|
Name |
Accession |
Description |
Interval |
E-value |
| COG3920 |
COG3920 |
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ... |
130-617 |
3.54e-60 |
|
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction mechanisms];
Pssm-ID: 443125 [Multi-domain] Cd Length: 495 Bit Score: 208.61 E-value: 3.54e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 130 IRDETGAIAGMFCAGAETTQTLLAERRLIDERERQKRMLQQMPGFAALLTGPEHRYEYVNDAYRQISGDRNFMGQAFREV 209
Cdd:COG3920 9 LLLALAALLLLAALLLLAAALLLALLALLLLALLLLALLLASALLALLALSAAALAAALAVALAAAVGAAAALLALLVLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 210 FPDIAGQGFYEIFDRVYESGEPFARRTMSVSLDREDGDRSIDLLVEPVRDNSGKVTGIFVGGFDITERVRAEGAVRESEA 289
Cdd:COG3920 89 LLLLLAAAALALALLLAALAGLLLLAALLLLRLVALLAALALLALLLLLLLLLAILALAELAVALAELAAALLLLAEELA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 290 RFRNMADHAPTMMWVTDAEGRCTYLNRAWYDFTGQSEAEGEGFGWLEAVHPDDRGWSGETFVSANANHEIFRvEYRLRRH 369
Cdd:COG3920 169 ALRLAAAALLLLLAALLDLGLALAALAAAALLALLLALELLLALLLLLLLLLALLLVLLAALLRLRAAVLEE-LERRRRA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 370 DGEYRWAIDAASPRFGSQGDFLGYIGTVIDIDDRREMEDALRDTSAHQILLINELNHRVKNTLATVQSIAMQTFRDrgga 449
Cdd:COG3920 248 RGLGRLLLLLLLLLLLLRALLLLAAGIRLVITERKRAEEELEASLEEKELLLRELHHRVKNNLQVVSSLLRLQARR---- 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 450 GASPEQRELFE---SRLIALAIAHDVLTR-ENWESAQLRDVV---LEAVAAHCGGDVNPFTVEGPEARLTPKMALGWSMA 522
Cdd:COG3920 324 ADDPEAREALEesqNRIQALALVHELLYQsEDWEGVDLRDYLrelLEPLRDSYGGRGIRIELDGPDVELPADAAVPLGLI 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 523 LHELCTNAVKYGALSVPDGTVAIRWSVEreekADQLNFIWEERGG---PSVTEPSSKGFGSRLIERqLARELGGHVElIY 599
Cdd:COG3920 404 LNELVTNALKHAFLSGEGGRIRVSWRRE----DGRLRLTVSDNGVglpEDVDPPARKGLGLRLIRA-LVRQLGGTLE-LD 477
|
490
....*....|....*...
gi 1905918357 600 APKGVNCTIKAPLSAADD 617
Cdd:COG3920 478 RPEGTRVRITFPLAELAA 495
|
|
| PRK13559 |
PRK13559 |
hypothetical protein; Provisional |
302-612 |
4.09e-34 |
|
hypothetical protein; Provisional
Pssm-ID: 237427 [Multi-domain] Cd Length: 361 Bit Score: 133.41 E-value: 4.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 302 MWVTDA-EGRC--TYLNRAWYDFTGQSEAE--GEGFGWLEAVHPDDRGWSgeTFVSANANHEIFRVEYRLRRHDGEYRWA 376
Cdd:PRK13559 56 MCITDPhQPDLpiVLANQAFLDLTGYAAEEvvGRNCRFLQGAATDPIAVA--KIRAAIAAEREIVVELLNYRKDGEPFWN 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 377 IDAASPRFGSQGDFLGYIGTVIDIDDRRemedALRDTSAHQILLINELNHRVKNTLATVQSIAMQTFRDRGgagASPEQR 456
Cdd:PRK13559 134 ALHLGPVYGEDGRLLYFFGSQWDVTDIR----AVRALEAHERRLAREVDHRSKNVFAVVDSIVRLTGRADD---PSLYAA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 457 ELFEsRLIALAIAHD-VLTRENWESAQLRDVVLEAVAAHcGGDVNPFTVEGPEARLTPKMALGWSMALHELCTNAVKYGA 535
Cdd:PRK13559 207 AIQE-RVQALARAHEtLLDERGWETVEVEELIRAQVAPY-APRATRVAFEGPGIRLGAASVQPLGLVLHELAVNAIKHGA 284
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1905918357 536 LSVPDGTVAIRWSVEREEKAdqLNFIWEERGGPSVTEPSSKGFGSRLIERQLARELGGHVELIYAPKGVNCTIKAPL 612
Cdd:PRK13559 285 LSADQGRISISWKPSPEGAG--FRIDWQEQGGPTPPKLAKRGFGTVIIGAMVESQLNGQLEKTWSDDGLLARIEIPS 359
|
|
| HWE_HK |
pfam07536 |
HWE histidine kinase; Two-component systems, consisting of a histidine kinase and a cognate ... |
423-508 |
1.48e-29 |
|
HWE histidine kinase; Two-component systems, consisting of a histidine kinase and a cognate response regulator protein, represent the best-known apparatus for transducing external cues into a physiological response in bacteria. The HWE domain is found in a subset of two-component system kinases, belonging to the same superfamily as pfam00512 and pfam07568. The family was defined by the presence of a highly conserved H residue in the kinase domain and a WxE motif in a C-terminal ATPase domain that is related to pfam02518. It has been demonstrated to show structural and functional correlation with pfam07568. These proteins are found in a variety of alpha- and gamma- proteobacteria, with significant enrichment in the rhizobia.
Pssm-ID: 429521 [Multi-domain] Cd Length: 83 Bit Score: 111.59 E-value: 1.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 423 ELNHRVKNTLATVQSIAMQTFRdrgGAGASPEQRELFESRLIALAIAHDVLTRENWESAQLRDVVLEAVAAHCGGDVNPF 502
Cdd:pfam07536 1 ELNHRVKNTLATVQSIARQTLR---NAASLDEFVEAFEGRLQALSRAHDLLSRASWAGADLSELLEAELAPYGGEAGTRI 77
|
....*.
gi 1905918357 503 TVEGPE 508
Cdd:pfam07536 78 TLSGPD 83
|
|
| HWE_HK |
smart00911 |
HWE histidine kinase; The HWE domain is found in a subset of two-component system kinases, ... |
423-508 |
4.45e-25 |
|
HWE histidine kinase; The HWE domain is found in a subset of two-component system kinases, belonging to the same superfamily as. In. the HWE family was defined by the presence of conserved a H residue and a WXE motifs and was limited to members of the proteobacteria. However, many homologues of this domain are lack the WXE motif. Furthermore, homologues are found in a wide range of Gram-positive and Gram-negative bacteria as well as in several archaea.
Pssm-ID: 214907 [Multi-domain] Cd Length: 84 Bit Score: 99.20 E-value: 4.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 423 ELNHRVKNTLATVQSIAMQTFRdrgGAGASPEQRELFESRLIALAIAHDVLTRENWESAQLRDVVLEAVAAHCGGDVNP- 501
Cdd:smart00911 1 ELNHRVKNLLAVVQAIARQTLR---SASSLEDFAEAFEGRLQALARAHDLLSRSDWSGADLRDLVRAELAPYGGPGDGEr 77
|
....*..
gi 1905918357 502 FTVEGPE 508
Cdd:smart00911 78 ITLSGPD 84
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
287-410 |
1.05e-23 |
|
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: 96.59 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 287 SEARFRNMADHAPTMMWVTDAEGRCTYLNRAWYDFTGQSEAEGEGFGWLEAVHPDDRGWS---------GEtfvsananH 357
Cdd:TIGR00229 1 SEERYRAIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVrerierrleGE--------P 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1905918357 358 EIFRVEYRLRRHDGEYRWAIDAASPRFgSQGDFLGYIGTVIDIDDRREMEDAL 410
Cdd:TIGR00229 73 EPVSEERRVRRKDGSEIWVEVSVSPIR-TNGGELGVVGIVRDITERKEAEEAL 124
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
298-400 |
1.36e-15 |
|
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: 72.67 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 298 APTMMWVTDAEGRCTYLNRAWYDFTGQSEAEGEGFGWLEAVHPDDRGWSGETFVSANANHEIFRVEYRLRRHDGEYRWAI 377
Cdd:cd00130 1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVL 80
|
90 100
....*....|....*....|...
gi 1905918357 378 DAASPRFGSQGDFLGYIGTVIDI 400
Cdd:cd00130 81 VSLTPIRDEGGEVIGLLGVVRDI 103
|
|
| PAS_4 |
pfam08448 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
47-149 |
1.03e-06 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain is associated to signalling systems and works as a signal sensor domain. It recognizes differently substituted aromatic hydrocarbons, oxygen, different dodecanoic acids, autoinducers, 3,5-dimethyl-pyrazin-2-ol and N-alanyl-aminoacetone (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 312075 [Multi-domain] Cd Length: 110 Bit Score: 47.79 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 47 MFVAWGPELSFLY-NDGYLPVFGTKHPDALGRPFREVWPEI-WDDLKPLIDAALSGESTWSenlpLVVERNGYPEEAWFT 124
Cdd:pfam08448 7 ALAVLDPDGRVRYaNAAAAELFGLPPEELLGKTLAELLPPEdAARLERALRRALEGEEPID----FLEELLLNGEERHYE 82
|
90 100
....*....|....*....|....*
gi 1905918357 125 FSYSPIRDETGAIAGMFCAGAETTQ 149
Cdd:pfam08448 83 LRLTPLRDPDGEVIGVLVISRDITE 107
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
67-177 |
1.91e-03 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 40.99 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 67 FGTKHPDALGRPFREVWPEIWDDLKPLIDAALSGESTWSENLPLVVeRNGypEEAWFTFSYSPIRDETGAIAgmfcagae 146
Cdd:COG3852 40 LGLSAEELLGRPLAELFPEDSPLRELLERALAEGQPVTEREVTLRR-KDG--EERPVDVSVSPLRDAEGEGG-------- 108
|
90 100 110
....*....|....*....|....*....|.
gi 1905918357 147 ttqtLLAERRLIDERERQKRMLQQMPGFAAL 177
Cdd:COG3852 109 ----VLLVLRDITERKRLERELRRAEKLAAV 135
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COG3920 |
COG3920 |
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ... |
130-617 |
3.54e-60 |
|
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction mechanisms];
Pssm-ID: 443125 [Multi-domain] Cd Length: 495 Bit Score: 208.61 E-value: 3.54e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 130 IRDETGAIAGMFCAGAETTQTLLAERRLIDERERQKRMLQQMPGFAALLTGPEHRYEYVNDAYRQISGDRNFMGQAFREV 209
Cdd:COG3920 9 LLLALAALLLLAALLLLAAALLLALLALLLLALLLLALLLASALLALLALSAAALAAALAVALAAAVGAAAALLALLVLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 210 FPDIAGQGFYEIFDRVYESGEPFARRTMSVSLDREDGDRSIDLLVEPVRDNSGKVTGIFVGGFDITERVRAEGAVRESEA 289
Cdd:COG3920 89 LLLLLAAAALALALLLAALAGLLLLAALLLLRLVALLAALALLALLLLLLLLLAILALAELAVALAELAAALLLLAEELA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 290 RFRNMADHAPTMMWVTDAEGRCTYLNRAWYDFTGQSEAEGEGFGWLEAVHPDDRGWSGETFVSANANHEIFRvEYRLRRH 369
Cdd:COG3920 169 ALRLAAAALLLLLAALLDLGLALAALAAAALLALLLALELLLALLLLLLLLLALLLVLLAALLRLRAAVLEE-LERRRRA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 370 DGEYRWAIDAASPRFGSQGDFLGYIGTVIDIDDRREMEDALRDTSAHQILLINELNHRVKNTLATVQSIAMQTFRDrgga 449
Cdd:COG3920 248 RGLGRLLLLLLLLLLLLRALLLLAAGIRLVITERKRAEEELEASLEEKELLLRELHHRVKNNLQVVSSLLRLQARR---- 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 450 GASPEQRELFE---SRLIALAIAHDVLTR-ENWESAQLRDVV---LEAVAAHCGGDVNPFTVEGPEARLTPKMALGWSMA 522
Cdd:COG3920 324 ADDPEAREALEesqNRIQALALVHELLYQsEDWEGVDLRDYLrelLEPLRDSYGGRGIRIELDGPDVELPADAAVPLGLI 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 523 LHELCTNAVKYGALSVPDGTVAIRWSVEreekADQLNFIWEERGG---PSVTEPSSKGFGSRLIERqLARELGGHVElIY 599
Cdd:COG3920 404 LNELVTNALKHAFLSGEGGRIRVSWRRE----DGRLRLTVSDNGVglpEDVDPPARKGLGLRLIRA-LVRQLGGTLE-LD 477
|
490
....*....|....*...
gi 1905918357 600 APKGVNCTIKAPLSAADD 617
Cdd:COG3920 478 RPEGTRVRITFPLAELAA 495
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
153-410 |
2.83e-42 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 153.26 E-value: 2.83e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 153 AERRLIDERERQKRMLQQMPGfAALLTGPEHRYEYVNDAYRQISG--DRNFMGQAFREVFPDIAGQGFYEIFDRVYESGE 230
Cdd:COG2202 2 AEEALEESERRLRALVESSPD-AIIITDLDGRILYVNPAFERLTGysAEELLGKTLRDLLPPEDDDEFLELLRAALAGGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 231 PFARRTMSVsldREDGD-RSIDLLVEPVRDNSGKVTGIFVGGFDITERVRAEGAVRESEARFRNMADHAPTMMWVTDAEG 309
Cdd:COG2202 81 VWRGELRNR---RKDGSlFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEERLRLLVENAPDGIFVLDLDG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 310 RCTYLNRAWYDFTGQSEAEGEGFGWLEAVHPDDRGWSGETFVSANANH-EIFRVEYRLRRHDGEYRWaIDAASPRFGSQG 388
Cdd:COG2202 158 RILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEGGrESYELELRLKDGDGRWVW-VEASAVPLRDGG 236
|
250 260
....*....|....*....|..
gi 1905918357 389 DFLGYIGTVIDIDDRREMEDAL 410
Cdd:COG2202 237 EVIGVLGIVRDITERKRAEEAL 258
|
|
| PRK13559 |
PRK13559 |
hypothetical protein; Provisional |
302-612 |
4.09e-34 |
|
hypothetical protein; Provisional
Pssm-ID: 237427 [Multi-domain] Cd Length: 361 Bit Score: 133.41 E-value: 4.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 302 MWVTDA-EGRC--TYLNRAWYDFTGQSEAE--GEGFGWLEAVHPDDRGWSgeTFVSANANHEIFRVEYRLRRHDGEYRWA 376
Cdd:PRK13559 56 MCITDPhQPDLpiVLANQAFLDLTGYAAEEvvGRNCRFLQGAATDPIAVA--KIRAAIAAEREIVVELLNYRKDGEPFWN 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 377 IDAASPRFGSQGDFLGYIGTVIDIDDRRemedALRDTSAHQILLINELNHRVKNTLATVQSIAMQTFRDRGgagASPEQR 456
Cdd:PRK13559 134 ALHLGPVYGEDGRLLYFFGSQWDVTDIR----AVRALEAHERRLAREVDHRSKNVFAVVDSIVRLTGRADD---PSLYAA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 457 ELFEsRLIALAIAHD-VLTRENWESAQLRDVVLEAVAAHcGGDVNPFTVEGPEARLTPKMALGWSMALHELCTNAVKYGA 535
Cdd:PRK13559 207 AIQE-RVQALARAHEtLLDERGWETVEVEELIRAQVAPY-APRATRVAFEGPGIRLGAASVQPLGLVLHELAVNAIKHGA 284
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1905918357 536 LSVPDGTVAIRWSVEREEKAdqLNFIWEERGGPSVTEPSSKGFGSRLIERQLARELGGHVELIYAPKGVNCTIKAPL 612
Cdd:PRK13559 285 LSADQGRISISWKPSPEGAG--FRIDWQEQGGPTPPKLAKRGFGTVIIGAMVESQLNGQLEKTWSDDGLLARIEIPS 359
|
|
| HWE_HK |
pfam07536 |
HWE histidine kinase; Two-component systems, consisting of a histidine kinase and a cognate ... |
423-508 |
1.48e-29 |
|
HWE histidine kinase; Two-component systems, consisting of a histidine kinase and a cognate response regulator protein, represent the best-known apparatus for transducing external cues into a physiological response in bacteria. The HWE domain is found in a subset of two-component system kinases, belonging to the same superfamily as pfam00512 and pfam07568. The family was defined by the presence of a highly conserved H residue in the kinase domain and a WxE motif in a C-terminal ATPase domain that is related to pfam02518. It has been demonstrated to show structural and functional correlation with pfam07568. These proteins are found in a variety of alpha- and gamma- proteobacteria, with significant enrichment in the rhizobia.
Pssm-ID: 429521 [Multi-domain] Cd Length: 83 Bit Score: 111.59 E-value: 1.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 423 ELNHRVKNTLATVQSIAMQTFRdrgGAGASPEQRELFESRLIALAIAHDVLTRENWESAQLRDVVLEAVAAHCGGDVNPF 502
Cdd:pfam07536 1 ELNHRVKNTLATVQSIARQTLR---NAASLDEFVEAFEGRLQALSRAHDLLSRASWAGADLSELLEAELAPYGGEAGTRI 77
|
....*.
gi 1905918357 503 TVEGPE 508
Cdd:pfam07536 78 TLSGPD 83
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
279-426 |
3.63e-27 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 110.88 E-value: 3.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 279 RAEGAVRESEARFRNMADHAPTMMWVTDAEGRCTYLNRAWYDFTGQSEAEGEGFGWLEAVHPDDRGWSGETFVSANANHE 358
Cdd:COG2202 1 TAEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGG 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1905918357 359 IFRVEYRLRRHDGEYRWAIDAASPRFGSQGDFLGYIGTVIDIDDRREMEDALRDTSAHQILLINELNH 426
Cdd:COG2202 81 VWRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEERLRLLVENAPD 148
|
|
| HWE_HK |
smart00911 |
HWE histidine kinase; The HWE domain is found in a subset of two-component system kinases, ... |
423-508 |
4.45e-25 |
|
HWE histidine kinase; The HWE domain is found in a subset of two-component system kinases, belonging to the same superfamily as. In. the HWE family was defined by the presence of conserved a H residue and a WXE motifs and was limited to members of the proteobacteria. However, many homologues of this domain are lack the WXE motif. Furthermore, homologues are found in a wide range of Gram-positive and Gram-negative bacteria as well as in several archaea.
Pssm-ID: 214907 [Multi-domain] Cd Length: 84 Bit Score: 99.20 E-value: 4.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 423 ELNHRVKNTLATVQSIAMQTFRdrgGAGASPEQRELFESRLIALAIAHDVLTRENWESAQLRDVVLEAVAAHCGGDVNP- 501
Cdd:smart00911 1 ELNHRVKNLLAVVQAIARQTLR---SASSLEDFAEAFEGRLQALARAHDLLSRSDWSGADLRDLVRAELAPYGGPGDGEr 77
|
....*..
gi 1905918357 502 FTVEGPE 508
Cdd:smart00911 78 ITLSGPD 84
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
151-413 |
4.23e-24 |
|
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: 106.21 E-value: 4.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 151 LLAERRLIDERERQKRMLQQMPgFAALLTGPEHRYEYVNDAYRQISGDR--NFMGQAFREVFPDIAGQGFYEIFDRVYES 228
Cdd:COG5809 4 SKMELQLRKSEQRFRSLFENAP-DAILILDLEGKILKVNPAAERIFGYTedELLGTNILDFLHPDDEKELREILKLLKEG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 229 GEpfaRRTMSVSLDREDGDR-SIDLLVEPVRDNSGKVTGIFVGGFDITERVRAEGAVRESEARFRNMADHAPTMMWVTDA 307
Cdd:COG5809 83 ES---RDELEFELRHKNGKRlEFSSKLSPIFDQNGDIEGMLAISRDITERKRMEEALRESEEKFRLIFNHSPDGIIVTDL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 308 EGRCTYLNRAWYDFTGQSEAEGEGFGWLEAVHPDDRGWSGETFVSANANHEIFRVEYRLRRHDGEYRWAIDAASPrFGSQ 387
Cdd:COG5809 160 DGRIIYANPAACKLLGISIEELIGKSILELIHSDDQENVAAFISQLLKDGGIAQGEVRFWTKDGRWRLLEASGAP-IKKN 238
|
250 260
....*....|....*....|....*.
gi 1905918357 388 GDFLGYIGTVIDIDDRREMEDALRDT 413
Cdd:COG5809 239 GEVDGIVIIFRDITERKKLEELLRKS 264
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
287-410 |
1.05e-23 |
|
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: 96.59 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 287 SEARFRNMADHAPTMMWVTDAEGRCTYLNRAWYDFTGQSEAEGEGFGWLEAVHPDDRGWS---------GEtfvsananH 357
Cdd:TIGR00229 1 SEERYRAIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVrerierrleGE--------P 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1905918357 358 EIFRVEYRLRRHDGEYRWAIDAASPRFgSQGDFLGYIGTVIDIDDRREMEDAL 410
Cdd:TIGR00229 73 EPVSEERRVRRKDGSEIWVEVSVSPIR-TNGGELGVVGIVRDITERKEAEEAL 124
|
|
| PRK13560 |
PRK13560 |
hypothetical protein; Provisional |
57-552 |
8.77e-19 |
|
hypothetical protein; Provisional
Pssm-ID: 106506 [Multi-domain] Cd Length: 807 Bit Score: 90.50 E-value: 8.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 57 FLYNDGYLPVFGTKHPDALGRPFREVWPEIWDDLKPLIDAALSGE------STWSENlplvveRNGYPEEAWFTFSYSPI 130
Cdd:PRK13560 227 FGCNDAACLACGFRREEIIGMSIHDFAPAQPADDYQEADAAKFDAdgsqiiEAEFQN------KDGRTRPVDVIFNHAEF 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 131 RDETGAIAGMFCAGAETTQTLLAERRLIDERERQKRMLQQMPgFAALLTGPEHRYEYV-NDAYRQISG------------ 197
Cdd:PRK13560 301 DDKENHCAGLVGAITDISGRRAAERELLEKEDMLRAIIEAAP-IAAIGLDADGNICFVnNNAAERMLGwsaaevmgkplp 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 198 ------DRNFMGQAFREVFPDIAGQGFYEI-FDRVYESGEPFarRTMSVSLDREDGDRS-IDLLVEPVRDNSGKVTGIFV 269
Cdd:PRK13560 380 gmdpelNEEFWCGDFQEWYPDGRPMAFDACpMAKTIKGGKIF--DGQEVLIEREDDGPAdCSAYAEPLHDADGNIIGAIA 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 270 GGFDITERVRAEGAVRESEArfrnMADHAPTMM--WVTDAEGRCTYLNRAWYDFTGQSEAEGEGFGWLEA-VHPDDRGW- 345
Cdd:PRK13560 458 LLVDITERKQVEEQLLLANL----IVENSPLVLfrWKAEEGWPVELVSKNITQFGYEPDEFISGKRMFAAiIHPADLEQv 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 346 SGETFVSANANHEIFRVEYRLRRHDGEYRWAIDAASPRFGSQGDFLGYIGTVIDIDDRREMEDALRDTSAHQILLINELN 425
Cdd:PRK13560 534 AAEVAEFAAQGVDRFEQEYRILGKGGAVCWIDDQSAAERDEEGQISHFEGIVIDISERKHAEEKIKAALTEKEVLLKEIH 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 426 HRVKNTLATVQS---IAMQTFRDRGGAGASPEQrelfESRLIALAIAHDVLTR-ENWESAQLRDVVlEAVAAHCGGD--- 498
Cdd:PRK13560 614 HRVKNNLQIISSlldLQAEKLHDEEAKCAFAES----QDRICAMALAHEKLYQsEDLADIDFLDYI-ESLTAHLKNSfai 688
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1905918357 499 ---VNPFTVEGPEARLTPKMALGWSMALHELCTNAVKYgalSVPDGTVA-IRWSVERE 552
Cdd:PRK13560 689 dfgRIDCKIDADDGCLDIDKAIPCGLIISELLSNALKH---AFPDGAAGnIKVEIREQ 743
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
283-460 |
1.01e-16 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 82.20 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 283 AVRESEARFRNMADHAPTMMWVTDAEGRCTYLNRAWYDFTGQSEAEGEGfGWLEAVHPDDRGWSGETFVSANANHEIFRV 362
Cdd:COG3852 1 ALRESEELLRAILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLG-RPLAELFPEDSPLRELLERALAEGQPVTER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 363 EYRLRRHDGEYRWAIDAASPRFGSQGDfLGYIGTVIDIDDRREMEDALRDTSAHQIL--LINELNHRVKNTLATVqSIAM 440
Cdd:COG3852 80 EVTLRRKDGEERPVDVSVSPLRDAEGE-GGVLLVLRDITERKRLERELRRAEKLAAVgeLAAGLAHEIRNPLTGI-RGAA 157
|
170 180
....*....|....*....|
gi 1905918357 441 QTFRDRggaGASPEQRELFE 460
Cdd:COG3852 158 QLLERE---LPDDELREYTQ 174
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
298-400 |
1.36e-15 |
|
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: 72.67 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 298 APTMMWVTDAEGRCTYLNRAWYDFTGQSEAEGEGFGWLEAVHPDDRGWSGETFVSANANHEIFRVEYRLRRHDGEYRWAI 377
Cdd:cd00130 1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVL 80
|
90 100
....*....|....*....|...
gi 1905918357 378 DAASPRFGSQGDFLGYIGTVIDI 400
Cdd:cd00130 81 VSLTPIRDEGGEVIGLLGVVRDI 103
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
274-423 |
6.67e-15 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 78.56 E-value: 6.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 274 ITERVRAEGA-VRESEARFRNMADHAPTMMWVTDAEGRCTYLNRAWYDFTGQSEAEGEGFGWLEAVHPDD---------R 343
Cdd:PRK09776 267 VMYAFRAERKhISESETRFRNAMEYSAIGMALVGTEGQWLQVNKALCQFLGYSQEELRGLTFQQLTWPEDlnkdlqqveK 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 344 GWSGETfvsananhEIFRVEYRLRRHDGEYRWAIDAASPRFGSQGDFLGYIGTVIDIDDRREMEDALRDTSaHQILLINE 423
Cdd:PRK09776 347 LLSGEI--------NSYSMEKRYYRRDGEVVWALLAVSLVRDTDGTPLYFIAQIEDINELKRTEQVNERLM-ERITLANE 417
|
|
| PAS_3 |
pfam08447 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
312-397 |
6.67e-14 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.
Pssm-ID: 430001 [Multi-domain] Cd Length: 89 Bit Score: 67.36 E-value: 6.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 312 TYLNRAWYDFTGQSEAE--GEGFGWLEAVHPDDRGWSGETFVSANANHEIFRVEYRLRRHDGEYRWAIDAASPRFGSQGD 389
Cdd:pfam08447 2 IYWSPRFEEILGYTPEEllGKGESWLDLVHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDENGK 81
|
....*...
gi 1905918357 390 FLGYIGTV 397
Cdd:pfam08447 82 PVRVIGVA 89
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
289-400 |
8.14e-14 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. 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: 67.83 E-value: 8.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 289 ARFRNMADHAPTMMWVTDAEGRCTYLNRAWYDFTGQSEAEGEGFGWLEAVHPDDRGWSGETFVSA-NANHEIFRVEYRLR 367
Cdd:pfam00989 1 EDLRAILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQAlLQGEESRGFEVSFR 80
|
90 100 110
....*....|....*....|....*....|...
gi 1905918357 368 RHDGEYRWAIDAASPRFGSQGDFLGYIGTVIDI 400
Cdd:pfam00989 81 VPDGRPRHVEVRASPVRDAGGEILGFLGVLRDI 113
|
|
| KinA |
COG5805 |
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ... |
162-435 |
1.16e-12 |
|
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: 70.53 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 162 ERQKRMLQQMPGfAALLTGPEHRYEYVNDAYRQISGdrNFMGQAFREVFPDIAGQGFYEIFDRVYESGEPFARRTMSVSL 241
Cdd:COG5805 34 EELETILENLPD-AIIAVNREGKVIYINPAMEKLLG--YTSEEIIGKTIFDFLEKEYHYRVKTRIERLQKGYDVVMIEQI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 242 DREDGdRSIDLLVE--PVRDNSGKVtgIFVGGFDITERVRAEGAVRESEARFRNMADHAPTMMWVTDAEGRCTYLNRAWY 319
Cdd:COG5805 111 YCKDG-ELIYVEVKlfPIYNQNGQA--AILALRDITKKKKIEEILQEQEERLQTLIENSPDLICVIDTDGRILFINESIE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 320 DFTGQSEAEGEGFGWLEAVHPDDRGWSGETFVSANANHEIFRVEYRLRRHDGEYRWaIDAA-SPRFGSQGDFLGYIGTVI 398
Cdd:COG5805 188 RLFGAPREELIGKNLLELLHPCDKEEFKERIESITEVWQEFIIEREIITKDGRIRY-FEAViVPLIDTDGSVKGILVILR 266
|
250 260 270
....*....|....*....|....*....|....*....
gi 1905918357 399 DIDDRREMEDALRDTSAHQIL--LINELNHRVKNTLATV 435
Cdd:COG5805 267 DITEKKEAEELMARSEKLSIAgqLAAGIAHEIRNPLTSI 305
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
156-289 |
1.41e-11 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 66.41 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 156 RLIDERERQKRMLQQMPgFAALLTGPEHRYEYVNDAYRQISG--DRNFMGQAFREVFPDiaGQGFYEIFDRVYESGEPFA 233
Cdd:COG3852 1 ALRESEELLRAILDSLP-DAVIVLDADGRITYVNPAAERLLGlsAEELLGRPLAELFPE--DSPLRELLERALAEGQPVT 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1905918357 234 RRtmSVSLDREDG-DRSIDLLVEPVRDNSGKvTGIFVGGFDITERVRAEGAVRESEA 289
Cdd:COG3852 78 ER--EVTLRRKDGeERPVDVSVSPLRDAEGE-GGVLLVLRDITERKRLERELRRAEK 131
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
279-422 |
1.74e-11 |
|
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: 66.92 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 279 RAEGAVRESEARFRNMADHAPTMMWVTDAEGRCTYLNRAWYDFTGQSEAEGEGFGWLEAVHPDDRGWSGEtFVSANANHE 358
Cdd:COG5809 5 KMELQLRKSEQRFRSLFENAPDAILILDLEGKILKVNPAAERIFGYTEDELLGTNILDFLHPDDEKELRE-ILKLLKEGE 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1905918357 359 IFR-VEYRLRRHDGEYRWAIDAASPRFGSQGDFLGYIGTVIDIDDRREMEDALRDTSAHQILLIN 422
Cdd:COG5809 84 SRDeLEFELRHKNGKRLEFSSKLSPIFDQNGDIEGMLAISRDITERKRMEEALRESEEKFRLIFN 148
|
|
| PAS_4 |
pfam08448 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
174-279 |
4.27e-10 |
|
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: 57.42 E-value: 4.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 174 FAALLTGPEHRYEYVNDAYRQISG--DRNFMGQAFREVFPDIAGQGFYEIFDRVYESGEPfarRTMSVSLDREDGDRSID 251
Cdd:pfam08448 6 DALAVLDPDGRVRYANAAAAELFGlpPEELLGKTLAELLPPEDAARLERALRRALEGEEP---IDFLEELLLNGEERHYE 82
|
90 100
....*....|....*....|....*...
gi 1905918357 252 LLVEPVRDNSGKVTGIFVGGFDITERVR 279
Cdd:pfam08448 83 LRLTPLRDPDGEVIGVLVISRDITERRR 110
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
289-343 |
6.99e-10 |
|
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: 55.48 E-value: 6.99e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1905918357 289 ARFRNMADHAPTMMWVTDAEGRCTYLNRAWYDFTGQSEAEGEGFGWLEAVHPDDR 343
Cdd:smart00091 1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDR 55
|
|
| PAC |
smart00086 |
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ... |
362-403 |
1.83e-08 |
|
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif occurs C-terminal to a subset of all known PAS motifs. It is proposed to contribute to the PAS domain fold.
Pssm-ID: 197509 Cd Length: 43 Bit Score: 50.64 E-value: 1.83e-08
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1905918357 362 VEYRLRRHDGEYRWAIDAASPRFGSQGDFLGYIGTVIDIDDR 403
Cdd:smart00086 2 VEYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITER 43
|
|
| NtrY |
COG5000 |
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
276-552 |
7.94e-08 |
|
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: 7.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 276 ERVRAEgaVRESEARFRNMADHAPTMMWVTDAEGRCTYLNRAWYDFTGQSEAEGEGFGWLEAVHPDDrgwSGETFVSANA 355
Cdd:COG5000 79 KEQREE--LEERRRYLETILENLPAGVIVLDADGRITLANPAAERLLGIPLEELIGKPLEELLPELD---LAELLREALE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 356 NHEIFRVEYRLrrhDGEYRWAIDAASprfgsqgdfLGYIGTVIDIDDRREMEDALRDTS--------AHQIllinelnhr 427
Cdd:COG5000 154 RGWQEEIELTR---DGRRTLLVRASP---------LRDDGYVIVFDDITELLRAERLAAwgelarriAHEI--------- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 428 vKNTLATVQSIAmQTFRDRGGAGASPEQRELFES------RLIALA-IAHDVLT-----RENWESAQLRDVVLEAVA--- 492
Cdd:COG5000 213 -KNPLTPIQLSA-ERLRRKLADKLEEDREDLERAldtiirQVDRLKrIVDEFLDfarlpEPQLEPVDLNELLREVLAlye 290
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1905918357 493 -AHCGGDVNpFTVEGPEARLtpkMALG----WSMALHELCTNAVKygALSvPDGTVAIRWSVERE 552
Cdd:COG5000 291 pALKEKDIR-LELDLDPDLP---EVLAdrdqLEQVLINLLKNAIE--AIE-EGGEIEVSTRREDG 348
|
|
| PAS_8 |
pfam13188 |
PAS domain; PAS domains are involved in many signalling proteins where they are used as a ... |
289-354 |
3.65e-07 |
|
PAS domain; PAS domains are involved in many signalling proteins where they are used as a signal sensor domain. PAS domains appear in archaea, bacteria and eukaryotes. Several PAS-domain proteins are known to detect their signal by way of an associated cofactor. Heme, flavin, and a 4-hydroxycinnamyl chromophore are used in different proteins. This domain recognizes oxygen and CO (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 463802 [Multi-domain] Cd Length: 65 Bit Score: 47.54 E-value: 3.65e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1905918357 289 ARFRNMADHAPTMMWVTDAEGRCTYLNRAWYDFTGQsEAEGEGFGWLEAVHPDDRGWSGETFVSAN 354
Cdd:pfam13188 1 ERLRALFESSPDGILVLDEGGRIIYVNPAALELLGY-ELLGELLGELLDLLDPLLEDALELLRELR 65
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
162-274 |
1.02e-06 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain 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: 47.80 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 162 ERQKRMLQQMPGFAALLTGpEHRYEYVNDAYRQISGDR--NFMGQAFREVFPDIAGQGFYEIFDRVYESGEPfaRRTMSV 239
Cdd:pfam00989 1 EDLRAILESLPDGIFVVDE-DGRILYVNAAAEELLGLSreEVIGKSLLDLIPEEDDAEVAELLRQALLQGEE--SRGFEV 77
|
90 100 110
....*....|....*....|....*....|....*.
gi 1905918357 240 SLDREDG-DRSIDLLVEPVRDNSGKVTGIFVGGFDI 274
Cdd:pfam00989 78 SFRVPDGrPRHVEVRASPVRDAGGEILGFLGVLRDI 113
|
|
| PAS_4 |
pfam08448 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
47-149 |
1.03e-06 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain is associated to signalling systems and works as a signal sensor domain. It recognizes differently substituted aromatic hydrocarbons, oxygen, different dodecanoic acids, autoinducers, 3,5-dimethyl-pyrazin-2-ol and N-alanyl-aminoacetone (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 312075 [Multi-domain] Cd Length: 110 Bit Score: 47.79 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 47 MFVAWGPELSFLY-NDGYLPVFGTKHPDALGRPFREVWPEI-WDDLKPLIDAALSGESTWSenlpLVVERNGYPEEAWFT 124
Cdd:pfam08448 7 ALAVLDPDGRVRYaNAAAAELFGLPPEELLGKTLAELLPPEdAARLERALRRALEGEEPID----FLEELLLNGEERHYE 82
|
90 100
....*....|....*....|....*
gi 1905918357 125 FSYSPIRDETGAIAGMFCAGAETTQ 149
Cdd:pfam08448 83 LRLTPLRDPDGEVIGVLVISRDITE 107
|
|
| HisKA_2 |
pfam07568 |
Histidine kinase; This is the dimerization and phosphoacceptor domain of a sub-family of ... |
423-494 |
2.62e-06 |
|
Histidine kinase; This is the dimerization and phosphoacceptor domain of a sub-family of histidine kinases. It shares sequence similarity with pfam00512 and pfam07536. It is usually found adjacent to a C-terminal ATPase domain (pfam02518). This domain is found in a wide range of Bacteria and also several Archaea.
Pssm-ID: 400108 [Multi-domain] Cd Length: 76 Bit Score: 45.59 E-value: 2.62e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1905918357 423 ELNHRVKNTLATVQSI-AMQTFRDRggagaSPEQRELF---ESRLIALAIAHDVLTR-ENWESAQLRDvVLEAVAAH 494
Cdd:pfam07568 1 EIHHRVKNNLQIISSLlRLQARRAK-----DEEVKEALresQNRIRSMALIHEELYKsEDLDRIDFSE-YLEKLTEN 71
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
182-276 |
1.43e-05 |
|
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: 43.99 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 182 EHRYEYVNDAYRQISG-DRN-FMGQAFREVFPDIAGQGFYEIFDRVYESGEPFarrtmSVSLDREDGDR-SIDLLVEPVR 258
Cdd:pfam13426 1 DGRIIYVNDAALRLLGyTREeLLGKSITDLFAEPEDSERLREALREGKAVREF-----EVVLYRKDGEPfPVLVSLAPIR 75
|
90
....*....|....*...
gi 1905918357 259 DNSGKVTGIFVGGFDITE 276
Cdd:pfam13426 76 DDGGELVGIIAILRDITE 93
|
|
| PAS_4 |
pfam08448 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
296-405 |
5.23e-05 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain 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: 42.79 E-value: 5.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 296 DHAPTMMWVTDAEGRCTYLNRAWYDFTGQSEAEGEGFGWLEAVHPDDRG---------WSGETFvsananheIFRVEYRL 366
Cdd:pfam08448 2 DSLPDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAELLPPEDAArleralrraLEGEEP--------IDFLEELL 73
|
90 100 110
....*....|....*....|....*....|....*....
gi 1905918357 367 rrHDGEYRWAIDAASPRFGSQGDFLGYIGTVIDIDDRRE 405
Cdd:pfam08448 74 --LNGEERHYELRLTPLRDPDGEVIGVLVISRDITERRR 110
|
|
| BaeS |
COG0642 |
Signal transduction histidine kinase [Signal transduction mechanisms]; |
313-613 |
9.53e-05 |
|
Signal transduction histidine kinase [Signal transduction mechanisms];
Pssm-ID: 440407 [Multi-domain] Cd Length: 328 Bit Score: 44.90 E-value: 9.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 313 YLNRAWYDFTGQSEAEGEGFGWLEAVHPDDRGWSGETFVSANANHEIFRVEYRLRRHDGEYRWAIDAASPRFGSQGDFLG 392
Cdd:COG0642 10 LLLLLLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLLLLLLLLLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 393 YIGTVIDIDDRREMEDALRDTSAhqilLINELNHRVKNTLATVQSIAmQTFRDRggagASPEQRELFES------RLiaL 466
Cdd:COG0642 90 LLLLLLLLALLLLLEEANEAKSR----FLANVSHELRTPLTAIRGYL-ELLLEE----LDEEQREYLETilrsadRL--L 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 467 AIAHDVLT---------RENWESAQLRDVVLEAVAA------------HCGGDVNPFTVEGPEARLtpkmalgwSMALHE 525
Cdd:COG0642 159 RLINDLLDlsrleagklELEPEPVDLAELLEEVVELfrplaeekgielELDLPDDLPTVRGDPDRL--------RQVLLN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 526 LCTNAVKYGAlsvPDGTVAIRWSVEREE------------KADQLNFIWE--ERGGPSVTEPSSkGFGsrL-IERQLARE 590
Cdd:COG0642 231 LLSNAIKYTP---EGGTVTVSVRREGDRvrisvedtgpgiPPEDLERIFEpfFRTDPSRRGGGT-GLG--LaIVKRIVEL 304
|
330 340
....*....|....*....|....
gi 1905918357 591 LGGHVELIYAP-KGVNCTIKAPLS 613
Cdd:COG0642 305 HGGTIEVESEPgKGTTFTVTLPLA 328
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
308-400 |
1.23e-04 |
|
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: 41.29 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 308 EGRCTYLNRAWYDFTGQSEAE--GEGFGWLEAvHPDDRGWSGETFvsaNANHEIFRVEYRLRRHDGEYRWAIDAASPRFG 385
Cdd:pfam13426 1 DGRIIYVNDAALRLLGYTREEllGKSITDLFA-EPEDSERLREAL---REGKAVREFEVVLYRKDGEPFPVLVSLAPIRD 76
|
90
....*....|....*
gi 1905918357 386 SQGDFLGYIGTVIDI 400
Cdd:pfam13426 77 DGGELVGIIAILRDI 91
|
|
| RsbW |
COG2172 |
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms]; |
521-553 |
6.92e-04 |
|
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
Pssm-ID: 441775 [Multi-domain] Cd Length: 127 Bit Score: 39.90 E-value: 6.92e-04
10 20 30
....*....|....*....|....*....|...
gi 1905918357 521 MALHELCTNAVKYGALSVPDGTVAIRWSVEREE 553
Cdd:COG2172 37 LAVSEAVTNAVRHAYGGDPDGPVEVELELDPDG 69
|
|
| KdpD |
COG2205 |
K+-sensing histidine kinase KdpD [Signal transduction mechanisms]; |
404-615 |
9.19e-04 |
|
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
Pssm-ID: 441807 [Multi-domain] Cd Length: 239 Bit Score: 41.43 E-value: 9.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 404 REMEDALRDTSAHQILLINELNHRVKNTLATVQSiAMQTFRDRGGAgASPEQRELFES------RLIALAiaHDVLT--- 474
Cdd:COG2205 3 EEALEELEELERLKSEFLANVSHELRTPLTSILG-AAELLLDEEDL-SPEERRELLEIiresaeRLLRLI--EDLLDlsr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 475 ------RENWESAQLRDVVLEAVA----AHCGGDVNpFTVEGPEARLTPKMALGW-SMALHELCTNAVKYGAlsvPDGTV 543
Cdd:COG2205 79 lesgklSLELEPVDLAELLEEAVEelrpLAEEKGIR-LELDLPPELPLVYADPELlEQVLANLLDNAIKYSP---PGGTI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 544 AIrwSVEREEK--------------ADQLNFIWE--ERGGPSVTEPSSkGFGsrL-IERQLARELGGHVELIYAP-KGVN 605
Cdd:COG2205 155 TI--SARREGDgvrisvsdngpgipEEELERIFErfYRGDNSRGEGGT-GLG--LaIVKRIVEAHGGTIWVESEPgGGTT 229
|
250
....*....|
gi 1905918357 606 CTIKAPLSAA 615
Cdd:COG2205 230 FTVTLPLAES 239
|
|
| PRK13560 |
PRK13560 |
hypothetical protein; Provisional |
152-411 |
1.46e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 106506 [Multi-domain] Cd Length: 807 Bit Score: 41.58 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 152 LAERRLIDERER-QKRMLQQMPGFA---ALLTGPEHRYEYVNDAYRQISGDRNFMGQAFREVFPD-IAGQGFYEIFDRVY 226
Cdd:PRK13560 57 IAEAEAQDCREQcERNLKANIPGGMflfALDGDGTFSFPSLLDANGELAAIAKHDLMADKGLLAMlIGGDDGDFFFANPF 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 227 ESGEPFARRTMSVSLDREDGD------RSIDLLVEPVRDNSGKvtgIFVGGF--DITERVRAEGAVRESEARFRNMADHA 298
Cdd:PRK13560 137 RSAETIAMALQSDDWQEEEGHfrcgdgRFIDCCLRFERHAHAD---DQVDGFaeDITERKRAEERIDEALHFLQQLLDNI 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 299 PTMMWVTDAEGRCTYLNRAWYDFTGQSEAEGEGfgwlEAVHPDDRGWSGETFVSANAnhEIFR------VEYRLRRHDGE 372
Cdd:PRK13560 214 ADPAFWKDEDAKVFGCNDAACLACGFRREEIIG----MSIHDFAPAQPADDYQEADA--AKFDadgsqiIEAEFQNKDGR 287
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1905918357 373 -YRWAIDAASPRF-GSQGDFLGYIGTVIDIDDRREMEDALR 411
Cdd:PRK13560 288 tRPVDVIFNHAEFdDKENHCAGLVGAITDISGRRAAERELL 328
|
|
| PRK11360 |
PRK11360 |
two-component system sensor histidine kinase AtoS; |
188-288 |
1.87e-03 |
|
two-component system sensor histidine kinase AtoS;
Pssm-ID: 236901 [Multi-domain] Cd Length: 607 Bit Score: 41.11 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 188 VNDAYRQISG--DRNFMGQAFREVFPdiAGQGFYEIFDRVYESGEpfarRTMSVSLDREDGDRSIDLLV--EPVRDNSGK 263
Cdd:PRK11360 287 MNPAAEVITGlqRHELVGKPYSELFP--PNTPFASPLLDTLEHGT----EHVDLEISFPGRDRTIELSVstSLLHNTHGE 360
|
90 100
....*....|....*....|....*
gi 1905918357 264 VTGIFVGGFDITERVRAEGAVRESE 288
Cdd:PRK11360 361 MIGALVIFSDLTERKRLQRRVARQE 385
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
67-177 |
1.91e-03 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 40.99 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 67 FGTKHPDALGRPFREVWPEIWDDLKPLIDAALSGESTWSENLPLVVeRNGypEEAWFTFSYSPIRDETGAIAgmfcagae 146
Cdd:COG3852 40 LGLSAEELLGRPLAELFPEDSPLRELLERALAEGQPVTEREVTLRR-KDG--EERPVDVSVSPLRDAEGEGG-------- 108
|
90 100 110
....*....|....*....|....*....|.
gi 1905918357 147 ttqtLLAERRLIDERERQKRMLQQMPGFAAL 177
Cdd:COG3852 109 ----VLLVLRDITERKRLERELRRAEKLAAV 135
|
|
| PRK13558 |
PRK13558 |
bacterio-opsin activator; Provisional |
179-312 |
2.00e-03 |
|
bacterio-opsin activator; Provisional
Pssm-ID: 237426 [Multi-domain] Cd Length: 665 Bit Score: 41.36 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 179 TGPEHRYEYVNDAYRQISG--DRNFMGQAFREVfpdiagQGFYEIFDRVYESGEPF-ARRTMSVSLD--REDGDRSIDLL 253
Cdd:PRK13558 167 TLPDEPLIYINDAFERITGysPDEVLGRNCRFL------QGEDTNEERVAELREAIdEERPTSVELRnyRKDGSTFWNQV 240
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1905918357 254 -VEPVRDNSGKVTGiFVGgF--DITERVRAEGAVRESEARFRNMADHAPTMMW-VTDAEGRCT 312
Cdd:PRK13558 241 dIAPIRDEDGTVTH-YVG-FqtDVTERKEAELALQRERRKLQRLLERVEGLVNdVTSALVRAT 301
|
|
| PAS_10 |
pfam13596 |
PAS domain; This is a sensor domain that recognizes O2, CO and NO (Matilla et. al., FEMS ... |
72-139 |
2.20e-03 |
|
PAS domain; This is a sensor domain that recognizes O2, CO and NO (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 404482 [Multi-domain] Cd Length: 106 Bit Score: 37.94 E-value: 2.20e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1905918357 72 PDALGRPFREVWP-EIWDDLKPLIDAALSGEStwsENLPLVVERNGYpeeaWFTFSYSPIRDETGAIAG 139
Cdd:pfam13596 36 PGDVGRPLADIHPpLIVPNVEEIIDALRTGET---DEVEVVVPKDGR----WYLVRYLPYRDEDGVIDG 97
|
|
| RocR |
COG3829 |
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ... |
154-290 |
2.50e-03 |
|
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: 40.52 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 154 ERRLIDERERQKRMLQQMPGfAALLTGPEHRYEYVNDAYRQISG--DRNFMGQAFREVFPDiagqgfyEIFDRVYESGEP 231
Cdd:COG3829 3 ELELKELEEELEAILDSLDD-GIIVVDADGRITYVNRAAERILGlpREEVIGKNVTELIPN-------SPLLEVLKTGKP 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1905918357 232 FARRTMSVsldredGDRSIDLLVE--PVRDNsGKVTGIFVGGFDITERVRAEGAVRESEAR 290
Cdd:COG3829 75 VTGVIQKT------GGKGKTVIVTaiPIFED-GEVIGAVETFRDITELKRLERKLREEELE 128
|
|
| PRK13558 |
PRK13558 |
bacterio-opsin activator; Provisional |
286-538 |
4.88e-03 |
|
bacterio-opsin activator; Provisional
Pssm-ID: 237426 [Multi-domain] Cd Length: 665 Bit Score: 39.82 E-value: 4.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 286 ESEARFRNMA-DHAPTMMWVTDA---EGRCTYLNRAWYDFTGQS--EAEGEGFGWLEAvhPDDRGWSGETFVSANANHEI 359
Cdd:PRK13558 144 ESDRRLKERAlDEAPVGITIADAtlpDEPLIYINDAFERITGYSpdEVLGRNCRFLQG--EDTNEERVAELREAIDEERP 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 360 FRVEYRLRRHDGEYRWAIDAASPRFGSQGDFLGYIGTVIDIDDRREMEDAL-RDTSAHQILL--INELNHRVknTLATVQ 436
Cdd:PRK13558 222 TSVELRNYRKDGSTFWNQVDIAPIRDEDGTVTHYVGFQTDVTERKEAELALqRERRKLQRLLerVEGLVNDV--TSALVR 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905918357 437 SIAMQTFR----DRGGAGASPE-----QRELFESRLIALAIAHDV---------LTRENWESAQLRDVVLEAVAahcggd 498
Cdd:PRK13558 300 ATDREEIEaavcDRVGAGGEYDgawigEYDPTSGTITVAEAAGGCdgadgdvldLAAAGPAAAALQSVVAETEA------ 373
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1905918357 499 vnpftVEGPEARLTPKMALGWSMALHELCTNAVKYGALSV 538
Cdd:PRK13558 374 -----VESTDVDGVSGTVDGSAVAAVPLVYRETTYGVLVV 408
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
334-410 |
6.72e-03 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 39.66 E-value: 6.72e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1905918357 334 WLEAVHPDDRGWSGETFVSANANHEIFRVEYRLRRHDGeYRWAIDAASPRFGSQGDFLGYIGTVIDIDDRREMEDAL 410
Cdd:PRK09776 456 WYACLHPEDRQRVEKEIRDALQGRSPFKLEFRIVVKDG-VRHIRALANRVLNKDGEVERLLGINMDMTEVRQLNEAL 531
|
|
| |
