|
Name |
Accession |
Description |
Interval |
E-value |
| PHY |
pfam00360 |
Phytochrome region; Phytochromes are red/far-red photochromic biliprotein photoreceptors which ... |
305-479 |
7.76e-67 |
|
Phytochrome region; Phytochromes are red/far-red photochromic biliprotein photoreceptors which regulate plant development. They are widely represented in both photosynthetic and non-photosynthetic bacteria and are known in a variety of fungi. Although sequence similarities are low, this domain is structurally related to pfam01590, which is generally located immediately N-terminal to this domain. Compared with pfam01590, this domain carries an additional tongue-like hairpin loop between the fifth beta-sheet and the sixth alpha-helix which functions to seal the chromophore pocket and stabilize the photoactivated far-red-absorbing state (Pfr). The tongue carries a conserved PRxSF motif, from which an arginine finger points into the chromophore pocket close to ring D forming a salt bridge with a conserved aspartate residue.
Pssm-ID: 425635 Cd Length: 178 Bit Score: 221.76 E-value: 7.76e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 305 ILRTQTLLCDMLMR--DAPLGIVSQSPNIMDLVKCDGAALLYKDKIWKLGTTPSEFHLQEIASWLCEYHmDSTGLSTDSL 382
Cdd:pfam00360 1 LRRIQDRLVEAMARadDLVDGLVDQSPNLLDLVKADGAALCFGGNLLTLGETPPEEAIRDLAQWLGRNH-DSEVFSTDSL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 383 HDAgFPRALSLGDSVCGMAAVRISSKDM--IFWFRSHTAGEVRWGGAKHDPDDRDDARR-MHPRSSFKAFLEVVKTRSLP 459
Cdd:pfam00360 80 SQA-YPEAAALADVASGLLAIPISRKPGnyLLWFRPEVVRTVNWGGDPHKAVEIDPGGVrLSPRKSFDAWKETVRGRSLP 158
|
170 180
....*....|....*....|
gi 186478305 460 WKDYEMDAIHSLQLILRNAF 479
Cdd:pfam00360 159 WSEVEIEAARELREALLGVV 178
|
|
| HATPase_Phy-like |
cd16932 |
Histidine kinase-like ATPase domain of plant phytochromes similar to Arabidopsis thaliana ... |
898-1009 |
1.29e-55 |
|
Histidine kinase-like ATPase domain of plant phytochromes similar to Arabidopsis thaliana Phytochrome A, B, C, D and E; This family includes the histidine kinase-like ATPase (HATPase) domains of plant red/far-red photoreceptors, the phytochromes, and includes the Arabidopsis thaliana phytochrome family phyA-phyE. Following red light absorption, biologically inactive forms of phytochromes convert to active forms, which rapidly convert back to inactive forms upon far-red light irradiation. Phytochromes can be considered as having an N-terminal photosensory region to which a bilin chromophore is bound, and a C-terminal output region, which includes the HATPase domain represented here, and is involved in dimerization and presumably contributes to relaying the light signal to downstream signaling events.
Pssm-ID: 340409 [Multi-domain] Cd Length: 113 Bit Score: 187.86 E-value: 1.29e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 898 YGDSIRLQQVLADFMLMAVNFTPS-GGQLTVSASLRKDQLGRSVHLANLEIRLTHTGAGIPEFLLNQMFGTEEDVSEEGL 976
Cdd:cd16932 1 YGDQIRLQQVLADFLLNAVRFTPSpGGWVEIKVSPTKKQIGDGVHVIHLEFRITHPGQGLPEELVQEMFEENQWTTQEGL 80
|
90 100 110
....*....|....*....|....*....|...
gi 186478305 977 SLMVSRKLVKLMNGDVQYLRQAGKSSFIITAEL 1009
Cdd:cd16932 81 GLSISRKLVKLMNGDVRYLREAGRSYFLITLEL 113
|
|
| PAS_2 |
pfam08446 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
17-77 |
3.91e-26 |
|
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: 400652 Cd Length: 107 Bit Score: 103.49 E-value: 3.91e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 186478305 17 IGTDIRSLFTAPSASALQKALGFGDVSLLNPILVHCRTSAKPFYAIIHRVTGSIIIDFEPV 77
Cdd:pfam08446 47 LGTDLRDLFGASSASLLRKALAAGEISLLNPILIHSRTSGKPFYAILHRSDGGLVLELEPA 107
|
|
| KdpD |
COG2205 |
K+-sensing histidine kinase KdpD [Signal transduction mechanisms]; |
770-1006 |
2.65e-25 |
|
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
Pssm-ID: 441807 [Multi-domain] Cd Length: 239 Bit Score: 105.76 E-value: 2.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 770 ELQQALhvQRLAERTAVKRlKALAYIKRQIRNPLSGIM-FTRKMIEGTELGPEQRR-----ILQTSALCQKQLSKILDDS 843
Cdd:COG2205 1 ELEEAL--EELEELERLKS-EFLANVSHELRTPLTSILgAAELLLDEEDLSPEERRelleiIRESAERLLRLIEDLLDLS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 844 DLESiieGCLDLEMKEFTLNEVLTASTSQVMMKSNGKSVRITNETGEEVMsdTLYGDSIRLQQVLADFMLMAVNFTPSGG 923
Cdd:COG2205 78 RLES---GKLSLELEPVDLAELLEEAVEELRPLAEEKGIRLELDLPPELP--LVYADPELLEQVLANLLDNAIKYSPPGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 924 QLTVSASLRKDQLgrsvhlanlEIRLTHTGAGIPEFLLNQMFG---TEEDVSEE---GLSLMVSRKLVKLMNGDVQYLRQ 997
Cdd:COG2205 153 TITISARREGDGV---------RISVSDNGPGIPEEELERIFErfyRGDNSRGEggtGLGLAIVKRIVEAHGGTIWVESE 223
|
250
....*....|
gi 186478305 998 AGK-SSFIIT 1006
Cdd:COG2205 224 PGGgTTFTVT 233
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
517-1006 |
4.51e-23 |
|
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: 104.29 E-value: 4.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 517 LIETATVPILAVDSDGLVNGWNTKIAELTGLSVDEAIGKHFLTLVEDSSVEIVKRMLENALEGTEEQNVQFEIKTHLSR- 595
Cdd:COG5809 20 LFENAPDAILILDLEGKILKVNPAAERIFGYTEDELLGTNILDFLHPDDEKELREILKLLKEGESRDELEFELRHKNGKr 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 596 ----ADAGPIslvvnacasRDLHENVVGVCFVAHDLTGQKTVMDKFTRIEGDYKAIIQNPNPLIppiFGTDEFGWCTEWN 671
Cdd:COG5809 100 lefsSKLSPI---------FDQNGDIEGMLAISRDITERKRMEEALRESEEKFRLIFNHSPDGI---IVTDLDGRIIYAN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 672 PAMSKLTGLKREEVIDKMLLgEVFgtqksccRLKNQEAFVNLgivLNNAVTSQDPEKVSFAFFTRGGKYVEcLLCVSKKL 751
Cdd:COG5809 168 PAACKLLGISIEELIGKSIL-ELI-------HSDDQENVAAF---ISQLLKDGGIAQGEVRFWTKDGRWRL-LEASGAPI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 752 DREGVVTGVFCFLQLASH--ELQQALhvqRLAERTAV-KRLkaLAYIKRQIRNPLSGIM-FTrKMIEGTELGpEQRRILQ 827
Cdd:COG5809 236 KKNGEVDGIVIIFRDITErkKLEELL---RKSEKLSVvGEL--AAGIAHEIRNPLTSLKgFI-QLLKDTIDE-EQKTYLD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 828 TsalcqkqlskILDDSD-LESIIEGCLDL------EMKEFTLNEVLTASTSQVMMKSNGKSVRITNETGEEVmsDTLYGD 900
Cdd:COG5809 309 I----------MLSELDrIESIISEFLVLakpqaiKYEPKDLNTLIEEVIPLLQPQALLKNVQIELELEDDI--PDILGD 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 901 SIRLQQVLADFMLMAVNFTPSGGQLTVSAslrKDQLGRSVhlanlEIRLTHTGAGIPEFLLNQMF---------GTeedv 971
Cdd:COG5809 377 ENQLKQVFINLLKNAIEAMPEGGNITIET---KAEDDDKV-----VISVTDEGCGIPEERLKKLGepfyttkekGT---- 444
|
490 500 510
....*....|....*....|....*....|....*.
gi 186478305 972 seeGLSLMVSRKLVKLMNGDVQYLRQAGK-SSFIIT 1006
Cdd:COG5809 445 ---GLGLMVSYKIIEEHGGKITVESEVGKgTTFSIT 477
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
513-626 |
1.08e-22 |
|
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: 94.02 E-value: 1.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 513 EMVRLIETATVPILAVDSDGLVNGWNTKIAELTGLSVDEAIGKHFLTLV-EDSSVEIVKRMLENALEGTEEQNVQFEIKT 591
Cdd:pfam00989 2 DLRAILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIpEEDDAEVAELLRQALLQGEESRGFEVSFRV 81
|
90 100 110
....*....|....*....|....*....|....*
gi 186478305 592 hlsrADAGPISLVVNACASRDLHENVVGVCFVAHD 626
Cdd:pfam00989 82 ----PDGRPRHVEVRASPVRDAGGEILGFLGVLRD 112
|
|
| HATPase_c |
smart00387 |
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases. |
899-1010 |
3.77e-18 |
|
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
Pssm-ID: 214643 [Multi-domain] Cd Length: 111 Bit Score: 80.77 E-value: 3.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 899 GDSIRLQQVLADFMLMAVNFTPSGGQLTVSASLRKDqlgrsvhlaNLEIRLTHTGAGIPEFLLNQMF-------GTEEDV 971
Cdd:smart00387 1 GDPDRLRQVLSNLLDNAIKYTPEGGRITVTLERDGD---------HVEITVEDNGPGIPPEDLEKIFepffrtdKRSRKI 71
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 186478305 972 SEEGLSLMVSRKLVKLMNGDVQYLRQAGK-SSFIITAELA 1010
Cdd:smart00387 72 GGTGLGLSIVKKLVELHGGEISVESEPGGgTTFTITLPLE 111
|
|
| PRK15347 |
PRK15347 |
two component system sensor kinase; |
768-990 |
7.27e-16 |
|
two component system sensor kinase;
Pssm-ID: 237951 [Multi-domain] Cd Length: 921 Bit Score: 82.77 E-value: 7.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 768 SHELQQAlhvQRLAERTAVKRLKALAYIKRQIRNPLSGIMFTRKMIEGTELGPEQRRILQTSALCQKQLSKI----LDDS 843
Cdd:PRK15347 381 TQALAEA---KQRAEQANKRKSEHLTTISHEIRTPLNGVLGALELLQNTPLTAEQMDLADTARQCTLSLLAIinnlLDFS 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 844 DLESiieGCLDLEMKEFTLNEVLtastSQVMM--KSNGKSVRITNET--GEEVmSDTLYGDSIRLQQVLADFMLMAVNFT 919
Cdd:PRK15347 458 RIES---GQMTLSLEETALLPLL----DQAMLtiQGPAQSKSLTLRTfvGAHV-PLYLHLDSLRLRQILVNLLGNAVKFT 529
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 186478305 920 PSGG-QLTVSaslRKDQlgrsvHLAnleIRLTHTGAGIPEFLLNQMFG----TEEDVSEEGLSLMVSRKLVKLMNG 990
Cdd:PRK15347 530 ETGGiRLRVK---RHEQ-----QLC---FTVEDTGCGIDIQQQQQIFTpfyqADTHSQGTGLGLTIASSLAKMMGG 594
|
|
| PRK10841 |
PRK10841 |
two-component system sensor histidine kinase RcsC; |
792-1005 |
8.89e-15 |
|
two-component system sensor histidine kinase RcsC;
Pssm-ID: 182772 [Multi-domain] Cd Length: 924 Bit Score: 79.25 E-value: 8.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 792 LAYIKRQIRNPLSGIMFTRKMIEGTELGPEQRRILQT----SALCQKQLSKILDDSDLESiiEGcLDLEMKEFTLNEVLT 867
Cdd:PRK10841 451 LATVSHELRTPLYGIIGNLDLLQTKELPKGVDRLVTAmnnsSSLLLKIISDILDFSKIES--EQ-LKIEPREFSPREVIN 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 868 ASTSQ----VMMKSNGKSVRItnetgEEVMSDTLYGDSIRLQQVLADFMLMAVNFTPSGGqLTVSASLRKDQlgrsvhla 943
Cdd:PRK10841 528 HITANylplVVKKRLGLYCFI-----EPDVPVALNGDPMRLQQVISNLLSNAIKFTDTGC-IVLHVRVDGDY-------- 593
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 186478305 944 nLEIRLTHTGAGIPEFLLNQMF--------GTEEDVSEEGLSLMVSRKLVKLMNGDVQYLRQAGKSS-FII 1005
Cdd:PRK10841 594 -LSFRVRDTGVGIPAKEVVRLFdpffqvgtGVQRNFQGTGLGLAICEKLINMMDGDISVDSEPGMGSqFTI 663
|
|
| HATPase_c |
pfam02518 |
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ... |
899-1010 |
2.04e-14 |
|
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: 70.09 E-value: 2.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 899 GDSIRLQQVLADFMLMAVNFTPSGGQLTVSasLRKDqlgrsvhlANLEIRLTHTGAGIPEFLLNQMFG-----TEEDVSE 973
Cdd:pfam02518 1 GDELRLRQVLSNLLDNALKHAAKAGEITVT--LSEG--------GELTLTVEDNGIGIPPEDLPRIFEpfstaDKRGGGG 70
|
90 100 110
....*....|....*....|....*....|....*...
gi 186478305 974 EGLSLMVSRKLVKLMNGDVQYLRQAGK-SSFIITAELA 1010
Cdd:pfam02518 71 TGLGLSIVRKLVELLGGTITVESEPGGgTTVTLTLPLA 108
|
|
| GAF |
smart00065 |
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ... |
111-296 |
1.88e-12 |
|
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these domains in PDE6B result in autosomal recessive inheritance of retinitis pigmentosa.
Pssm-ID: 214500 [Multi-domain] Cd Length: 149 Bit Score: 65.87 E-value: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 111 MERLCDTMVQEVFELTGYDRVMAYKFHEDDHGEVVSEVTKPGLEPYLGLHYPATDipQAARFLFMKNKVRMIVDCNAkha 190
Cdd:smart00065 2 LEELLQTILEELRQLLGADRVLIYLVDENDRGELVLVAADGLTLPTLGIRFPLDE--GLAGRVAETGRPLNIPDVEA--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 191 rvlqdeklsfdltlcgstlrAPHSCHLQYMANMDSIASLVMAVVVNEEdgegdapdattqpqkrkrLWGLVVCHNTTprf 270
Cdd:smart00065 77 --------------------DPLFAEDLLGRYQGVRSFLAVPLVADGE------------------LVGVLALHNKK--- 115
|
170 180
....*....|....*....|....*.
gi 186478305 271 VPFPLRYACEFLAQVFAIHVNKEVEL 296
Cdd:smart00065 116 SPRPFTEEDEELLQALANQLAIALAN 141
|
|
| GAF |
pfam01590 |
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ... |
110-294 |
2.40e-10 |
|
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl cyclases, phytochromes, FhlA and NifA. Adenylyl and guanylyl cyclases catalyze ATP and GTP to the second messengers cAMP and cGMP, respectively, these products up-regulating catalytic activity by binding to the regulatory GAF domain(s). The opposite hydrolysis reaction is catalyzed by phosphodiesterase. cGMP-dependent 3',5'-cyclic phosphodiesterase catalyzes the conversion of guanosine 3',5'-cyclic phosphate to guanosine 5'-phosphate. Here too, cGMP regulates catalytic activity by GAF-domain binding. Phytochromes are regulatory photoreceptors in plants and bacteria which exist in two thermally-stable states that are reversibly inter-convertible by light: the Pr state absorbs maximally in the red region of the spectrum, while the Pfr state absorbs maximally in the far-red region. This domain is also found in FhlA (formate hydrogen lyase transcriptional activator) and NifA, a transcriptional activator which is required for activation of most Nif operons which are directly involved in nitrogen fixation. NifA interacts with sigma-54. This domain can bind biliverdine and phycocyanobilin (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 460259 [Multi-domain] Cd Length: 133 Bit Score: 59.41 E-value: 2.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 110 SMERLCDTMVQEVFELTGYDRVMAYkfheddhgevvsevtkpgLEPYLGLHYpatdIPQAARFLfmknKVRMIVDCNAKH 189
Cdd:pfam01590 1 DLEEILQTILEELRELLGADRCALY------------------LPDADGLEY----LPPGARWL----KAAGLEIPPGTG 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 190 ARVLQDEKlsfDLTLCGStlrAPHSCHLQ---YMANMDSIASLVMAVVVNEedgegdapdattqpqkrkRLWGLVVCHNT 266
Cdd:pfam01590 55 VTVLRTGR---PLVVPDA---AGDPRFLDpllLLRNFGIRSLLAVPIIDDG------------------ELLGVLVLHHP 110
|
170 180
....*....|....*....|....*...
gi 186478305 267 TPRFvpfpLRYACEFLaQVFAIHVNKEV 294
Cdd:pfam01590 111 RPPF----TEEELELL-EVLADQVAIAL 133
|
|
| HisKA |
smart00388 |
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ... |
787-850 |
5.70e-10 |
|
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine kinases.
Pssm-ID: 214644 [Multi-domain] Cd Length: 66 Bit Score: 56.04 E-value: 5.70e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 186478305 787 KRLKALAYIKRQIRNPLSGIMFTRKMIEGTELGPEQRRILQTSALCQKQLSKILDDSDLESIIE 850
Cdd:smart00388 1 AKREFLANLSHELRTPLTAIRGYLELLLDTELSEEQREYLETILREAERLLRLINDLLDLSRIE 64
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
513-632 |
1.44e-09 |
|
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: 56.92 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 513 EMVRLI-ETATVPILAVDSDGLVNGWNTKIAELTGLSVDEAIGKHFLTLVEDSSVEIVKRMLENALEGTEEQNVQFEIKT 591
Cdd:TIGR00229 3 ERYRAIfESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEPEPVSEERRVR 82
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 186478305 592 hlsRADAGPISLVVNAcASRDLHENVVGVCFVAHDLTGQKT 632
Cdd:TIGR00229 83 ---RKDGSEIWVEVSV-SPIRTNGGELGVVGIVRDITERKE 119
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
521-627 |
1.63e-09 |
|
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: 56.10 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 521 ATVPILAVDSDGLVNGWNTKIAELTGLSVDEAIGKHFLTLVEDSSVEIVKRMLENALEGTEEQNVQFEIKTHlsraDAGP 600
Cdd:cd00130 1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRK----DGSV 76
|
90 100
....*....|....*....|....*..
gi 186478305 601 ISLVVNACASRDLHENVVGVCFVAHDL 627
Cdd:cd00130 77 IWVLVSLTPIRDEGGEVIGLLGVVRDI 103
|
|
| KinB |
COG5806 |
Sporulation sensor histidine kinase B [Cell cycle control, cell division, chromosome ... |
793-1006 |
1.82e-09 |
|
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: 61.04 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 793 AYIKRQIRNPLS---GIMftrKMIEGTELGPEQRRilQTSALCQKQLSKIlddsdlESIIEGCLDL------EMKEFTLN 863
Cdd:COG5806 206 ASIAHEVRNPLTvvrGFI---QLLQEPELSDEKRK--QYIRIALEELDRA------EAIITDYLTFakpqpeKLEKIDVS 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 864 EVLTASTSqvMMKS--NGKSVRITNETGEEVmsdTLYGDSIRLQQVLADFMLMAVNFTPSGGQLTVSASLRKDQlgrsVH 941
Cdd:COG5806 275 EELEHVID--VLSPyaNMNNVEIQTELEPGL---YIEGDRQKLQQCLINIIKNGIEAMPNGGTLTIDVSIDKNK----VI 345
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 942 lanleIRLTHTGAGIPEFLLNQM----FGTEEDVSeeGLSLMVSRKLVKLMNGDVQYLRQAGK-SSFIIT 1006
Cdd:COG5806 346 -----ISIKDTGVGMTKEQLERLgepyFSTKEKGT--GLGTMVSYRIIEAMNGTIRVESEVGKgTTFTIT 408
|
|
| HisKA |
pfam00512 |
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ... |
787-851 |
5.51e-09 |
|
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine kinases.
Pssm-ID: 459839 [Multi-domain] Cd Length: 66 Bit Score: 53.37 E-value: 5.51e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 186478305 787 KRLKALAYIKRQIRNPLSGIMFTRKMIEGTELGPEQRRILQTSALCQKQLSKILDD-SDLESIIEG 851
Cdd:pfam00512 1 AKSEFLANLSHELRTPLTAIRGYLELLRDEKLDEEQREYLETILRSAERLLRLINDlLDLSRIEAG 66
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
516-578 |
1.41e-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.
Pssm-ID: 214512 Cd Length: 67 Bit Score: 52.40 E-value: 1.41e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 186478305 516 RLIETATVPILAVDSDGLVNGWNTKIAELTGLSVDEAIGKHFLTLVEDSSVEIVKRMLENALE 578
Cdd:smart00091 5 AILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLLS 67
|
|
| PRK11360 |
PRK11360 |
two-component system sensor histidine kinase AtoS; |
518-641 |
1.90e-07 |
|
two-component system sensor histidine kinase AtoS;
Pssm-ID: 236901 [Multi-domain] Cd Length: 607 Bit Score: 54.97 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 518 IETATVPILAVDSDGLVNGWNTKIAELTGLSVDEAIGKHFLTLVEDSS--VEIVKRMLENaleGTEEqnVQFEIKTHlsr 595
Cdd:PRK11360 268 LESIADGVIAIDRQGKITTMNPAAEVITGLQRHELVGKPYSELFPPNTpfASPLLDTLEH---GTEH--VDLEISFP--- 339
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 186478305 596 ADAGPISLVVNACASRDLHENVVGVCFVAHDLTGQKTVMDKFTRIE 641
Cdd:PRK11360 340 GRDRTIELSVSTSLLHNTHGEMIGALVIFSDLTERKRLQRRVARQE 385
|
|
| HisKA |
cd00082 |
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ... |
792-842 |
4.81e-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: 39.50 E-value: 4.81e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 186478305 792 LAYIKRQIRNPLSGIMFTRKMIEGTELGPE-QRRILQTSALCQKQLSKILDD 842
Cdd:cd00082 8 LANVSHELRTPLTAIRGALELLEEELLDDEeQREYLERIREEAERLLRLIND 59
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PHY |
pfam00360 |
Phytochrome region; Phytochromes are red/far-red photochromic biliprotein photoreceptors which ... |
305-479 |
7.76e-67 |
|
Phytochrome region; Phytochromes are red/far-red photochromic biliprotein photoreceptors which regulate plant development. They are widely represented in both photosynthetic and non-photosynthetic bacteria and are known in a variety of fungi. Although sequence similarities are low, this domain is structurally related to pfam01590, which is generally located immediately N-terminal to this domain. Compared with pfam01590, this domain carries an additional tongue-like hairpin loop between the fifth beta-sheet and the sixth alpha-helix which functions to seal the chromophore pocket and stabilize the photoactivated far-red-absorbing state (Pfr). The tongue carries a conserved PRxSF motif, from which an arginine finger points into the chromophore pocket close to ring D forming a salt bridge with a conserved aspartate residue.
Pssm-ID: 425635 Cd Length: 178 Bit Score: 221.76 E-value: 7.76e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 305 ILRTQTLLCDMLMR--DAPLGIVSQSPNIMDLVKCDGAALLYKDKIWKLGTTPSEFHLQEIASWLCEYHmDSTGLSTDSL 382
Cdd:pfam00360 1 LRRIQDRLVEAMARadDLVDGLVDQSPNLLDLVKADGAALCFGGNLLTLGETPPEEAIRDLAQWLGRNH-DSEVFSTDSL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 383 HDAgFPRALSLGDSVCGMAAVRISSKDM--IFWFRSHTAGEVRWGGAKHDPDDRDDARR-MHPRSSFKAFLEVVKTRSLP 459
Cdd:pfam00360 80 SQA-YPEAAALADVASGLLAIPISRKPGnyLLWFRPEVVRTVNWGGDPHKAVEIDPGGVrLSPRKSFDAWKETVRGRSLP 158
|
170 180
....*....|....*....|
gi 186478305 460 WKDYEMDAIHSLQLILRNAF 479
Cdd:pfam00360 159 WSEVEIEAARELREALLGVV 178
|
|
| HATPase_Phy-like |
cd16932 |
Histidine kinase-like ATPase domain of plant phytochromes similar to Arabidopsis thaliana ... |
898-1009 |
1.29e-55 |
|
Histidine kinase-like ATPase domain of plant phytochromes similar to Arabidopsis thaliana Phytochrome A, B, C, D and E; This family includes the histidine kinase-like ATPase (HATPase) domains of plant red/far-red photoreceptors, the phytochromes, and includes the Arabidopsis thaliana phytochrome family phyA-phyE. Following red light absorption, biologically inactive forms of phytochromes convert to active forms, which rapidly convert back to inactive forms upon far-red light irradiation. Phytochromes can be considered as having an N-terminal photosensory region to which a bilin chromophore is bound, and a C-terminal output region, which includes the HATPase domain represented here, and is involved in dimerization and presumably contributes to relaying the light signal to downstream signaling events.
Pssm-ID: 340409 [Multi-domain] Cd Length: 113 Bit Score: 187.86 E-value: 1.29e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 898 YGDSIRLQQVLADFMLMAVNFTPS-GGQLTVSASLRKDQLGRSVHLANLEIRLTHTGAGIPEFLLNQMFGTEEDVSEEGL 976
Cdd:cd16932 1 YGDQIRLQQVLADFLLNAVRFTPSpGGWVEIKVSPTKKQIGDGVHVIHLEFRITHPGQGLPEELVQEMFEENQWTTQEGL 80
|
90 100 110
....*....|....*....|....*....|...
gi 186478305 977 SLMVSRKLVKLMNGDVQYLRQAGKSSFIITAEL 1009
Cdd:cd16932 81 GLSISRKLVKLMNGDVRYLREAGRSYFLITLEL 113
|
|
| PAS_2 |
pfam08446 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
17-77 |
3.91e-26 |
|
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: 400652 Cd Length: 107 Bit Score: 103.49 E-value: 3.91e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 186478305 17 IGTDIRSLFTAPSASALQKALGFGDVSLLNPILVHCRTSAKPFYAIIHRVTGSIIIDFEPV 77
Cdd:pfam08446 47 LGTDLRDLFGASSASLLRKALAAGEISLLNPILIHSRTSGKPFYAILHRSDGGLVLELEPA 107
|
|
| KdpD |
COG2205 |
K+-sensing histidine kinase KdpD [Signal transduction mechanisms]; |
770-1006 |
2.65e-25 |
|
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
Pssm-ID: 441807 [Multi-domain] Cd Length: 239 Bit Score: 105.76 E-value: 2.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 770 ELQQALhvQRLAERTAVKRlKALAYIKRQIRNPLSGIM-FTRKMIEGTELGPEQRR-----ILQTSALCQKQLSKILDDS 843
Cdd:COG2205 1 ELEEAL--EELEELERLKS-EFLANVSHELRTPLTSILgAAELLLDEEDLSPEERRelleiIRESAERLLRLIEDLLDLS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 844 DLESiieGCLDLEMKEFTLNEVLTASTSQVMMKSNGKSVRITNETGEEVMsdTLYGDSIRLQQVLADFMLMAVNFTPSGG 923
Cdd:COG2205 78 RLES---GKLSLELEPVDLAELLEEAVEELRPLAEEKGIRLELDLPPELP--LVYADPELLEQVLANLLDNAIKYSPPGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 924 QLTVSASLRKDQLgrsvhlanlEIRLTHTGAGIPEFLLNQMFG---TEEDVSEE---GLSLMVSRKLVKLMNGDVQYLRQ 997
Cdd:COG2205 153 TITISARREGDGV---------RISVSDNGPGIPEEELERIFErfyRGDNSRGEggtGLGLAIVKRIVEAHGGTIWVESE 223
|
250
....*....|
gi 186478305 998 AGK-SSFIIT 1006
Cdd:COG2205 224 PGGgTTFTVT 233
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
517-1006 |
4.51e-23 |
|
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: 104.29 E-value: 4.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 517 LIETATVPILAVDSDGLVNGWNTKIAELTGLSVDEAIGKHFLTLVEDSSVEIVKRMLENALEGTEEQNVQFEIKTHLSR- 595
Cdd:COG5809 20 LFENAPDAILILDLEGKILKVNPAAERIFGYTEDELLGTNILDFLHPDDEKELREILKLLKEGESRDELEFELRHKNGKr 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 596 ----ADAGPIslvvnacasRDLHENVVGVCFVAHDLTGQKTVMDKFTRIEGDYKAIIQNPNPLIppiFGTDEFGWCTEWN 671
Cdd:COG5809 100 lefsSKLSPI---------FDQNGDIEGMLAISRDITERKRMEEALRESEEKFRLIFNHSPDGI---IVTDLDGRIIYAN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 672 PAMSKLTGLKREEVIDKMLLgEVFgtqksccRLKNQEAFVNLgivLNNAVTSQDPEKVSFAFFTRGGKYVEcLLCVSKKL 751
Cdd:COG5809 168 PAACKLLGISIEELIGKSIL-ELI-------HSDDQENVAAF---ISQLLKDGGIAQGEVRFWTKDGRWRL-LEASGAPI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 752 DREGVVTGVFCFLQLASH--ELQQALhvqRLAERTAV-KRLkaLAYIKRQIRNPLSGIM-FTrKMIEGTELGpEQRRILQ 827
Cdd:COG5809 236 KKNGEVDGIVIIFRDITErkKLEELL---RKSEKLSVvGEL--AAGIAHEIRNPLTSLKgFI-QLLKDTIDE-EQKTYLD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 828 TsalcqkqlskILDDSD-LESIIEGCLDL------EMKEFTLNEVLTASTSQVMMKSNGKSVRITNETGEEVmsDTLYGD 900
Cdd:COG5809 309 I----------MLSELDrIESIISEFLVLakpqaiKYEPKDLNTLIEEVIPLLQPQALLKNVQIELELEDDI--PDILGD 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 901 SIRLQQVLADFMLMAVNFTPSGGQLTVSAslrKDQLGRSVhlanlEIRLTHTGAGIPEFLLNQMF---------GTeedv 971
Cdd:COG5809 377 ENQLKQVFINLLKNAIEAMPEGGNITIET---KAEDDDKV-----VISVTDEGCGIPEERLKKLGepfyttkekGT---- 444
|
490 500 510
....*....|....*....|....*....|....*.
gi 186478305 972 seeGLSLMVSRKLVKLMNGDVQYLRQAGK-SSFIIT 1006
Cdd:COG5809 445 ---GLGLMVSYKIIEEHGGKITVESEVGKgTTFSIT 477
|
|
| BaeS |
COG0642 |
Signal transduction histidine kinase [Signal transduction mechanisms]; |
763-1006 |
7.81e-23 |
|
Signal transduction histidine kinase [Signal transduction mechanisms];
Pssm-ID: 440407 [Multi-domain] Cd Length: 328 Bit Score: 100.75 E-value: 7.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 763 FLQLASHELQQALHVQRLAERTAVKRLKALAYIKRQIRNPLSGIM-FTRKMIEgtELGPEQRRILQTSALCQKQLSKILD 841
Cdd:COG0642 85 LLLLLLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRgYLELLLE--ELDEEQREYLETILRSADRLLRLIN 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 842 D-SDLESIIEGCLDLEMKEFTLNEVLTASTSQVMMKSNGKSVRITNETGEEVMsdTLYGDSIRLQQVLADFMLMAVNFTP 920
Cdd:COG0642 163 DlLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDDLP--TVRGDPDRLRQVLLNLLSNAIKYTP 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 921 SGGQLTVSASLRKDQlgrsvhlanLEIRLTHTGAGIPEFLLNQMFG----TEEDVSEE--GLSLMVSRKLVKLMNGDVQY 994
Cdd:COG0642 241 EGGTVTVSVRREGDR---------VRISVEDTGPGIPPEDLERIFEpffrTDPSRRGGgtGLGLAIVKRIVELHGGTIEV 311
|
250
....*....|...
gi 186478305 995 LRQAGK-SSFIIT 1006
Cdd:COG0642 312 ESEPGKgTTFTVT 324
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
513-626 |
1.08e-22 |
|
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: 94.02 E-value: 1.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 513 EMVRLIETATVPILAVDSDGLVNGWNTKIAELTGLSVDEAIGKHFLTLV-EDSSVEIVKRMLENALEGTEEQNVQFEIKT 591
Cdd:pfam00989 2 DLRAILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIpEEDDAEVAELLRQALLQGEESRGFEVSFRV 81
|
90 100 110
....*....|....*....|....*....|....*
gi 186478305 592 hlsrADAGPISLVVNACASRDLHENVVGVCFVAHD 626
Cdd:pfam00989 82 ----PDGRPRHVEVRASPVRDAGGEILGFLGVLRD 112
|
|
| KinA |
COG5805 |
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ... |
511-1006 |
8.19e-21 |
|
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: 97.11 E-value: 8.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 511 TSEMVRLIETATVPILAVDSDGLVNGWNTKIAELTGLSVDEAIGKHFLTLVEDSSVEIVKRMLENALEGteeqNVQFEIK 590
Cdd:COG5805 33 TEELETILENLPDAIIAVNREGKVIYINPAMEKLLGYTSEEIIGKTIFDFLEKEYHYRVKTRIERLQKG----YDVVMIE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 591 THLsRADAGPISLVVNACASRDLHENVVGVCFVahDLTGQKTVMDKFTRIEGDYKAIIQNPNPLippIFGTDEFGWCTEW 670
Cdd:COG5805 109 QIY-CKDGELIYVEVKLFPIYNQNGQAAILALR--DITKKKKIEEILQEQEERLQTLIENSPDL---ICVIDTDGRILFI 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 671 NPAMSKLTGLKREEVIDKMLLgEVFgtqkSCCrlkNQEAFVNlgiVLNNAVTSQDPEKVSFAFFTRGGKYVECLLCVSKK 750
Cdd:COG5805 183 NESIERLFGAPREELIGKNLL-ELL----HPC---DKEEFKE---RIESITEVWQEFIIEREIITKDGRIRYFEAVIVPL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 751 LDREGVVTGVFCFLQLASHelqqalhvQRLAERTAVK--RLKAL----AYIKRQIRNPLSGIM-FTRKMIEGTElgpEQR 823
Cdd:COG5805 252 IDTDGSVKGILVILRDITE--------KKEAEELMARseKLSIAgqlaAGIAHEIRNPLTSIKgFLQLLQPGIE---DKE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 824 RILQtsaLCQKQLSKIlddsdlESIIEGCLDL------EMKEFTLNEVLTASTSQVMMKSNGKSVRITNETGEEVMsdTL 897
Cdd:COG5805 321 EYFD---IMLSELDRI------ESIISEFLALakpqavNKEKENINELIQDVVTLLETEAILHNIQIRLELLDEDP--FI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 898 YGDSIRLQQVLADFMLMAVNFTPSGGQLTVSASlrkdQLGRSVHlanleIRLTHTGAGIPEFLLNQM----FGTEEdvSE 973
Cdd:COG5805 390 YCDENQIKQVFINLIKNAIEAMPNGGTITIHTE----EEDNSVI-----IRVIDEGIGIPEERLKKLgepfFTTKE--KG 458
|
490 500 510
....*....|....*....|....*....|....
gi 186478305 974 EGLSLMVSRKLVKLMNGDVQYLRQAGK-SSFIIT 1006
Cdd:COG5805 459 TGLGLMVSYKIIENHNGTIDIDSKVGKgTTFTIT 492
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
642-765 |
1.23e-19 |
|
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: 85.16 E-value: 1.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 642 GDYKAIIQNpnpLIPPIFGTDEFGWCTEWNPAMSKLTGLKREEVIDKMLLGEVFGTQksccRLKNQEafvnlgIVLNNAV 721
Cdd:pfam00989 1 EDLRAILES---LPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEED----DAEVAE------LLRQALL 67
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 186478305 722 TSQDPEKVSFAFFTRGGKYVECLLCVSKKLDREGVVTGVFCFLQ 765
Cdd:pfam00989 68 QGEESRGFEVSFRVPDGRPRHVEVRASPVRDAGGEILGFLGVLR 111
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
505-691 |
1.24e-19 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 89.70 E-value: 1.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 505 QELEAVTSEMVRLIETATVPILAVDSDGLVNGWNTKIAELTGLSVDEAIGKHFLTLVEDSSVEIVKRMLENALEGTEEQN 584
Cdd:COG2202 4 EALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVWR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 585 VQFEIKthlsRADAGPISLVVNACASRDLHENVVGVCFVAHDLTGQKTVMDKFTRIEGDYKAIIQNpNPLIppIFGTDEF 664
Cdd:COG2202 84 GELRNR----RKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEERLRLLVEN-APDG--IFVLDLD 156
|
170 180
....*....|....*....|....*..
gi 186478305 665 GWCTEWNPAMSKLTGLKREEVIDKMLL 691
Cdd:COG2202 157 GRILYVNPAAEELLGYSPEELLGKSLL 183
|
|
| HATPase_c |
smart00387 |
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases. |
899-1010 |
3.77e-18 |
|
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
Pssm-ID: 214643 [Multi-domain] Cd Length: 111 Bit Score: 80.77 E-value: 3.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 899 GDSIRLQQVLADFMLMAVNFTPSGGQLTVSASLRKDqlgrsvhlaNLEIRLTHTGAGIPEFLLNQMF-------GTEEDV 971
Cdd:smart00387 1 GDPDRLRQVLSNLLDNAIKYTPEGGRITVTLERDGD---------HVEITVEDNGPGIPPEDLEKIFepffrtdKRSRKI 71
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 186478305 972 SEEGLSLMVSRKLVKLMNGDVQYLRQAGK-SSFIITAELA 1010
Cdd:smart00387 72 GGTGLGLSIVKKLVELHGGEISVESEPGGgTTFTITLPLE 111
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
638-1005 |
3.70e-17 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 84.51 E-value: 3.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 638 TRIEGDYKAIIQNpnplIP-PIFGTDEFGWCTEWNPAMSKLTGLKREEVIDKMlLGEVFGTQKSCCRLKNQeafvnlgiV 716
Cdd:COG3852 3 RESEELLRAILDS----LPdAVIVLDADGRITYVNPAAERLLGLSAEELLGRP-LAELFPEDSPLRELLER--------A 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 717 LNNAVTSQDPEkvsFAFFTRGGKYVECLLCVSKKLDREGvVTGVFCFLQLASHELQQALHVQRLAERTAVKRLKA-LAYi 795
Cdd:COG3852 70 LAEGQPVTERE---VTLRRKDGEERPVDVSVSPLRDAEG-EGGVLLVLRDITERKRLERELRRAEKLAAVGELAAgLAH- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 796 krQIRNPLSGIM-FTrKMIEgTELGPEQRRilqtsalcqKQLSKILDDSD-LESIIEGCLDL------EMKEFTLNEVLt 867
Cdd:COG3852 145 --EIRNPLTGIRgAA-QLLE-RELPDDELR---------EYTQLIIEEADrLNNLVDRLLSFsrprppEREPVNLHEVL- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 868 ASTSQVMMKSNGKSVRITNETGEEVmsDTLYGDSIRLQQVLADFMLMAVNFTPSGGQLTVSAS-LRKDQLGRSVHLANLE 946
Cdd:COG3852 211 ERVLELLRAEAPKNIRIVRDYDPSL--PEVLGDPDQLIQVLLNLVRNAAEAMPEGGTITIRTRvERQVTLGGLRPRLYVR 288
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 186478305 947 IRLTHTGAGIPEFLLNQMF---------GTeedvseeGLSLMVSRKLVKLMNGDVQYLRQAGK-SSFII 1005
Cdd:COG3852 289 IEVIDNGPGIPEEILDRIFepffttkekGT-------GLGLAIVQKIVEQHGGTIEVESEPGKgTTFRI 350
|
|
| PRK15347 |
PRK15347 |
two component system sensor kinase; |
768-990 |
7.27e-16 |
|
two component system sensor kinase;
Pssm-ID: 237951 [Multi-domain] Cd Length: 921 Bit Score: 82.77 E-value: 7.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 768 SHELQQAlhvQRLAERTAVKRLKALAYIKRQIRNPLSGIMFTRKMIEGTELGPEQRRILQTSALCQKQLSKI----LDDS 843
Cdd:PRK15347 381 TQALAEA---KQRAEQANKRKSEHLTTISHEIRTPLNGVLGALELLQNTPLTAEQMDLADTARQCTLSLLAIinnlLDFS 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 844 DLESiieGCLDLEMKEFTLNEVLtastSQVMM--KSNGKSVRITNET--GEEVmSDTLYGDSIRLQQVLADFMLMAVNFT 919
Cdd:PRK15347 458 RIES---GQMTLSLEETALLPLL----DQAMLtiQGPAQSKSLTLRTfvGAHV-PLYLHLDSLRLRQILVNLLGNAVKFT 529
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 186478305 920 PSGG-QLTVSaslRKDQlgrsvHLAnleIRLTHTGAGIPEFLLNQMFG----TEEDVSEEGLSLMVSRKLVKLMNG 990
Cdd:PRK15347 530 ETGGiRLRVK---RHEQ-----QLC---FTVEDTGCGIDIQQQQQIFTpfyqADTHSQGTGLGLTIASSLAKMMGG 594
|
|
| WalK |
COG5002 |
Sensor histidine kinase WalK [Signal transduction mechanisms]; |
772-1006 |
3.01e-15 |
|
Sensor histidine kinase WalK [Signal transduction mechanisms];
Pssm-ID: 444026 [Multi-domain] Cd Length: 390 Bit Score: 78.83 E-value: 3.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 772 QQALHVQRLAERTAVKRLKALAYIKRQ--------IRNPLSGI-MFTRKMIEGTELGPEQRR----ILQTSAlcqKQLSK 838
Cdd:COG5002 141 LLLGLLLLAAVERDITELERLEQMRREfvanvsheLRTPLTSIrGYLELLLDGAADDPEERReyleIILEEA---ERLSR 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 839 ILDD-SDLESIIEGCLDLEMKEFTLNEVLTASTSQVMMKSNGKSVRITNETGEEVMsdTLYGDSIRLQQVLADFMLMAVN 917
Cdd:COG5002 218 LVNDlLDLSRLESGELKLEKEPVDLAELLEEVVEELRPLAEEKGIELELDLPEDPL--LVLGDPDRLEQVLTNLLDNAIK 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 918 FTPSGGQLTVSASLRKDQlgrsvhlanLEIRLTHTGAGIPEFLLNQMF---------------GTeedvseeGLSLMVSR 982
Cdd:COG5002 296 YTPEGGTITVSLREEDDQ---------VRISVRDTGIGIPEEDLPRIFerfyrvdksrsretgGT-------GLGLAIVK 359
|
250 260
....*....|....*....|....*
gi 186478305 983 KLVKLMNGDVQYLRQAGK-SSFIIT 1006
Cdd:COG5002 360 HIVEAHGGRIWVESEPGKgTTFTIT 384
|
|
| PRK10841 |
PRK10841 |
two-component system sensor histidine kinase RcsC; |
792-1005 |
8.89e-15 |
|
two-component system sensor histidine kinase RcsC;
Pssm-ID: 182772 [Multi-domain] Cd Length: 924 Bit Score: 79.25 E-value: 8.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 792 LAYIKRQIRNPLSGIMFTRKMIEGTELGPEQRRILQT----SALCQKQLSKILDDSDLESiiEGcLDLEMKEFTLNEVLT 867
Cdd:PRK10841 451 LATVSHELRTPLYGIIGNLDLLQTKELPKGVDRLVTAmnnsSSLLLKIISDILDFSKIES--EQ-LKIEPREFSPREVIN 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 868 ASTSQ----VMMKSNGKSVRItnetgEEVMSDTLYGDSIRLQQVLADFMLMAVNFTPSGGqLTVSASLRKDQlgrsvhla 943
Cdd:PRK10841 528 HITANylplVVKKRLGLYCFI-----EPDVPVALNGDPMRLQQVISNLLSNAIKFTDTGC-IVLHVRVDGDY-------- 593
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 186478305 944 nLEIRLTHTGAGIPEFLLNQMF--------GTEEDVSEEGLSLMVSRKLVKLMNGDVQYLRQAGKSS-FII 1005
Cdd:PRK10841 594 -LSFRVRDTGVGIPAKEVVRLFdpffqvgtGVQRNFQGTGLGLAICEKLINMMDGDISVDSEPGMGSqFTI 663
|
|
| HATPase_c |
pfam02518 |
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ... |
899-1010 |
2.04e-14 |
|
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: 70.09 E-value: 2.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 899 GDSIRLQQVLADFMLMAVNFTPSGGQLTVSasLRKDqlgrsvhlANLEIRLTHTGAGIPEFLLNQMFG-----TEEDVSE 973
Cdd:pfam02518 1 GDELRLRQVLSNLLDNALKHAAKAGEITVT--LSEG--------GELTLTVEDNGIGIPPEDLPRIFEpfstaDKRGGGG 70
|
90 100 110
....*....|....*....|....*....|....*...
gi 186478305 974 EGLSLMVSRKLVKLMNGDVQYLRQAGK-SSFIITAELA 1010
Cdd:pfam02518 71 TGLGLSIVRKLVELLGGTITVESEPGGgTTVTLTLPLA 108
|
|
| NtrY |
COG5000 |
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
658-1006 |
8.78e-13 |
|
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: 71.53 E-value: 8.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 658 IFGTDEFGWCTEWNPAMSKLTGLKREEVIDKmLLGEVFGTQksccrlknqeafvNLGIVLNNAVTSQDPEKVSFaffTRG 737
Cdd:COG5000 103 VIVLDADGRITLANPAAERLLGIPLEELIGK-PLEELLPEL-------------DLAELLREALERGWQEEIEL---TRD 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 738 GKyvECLLCVSKKLDREGVVtgvfcflqLASHELQQALHVQRLAertAVKRLkalayIKR---QIRNPLSGI-----MFT 809
Cdd:COG5000 166 GR--RTLLVRASPLRDDGYV--------IVFDDITELLRAERLA---AWGEL-----ARRiahEIKNPLTPIqlsaeRLR 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 810 RKMIEGTELGPEQRrilqtsalcQKQLSKILDDSD-LESIIEGCLDL------EMKEFTLNEVLTASTSQVMMKSNGKSV 882
Cdd:COG5000 228 RKLADKLEEDREDL---------ERALDTIIRQVDrLKRIVDEFLDFarlpepQLEPVDLNELLREVLALYEPALKEKDI 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 883 RITNETGEEVMsdTLYGDSIRLQQVLADFMLMAVNFTPSGGQLTVSASLRKDQlgrsvhlanLEIRLTHTGAGIPEFLLN 962
Cdd:COG5000 299 RLELDLDPDLP--EVLADRDQLEQVLINLLKNAIEAIEEGGEIEVSTRREDGR---------VRIEVSDNGPGIPEEVLE 367
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 186478305 963 QMF---------GTeedvseeGLSLMVSRKLVKLMNGDVQYLRQAGK-SSFIIT 1006
Cdd:COG5000 368 RIFepffttkpkGT-------GLGLAIVKKIVEEHGGTIELESRPGGgTTFTIR 414
|
|
| GAF |
smart00065 |
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ... |
111-296 |
1.88e-12 |
|
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these domains in PDE6B result in autosomal recessive inheritance of retinitis pigmentosa.
Pssm-ID: 214500 [Multi-domain] Cd Length: 149 Bit Score: 65.87 E-value: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 111 MERLCDTMVQEVFELTGYDRVMAYKFHEDDHGEVVSEVTKPGLEPYLGLHYPATDipQAARFLFMKNKVRMIVDCNAkha 190
Cdd:smart00065 2 LEELLQTILEELRQLLGADRVLIYLVDENDRGELVLVAADGLTLPTLGIRFPLDE--GLAGRVAETGRPLNIPDVEA--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 191 rvlqdeklsfdltlcgstlrAPHSCHLQYMANMDSIASLVMAVVVNEEdgegdapdattqpqkrkrLWGLVVCHNTTprf 270
Cdd:smart00065 77 --------------------DPLFAEDLLGRYQGVRSFLAVPLVADGE------------------LVGVLALHNKK--- 115
|
170 180
....*....|....*....|....*.
gi 186478305 271 VPFPLRYACEFLAQVFAIHVNKEVEL 296
Cdd:smart00065 116 SPRPFTEEDEELLQALANQLAIALAN 141
|
|
| PRK11107 |
PRK11107 |
hybrid sensory histidine kinase BarA; Provisional |
788-1009 |
2.38e-12 |
|
hybrid sensory histidine kinase BarA; Provisional
Pssm-ID: 236848 [Multi-domain] Cd Length: 919 Bit Score: 71.42 E-value: 2.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 788 RLKA--LAYIKRQIRNPLSG-IMFTRKMIEgTELGPEQRRILQT---SA---LCQkqLSKILDDSDLESiieGCLDLEMK 858
Cdd:PRK11107 291 RIKSefLANMSHELRTPLNGvIGFTRQTLK-TPLTPTQRDYLQTierSAnnlLAI--INDILDFSKLEA---GKLVLENI 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 859 EF----TLNEVLT--ASTSQvmmksnGKSVRITNETGEEVmSDTLYGDSIRLQQVLADFMLMAVNFTPSgGQLTVSASLR 932
Cdd:PRK11107 365 PFslreTLDEVVTllAHSAH------EKGLELTLNIDPDV-PDNVIGDPLRLQQIITNLVGNAIKFTES-GNIDILVELR 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 933 KdQLGRSVHlanLEIRLTHTGAGIPEFLLNQMF---------------GTeedvseeGLSLMVSRKLVKLMNGDVQYLRQ 997
Cdd:PRK11107 437 A-LSNTKVQ---LEVQIRDTGIGISERQQSQLFqafrqadasisrrhgGT-------GLGLVITQKLVNEMGGDISFHSQ 505
|
250
....*....|....*
gi 186478305 998 AGKSS---FIITAEL 1009
Cdd:PRK11107 506 PNRGStfwFHLPLDL 520
|
|
| HATPase_EvgS-ArcB-TorS-like |
cd16922 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ... |
904-1009 |
2.04e-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: 58.66 E-value: 2.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 904 LQQVLADFMLMAVNFTPSGgQLTVSASLRKDQLGRSVhlanLEIRLTHTGAGIPEFLLNQMF---------------GTe 968
Cdd:cd16922 1 LRQILLNLLGNAIKFTEEG-EVTLRVSLEEEEEDGVQ----LRFSVEDTGIGIPEEQQARLFepfsqadssttrkygGT- 74
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 186478305 969 edvseeGLSLMVSRKLVKLMNGDVQYLRQAGK-SSFIITAEL 1009
Cdd:cd16922 75 ------GLGLAISKKLVELMGGDISVESEPGQgSTFTFTLPL 110
|
|
| GAF |
pfam01590 |
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ... |
110-294 |
2.40e-10 |
|
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl cyclases, phytochromes, FhlA and NifA. Adenylyl and guanylyl cyclases catalyze ATP and GTP to the second messengers cAMP and cGMP, respectively, these products up-regulating catalytic activity by binding to the regulatory GAF domain(s). The opposite hydrolysis reaction is catalyzed by phosphodiesterase. cGMP-dependent 3',5'-cyclic phosphodiesterase catalyzes the conversion of guanosine 3',5'-cyclic phosphate to guanosine 5'-phosphate. Here too, cGMP regulates catalytic activity by GAF-domain binding. Phytochromes are regulatory photoreceptors in plants and bacteria which exist in two thermally-stable states that are reversibly inter-convertible by light: the Pr state absorbs maximally in the red region of the spectrum, while the Pfr state absorbs maximally in the far-red region. This domain is also found in FhlA (formate hydrogen lyase transcriptional activator) and NifA, a transcriptional activator which is required for activation of most Nif operons which are directly involved in nitrogen fixation. NifA interacts with sigma-54. This domain can bind biliverdine and phycocyanobilin (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 460259 [Multi-domain] Cd Length: 133 Bit Score: 59.41 E-value: 2.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 110 SMERLCDTMVQEVFELTGYDRVMAYkfheddhgevvsevtkpgLEPYLGLHYpatdIPQAARFLfmknKVRMIVDCNAKH 189
Cdd:pfam01590 1 DLEEILQTILEELRELLGADRCALY------------------LPDADGLEY----LPPGARWL----KAAGLEIPPGTG 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 190 ARVLQDEKlsfDLTLCGStlrAPHSCHLQ---YMANMDSIASLVMAVVVNEedgegdapdattqpqkrkRLWGLVVCHNT 266
Cdd:pfam01590 55 VTVLRTGR---PLVVPDA---AGDPRFLDpllLLRNFGIRSLLAVPIIDDG------------------ELLGVLVLHHP 110
|
170 180
....*....|....*....|....*...
gi 186478305 267 TPRFvpfpLRYACEFLaQVFAIHVNKEV 294
Cdd:pfam01590 111 RPPF----TEEELELL-EVLADQVAIAL 133
|
|
| PRK10364 |
PRK10364 |
two-component system sensor histidine kinase ZraS; |
778-1005 |
2.41e-10 |
|
two-component system sensor histidine kinase ZraS;
Pssm-ID: 236674 [Multi-domain] Cd Length: 457 Bit Score: 64.04 E-value: 2.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 778 QRLAERTAVK-RLKAL----AYIKRQIRNPLSGIM-FTRKMIEGTELGPEQRRILQTSALCQKQLSKILddSDLESIIEG 851
Cdd:PRK10364 222 QLLQDEMKRKeKLVALghlaAGVAHEIRNPLSSIKgLAKYFAERAPAGGEAHQLAQVMAKEADRLNRVV--SELLELVKP 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 852 ClDLEMKEFTLNEVLTASTSQVMM--KSNGKSVRIT-NETGEEVMSDtlygdSIRLQQVLADFMLMAVNFTPSGGQLTVS 928
Cdd:PRK10364 300 T-HLALQAVDLNDLINHSLQLVSQdaNSREIQLRFTaNDTLPEIQAD-----PDRLTQVLLNLYLNAIQAIGQHGVISVT 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 929 ASLRKDQlgrsvhlanLEIRLTHTGAGIP----EFLLNQMFGTEEDVSeeGLSLMVSRKLVKLMNGDVQYLRQAGKSS-F 1003
Cdd:PRK10364 374 ASESGAG---------VKISVTDSGKGIAadqlEAIFTPYFTTKAEGT--GLGLAVVHNIVEQHGGTIQVASQEGKGAtF 442
|
..
gi 186478305 1004 II 1005
Cdd:PRK10364 443 TL 444
|
|
| HisKA |
smart00388 |
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ... |
787-850 |
5.70e-10 |
|
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine kinases.
Pssm-ID: 214644 [Multi-domain] Cd Length: 66 Bit Score: 56.04 E-value: 5.70e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 186478305 787 KRLKALAYIKRQIRNPLSGIMFTRKMIEGTELGPEQRRILQTSALCQKQLSKILDDSDLESIIE 850
Cdd:smart00388 1 AKREFLANLSHELRTPLTAIRGYLELLLDTELSEEQREYLETILREAERLLRLINDLLDLSRIE 64
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
513-632 |
1.44e-09 |
|
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: 56.92 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 513 EMVRLI-ETATVPILAVDSDGLVNGWNTKIAELTGLSVDEAIGKHFLTLVEDSSVEIVKRMLENALEGTEEQNVQFEIKT 591
Cdd:TIGR00229 3 ERYRAIfESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEPEPVSEERRVR 82
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 186478305 592 hlsRADAGPISLVVNAcASRDLHENVVGVCFVAHDLTGQKT 632
Cdd:TIGR00229 83 ---RKDGSEIWVEVSV-SPIRTNGGELGVVGIVRDITERKE 119
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
521-627 |
1.63e-09 |
|
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: 56.10 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 521 ATVPILAVDSDGLVNGWNTKIAELTGLSVDEAIGKHFLTLVEDSSVEIVKRMLENALEGTEEQNVQFEIKTHlsraDAGP 600
Cdd:cd00130 1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRK----DGSV 76
|
90 100
....*....|....*....|....*..
gi 186478305 601 ISLVVNACASRDLHENVVGVCFVAHDL 627
Cdd:cd00130 77 IWVLVSLTPIRDEGGEVIGLLGVVRDI 103
|
|
| KinB |
COG5806 |
Sporulation sensor histidine kinase B [Cell cycle control, cell division, chromosome ... |
793-1006 |
1.82e-09 |
|
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: 61.04 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 793 AYIKRQIRNPLS---GIMftrKMIEGTELGPEQRRilQTSALCQKQLSKIlddsdlESIIEGCLDL------EMKEFTLN 863
Cdd:COG5806 206 ASIAHEVRNPLTvvrGFI---QLLQEPELSDEKRK--QYIRIALEELDRA------EAIITDYLTFakpqpeKLEKIDVS 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 864 EVLTASTSqvMMKS--NGKSVRITNETGEEVmsdTLYGDSIRLQQVLADFMLMAVNFTPSGGQLTVSASLRKDQlgrsVH 941
Cdd:COG5806 275 EELEHVID--VLSPyaNMNNVEIQTELEPGL---YIEGDRQKLQQCLINIIKNGIEAMPNGGTLTIDVSIDKNK----VI 345
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 942 lanleIRLTHTGAGIPEFLLNQM----FGTEEDVSeeGLSLMVSRKLVKLMNGDVQYLRQAGK-SSFIIT 1006
Cdd:COG5806 346 -----ISIKDTGVGMTKEQLERLgepyFSTKEKGT--GLGTMVSYRIIEAMNGTIRVESEVGKgTTFTIT 408
|
|
| PRK11091 |
PRK11091 |
aerobic respiration control sensor protein ArcB; Provisional |
795-1006 |
1.97e-09 |
|
aerobic respiration control sensor protein ArcB; Provisional
Pssm-ID: 236842 [Multi-domain] Cd Length: 779 Bit Score: 61.50 E-value: 1.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 795 IKRQIRNPLSGIMFTRKMIEGTELGPEQRRILQT---SALcqkQLSKILDDsdlesIIEgcLD-------------LEMK 858
Cdd:PRK11091 290 ISHELRTPLNGIVGLSRILLDTELTAEQRKYLKTihvSAI---TLGNIFND-----IID--MDkmerrklqldnqpIDFT 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 859 EFtLNEVLTASTSQVmmksNGKSVRITNETgEEVMSDTLYGDSIRLQQVLADFMLMAVNFTPSGG-QLTVSASLRKDqlg 937
Cdd:PRK11091 360 DF-LADLENLSGLQA----EQKGLRFDLEP-LLPLPHKVITDGTRLRQILWNLISNAVKFTQQGGvTVRVRYEEGDM--- 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 938 rsvhlanLEIRLTHTGAGIPEFLLNQMF----------------GTeedvseeGLSLMVSRKLVKLMNGDVQYLRQAGK- 1000
Cdd:PRK11091 431 -------LTFEVEDSGIGIPEDELDKIFamyyqvkdshggkpatGT-------GIGLAVSKRLAQAMGGDITVTSEEGKg 496
|
....*.
gi 186478305 1001 SSFIIT 1006
Cdd:PRK11091 497 SCFTLT 502
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
505-631 |
2.58e-09 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 59.27 E-value: 2.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 505 QELEAVTSEMVRLIETATVPILAVDSDGLVNGWNTKIAELTGLSVDEAIGKHFLTLVEDSSVEIVKRMLENALEGTEEqn 584
Cdd:COG2202 130 EALRESEERLRLLVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEGGRE-- 207
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 186478305 585 vQFEIKTHLSRADAGPISLVVNAcASRDLHENVVGVCFVAHDLTGQK 631
Cdd:COG2202 208 -SYELELRLKDGDGRWVWVEASA-VPLRDGGEVIGVLGIVRDITERK 252
|
|
| PRK11360 |
PRK11360 |
two-component system sensor histidine kinase AtoS; |
662-993 |
3.68e-09 |
|
two-component system sensor histidine kinase AtoS;
Pssm-ID: 236901 [Multi-domain] Cd Length: 607 Bit Score: 60.75 E-value: 3.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 662 DEFGWCTEWNPAMSKLTGLKREEVIDKMLlGEVFgtqksccrlKNQEAFVNlgIVLNN-----AVTSQDPEkvsfafFTR 736
Cdd:PRK11360 279 DRQGKITTMNPAAEVITGLQRHELVGKPY-SELF---------PPNTPFAS--PLLDTlehgtEHVDLEIS------FPG 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 737 GGKYVECLLCVSKKLDREGVVTG-VFCFLQLASH-ELQQALHVQ-RLAertAVKRLkaLAYIKRQIRNPLSGIMFTRKMI 813
Cdd:PRK11360 341 RDRTIELSVSTSLLHNTHGEMIGaLVIFSDLTERkRLQRRVARQeRLA---ALGEL--VAGVAHEIRNPLTAIRGYVQIW 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 814 EGTELGPEQrrilqtsalcQKQLSKILDDSD-LESIIEGCLDL------EMKEFTLNEvLTASTSQVMMKSNGKS-VRIT 885
Cdd:PRK11360 416 RQQTSDPPS----------QEYLSVVLREVDrLNKVIDQLLEFsrpresQWQPVSLNA-LVEEVLQLFQTAGVQArVDFE 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 886 NETGEEVmsDTLYGDSIRLQQVLADFMLMAVNFTPSGGQLTVSASLRKDqlgrsvhlANLEIRLTHTGAGIPEFLLNQMF 965
Cdd:PRK11360 485 TELDNEL--PPIWADPELLKQVLLNILINAVQAISARGKIRIRTWQYSD--------GQVAVSIEDNGCGIDPELLKKIF 554
|
330 340 350
....*....|....*....|....*....|....*..
gi 186478305 966 ---------GTeedvseeGLSLMVSRKLVKLMNGDVQ 993
Cdd:PRK11360 555 dpffttkakGT-------GLGLALSQRIINAHGGDIE 584
|
|
| HisKA |
pfam00512 |
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ... |
787-851 |
5.51e-09 |
|
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine kinases.
Pssm-ID: 459839 [Multi-domain] Cd Length: 66 Bit Score: 53.37 E-value: 5.51e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 186478305 787 KRLKALAYIKRQIRNPLSGIMFTRKMIEGTELGPEQRRILQTSALCQKQLSKILDD-SDLESIIEG 851
Cdd:pfam00512 1 AKSEFLANLSHELRTPLTAIRGYLELLRDEKLDEEQREYLETILRSAERLLRLINDlLDLSRIEAG 66
|
|
| COG4191 |
COG4191 |
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ... |
764-1006 |
1.19e-08 |
|
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal transduction mechanisms];
Pssm-ID: 443345 [Multi-domain] Cd Length: 361 Bit Score: 58.27 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 764 LQLASHELQQA----LHVQRLAertAVKRLKA-LAYikrQIRNPLSGIM----FTRKMIEGTELGPEQRRILQTSALCQK 834
Cdd:COG4191 119 LERAEEELRELqeqlVQSEKLA---ALGELAAgIAH---EINNPLAAILgnaeLLRRRLEDEPDPEELREALERILEGAE 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 835 QLSKILDD----SDLESiiegcldLEMKEFTLNEVL--TASTSQVMMKSNGksVRITNETGEEVMsdTLYGDSIRLQQVL 908
Cdd:COG4191 193 RAAEIVRSlrafSRRDE-------EEREPVDLNELIdeALELLRPRLKARG--IEVELDLPPDLP--PVLGDPGQLEQVL 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 909 ADFMLMAVNFTPSG--GQLTVSASLRKDQLgrsvhlanlEIRLTHTGAGIPEFLLNQMF-----------GTeedvseeG 975
Cdd:COG4191 262 LNLLINAIDAMEEGegGRITISTRREGDYV---------VISVRDNGPGIPPEVLERIFepffttkpvgkGT-------G 325
|
250 260 270
....*....|....*....|....*....|..
gi 186478305 976 LSLMVSRKLVKLMNGDVQYLRQAGK-SSFIIT 1006
Cdd:COG4191 326 LGLSISYGIVEKHGGRIEVESEPGGgTTFTIT 357
|
|
| PRK11466 |
PRK11466 |
hybrid sensory histidine kinase TorS; Provisional |
764-1002 |
1.23e-08 |
|
hybrid sensory histidine kinase TorS; Provisional
Pssm-ID: 236914 [Multi-domain] Cd Length: 914 Bit Score: 59.15 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 764 LQLASHELQQAL--HVQRLAERTAVKRLKA--LAYIKRQIRNPLSGIMFTRKMIEGTELGPEQRRILQTSALCQKQLSKI 839
Cdd:PRK11466 416 VKARTAELQELVieHRQARAEAEKASQAKSafLAAMSHEIRTPLYGILGTAQLLADNPALNAQRDDLRAITDSGESLLTI 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 840 LDDS-DLESIIEGCLDLEMKE--FTLNEVLTASTSQVMMKSNGKSVRITNETGEEVMSdTLYGDSIRLQQVLADFMLMAV 916
Cdd:PRK11466 496 LNDIlDYSAIEAGGKNVSVSDepFEPRPLLESTLQLMSGRVKGRPIRLATDIADDLPT-ALMGDPRRIRQVITNLLSNAL 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 917 NFTPSGgqlTVSASLRKDQlgrsvhlANLEIRLTHTGAGIPEFLLNQMFGTEEDVSEE----GLSLMVSRKLVKLMNGDV 992
Cdd:PRK11466 575 RFTDEG---SIVLRSRTDG-------EQWLVEVEDSGCGIDPAKLAEIFQPFVQVSGKrggtGLGLTISSRLAQAMGGEL 644
|
250
....*....|
gi 186478305 993 QYLRQAGKSS 1002
Cdd:PRK11466 645 SATSTPEVGS 654
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
516-578 |
1.41e-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.
Pssm-ID: 214512 Cd Length: 67 Bit Score: 52.40 E-value: 1.41e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 186478305 516 RLIETATVPILAVDSDGLVNGWNTKIAELTGLSVDEAIGKHFLTLVEDSSVEIVKRMLENALE 578
Cdd:smart00091 5 AILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLLS 67
|
|
| PAS_4 |
pfam08448 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
523-628 |
9.79e-08 |
|
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: 51.26 E-value: 9.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 523 VPILAVDSDGLVNGWNTKIAELTGLSVDEAIGKHFLTLVEDSSVEIVKRMLENALEGteEQNVQFEIKTHLSRADAgpiS 602
Cdd:pfam08448 6 DALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAELLPPEDAARLERALRRALEG--EEPIDFLEELLLNGEER---H 80
|
90 100
....*....|....*....|....*.
gi 186478305 603 LVVNACASRDLHENVVGVCFVAHDLT 628
Cdd:pfam08448 81 YELRLTPLRDPDGEVIGVLVISRDIT 106
|
|
| RocR |
COG3829 |
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ... |
504-641 |
1.65e-07 |
|
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: 54.78 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 504 IQELEAVTSEMVRLIETATVPILAVDSDGLVNGWNTKIAELTGLSVDEAIGKHFLTLVEDSSVEIVKRmlenalEGTEEQ 583
Cdd:COG3829 3 ELELKELEEELEAILDSLDDGIIVVDADGRITYVNRAAERILGLPREEVIGKNVTELIPNSPLLEVLK------TGKPVT 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 186478305 584 NVQFEIKThlsradaGPISLVVNACASRDlHENVVGVCFVAHDLTGQKTVMDKFTRIE 641
Cdd:COG3829 77 GVIQKTGG-------KGKTVIVTAIPIFE-DGEVIGAVETFRDITELKRLERKLREEE 126
|
|
| PRK11360 |
PRK11360 |
two-component system sensor histidine kinase AtoS; |
518-641 |
1.90e-07 |
|
two-component system sensor histidine kinase AtoS;
Pssm-ID: 236901 [Multi-domain] Cd Length: 607 Bit Score: 54.97 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 518 IETATVPILAVDSDGLVNGWNTKIAELTGLSVDEAIGKHFLTLVEDSS--VEIVKRMLENaleGTEEqnVQFEIKTHlsr 595
Cdd:PRK11360 268 LESIADGVIAIDRQGKITTMNPAAEVITGLQRHELVGKPYSELFPPNTpfASPLLDTLEH---GTEH--VDLEISFP--- 339
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 186478305 596 ADAGPISLVVNACASRDLHENVVGVCFVAHDLTGQKTVMDKFTRIE 641
Cdd:PRK11360 340 GRDRTIELSVSTSLLHNTHGEMIGALVIFSDLTERKRLQRRVARQE 385
|
|
| PRK09959 |
PRK09959 |
acid-sensing system histidine kinase EvgS; |
768-1006 |
5.18e-07 |
|
acid-sensing system histidine kinase EvgS;
Pssm-ID: 182169 [Multi-domain] Cd Length: 1197 Bit Score: 53.97 E-value: 5.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 768 SHELQQALHVQR-LAERTAVKRLKALAYIKRQIRNPLSGIMFTRKMIEGTELGPEQR--RILQTSALCQKQLSKILDDSD 844
Cdd:PRK09959 691 TRDLIHALEVERnKAINATVAKSQFLATMSHEIRTPISSIMGFLELLSGSGLSKEQRveAISLAYATGQSLLGLIGEILD 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 845 LESIIEGCLDLEMKEFTLNEVLTASTSQVMMKSNGKSVRITNETgeeVMSD--TLYGDSIRLQQVLADFMLMAVNFTPSG 922
Cdd:PRK09959 771 VDKIESGNYQLQPQWVDIPTLVQNTCHSFGAIAASKSIALSCSS---TFPDhyLVKIDPQAFKQVLSNLLSNALKFTTEG 847
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 923 GqLTVSASLrkdqlgrsVHL----ANLEIRLTHTGAGIPEFLLNQMFGTEEDVSE------EGLSLMVSRKLVKLMNGDV 992
Cdd:PRK09959 848 A-VKITTSL--------GHIddnhAVIKMTIMDSGSGLSQEEQQQLFKRYSQTSAgrqqtgSGLGLMICKELIKNMQGDL 918
|
250
....*....|....*
gi 186478305 993 QYLRQAG-KSSFIIT 1006
Cdd:PRK09959 919 SLESHPGiGTTFTIT 933
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
654-765 |
8.46e-07 |
|
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: 48.40 E-value: 8.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 654 LIPPIFGTDEFGWCTEWNPAMSKLTGLKREEVIDKMLLGEVFGTQksccRLKNQEAfvnlgivLNNAVTSQDPEKVSFAF 733
Cdd:cd00130 1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPED----REELRER-------LENLLSGGEPVTLEVRL 69
|
90 100 110
....*....|....*....|....*....|..
gi 186478305 734 FTRGGKYVECLLCVSKKLDREGVVTGVFCFLQ 765
Cdd:cd00130 70 RRKDGSVIWVLVSLTPIRDEGGEVIGLLGVVR 101
|
|
| PRK11100 |
PRK11100 |
sensory histidine kinase CreC; Provisional |
770-993 |
5.32e-06 |
|
sensory histidine kinase CreC; Provisional
Pssm-ID: 236846 [Multi-domain] Cd Length: 475 Bit Score: 50.23 E-value: 5.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 770 ELQQALHVQRLaertavkRLKALAYIKRQIRN-------PLSGIMFTRKMIEGtELGPEQRR-----ILQTSALCQKQLS 837
Cdd:PRK11100 238 ELAQALESMRV-------KLEGKAYVEQYVQTlthelksPLAAIRGAAELLQE-DPPPEDRArftgnILTQSARLQQLID 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 838 KILDDSDLESI--IEGCLDLEMKEFtLNEVLTASTSQVmmksNGKSVRITNETGEEVMSdtlyGDSIRLQQVLADFMLMA 915
Cdd:PRK11100 310 RLLELARLEQRqeLEVLEPVALAAL-LEELVEAREAQA----AAKGITLRLRPDDARVL----GDPFLLRQALGNLLDNA 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 916 VNFTPSGGQLTVSASLRKDQlgrsvhlanLEIRLTHTGAGIPEFLLNQMF---------GTEEDVSeeGLSLMVSRKLVK 986
Cdd:PRK11100 381 IDFSPEGGTITLSAEVDGEQ---------VALSVEDQGPGIPDYALPRIFerfyslprpANGRKST--GLGLAFVREVAR 449
|
....*..
gi 186478305 987 LMNGDVQ 993
Cdd:PRK11100 450 LHGGEVT 456
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
643-691 |
7.26e-06 |
|
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: 44.70 E-value: 7.26e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 186478305 643 DYKAIIQNpnpLIPPIFGTDEFGWCTEWNPAMSKLTGLKREEVIDKMLL 691
Cdd:smart00091 2 RLRAILES---LPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLL 47
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
537-628 |
8.78e-06 |
|
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: 45.14 E-value: 8.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 537 WNTKIAELTGLSVDEAIGKHFLTLVEDSSVEIVKRMLENALEGTEEQNVQFEikthlsRADAGPISLVVNACASRDLHEN 616
Cdd:pfam13426 7 VNDAALRLLGYTREELLGKSITDLFAEPEDSERLREALREGKAVREFEVVLY------RKDGEPFPVLVSLAPIRDDGGE 80
|
90
....*....|..
gi 186478305 617 VVGVCFVAHDLT 628
Cdd:pfam13426 81 LVGIIAILRDIT 92
|
|
| HATPase_CreC-like |
cd16945 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
900-993 |
1.67e-05 |
|
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: 44.76 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 900 DSIRLQQVLADFMLMAVNFTPSGGQLTVSASLRKDQlgrsvhlanLEIRLTHTGAGIPEFLLNQMFGT-------EEDVS 972
Cdd:cd16945 1 DPFLLRQAINNLLDNAIDFSPEGGLIALQLEADTEG---------IELLVFDEGSGIPDYALNRVFERfyslprpHSGQK 71
|
90 100
....*....|....*....|.
gi 186478305 973 EEGLSLMVSRKLVKLMNGDVQ 993
Cdd:cd16945 72 STGLGLAFVQEVAQLHGGRIT 92
|
|
| HisKA |
cd00082 |
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ... |
792-842 |
4.81e-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: 39.50 E-value: 4.81e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 186478305 792 LAYIKRQIRNPLSGIMFTRKMIEGTELGPE-QRRILQTSALCQKQLSKILDD 842
Cdd:cd00082 8 LANVSHELRTPLTAIRGALELLEEELLDDEeQREYLERIREEAERLLRLIND 59
|
|
| HATPase_TutC-TodS-like |
cd16925 |
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ... |
900-992 |
4.95e-04 |
|
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas putida TodS and Thauera aromatica TutC; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinase (HKs) such Pseudomonas putida TodS HK of the TodS-TodT two-component regulatory system (TCS) which controls the expression of a toluene degradation pathway. Thauera aromatica TutC may be part of a TCS that is involved in anaerobic toluene metabolism. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), PAS sensor domain(s) and a REC domain.
Pssm-ID: 340402 [Multi-domain] Cd Length: 110 Bit Score: 40.55 E-value: 4.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 900 DSIRLQQVLADFMLMAVNFTPSGGQltVSASLRKDQLGRSVhlanleIRLTHTGAGIPEFLLNQMFGTEEDVSEE----- 974
Cdd:cd16925 1 DAEKYERVVLNLLSNAFKFTPDGGR--IRCILEKFRLNRFL------LTVSDSGPGIPPNLREEIFERFRQGDGSstrah 72
|
90 100
....*....|....*....|.
gi 186478305 975 ---GLSLMVSRKLVKLMNGDV 992
Cdd:cd16925 73 ggtGLGLSIVKEFVELHGGTV 93
|
|
| PRK13560 |
PRK13560 |
hypothetical protein; Provisional |
499-692 |
1.09e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 106506 [Multi-domain] Cd Length: 807 Bit Score: 43.12 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 499 LKIDGIQELEAVTSEMVR----LIETATVPILAVDSDGLVNGWNTKIAELTGLSVDEAIGKHFLTLVEDSSVEIVKRMLE 574
Cdd:PRK13560 187 EDITERKRAEERIDEALHflqqLLDNIADPAFWKDEDAKVFGCNDAACLACGFRREEIIGMSIHDFAPAQPADDYQEADA 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 575 NALEGTEEQNVQFEIKTHLSRADagPISLVVNACASRDLHENVVGVCFVAHDLTGQKTVMDKFTRIEGDYKAIIQnpnpL 654
Cdd:PRK13560 267 AKFDADGSQIIEAEFQNKDGRTR--PVDVIFNHAEFDDKENHCAGLVGAITDISGRRAAERELLEKEDMLRAIIE----A 340
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 186478305 655 IP-PIFGTDEFG-WCTEWNPAMSKLTGLKREEVIDKMLLG 692
Cdd:PRK13560 341 APiAAIGLDADGnICFVNNNAAERMLGWSAAEVMGKPLPG 380
|
|
| PRK09303 |
PRK09303 |
histidine kinase; |
896-958 |
1.35e-03 |
|
histidine kinase;
Pssm-ID: 236462 [Multi-domain] Cd Length: 380 Bit Score: 42.25 E-value: 1.35e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 186478305 896 TLYGDSIRLQQVLADFMLMAVNFTPSGGQLTVSASLRKDQlgrsvhlaNLEIRLTHTGAGIPE 958
Cdd:PRK09303 265 SVYADQERIRQVLLNLLDNAIKYTPEGGTITLSMLHRTTQ--------KVQVSICDTGPGIPE 319
|
|
| HATPase_ETR2_ERS2-EIN4-like |
cd16938 |
Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related ... |
895-992 |
1.37e-03 |
|
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: 39.75 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 895 DTLYGDSIRLQQVLADFMLMAVNFTPSGGQLTVSASLRKDQLGRSVHLA----------NLEIRL------THTGAGIPE 958
Cdd:cd16938 3 DVVVGDERRVFQVLLHMLGNLLKMRNGGGNITFRVFLEGGSEDRSDRDWgpwrpsmsdeSVEIRFeveindSGSPSIESA 82
|
90 100 110
....*....|....*....|....*....|....*
gi 186478305 959 FLLN-QMFGTEEDVSEEGLSLMVSRKLVKLMNGDV 992
Cdd:cd16938 83 SMRNsLNRRYNLSELGEHLSFSICKQLVQLMGGNI 117
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
670-765 |
2.45e-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: 38.21 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478305 670 WNPAMSKLTGLKREEVIDKmLLGEVFGTQKSCCRLKNQEAfvnlgivlnnavTSQDPEKVSFAFFTRGGKYVECLLCVSK 749
Cdd:pfam13426 7 VNDAALRLLGYTREELLGK-SITDLFAEPEDSERLREALR------------EGKAVREFEVVLYRKDGEPFPVLVSLAP 73
|
90
....*....|....*.
gi 186478305 750 KLDREGVVTGVFCFLQ 765
Cdd:pfam13426 74 IRDDGGELVGIIAILR 89
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
644-691 |
9.08e-03 |
|
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: 37.27 E-value: 9.08e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 186478305 644 YKAIIQNPNPlipPIFGTDEFGWCTEWNPAMSKLTGLKREEVIDKMLL 691
Cdd:TIGR00229 5 YRAIFESSPD---AIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVL 49
|
|
| |
