|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10618 |
PRK10618 |
phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional |
8-890 |
0e+00 |
|
phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional
Pssm-ID: 236726 [Multi-domain] Cd Length: 894 Bit Score: 1531.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 8 APSKFSLLPGSITRFFLLLIVVLLVTMGVMVQSAVNAWLKDKSYQVVDITHAVHKRIDTWRYATWQIYDNIAAAPATSSG 87
Cdd:PRK10618 1 ATTRFSLLPGSITRFFLLFIILLLVTMGLMVYNYVNAWLKDKKYAIVDIAHAIQKRIDTYRYVTWQIYDNIAATTSPSSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 88 EGLQETRLKQDVYYLEKPQRKTEALIFGSHDSATLEMTQRISTYLDTLWGAETVPWSMYYLNGQDNSMILISTLPLKDLS 167
Cdd:PRK10618 81 EGLQETRLRPDVYYLEKPRRKTDALIFGSHDSSTLEMTQRMSTYLDTLWGAENVPWSMYYLNGQDNSLILISTLPLKDLS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 168 SGFKETTVGSIVDSRRAEMLQQANALDERESFSSLRRLAWQNGHYFTLRTTFNQPGHLATVVAFDLPINDLIPPDMPLDS 247
Cdd:PRK10618 161 SRFKESYLSNIVESRRAEMLQQANALDERESFSPLRKLRWQNGYYFTLRTTFNQPGHLATVIAFDLPINDLIPPGMPLDN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 248 FRLEPDNSTQNMRaAADKEAVESVSISFNGSKIEIASSLNSTGMRLVWQVPFGTLLLDTLQNILLPLLLNIGLLALALFG 327
Cdd:PRK10618 241 FRLEPDATATNND-DNEKEGTDSVSISFNGSWIEISAALNSTPLKLVYQVPLGTLLLDLLQNNLWPLLLNLGLLALSLFG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 328 YSTFRFQPGRQSDAstvpagTSNELRVLRALNEEIISVLPLGVLVHDQEANRTVMSNKIADHLLPHLNLQNITTMADQHQ 407
Cdd:PRK10618 320 YYTFRHQYGRPTES------MSHELRILRALNEEIVSNLPLGLLVYDFESNRTVISNKIADHLLPHLNLQKITTMAEQHQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 408 GIIQATINNELYEIRQFRSQVASRTQIFIIRDQDREVLVNKKLKQAQRLYEKNQQGRAAFMQNIGDAFKQPLRALATQAA 487
Cdd:PRK10618 394 GVIQATINNELYEIRMFRSQLAPRTQLFLLRDQDREVLVNKKLQQAQREYEKNQQARKAFLQNIGDELKQPLQSLAQLAA 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 488 AL--------STPDSQQLASQADSLVRMVDEIQLANMLENDFWKGTPTLFSIQDLIDEVVPDVLPVIKRKGLQLLINNHL 559
Cdd:PRK10618 474 QLrqtsdeeqQQPELDQLAEQSDVLVRLVDNIQLLNMLETQDWKPEQELFSLQDLIDEVLPEVLPAIKRKGLQLLIHNHL 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 560 PANDERHGDREALRRILLMIIQYAVTTTQIGKITLEVNTDESAEDRLTFRILDTGEGVTTSEIDNLHFPFLNDTQSDHYG 639
Cdd:PRK10618 554 KAEQLRIGDRDALRKILLLLLNYAITTTAYGKITLEVDQDESSPDRLTIRILDTGAGVSIKELDNLHFPFLNQTQGDRYG 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 640 KANALTFWLCDQLARKLGGHLNIKARESLGTRYSLHVKMAA--NPQEEDEERLLDDVIVMVDVTSNEIRNIVVRQLENWG 717
Cdd:PRK10618 634 KASGLTFFLCNQLCRKLGGHLTIKSREGLGTRYSIHLKMLAadPEVEEEEEKLLDGVTVLLDITSEEVRKIVTRQLENWG 713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 718 AACITPDERLSSQEFDLFLTDNPSNLTASGLLLSDDEPGVRKIGPGQLRVNFNISNAMQEAVLQLIEEQLAQEEIAESPL 797
Cdd:PRK10618 714 ATCITPDERLISQEYDIFLTDNPSNLTASTLLLSDDESGFRQIGPGQLRVNFNISNAMQEAILQLIEQQLAQEEVTESPL 793
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 798 GGNENA------ELHASGYYSLFVDTVPDDVKRLYTESAANDFAALAQTAHRLKGVFAMLNLVPGKQLCETLEHLIREKD 871
Cdd:PRK10618 794 GGDENAlnfyqkQLHASDYYALFVDTVPDDVKRLYTEAATSDFASLAQTAHRLKGVFAMLNLVPGKQLCETLEHLIREKD 873
|
890
....*....|....*....
gi 504645629 872 ASGIEKYISDIDAYVKSLL 890
Cdd:PRK10618 874 EPGIENYISDIDSFVKSLL 892
|
|
| RcsD_ABL |
pfam16359 |
RcsD-ABL domain; This domain is part of the RcsD histidine kinase. It recognizes the effector ... |
688-790 |
3.93e-51 |
|
RcsD-ABL domain; This domain is part of the RcsD histidine kinase. It recognizes the effector domain of RcsB.
Pssm-ID: 435297 [Multi-domain] Cd Length: 103 Bit Score: 174.40 E-value: 3.93e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 688 ERLLDDVIVMVDVTSNEIRNIVVRQLENWGAACITPDERLSSQEFDLFLTDNPSNLTASGLLLSDDEPGVRKIGPGQLRV 767
Cdd:pfam16359 1 EKLLEDITVLLDITSPEVRKIVTRMLENWGATCFDKDERLISQEYDILLTDDPSNLAKSTLLLSDDESGVRQIGPGRLRV 80
|
90 100
....*....|....*....|...
gi 504645629 768 NFNISNAMQEAVLQLIEEQLAQE 790
Cdd:pfam16359 81 NYNISDALLEAILQLIEQQLSED 103
|
|
| BaeS |
COG0642 |
Signal transduction histidine kinase [Signal transduction mechanisms]; |
352-679 |
4.55e-19 |
|
Signal transduction histidine kinase [Signal transduction mechanisms];
Pssm-ID: 440407 [Multi-domain] Cd Length: 328 Bit Score: 89.20 E-value: 4.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 352 LRVLRALNEEIISVLPLGVLVHDQEANRTVMSNKIADHLLPHLNLQNITTMADQHQGIIQATINNELYEIRQFRSQVASR 431
Cdd:COG0642 2 LLLLLLLVLLLLLLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 432 TQIFIIRDQDREVLVNKKLKQAQRLyeknQQGRAAFMQNIGDAFKQPLRALATQAAAL-STPDSQQ------LASQADSL 504
Cdd:COG0642 82 LLLLLLLLLLLLLLLLALLLLLEEA----NEAKSRFLANVSHELRTPLTAIRGYLELLlEELDEEQreyletILRSADRL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 505 VRMVDEIQLANMLENDFWKGTPTLFSIQDLIDEVVPDVLPVIKRKGLQLLInnHLPANDER-HGDREALRRILLMIIQYA 583
Cdd:COG0642 158 LRLINDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELEL--DLPDDLPTvRGDPDRLRQVLLNLLSNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 584 VT-TTQIGKITLEVNTDesaEDRLTFRILDTGEGVTTSEIDNLHFPFL---NDTQSDHYGkanaLTFWLCDQLARKLGGH 659
Cdd:COG0642 236 IKyTPEGGTVTVSVRRE---GDRVRISVEDTGPGIPPEDLERIFEPFFrtdPSRRGGGTG----LGLAIVKRIVELHGGT 308
|
330 340
....*....|....*....|
gi 504645629 660 LNIKARESLGTRYSLHVKMA 679
Cdd:COG0642 309 IEVESEPGKGTTFTVTLPLA 328
|
|
| HATPase_ETR2_ERS2-EIN4-like |
cd16938 |
Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related ... |
539-676 |
2.52e-18 |
|
Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related domains; This family includes the histidine kinase-like ATPase domains (HATPase) of three out of the five receptors that recognize the plant hormone ethylene in Arabidopsis thaliana. These three proteins have been classified as belonging to subfamily 2: ETR2, ERS2, and EIN4. They lack most of the motifs characteristic of histidine kinases, and EIN4 is the only one in this group containing the conserved histidine that is phosphorylated in two-component and phosphorelay systems. This family also includes the HATPase domains of Escherichia coli RcsD phosphotransferase which is a component of the Rcs-signaling system, a complex multistep phosphorelay involving five proteins, and is involved in many transcriptional networks such as cell division, biofilm formation, and virulence, among others. Also included is Schizosaccharomyces pombe Mak3 (Phk1) which participates in a multi-step two-component related system which regulates H2O2-induced activation of the Sty1 stress-activated protein kinase pathway. Most proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and a GAF sensor domain; most are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.
Pssm-ID: 340415 [Multi-domain] Cd Length: 133 Bit Score: 82.12 E-value: 2.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 539 VPDVLPVIKRKGLQLLINNHLPANDERHGDREALRRILLMIIQYAVTTTQIGKITlEVNTDESAEDRLTFRILDTGEGVT 618
Cdd:cd16938 1 LPDVVVGDERRVFQVLLHMLGNLLKMRNGGGNITFRVFLEGGSEDRSDRDWGPWR-PSMSDESVEIRFEVEINDSGSPSI 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504645629 619 TSeidnlhfPFLNDTQSDHY---GKANALTFWLCDQLARKLGGHLNIKARESLGTRYSLHV 676
Cdd:cd16938 80 ES-------ASMRNSLNRRYnlsELGEHLSFSICKQLVQLMGGNIWIVPGSGLGTTMSLLL 133
|
|
| HATPase_c |
smart00387 |
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases. |
567-679 |
7.37e-12 |
|
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
Pssm-ID: 214643 [Multi-domain] Cd Length: 111 Bit Score: 62.67 E-value: 7.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 567 GDREALRRILLMIIQYAV-TTTQIGKITLEVNTDEsaeDRLTFRILDTGEGVTTSEIDNLHFPFLNDTQSDHYGKANALT 645
Cdd:smart00387 1 GDPDRLRQVLSNLLDNAIkYTPEGGRITVTLERDG---DHVEITVEDNGPGIPPEDLEKIFEPFFRTDKRSRKIGGTGLG 77
|
90 100 110
....*....|....*....|....*....|....
gi 504645629 646 FWLCDQLARKLGGHLNIKARESLGTRYSLHVKMA 679
Cdd:smart00387 78 LSIVKKLVELHGGEISVESEPGGGTTFTITLPLE 111
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10618 |
PRK10618 |
phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional |
8-890 |
0e+00 |
|
phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional
Pssm-ID: 236726 [Multi-domain] Cd Length: 894 Bit Score: 1531.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 8 APSKFSLLPGSITRFFLLLIVVLLVTMGVMVQSAVNAWLKDKSYQVVDITHAVHKRIDTWRYATWQIYDNIAAAPATSSG 87
Cdd:PRK10618 1 ATTRFSLLPGSITRFFLLFIILLLVTMGLMVYNYVNAWLKDKKYAIVDIAHAIQKRIDTYRYVTWQIYDNIAATTSPSSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 88 EGLQETRLKQDVYYLEKPQRKTEALIFGSHDSATLEMTQRISTYLDTLWGAETVPWSMYYLNGQDNSMILISTLPLKDLS 167
Cdd:PRK10618 81 EGLQETRLRPDVYYLEKPRRKTDALIFGSHDSSTLEMTQRMSTYLDTLWGAENVPWSMYYLNGQDNSLILISTLPLKDLS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 168 SGFKETTVGSIVDSRRAEMLQQANALDERESFSSLRRLAWQNGHYFTLRTTFNQPGHLATVVAFDLPINDLIPPDMPLDS 247
Cdd:PRK10618 161 SRFKESYLSNIVESRRAEMLQQANALDERESFSPLRKLRWQNGYYFTLRTTFNQPGHLATVIAFDLPINDLIPPGMPLDN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 248 FRLEPDNSTQNMRaAADKEAVESVSISFNGSKIEIASSLNSTGMRLVWQVPFGTLLLDTLQNILLPLLLNIGLLALALFG 327
Cdd:PRK10618 241 FRLEPDATATNND-DNEKEGTDSVSISFNGSWIEISAALNSTPLKLVYQVPLGTLLLDLLQNNLWPLLLNLGLLALSLFG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 328 YSTFRFQPGRQSDAstvpagTSNELRVLRALNEEIISVLPLGVLVHDQEANRTVMSNKIADHLLPHLNLQNITTMADQHQ 407
Cdd:PRK10618 320 YYTFRHQYGRPTES------MSHELRILRALNEEIVSNLPLGLLVYDFESNRTVISNKIADHLLPHLNLQKITTMAEQHQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 408 GIIQATINNELYEIRQFRSQVASRTQIFIIRDQDREVLVNKKLKQAQRLYEKNQQGRAAFMQNIGDAFKQPLRALATQAA 487
Cdd:PRK10618 394 GVIQATINNELYEIRMFRSQLAPRTQLFLLRDQDREVLVNKKLQQAQREYEKNQQARKAFLQNIGDELKQPLQSLAQLAA 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 488 AL--------STPDSQQLASQADSLVRMVDEIQLANMLENDFWKGTPTLFSIQDLIDEVVPDVLPVIKRKGLQLLINNHL 559
Cdd:PRK10618 474 QLrqtsdeeqQQPELDQLAEQSDVLVRLVDNIQLLNMLETQDWKPEQELFSLQDLIDEVLPEVLPAIKRKGLQLLIHNHL 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 560 PANDERHGDREALRRILLMIIQYAVTTTQIGKITLEVNTDESAEDRLTFRILDTGEGVTTSEIDNLHFPFLNDTQSDHYG 639
Cdd:PRK10618 554 KAEQLRIGDRDALRKILLLLLNYAITTTAYGKITLEVDQDESSPDRLTIRILDTGAGVSIKELDNLHFPFLNQTQGDRYG 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 640 KANALTFWLCDQLARKLGGHLNIKARESLGTRYSLHVKMAA--NPQEEDEERLLDDVIVMVDVTSNEIRNIVVRQLENWG 717
Cdd:PRK10618 634 KASGLTFFLCNQLCRKLGGHLTIKSREGLGTRYSIHLKMLAadPEVEEEEEKLLDGVTVLLDITSEEVRKIVTRQLENWG 713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 718 AACITPDERLSSQEFDLFLTDNPSNLTASGLLLSDDEPGVRKIGPGQLRVNFNISNAMQEAVLQLIEEQLAQEEIAESPL 797
Cdd:PRK10618 714 ATCITPDERLISQEYDIFLTDNPSNLTASTLLLSDDESGFRQIGPGQLRVNFNISNAMQEAILQLIEQQLAQEEVTESPL 793
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 798 GGNENA------ELHASGYYSLFVDTVPDDVKRLYTESAANDFAALAQTAHRLKGVFAMLNLVPGKQLCETLEHLIREKD 871
Cdd:PRK10618 794 GGDENAlnfyqkQLHASDYYALFVDTVPDDVKRLYTEAATSDFASLAQTAHRLKGVFAMLNLVPGKQLCETLEHLIREKD 873
|
890
....*....|....*....
gi 504645629 872 ASGIEKYISDIDAYVKSLL 890
Cdd:PRK10618 874 EPGIENYISDIDSFVKSLL 892
|
|
| RcsD_ABL |
pfam16359 |
RcsD-ABL domain; This domain is part of the RcsD histidine kinase. It recognizes the effector ... |
688-790 |
3.93e-51 |
|
RcsD-ABL domain; This domain is part of the RcsD histidine kinase. It recognizes the effector domain of RcsB.
Pssm-ID: 435297 [Multi-domain] Cd Length: 103 Bit Score: 174.40 E-value: 3.93e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 688 ERLLDDVIVMVDVTSNEIRNIVVRQLENWGAACITPDERLSSQEFDLFLTDNPSNLTASGLLLSDDEPGVRKIGPGQLRV 767
Cdd:pfam16359 1 EKLLEDITVLLDITSPEVRKIVTRMLENWGATCFDKDERLISQEYDILLTDDPSNLAKSTLLLSDDESGVRQIGPGRLRV 80
|
90 100
....*....|....*....|...
gi 504645629 768 NFNISNAMQEAVLQLIEEQLAQE 790
Cdd:pfam16359 81 NYNISDALLEAILQLIEQQLSED 103
|
|
| BaeS |
COG0642 |
Signal transduction histidine kinase [Signal transduction mechanisms]; |
352-679 |
4.55e-19 |
|
Signal transduction histidine kinase [Signal transduction mechanisms];
Pssm-ID: 440407 [Multi-domain] Cd Length: 328 Bit Score: 89.20 E-value: 4.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 352 LRVLRALNEEIISVLPLGVLVHDQEANRTVMSNKIADHLLPHLNLQNITTMADQHQGIIQATINNELYEIRQFRSQVASR 431
Cdd:COG0642 2 LLLLLLLVLLLLLLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 432 TQIFIIRDQDREVLVNKKLKQAQRLyeknQQGRAAFMQNIGDAFKQPLRALATQAAAL-STPDSQQ------LASQADSL 504
Cdd:COG0642 82 LLLLLLLLLLLLLLLLALLLLLEEA----NEAKSRFLANVSHELRTPLTAIRGYLELLlEELDEEQreyletILRSADRL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 505 VRMVDEIQLANMLENDFWKGTPTLFSIQDLIDEVVPDVLPVIKRKGLQLLInnHLPANDER-HGDREALRRILLMIIQYA 583
Cdd:COG0642 158 LRLINDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELEL--DLPDDLPTvRGDPDRLRQVLLNLLSNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 584 VT-TTQIGKITLEVNTDesaEDRLTFRILDTGEGVTTSEIDNLHFPFL---NDTQSDHYGkanaLTFWLCDQLARKLGGH 659
Cdd:COG0642 236 IKyTPEGGTVTVSVRRE---GDRVRISVEDTGPGIPPEDLERIFEPFFrtdPSRRGGGTG----LGLAIVKRIVELHGGT 308
|
330 340
....*....|....*....|
gi 504645629 660 LNIKARESLGTRYSLHVKMA 679
Cdd:COG0642 309 IEVESEPGKGTTFTVTLPLA 328
|
|
| HATPase_ETR2_ERS2-EIN4-like |
cd16938 |
Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related ... |
539-676 |
2.52e-18 |
|
Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related domains; This family includes the histidine kinase-like ATPase domains (HATPase) of three out of the five receptors that recognize the plant hormone ethylene in Arabidopsis thaliana. These three proteins have been classified as belonging to subfamily 2: ETR2, ERS2, and EIN4. They lack most of the motifs characteristic of histidine kinases, and EIN4 is the only one in this group containing the conserved histidine that is phosphorylated in two-component and phosphorelay systems. This family also includes the HATPase domains of Escherichia coli RcsD phosphotransferase which is a component of the Rcs-signaling system, a complex multistep phosphorelay involving five proteins, and is involved in many transcriptional networks such as cell division, biofilm formation, and virulence, among others. Also included is Schizosaccharomyces pombe Mak3 (Phk1) which participates in a multi-step two-component related system which regulates H2O2-induced activation of the Sty1 stress-activated protein kinase pathway. Most proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and a GAF sensor domain; most are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.
Pssm-ID: 340415 [Multi-domain] Cd Length: 133 Bit Score: 82.12 E-value: 2.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 539 VPDVLPVIKRKGLQLLINNHLPANDERHGDREALRRILLMIIQYAVTTTQIGKITlEVNTDESAEDRLTFRILDTGEGVT 618
Cdd:cd16938 1 LPDVVVGDERRVFQVLLHMLGNLLKMRNGGGNITFRVFLEGGSEDRSDRDWGPWR-PSMSDESVEIRFEVEINDSGSPSI 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504645629 619 TSeidnlhfPFLNDTQSDHY---GKANALTFWLCDQLARKLGGHLNIKARESLGTRYSLHV 676
Cdd:cd16938 80 ES-------ASMRNSLNRRYnlsELGEHLSFSICKQLVQLMGGNIWIVPGSGLGTTMSLLL 133
|
|
| KdpD |
COG2205 |
K+-sensing histidine kinase KdpD [Signal transduction mechanisms]; |
449-676 |
1.71e-15 |
|
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
Pssm-ID: 441807 [Multi-domain] Cd Length: 239 Bit Score: 76.87 E-value: 1.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 449 KLKQAQRLYEKNQQGRAAFMQNIGDAFKQPLRALATQAAAL------STPDSQQLA----SQADSLVRMVDEIQLANMLE 518
Cdd:COG2205 1 ELEEALEELEELERLKSEFLANVSHELRTPLTSILGAAELLldeedlSPEERRELLeiirESAERLLRLIEDLLDLSRLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 519 NDFWKGTPTLFSIQDLIDEVVPDVLPVIKRKGLQLLInnHLPANDER-HGDREALRRILLMIIQYAVT-TTQIGKITLEV 596
Cdd:COG2205 81 SGKLSLELEPVDLAELLEEAVEELRPLAEEKGIRLEL--DLPPELPLvYADPELLEQVLANLLDNAIKySPPGGTITISA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 597 ntdESAEDRLTFRILDTGEGVTTSEIDNLHFPF---LNDTQSDHYGkanaLTFWLCDQLARKLGGHLNIKARESLGTRYS 673
Cdd:COG2205 159 ---RREGDGVRISVSDNGPGIPEEELERIFERFyrgDNSRGEGGTG----LGLAIVKRIVEAHGGTIWVESEPGGGTTFT 231
|
...
gi 504645629 674 LHV 676
Cdd:COG2205 232 VTL 234
|
|
| HATPase_c |
pfam02518 |
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ... |
567-679 |
1.41e-12 |
|
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: 64.70 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 567 GDREALRRILLMIIQYAVT-TTQIGKITLEVntdeSAEDRLTFRILDTGEGVTTSEIDNLHFPFLNDTQSDHYGkaNALT 645
Cdd:pfam02518 1 GDELRLRQVLSNLLDNALKhAAKAGEITVTL----SEGGELTLTVEDNGIGIPPEDLPRIFEPFSTADKRGGGG--TGLG 74
|
90 100 110
....*....|....*....|....*....|....
gi 504645629 646 FWLCDQLARKLGGHLNIKARESLGTRYSLHVKMA 679
Cdd:pfam02518 75 LSIVRKLVELLGGTITVESEPGGGTTVTLTLPLA 108
|
|
| HATPase_c |
smart00387 |
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases. |
567-679 |
7.37e-12 |
|
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
Pssm-ID: 214643 [Multi-domain] Cd Length: 111 Bit Score: 62.67 E-value: 7.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 567 GDREALRRILLMIIQYAV-TTTQIGKITLEVNTDEsaeDRLTFRILDTGEGVTTSEIDNLHFPFLNDTQSDHYGKANALT 645
Cdd:smart00387 1 GDPDRLRQVLSNLLDNAIkYTPEGGRITVTLERDG---DHVEITVEDNGPGIPPEDLEKIFEPFFRTDKRSRKIGGTGLG 77
|
90 100 110
....*....|....*....|....*....|....
gi 504645629 646 FWLCDQLARKLGGHLNIKARESLGTRYSLHVKMA 679
Cdd:smart00387 78 LSIVKKLVELHGGEISVESEPGGGTTFTITLPLE 111
|
|
| Hpt |
pfam01627 |
Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module ... |
810-889 |
1.65e-11 |
|
Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module with an active histidine residue that mediates phosphotransfer reactions in the two-component signaling systems. A multistep phosphorelay involving the HPt domain has been suggested for these signaling pathways. The crystal structure of the HPt domain of the anaerobic sensor kinase ArcB has been determined. The domain consists of six alpha helices containing a four-helix bundle-folding. The pattern of sequence similarity of the HPt domains of ArcB and components in other signaling systems can be interpreted in light of the three-dimensional structure and supports the conclusion that the HPt domains have a common structural motif both in prokaryotes and eukaryotes. In S. cerevisiae ypd1p this domain has been shown to contain a binding surface for Ssk1p (response regulator receiver domain containing protein pfam00072).
Pssm-ID: 426352 [Multi-domain] Cd Length: 84 Bit Score: 60.83 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 810 YYSLFVDTVPDDVKRLYTESAANDFAALAQTAHRLKGVFAMLNLVPGKQLCETLEHLIREKDASGIEKYISDIDAYVKSL 889
Cdd:pfam01627 2 LLELFLEEAPELLEQLEQALDAEDLEALFRAAHTLKGSAGSLGLPALAELAHELEDLLREGELPLDPELLEALRDLLEAL 81
|
|
| PRK15347 |
PRK15347 |
two component system sensor kinase; |
549-731 |
5.56e-10 |
|
two component system sensor kinase;
Pssm-ID: 237951 [Multi-domain] Cd Length: 921 Bit Score: 63.12 E-value: 5.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 549 KGLQL--LINNHLPAndERHGDREALRRILLMIIQYAVTTTQIGKITLEVntdESAEDRLTFRILDTGEGVTTSEIDNLH 626
Cdd:PRK15347 491 KSLTLrtFVGAHVPL--YLHLDSLRLRQILVNLLGNAVKFTETGGIRLRV---KRHEQQLCFTVEDTGCGIDIQQQQQIF 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 627 FPFLndtQSDHYGKANALTFWLCDQLARKLGGHLNIKARESLGTRYSLhvkmaanpqeedeerllddVIVMVDVTSNEIR 706
Cdd:PRK15347 566 TPFY---QADTHSQGTGLGLTIASSLAKMMGGELTLFSTPGVGSCFSL-------------------VLPLNEYAPPEPL 623
|
170 180 190
....*....|....*....|....*....|....
gi 504645629 707 N--IVV-----RQLENWGAACI--TPDERLSSQE 731
Cdd:PRK15347 624 KgeLSAplalhRQLSAWGITCQpgHQNPALLDPE 657
|
|
| HPT |
cd00088 |
Histidine Phosphotransfer domain, involved in signalling through a two part component systems ... |
808-889 |
5.10e-09 |
|
Histidine Phosphotransfer domain, involved in signalling through a two part component systems in which an autophosphorylating histidine protein kinase serves as a phosphoryl donor to a response regulator protein; the response regulator protein is modulated by phosphorylation and dephosphorylation of a conserved aspartic acid residue; two-component proteins are abundant in most eubacteria; In E. coli there are 62 two-component proteins involved in a variety of processes such as chemotaxis, osmoregulation, metabolism and transport 1; also present in both Gram positive and Gram negative pathogenic bacteria where they regulate basic housekeeping functions and control expression of toxins and other proteins important for pathogenesis; in archaea and eukaryotes, two-component pathways constitute a very small number of all signaling systems; in fungi they mediate environmental stress responses and, in pathogenic yeast, hyphal development. In Dictyostelium and in plants, they are involved in important processes such as osmoregulation, cell growth, and differentiation; to date two-component proteins have not been identified in animals; in most prokaryotic systems, the output response is effected directly by the RR, which functions as a transcription factor while in eukaryotic systems, two-component proteins are found at the beginning of signaling pathways where they interface with more conventional eukaryotic signaling strategies such as MAP kinase and cyclic nucleotide cascades
Pssm-ID: 238041 [Multi-domain] Cd Length: 94 Bit Score: 54.31 E-value: 5.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 808 SGYYSLFVDTVPDDVKRLYTE----SAANDFAALAQTAHRLKGVFAMLNLVPGKQLCETLEHLIREkDASGIEKYISDID 883
Cdd:cd00088 2 EELLELFLEEAEELLEELERAllelEDAEDLNEIFRAAHTLKGSAASLGLQRLAQLAHQLEDLLDA-LRDGLEVTPELID 80
|
....*.
gi 504645629 884 AYVKSL 889
Cdd:cd00088 81 LLLDAL 86
|
|
| PRK11091 |
PRK11091 |
aerobic respiration control sensor protein ArcB; Provisional |
549-738 |
6.94e-09 |
|
aerobic respiration control sensor protein ArcB; Provisional
Pssm-ID: 236842 [Multi-domain] Cd Length: 779 Bit Score: 59.57 E-value: 6.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 549 KGLQLL--INNHLPANDERHGDReaLRRILLMIIQYAVTTTQIGKITLEVNTDEsaEDRLTFRILDTGEGVTTSEIDNLh 626
Cdd:PRK11091 376 KGLRFDlePLLPLPHKVITDGTR--LRQILWNLISNAVKFTQQGGVTVRVRYEE--GDMLTFEVEDSGIGIPEDELDKI- 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 627 FPFLNDTQSDHYGKANALT---FWLCDQLARKLGGHLNIKARESLGTRYSLHVKMAANPQEEDEERLLDDV------IVM 697
Cdd:PRK11091 451 FAMYYQVKDSHGGKPATGTgigLAVSKRLAQAMGGDITVTSEEGKGSCFTLTIHAPAVAEEVEDAFDEDDMplpalnILL 530
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 504645629 698 V-DVtsnEIRNIVVRQ-LENWGAACI---TPDERLSS---QEFDLFLTD 738
Cdd:PRK11091 531 VeDI---ELNVIVARSvLEKLGNSVDvamTGKEALEMfdpDEYDLVLLD 576
|
|
| HPtr |
COG2198 |
HPt (histidine-containing phosphotransfer) domain [Signal transduction mechanisms]; |
177-890 |
8.71e-09 |
|
HPt (histidine-containing phosphotransfer) domain [Signal transduction mechanisms];
Pssm-ID: 441800 [Multi-domain] Cd Length: 871 Bit Score: 59.29 E-value: 8.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 177 SIVDSRRAEMLQQANALDERESFSSLRRLAWQNGHYFTLRTTFNQPGHLATVVAFDLPINDLIPPDMPLDSFRLEPDNST 256
Cdd:COG2198 120 LLLLLLLLLLLLLALLLLLLLLLALLLLLLLLLVLAALLLLLLLALLLALLLLVLLVLLLLLLLLLLLLLLLLLLLLLLL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 257 QNMRAAADKEAVESVSISFNGSKIEIASSLNSTGMRLVWQVPFGTLLLDTLQNILLPLLLNIGLLALALFGYSTFRFQPG 336
Cdd:COG2198 200 LALTLAALLELLAAELALEALLAELAAEAAAALAAELALAELAALLLLLLLLLLLLILLLLLLLLLLLLLLLLLLLLLLL 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 337 RQSDASTVPAGTSNELRVLRALNEEIISVLPLGVLVHDQEANRTVMSNKIADHLLPHLNLQNITTMADQHQGIIQATINN 416
Cdd:COG2198 280 LLLLLLLLLLLLLLLLLLLLELLLLLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLLLALLLA 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 417 ELYEIRQFRSQVASRTQIFIIRDQDREVLVNKKLKQAQRLYEKNQQGRAAFMQNIGDAFKQPLRALATQAAALSTPDSQQ 496
Cdd:COG2198 360 LLLAAAAALAAALEALLTELALILLLLLLLLLLLILLGLLLLLLLSLLLSLLLLLLLLLLLLLLLLLLLLLLLLLLLLLL 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 497 LASQADSLVRMVDEIQLANMLENDFWKGTPTLFSIQDLIDEVVPDVLPVIKRKGLQLLINNHLPANDERHGDREALRRIL 576
Cdd:COG2198 440 LGLLLLLLLLLGLLLLLLLGLLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVAAALAALALLLL 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 577 LMIIQYAVTTTQIGKITLEVNTDESAEDRLTFRILDTGEGVTTSEIDNLHFPFLNDTQSDHYGKANALTFWLCDQLARKL 656
Cdd:COG2198 520 LALLLLLLLDLLILGLLLILLLLLLGLLALGLAALLLLLALLLGLGLLLGLLLGGLLLLLLLLLLLLLLLLLLLLLLLLL 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 657 GGHLNIKARESLGTRYSLHVKMAANPQEEDEERLLDDVIVMVDVTSNEIRNIVVRQLENWGAAC---------------- 720
Cdd:COG2198 600 LALLLALLAAAAALLLLLLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAVLLAAAAAAAalaaldllldlddmmm 679
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 721 ----ITPDERLSSQEFDLFLTDNPSNLTASGLLLSDDEPGVRKIGPGQLRVNFNISNAMQEAVLQLIEEQLAQEEIAESP 796
Cdd:COG2198 680 mlddMMAEAARARALAARAAAIAAAAAAAAAAAAAAAAAAAALLAALLLLLLLLLLLLLLLLLLLLAAAAAAAASPAAPA 759
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 797 LGGNENAELHASG--------YYSLFVDTVPDDVKRLYTESAANDFAALAQTAHRLKGVFAMLNLVPGKQLCETLEHLIR 868
Cdd:COG2198 760 LPVLDLEALRRLGgdpellreLLELFLEELPELLAELRQALAAGDLEALARLAHKLKGSAGNLGAPRLAELAAELEQAAR 839
|
730 740
....*....|....*....|..
gi 504645629 869 EKDASGIEKYISDIDAYVKSLL 890
Cdd:COG2198 840 AGDLEEAEELLAELEAELERVL 861
|
|
| NtrY |
COG5000 |
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
350-629 |
1.26e-07 |
|
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: 54.97 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 350 NELRVLRALNEEIISVLPLGVLVHDQEaNRTVMSNKIADHLLphlnlqNITTMADQHQGIIQATINNELYEIRQFRSQVA 429
Cdd:COG5000 83 EELEERRRYLETILENLPAGVIVLDAD-GRITLANPAAERLL------GIPLEELIGKPLEELLPELDLAELLREALERG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 430 SRTQIFIIRDQDREVLVNK----------------KLKQAQRLyeknqqgrAA---FMQNIGDAFKQPLRALATQAAALS 490
Cdd:COG5000 156 WQEEIELTRDGRRTLLVRAsplrddgyvivfdditELLRAERL--------AAwgeLARRIAHEIKNPLTPIQLSAERLR 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 491 TPDSQQLASQADSLVRMVDEIQ-----LANMLEN--DFWKG---TPTLFSIQDLIDEVVPDVLPVIKRKGLQllINNHLP 560
Cdd:COG5000 228 RKLADKLEEDREDLERALDTIIrqvdrLKRIVDEflDFARLpepQLEPVDLNELLREVLALYEPALKEKDIR--LELDLD 305
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504645629 561 ANDER-HGDREALRRILLMIIQYAVT-TTQIGKITLEVNTDEsaeDRLTFRILDTGEGVTTSEIDNLhF-PF 629
Cdd:COG5000 306 PDLPEvLADRDQLEQVLINLLKNAIEaIEEGGEIEVSTRRED---GRVRIEVSDNGPGIPEEVLERI-FePF 373
|
|
| HATPase_EvgS-ArcB-TorS-like |
cd16922 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ... |
572-678 |
5.39e-06 |
|
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: 45.95 E-value: 5.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 572 LRRILLMIIQYAVTTTQIGKITLEVN--TDESAEDRLTFRILDTGEGVTTSEIDNLHFPFlndTQSDH-----YGkANAL 644
Cdd:cd16922 1 LRQILLNLLGNAIKFTEEGEVTLRVSleEEEEDGVQLRFSVEDTGIGIPEEQQARLFEPF---SQADSsttrkYG-GTGL 76
|
90 100 110
....*....|....*....|....*....|....
gi 504645629 645 TFWLCDQLARKLGGHLNIKARESLGTRYSLHVKM 678
Cdd:cd16922 77 GLAISKKLVELMGGDISVESEPGQGSTFTFTLPL 110
|
|
| PRK10841 |
PRK10841 |
two-component system sensor histidine kinase RcsC; |
526-747 |
1.12e-04 |
|
two-component system sensor histidine kinase RcsC;
Pssm-ID: 182772 [Multi-domain] Cd Length: 924 Bit Score: 46.12 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 526 PTLFSIQDLIDEVVPDVLPVIKRKGLQL--LINNHLPanDERHGDREALRRILLMIIQYAVTTTQIGKITLEVNTDEsae 603
Cdd:PRK10841 517 PREFSPREVINHITANYLPLVVKKRLGLycFIEPDVP--VALNGDPMRLQQVISNLLSNAIKFTDTGCIVLHVRVDG--- 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 604 DRLTFRILDTGEGVTTSEIDNLHFPFL---NDTQSDHYGkaNALTFWLCDQLARKLGGHLNIKARESLGTRYSLHVKM-- 678
Cdd:PRK10841 592 DYLSFRVRDTGVGIPAKEVVRLFDPFFqvgTGVQRNFQG--TGLGLAICEKLINMMDGDISVDSEPGMGSQFTIRIPLyg 669
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504645629 679 AANPQEEDEERLLDDVIVMvdvtsnEIRN-----IVVRQLENWGAACITPDERLSSQEfDLFLTDNPSNLTASG 747
Cdd:PRK10841 670 AQYPQKKGVEGLQGKRCWL------AVRNasleqFLETLLQRSGIQVQRYEGQEPTPE-DVLITDDPVQKKWQG 736
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
351-685 |
2.94e-04 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 44.07 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 351 ELRVLRALNEEIISVLPLGVLVHDqEANRTVMSNKIADHLLPH-------LNLQNITTMADQHQGIIQATINNE----LY 419
Cdd:COG3852 1 ALRESEELLRAILDSLPDAVIVLD-ADGRITYVNPAAERLLGLsaeellgRPLAELFPEDSPLRELLERALAEGqpvtER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 420 EIRQFRSQVASRT---QIFIIRDQDRE---VLVNKKLKQAQRLYEKNQQgrAAFMQNIGDA-------FKQPLRAL--AT 484
Cdd:COG3852 80 EVTLRRKDGEERPvdvSVSPLRDAEGEggvLLVLRDITERKRLERELRR--AEKLAAVGELaaglaheIRNPLTGIrgAA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 485 QAAALSTPDS------QQLASQADSLVRMVDEI-QLANMLENDFwkgtpTLFSIQDLIDEVVPDVLP-VIKRKGLQLLIN 556
Cdd:COG3852 158 QLLERELPDDelreytQLIIEEADRLNNLVDRLlSFSRPRPPER-----EPVNLHEVLERVLELLRAeAPKNIRIVRDYD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 557 NHLPandERHGDREALRRILLMIIQYAVT-TTQIGKITLEV-------NTDESAEDRLTFRILDTGEGVTTSEIDNLHFP 628
Cdd:COG3852 233 PSLP---EVLGDPDQLIQVLLNLVRNAAEaMPEGGTITIRTrverqvtLGGLRPRLYVRIEVIDNGPGIPEEILDRIFEP 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 504645629 629 FLndTqsdhyGKANA--LTFWLCDQLARKLGGHLNIKARESLGTRYSLHVKMAANPQEE 685
Cdd:COG3852 310 FF--T-----TKEKGtgLGLAIVQKIVEQHGGTIEVESEPGKGTTFRIYLPLEQAEEEP 361
|
|
| HPT |
smart00073 |
Histidine Phosphotransfer domain; Contains an active histidine residue that mediates ... |
814-869 |
3.37e-04 |
|
Histidine Phosphotransfer domain; Contains an active histidine residue that mediates phosphotransfer reactions. Domain detected only in eubacteria. This alignment is an extension to that shown in the Cell structure paper.
Pssm-ID: 197502 [Multi-domain] Cd Length: 92 Bit Score: 40.31 E-value: 3.37e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 504645629 814 FVDTVPDDVKRLYTESAANDFAALAQTAHRLKGVFAMLNLVPGKQLCETLEHLIRE 869
Cdd:smart00073 13 FLQSLEEGLLELEKALDAQDVNEIFRAAHTLKGSAGSLGLQQLAQLCHQLENLLDA 68
|
|
| HATPase_SpaK_NisK-like |
cd16975 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
568-662 |
4.38e-04 |
|
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis SpaK and Lactococcus lactis NisK; This family includes histidine kinase-like ATPase (HATPase) domain of two-component sensor histidine kinases similar to Bacillus subtilis SpaK and Lactococcus lactis NisK. SpaK is the histidine kinase (HK) of the SpaK-SpaR two-component regulatory system (TCS), which is involved in the regulation of the biosynthesis of lantibiotic subtilin. NisK is the HK of the NisK-NisR TCS, which is involved in the regulation of the biosynthesis of lantibiotic nisin. SpaK and NisK may function as membrane-associated protein kinases that phosphorylate SpaR and NisR, respectively, in response to environmental signals.
Pssm-ID: 340434 [Multi-domain] Cd Length: 107 Bit Score: 40.52 E-value: 4.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 568 DREALRRILLMIIQYAVTTTQIGK-ITLEVNTDESAedrLTFRILDTGEGVTTSEIDNLHFPFLNDTQSDHYGKANALTF 646
Cdd:cd16975 1 DTLLLSRALINIISNACQYAPEGGtVSISIYDEEEY---LYFEIWDNGHGFSEQDLKKALELFYRDDTSRRSGGHYGMGL 77
|
90
....*....|....*.
gi 504645629 647 WLCDQLARKLGGHLNI 662
Cdd:cd16975 78 YIAKNLVEKHGGSLII 93
|
|
| HATPase_BceS-YxdK-YvcQ-like |
cd16948 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
568-674 |
8.51e-03 |
|
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: 36.88 E-value: 8.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645629 568 DREALRRILLMIIQYAVT-TTQIGKITLEVNTDEsaeDRLTFRILDTGEGVTTSEIDNLHFPFLNDTQSDHYGKANALTF 646
Cdd:cd16948 2 DAKWLSFIIGQIVSNALKySKQGGKIEIYSETNE---QGVVLSIKDFGIGIPEEDLPRVFDKGFTGENGRNFQESTGMGL 78
|
90 100
....*....|....*....|....*...
gi 504645629 647 WLCDQLARKLGGHLNIKARESLGTRYSL 674
Cdd:cd16948 79 YLVKKLCDKLGHKIDVESEVGEGTTFTI 106
|
|
| |
