Length: 542 Bit Score: 52.22 E-value: 6.79e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720335109 497 VLVNLVRNAMEAMrANIETARvIVVRSRGADGQVQVEVADTGSGIAEPAL--IFEPLFTTKARGMGLGLAVSRSILE 571
Cdd:PRK11086 437 ILGNLIENALEAV-GGEEGGE-ISVSLHYRNGWLHCEVSDDGPGIAPDEIdaIFDKGYSTKGSNRGVGLYLVKQSVE 511
|
|
| PAS_4 |
pfam08448 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
240-357 |
1.11e-06 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain is associated to signalling systems and works as a signal sensor domain. It recognizes differently substituted aromatic hydrocarbons, oxygen, different dodecanoic acids, autoinducers, 3,5-dimethyl-pyrazin-2-ol and N-alanyl-aminoacetone (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 312075 [Multi-domain] Cd Length: 110 Bit Score: 47.41 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 240 VDTVPALIYLVGSDGVPSYMNRRIQDYYGiafdklpqVDGAQVRAALEARVHPD-DEPAVAAALKHAYATGEPFALRYRn 318
Cdd:pfam08448 1 LDSLPDALAVLDPDGRVRYANAAAAELFG--------LPPEELLGKTLAELLPPeDAARLERALRRALEGEEPIDFLEE- 71
|
90 100 110
....*....|....*....|....*....|....*....
gi 1720335109 319 YTADGVPRWVDGRVQPLRDDTGRVERWYGLVIDVEDEVR 357
Cdd:pfam08448 72 LLLNGEERHYELRLTPLRDPDGEVIGVLVISRDITERRR 110
|
|
| PRK13559 |
PRK13559 |
hypothetical protein; Provisional |
292-464 |
3.51e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 237427 [Multi-domain] Cd Length: 361 Bit Score: 49.43 E-value: 3.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 292 PDDEPAVAAALKHAYATGEPFALRYRNYTADGVPRWVDGRVQPLRDDTGRVERWYGLVIDVEDeVRAQENLRAAQRKLAR 371
Cdd:PRK13559 97 AATDPIAVAKIRAAIAAEREIVVELLNYRKDGEPFWNALHLGPVYGEDGRLLYFFGSQWDVTD-IRAVRALEAHERRLAR 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 372 A---------SQLASLAELSaSIAHEVRQPLAAVVSNSQAcqrwlssqsldLGRI-RAIMDRIVRDANAAAATVTSVRAL 441
Cdd:PRK13559 176 EvdhrsknvfAVVDSIVRLT-GRADDPSLYAAAIQERVQA-----------LARAhETLLDERGWETVEVEELIRAQVAP 243
|
170 180
....*....|....*....|...
gi 1720335109 442 YANTATsRVSIDVNAVVEEARLL 464
Cdd:PRK13559 244 YAPRAT-RVAFEGPGIRLGAASV 265
|
|
| PAS_4 |
pfam08448 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
115-219 |
6.98e-06 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain is associated to signalling systems and works as a signal sensor domain. It recognizes differently substituted aromatic hydrocarbons, oxygen, different dodecanoic acids, autoinducers, 3,5-dimethyl-pyrazin-2-ol and N-alanyl-aminoacetone (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 312075 [Multi-domain] Cd Length: 110 Bit Score: 45.10 E-value: 6.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 115 DALPTLVWSTDADGTVTFVNQRWRTYTGLSREEAAEGGWIDAVHPEDRDRLLAYWQALRGAGTPGEIEGRLRRADGHyRW 194
Cdd:pfam08448 2 DSLPDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAELLPPEDAARLERALRRALEGEEPIDFLEELLLNGEE-RH 80
|
90 100
....*....|....*....|....*
gi 1720335109 195 FLFRGEPFRDAAGAVVQWFGSTTDI 219
Cdd:pfam08448 81 YELRLTPLRDPDGEVIGVLVISRDI 105
|
|
| HATPase_BaeS-like |
cd16946 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
490-571 |
8.92e-06 |
|
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli BasS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) similar to Escherichia coli BaeS HK of the BaeS/BaeR two-component regulatory system (TCS), which responds to envelope stress. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and a HAMP sensory domain.
Pssm-ID: 340422 [Multi-domain] Cd Length: 109 Bit Score: 44.76 E-value: 8.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 490 DRIQIQQVLVNLVRNAMEAMraniETARVIVVRSRGADGQVQVEVADTGSGIA--EPALIFEPLF---TTKAR---GMGL 561
Cdd:cd16946 1 DRDRLQQLFVNLLENSLRYT----DTGGKLRIRAAQTPQEVRLDVEDSAPGVSddQLARLFERFYrveSSRNRasgGSGL 76
|
90
....*....|
gi 1720335109 562 GLAVSRSILE 571
Cdd:cd16946 77 GLAICHNIAL 86
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
232-362 |
9.13e-06 |
|
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions]
Pssm-ID: 272971 [Multi-domain] Cd Length: 124 Bit Score: 45.36 E-value: 9.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 232 RERELRLIVDTVPALIYLVGSDGVPSYMNRRIQDYYGIAFDKLpqvdgaQVRAALEARVHPDDEPAVAAALKHAYATGEP 311
Cdd:TIGR00229 1 SEERYRAIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEEL------IGRNVLELIPEEDREEVRERIERRLEGEPEP 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1720335109 312 FALRYRNYTADGVPRWVDGRVQPLRDDtGRVERWYGLVIDVEDEVRAQENL 362
Cdd:TIGR00229 75 VSEERRVRRKDGSEIWVEVSVSPIRTN-GGELGVVGIVRDITERKEAEEAL 124
|
|
| PRK10490 |
PRK10490 |
sensor protein KdpD; Provisional |
479-571 |
1.30e-05 |
|
sensor protein KdpD; Provisional
Pssm-ID: 236701 [Multi-domain] Cd Length: 895 Bit Score: 48.11 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 479 ELDPDLPPVLADRIQIQQVLVNLVRNAMEAMRANIEtarvIVVRSRGADGQVQVEVADTGSGIA--EPALIFEPLfttkA 556
Cdd:PRK10490 764 SLPEPLTLIHVDGPLFERVLINLLENAVKYAGAQAE----IGIDAHVEGERLQLDVWDNGPGIPpgQEQLIFDKF----A 835
|
90 100
....*....|....*....|...
gi 1720335109 557 R--------GMGLGLAVSRSILE 571
Cdd:PRK10490 836 RgnkesaipGVGLGLAICRAIVE 858
|
|
| HATPase_BvrS-ChvG-like |
cd16953 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
496-571 |
1.54e-05 |
|
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Brucella abortus BvrS and Sinorhizobium meliloti ChvG; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Brucella abortus BvrS of the BvrR-BvrS two-component regulatory system (TCS), which controls cell invasion and intracellular survival, as well as Sinorhizobium meliloti and Agrobacterium tumefaciens ChvG of the ChvI-ChvG TCS necessary for endosymbiosis and pathogenicity in plants. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), an accessory HAMP sensor domain, a periplasmic stimulus-sensing domain, and some also have a sensor N-terminal transmembrane domain.
Pssm-ID: 340429 [Multi-domain] Cd Length: 110 Bit Score: 44.10 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 496 QVLVNLVRNAMEAMRAniETARVIVVRSRGADgQVQVEVADTGSGIAEPAL--IFEPLFTTKARG------MGLGLAVSR 567
Cdd:cd16953 3 QVLRNLIGNAISFSPP--DTGRITVSAMPTGK-MVTISVEDEGPGIPQEKLesIFDRFYTERPANeafgqhSGLGLSISR 79
|
....
gi 1720335109 568 SILE 571
Cdd:cd16953 80 QIIE 83
|
|
| PRK13558 |
PRK13558 |
bacterio-opsin activator; Provisional |
292-371 |
2.08e-05 |
|
bacterio-opsin activator; Provisional
Pssm-ID: 237426 [Multi-domain] Cd Length: 665 Bit Score: 47.52 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 292 PDDEPAVAAALKHAYATGEPFALRYRNYTADGVPRWVDGRVQPLRDDTGRVERWYGLVIDVEDEVRAQENLRAAQRKLAR 371
Cdd:PRK13558 202 EDTNEERVAELREAIDEERPTSVELRNYRKDGSTFWNQVDIAPIRDEDGTVTHYVGFQTDVTERKEAELALQRERRKLQR 281
|
|
| PAC |
smart00086 |
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ... |
180-219 |
2.71e-05 |
|
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif occurs C-terminal to a subset of all known PAS motifs. It is proposed to contribute to the PAS domain fold.
Pssm-ID: 197509 Cd Length: 43 Bit Score: 41.40 E-value: 2.71e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1720335109 180 EIEGRLRRADGHYRWFLFRGEPFRDAAGAVVQWFGSTTDI 219
Cdd:smart00086 1 TVEYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDI 40
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
234-352 |
2.89e-05 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 395786 [Multi-domain] Cd Length: 113 Bit Score: 43.56 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 234 RELRLIVDTVPALIYLVGSDGVPSYMNRRIQDYYGIAfdkLPQVDGaqvRAALEARVHPDDEPAVAAALKHAYATGEPFA 313
Cdd:pfam00989 1 EDLRAILESLPDGIFVVDEDGRILYVNAAAEELLGLS---REEVIG---KSLLDLIPEEDDAEVAELLRQALLQGEESRG 74
|
90 100 110
....*....|....*....|....*....|....*....
gi 1720335109 314 LRYRNYTADGVPRWVDGRVQPLRDDTGRVERWYGLVIDV 352
Cdd:pfam00989 75 FEVSFRVPDGRPRHVEVRASPVRDAGGEILGFLGVLRDI 113
|
|
| PRK10841 |
PRK10841 |
two-component system sensor histidine kinase RcsC; |
480-565 |
4.10e-05 |
|
two-component system sensor histidine kinase RcsC;
Pssm-ID: 182772 [Multi-domain] Cd Length: 924 Bit Score: 46.51 E-value: 4.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 480 LDPDLPPVL-ADRIQIQQVLVNLVRNAMEamranIETARVIVVRSRGADGQVQVEVADTGSGIAEPALI--FEPLF---T 553
Cdd:PRK10841 548 IEPDVPVALnGDPMRLQQVISNLLSNAIK-----FTDTGCIVLHVRVDGDYLSFRVRDTGVGIPAKEVVrlFDPFFqvgT 622
|
90
....*....|....*
gi 1720335109 554 TKAR---GMGLGLAV 565
Cdd:PRK10841 623 GVQRnfqGTGLGLAI 637
|
|
| HATPase_FilI-like |
cd16921 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
494-571 |
5.06e-05 |
|
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Methanosaeta harundinacea FilI and some hybrid sensor histidine kinases; This family includes FilI, the histidine kinase (HK) component of FilI-FilRs, a two-component signal transduction system (TCS) of the methanogenic archaeon, Methanosaeta harundinacea, which is involved in regulating methanogenesis. The cytoplasmic HK core consists of a C-terminal HK-like ATPase domain (represented here) and a histidine kinase dimerization and phosphoacceptor domain (HisKA) domain, which, in FilI, are coupled to CHASE, HAMP, PAS, and GAF sensor domains. FilI-FilRs catalyzes the phosphotransfer between FilI (HK) and FilRs (FilR1 and FilR2, response regulators) of the TCS. TCSs are predicted to be of bacterial origin, and acquired by archaea by horizontal gene transfer. This model also includes related HATPase domains such as that of Synechocystis sp. PCC6803 phytochrome-like protein Cph1. Proteins having this HATPase domain and HisKA domain also have accessory sensor domains such as CHASE, GAF, HAMP and PAS; some are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.
Pssm-ID: 340398 [Multi-domain] Cd Length: 105 Bit Score: 42.70 E-value: 5.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 494 IQQVLVNLVRNAMEAMRANiETARVIVVRSRGADGQvQVEVADTGSGIAEPalIFEPLFTTKAR--------GMGLGLAV 565
Cdd:cd16921 1 LGQVLTNLLGNAIKFRRPR-RPPRIEVGAEDVGEEW-TFYVRDNGIGIDPE--YAEKVFGIFQRlhsreeyeGTGVGLAI 76
|
....*.
gi 1720335109 566 SRSILE 571
Cdd:cd16921 77 VRKIIE 82
|
|
| HATPase_EnvZ-like |
cd16950 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
494-570 |
5.32e-05 |
|
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli EnvZ and Pseudomonas aeruginosa BfmS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Escherichia coli EnvZ of the EnvZ-OmpR two-component regulatory system (TCS), which functions in osmoregulation. It also contains the HATPase domain of Pseudomonas aeruginosa BfmS, the HK of the BfmSR TCS, which functions in the regulation of the rhl quorum-sensing system and bacterial virulence in P. aeruginosa. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and a HAMP sensor domain; some also contain a periplasmic domain.
Pssm-ID: 340426 [Multi-domain] Cd Length: 101 Bit Score: 42.44 E-value: 5.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 494 IQQVLVNLVRNAMEAMRANIEtarvivVRSRGADGQVQVEVADTGSGIAEPAL--IFEPLFT-TKAR---GMGLGLAVSR 567
Cdd:cd16950 1 LKRVLSNLVDNALRYGGGWVE------VSSDGEGNRTRIQVLDNGPGIAPEEVdeLFQPFYRgDNARgtsGTGLGLAIVQ 74
|
...
gi 1720335109 568 SIL 570
Cdd:cd16950 75 RIS 77
|
|
| PRK11091 |
PRK11091 |
aerobic respiration control sensor protein ArcB; Provisional |
314-567 |
5.42e-05 |
|
aerobic respiration control sensor protein ArcB; Provisional
Pssm-ID: 236842 [Multi-domain] Cd Length: 779 Bit Score: 46.09 E-value: 5.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 314 LRYrnytADGVPRWVDGRVQPLRDDTGRverWYGLV---IDVEDEVRAQENLRAAQRKLARasqlaslaeLSASIAHEVR 390
Cdd:PRK11091 232 LDY----PDGRKACFELRKVPFYDRVGK---RHGLMgfgRDITERKRYQDALEKASRDKTT---------FISTISHELR 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 391 QPLAAVVS----------NSQACQrWLS---SQSLDLGRI-RAI--MDRIVRDanaaaatvtsvRALYANTAtsrvsIDV 454
Cdd:PRK11091 296 TPLNGIVGlsrilldtelTAEQRK-YLKtihVSAITLGNIfNDIidMDKMERR-----------KLQLDNQP-----IDF 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 455 NAVVEE----ARLLLAD-DLSkaattFRAELDPDLPP-VLADRIQIQQVLVNLVRNAMEAMRANIETARVIvvRSRGADg 528
Cdd:PRK11091 359 TDFLADlenlSGLQAEQkGLR-----FDLEPLLPLPHkVITDGTRLRQILWNLISNAVKFTQQGGVTVRVR--YEEGDM- 430
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1720335109 529 qVQVEVADTGSGIAEPAL--IFEPLFTTK-------ARGMGLGLAVSR 567
Cdd:PRK11091 431 -LTFEVEDSGIGIPEDELdkIFAMYYQVKdshggkpATGTGIGLAVSK 477
|
|
| PRK11107 |
PRK11107 |
hybrid sensory histidine kinase BarA; Provisional |
480-543 |
5.93e-05 |
|
hybrid sensory histidine kinase BarA; Provisional
Pssm-ID: 236848 [Multi-domain] Cd Length: 919 Bit Score: 46.00 E-value: 5.93e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720335109 480 LDPDLPP-VLADRIQIQQVLVNLVRNAM---EamRANIEtarvIVVRSRGADG---QVQVEVADTGSGIAE 543
Cdd:PRK11107 394 IDPDVPDnVIGDPLRLQQIITNLVGNAIkftE--SGNID----ILVELRALSNtkvQLEVQIRDTGIGISE 458
|
|
| PAS_8 |
pfam13188 |
PAS domain; PAS domains are involved in many signalling proteins where they are used as a ... |
111-165 |
6.75e-05 |
|
PAS domain; PAS domains are involved in many signalling proteins where they are used as a signal sensor domain. PAS domains appear in archaea, bacteria and eukaryotes. Several PAS-domain proteins are known to detect their signal by way of an associated cofactor. Heme, flavin, and a 4-hydroxycinnamyl chromophore are used in different proteins. This domain recognizes oxygen and CO (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 463802 [Multi-domain] Cd Length: 65 Bit Score: 41.00 E-value: 6.75e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1720335109 111 QQLIDALPTLVWSTDADGTVTFVNQRWRTYTGLSREEAAEGGWIDAVHPEDRDRL 165
Cdd:pfam13188 4 RALFESSPDGILVLDEGGRIIYVNPAALELLGYELLGELLGELLDLLDPLLEDAL 58
|
|
| PAC |
smart00086 |
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ... |
316-355 |
8.08e-05 |
|
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif occurs C-terminal to a subset of all known PAS motifs. It is proposed to contribute to the PAS domain fold.
Pssm-ID: 197509 Cd Length: 43 Bit Score: 40.24 E-value: 8.08e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1720335109 316 YRNYTADGVPRWVDGRVQPLRDDTGRVERWYGLVIDVEDE 355
Cdd:smart00086 4 YRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITER 43
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
153-243 |
9.27e-05 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 45.43 E-value: 9.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 153 WIDAVHPEDRDRLLA-YWQALRGAgTPGEIEGRLRRADG--HYRWFLFRgepFRDAAGAVVQWFGSTTDIHAGRLVREAL 229
Cdd:PRK09776 456 WYACLHPEDRQRVEKeIRDALQGR-SPFKLEFRIVVKDGvrHIRALANR---VLNKDGEVERLLGINMDMTEVRQLNEAL 531
|
90
....*....|....*...
gi 1720335109 230 -KERER---ELRLIVDTV 243
Cdd:PRK09776 532 fQEKERlhiTLDSIGEAV 549
|
|
| HisKA |
pfam00512 |
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ... |
377-426 |
1.56e-04 |
|
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine kinases.
Pssm-ID: 459839 [Multi-domain] Cd Length: 66 Bit Score: 39.89 E-value: 1.56e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1720335109 377 SLAELSASIAHEVRQPLAAVVSNSQACQRWLSSQSLD--LGRIRAIMDRIVR 426
Cdd:pfam00512 1 AKSEFLANLSHELRTPLTAIRGYLELLRDEKLDEEQReyLETILRSAERLLR 52
|
|
| HisKA |
cd00082 |
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ... |
375-441 |
1.71e-04 |
|
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed through parallel association of 2 domains creating 4-helix bundles; usually these domains contain a conserved His residue and are activated via trans-autophosphorylation by the catalytic domain of the histidine kinase. They subsequently transfer the phosphoryl group to the Asp acceptor residue of a response regulator protein. Two-component signalling systems, consisting of a histidine protein kinase that senses a signal input and a response regulator that mediates the output, are ancient and evolutionarily conserved signaling mechanisms in prokaryotes and eukaryotes.
Pssm-ID: 119399 [Multi-domain] Cd Length: 65 Bit Score: 39.89 E-value: 1.71e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720335109 375 LASLAELSASIAHEVRQPLAAVVSNSQACQRWLssqsLDLGRIRAIMDRIVRDANAAAATVTSVRAL 441
Cdd:cd00082 1 LQAKGEFLANVSHELRTPLTAIRGALELLEEEL----LDDEEQREYLERIREEAERLLRLINDLLDL 63
|
|
| RsbW |
COG2172 |
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms]; |
466-564 |
1.91e-04 |
|
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
Pssm-ID: 441775 [Multi-domain] Cd Length: 127 Bit Score: 41.44 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 466 ADDLSKAATTFRAELDP-DLPPVLADRIQIqqVLVNLVRNAME-AMRANIETarVIVVRSRGADGQVQVEVADTGSGIaE 543
Cdd:COG2172 8 LEDLGLARRAVRALLRElGLDEDDADDLVL--AVSEAVTNAVRhAYGGDPDG--PVEVELELDPDGLEIEVRDEGPGF-D 82
|
90 100
....*....|....*....|.
gi 1720335109 544 PALIFEPLFTTKARGMGLGLA 564
Cdd:COG2172 83 PEDLPDPYSTLAEGGRGLFLI 103
|
|
| RocR |
COG3829 |
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ... |
229-374 |
2.38e-04 |
|
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis domains [Transcription, Signal transduction mechanisms];
Pssm-ID: 443041 [Multi-domain] Cd Length: 448 Bit Score: 43.61 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 229 LKERERELRLIVDTVPALIYLVGSDGVPSYMNRRIQDYYGIafdKLPQVDGAQVRAALEarvhpddEPAVAAALKhayaT 308
Cdd:COG3829 6 LKELEEELEAILDSLDDGIIVVDADGRITYVNRAAERILGL---PREEVIGKNVTELIP-------NSPLLEVLK----T 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720335109 309 GEPFALRYRNYtaDGVPRWVDGRVQPLRDDtGRVERWYGLVIDVEDEVRAQENLRAAQRKLARASQ 374
Cdd:COG3829 72 GKPVTGVIQKT--GGKGKTVIVTAIPIFED-GEVIGAVETFRDITELKRLERKLREEELERGLSAK 134
|
|
| HATPase_BasS-like |
cd16940 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
487-571 |
3.19e-04 |
|
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli BasS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) similar to Escherichia coli BasS HK of the BasS-BasR two-component regulatory system (TCS). Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some contain a HAMP sensory domain, while some an N-terminal two-component sensor kinase domain.
Pssm-ID: 340417 [Multi-domain] Cd Length: 113 Bit Score: 40.47 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 487 VLADRIQIQQVLVNLVRNameAMRANIETARVIVVRSrgADGQVQVEVADTGSGIAEPAL--IFEPLF---TTKARGMGL 561
Cdd:cd16940 7 VQGDALLLFLLLRNLVDN---AVRYSPQGSRVEIKLS--ADDGAVIRVEDNGPGIDEEELeaLFERFYrsdGQNYGGSGL 81
|
90
....*....|
gi 1720335109 562 GLAVSRSILE 571
Cdd:cd16940 82 GLSIVKRIVE 91
|
|
| HATPase_SpoIIAB-like |
cd16942 |
Histidine kinase-like ATPase domain of SpoIIAB, an anti sigma-F factor and serine-protein ... |
472-560 |
3.34e-04 |
|
Histidine kinase-like ATPase domain of SpoIIAB, an anti sigma-F factor and serine-protein kinase involved in regulating sigma-F during sporulation in Bacilli, and related domains; This family includes histidine kinase-like ATPase (HATPase) domain of SpoIIAB, an anti sigma-F factor and a serine-protein kinase involved in regulating sigma-F during sporulation in Bacilli where, early in sporulation, the cell divides into two unequal compartments: a larger mother cell and a smaller forespore. Sigma-F transcription factor is activated in the forespore directly after the asymmetric septum forms, and its spatial and temporal activation is required for sporulation. Free sigma-F can associate with the RNA polymerase core and activate transcription of the sigma-F regulon, its regulation may comprise a partner-switching mechanism involving SpoIIAB, SpoIIAA, and sigma-F as follows: SpoIIAB can form alternative complexes with either: i) sigma-F, holding it in an inactive form and preventing its association with RNA polymerase, or ii) unphosphorylated SpoIIAA and a nucleotide, either ATP or ADP. In the presence of ATP, SpoIIAB acts as a kinase to specifically phosphorylate a serine residue of SpoIIAA; this phosphorylated form has low affinity for SpoIIAB and dissociates, making SpoIIAB available to capture sigma-F. SpoIIAA may then be dephosphorylated by a SpoIIE serine phosphatase and be free to attack the SpoIIAB sigma-F complex to induce the release of sigma-F.
Pssm-ID: 340418 [Multi-domain] Cd Length: 135 Bit Score: 40.98 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 472 AATTFRAELDPdlppVLADRIQIQQVLVNLVRNAMEAMRANIETARVIVVRSRgADGQVQVEVADTGSGIAEPALIFEPL 551
Cdd:cd16942 21 TVAAFVAQLDP----TIDELTEIKTVVSEAVTNAIIHGYNNDPNGIVSISVII-EDGVVHLTVRDEGVGIPDIEEARQPL 95
|
90
....*....|...
gi 1720335109 552 FTTKAR----GMG 560
Cdd:cd16942 96 FTTKPElersGMG 108
|
|
| RocR |
COG3829 |
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ... |
111-237 |
6.81e-04 |
|
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis domains [Transcription, Signal transduction mechanisms];
Pssm-ID: 443041 [Multi-domain] Cd Length: 448 Bit Score: 42.45 E-value: 6.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 111 QQLIDALPTLVWSTDADGTVTFVNQRWRTYTGLSREEaAEGGWIDAVHPEDRDRllaywQALRgAGTPgeIEGRLRRADG 190
Cdd:COG3829 14 EAILDSLDDGIIVVDADGRITYVNRAAERILGLPREE-VIGKNVTELIPNSPLL-----EVLK-TGKP--VTGVIQKTGG 84
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1720335109 191 HYRWFLFRGEPFRDaAGAVVQWFGSTTDI-HAGRLVREALKERERELR 237
Cdd:COG3829 85 KGKTVIVTAIPIFE-DGEVIGAVETFRDItELKRLERKLREEELERGL 131
|
|
| HATPase_BceS-YxdK-YvcQ-like |
cd16948 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
494-564 |
7.36e-04 |
|
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis BceS, YxdK, and Bacillus thuringiensis YvcQ; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Bacillus subtilis BceS and Bacillus thuringiensis YvcQ, the HKs of the two-component regulatory system (TCSs) BceS-BceR and YvcQ-YvcP, repsectively, which are both involved in regulating bacitracin resistance. It also includes the HATPase domain of YxdK, the HK of YxdK-YxdJ TCS involved in sensing antimicrobial compounds.
Pssm-ID: 340424 [Multi-domain] Cd Length: 109 Bit Score: 39.19 E-value: 7.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 494 IQQVLVNLVRNAMEAMRanietarvIVVRSRGADGQVQVEVADTGSGIAEPAL--IFEPLFT-------TKARGMGLGLA 564
Cdd:cd16948 10 IGQIVSNALKYSKQGGK--------IEIYSETNEQGVVLSIKDFGIGIPEEDLprVFDKGFTgengrnfQESTGMGLYLV 81
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
20-545 |
1.05e-03 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 42.17 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 20 RLSIATKGFLRSPRLLNPATVCAACLVVFWYVGDFVGAYHPQTIFRAGLLLLLAACAGLIIDYVNQIRASTDAMRAEMAV 99
Cdd:COG3321 860 RVPLPTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAA 939
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 100 VEQALHAQLYQQQLIDALPTLVWSTDADGTVTFVNQRWRTYTGLSREEAAEGGWIDAVHPEDRDRLLAYWQALRGAGTPG 179
Cdd:COG3321 940 AALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAA 1019
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 180 EIEGRLRRADGHYRWFLFRGEPFRDAAGAVVQWFGSTTDIHAGRLVREALKERERELRLIVDTVPALIYLVGSDGVPSYM 259
Cdd:COG3321 1020 ALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALAL 1099
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 260 NRRIQDYYGIAFDKLPQVDGAQVRAALEARVHPDDEPAVAAALKHAYATGEPFALRYRNYTADGVPRWVDGRVQPLRDDT 339
Cdd:COG3321 1100 AALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALAL 1179
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 340 GRVERWYGLVIDVEDEVRAQENLRAAQRKLARASQLASLAELSASIAHEVRQPLAAVVSNSQACQRWLSSQSLDLGRIRA 419
Cdd:COG3321 1180 ALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAAL 1259
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 420 IMDRIVRDANAAAATVTSVRALYANTATSRVSIDVNAVVEEARLLLADDLSKAATTFRAELDPDLPPVLADRIQIQQVLV 499
Cdd:COG3321 1260 AALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAVAA 1339
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1720335109 500 NLVRNAMEAMRANIETARVIVVRSRGADGQVQVEVADTGSGIAEPA 545
Cdd:COG3321 1340 ALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAAAV 1385
|
|
| HATPase_RstB-like |
cd16939 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
494-569 |
1.13e-03 |
|
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Salmonella typhimurium RstB; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Salmonella typhimurium RstB HK of the RstA-RstB two-component regulatory system (TCS), which regulates expression of the constituents participating in pyrimidine metabolism and iron acquisition, and may be required for regulation of Salmonella motility and invasion. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and a HAMP sensor domain.
Pssm-ID: 340416 [Multi-domain] Cd Length: 104 Bit Score: 38.57 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 494 IQQVLVNLVRNAMEAMRANIETArvivvrSRGADGQVQVEVADTGSGIAEPAL--IFEP---LFTTKAR---GMGLGLAV 565
Cdd:cd16939 1 MARALDNLLRNALRYAHRTVRIA------LLVSGGRLTLIVEDDGPGIPAAARerVFEPfvrLDPSRDRatgGFGLGLAI 74
|
....
gi 1720335109 566 SRSI 569
Cdd:cd16939 75 VHRV 78
|
|
| HisKA |
smart00388 |
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ... |
377-426 |
1.19e-03 |
|
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine kinases.
Pssm-ID: 214644 [Multi-domain] Cd Length: 66 Bit Score: 37.55 E-value: 1.19e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1720335109 377 SLAELSASIAHEVRQPLAAVVSNSQACQRW--LSSQSLDLGRIRAIMDRIVR 426
Cdd:smart00388 1 AKREFLANLSHELRTPLTAIRGYLELLLDTelSEEQREYLETILREAERLLR 52
|
|
| PRK10604 |
PRK10604 |
sensor protein RstB; Provisional |
375-569 |
1.30e-03 |
|
sensor protein RstB; Provisional
Pssm-ID: 236724 [Multi-domain] Cd Length: 433 Bit Score: 41.51 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 375 LASLAELSASIAHEVRQPLAAV-----------VSNSQACQRwlssqslDLGRIRAIMDRIVR----DANAAAATVTSVR 439
Cdd:PRK10604 209 IASKKQLIDGIAHELRTPLVRLryrlemsdnlsAAESQALNR-------DIGQLEALIEELLTyarlDRPQNELHLSEPD 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 440 AlyANTATSRVSiDVNAVVEEARLlladDLSKAATTFRAELDPDLppvladriqIQQVLVNLVRNAMeamRANIETARVI 519
Cdd:PRK10604 282 L--PAWLSTHLA-DIQAVTPEKTV----RLDTPHQGDYGALDMRL---------MERVLDNLLNNAL---RYAHSRVRVS 342
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720335109 520 VVRSrgaDGQVQVEVADTGSGIAEPAL--IFEPlFT-------TKARGMGLGLAVSRSI 569
Cdd:PRK10604 343 LLLD---GNQACLIVEDDGPGIPPEERerVFEP-FVrldpsrdRATGGCGLGLAIVHSI 397
|
|
| HATPase_CpxA-like |
cd16949 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
494-571 |
1.76e-03 |
|
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli CpxA; This family includes the histidine kinase-like ATPase (HATPase) domains of two-component sensor histidine kinase (HKs) similar to Escherichia coli CpxA, HK of the CpxA-CpxR two-component regulatory system (TCS) which may function in acid stress and in cell wall stability. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and a HAMP sensor domain; some also contain a CpxA family periplasmic domain.
Pssm-ID: 340425 [Multi-domain] Cd Length: 104 Bit Score: 38.08 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 494 IQQVLVNLVRNAMEAMRANIEtarvivVRSRGADGQVQVEVADTGSGIAEPAL--IFEPLF------TTKARGMGLGLAV 565
Cdd:cd16949 1 LARALENVLRNALRYSPSKIL------LDISQDGDQWTITITDDGPGVPEDQLeqIFLPFYrvdsarDRESGGTGLGLAI 74
|
....*.
gi 1720335109 566 SRSILE 571
Cdd:cd16949 75 AERAIE 80
|
|
| PRK13560 |
PRK13560 |
hypothetical protein; Provisional |
107-379 |
1.83e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 106506 [Multi-domain] Cd Length: 807 Bit Score: 41.20 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 107 QLYQQQLIDALPTLVW--STDADGTVTF--VNQRWRTYTGLSREE--AAEGGWIDAVHPEDRDRLLAywQALRGAGTPG- 179
Cdd:PRK13560 67 EQCERNLKANIPGGMFlfALDGDGTFSFpsLLDANGELAAIAKHDlmADKGLLAMLIGGDDGDFFFA--NPFRSAETIAm 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 180 --------EIEGRLRRADGHYRWFLFRgepFRDAAGAVVQWFGSTTDIHAGRLVREALKERERELRLIVDTVPALIYLVG 251
Cdd:PRK13560 145 alqsddwqEEEGHFRCGDGRFIDCCLR---FERHAHADDQVDGFAEDITERKRAEERIDEALHFLQQLLDNIADPAFWKD 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 252 SDGVPSYMNRRIQDYYGIAFDKLPQVDGAQVRAALEArvhpDDEPAVAAALKHAYATgEPFALRYRNytADGVPRWVDGR 331
Cdd:PRK13560 222 EDAKVFGCNDAACLACGFRREEIIGMSIHDFAPAQPA----DDYQEADAAKFDADGS-QIIEAEFQN--KDGRTRPVDVI 294
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1720335109 332 VQPLR--DDTGRVERWYGLVIDVEDEVRAQENLRAAQRKLARASQLASLA 379
Cdd:PRK13560 295 FNHAEfdDKENHCAGLVGAITDISGRRAAERELLEKEDMLRAIIEAAPIA 344
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
294-352 |
2.75e-03 |
|
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 463873 [Multi-domain] Cd Length: 93 Bit Score: 37.44 E-value: 2.75e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 294 DEPAVAAALKHAYATGEPF-ALRYRNYTADGVPRWVDGRVQPLRDDTGRVERWYGLVIDV 352
Cdd:pfam13426 32 AEPEDSERLREALREGKAVrEFEVVLYRKDGEPFPVLVSLAPIRDDGGELVGIIAILRDI 91
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
234-305 |
3.24e-03 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.
Pssm-ID: 214512 Cd Length: 67 Bit Score: 36.22 E-value: 3.24e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720335109 234 RELRLIVDTVPALIYLVGSDGVPSYMNRRIQDYYGIAFDKLPQVDGAQVraalearVHPDDEPAVAAALKHA 305
Cdd:smart00091 1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLEL-------IHPEDRERVQEALQRL 65
|
|
| HATPase_VanS-like |
cd16923 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
495-571 |
3.25e-03 |
|
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Enterococcus faecium VanS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Enterococcus faecium VanS HK of the VanS-VanR two-component regulatory system (TCS) which activates the transcription of vanH, vanA and vanX vancomycin resistance genes. It also contains Ecoli YedV and PcoS, probable members of YedW-YedV TCS and PcoS-PcoR TCS, repectively. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); most also have a HAMP sensor domain.
Pssm-ID: 340400 [Multi-domain] Cd Length: 102 Bit Score: 37.37 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 495 QQVLVNLVRNA----MEAMRANIETARvivvrsrgADGQVQVEVADTGSGIAE--PALIFEPLF-TTKAR---GMGLGLA 564
Cdd:cd16923 2 QRVFSNLLSNAikysPENTRIYITSFL--------TDDVVNIMFKNPSSHPLDfkLEKLFERFYrGDNSRnteGAGLGLS 73
|
....*..
gi 1720335109 565 VSRSILE 571
Cdd:cd16923 74 IAKAIIE 80
|
|
| PRK13558 |
PRK13558 |
bacterio-opsin activator; Provisional |
111-247 |
3.40e-03 |
|
bacterio-opsin activator; Provisional
Pssm-ID: 237426 [Multi-domain] Cd Length: 665 Bit Score: 40.21 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 111 QQLIDALP---TLVWSTDADGTVTFVNQRWRTYTGLSREEAAeGGWIDAVHPEDRD--RLLAYWQALRgAGTPGEIEGRL 185
Cdd:PRK13558 151 ERALDEAPvgiTIADATLPDEPLIYINDAFERITGYSPDEVL-GRNCRFLQGEDTNeeRVAELREAID-EERPTSVELRN 228
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720335109 186 RRADGHYRWFLFRGEPFRDAAGAVVQWFGSTTDIHAGRLVREALKERERELRLIVDTVPALI 247
Cdd:PRK13558 229 YRKDGSTFWNQVDIAPIRDEDGTVTHYVGFQTDVTERKEAELALQRERRKLQRLLERVEGLV 290
|
|
| HATPase_CreC-like |
cd16945 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
494-569 |
4.58e-03 |
|
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli CreC; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Escherichia coli CreC of the CreC-CreB two-component regulatory system (TCS) involved in catabolic regulation. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and accessory sensory domain(s) such as HAMP, CACHE or PAS.
Pssm-ID: 340421 [Multi-domain] Cd Length: 106 Bit Score: 37.05 E-value: 4.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 494 IQQVLVNLVRNAMEAMRANIEtarvIVVRSRGADGQVQVEVADTGSGIAEPAL--IFEPLFT-----TKARGMGLGLAVS 566
Cdd:cd16945 5 LRQAINNLLDNAIDFSPEGGL----IALQLEADTEGIELLVFDEGSGIPDYALnrVFERFYSlprphSGQKSTGLGLAFV 80
|
...
gi 1720335109 567 RSI 569
Cdd:cd16945 81 QEV 83
|
|
| phoR |
PRK11006 |
phosphate regulon sensor histidine kinase PhoR; |
452-565 |
6.14e-03 |
|
phosphate regulon sensor histidine kinase PhoR;
Pssm-ID: 182895 [Multi-domain] Cd Length: 430 Bit Score: 39.22 E-value: 6.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 452 IDVNAVVEEARLLL-----ADDLSKAATTFRAELDPDLPpVLADRIQIQQVLVNLVRNAMeamRANIETARVIVVRSRGA 526
Cdd:PRK11006 272 IDLNEKVDVPMMLRvlereAQTLSQGKHTITFEVDNSLK-VFGNEDQLRSAISNLVYNAV---NHTPEGTHITVRWQRVP 347
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1720335109 527 DGqVQVEVADTGSGIAEPALifePLFTT------KAR-----GMGLGLAV 565
Cdd:PRK11006 348 QG-AEFSVEDNGPGIAPEHI---PRLTErfyrvdKARsrqtgGSGLGLAI 393
|
|
| COG3920 |
COG3920 |
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ... |
87-563 |
6.24e-03 |
|
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction mechanisms];
Pssm-ID: 443125 [Multi-domain] Cd Length: 495 Bit Score: 39.50 E-value: 6.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 87 RASTDAMRAEMAVVEQALHAQLYQQQLIDALPTLVWSTDADGTVTFVNQRWRTYTGLSREEAAEGGWIDAVHPEDRDRLL 166
Cdd:COG3920 15 ALLLLAALLLLAAALLLALLALLLLALLLLALLLASALLALLALSAAALAAALAVALAAAVGAAAALLALLVLLLLLLLA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 167 AYWQALRGAGTPGEIEGRLRRADGHYRWFLFRGEPFRDAAGAVVQWFGSTTDIHAGRLVREALKERERELRLIVDTVPAL 246
Cdd:COG3920 95 AAALALALLLAALAGLLLLAALLLLRLVALLAALALLALLLLLLLLLAILALAELAVALAELAAALLLLAEELAALRLAA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 247 IYLVGSDGVPSYMNRRIQDYYGIAFDKLPQVDGAQVRAALEARVHPDDEPAVAAALKHAYATGEPFALRYRNYTADGVPR 326
Cdd:COG3920 175 AALLLLLAALLDLGLALAALAAAALLALLLALELLLALLLLLLLLLALLLVLLAALLRLRAAVLEELERRRRARGLGRLL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 327 WVDGRVQPLRDDTGRVERWyglVIDVEDEVRAQEnlRAAQRKLARASQLasLAELSasiaHEVRQPLAAVVS--NSQAcq 404
Cdd:COG3920 255 LLLLLLLLLLRALLLLAAG---IRLVITERKRAE--EELEASLEEKELL--LRELH----HRVKNNLQVVSSllRLQA-- 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 405 RWLSSQSLDlGRIRAIMDRIvrdanAAAATVTsvRALYANTATSRVSIDvnAVVEEarllLADDLSKAATTFRAELDPDL 484
Cdd:COG3920 322 RRADDPEAR-EALEESQNRI-----QALALVH--ELLYQSEDWEGVDLR--DYLRE----LLEPLRDSYGGRGIRIELDG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 485 PPVLADRIQIQQV--LVN-LVRNAMEAMRANIETARvIVVRSRGADGQVQVEVADTGSGIAEPALIfeplftTKARGMGL 561
Cdd:COG3920 388 PDVELPADAAVPLglILNeLVTNALKHAFLSGEGGR-IRVSWRREDGRLRLTVSDNGVGLPEDVDP------PARKGLGL 460
|
..
gi 1720335109 562 GL 563
Cdd:COG3920 461 RL 462
|
|
| YesM |
COG2972 |
Sensor histidine kinase YesM [Signal transduction mechanisms]; |
475-564 |
9.26e-03 |
|
Sensor histidine kinase YesM [Signal transduction mechanisms];
Pssm-ID: 442211 [Multi-domain] Cd Length: 445 Bit Score: 38.85 E-value: 9.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720335109 475 TFRAELDPDL-----PPVLadrIQIqqvlvnLVRNAMEAMRANIETARVIVVRSRGADGQVQVEVADTGSGIAEPAL--I 547
Cdd:COG2972 322 EVEIEIDEELldlliPKLI---LQP------LVENAIEHGIEPKEGGGTIRISIRKEGDRLVITVEDNGVGMPEEKLekL 392
|
90
....*....|....*..
gi 1720335109 548 FEPLfTTKARGMGLGLA 564
Cdd:COG2972 393 LEEL-SSKGEGRGIGLR 408
|
|
| |
