|
Name |
Accession |
Description |
Interval |
E-value |
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
297-544 |
2.54e-83 |
|
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: 261.84 E-value: 2.54e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 297 AVAENAQAITSGSNEIRMSADDLAKRTEQQAASVEETAAALEQITTTVKDSSQRAEEAGRLVARTKDHANHSGAVVREAI 376
Cdd:smart00283 1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 377 GAMDQIDASSKAISNIIGVIDEIAFQTNLLALNAGVEAARAGEAGKGFAVVAQEVRELAQRSATAAKEIKTLIT------ 450
Cdd:smart00283 81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKeiqeet 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 451 --------ASGSYVSNGVTLVTKAGAALQEIASHVENINGDITAIVEASREQSTALSEINRAINSVDQGTQQNAAMVEEQ 522
Cdd:smart00283 161 neavaameESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240
|
250 260
....*....|....*....|..
gi 2017767191 523 TAASHELAKEAAALFELLDQFR 544
Cdd:smart00283 241 SAAAEELSGLAEELDELVERFK 262
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
247-544 |
1.40e-82 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 268.81 E-value: 1.40e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 247 VENVEQLALGLTRFADGDLSQQINQPFIPSLERLRTDFNSASNKLKLAMAAVAENAQAITSGSNEIRMSADDLAKRTEQQ 326
Cdd:COG0840 207 TRPLRELLEVLERIAEGDLTVRIDVDSKDEIGQLADAFNRMIENLRELVGQVRESAEQVASASEELAASAEELAAGAEEQ 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 327 AASVEETAAALEQITTTVKDSSQRAEEAGRLVARTKDHANHSGAVVREAI--------------GAMDQIDASSKAISNI 392
Cdd:COG0840 287 AASLEETAAAMEELSATVQEVAENAQQAAELAEEASELAEEGGEVVEEAVegieeiresveetaETIEELGESSQEIGEI 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 393 IGVIDEIAFQTNLLALNAGVEAARAGEAGKGFAVVAQEVRELAQRSATAAKEIKTLITAS--------------GSYVSN 458
Cdd:COG0840 367 VDVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAEATKEIEELIEEIqseteeaveameegSEEVEE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 459 GVTLVTKAGAALQEIASHVENINGDITAIVEASREQSTALSEINRAINSVDQGTQQNAAMVEEQTAASHELAKEAAALFE 538
Cdd:COG0840 447 GVELVEEAGEALEEIVEAVEEVSDLIQEIAAASEEQSAGTEEVNQAIEQIAAAAQENAASVEEVAAAAEELAELAEELQE 526
|
....*.
gi 2017767191 539 LLDQFR 544
Cdd:COG0840 527 LVSRFK 532
|
|
| PRK15041 |
PRK15041 |
methyl-accepting chemotaxis protein; |
261-576 |
1.05e-70 |
|
methyl-accepting chemotaxis protein;
Pssm-ID: 185001 [Multi-domain] Cd Length: 554 Bit Score: 237.93 E-value: 1.05e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 261 ADGDLSQQINQPFIPSLERLRTDFNSASNKLKLAMAAVAENAQAITSGSNEIRMSADDLAKRTEQQAASVEETAAALEQI 340
Cdd:PRK15041 233 AGGDLVKPIEVDGSNEMGQLAESLRHMQGELMRTVGDVRNGANAIYSGASEIATGNNDLSSRTEQQAASLEETAASMEQL 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 341 TTTVKDSSQRAEEAGRLVARTKDHANHSGAVVREAIGAMDQIDASSKAISNIIGVIDEIAFQTNLLALNAGVEAARAGEA 420
Cdd:PRK15041 313 TATVKQNAENARQASHLALSASETAQRGGKVVDNVVQTMRDISTSSQKIADIISVIDGIAFQTNILALNAAVEAARAGEQ 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 421 GKGFAVVAQEVRELAQRSATAAKEIKTLITASGSYVSNGVTLVTKAGAALQEIASHVENINGDITAIVEASREQSTALSE 500
Cdd:PRK15041 393 GRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLVESAGETMAEIVSAVTRVTDIMGEIASASDEQSRGIDQ 472
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2017767191 501 INRAINSVDQGTQQNAAMVEEQTAASHELAKEAAALFELLDQFRF-GEGNRSQTTKPLDSKRPSAFKPKPSVPTHSQ 576
Cdd:PRK15041 473 VGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAVFRIqQQQQQQRETSAVVKTVTPATPRKMAVADSGE 549
|
|
| MCP_signal |
cd11386 |
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ... |
324-521 |
3.91e-62 |
|
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: 204.01 E-value: 3.91e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 324 EQQAASVEETAAALEQITTTVKDSSQRAEEAGRLVARTKDHANHSGAVVREAIGAMDQIDASSKAISNIIGVIDEIAFQT 403
Cdd:cd11386 1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 404 NLLALNAGVEAARAGEAGKGFAVVAQEVRELAQRSATAAKEIKTLITASGSYVSNGVTLVTKAGAALQEIASHVENINGD 483
Cdd:cd11386 81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 2017767191 484 ITAIVEASREQSTALSEINRAINSVDQGTQQNAAMVEE 521
Cdd:cd11386 161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEE 198
|
|
| MCPsignal |
pfam00015 |
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ... |
365-512 |
1.29e-45 |
|
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: 159.14 E-value: 1.29e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 365 ANHSGAVVREAIGAMDQIDASSKAISNIIGVIDEIAFQTNLLALNAGVEAARAGEAGKGFAVVAQEVRELAQRSATAAKE 444
Cdd:pfam00015 11 AQDGGKEVANVVGQMEQIAQSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLAERSAQAAKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 445 IKTLITA--------------SGSYVSNGVTLVTKAGAALQEIASHVENINGDITAIVEASREQSTALSEINRAINSVDQ 510
Cdd:pfam00015 91 IEALIIEiqkqtndstasiesTRQRVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDEQSAGIDQVNQAVARMDQ 170
|
..
gi 2017767191 511 GT 512
Cdd:pfam00015 171 VT 172
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
21-253 |
1.91e-30 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 120.13 E-value: 1.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 21 AIIEFDTQGNILRANKNFCDLMGYSENEIIGKHHRIFVEKDYAgSSDYTAFWKKLQGGTFECSEFKRIAKNGDDIWIRGN 100
Cdd:COG2202 23 AIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDD-DEFLELLRAALAGGGVWRGELRNRRKDGSLFWVELS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 101 YNPVKSASGKVLKIIKFANDITQTKM--DGL-DSSAKLTAV--SRAQATIEFTPDGKILAANENFLKALGYTLNEIVGQH 175
Cdd:COG2202 102 ISPVRDEDGEITGFVGIARDITERKRaeEALrESEERLRLLveNAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKS 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 176 HRMFVEPAEAnsQRYLEFWTRLRMGEYVA--DEFLRIGKGGRHVHIQASYNPVFDpSGKIIKVVKFATDVTGRVENVEQL 253
Cdd:COG2202 182 LLDLLHPEDR--ERLLELLRRLLEGGRESyeLELRLKDGDGRWVWVEASAVPLRD-GGEVIGVLGIVRDITERKRAEEAL 258
|
|
| PAS_4 |
pfam08448 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
142-248 |
4.30e-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: 68.59 E-value: 4.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 142 QATIEFTPDGKILAANENFLKALGYTLNEIVGQHHR-MFVEPAeanSQRYLEFWTRLRMGEYVADEFLRIGKGGRHVHIQ 220
Cdd:pfam08448 6 DALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAeLLPPED---AARLERALRRALEGEEPIDFLEELLLNGEERHYE 82
|
90 100
....*....|....*....|....*...
gi 2017767191 221 ASYNPVFDPSGKIIKVVKFATDVTGRVE 248
Cdd:pfam08448 83 LRLTPLRDPDGEVIGVLVISRDITERRR 110
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
18-121 |
1.99e-12 |
|
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: 63.81 E-value: 1.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 18 LSFAIIEFDTQGNILRANKNFCDLMGYSENEIIGKHHRIFVEKDYAGSSdYTAFWKKLQGGTFECSEFKRIAKNGDDIWI 97
Cdd:cd00130 1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREEL-RERLENLLSGGEPVTLEVRLRRKDGSVIWV 79
|
90 100
....*....|....*....|....
gi 2017767191 98 RGNYNPVKSASGKVLKIIKFANDI 121
Cdd:cd00130 80 LVSLTPIRDEGGEVIGLLGVVRDI 103
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
21-126 |
2.26e-12 |
|
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: 64.23 E-value: 2.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 21 AIIEFDTQGNILRANKNFCDLMGYSENEIIGKHHRIFVEKDYAGSSDyTAFWKKLQGGTFECSEFKRIA-KNGDDIWIRG 99
Cdd:TIGR00229 15 AIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVR-ERIERRLEGEPEPVSEERRVRrKDGSEIWVEV 93
|
90 100
....*....|....*....|....*..
gi 2017767191 100 NYNPVkSASGKVLKIIKFANDITQTKM 126
Cdd:TIGR00229 94 SVSPI-RTNGGELGVVGIVRDITERKE 119
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
1-244 |
1.26e-08 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 57.86 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 1 MISMFASNSNQILSALDLSF-AIIEFDTQGNILRANKNFCDLMGYSENEIIGKHHRIFVEKDYAGS-SDYTAfwKKLQGG 78
Cdd:PRK11359 3 LTDADNAADGIFFPALEQNMmGAVLINENDEVLFFNPAAEKLWGYKREEVIGNNIDMLIPRDLRPAhPEYIR--HNREGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 79 TFE----CSEFKRIAKNGDDIWIRGNYNPVkSASGKVLKIIkFANDIT-------QTKMdgldssaKLTAVSRA-QATIE 146
Cdd:PRK11359 81 KARvegmSRELQLEKKDGSKIWTRFALSKV-SAEGKVYYLA-LVRDASvemaqkeQTRQ-------LIIAVDHLdRPVIV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 147 FTPDGKILAANENFLKALGYTLNEIVGQHHRMFVEPAEANSQRYLEFWTRLRMGEYVADEFLRIGKGGRHVHIQASYNPV 226
Cdd:PRK11359 152 LDPERRIVQCNRAFTEMFGYCISEASGMQPDTLLNIPEFPADNRIRLQQLLWKTARDQDEFLLLTRTGEKIWIKASISPV 231
|
250
....*....|....*...
gi 2017767191 227 FDPSGKIIKVVKFATDVT 244
Cdd:PRK11359 232 YDVLAHLQNLVMTFSDIT 249
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
10-53 |
3.05e-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: 42.00 E-value: 3.05e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2017767191 10 NQILSALDlsFAIIEFDTQGNILRANKNFCDLMGYSENEIIGKH 53
Cdd:smart00091 4 RAILESLP--DGIFVLDLDGRILYANPAAEELLGYSPEELIGKS 45
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
297-544 |
2.54e-83 |
|
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: 261.84 E-value: 2.54e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 297 AVAENAQAITSGSNEIRMSADDLAKRTEQQAASVEETAAALEQITTTVKDSSQRAEEAGRLVARTKDHANHSGAVVREAI 376
Cdd:smart00283 1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 377 GAMDQIDASSKAISNIIGVIDEIAFQTNLLALNAGVEAARAGEAGKGFAVVAQEVRELAQRSATAAKEIKTLIT------ 450
Cdd:smart00283 81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKeiqeet 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 451 --------ASGSYVSNGVTLVTKAGAALQEIASHVENINGDITAIVEASREQSTALSEINRAINSVDQGTQQNAAMVEEQ 522
Cdd:smart00283 161 neavaameESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240
|
250 260
....*....|....*....|..
gi 2017767191 523 TAASHELAKEAAALFELLDQFR 544
Cdd:smart00283 241 SAAAEELSGLAEELDELVERFK 262
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
247-544 |
1.40e-82 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 268.81 E-value: 1.40e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 247 VENVEQLALGLTRFADGDLSQQINQPFIPSLERLRTDFNSASNKLKLAMAAVAENAQAITSGSNEIRMSADDLAKRTEQQ 326
Cdd:COG0840 207 TRPLRELLEVLERIAEGDLTVRIDVDSKDEIGQLADAFNRMIENLRELVGQVRESAEQVASASEELAASAEELAAGAEEQ 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 327 AASVEETAAALEQITTTVKDSSQRAEEAGRLVARTKDHANHSGAVVREAI--------------GAMDQIDASSKAISNI 392
Cdd:COG0840 287 AASLEETAAAMEELSATVQEVAENAQQAAELAEEASELAEEGGEVVEEAVegieeiresveetaETIEELGESSQEIGEI 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 393 IGVIDEIAFQTNLLALNAGVEAARAGEAGKGFAVVAQEVRELAQRSATAAKEIKTLITAS--------------GSYVSN 458
Cdd:COG0840 367 VDVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAEATKEIEELIEEIqseteeaveameegSEEVEE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 459 GVTLVTKAGAALQEIASHVENINGDITAIVEASREQSTALSEINRAINSVDQGTQQNAAMVEEQTAASHELAKEAAALFE 538
Cdd:COG0840 447 GVELVEEAGEALEEIVEAVEEVSDLIQEIAAASEEQSAGTEEVNQAIEQIAAAAQENAASVEEVAAAAEELAELAEELQE 526
|
....*.
gi 2017767191 539 LLDQFR 544
Cdd:COG0840 527 LVSRFK 532
|
|
| PRK15041 |
PRK15041 |
methyl-accepting chemotaxis protein; |
261-576 |
1.05e-70 |
|
methyl-accepting chemotaxis protein;
Pssm-ID: 185001 [Multi-domain] Cd Length: 554 Bit Score: 237.93 E-value: 1.05e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 261 ADGDLSQQINQPFIPSLERLRTDFNSASNKLKLAMAAVAENAQAITSGSNEIRMSADDLAKRTEQQAASVEETAAALEQI 340
Cdd:PRK15041 233 AGGDLVKPIEVDGSNEMGQLAESLRHMQGELMRTVGDVRNGANAIYSGASEIATGNNDLSSRTEQQAASLEETAASMEQL 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 341 TTTVKDSSQRAEEAGRLVARTKDHANHSGAVVREAIGAMDQIDASSKAISNIIGVIDEIAFQTNLLALNAGVEAARAGEA 420
Cdd:PRK15041 313 TATVKQNAENARQASHLALSASETAQRGGKVVDNVVQTMRDISTSSQKIADIISVIDGIAFQTNILALNAAVEAARAGEQ 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 421 GKGFAVVAQEVRELAQRSATAAKEIKTLITASGSYVSNGVTLVTKAGAALQEIASHVENINGDITAIVEASREQSTALSE 500
Cdd:PRK15041 393 GRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLVESAGETMAEIVSAVTRVTDIMGEIASASDEQSRGIDQ 472
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2017767191 501 INRAINSVDQGTQQNAAMVEEQTAASHELAKEAAALFELLDQFRF-GEGNRSQTTKPLDSKRPSAFKPKPSVPTHSQ 576
Cdd:PRK15041 473 VGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAVFRIqQQQQQQRETSAVVKTVTPATPRKMAVADSGE 549
|
|
| PRK15048 |
PRK15048 |
methyl-accepting chemotaxis protein II; Provisional |
261-572 |
1.46e-69 |
|
methyl-accepting chemotaxis protein II; Provisional
Pssm-ID: 185008 [Multi-domain] Cd Length: 553 Bit Score: 234.90 E-value: 1.46e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 261 ADGDLSQQINQPFIPSLERLRTDFNSASNKLKLAMAAVAENAQAITSGSNEIRMSADDLAKRTEQQAASVEETAAALEQI 340
Cdd:PRK15048 231 AGGNLANTLTIDGRSEMGDLAQSVSHMQRSLTDTVTHVREGSDAIYAGTREIAAGNTDLSSRTEQQASALEETAASMEQL 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 341 TTTVKDSSQRAEEAGRLVARTKDHANHSGAVVREAIGAMDQIDASSKAISNIIGVIDEIAFQTNLLALNAGVEAARAGEA 420
Cdd:PRK15048 311 TATVKQNADNARQASQLAQSASDTAQHGGKVVDGVVKTMHEIADSSKKIADIISVIDGIAFQTNILALNAAVEAARAGEQ 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 421 GKGFAVVAQEVRELAQRSATAAKEIKTLITASGSYVSNGVTLVTKAGAALQEIASHVENINGDITAIVEASREQSTALSE 500
Cdd:PRK15048 391 GRGFAVVAGEVRNLASRSAQAAKEIKALIEDSVSRVDTGSVLVESAGETMNNIVNAVTRVTDIMGEIASASDEQSRGIDQ 470
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2017767191 501 INRAINSVDQGTQQNAAMVEEQTAASHELAKEAAALFELLDQFRFgeGNRSQTTKPLDSKRPSAfKPKPSVP 572
Cdd:PRK15048 471 VALAVSEMDRVTQQNASLVQESAAAAAALEEQASRLTQAVSAFRL--AASPLTNKPQTPSRPAS-EQPPAQP 539
|
|
| PRK09793 |
PRK09793 |
methyl-accepting chemotaxis protein IV; |
250-547 |
2.00e-63 |
|
methyl-accepting chemotaxis protein IV;
Pssm-ID: 182079 [Multi-domain] Cd Length: 533 Bit Score: 218.02 E-value: 2.00e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 250 VEQLALGLTRF---ADGDLSQQINQPFIPSLERLRTDFNSASNKLKLAMAAVAENAQAITSGSNEIRMSADDLAKRTEQQ 326
Cdd:PRK09793 215 VQPLAIIGSHFdsiAAGNLARPIAVYGRNEITAIFASLKTMQQALRGTVSDVRKGSQEMHIGIAEIVAGNNDLSSRTEQQ 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 327 AASVEETAAALEQITTTVKDSSQRAEEAGRLVARTKDHANHSGAVVREAIGAMDQIDASSKAISNIIGVIDEIAFQTNLL 406
Cdd:PRK09793 295 AASLAQTAASMEQLTATVGQNADNARQASELAKNAATTAQAGGVQVSTMTHTMQEIATSSQKIGDIISVIDGIAFQTNIL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 407 ALNAGVEAARAGEAGKGFAVVAQEVRELAQRSATAAKEIKTLITASGSYVSNGVTLVTKAGAALQEIASHVENINGDITA 486
Cdd:PRK09793 375 ALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKGLIEESVNRVQQGSKLVNNAAATMTDIVSSVTRVNDIMGE 454
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2017767191 487 IVEASREQSTALSEINRAINSVDQGTQQNAAMVEEQTAASHELAKEAAALFELLDQFRFGE 547
Cdd:PRK09793 455 IASASEEQRRGIEQVAQAVSQMDQVTQQNASLVEEAAVATEQLANQADHLSSRVAVFTLEE 515
|
|
| MCP_signal |
cd11386 |
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ... |
324-521 |
3.91e-62 |
|
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: 204.01 E-value: 3.91e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 324 EQQAASVEETAAALEQITTTVKDSSQRAEEAGRLVARTKDHANHSGAVVREAIGAMDQIDASSKAISNIIGVIDEIAFQT 403
Cdd:cd11386 1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 404 NLLALNAGVEAARAGEAGKGFAVVAQEVRELAQRSATAAKEIKTLITASGSYVSNGVTLVTKAGAALQEIASHVENINGD 483
Cdd:cd11386 81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 2017767191 484 ITAIVEASREQSTALSEINRAINSVDQGTQQNAAMVEE 521
Cdd:cd11386 161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEE 198
|
|
| MCPsignal |
pfam00015 |
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ... |
365-512 |
1.29e-45 |
|
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: 159.14 E-value: 1.29e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 365 ANHSGAVVREAIGAMDQIDASSKAISNIIGVIDEIAFQTNLLALNAGVEAARAGEAGKGFAVVAQEVRELAQRSATAAKE 444
Cdd:pfam00015 11 AQDGGKEVANVVGQMEQIAQSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLAERSAQAAKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 445 IKTLITA--------------SGSYVSNGVTLVTKAGAALQEIASHVENINGDITAIVEASREQSTALSEINRAINSVDQ 510
Cdd:pfam00015 91 IEALIIEiqkqtndstasiesTRQRVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDEQSAGIDQVNQAVARMDQ 170
|
..
gi 2017767191 511 GT 512
Cdd:pfam00015 171 VT 172
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
21-253 |
1.91e-30 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 120.13 E-value: 1.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 21 AIIEFDTQGNILRANKNFCDLMGYSENEIIGKHHRIFVEKDYAgSSDYTAFWKKLQGGTFECSEFKRIAKNGDDIWIRGN 100
Cdd:COG2202 23 AIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDD-DEFLELLRAALAGGGVWRGELRNRRKDGSLFWVELS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 101 YNPVKSASGKVLKIIKFANDITQTKM--DGL-DSSAKLTAV--SRAQATIEFTPDGKILAANENFLKALGYTLNEIVGQH 175
Cdd:COG2202 102 ISPVRDEDGEITGFVGIARDITERKRaeEALrESEERLRLLveNAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKS 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 176 HRMFVEPAEAnsQRYLEFWTRLRMGEYVA--DEFLRIGKGGRHVHIQASYNPVFDpSGKIIKVVKFATDVTGRVENVEQL 253
Cdd:COG2202 182 LLDLLHPEDR--ERLLELLRRLLEGGRESyeLELRLKDGDGRWVWVEASAVPLRD-GGEVIGVLGIVRDITERKRAEEAL 258
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
19-253 |
1.08e-21 |
|
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: 98.51 E-value: 1.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 19 SFAIIEFDTQGNILRANKNFCDLMGYSENEIIGKHHRIFVEKDYAG-SSDYTAFWKKlqGGTFECSEFKRIAKNGDDIWI 97
Cdd:COG5809 25 PDAILILDLEGKILKVNPAAERIFGYTEDELLGTNILDFLHPDDEKeLREILKLLKE--GESRDELEFELRHKNGKRLEF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 98 RGNYNPVKSASGKVLKIIKFANDITQTK-MDG--LDSSAKLTAVSRA--QATIEFTPDGKILAANENFLKALGYTLNEIV 172
Cdd:COG5809 103 SSKLSPIFDQNGDIEGMLAISRDITERKrMEEalRESEEKFRLIFNHspDGIIVTDLDGRIIYANPAACKLLGISIEELI 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 173 GQHHRMFVEPAEANSQRYLeFWTRLRMGEYVADEFLRIGKGGRHVHIQASYNPVfDPSGKIIKVVKFATDVTGRVENVEQ 252
Cdd:COG5809 183 GKSILELIHSDDQENVAAF-ISQLLKDGGIAQGEVRFWTKDGRWRLLEASGAPI-KKNGEVDGIVIIFRDITERKKLEEL 260
|
.
gi 2017767191 253 L 253
Cdd:COG5809 261 L 261
|
|
| PAS_4 |
pfam08448 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
142-248 |
4.30e-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: 68.59 E-value: 4.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 142 QATIEFTPDGKILAANENFLKALGYTLNEIVGQHHR-MFVEPAeanSQRYLEFWTRLRMGEYVADEFLRIGKGGRHVHIQ 220
Cdd:pfam08448 6 DALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAeLLPPED---AARLERALRRALEGEEPIDFLEELLLNGEERHYE 82
|
90 100
....*....|....*....|....*...
gi 2017767191 221 ASYNPVFDPSGKIIKVVKFATDVTGRVE 248
Cdd:pfam08448 83 LRLTPLRDPDGEVIGVLVISRDITERRR 110
|
|
| PAS_3 |
pfam08447 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
31-118 |
9.69e-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: 66.98 E-value: 9.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 31 ILRANKNFCDLMGYSENEIIGK--HHRIFVEKDYAgSSDYTAFWKKLQGGTFECSEFKRIAKNGDDIWIRGNYNPVKSAS 108
Cdd:pfam08447 1 IIYWSPRFEEILGYTPEELLGKgeSWLDLVHPDDR-ERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDEN 79
|
90
....*....|
gi 2017767191 109 GKVLKIIKFA 118
Cdd:pfam08447 80 GKPVRVIGVA 89
|
|
| KinA |
COG5805 |
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ... |
18-255 |
4.66e-13 |
|
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: 71.69 E-value: 4.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 18 LSFAIIEFDTQGNILRANKNFCDLMGYSENEIIGKHHRIFVEKDYagSSDYTAFWKKLQGGTFECSEFKRIAKNGDDIWI 97
Cdd:COG5805 43 LPDAIIAVNREGKVIYINPAMEKLLGYTSEEIIGKTIFDFLEKEY--HYRVKTRIERLQKGYDVVMIEQIYCKDGELIYV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 98 RGNYNPVKSASGKVlkIIKFANDITQTKMdgLDSSAKLTaVSRAQATIEFTPD--------GKILAANENFLKALGYTLN 169
Cdd:COG5805 121 EVKLFPIYNQNGQA--AILALRDITKKKK--IEEILQEQ-EERLQTLIENSPDlicvidtdGRILFINESIERLFGAPRE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 170 EIVGQHHRMFVEPAEANS-QRYLEFWTRLR-MGEYVADeflRIGKGGRHVHIQASYNPVFDPSGKIIKVVKFATDVTGRv 247
Cdd:COG5805 196 ELIGKNLLELLHPCDKEEfKERIESITEVWqEFIIERE---IITKDGRIRYFEAVIVPLIDTDGSVKGILVILRDITEK- 271
|
....*...
gi 2017767191 248 ENVEQLAL 255
Cdd:COG5805 272 KEAEELMA 279
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
150-244 |
5.35e-13 |
|
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: 64.79 E-value: 5.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 150 DGKILAANENFLKALGYTLNEIVGQHHRMFVEPAEANsQRYLEFWTRLRMGEyvADEFLRIGKGGRHVHIQASYNPVFDP 229
Cdd:pfam13426 1 DGRIIYVNDAALRLLGYTREELLGKSITDLFAEPEDS-ERLREALREGKAVR--EFEVVLYRKDGEPFPVLVSLAPIRDD 77
|
90
....*....|....*
gi 2017767191 230 SGKIIKVVKFATDVT 244
Cdd:pfam13426 78 GGELVGIIAILRDIT 92
|
|
| PAS_3 |
pfam08447 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
153-240 |
8.60e-13 |
|
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: 64.28 E-value: 8.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 153 ILAANENFLKALGYTLNEIVG--QHHRMFVEPAEANSQRyLEFWTRLRMGEYVADEFLRIGKGGRHVHIQASYNPVFDPS 230
Cdd:pfam08447 1 IIYWSPRFEEILGYTPEELLGkgESWLDLVHPDDRERVR-EALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDEN 79
|
90
....*....|
gi 2017767191 231 GKIIKVVKFA 240
Cdd:pfam08447 80 GKPVRVIGVA 89
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
18-121 |
1.99e-12 |
|
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: 63.81 E-value: 1.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 18 LSFAIIEFDTQGNILRANKNFCDLMGYSENEIIGKHHRIFVEKDYAGSSdYTAFWKKLQGGTFECSEFKRIAKNGDDIWI 97
Cdd:cd00130 1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREEL-RERLENLLSGGEPVTLEVRLRRKDGSVIWV 79
|
90 100
....*....|....*....|....
gi 2017767191 98 RGNYNPVKSASGKVLKIIKFANDI 121
Cdd:cd00130 80 LVSLTPIRDEGGEVIGLLGVVRDI 103
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
21-126 |
2.26e-12 |
|
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: 64.23 E-value: 2.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 21 AIIEFDTQGNILRANKNFCDLMGYSENEIIGKHHRIFVEKDYAGSSDyTAFWKKLQGGTFECSEFKRIA-KNGDDIWIRG 99
Cdd:TIGR00229 15 AIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVR-ERIERRLEGEPEPVSEERRVRrKDGSEIWVEV 93
|
90 100
....*....|....*....|....*..
gi 2017767191 100 NYNPVkSASGKVLKIIKFANDITQTKM 126
Cdd:TIGR00229 94 SVSPI-RTNGGELGVVGIVRDITERKE 119
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
28-123 |
4.70e-12 |
|
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: 62.48 E-value: 4.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 28 QGNILRANKNFCDLMGYSENEIIGKHHRIFVEKDYAgSSDYTAFWKklQGGTFECSEFKRIAKNGDDIWIRGNYNPVKSA 107
Cdd:pfam13426 1 DGRIIYVNDAALRLLGYTREELLGKSITDLFAEPED-SERLREALR--EGKAVREFEVVLYRKDGEPFPVLVSLAPIRDD 77
|
90
....*....|....*.
gi 2017767191 108 SGKVLKIIKFANDITQ 123
Cdd:pfam13426 78 GGELVGIIAILRDITE 93
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
17-145 |
1.05e-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: 67.31 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 17 DLSFAIIEFDTQGNILRANKNFCDLMGYSENEIIGKHHRIFVEKDYAGSSDyTAFWKKLQGGTFECSEFKRIAKNGDDIW 96
Cdd:COG5809 149 HSPDGIIVTDLDGRIIYANPAACKLLGISIEELIGKSILELIHSDDQENVA-AFISQLLKDGGIAQGEVRFWTKDGRWRL 227
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2017767191 97 IRGNYNPVKSaSGKVLKIIKFANDITQTK--MDGLDSSAKLTAVSRAQATI 145
Cdd:COG5809 228 LEASGAPIKK-NGEVDGIVIIFRDITERKklEELLRKSEKLSVVGELAAGI 277
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
143-243 |
1.86e-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: 58.03 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 143 ATIEFTPDGKILAANENFLKALGYTLNEIVGQHHRMFVEPAEanSQRYLEFWTR-LRMGEYVADEFLRIGKGGRHVHIQA 221
Cdd:cd00130 4 GVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPED--REELRERLENlLSGGEPVTLEVRLRRKDGSVIWVLV 81
|
90 100
....*....|....*....|..
gi 2017767191 222 SYNPVFDPSGKIIKVVKFATDV 243
Cdd:cd00130 82 SLTPIRDEGGEVIGLLGVVRDI 103
|
|
| PAS_4 |
pfam08448 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
18-125 |
2.48e-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: 57.81 E-value: 2.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 18 LSFAIIEFDTQGNILRANKNFCDLMGYSENEIIGKHHRIFVEKDYAGssDYTAFWKK-LQGGTFECSEFKRIAkNGDDIW 96
Cdd:pfam08448 4 LPDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAELLPPEDAA--RLERALRRaLEGEEPIDFLEELLL-NGEERH 80
|
90 100
....*....|....*....|....*....
gi 2017767191 97 IRGNYNPVKSASGKVLKIIKFANDITQTK 125
Cdd:pfam08448 81 YELRLTPLRDPDGEVIGVLVISRDITERR 109
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
143-253 |
2.33e-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: 55.37 E-value: 2.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 143 ATIEFTPDGKILAANENFLKALGYTLNEIVGQHHRMFVepAEANSQRYLEFWTRLRMGEY--VADEFLRIGKGGRHVHIQ 220
Cdd:TIGR00229 15 AIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELI--PEEDREEVRERIERRLEGEPepVSEERRVRRKDGSEIWVE 92
|
90 100 110
....*....|....*....|....*....|...
gi 2017767191 221 ASYNPVFDpSGKIIKVVKFATDVTGRVENVEQL 253
Cdd:TIGR00229 93 VSVSPIRT-NGGELGVVGIVRDITERKEAEEAL 124
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
11-121 |
6.33e-09 |
|
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: 53.96 E-value: 6.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 11 QILSALDlsFAIIEFDTQGNILRANKNFCDLMGYSENEIIGKHHRIFVEKDYAgSSDYTAFWKKLQGGTFECS-EFKRIA 89
Cdd:pfam00989 5 AILESLP--DGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDD-AEVAELLRQALLQGEESRGfEVSFRV 81
|
90 100 110
....*....|....*....|....*....|..
gi 2017767191 90 KNGDDIWIRGNYNPVKSASGKVLKIIKFANDI 121
Cdd:pfam00989 82 PDGRPRHVEVRASPVRDAGGEILGFLGVLRDI 113
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
1-244 |
1.26e-08 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 57.86 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 1 MISMFASNSNQILSALDLSF-AIIEFDTQGNILRANKNFCDLMGYSENEIIGKHHRIFVEKDYAGS-SDYTAfwKKLQGG 78
Cdd:PRK11359 3 LTDADNAADGIFFPALEQNMmGAVLINENDEVLFFNPAAEKLWGYKREEVIGNNIDMLIPRDLRPAhPEYIR--HNREGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 79 TFE----CSEFKRIAKNGDDIWIRGNYNPVkSASGKVLKIIkFANDIT-------QTKMdgldssaKLTAVSRA-QATIE 146
Cdd:PRK11359 81 KARvegmSRELQLEKKDGSKIWTRFALSKV-SAEGKVYYLA-LVRDASvemaqkeQTRQ-------LIIAVDHLdRPVIV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 147 FTPDGKILAANENFLKALGYTLNEIVGQHHRMFVEPAEANSQRYLEFWTRLRMGEYVADEFLRIGKGGRHVHIQASYNPV 226
Cdd:PRK11359 152 LDPERRIVQCNRAFTEMFGYCISEASGMQPDTLLNIPEFPADNRIRLQQLLWKTARDQDEFLLLTRTGEKIWIKASISPV 231
|
250
....*....|....*...
gi 2017767191 227 FDPSGKIIKVVKFATDVT 244
Cdd:PRK11359 232 YDVLAHLQNLVMTFSDIT 249
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
18-125 |
3.15e-07 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 52.93 E-value: 3.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 18 LSFAIIEFDTQGNILRANKNFCDLMGYSENEIIGKH-HRIFVEkdyaGSSDYTAFWKKLQ-GGTFECSEFKRIAKNGDDI 95
Cdd:COG3852 16 LPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPlAELFPE----DSPLRELLERALAeGQPVTEREVTLRRKDGEER 91
|
90 100 110
....*....|....*....|....*....|
gi 2017767191 96 WIRGNYNPVKSASGKVLkIIKFANDITQTK 125
Cdd:COG3852 92 PVDVSVSPLRDAEGEGG-VLLVLRDITERK 120
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
150-243 |
8.61e-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: 47.80 E-value: 8.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 150 DGKILAANENFLKALGYTLNEIVGQHHRMFVEPaEANSQRYLEFWTRLRMGE-YVADEFLRIGKGGRHVHIQASYNPVFD 228
Cdd:pfam00989 20 DGRILYVNAAAEELLGLSREEVIGKSLLDLIPE-EDDAEVAELLRQALLQGEeSRGFEVSFRVPDGRPRHVEVRASPVRD 98
|
90
....*....|....*
gi 2017767191 229 PSGKIIKVVKFATDV 243
Cdd:pfam00989 99 AGGEILGFLGVLRDI 113
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
10-53 |
3.05e-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: 42.00 E-value: 3.05e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2017767191 10 NQILSALDlsFAIIEFDTQGNILRANKNFCDLMGYSENEIIGKH 53
Cdd:smart00091 4 RAILESLP--DGIFVLDLDGRILYANPAAEELLGYSPEELIGKS 45
|
|
| PRK13558 |
PRK13558 |
bacterio-opsin activator; Provisional |
149-248 |
4.66e-05 |
|
bacterio-opsin activator; Provisional
Pssm-ID: 237426 [Multi-domain] Cd Length: 665 Bit Score: 46.37 E-value: 4.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 149 PDGKILAANENFLKALGYTLNEIVGQHHRmFVEPAEANSQRYLEFWTRLRMGEYVADEFLRIGKGGRHVHIQASYNPVFD 228
Cdd:PRK13558 169 PDEPLIYINDAFERITGYSPDEVLGRNCR-FLQGEDTNEERVAELREAIDEERPTSVELRNYRKDGSTFWNQVDIAPIRD 247
|
90 100
....*....|....*....|
gi 2017767191 229 PSGKIIKVVKFATDVTGRVE 248
Cdd:PRK13558 248 EDGTVTHYVGFQTDVTERKE 267
|
|
| PRK11360 |
PRK11360 |
two-component system sensor histidine kinase AtoS; |
149-254 |
8.54e-05 |
|
two-component system sensor histidine kinase AtoS;
Pssm-ID: 236901 [Multi-domain] Cd Length: 607 Bit Score: 45.34 E-value: 8.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 149 PDGKILAANENFLKALGYTLNEIVGQHHRMFVEPAEANSQRYLEfwtRLRMGEYVADEFLRIGKGGRHVHIQASYNPVFD 228
Cdd:PRK11360 280 RQGKITTMNPAAEVITGLQRHELVGKPYSELFPPNTPFASPLLD---TLEHGTEHVDLEISFPGRDRTIELSVSTSLLHN 356
|
90 100
....*....|....*....|....*.
gi 2017767191 229 PSGKIIKVVKFATDVTGRVENVEQLA 254
Cdd:PRK11360 357 THGEMIGALVIFSDLTERKRLQRRVA 382
|
|
| RocR |
COG3829 |
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ... |
10-178 |
1.89e-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: 44.38 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 10 NQILSALDLSFAIIefDTQGNILRANKNFCDLMGYSENEIIGKHhrifVEKDYAGSSDYTAfwkkLQGGTFECSEFKRIa 89
Cdd:COG3829 14 EAILDSLDDGIIVV--DADGRITYVNRAAERILGLPREEVIGKN----VTELIPNSPLLEV----LKTGKPVTGVIQKT- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 90 kNGDDIWIRGNYNPVKSaSGKVLKIIKFANDITQtkmdgldssakltaVSRAQATIEFTPDGKILAAnenflkalGYTLN 169
Cdd:COG3829 83 -GGKGKTVIVTAIPIFE-DGEVIGAVETFRDITE--------------LKRLERKLREEELERGLSA--------KYTFD 138
|
....*....
gi 2017767191 170 EIVGQHHRM 178
Cdd:COG3829 139 DIIGKSPAM 147
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
149-255 |
9.52e-04 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 41.76 E-value: 9.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 149 PDGKILAANENFLKALGYTLNEIVGQHHRMFVEPAEANSQRYLEfwTRLRMGEYVADEFLRIGKGGRHVHIQASYNPVFD 228
Cdd:COG3852 25 ADGRITYVNPAAERLLGLSAEELLGRPLAELFPEDSPLRELLER--ALAEGQPVTEREVTLRRKDGEERPVDVSVSPLRD 102
|
90 100
....*....|....*....|....*..
gi 2017767191 229 PSGKiIKVVKFATDVTGRVENVEQLAL 255
Cdd:COG3852 103 AEGE-GGVLLVLRDITERKRLERELRR 128
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
296-544 |
4.58e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.31 E-value: 4.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 296 AAVAENAQAITSGSNEIRMSA-----DDLAKRTEQQAASVEETAAALEQITTTVKDSSQRAEEAGRLVARTKDHANHSGA 370
Cdd:COG1196 209 AEKAERYRELKEELKELEAELlllklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 371 VVREAIGAMDQIDASSKAISNiigviDEIAFQTNLLALNAGVEAARAGEAGkgfavVAQEVRELAQRSATAAKEIKTLIT 450
Cdd:COG1196 289 EEYELLAELARLEQDIARLEE-----RRRELEERLEELEEELAELEEELEE-----LEEELEELEEELEEAEEELEEAEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017767191 451 ASgsyvsngVTLVTKAGAALQEIASHVENINGDITAIVEASREQSTALSEINRAINSVDQGTQQNAAMVEEQTAASHELA 530
Cdd:COG1196 359 EL-------AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
|
250
....*....|....
gi 2017767191 531 KEAAALFELLDQFR 544
Cdd:COG1196 432 ELEEEEEEEEEALE 445
|
|
| PAC |
smart00086 |
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ... |
84-123 |
5.74e-03 |
|
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: 34.85 E-value: 5.74e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2017767191 84 EFKRIAKNGDDIWIRGNYNPVKSASGKVLKIIKFANDITQ 123
Cdd:smart00086 3 EYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITE 42
|
|
| PAC |
smart00086 |
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ... |
206-246 |
9.49e-03 |
|
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: 34.47 E-value: 9.49e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2017767191 206 EFLRIGKGGRHVHIQASYNPVFDPSGKIIKVVKFATDVTGR 246
Cdd:smart00086 3 EYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITER 43
|
|
| |
