|
Name |
Accession |
Description |
Interval |
E-value |
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
198-426 |
1.86e-46 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 167.89 E-value: 1.86e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 198 QRLARGEFiTGRFErVNRRGERVWLEASYNPILDNDGQVVKVVK---------------IAQDITRLMQQQQHE------ 256
Cdd:COG0840 218 ERIAEGDL-TVRID-VDSKDEIGQLADAFNRMIENLRELVGQVResaeqvasaseelaaSAEELAAGAEEQAASleetaa 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 257 --EEM----------VRNAHHLSLDTDRQAAQGAIIVQQAVKGMQQVEAAARETSDVVTELGKCSQQIGTIVEAIRKIAS 324
Cdd:COG0840 296 amEELsatvqevaenAQQAAELAEEASELAEEGGEVVEEAVEGIEEIRESVEETAETIEELGESSQEIGEIVDVIDDIAE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 325 QTNLLAINASIEAAHAGEHGRGFAVVANEVRTLAEQSRKAATEIERMTKSIQQGVAAAIAGMATCVEQAGGGVALTHDAG 404
Cdd:COG0840 376 QTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAEATKEIEELIEEIQSETEEAVEAMEEGSEEVEEGVELVEEAG 455
|
250 260
....*....|....*....|..
gi 1275746313 405 EVINQVNIGMHDVVKLMQAFTS 426
Cdd:COG0840 456 EALEEIVEAVEEVSDLIQEIAA 477
|
|
| MCP_signal |
cd11386 |
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ... |
269-426 |
6.79e-42 |
|
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis proteins (MCPs or chemotaxis receptors) are an integral part of the transmembrane protein complex that controls bacterial chemotaxis, together with the histidine kinase CheA, the receptor-coupling protein CheW, receptor-modification enzymes, and localized phosphatases. MCPs contain a four helix trans membrane region, an N-terminal periplasmic ligand binding domain, and a C-terminal HAMP domain followed by a cytoplasmic signaling domain. This C-terminal signaling domain dimerizes into a four-helix bundle and interacts with CheA through the adaptor protein CheW.
Pssm-ID: 206779 [Multi-domain] Cd Length: 200 Bit Score: 147.00 E-value: 6.79e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 269 DTDRQAAQGAIIVQQAVKGMQQVEAAARETSDVVTELGKCSQQIGTIVEAIRKIASQTNLLAINASIEAAHAGEHGRGFA 348
Cdd:cd11386 23 QAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQTNLLALNAAIEAARAGEAGRGFA 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1275746313 349 VVANEVRTLAEQSRKAATEIERMTKSIQQGVAAAIAGMATCVEQAGGGVALTHDAGEVINQVNIGMHDVVKLMQAFTS 426
Cdd:cd11386 103 VVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRAFEEIVASVEEVADGIQEISA 180
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
257-422 |
9.83e-41 |
|
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.
Pssm-ID: 214599 [Multi-domain] Cd Length: 262 Bit Score: 145.89 E-value: 9.83e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 257 EEMVRNAHhlslDTDRQAAQGAIIVQQAVKGMQQVEAAARETSDVVTELGKCSQQIGTIVEAIRKIASQTNLLAINASIE 336
Cdd:smart00283 42 DEIAATAQ----SAAEAAEEGREAVEDAITAMDQIREVVEEAVSAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 337 AAHAGEHGRGFAVVANEVRTLAEQSRKAATEIERMTKSIQQGVAAAIAGMATCVEQAGGGVALTHDAGEVINQVNIGMHD 416
Cdd:smart00283 118 AARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEETNEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEE 197
|
....*.
gi 1275746313 417 VVKLMQ 422
Cdd:smart00283 198 IADLVQ 203
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
16-254 |
1.39e-33 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 126.68 E-value: 1.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 16 LSAIEHA-VPMIVFSLDGTVLRANDLFLSTLGFQRDDVIGQHHRIFCDPNYvASPLYRKHWETLNKGQPITDTIKRIAKN 94
Cdd:COG2202 14 RALVESSpDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPED-DDEFLELLRAALAGGGVWRGELRNRRKD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 95 GEAVWLQGTYAPVLNNQGKVVEIVKIASEVTERVT-----QAQEHRSLLAALNRSMAMISFTPQGTIVSANDNMLALMGY 169
Cdd:COG2202 93 GSLFWVELSISPVRDEDGEITGFVGIARDITERKRaeealRESEERLRLLVENAPDGIFVLDLDGRILYVNPAAEELLGY 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 170 RLEEACGQSHAVLCPPEFAasDDYRRHWQRLARGEFITGRFE--RVNRRGERVWLEASYNPIlDNDGQVVKVVKIAQDIT 247
Cdd:COG2202 173 SPEELLGKSLLDLLHPEDR--ERLLELLRRLLEGGRESYELElrLKDGDGRWVWVEASAVPL-RDGGEVIGVLGIVRDIT 249
|
....*..
gi 1275746313 248 RLMQQQQ 254
Cdd:COG2202 250 ERKRAEE 256
|
|
| MCPsignal |
pfam00015 |
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ... |
265-422 |
3.43e-28 |
|
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to transduce the signal to CheA since it is highly conserved in very diverse MCPs.
Pssm-ID: 333767 [Multi-domain] Cd Length: 172 Bit Score: 109.44 E-value: 3.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 265 HLSLDTDRQAAQGAIIVQQAVKGMQQVEaaaretsdvvtelgKCSQQIGTIVEAIRKIASQTNLLAINASIEAAHAGEHG 344
Cdd:pfam00015 2 DLAQLASEEAQDGGKEVANVVGQMEQIA--------------QSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQG 67
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1275746313 345 RGFAVVANEVRTLAEQSRKAATEIERMTKSIQQGVAAAIAGMATCVEQAGGGVALTHDAGEVINQVNIGMHDVVKLMQ 422
Cdd:pfam00015 68 RGFAVVADEVRKLAERSAQAAKEIEALIIEIQKQTNDSTASIESTRQRVEVGSTIVESTGEALKEIVDAVAEIADIVQ 145
|
|
| PRK15041 |
PRK15041 |
methyl-accepting chemotaxis protein; |
235-410 |
1.37e-21 |
|
methyl-accepting chemotaxis protein;
Pssm-ID: 185001 [Multi-domain] Cd Length: 554 Bit Score: 97.33 E-value: 1.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 235 QVVKVVKIAQDITRLMQQQQHEEEMVRNAHHLSLDTDRQAAQGAIIVQQAVKGMQQVEAAaretsdvvtelgkcSQQIGT 314
Cdd:PRK15041 298 QAASLEETAASMEQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQTMRDISTS--------------SQKIAD 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 315 IVEAIRKIASQTNLLAINASIEAAHAGEHGRGFAVVANEVRTLAEQSRKAATEIERMtksIQQGVAAAIAGmATCVEQAG 394
Cdd:PRK15041 364 IISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSL---IEDSVGKVDVG-STLVESAG 439
|
170
....*....|....*.
gi 1275746313 395 ggvaltHDAGEVINQV 410
Cdd:PRK15041 440 ------ETMAEIVSAV 449
|
|
| PAS_4 |
pfam08448 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
141-249 |
3.88e-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 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: 68.21 E-value: 3.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 141 LNRSMAMI-SFTPQGTIVSANDNMLALMGYRLEEACGQSHAVLCPPEFAAsdDYRRHWQRLARGEFITGRFERVNRRGER 219
Cdd:pfam08448 1 LDSLPDALaVLDPDGRVRYANAAAAELFGLPPEELLGKTLAELLPPEDAA--RLERALRRALEGEEPIDFLEELLLNGEE 78
|
90 100 110
....*....|....*....|....*....|
gi 1275746313 220 VWLEASYNPILDNDGQVVKVVKIAQDITRL 249
Cdd:pfam08448 79 RHYELRLTPLRDPDGEVIGVLVISRDITER 108
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
146-255 |
1.30e-13 |
|
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: 67.32 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 146 AMISFTPQGTIVSANDNMLALMGYRLEEACGQSHAVLCPPEFAASDDyRRHWQRLARGEFITGRFERVNRR-GERVWLEA 224
Cdd:TIGR00229 15 AIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVR-ERIERRLEGEPEPVSEERRVRRKdGSEIWVEV 93
|
90 100 110
....*....|....*....|....*....|..
gi 1275746313 225 SYNPIlDNDGQVVKVVKIAQDIT-RLMQQQQH 255
Cdd:TIGR00229 94 SVSPI-RTNGGELGVVGIVRDITeRKEAEEAL 124
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
144-246 |
2.18e-13 |
|
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: 66.12 E-value: 2.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 144 SMAMISFTPQGTIVSANDNMLALMGYRLEEACGQSHAVLCPPEFAAsDDYRRHWQRLARGEFITGRFERVNRRGERVWLE 223
Cdd:cd00130 2 PDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDRE-ELRERLENLLSGGEPVTLEVRLRRKDGSVIWVL 80
|
90 100
....*....|....*....|...
gi 1275746313 224 ASYNPILDNDGQVVKVVKIAQDI 246
Cdd:cd00130 81 VSLTPIRDEGGEVIGLLGVVRDI 103
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
17-134 |
6.98e-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: 53.83 E-value: 6.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 17 SAIEHA-VPMIVFSLDGTVLRANDLFLSTLGFQRDDVIGQHHRIFCDPNYvASPLYRKHWETLNKGQPITDTIKRIA-KN 94
Cdd:TIGR00229 7 AIFESSpDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEED-REEVRERIERRLEGEPEPVSEERRVRrKD 85
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1275746313 95 GEAVWLQGTYAPVLNNQGKVVeIVKIASEVTERVTQAQEH 134
Cdd:TIGR00229 86 GSEIWVEVSVSPIRTNGGELG-VVGIVRDITERKEAEEAL 124
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
46-256 |
1.98e-08 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 56.70 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 46 GFQRDDVIGQHHRIFcdpnyVASPLYRKHWETLNK----GQPITDTIKRI----AKNGEAVWLQGTYAPVlNNQGKVVEI 117
Cdd:PRK11359 46 GYKREEVIGNNIDML-----IPRDLRPAHPEYIRHnregGKARVEGMSRElqleKKDGSKIWTRFALSKV-SAEGKVYYL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 118 VkIASEVTERVTQAQEHRSLLAALNRS-MAMISFTPQGTIVSANDNMLALMGYRLEEACGQS-HAVLCPPEFaaSDDYRR 195
Cdd:PRK11359 120 A-LVRDASVEMAQKEQTRQLIIAVDHLdRPVIVLDPERRIVQCNRAFTEMFGYCISEASGMQpDTLLNIPEF--PADNRI 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1275746313 196 HWQRLARGefiTGRFER----VNRRGERVWLEASYNPILDNDGQVVKVVKIAQDITRLMQQQQHE 256
Cdd:PRK11359 197 RLQQLLWK---TARDQDefllLTRTGEKIWIKASISPVYDVLAHLQNLVMTFSDITEERQIRQLE 258
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
132-203 |
2.61e-04 |
|
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: 38.92 E-value: 2.61e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1275746313 132 QEHRSLLAALNrsMAMISFTPQGTIVSANDNMLALMGYRLEEACGQShavlcPPEFAASDDYRRHWQRLARG 203
Cdd:smart00091 1 ERLRAILESLP--DGIFVLDLDGRILYANPAAEELLGYSPEELIGKS-----LLELIHPEDRERVQEALQRL 65
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
198-426 |
1.86e-46 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 167.89 E-value: 1.86e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 198 QRLARGEFiTGRFErVNRRGERVWLEASYNPILDNDGQVVKVVK---------------IAQDITRLMQQQQHE------ 256
Cdd:COG0840 218 ERIAEGDL-TVRID-VDSKDEIGQLADAFNRMIENLRELVGQVResaeqvasaseelaaSAEELAAGAEEQAASleetaa 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 257 --EEM----------VRNAHHLSLDTDRQAAQGAIIVQQAVKGMQQVEAAARETSDVVTELGKCSQQIGTIVEAIRKIAS 324
Cdd:COG0840 296 amEELsatvqevaenAQQAAELAEEASELAEEGGEVVEEAVEGIEEIRESVEETAETIEELGESSQEIGEIVDVIDDIAE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 325 QTNLLAINASIEAAHAGEHGRGFAVVANEVRTLAEQSRKAATEIERMTKSIQQGVAAAIAGMATCVEQAGGGVALTHDAG 404
Cdd:COG0840 376 QTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAEATKEIEELIEEIQSETEEAVEAMEEGSEEVEEGVELVEEAG 455
|
250 260
....*....|....*....|..
gi 1275746313 405 EVINQVNIGMHDVVKLMQAFTS 426
Cdd:COG0840 456 EALEEIVEAVEEVSDLIQEIAA 477
|
|
| MCP_signal |
cd11386 |
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ... |
269-426 |
6.79e-42 |
|
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis proteins (MCPs or chemotaxis receptors) are an integral part of the transmembrane protein complex that controls bacterial chemotaxis, together with the histidine kinase CheA, the receptor-coupling protein CheW, receptor-modification enzymes, and localized phosphatases. MCPs contain a four helix trans membrane region, an N-terminal periplasmic ligand binding domain, and a C-terminal HAMP domain followed by a cytoplasmic signaling domain. This C-terminal signaling domain dimerizes into a four-helix bundle and interacts with CheA through the adaptor protein CheW.
Pssm-ID: 206779 [Multi-domain] Cd Length: 200 Bit Score: 147.00 E-value: 6.79e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 269 DTDRQAAQGAIIVQQAVKGMQQVEAAARETSDVVTELGKCSQQIGTIVEAIRKIASQTNLLAINASIEAAHAGEHGRGFA 348
Cdd:cd11386 23 QAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQTNLLALNAAIEAARAGEAGRGFA 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1275746313 349 VVANEVRTLAEQSRKAATEIERMTKSIQQGVAAAIAGMATCVEQAGGGVALTHDAGEVINQVNIGMHDVVKLMQAFTS 426
Cdd:cd11386 103 VVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRAFEEIVASVEEVADGIQEISA 180
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
257-422 |
9.83e-41 |
|
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.
Pssm-ID: 214599 [Multi-domain] Cd Length: 262 Bit Score: 145.89 E-value: 9.83e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 257 EEMVRNAHhlslDTDRQAAQGAIIVQQAVKGMQQVEAAARETSDVVTELGKCSQQIGTIVEAIRKIASQTNLLAINASIE 336
Cdd:smart00283 42 DEIAATAQ----SAAEAAEEGREAVEDAITAMDQIREVVEEAVSAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 337 AAHAGEHGRGFAVVANEVRTLAEQSRKAATEIERMTKSIQQGVAAAIAGMATCVEQAGGGVALTHDAGEVINQVNIGMHD 416
Cdd:smart00283 118 AARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEETNEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEE 197
|
....*.
gi 1275746313 417 VVKLMQ 422
Cdd:smart00283 198 IADLVQ 203
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
16-254 |
1.39e-33 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 126.68 E-value: 1.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 16 LSAIEHA-VPMIVFSLDGTVLRANDLFLSTLGFQRDDVIGQHHRIFCDPNYvASPLYRKHWETLNKGQPITDTIKRIAKN 94
Cdd:COG2202 14 RALVESSpDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPED-DDEFLELLRAALAGGGVWRGELRNRRKD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 95 GEAVWLQGTYAPVLNNQGKVVEIVKIASEVTERVT-----QAQEHRSLLAALNRSMAMISFTPQGTIVSANDNMLALMGY 169
Cdd:COG2202 93 GSLFWVELSISPVRDEDGEITGFVGIARDITERKRaeealRESEERLRLLVENAPDGIFVLDLDGRILYVNPAAEELLGY 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 170 RLEEACGQSHAVLCPPEFAasDDYRRHWQRLARGEFITGRFE--RVNRRGERVWLEASYNPIlDNDGQVVKVVKIAQDIT 247
Cdd:COG2202 173 SPEELLGKSLLDLLHPEDR--ERLLELLRRLLEGGRESYELElrLKDGDGRWVWVEASAVPL-RDGGEVIGVLGIVRDIT 249
|
....*..
gi 1275746313 248 RLMQQQQ 254
Cdd:COG2202 250 ERKRAEE 256
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
19-268 |
2.61e-28 |
|
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: 116.61 E-value: 2.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 19 IEHA-VPMIVFSLDGTVLRANDLFLSTLGFQRDDVIGQHHRIFCDPNYVAsplYRKHWETLNKGQPITDT--IKRIAKNG 95
Cdd:COG5809 21 FENApDAILILDLEGKILKVNPAAERIFGYTEDELLGTNILDFLHPDDEK---ELREILKLLKEGESRDEleFELRHKNG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 96 EAVWLQGTYAPVLNNQGKVVEIVKIASEVTERV-------TQAQEHRSLLAALnrSMAMISFTPQGTIVSANDNMLALMG 168
Cdd:COG5809 98 KRLEFSSKLSPIFDQNGDIEGMLAISRDITERKrmeealrESEEKFRLIFNHS--PDGIIVTDLDGRIIYANPAACKLLG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 169 YRLEEACGQSHAVLCPPEFAASDDyRRHWQRLARGEFITGRFERVNRRGERVWLEASYNPILDNDGQVVKVVkIAQDITR 248
Cdd:COG5809 176 ISIEELIGKSILELIHSDDQENVA-AFISQLLKDGGIAQGEVRFWTKDGRWRLLEASGAPIKKNGEVDGIVI-IFRDITE 253
|
250 260
....*....|....*....|
gi 1275746313 249 LMQQqqheEEMVRNAHHLSL 268
Cdd:COG5809 254 RKKL----EELLRKSEKLSV 269
|
|
| MCPsignal |
pfam00015 |
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ... |
265-422 |
3.43e-28 |
|
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to transduce the signal to CheA since it is highly conserved in very diverse MCPs.
Pssm-ID: 333767 [Multi-domain] Cd Length: 172 Bit Score: 109.44 E-value: 3.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 265 HLSLDTDRQAAQGAIIVQQAVKGMQQVEaaaretsdvvtelgKCSQQIGTIVEAIRKIASQTNLLAINASIEAAHAGEHG 344
Cdd:pfam00015 2 DLAQLASEEAQDGGKEVANVVGQMEQIA--------------QSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQG 67
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1275746313 345 RGFAVVANEVRTLAEQSRKAATEIERMTKSIQQGVAAAIAGMATCVEQAGGGVALTHDAGEVINQVNIGMHDVVKLMQ 422
Cdd:pfam00015 68 RGFAVVADEVRKLAERSAQAAKEIEALIIEIQKQTNDSTASIESTRQRVEVGSTIVESTGEALKEIVDAVAEIADIVQ 145
|
|
| PRK15041 |
PRK15041 |
methyl-accepting chemotaxis protein; |
235-410 |
1.37e-21 |
|
methyl-accepting chemotaxis protein;
Pssm-ID: 185001 [Multi-domain] Cd Length: 554 Bit Score: 97.33 E-value: 1.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 235 QVVKVVKIAQDITRLMQQQQHEEEMVRNAHHLSLDTDRQAAQGAIIVQQAVKGMQQVEAAaretsdvvtelgkcSQQIGT 314
Cdd:PRK15041 298 QAASLEETAASMEQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQTMRDISTS--------------SQKIAD 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 315 IVEAIRKIASQTNLLAINASIEAAHAGEHGRGFAVVANEVRTLAEQSRKAATEIERMtksIQQGVAAAIAGmATCVEQAG 394
Cdd:PRK15041 364 IISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSL---IEDSVGKVDVG-STLVESAG 439
|
170
....*....|....*.
gi 1275746313 395 ggvaltHDAGEVINQV 410
Cdd:PRK15041 440 ------ETMAEIVSAV 449
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
126-273 |
5.56e-21 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 92.01 E-value: 5.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 126 ERVTQAQEHRSLLAALNRSMAMISFTPQGTIVSANDNMLALMGYRLEEACGQSHAVLCPPEFAAsDDYRRHWQRLARGEF 205
Cdd:COG2202 3 EEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDD-EFLELLRAALAGGGV 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1275746313 206 ITGRFERVNRRGERVWLEASYNPILDNDGQVVKVVKIAQDIT-------RLMQQQQHEEEMVRNAHHLSLDTDRQ 273
Cdd:COG2202 82 WRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITerkraeeALRESEERLRLLVENAPDGIFVLDLD 156
|
|
| PRK09793 |
PRK09793 |
methyl-accepting chemotaxis protein IV; |
269-391 |
2.27e-19 |
|
methyl-accepting chemotaxis protein IV;
Pssm-ID: 182079 [Multi-domain] Cd Length: 533 Bit Score: 90.52 E-value: 2.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 269 DTDRQAAQGAI-IVQQAVKGMQQVEAAARETSDVVTElgkcSQQIGTIVEAIRKIASQTNLLAINASIEAAHAGEHGRGF 347
Cdd:PRK09793 317 DNARQASELAKnAATTAQAGGVQVSTMTHTMQEIATS----SQKIGDIISVIDGIAFQTNILALNAAVEAARAGEQGRGF 392
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1275746313 348 AVVANEVRTLAEQSRKAATE----IERMTKSIQQGVAAAIAGMATCVE 391
Cdd:PRK09793 393 AVVAGEVRNLASRSAQAAKEikglIEESVNRVQQGSKLVNNAAATMTD 440
|
|
| PRK15048 |
PRK15048 |
methyl-accepting chemotaxis protein II; Provisional |
261-394 |
9.56e-19 |
|
methyl-accepting chemotaxis protein II; Provisional
Pssm-ID: 185008 [Multi-domain] Cd Length: 553 Bit Score: 88.52 E-value: 9.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 261 RNAHHLSLDTDRQAAQGAIIVQQAVKGMQqveaaaretsdvvtELGKCSQQIGTIVEAIRKIASQTNLLAINASIEAAHA 340
Cdd:PRK15048 322 RQASQLAQSASDTAQHGGKVVDGVVKTMH--------------EIADSSKKIADIISVIDGIAFQTNILALNAAVEAARA 387
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1275746313 341 GEHGRGFAVVANEVRTLAEQSRKAATEIERMtksIQQGVAAAIAGmATCVEQAG 394
Cdd:PRK15048 388 GEQGRGFAVVAGEVRNLASRSAQAAKEIKAL---IEDSVSRVDTG-SVLVESAG 437
|
|
| PAS_3 |
pfam08447 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
156-243 |
1.35e-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: 68.90 E-value: 1.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 156 IVSANDNMLALMGYRLEEACG--QSHAVLCPPefaasDD----YRRHWQRLARGEFITGRFERVNRRGERVWLEASYNPI 229
Cdd:pfam08447 1 IIYWSPRFEEILGYTPEELLGkgESWLDLVHP-----DDrervREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPI 75
|
90
....*....|....
gi 1275746313 230 LDNDGQVVKVVKIA 243
Cdd:pfam08447 76 RDENGKPVRVIGVA 89
|
|
| PAS_4 |
pfam08448 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
141-249 |
3.88e-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 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: 68.21 E-value: 3.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 141 LNRSMAMI-SFTPQGTIVSANDNMLALMGYRLEEACGQSHAVLCPPEFAAsdDYRRHWQRLARGEFITGRFERVNRRGER 219
Cdd:pfam08448 1 LDSLPDALaVLDPDGRVRYANAAAAELFGLPPEELLGKTLAELLPPEDAA--RLERALRRALEGEEPIDFLEELLLNGEE 78
|
90 100 110
....*....|....*....|....*....|
gi 1275746313 220 VWLEASYNPILDNDGQVVKVVKIAQDITRL 249
Cdd:pfam08448 79 RHYELRLTPLRDPDGEVIGVLVISRDITER 108
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
146-255 |
1.30e-13 |
|
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: 67.32 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 146 AMISFTPQGTIVSANDNMLALMGYRLEEACGQSHAVLCPPEFAASDDyRRHWQRLARGEFITGRFERVNRR-GERVWLEA 224
Cdd:TIGR00229 15 AIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVR-ERIERRLEGEPEPVSEERRVRRKdGSEIWVEV 93
|
90 100 110
....*....|....*....|....*....|..
gi 1275746313 225 SYNPIlDNDGQVVKVVKIAQDIT-RLMQQQQH 255
Cdd:TIGR00229 94 SVSPI-RTNGGELGVVGIVRDITeRKEAEEAL 124
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
144-246 |
2.18e-13 |
|
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: 66.12 E-value: 2.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 144 SMAMISFTPQGTIVSANDNMLALMGYRLEEACGQSHAVLCPPEFAAsDDYRRHWQRLARGEFITGRFERVNRRGERVWLE 223
Cdd:cd00130 2 PDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDRE-ELRERLENLLSGGEPVTLEVRLRRKDGSVIWVL 80
|
90 100
....*....|....*....|...
gi 1275746313 224 ASYNPILDNDGQVVKVVKIAQDI 246
Cdd:cd00130 81 VSLTPIRDEGGEVIGLLGVVRDI 103
|
|
| PAS_3 |
pfam08447 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
34-121 |
2.20e-12 |
|
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: 62.74 E-value: 2.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 34 VLRANDLFLSTLGFQRDDVIG--QHHRIFCDPNYVAsPLYRKHWETLNKGQPITDTIKRIAKNGEAVWLQGTYAPVLNNQ 111
Cdd:pfam08447 1 IIYWSPRFEEILGYTPEELLGkgESWLDLVHPDDRE-RVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDEN 79
|
90
....*....|
gi 1275746313 112 GKVVEIVKIA 121
Cdd:pfam08447 80 GKPVRVIGVA 89
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
31-126 |
1.31e-10 |
|
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: 57.86 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 31 DGTVLRANDLFLSTLGFQRDDVIGQHHRIFCDPNYVASPLyRKHWETLNKGQPITDTIKRiaKNGEAVWLQGTYAPVLNN 110
Cdd:pfam13426 1 DGRIIYVNDAALRLLGYTREELLGKSITDLFAEPEDSERL-REALREGKAVREFEVVLYR--KDGEPFPVLVSLAPIRDD 77
|
90
....*....|....*.
gi 1275746313 111 QGKVVEIVKIASEVTE 126
Cdd:pfam13426 78 GGELVGIIAILRDITE 93
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
22-124 |
7.40e-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. 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: 7.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 22 AVPMIVFSLDGTVLRANDLFLSTLGFQRDDVIGQHHRIFCDPNYVAsPLYRKHWETLNKGQPITDTIKRIAKNGEAVWLQ 101
Cdd:cd00130 2 PDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDRE-ELRERLENLLSGGEPVTLEVRLRRKDGSVIWVL 80
|
90 100
....*....|....*....|...
gi 1275746313 102 GTYAPVLNNQGKVVEIVKIASEV 124
Cdd:cd00130 81 VSLTPIRDEGGEVIGLLGVVRDI 103
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
153-247 |
1.03e-09 |
|
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: 55.16 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 153 QGTIVSANDNMLALMGYRLEEACGQSHAVLCPPEfAASDDYRRHWQRLarGEFITGRFERVNRRGERVWLEASYNPILDN 232
Cdd:pfam13426 1 DGRIIYVNDAALRLLGYTREELLGKSITDLFAEP-EDSERLREALREG--KAVREFEVVLYRKDGEPFPVLVSLAPIRDD 77
|
90
....*....|....*
gi 1275746313 233 DGQVVKVVKIAQDIT 247
Cdd:pfam13426 78 GGELVGIIAILRDIT 92
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
132-280 |
1.65e-09 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 59.09 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 132 QEHRSLLAALnrSMAMISFTPQGTIVSANDNMLALMGYRLEEACGQSHAVLCPPEfaaSDDYRRHWQRLARGEFITGR-F 210
Cdd:COG3852 7 ELLRAILDSL--PDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFPED---SPLRELLERALAEGQPVTEReV 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 211 ERVNRRGERVWLEASYNPILDNDGQvVKVVKIAQDITrlmQQQQHEEEMVRNahhlsldtDRQAAQGAII 280
Cdd:COG3852 82 TLRRKDGEERPVDVSVSPLRDAEGE-GGVLLVLRDIT---ERKRLERELRRA--------EKLAAVGELA 139
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
17-134 |
6.98e-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: 53.83 E-value: 6.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 17 SAIEHA-VPMIVFSLDGTVLRANDLFLSTLGFQRDDVIGQHHRIFCDPNYvASPLYRKHWETLNKGQPITDTIKRIA-KN 94
Cdd:TIGR00229 7 AIFESSpDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEED-REEVRERIERRLEGEPEPVSEERRVRrKD 85
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1275746313 95 GEAVWLQGTYAPVLNNQGKVVeIVKIASEVTERVTQAQEH 134
Cdd:TIGR00229 86 GSEIWVEVSVSPIRTNGGELG-VVGIVRDITERKEAEEAL 124
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
46-256 |
1.98e-08 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 56.70 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 46 GFQRDDVIGQHHRIFcdpnyVASPLYRKHWETLNK----GQPITDTIKRI----AKNGEAVWLQGTYAPVlNNQGKVVEI 117
Cdd:PRK11359 46 GYKREEVIGNNIDML-----IPRDLRPAHPEYIRHnregGKARVEGMSRElqleKKDGSKIWTRFALSKV-SAEGKVYYL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 118 VkIASEVTERVTQAQEHRSLLAALNRS-MAMISFTPQGTIVSANDNMLALMGYRLEEACGQS-HAVLCPPEFaaSDDYRR 195
Cdd:PRK11359 120 A-LVRDASVEMAQKEQTRQLIIAVDHLdRPVIVLDPERRIVQCNRAFTEMFGYCISEASGMQpDTLLNIPEF--PADNRI 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1275746313 196 HWQRLARGefiTGRFER----VNRRGERVWLEASYNPILDNDGQVVKVVKIAQDITRLMQQQQHE 256
Cdd:PRK11359 197 RLQQLLWK---TARDQDefllLTRTGEKIWIKASISPVYDVLAHLQNLVMTFSDITEERQIRQLE 258
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
17-146 |
6.95e-07 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 51.00 E-value: 6.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 17 SAIEHA-VPMIVFSLDGTVLRANDLFLSTLGFQRDDVIGQH-HRIFCDPnyvaSPLYRKHWETLNKGQPITDT-IKRIAK 93
Cdd:COG3852 11 AILDSLpDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPlAELFPED----SPLRELLERALAEGQPVTEReVTLRRK 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1275746313 94 NGEAVWLQGTYAPVLNNQGKvVEIVKIASEVTERV-TQAQEHRSLLAALNRSMA 146
Cdd:COG3852 87 DGEERPVDVSVSPLRDAEGE-GGVLLVLRDITERKrLERELRRAEKLAAVGELA 139
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
14-118 |
3.29e-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: 45.87 E-value: 3.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 14 AELSAIEHA--VPMIVFSLDGTVLRANDLFLSTLGFQRDDVIGQHHRIFCDPNYVASpLYRKHWETLNKGQPITD-TIKR 90
Cdd:pfam00989 1 EDLRAILESlpDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAE-VAELLRQALLQGEESRGfEVSF 79
|
90 100
....*....|....*....|....*...
gi 1275746313 91 IAKNGEAVWLQGTYAPVLNNQGKVVEIV 118
Cdd:pfam00989 80 RVPDGRPRHVEVRASPVRDAGGEILGFL 107
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
146-246 |
3.53e-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: 45.87 E-value: 3.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 146 AMISFTPQGTIVSANDNMLALMGYRLEEACGQSHAVLCPPEFAAsDDYRRHWQRL-ARGEFITGRFERVNRRGERVWLEA 224
Cdd:pfam00989 13 GIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDA-EVAELLRQALlQGEESRGFEVSFRVPDGRPRHVEV 91
|
90 100
....*....|....*....|..
gi 1275746313 225 SYNPILDNDGQVVKVVKIAQDI 246
Cdd:pfam00989 92 RASPVRDAGGEILGFLGVLRDI 113
|
|
| RocR |
COG3829 |
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ... |
14-167 |
4.08e-06 |
|
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: 49.00 E-value: 4.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 14 AELSAIEHAVPMIVFSLD--GTVLRANDLFLSTLGFQRDDVIGQH-HRIFcdPNYVasplyrkHWETLNKGQPITDTIKR 90
Cdd:COG3829 11 EELEAILDSLDDGIIVVDadGRITYVNRAAERILGLPREEVIGKNvTELI--PNSP-------LLEVLKTGKPVTGVIQK 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1275746313 91 IAKNGEAVWLQGTyaPVLNNqGKVVEIVKIASEVTERVTQAQEHRSLLAALNRSmAMISFtpqGTIVSANDNMLALM 167
Cdd:COG3829 82 TGGKGKTVIVTAI--PIFED-GEVIGAVETFRDITELKRLERKLREEELERGLS-AKYTF---DDIIGKSPAMKELL 151
|
|
| RocR |
COG3829 |
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ... |
132-270 |
4.16e-06 |
|
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: 48.61 E-value: 4.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 132 QEHRSLLAALNRS-MAMISFTPQGTIVSANDNMLALMGYRLEEACGQSHAVLCPPEfaasddyrRHWQRLARGEFITGRF 210
Cdd:COG3829 8 ELEEELEAILDSLdDGIIVVDADGRITYVNRAAERILGLPREEVIGKNVTELIPNS--------PLLEVLKTGKPVTGVI 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 211 ERVNRRGERVwlEASYNPILDnDGQVVKVVKIAQDITRLMQQQQHEEEMVRNAHHLSLDT 270
Cdd:COG3829 80 QKTGGKGKTV--IVTAIPIFE-DGEVIGAVETFRDITELKRLERKLREEELERGLSAKYT 136
|
|
| PAS_4 |
pfam08448 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
23-128 |
4.26e-06 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain is associated to signalling systems and works as a signal sensor domain. It recognizes differently substituted aromatic hydrocarbons, oxygen, different dodecanoic acids, autoinducers, 3,5-dimethyl-pyrazin-2-ol and N-alanyl-aminoacetone (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 312075 [Multi-domain] Cd Length: 110 Bit Score: 45.48 E-value: 4.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 23 VPMIVFSLDGTVLRANDLFLSTLGFQRDDVIGQHHRIFCDPNYVA--SPLYRKHWETlnkGQPITDTIKRIAkNGEAVWL 100
Cdd:pfam08448 6 DALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAELLPPEDAArlERALRRALEG---EEPIDFLEELLL-NGEERHY 81
|
90 100
....*....|....*....|....*...
gi 1275746313 101 QGTYAPVLNNQGKVVEIVKIASEVTERV 128
Cdd:pfam08448 82 ELRLTPLRDPDGEVIGVLVISRDITERR 109
|
|
| NtrY |
COG5000 |
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
119-296 |
6.75e-06 |
|
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: 48.03 E-value: 6.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 119 KIASEVTERVTQAQEHRSLLAAL--NRSMAMISFTPQGTIVSANDNMLALMGYRLEEACGQSHAVLCPPEFAAS---DDY 193
Cdd:COG5000 73 RMTDQLKEQREELEERRRYLETIleNLPAGVIVLDADGRITLANPAAERLLGIPLEELIGKPLEELLPELDLAEllrEAL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 194 RRHWQRLArgefitgrfeRVNRRGERVWLEASYNpiLDNDGQVVkvvkIAQDITRLMQQQQ------------HEeemVR 261
Cdd:COG5000 153 ERGWQEEI----------ELTRDGRRTLLVRASP--LRDDGYVI----VFDDITELLRAERlaawgelarriaHE---IK 213
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1275746313 262 N--------AHHLSLDTDRQAAQGAIIVQQAVKG-MQQVEAAAR 296
Cdd:COG5000 214 NpltpiqlsAERLRRKLADKLEEDREDLERALDTiIRQVDRLKR 257
|
|
| PRK13558 |
PRK13558 |
bacterio-opsin activator; Provisional |
38-133 |
5.80e-05 |
|
bacterio-opsin activator; Provisional
Pssm-ID: 237426 [Multi-domain] Cd Length: 665 Bit Score: 45.60 E-value: 5.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 38 NDLFLSTLGFQRDDVIGQHHRIFCDPNYVASPLyRKHWETLNKGQPITDTIKRIAKNGEAVWLQGTYAPVLNNQGKVVEI 117
Cdd:PRK13558 177 NDAFERITGYSPDEVLGRNCRFLQGEDTNEERV-AELREAIDEERPTSVELRNYRKDGSTFWNQVDIAPIRDEDGTVTHY 255
|
90
....*....|....*.
gi 1275746313 118 VKIASEVTERVTQAQE 133
Cdd:PRK13558 256 VGFQTDVTERKEAELA 271
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
132-203 |
2.61e-04 |
|
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: 38.92 E-value: 2.61e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1275746313 132 QEHRSLLAALNrsMAMISFTPQGTIVSANDNMLALMGYRLEEACGQShavlcPPEFAASDDYRRHWQRLARG 203
Cdd:smart00091 1 ERLRAILESLP--DGIFVLDLDGRILYANPAAEELLGYSPEELIGKS-----LLELIHPEDRERVQEALQRL 65
|
|
| PAC |
smart00086 |
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ... |
207-247 |
4.17e-04 |
|
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: 37.93 E-value: 4.17e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1275746313 207 TGRFERVNRRGERVWLEASYNPILDNDGQVVKVVKIAQDIT 247
Cdd:smart00086 1 TVEYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDIT 41
|
|
| PRK11360 |
PRK11360 |
two-component system sensor histidine kinase AtoS; |
146-277 |
8.91e-04 |
|
two-component system sensor histidine kinase AtoS;
Pssm-ID: 236901 [Multi-domain] Cd Length: 607 Bit Score: 41.49 E-value: 8.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 146 AMISFTPQGTIVSANDNMLALMGYRLEEACGQSHAVLCPPEFAASDDYRRHWQrlaRGEFITGRFERVNRRGERVWLEAS 225
Cdd:PRK11360 274 GVIAIDRQGKITTMNPAAEVITGLQRHELVGKPYSELFPPNTPFASPLLDTLE---HGTEHVDLEISFPGRDRTIELSVS 350
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1275746313 226 YNPILDNDGQVVKVVKIAQDITrlmQQQQHEEEMVRnahhlsldTDRQAAQG 277
Cdd:PRK11360 351 TSLLHNTHGEMIGALVIFSDLT---ERKRLQRRVAR--------QERLAALG 391
|
|
| PRK13559 |
PRK13559 |
hypothetical protein; Provisional |
31-223 |
1.26e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237427 [Multi-domain] Cd Length: 361 Bit Score: 40.96 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 31 DGTVLRANDLFLSTLGFQRDDVIGQHHRIF----CDPNYVAsplyrKHWETLNKGQPITDTIKRIAKNGEAVWLQGTYAP 106
Cdd:PRK13559 65 DLPIVLANQAFLDLTGYAAEEVVGRNCRFLqgaaTDPIAVA-----KIRAAIAAEREIVVELLNYRKDGEPFWNALHLGP 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 107 VLNNQGKVVEIVKIASEVTE----RVTQAQEHRSLLAALNRSMAMISFTpqGTIV--SANDNMLALMGYRLEE---ACGQ 177
Cdd:PRK13559 140 VYGEDGRLLYFFGSQWDVTDiravRALEAHERRLAREVDHRSKNVFAVV--DSIVrlTGRADDPSLYAAAIQErvqALAR 217
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1275746313 178 SHAVLCPpefaasddyRRHWQRLARGEFITGRFERVNRRGERVWLE 223
Cdd:PRK13559 218 AHETLLD---------ERGWETVEVEELIRAQVAPYAPRATRVAFE 254
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
18-197 |
1.32e-03 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 41.29 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 18 AIEHA-VPMIVFSLDGTVLRANDLFLSTLGFQRDDVIGQH-HRIFCDPNYVASPLYRKHwETLNKGQPITDTIKRIAKNG 95
Cdd:PRK11359 141 AVDHLdRPVIVLDPERRIVQCNRAFTEMFGYCISEASGMQpDTLLNIPEFPADNRIRLQ-QLLWKTARDQDEFLLLTRTG 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 96 EAVWLQGTYAPVLNNQGKVVEIVKIASEVTERVTQAQEHRSLLAALNRSMamiSFTPQGTIVSANdnmlalmgyrLEEAC 175
Cdd:PRK11359 220 EKIWIKASISPVYDVLAHLQNLVMTFSDITEERQIRQLEGNILAAMCSSP---PFHEMGEIICRN----------IESVL 286
|
170 180
....*....|....*....|..
gi 1275746313 176 GQSHAVLCppefAASDDYRRHW 197
Cdd:PRK11359 287 NESHVSLF----ALRNGMPIHW 304
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
17-56 |
5.19e-03 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.
Pssm-ID: 214512 Cd Length: 67 Bit Score: 35.45 E-value: 5.19e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1275746313 17 SAIEHA-VPMIVFSLDGTVLRANDLFLSTLGFQRDDVIGQH 56
Cdd:smart00091 5 AILESLpDGIFVLDLDGRILYANPAAEELLGYSPEELIGKS 45
|
|
| PLN02900 |
PLN02900 |
alanyl-tRNA synthetase |
265-397 |
5.93e-03 |
|
alanyl-tRNA synthetase
Pssm-ID: 215487 [Multi-domain] Cd Length: 936 Bit Score: 39.23 E-value: 5.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275746313 265 HLSlDTdRQAAQGAIIVQQAV-KGMQQVEAAARE--------TSDVVTELGKCSQQIGTIVEaiRKIASQTNLLAiNASI 335
Cdd:PLN02900 706 HVS-NT-AEAEAFKLLSEEGIaKGIRRITAVTGGaaveainaADSLERELDSALKVEGSDLE--KKVASLKSRVD-AAVI 780
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1275746313 336 EAAHAGEhgrgfavVANEVRTLAEQSRKAATEI--ERMTKSIQQGVAAA----IAGMATCVEQAGGGV 397
Cdd:PLN02900 781 PAAKKEE-------IRARVSALQKELRAAQKEAaaLRAKLAVAKATELAskalSAGKSVLVARLDVGV 841
|
|
| |
