|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13559 |
PRK13559 |
hypothetical protein; Provisional |
23-369 |
3.41e-70 |
|
hypothetical protein; Provisional
Pssm-ID: 237427 [Multi-domain] Cd Length: 361 Bit Score: 223.93 E-value: 3.41e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493748890 23 ASEDPFAAAFKATRMPMLITDPRQPDNPIIFCNKAFCTLTGYEVGELIGRNCRLLQGPQTDPDAVTKLRDAVASQKDIAV 102
Cdd:PRK13559 40 ASGRLFEQAMEQTRMAMCITDPHQPDLPIVLANQAFLDLTGYAAEEVVGRNCRFLQGAATDPIAVAKIRAAIAAEREIVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493748890 103 DILNYRKDGSKFWNALFVSPVRDVSGAVIYFFASQLDFTNIKSKEAELARARHIAEeevalrtadltealraktalvhEV 182
Cdd:PRK13559 120 ELLNYRKDGEPFWNALHLGPVYGEDGRLLYFFGSQWDVTDIRAVRALEAHERRLAR----------------------EV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493748890 183 DHRVKNNLLTIASIVKLQARMTDNEVVERTLMsvlNRVEALSTVQRKLLNDEDVGHFDVADFANTLMLDKIGALKRTdis 262
Cdd:PRK13559 178 DHRSKNVFAVVDSIVRLTGRADDPSLYAAAIQ---ERVQALARAHETLLDERGWETVEVEELIRAQVAPYAPRATRV--- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493748890 263 lTTDLHEVVVPATKASPLALIINELIGDAIGRG-LKEGGGELHLEVK--RLNGHFLIRVVDTVVPVEVDSEQAAFSKKML 339
Cdd:PRK13559 252 -AFEGPGIRLGAASVQPLGLVLHELAVNAIKHGaLSADQGRISISWKpsPEGAGFRIDWQEQGGPTPPKLAKRGFGTVII 330
|
330 340 350
....*....|....*....|....*....|.
gi 493748890 340 EAS-LKQLRATIVRTVDGRRTDVRVTLSVKD 369
Cdd:PRK13559 331 GAMvESQLNGQLEKTWSDDGLLARIEIPSRQ 361
|
|
| COG3920 |
COG3920 |
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ... |
117-368 |
1.36e-32 |
|
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction mechanisms];
Pssm-ID: 443125 [Multi-domain] Cd Length: 495 Bit Score: 127.33 E-value: 1.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493748890 117 ALFVSPVRDVSGAVIYFFASQLDFTNIKSKEAELARARHIAEEEVALRTADLTEALRAKTALVHEVDHRVKNNLLTIASI 196
Cdd:COG3920 237 VLEELERRRRARGLGRLLLLLLLLLLLLRALLLLAAGIRLVITERKRAEEELEASLEEKELLLRELHHRVKNNLQVVSSL 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493748890 197 VKLQARMTDNEVVERTLMSVLNRVEALSTVQRKLLNDEDVGHFDVADFANTLMLDKIGALKRTDISLTTDLHEVVVPATK 276
Cdd:COG3920 317 LRLQARRADDPEAREALEESQNRIQALALVHELLYQSEDWEGVDLRDYLRELLEPLRDSYGGRGIRIELDGPDVELPADA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493748890 277 ASPLALIINELIGDAIGRGLKEG-GGELHLEVKRLNGHFLIR---VVDTVVPVEVDSEQAAFSKKMLEASLKQLRATIVR 352
Cdd:COG3920 397 AVPLGLILNELVTNALKHAFLSGeGGRIRVSWRREDGRLRLTvsdNGVGLPEDVDPPARKGLGLRLIRALVRQLGGTLEL 476
|
250
....*....|....*.
gi 493748890 353 TvdgRRTDVRVTLSVK 368
Cdd:COG3920 477 D---RPEGTRVRITFP 489
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
48-139 |
8.47e-18 |
|
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: 77.50 E-value: 8.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493748890 48 DNPIIFCNKAFCTLTGYEVGELIGRNCRLLQGpqtDPDAVTKLRDAVASQKD-IAVDILNYRKDGSKFWNALFVSPVRDV 126
Cdd:pfam13426 1 DGRIIYVNDAALRLLGYTREELLGKSITDLFA---EPEDSERLREALREGKAvREFEVVLYRKDGEPFPVLVSLAPIRDD 77
|
90
....*....|...
gi 493748890 127 SGAVIYFFASQLD 139
Cdd:pfam13426 78 GGELVGIIAILRD 90
|
|
| nifL_nitrog |
TIGR02938 |
nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation ... |
51-162 |
9.53e-13 |
|
nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation positive regulator protein NifA, and is therefore a negative regulator. It binds NifA. NifA and NifL are encoded by adjacent genes. [Central intermediary metabolism, Nitrogen fixation, Regulatory functions, Protein interactions]
Pssm-ID: 131984 [Multi-domain] Cd Length: 494 Bit Score: 69.16 E-value: 9.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493748890 51 IIFCNKAFCTLTGYEVGELIGRNCRLLQGPQTDPDAVTKLRDAVASQKDIAVDILNYRKDGSKFWNALFVSPVRDVSGAV 130
Cdd:TIGR02938 26 ILYANDAFTRITGYTKEEIIGKNESVLSNHTTPPEVYQALWGSLAEQKPWAGKLLNRRKDGELYLAELTVAPVLNEAGET 105
|
90 100 110
....*....|....*....|....*....|..
gi 493748890 131 IYFFASQLDFTNIKSKEAELARARHIAEEEVA 162
Cdd:TIGR02938 106 THFLGMHRDITELHRLEQVVANQKLLIESVVD 137
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
35-139 |
5.52e-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: 53.02 E-value: 5.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493748890 35 TRMPMLITDPrqpDNPIIFCNKAFCTLTGYEVGELIGRNCRLLQGPQTDPDAVTKLRDAVASQKDIAVDILNYRKDGSKF 114
Cdd:cd00130 1 LPDGVIVLDL---DGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVI 77
|
90 100
....*....|....*....|....*
gi 493748890 115 WNALFVSPVRDVSGAVIYFFASQLD 139
Cdd:cd00130 78 WVLVSLTPIRDEGGEVIGLLGVVRD 102
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
28-73 |
2.66e-05 |
|
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: 41.62 E-value: 2.66e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 493748890 28 FAAAFKATRMPMLITDPrqpDNPIIFCNKAFCTLTGYEVGELIGRN 73
Cdd:smart00091 3 LRAILESLPDGIFVLDL---DGRILYANPAAEELLGYSPEELIGKS 45
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13559 |
PRK13559 |
hypothetical protein; Provisional |
23-369 |
3.41e-70 |
|
hypothetical protein; Provisional
Pssm-ID: 237427 [Multi-domain] Cd Length: 361 Bit Score: 223.93 E-value: 3.41e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493748890 23 ASEDPFAAAFKATRMPMLITDPRQPDNPIIFCNKAFCTLTGYEVGELIGRNCRLLQGPQTDPDAVTKLRDAVASQKDIAV 102
Cdd:PRK13559 40 ASGRLFEQAMEQTRMAMCITDPHQPDLPIVLANQAFLDLTGYAAEEVVGRNCRFLQGAATDPIAVAKIRAAIAAEREIVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493748890 103 DILNYRKDGSKFWNALFVSPVRDVSGAVIYFFASQLDFTNIKSKEAELARARHIAEeevalrtadltealraktalvhEV 182
Cdd:PRK13559 120 ELLNYRKDGEPFWNALHLGPVYGEDGRLLYFFGSQWDVTDIRAVRALEAHERRLAR----------------------EV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493748890 183 DHRVKNNLLTIASIVKLQARMTDNEVVERTLMsvlNRVEALSTVQRKLLNDEDVGHFDVADFANTLMLDKIGALKRTdis 262
Cdd:PRK13559 178 DHRSKNVFAVVDSIVRLTGRADDPSLYAAAIQ---ERVQALARAHETLLDERGWETVEVEELIRAQVAPYAPRATRV--- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493748890 263 lTTDLHEVVVPATKASPLALIINELIGDAIGRG-LKEGGGELHLEVK--RLNGHFLIRVVDTVVPVEVDSEQAAFSKKML 339
Cdd:PRK13559 252 -AFEGPGIRLGAASVQPLGLVLHELAVNAIKHGaLSADQGRISISWKpsPEGAGFRIDWQEQGGPTPPKLAKRGFGTVII 330
|
330 340 350
....*....|....*....|....*....|.
gi 493748890 340 EAS-LKQLRATIVRTVDGRRTDVRVTLSVKD 369
Cdd:PRK13559 331 GAMvESQLNGQLEKTWSDDGLLARIEIPSRQ 361
|
|
| PRK13557 |
PRK13557 |
histidine kinase; Provisional |
21-231 |
3.62e-65 |
|
histidine kinase; Provisional
Pssm-ID: 237425 [Multi-domain] Cd Length: 540 Bit Score: 215.69 E-value: 3.62e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493748890 21 AHASEDPFAAAFKATRMPMLITDPRQPDNPIIFCNKAFCTLTGYEVGELIGRNCRLLQGPQTDPDAVTKLRDAVASQKDI 100
Cdd:PRK13557 25 SDHRSDIFFAAVETTRMPMIVTDPNQPDNPIVFANRAFLEMTGYAAEEIIGNNCRFLQGPETDRATVAEVRDAIAERREI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493748890 101 AVDILNYRKDGSKFWNALFVSPVRDVSGAVIYFFASQLDFTNikskeaelaraRHIAEEevALRTADLTEALRAKT-ALV 179
Cdd:PRK13557 105 ATEILNYRKDGSSFWNALFVSPVYNDAGDLVYFFGSQLDVSR-----------RRDAED--ALRQAQKMEALGQLTgGIA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 493748890 180 HEVdhrvkNNLLTIAS------IVKLQARMTDNEVVERTLMSVLNRVEALSTVQRKLL 231
Cdd:PRK13557 172 HDF-----NNLLQVMSgyldviQAALSHPDADRGRMARSVENIRAAAERAATLTQQLL 224
|
|
| PRK13558 |
PRK13558 |
bacterio-opsin activator; Provisional |
41-186 |
9.93e-34 |
|
bacterio-opsin activator; Provisional
Pssm-ID: 237426 [Multi-domain] Cd Length: 665 Bit Score: 131.88 E-value: 9.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493748890 41 ITDPRQPDNPIIFCNKAFCTLTGYEVGELIGRNCRLLQGPQTDPDAVTKLRDAVASQKDIAVDILNYRKDGSKFWNALFV 120
Cdd:PRK13558 163 IADATLPDEPLIYINDAFERITGYSPDEVLGRNCRFLQGEDTNEERVAELREAIDEERPTSVELRNYRKDGSTFWNQVDI 242
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493748890 121 SPVRDVSGAVIYFFASQLDFTNIKSKEAELARARHIAE---EEVALRTADLTEAL-RAKTAlvHEVDHRV 186
Cdd:PRK13558 243 APIRDEDGTVTHYVGFQTDVTERKEAELALQRERRKLQrllERVEGLVNDVTSALvRATDR--EEIEAAV 310
|
|
| COG3920 |
COG3920 |
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ... |
117-368 |
1.36e-32 |
|
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction mechanisms];
Pssm-ID: 443125 [Multi-domain] Cd Length: 495 Bit Score: 127.33 E-value: 1.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493748890 117 ALFVSPVRDVSGAVIYFFASQLDFTNIKSKEAELARARHIAEEEVALRTADLTEALRAKTALVHEVDHRVKNNLLTIASI 196
Cdd:COG3920 237 VLEELERRRRARGLGRLLLLLLLLLLLLRALLLLAAGIRLVITERKRAEEELEASLEEKELLLRELHHRVKNNLQVVSSL 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493748890 197 VKLQARMTDNEVVERTLMSVLNRVEALSTVQRKLLNDEDVGHFDVADFANTLMLDKIGALKRTDISLTTDLHEVVVPATK 276
Cdd:COG3920 317 LRLQARRADDPEAREALEESQNRIQALALVHELLYQSEDWEGVDLRDYLRELLEPLRDSYGGRGIRIELDGPDVELPADA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493748890 277 ASPLALIINELIGDAIGRGLKEG-GGELHLEVKRLNGHFLIR---VVDTVVPVEVDSEQAAFSKKMLEASLKQLRATIVR 352
Cdd:COG3920 397 AVPLGLILNELVTNALKHAFLSGeGGRIRVSWRREDGRLRLTvsdNGVGLPEDVDPPARKGLGLRLIRALVRQLGGTLEL 476
|
250
....*....|....*.
gi 493748890 353 TvdgRRTDVRVTLSVK 368
Cdd:COG3920 477 D---RPEGTRVRITFP 489
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
21-158 |
2.20e-22 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 95.09 E-value: 2.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493748890 21 AHASEDPFAAAFKATRMPMLITDPrqpDNPIIFCNKAFCTLTGYEVGELIGRNCRLLQGPQTDPDAVTKLRDAVASQKDI 100
Cdd:COG2202 6 LEESERRLRALVESSPDAIIITDL---DGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVW 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493748890 101 AVDILNYRKDGSKFWNALFVSPVRDVSGAVIYFFASQLDFTNIKSKEAEL----ARARHIAE 158
Cdd:COG2202 83 RGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALreseERLRLLVE 144
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
48-139 |
8.47e-18 |
|
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: 77.50 E-value: 8.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493748890 48 DNPIIFCNKAFCTLTGYEVGELIGRNCRLLQGpqtDPDAVTKLRDAVASQKD-IAVDILNYRKDGSKFWNALFVSPVRDV 126
Cdd:pfam13426 1 DGRIIYVNDAALRLLGYTREELLGKSITDLFA---EPEDSERLREALREGKAvREFEVVLYRKDGEPFPVLVSLAPIRDD 77
|
90
....*....|...
gi 493748890 127 SGAVIYFFASQLD 139
Cdd:pfam13426 78 GGELVGIIAILRD 90
|
|
| HisKA_2 |
pfam07568 |
Histidine kinase; This is the dimerization and phosphoacceptor domain of a sub-family of ... |
181-251 |
1.48e-14 |
|
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: 67.93 E-value: 1.48e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493748890 181 EVDHRVKNNLLTIASIVKLQARMTDNEVVERTLMSVLNRVEALSTVQRKLLNDEDVGHFDVADFANTLMLD 251
Cdd:pfam07568 1 EIHHRVKNNLQIISSLLRLQARRAKDEEVKEALRESQNRIRSMALIHEELYKSEDLDRIDFSEYLEKLTEN 71
|
|
| PRK13560 |
PRK13560 |
hypothetical protein; Provisional |
124-309 |
5.79e-13 |
|
hypothetical protein; Provisional
Pssm-ID: 106506 [Multi-domain] Cd Length: 807 Bit Score: 70.09 E-value: 5.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493748890 124 RDVSGAVIYFFASQLDFTNikskeaelaraRHIAEEEValrTADLTEalraKTALVHEVDHRVKNNLLTIASIVKLQARM 203
Cdd:PRK13560 572 RDEEGQISHFEGIVIDISE-----------RKHAEEKI---KAALTE----KEVLLKEIHHRVKNNLQIISSLLDLQAEK 633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493748890 204 TDNEVVERTLMSVLNRVEALSTVQRKLLNDEDVGHFDVADFANTLM--LDKIGALKRTDISLTTDLHEVVVPATKASPLA 281
Cdd:PRK13560 634 LHDEEAKCAFAESQDRICAMALAHEKLYQSEDLADIDFLDYIESLTahLKNSFAIDFGRIDCKIDADDGCLDIDKAIPCG 713
|
170 180
....*....|....*....|....*....
gi 493748890 282 LIINELIGDAIGRGLKEGG-GELHLEVKR 309
Cdd:PRK13560 714 LIISELLSNALKHAFPDGAaGNIKVEIRE 742
|
|
| nifL_nitrog |
TIGR02938 |
nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation ... |
51-162 |
9.53e-13 |
|
nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation positive regulator protein NifA, and is therefore a negative regulator. It binds NifA. NifA and NifL are encoded by adjacent genes. [Central intermediary metabolism, Nitrogen fixation, Regulatory functions, Protein interactions]
Pssm-ID: 131984 [Multi-domain] Cd Length: 494 Bit Score: 69.16 E-value: 9.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493748890 51 IIFCNKAFCTLTGYEVGELIGRNCRLLQGPQTDPDAVTKLRDAVASQKDIAVDILNYRKDGSKFWNALFVSPVRDVSGAV 130
Cdd:TIGR02938 26 ILYANDAFTRITGYTKEEIIGKNESVLSNHTTPPEVYQALWGSLAEQKPWAGKLLNRRKDGELYLAELTVAPVLNEAGET 105
|
90 100 110
....*....|....*....|....*....|..
gi 493748890 131 IYFFASQLDFTNIKSKEAELARARHIAEEEVA 162
Cdd:TIGR02938 106 THFLGMHRDITELHRLEQVVANQKLLIESVVD 137
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
23-227 |
1.68e-09 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 58.70 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493748890 23 ASEDPFAAAFKATRMPMLITDPrqpDNPIIFCNKAFCTLTGYEVGELIGRNCRLLQGPqtDPDAVTKLRDAVASQKDIAV 102
Cdd:COG3852 4 ESEELLRAILDSLPDAVIVLDA---DGRITYVNPAAERLLGLSAEELLGRPLAELFPE--DSPLRELLERALAEGQPVTE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493748890 103 -DILNYRKDGSKFWNALFVSPVRDVSGAVIYFFASQlDFTNIKSKEAELAR----------ARHIAEE------------ 159
Cdd:COG3852 79 rEVTLRRKDGEERPVDVSVSPLRDAEGEGGVLLVLR-DITERKRLERELRRaeklaavgelAAGLAHEirnpltgirgaa 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493748890 160 EVALRTADlTEALRAKTALV-HEVDhRVKN---NLLTIASIVKLQARMTD-NEVVERTLMSVlnRVEALSTVQ 227
Cdd:COG3852 158 QLLERELP-DDELREYTQLIiEEAD-RLNNlvdRLLSFSRPRPPEREPVNlHEVLERVLELL--RAEAPKNIR 226
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
35-139 |
5.52e-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: 53.02 E-value: 5.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493748890 35 TRMPMLITDPrqpDNPIIFCNKAFCTLTGYEVGELIGRNCRLLQGPQTDPDAVTKLRDAVASQKDIAVDILNYRKDGSKF 114
Cdd:cd00130 1 LPDGVIVLDL---DGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVI 77
|
90 100
....*....|....*....|....*
gi 493748890 115 WNALFVSPVRDVSGAVIYFFASQLD 139
Cdd:cd00130 78 WVLVSLTPIRDEGGEVIGLLGVVRD 102
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
24-150 |
9.75e-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: 53.06 E-value: 9.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493748890 24 SEDPFAAAFKATRMPMLITDPrqpDNPIIFCNKAFCTLTGYEVGELIGRNCR-LLQGPQTDPDAVTKLRDAVASQKDIAV 102
Cdd:TIGR00229 1 SEERYRAIFESSPDAIIVIDL---EGNILYVNPAFEEIFGYSAEELIGRNVLeLIPEEDREEVRERIERRLEGEPEPVSE 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 493748890 103 DILNYRKDGSKFWNALFVSPVRDvSGAVIYFFASQLDFTNIKSKEAEL 150
Cdd:TIGR00229 78 ERRVRRKDGSEIWVEVSVSPIRT-NGGELGVVGIVRDITERKEAEEAL 124
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
24-150 |
9.06e-08 |
|
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: 53.83 E-value: 9.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493748890 24 SEDPFAAAFKATRMPMLITDPRQPdnpIIFCNKAFCTLTGYEVGELIGRNCRLLQGPqtDPDAVTKLRDAVASQKDIAVD 103
Cdd:COG5809 13 SEQRFRSLFENAPDAILILDLEGK---ILKVNPAAERIFGYTEDELLGTNILDFLHP--DDEKELREILKLLKEGESRDE 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 493748890 104 ILNYR--KDGSKFWNALFVSPVRDVSGAVIYFFASQLDFTNIKSKEAEL 150
Cdd:COG5809 88 LEFELrhKNGKRLEFSSKLSPIFDQNGDIEGMLAISRDITERKRMEEAL 136
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
23-150 |
4.97e-07 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 50.41 E-value: 4.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493748890 23 ASEDPFAAAFKATRMPMLITDPrqpDNPIIFCNKAFCTLTGYEVGELIGRNCRLLQGPQTDPDAVTKLRDAVASQKDIaV 102
Cdd:COG2202 134 ESEERLRLLVENAPDGIFVLDL---DGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEGGRES-Y 209
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 493748890 103 DILNYRKDGSKFWNALFVSPVRD-VSGAVIYFFASQLDFTNIKSKEAEL 150
Cdd:COG2202 210 ELELRLKDGDGRWVWVEASAVPLrDGGEVIGVLGIVRDITERKRAEEAL 258
|
|
| PAS_3 |
pfam08447 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
51-133 |
5.26e-07 |
|
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: 46.95 E-value: 5.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493748890 51 IIFCNKAFCTLTGYEVGELIGRNCRLLQG--PQTDPDAVTKLRDAVASQKDIAVDILNYRKDGSKFWNALFVSPVRDVSG 128
Cdd:pfam08447 1 IIYWSPRFEEILGYTPEELLGKGESWLDLvhPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDENG 80
|
....*
gi 493748890 129 AVIYF 133
Cdd:pfam08447 81 KPVRV 85
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
38-139 |
7.00e-07 |
|
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: 47.41 E-value: 7.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493748890 38 PMLITDPrqpDNPIIFCNKAFCTLTGYEVGELIGRNC-RLLQGPQTDPDAVTKLRDAVASQKDIAVDILNYRKDGSKFWN 116
Cdd:pfam00989 13 GIFVVDE---DGRILYVNAAAEELLGLSREEVIGKSLlDLIPEEDDAEVAELLRQALLQGEESRGFEVSFRVPDGRPRHV 89
|
90 100
....*....|....*....|...
gi 493748890 117 ALFVSPVRDVSGAVIYFFASQLD 139
Cdd:pfam00989 90 EVRASPVRDAGGEILGFLGVLRD 112
|
|
| KinA |
COG5805 |
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ... |
51-271 |
1.46e-05 |
|
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: 46.65 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493748890 51 IIFCNKAFCTLTGYEVGELIGRNCRLLQGPQTDPDAVTKLRDAVASQKDIAVDILNYRKDGSKFWNALFVSPVRDVSGAV 130
Cdd:COG5805 179 ILFINESIERLFGAPREELIGKNLLELLHPCDKEEFKERIESITEVWQEFIIEREIITKDGRIRYFEAVIVPLIDTDGSV 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493748890 131 IYFFASQLDFTNIKSKEAELARarhiaeeevalrtadlTEALRAKTALVHEVDHRVKNNLLTIASIVKL-QARMTDNEVV 209
Cdd:COG5805 259 KGILVILRDITEKKEAEELMAR----------------SEKLSIAGQLAAGIAHEIRNPLTSIKGFLQLlQPGIEDKEEY 322
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493748890 210 ERTLMSVLNRVEALSTvqrkllndedvghfdvaDFantLMLDKIGALKRTDISLTTDLHEVV 271
Cdd:COG5805 323 FDIMLSELDRIESIIS-----------------EF---LALAKPQAVNKEKENINELIQDVV 364
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
28-73 |
2.66e-05 |
|
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: 41.62 E-value: 2.66e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 493748890 28 FAAAFKATRMPMLITDPrqpDNPIIFCNKAFCTLTGYEVGELIGRN 73
Cdd:smart00091 3 LRAILESLPDGIFVLDL---DGRILYANPAAEELLGYSPEELIGKS 45
|
|
| PAC |
smart00086 |
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ... |
102-139 |
4.08e-05 |
|
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif occurs C-terminal to a subset of all known PAS motifs. It is proposed to contribute to the PAS domain fold.
Pssm-ID: 197509 Cd Length: 43 Bit Score: 40.24 E-value: 4.08e-05
10 20 30
....*....|....*....|....*....|....*...
gi 493748890 102 VDILNYRKDGSKFWNALFVSPVRDVSGAVIYFFASQLD 139
Cdd:smart00086 2 VEYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRD 39
|
|
| RocR |
COG3829 |
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ... |
22-168 |
1.18e-04 |
|
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis domains [Transcription, Signal transduction mechanisms];
Pssm-ID: 443041 [Multi-domain] Cd Length: 448 Bit Score: 43.99 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493748890 22 HASEDPFAAAFKATRMPMLITDPrqpDNPIIFCNKAFCTLTGYEVGELIGRNCRLLQGPqtdpdavTKLRDAVASQKDIA 101
Cdd:COG3829 7 KELEEELEAILDSLDDGIIVVDA---DGRITYVNRAAERILGLPREEVIGKNVTELIPN-------SPLLEVLKTGKPVT 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493748890 102 VDILNYRKDGSKFWNAlfVSPVRDvSGAVIYFFASQLDFTNIKSKEAELARARHIAEEEVALRTADL 168
Cdd:COG3829 77 GVIQKTGGKGKTVIVT--AIPIFE-DGEVIGAVETFRDITELKRLERKLREEELERGLSAKYTFDDI 140
|
|
| PAS_8 |
pfam13188 |
PAS domain; PAS domains are involved in many signalling proteins where they are used as a ... |
28-89 |
5.20e-04 |
|
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: 37.91 E-value: 5.20e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493748890 28 FAAAFKATRMPMLITDPrqpDNPIIFCNKAFCTLTGYEV-GELIGRNCRLLQGPQTDPDAVTK 89
Cdd:pfam13188 3 LRALFESSPDGILVLDE---GGRIIYVNPAALELLGYELlGELLGELLDLLDPLLEDALELLR 62
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
55-152 |
6.27e-04 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 41.97 E-value: 6.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493748890 55 NKAFCTLTGYEVGELigrncRLLQGPQ-TDPDAVTKLRDAVasQKDIAVDILNY-------RKDGSKFWNALFVSPVRDV 126
Cdd:PRK09776 309 NKALCQFLGYSQEEL-----RGLTFQQlTWPEDLNKDLQQV--EKLLSGEINSYsmekryyRRDGEVVWALLAVSLVRDT 381
|
90 100
....*....|....*....|....*.
gi 493748890 127 SGAVIYFFASQLDFTNIKSKEAELAR 152
Cdd:PRK09776 382 DGTPLYFIAQIEDINELKRTEQVNER 407
|
|
| PAS_4 |
pfam08448 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
51-142 |
6.81e-04 |
|
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: 38.93 E-value: 6.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493748890 51 IIFCNKAFCTLTGYEVGELIGRNCR-LLqgPQTDPDAVTKLRDAVASQKDIAVDILNYRKDGSKFWNALFVSPVRDVSGA 129
Cdd:pfam08448 17 VRYANAAAAELFGLPPEELLGKTLAeLL--PPEDAARLERALRRALEGEEPIDFLEELLLNGEERHYELRLTPLRDPDGE 94
|
90
....*....|...
gi 493748890 130 VIYFFASQLDFTN 142
Cdd:pfam08448 95 VIGVLVISRDITE 107
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
10-132 |
2.02e-03 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 40.14 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493748890 10 DAKDAGERLVSAhASEDPFAAAfkatrmpMLITDprqpDNPIIFCNKAFCTLTGYEVGELIGRNCRLLQGPQ---TDPDA 86
Cdd:PRK11359 5 DADNAADGIFFP-ALEQNMMGA-------VLINE----NDEVLFFNPAAEKLWGYKREEVIGNNIDMLIPRDlrpAHPEY 72
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 493748890 87 VTKLRD-AVASQKDIAVDILNYRKDGSKFWNALFVSPVrDVSGAVIY 132
Cdd:PRK11359 73 IRHNREgGKARVEGMSRELQLEKKDGSKIWTRFALSKV-SAEGKVYY 118
|
|
| HWE_HK |
smart00911 |
HWE histidine kinase; The HWE domain is found in a subset of two-component system kinases, ... |
181-237 |
3.31e-03 |
|
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: 36.02 E-value: 3.31e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 493748890 181 EVDHRVKNNLLTIASIVKLQARMTDN--EVVERtlmsVLNRVEALSTVQRKLLNDEDVG 237
Cdd:smart00911 1 ELNHRVKNLLAVVQAIARQTLRSASSleDFAEA----FEGRLQALARAHDLLSRSDWSG 55
|
|
| |
