|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13559 |
PRK13559 |
hypothetical protein; Provisional |
15-151 |
8.20e-27 |
|
hypothetical protein; Provisional
Pssm-ID: 237427 [Multi-domain] Cd Length: 361 Bit Score: 102.97 E-value: 8.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500088192 15 RLLESVMVNANDAIVITEAEPIDAPgprVVYCNAAFTHTTGFQPEEIIGRTPRILQNANTCRETLDRIRQSLSVWQPVEA 94
Cdd:PRK13559 43 RLFEQAMEQTRMAMCITDPHQPDLP---IVLANQAFLDLTGYAAEEVVGRNCRFLQGAATDPIAVAKIRAAIAAEREIVV 119
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2500088192 95 ELLNQRRDGSEFWVEVSIVPVANDSGFFTHWVAVQRDITDRRRAEEIE----RLLRDGSHR 151
Cdd:PRK13559 120 ELLNYRKDGEPFWNALHLGPVYGEDGRLLYFFGSQWDVTDIRAVRALEaherRLAREVDHR 180
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
13-140 |
2.39e-26 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 99.71 E-value: 2.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500088192 13 RLRLLESVMVNANDAIVITEAEPidapgpRVVYCNAAFTHTTGFQPEEIIGRTPRILQNANTCRETLDRIRQSLSVWQPV 92
Cdd:COG2202 9 SERRLRALVESSPDAIIITDLDG------RILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVW 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2500088192 93 EAELLNQRRDGSEFWVEVSIVPVANDSGFFTHWVAVQRDITDRRRAEE 140
Cdd:COG2202 83 RGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEE 130
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
42-134 |
1.35e-19 |
|
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 463873 [Multi-domain] Cd Length: 93 Bit Score: 77.89 E-value: 1.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500088192 42 RVVYCNAAFTHTTGFQPEEIIGRTPRILQNANTCRETLDRIRQSLSvwQPVEAELLNQRRDGSEFWVEVSIVPVANDSGF 121
Cdd:pfam13426 3 RIIYVNDAALRLLGYTREELLGKSITDLFAEPEDSERLREALREGK--AVREFEVVLYRKDGEPFPVLVSLAPIRDDGGE 80
|
90
....*....|...
gi 2500088192 122 FTHWVAVQRDITD 134
Cdd:pfam13426 81 LVGIIAILRDITE 93
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
13-140 |
3.18e-15 |
|
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: 3.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500088192 13 RLRLLESVMVNANDAIVIteaepIDAPGpRVVYCNAAFTHTTGFQPEEIIGRTPRIL---QNANTCRETLDRIRQSLSVw 89
Cdd:TIGR00229 1 SEERYRAIFESSPDAIIV-----IDLEG-NILYVNPAFEEIFGYSAEELIGRNVLELipeEDREEVRERIERRLEGEPE- 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2500088192 90 qPVEAELLNQRRDGSEFWVEVSIVPVANDSGfFTHWVAVQRDITDRRRAEE 140
Cdd:TIGR00229 74 -PVSEERRVRRKDGSEIWVEVSVSPIRTNGG-ELGVVGIVRDITERKEAEE 122
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
42-132 |
2.38e-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: 54.18 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500088192 42 RVVYCNAAFTHTTGFQPEEIIGRTPRILQNANTCRETLDRIRQSLSVWQPVEAELLNQRRDGSEFWVEVSIVPVANDSGF 121
Cdd:cd00130 13 RILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLTPIRDEGGE 92
|
90
....*....|.
gi 2500088192 122 FTHWVAVQRDI 132
Cdd:cd00130 93 VIGLLGVVRDI 103
|
|
| PAC |
smart00086 |
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ... |
95-135 |
1.19e-09 |
|
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif occurs C-terminal to a subset of all known PAS motifs. It is proposed to contribute to the PAS domain fold.
Pssm-ID: 197509 Cd Length: 43 Bit Score: 50.64 E-value: 1.19e-09
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2500088192 95 ELLNQRRDGSEFWVEVSIVPVANDSGFFTHWVAVQRDITDR 135
Cdd:smart00086 3 EYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITER 43
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13559 |
PRK13559 |
hypothetical protein; Provisional |
15-151 |
8.20e-27 |
|
hypothetical protein; Provisional
Pssm-ID: 237427 [Multi-domain] Cd Length: 361 Bit Score: 102.97 E-value: 8.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500088192 15 RLLESVMVNANDAIVITEAEPIDAPgprVVYCNAAFTHTTGFQPEEIIGRTPRILQNANTCRETLDRIRQSLSVWQPVEA 94
Cdd:PRK13559 43 RLFEQAMEQTRMAMCITDPHQPDLP---IVLANQAFLDLTGYAAEEVVGRNCRFLQGAATDPIAVAKIRAAIAAEREIVV 119
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2500088192 95 ELLNQRRDGSEFWVEVSIVPVANDSGFFTHWVAVQRDITDRRRAEEIE----RLLRDGSHR 151
Cdd:PRK13559 120 ELLNYRKDGEPFWNALHLGPVYGEDGRLLYFFGSQWDVTDIRAVRALEaherRLAREVDHR 180
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
13-140 |
2.39e-26 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 99.71 E-value: 2.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500088192 13 RLRLLESVMVNANDAIVITEAEPidapgpRVVYCNAAFTHTTGFQPEEIIGRTPRILQNANTCRETLDRIRQSLSVWQPV 92
Cdd:COG2202 9 SERRLRALVESSPDAIIITDLDG------RILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVW 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2500088192 93 EAELLNQRRDGSEFWVEVSIVPVANDSGFFTHWVAVQRDITDRRRAEE 140
Cdd:COG2202 83 RGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEE 130
|
|
| PRK13558 |
PRK13558 |
bacterio-opsin activator; Provisional |
14-143 |
1.30e-25 |
|
bacterio-opsin activator; Provisional
Pssm-ID: 237426 [Multi-domain] Cd Length: 665 Bit Score: 101.07 E-value: 1.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500088192 14 LRLLESVMVNANDAIVITEAEPIDAPgprVVYCNAAFTHTTGFQPEEIIGRTPRILQNANTCRETLDRIRQSLSVWQPVE 93
Cdd:PRK13558 147 RRLKERALDEAPVGITIADATLPDEP---LIYINDAFERITGYSPDEVLGRNCRFLQGEDTNEERVAELREAIDEERPTS 223
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2500088192 94 AELLNQRRDGSEFWVEVSIVPVANDSGFFTHWVAVQRDITDRRRAE-EIER 143
Cdd:PRK13558 224 VELRNYRKDGSTFWNQVDIAPIRDEDGTVTHYVGFQTDVTERKEAElALQR 274
|
|
| PRK13557 |
PRK13557 |
histidine kinase; Provisional |
43-140 |
3.37e-22 |
|
histidine kinase; Provisional
Pssm-ID: 237425 [Multi-domain] Cd Length: 540 Bit Score: 91.27 E-value: 3.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500088192 43 VVYCNAAFTHTTGFQPEEIIGRTPRILQNANTCRETLDRIRQSLSVWQPVEAELLNQRRDGSEFWVEVSIVPVANDSGFF 122
Cdd:PRK13557 55 IVFANRAFLEMTGYAAEEIIGNNCRFLQGPETDRATVAEVRDAIAERREIATEILNYRKDGSSFWNALFVSPVYNDAGDL 134
|
90
....*....|....*...
gi 2500088192 123 THWVAVQRDITDRRRAEE 140
Cdd:PRK13557 135 VYFFGSQLDVSRRRDAED 152
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
42-134 |
1.35e-19 |
|
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 463873 [Multi-domain] Cd Length: 93 Bit Score: 77.89 E-value: 1.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500088192 42 RVVYCNAAFTHTTGFQPEEIIGRTPRILQNANTCRETLDRIRQSLSvwQPVEAELLNQRRDGSEFWVEVSIVPVANDSGF 121
Cdd:pfam13426 3 RIIYVNDAALRLLGYTREELLGKSITDLFAEPEDSERLREALREGK--AVREFEVVLYRKDGEPFPVLVSLAPIRDDGGE 80
|
90
....*....|...
gi 2500088192 122 FTHWVAVQRDITD 134
Cdd:pfam13426 81 LVGIIAILRDITE 93
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
15-145 |
2.78e-16 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 74.11 E-value: 2.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500088192 15 RLLESVMVNANDAIVIteaepIDAPGpRVVYCNAAFTHTTGFQPEEIIGRTPR-ILQNANTCRETLDRIRQSLSvwQPVE 93
Cdd:COG3852 7 ELLRAILDSLPDAVIV-----LDADG-RITYVNPAAERLLGLSAEELLGRPLAeLFPEDSPLRELLERALAEGQ--PVTE 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2500088192 94 AELLNQRRDGSEFWVEVSIVPVANDSGfFTHWVAVQRDITDRRRAEEIERLL 145
Cdd:COG3852 79 REVTLRRKDGEERPVDVSVSPLRDAEG-EGGVLLVLRDITERKRLERELRRA 129
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
13-140 |
3.18e-15 |
|
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: 3.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500088192 13 RLRLLESVMVNANDAIVIteaepIDAPGpRVVYCNAAFTHTTGFQPEEIIGRTPRIL---QNANTCRETLDRIRQSLSVw 89
Cdd:TIGR00229 1 SEERYRAIFESSPDAIIV-----IDLEG-NILYVNPAFEEIFGYSAEELIGRNVLELipeEDREEVRERIERRLEGEPE- 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2500088192 90 qPVEAELLNQRRDGSEFWVEVSIVPVANDSGfFTHWVAVQRDITDRRRAEE 140
Cdd:TIGR00229 74 -PVSEERRVRRKDGSEIWVEVSVSPIRTNGG-ELGVVGIVRDITERKEAEE 122
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
15-132 |
7.02e-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. 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: 60.89 E-value: 7.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500088192 15 RLLESVMVNANDAIVIteaepIDAPGpRVVYCNAAFTHTTGFQPEEIIGRTPRILQNANTCRETLDRIRQSLSVWQPVEA 94
Cdd:pfam00989 1 EDLRAILESLPDGIFV-----VDEDG-RILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALLQGEESRG 74
|
90 100 110
....*....|....*....|....*....|....*....
gi 2500088192 95 ELLNQRR-DGSEFWVEVSIVPVANDSGFFTHWVAVQRDI 132
Cdd:pfam00989 75 FEVSFRVpDGRPRHVEVRASPVRDAGGEILGFLGVLRDI 113
|
|
| KinA |
COG5805 |
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ... |
17-144 |
4.02e-12 |
|
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 444507 [Multi-domain] Cd Length: 496 Bit Score: 62.44 E-value: 4.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500088192 17 LESVMVNANDAIVITEAEPidapgpRVVYCNAAFTHTTGFQPEEIIGRT-PRILQNANTCrETLDRIRQSLSVWQPVEAE 95
Cdd:COG5805 159 LQTLIENSPDLICVIDTDG------RILFINESIERLFGAPREELIGKNlLELLHPCDKE-EFKERIESITEVWQEFIIE 231
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2500088192 96 LLNQRRDGSEFWVEVSIVPVANDSGFFTHWVAVQRDITDRRRAEEI----ERL 144
Cdd:COG5805 232 REIITKDGRIRYFEAVIVPLIDTDGSVKGILVILRDITEKKEAEELmarsEKL 284
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
15-140 |
4.69e-12 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 61.58 E-value: 4.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500088192 15 RLLESVMVNANDAIVITEAEPidapgpRVVYCNAAFTHTTGFQPEEIIGRTPRILQNANTCRETLDRIRQSLS-VWQPVE 93
Cdd:COG2202 137 ERLRLLVENAPDGIFVLDLDG------RILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEgGRESYE 210
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2500088192 94 AELLNQRRDGSEFWVEVSIVPVaNDSGFFTHWVAVQRDITDRRRAEE 140
Cdd:COG2202 211 LELRLKDGDGRWVWVEASAVPL-RDGGEVIGVLGIVRDITERKRAEE 256
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
5-143 |
9.17e-12 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 61.71 E-value: 9.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500088192 5 QVGARRSPRLRLLesVMVNANDAIVITEAEPidapgpRVVYCNAAFTHTTGFQPEEIIGRTP-RILQNANTCRETLDRIR 83
Cdd:PRK11359 128 EMAQKEQTRQLII--AVDHLDRPVIVLDPER------RIVQCNRAFTEMFGYCISEASGMQPdTLLNIPEFPADNRIRLQ 199
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500088192 84 QSLSVWQPVEAELLNQRRDGSEFWVEVSIVPVANDSGFFTHWVAVQRDITDRRRAEEIER 143
Cdd:PRK11359 200 QLLWKTARDQDEFLLLTRTGEKIWIKASISPVYDVLAHLQNLVMTFSDITEERQIRQLEG 259
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
42-132 |
2.38e-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: 54.18 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500088192 42 RVVYCNAAFTHTTGFQPEEIIGRTPRILQNANTCRETLDRIRQSLSVWQPVEAELLNQRRDGSEFWVEVSIVPVANDSGF 121
Cdd:cd00130 13 RILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLTPIRDEGGE 92
|
90
....*....|.
gi 2500088192 122 FTHWVAVQRDI 132
Cdd:cd00130 93 VIGLLGVVRDI 103
|
|
| PAC |
smart00086 |
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ... |
95-135 |
1.19e-09 |
|
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif occurs C-terminal to a subset of all known PAS motifs. It is proposed to contribute to the PAS domain fold.
Pssm-ID: 197509 Cd Length: 43 Bit Score: 50.64 E-value: 1.19e-09
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2500088192 95 ELLNQRRDGSEFWVEVSIVPVANDSGFFTHWVAVQRDITDR 135
Cdd:smart00086 3 EYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITER 43
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
17-146 |
2.73e-09 |
|
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: 54.21 E-value: 2.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500088192 17 LESVMVNANDAIVITEAEpidapGpRVVYCNAAFTHTTGFQPEEIIGRTPRILQNANTCRETLDRIRQSLSVWQPVEAEL 96
Cdd:COG5809 143 FRLIFNHSPDGIIVTDLD-----G-RIIYANPAACKLLGISIEELIGKSILELIHSDDQENVAAFISQLLKDGGIAQGEV 216
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2500088192 97 LNQRRDGSEFWVEVSIVPVANDSGffTHW-VAVQRDITDRRraeEIERLLR 146
Cdd:COG5809 217 RFWTKDGRWRLLEASGAPIKKNGE--VDGiVIIFRDITERK---KLEELLR 262
|
|
| RocR |
COG3829 |
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ... |
15-140 |
1.26e-08 |
|
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: 52.47 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500088192 15 RLLESVMVNANDAIVIteaepIDAPGpRVVYCNAAFTHTTGFQPEEIIGRTPRILqnantcrETLDRIRQSLSVWQPVEA 94
Cdd:COG3829 11 EELEAILDSLDDGIIV-----VDADG-RITYVNRAAERILGLPREEVIGKNVTEL-------IPNSPLLEVLKTGKPVTG 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2500088192 95 ELlnQRRDGSEFWVEVSIVPVANDsGFFTHWVAVQRDITDRRRAEE 140
Cdd:COG3829 78 VI--QKTGGKGKTVIVTAIPIFED-GEVIGAVETFRDITELKRLER 120
|
|
| PAS_3 |
pfam08447 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
43-128 |
1.54e-08 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.
Pssm-ID: 430001 [Multi-domain] Cd Length: 89 Bit Score: 49.26 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500088192 43 VVYCNAAFTHTTGFQPEEIIGRTPRILQNanTCRETLDRIRQSLSVW----QPVEAELLNQRRDGSEFWVEVSIVPVAND 118
Cdd:pfam08447 1 IIYWSPRFEEILGYTPEELLGKGESWLDL--VHPDDRERVREALWEAlkggEPYSGEYRIRRKDGEYRWVEARARPIRDE 78
|
90
....*....|
gi 2500088192 119 SGFFTHWVAV 128
Cdd:pfam08447 79 NGKPVRVIGV 88
|
|
| PAS_4 |
pfam08448 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
42-137 |
1.49e-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 is associated to signalling systems and works as a signal sensor domain. It recognizes differently substituted aromatic hydrocarbons, oxygen, different dodecanoic acids, autoinducers, 3,5-dimethyl-pyrazin-2-ol and N-alanyl-aminoacetone (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 312075 [Multi-domain] Cd Length: 110 Bit Score: 47.02 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500088192 42 RVVYCNAAFTHTTGFQPEEIIGRTPRILQNANTCRETLDRIRQSLSVWQPVEaELLNQRRDGSEFWVEVSIVPVANDSGF 121
Cdd:pfam08448 16 RVRYANAAAAELFGLPPEELLGKTLAELLPPEDAARLERALRRALEGEEPID-FLEELLLNGEERHYELRLTPLRDPDGE 94
|
90
....*....|....*.
gi 2500088192 122 FTHWVAVQRDITDRRR 137
Cdd:pfam08448 95 VIGVLVISRDITERRR 110
|
|
| PRK13560 |
PRK13560 |
hypothetical protein; Provisional |
4-147 |
1.20e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 106506 [Multi-domain] Cd Length: 807 Bit Score: 43.89 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500088192 4 RQVGARRSPRLRLLESVMVNANDAIVITEAEPIdapgprVVYCNAAFTHTTGFQPEEIIGRTPRILQNAntcretldrir 83
Cdd:PRK13560 193 KRAEERIDEALHFLQQLLDNIADPAFWKDEDAK------VFGCNDAACLACGFRREEIIGMSIHDFAPA----------- 255
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2500088192 84 QSLSVWQPVEAELLN-----------QRRDGSEFWVEVSIVPVANDSGFF--THWVAVQRDITDRRRAEEIERLLRD 147
Cdd:PRK13560 256 QPADDYQEADAAKFDadgsqiieaefQNKDGRTRPVDVIFNHAEFDDKENhcAGLVGAITDISGRRAAERELLEKED 332
|
|
| PRK11091 |
PRK11091 |
aerobic respiration control sensor protein ArcB; Provisional |
46-147 |
8.12e-05 |
|
aerobic respiration control sensor protein ArcB; Provisional
Pssm-ID: 236842 [Multi-domain] Cd Length: 779 Bit Score: 41.46 E-value: 8.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500088192 46 CNAAFTHTTGFQPEEIIGRTPRILQNANTCRETLDRIRQSLSVWQPVEAELLNQRRDGSEFWVEVSIVPVANDSGFFTHW 125
Cdd:PRK11091 180 CNRAMELLTGKSEKQLIGLTPKDVYSPEAAEKVIETDEKVFRHNVSLTYEQWLDYPDGRKACFELRKVPFYDRVGKRHGL 259
|
90 100
....*....|....*....|...
gi 2500088192 126 VAVQRDITDRRRAEE-IERLLRD 147
Cdd:PRK11091 260 MGFGRDITERKRYQDaLEKASRD 282
|
|
| NtrY |
COG5000 |
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
13-142 |
3.00e-04 |
|
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: 39.56 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500088192 13 RLRLLESVMVNANDAIVIteaepIDAPGpRVVYCNAAFTHTTGFQPEEIIGRTpriLQNANTCRETLDRIRQSLSVWQPV 92
Cdd:COG5000 88 RRRYLETILENLPAGVIV-----LDADG-RITLANPAAERLLGIPLEELIGKP---LEELLPELDLAELLREALERGWQE 158
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2500088192 93 EAELlnqrRDGSEFWVEVSIVPVANDSgffthWVAVQRDITDRRRAEEIE 142
Cdd:COG5000 159 EIEL----TRDGRRTLLVRASPLRDDG-----YVIVFDDITELLRAERLA 199
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
15-65 |
8.07e-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: 33.14 E-value: 8.07e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2500088192 15 RLLESVMVNANDAIVIteaepIDAPGpRVVYCNAAFTHTTGFQPEEIIGRT 65
Cdd:smart00091 1 ERLRAILESLPDGIFV-----LDLDG-RILYANPAAEELLGYSPEELIGKS 45
|
|
| |
