|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
175-510 |
4.86e-21 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 97.25 E-value: 4.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221040866 175 SGHLQRREKNKLKINNNVFVDKPAF--PEYKVSDAKKSKFILLHFSTFKAGWDWLILLATFYVAVTVPYNVCFIgndDLS 252
Cdd:PLN03192 13 KGTGEEDDSGSLSLRNLSKVILPPLgvPSYNQNHIGSDGWIISPMDSRYRWWETLMVVLVAYSAWVYPFEVAFL---NAS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221040866 253 TTRSTTVSDIAVEILFIIDIILNFRTTYVSKSGQVIF-EARSICIHYVTTWFIIDLIAALPFDLLYAF---------NVT 322
Cdd:PLN03192 90 PKRGLEIADNVVDLFFAVDIVLTFFVAYIDPRTQLLVrDRKKIAVRYLSTWFLMDVASTIPFQALAYLitgtvklnlSYS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221040866 323 VVSLVHLLKTVRLLRLLRLLQKLDRYSqHSTIVLTLLMSMFALLAHWMACIWYVIGkmEREDNSLLKWevgwlheLGKRL 402
Cdd:PLN03192 170 LLGLLRFWRLRRVKQLFTRLEKDIRFS-YFWIRCARLLSVTLFLVHCAGCLYYLIA--DRYPHQGKTW-------IGAVI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221040866 403 esPYYGNNTLGgpsIQsaYIAALYFTLSSLTSVGFGNVSANTDAEKIFSICTMLIGALMHALVFGNVTAIIQRMYSRWSL 482
Cdd:PLN03192 240 --PNFRETSLW---IR--YISAIYWSITTMTTVGYGDLHAVNTIEMIFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTME 312
|
330 340
....*....|....*....|....*...
gi 221040866 483 YHTRTKDLKDFIRVHHLPQQLKQRMLEY 510
Cdd:PLN03192 313 FRNSIEAASNFVGRNRLPPRLKDQILAY 340
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
40-135 |
9.29e-20 |
|
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: 84.05 E-value: 9.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221040866 40 FPIVYCSDGFCELAGFARTEVMQKSCSCkfLFGVETNEQLMLQIEKSLeeKTEFKGEIMFYKKNGSPFWCLLDIVPIKNE 119
Cdd:pfam13426 2 GRIIYVNDAALRLLGYTREELLGKSITD--LFAEPEDSERLREALREG--KAVREFEVVLYRKDGEPFPVLVSLAPIRDD 77
|
90
....*....|....*.
gi 221040866 120 KGDVVLFLASFKDITD 135
Cdd:pfam13426 78 GGELVGIIAILRDITE 93
|
|
| Ion_trans |
pfam00520 |
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ... |
224-481 |
3.23e-17 |
|
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This family is 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some sub-families (e.g. Na channels) the domain is repeated four times, whereas in others (e.g. K channels) the protein forms as a tetramer in the membrane.
Pssm-ID: 459842 [Multi-domain] Cd Length: 238 Bit Score: 81.16 E-value: 3.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221040866 224 WDWLILLATFYVAVTVPYNVCFIGNDDLSTTrsTTVSDIAVEILFIIDIILNFRTTYvsksgqvifearsICIHYVTT-W 302
Cdd:pfam00520 4 FELFILLLILLNTIFLALETYFQPEEPLTTV--LEILDYVFTGIFTLEMLLKIIAAG-------------FKKRYFRSpW 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221040866 303 FIIDLIAALPFDL-LYAFNVTVVSLVHLLKTVRLLRLLRLLQKLDRYsqhSTIVLTLLMSM-----FALLAHWMACIWYV 376
Cdd:pfam00520 69 NILDFVVVLPSLIsLVLSSVGSLSGLRVLRLLRLLRLLRLIRRLEGL---RTLVNSLIRSLkslgnLLLLLLLFLFIFAI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221040866 377 IGkMEREDNSLLKWevgwlhelgkrlESPYYGNNTLggpsiqSAYIAALYFTLSSLTSVGFGNVSANTDAEK-------I 449
Cdd:pfam00520 146 IG-YQLFGGKLKTW------------ENPDNGRTNF------DNFPNAFLWLFQTMTTEGWGDIMYDTIDGKgefwayiY 206
|
250 260 270
....*....|....*....|....*....|..
gi 221040866 450 FSICTMLIGALMHALVFGNVTAIIQRMYSRWS 481
Cdd:pfam00520 207 FVSFIILGGFLLLNLFIAVIIDNFQELTERTE 238
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
42-137 |
8.02e-17 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 80.45 E-value: 8.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221040866 42 IVYCSDGFCELAGFARTEVMQKSCSckFLFGVETNEQLMLQIEKSLEEKTEFKGEIMFYKKNGSPFWCLLDIVPIKNEKG 121
Cdd:COG2202 33 ILYVNPAFERLTGYSAEELLGKTLR--DLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGSLFWVELSISPVRDEDG 110
|
90
....*....|....*.
gi 221040866 122 DVVLFLASFKDITDTK 137
Cdd:COG2202 111 EITGFVGIARDITERK 126
|
|
| PRK13557 |
PRK13557 |
histidine kinase; Provisional |
41-134 |
3.32e-16 |
|
histidine kinase; Provisional
Pssm-ID: 237425 [Multi-domain] Cd Length: 540 Bit Score: 81.64 E-value: 3.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221040866 41 PIVYCSDGFCELAGFARTEVMQKSCscKFLFGVETNEQLMLQIEKSLEEKTEFKGEIMFYKKNGSPFWCLLDIVPIKNEK 120
Cdd:PRK13557 54 PIVFANRAFLEMTGYAAEEIIGNNC--RFLQGPETDRATVAEVRDAIAERREIATEILNYRKDGSSFWNALFVSPVYNDA 131
|
90
....*....|....
gi 221040866 121 GDVVLFLASFKDIT 134
Cdd:PRK13557 132 GDLVYFFGSQLDVS 145
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
42-133 |
2.50e-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: 57.64 E-value: 2.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221040866 42 IVYCSDGFCELAGFARTEVMQKSCSckFLFGVETNEQLMLQIEKSLEEKTEFKGEIMFYKKNGSPFWCLLDIVPIKNEKG 121
Cdd:cd00130 14 ILYANPAAEQLLGYSPEELIGKSLL--DLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLTPIRDEGG 91
|
90
....*....|..
gi 221040866 122 DVVLFLASFKDI 133
Cdd:cd00130 92 EVIGLLGVVRDI 103
|
|
| PAC |
smart00086 |
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ... |
94-135 |
9.33e-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: 51.03 E-value: 9.33e-09
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 221040866 94 KGEIMFYKKNGSPFWCLLDIVPIKNEKGDVVLFLASFKDITD 135
Cdd:smart00086 1 TVEYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITE 42
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
42-137 |
6.71e-07 |
|
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: 48.44 E-value: 6.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221040866 42 IVYCSDGFCELAGFARTEVMQKSCSckFLFGVETNEQLMLQIEKSLEEKTEFKG-EIMFYKKNGSPFWCLLDIVPIkNEK 120
Cdd:TIGR00229 25 ILYVNPAFEEIFGYSAEELIGRNVL--ELIPEEDREEVRERIERRLEGEPEPVSeERRVRRKDGSEIWVEVSVSPI-RTN 101
|
90
....*....|....*..
gi 221040866 121 GDVVLFLASFKDITDTK 137
Cdd:TIGR00229 102 GGELGVVGIVRDITERK 118
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
175-510 |
4.86e-21 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 97.25 E-value: 4.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221040866 175 SGHLQRREKNKLKINNNVFVDKPAF--PEYKVSDAKKSKFILLHFSTFKAGWDWLILLATFYVAVTVPYNVCFIgndDLS 252
Cdd:PLN03192 13 KGTGEEDDSGSLSLRNLSKVILPPLgvPSYNQNHIGSDGWIISPMDSRYRWWETLMVVLVAYSAWVYPFEVAFL---NAS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221040866 253 TTRSTTVSDIAVEILFIIDIILNFRTTYVSKSGQVIF-EARSICIHYVTTWFIIDLIAALPFDLLYAF---------NVT 322
Cdd:PLN03192 90 PKRGLEIADNVVDLFFAVDIVLTFFVAYIDPRTQLLVrDRKKIAVRYLSTWFLMDVASTIPFQALAYLitgtvklnlSYS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221040866 323 VVSLVHLLKTVRLLRLLRLLQKLDRYSqHSTIVLTLLMSMFALLAHWMACIWYVIGkmEREDNSLLKWevgwlheLGKRL 402
Cdd:PLN03192 170 LLGLLRFWRLRRVKQLFTRLEKDIRFS-YFWIRCARLLSVTLFLVHCAGCLYYLIA--DRYPHQGKTW-------IGAVI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221040866 403 esPYYGNNTLGgpsIQsaYIAALYFTLSSLTSVGFGNVSANTDAEKIFSICTMLIGALMHALVFGNVTAIIQRMYSRWSL 482
Cdd:PLN03192 240 --PNFRETSLW---IR--YISAIYWSITTMTTVGYGDLHAVNTIEMIFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTME 312
|
330 340
....*....|....*....|....*...
gi 221040866 483 YHTRTKDLKDFIRVHHLPQQLKQRMLEY 510
Cdd:PLN03192 313 FRNSIEAASNFVGRNRLPPRLKDQILAY 340
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
40-135 |
9.29e-20 |
|
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: 84.05 E-value: 9.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221040866 40 FPIVYCSDGFCELAGFARTEVMQKSCSCkfLFGVETNEQLMLQIEKSLeeKTEFKGEIMFYKKNGSPFWCLLDIVPIKNE 119
Cdd:pfam13426 2 GRIIYVNDAALRLLGYTREELLGKSITD--LFAEPEDSERLREALREG--KAVREFEVVLYRKDGEPFPVLVSLAPIRDD 77
|
90
....*....|....*.
gi 221040866 120 KGDVVLFLASFKDITD 135
Cdd:pfam13426 78 GGELVGIIAILRDITE 93
|
|
| Ion_trans |
pfam00520 |
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ... |
224-481 |
3.23e-17 |
|
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This family is 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some sub-families (e.g. Na channels) the domain is repeated four times, whereas in others (e.g. K channels) the protein forms as a tetramer in the membrane.
Pssm-ID: 459842 [Multi-domain] Cd Length: 238 Bit Score: 81.16 E-value: 3.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221040866 224 WDWLILLATFYVAVTVPYNVCFIGNDDLSTTrsTTVSDIAVEILFIIDIILNFRTTYvsksgqvifearsICIHYVTT-W 302
Cdd:pfam00520 4 FELFILLLILLNTIFLALETYFQPEEPLTTV--LEILDYVFTGIFTLEMLLKIIAAG-------------FKKRYFRSpW 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221040866 303 FIIDLIAALPFDL-LYAFNVTVVSLVHLLKTVRLLRLLRLLQKLDRYsqhSTIVLTLLMSM-----FALLAHWMACIWYV 376
Cdd:pfam00520 69 NILDFVVVLPSLIsLVLSSVGSLSGLRVLRLLRLLRLLRLIRRLEGL---RTLVNSLIRSLkslgnLLLLLLLFLFIFAI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221040866 377 IGkMEREDNSLLKWevgwlhelgkrlESPYYGNNTLggpsiqSAYIAALYFTLSSLTSVGFGNVSANTDAEK-------I 449
Cdd:pfam00520 146 IG-YQLFGGKLKTW------------ENPDNGRTNF------DNFPNAFLWLFQTMTTEGWGDIMYDTIDGKgefwayiY 206
|
250 260 270
....*....|....*....|....*....|..
gi 221040866 450 FSICTMLIGALMHALVFGNVTAIIQRMYSRWS 481
Cdd:pfam00520 207 FVSFIILGGFLLLNLFIAVIIDNFQELTERTE 238
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
42-137 |
8.02e-17 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 80.45 E-value: 8.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221040866 42 IVYCSDGFCELAGFARTEVMQKSCSckFLFGVETNEQLMLQIEKSLEEKTEFKGEIMFYKKNGSPFWCLLDIVPIKNEKG 121
Cdd:COG2202 33 ILYVNPAFERLTGYSAEELLGKTLR--DLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGSLFWVELSISPVRDEDG 110
|
90
....*....|....*.
gi 221040866 122 DVVLFLASFKDITDTK 137
Cdd:COG2202 111 EITGFVGIARDITERK 126
|
|
| PRK13557 |
PRK13557 |
histidine kinase; Provisional |
41-134 |
3.32e-16 |
|
histidine kinase; Provisional
Pssm-ID: 237425 [Multi-domain] Cd Length: 540 Bit Score: 81.64 E-value: 3.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221040866 41 PIVYCSDGFCELAGFARTEVMQKSCscKFLFGVETNEQLMLQIEKSLEEKTEFKGEIMFYKKNGSPFWCLLDIVPIKNEK 120
Cdd:PRK13557 54 PIVFANRAFLEMTGYAAEEIIGNNC--RFLQGPETDRATVAEVRDAIAERREIATEILNYRKDGSSFWNALFVSPVYNDA 131
|
90
....*....|....
gi 221040866 121 GDVVLFLASFKDIT 134
Cdd:PRK13557 132 GDLVYFFGSQLDVS 145
|
|
| PRK13558 |
PRK13558 |
bacterio-opsin activator; Provisional |
41-180 |
1.30e-14 |
|
bacterio-opsin activator; Provisional
Pssm-ID: 237426 [Multi-domain] Cd Length: 665 Bit Score: 76.80 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221040866 41 PIVYCSDGFCELAGFARTEVMQKSCscKFLFGVETNEQLMLQIEKSLEEKTEFKGEIMFYKKNGSPFWCLLDIVPIKNEK 120
Cdd:PRK13558 172 PLIYINDAFERITGYSPDEVLGRNC--RFLQGEDTNEERVAELREAIDEERPTSVELRNYRKDGSTFWNQVDIAPIRDED 249
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 221040866 121 GDVVLFLASFKDITDTKvkitpedKKEDKVKGRsragthfdsaRRRSRAVLYHISGHLQR 180
Cdd:PRK13558 250 GTVTHYVGFQTDVTERK-------EAELALQRE----------RRKLQRLLERVEGLVND 292
|
|
| PRK13559 |
PRK13559 |
hypothetical protein; Provisional |
41-135 |
1.31e-14 |
|
hypothetical protein; Provisional
Pssm-ID: 237427 [Multi-domain] Cd Length: 361 Bit Score: 75.24 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221040866 41 PIVYCSDGFCELAGFARTEVMQKSCscKFLFGVETNEQLMLQIEKSLEEKTEFKGEIMFYKKNGSPFWCLLDIVPIKNEK 120
Cdd:PRK13559 67 PIVLANQAFLDLTGYAAEEVVGRNC--RFLQGAATDPIAVAKIRAAIAAEREIVVELLNYRKDGEPFWNALHLGPVYGED 144
|
90
....*....|....*
gi 221040866 121 GDVVLFLASFKDITD 135
Cdd:PRK13559 145 GRLLYFFGSQWDVTD 159
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
42-133 |
2.50e-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: 57.64 E-value: 2.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221040866 42 IVYCSDGFCELAGFARTEVMQKSCSckFLFGVETNEQLMLQIEKSLEEKTEFKGEIMFYKKNGSPFWCLLDIVPIKNEKG 121
Cdd:cd00130 14 ILYANPAAEQLLGYSPEELIGKSLL--DLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLTPIRDEGG 91
|
90
....*....|..
gi 221040866 122 DVVLFLASFKDI 133
Cdd:cd00130 92 EVIGLLGVVRDI 103
|
|
| PAC |
smart00086 |
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ... |
94-135 |
9.33e-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: 51.03 E-value: 9.33e-09
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 221040866 94 KGEIMFYKKNGSPFWCLLDIVPIKNEKGDVVLFLASFKDITD 135
Cdd:smart00086 1 TVEYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITE 42
|
|
| Ion_trans_2 |
pfam07885 |
Ion channel; This family includes the two membrane helix type ion channels found in bacteria. |
421-475 |
2.37e-08 |
|
Ion channel; This family includes the two membrane helix type ion channels found in bacteria.
Pssm-ID: 462301 [Multi-domain] Cd Length: 78 Bit Score: 51.11 E-value: 2.37e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 221040866 421 YIAALYFTLSSLTSVGFGNVSANTDAEKIFSICTMLIGALMHALVFGNVTAIIQR 475
Cdd:pfam07885 24 FLDALYFSFVTLTTVGYGDIVPLTDAGRLFTIFYILIGIPLFAIFLAVLGRFLTE 78
|
|
| PAS_3 |
pfam08447 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
42-128 |
2.43e-07 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.
Pssm-ID: 430001 [Multi-domain] Cd Length: 89 Bit Score: 48.49 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221040866 42 IVYCSDGFCELAGFARTEVMQKSCSCKFLFGVETNEQLMLQIEKSLEEKTEFKGEIMFYKKNGSPFWCLLDIVPIKNEKG 121
Cdd:pfam08447 1 IIYWSPRFEEILGYTPEELLGKGESWLDLVHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDENG 80
|
....*..
gi 221040866 122 DVVLFLA 128
Cdd:pfam08447 81 KPVRVIG 87
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
4-137 |
2.78e-07 |
|
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 444511 [Multi-domain] Cd Length: 489 Bit Score: 53.05 E-value: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221040866 4 MKGLLAPQ--NTFLDTIATRFDGTHSNFILANAQvakGFpIVYCSDGFCELAGFARTEVMQKscscKFLFGVETNEQLML 81
Cdd:COG5809 1 MKSSKMELqlRKSEQRFRSLFENAPDAILILDLE---GK-ILKVNPAAERIFGYTEDELLGT----NILDFLHPDDEKEL 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 221040866 82 QIEKSLEEKTEFKGEIMF--YKKNGSPFWCLLDIVPIKNEKGDVVLFLASFKDITDTK 137
Cdd:COG5809 73 REILKLLKEGESRDELEFelRHKNGKRLEFSSKLSPIFDQNGDIEGMLAISRDITERK 130
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
42-137 |
6.71e-07 |
|
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: 48.44 E-value: 6.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221040866 42 IVYCSDGFCELAGFARTEVMQKSCSckFLFGVETNEQLMLQIEKSLEEKTEFKG-EIMFYKKNGSPFWCLLDIVPIkNEK 120
Cdd:TIGR00229 25 ILYVNPAFEEIFGYSAEELIGRNVL--ELIPEEDREEVRERIERRLEGEPEPVSeERRVRRKDGSEIWVEVSVSPI-RTN 101
|
90
....*....|....*..
gi 221040866 121 GDVVLFLASFKDITDTK 137
Cdd:TIGR00229 102 GGELGVVGIVRDITERK 118
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
42-133 |
3.17e-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: 46.26 E-value: 3.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221040866 42 IVYCSDGFCELAGFARTEVMQKScsckfLFGVETNEQ------LMLQIEKSLEEKTEFkgEIMFYKKNGSPFWCLLDIVP 115
Cdd:pfam00989 23 ILYVNAAAEELLGLSREEVIGKS-----LLDLIPEEDdaevaeLLRQALLQGEESRGF--EVSFRVPDGRPRHVEVRASP 95
|
90
....*....|....*...
gi 221040866 116 IKNEKGDVVLFLASFKDI 133
Cdd:pfam00989 96 VRDAGGEILGFLGVLRDI 113
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
42-137 |
3.46e-06 |
|
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: 49.59 E-value: 3.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221040866 42 IVYCSDGFCELAGFARTEVMQKSCSCkfLFGVETNEQLMLQIEKSLEEKTEFKGEIMFYKKNGSPFWCLLDIVPIkNEKG 121
Cdd:COG5809 163 IIYANPAACKLLGISIEELIGKSILE--LIHSDDQENVAAFISQLLKDGGIAQGEVRFWTKDGRWRLLEASGAPI-KKNG 239
|
90
....*....|....*.
gi 221040866 122 DVVLFLASFKDITDTK 137
Cdd:COG5809 240 EVDGIVIIFRDITERK 255
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
42-137 |
5.88e-06 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 48.69 E-value: 5.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221040866 42 IVYCSDGFCELAGFARTEVMQKSCSCKFLFGvetnEQLMLQIEKSLEEKTEFK-GEIMFYKKNGSPFWCLLDIVPIKNEK 120
Cdd:COG3852 29 ITYVNPAAERLLGLSAEELLGRPLAELFPED----SPLRELLERALAEGQPVTeREVTLRRKDGEERPVDVSVSPLRDAE 104
|
90
....*....|....*..
gi 221040866 121 GDvVLFLASFKDITDTK 137
Cdd:COG3852 105 GE-GGVLLVLRDITERK 120
|
|
| PAS_4 |
pfam08448 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
42-137 |
3.24e-05 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain is associated to signalling systems and works as a signal sensor domain. It recognizes differently substituted aromatic hydrocarbons, oxygen, different dodecanoic acids, autoinducers, 3,5-dimethyl-pyrazin-2-ol and N-alanyl-aminoacetone (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 312075 [Multi-domain] Cd Length: 110 Bit Score: 43.17 E-value: 3.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221040866 42 IVYCSDGFCELAGFARTEVMQKSCSCkfLFGVETNEQLMLQIEKSLEEKTEFKGEImFYKKNGSPFWCLLDIVPIKNEKG 121
Cdd:pfam08448 17 VRYANAAAAELFGLPPEELLGKTLAE--LLPPEDAARLERALRRALEGEEPIDFLE-ELLLNGEERHYELRLTPLRDPDG 93
|
90
....*....|....*.
gi 221040866 122 DVVLFLASFKDITDTK 137
Cdd:pfam08448 94 EVIGVLVISRDITERR 109
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
42-137 |
8.47e-05 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 44.25 E-value: 8.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221040866 42 IVYCSDGFCELAGFARTEVMQKSCSckFLFGVETNEQLMLQIEKSLEEKTEFkGEIMFYKKNGSPFWCLLDIVPIKNEKG 121
Cdd:COG2202 159 ILYVNPAAEELLGYSPEELLGKSLL--DLLHPEDRERLLELLRRLLEGGRES-YELELRLKDGDGRWVWVEASAVPLRDG 235
|
90
....*....|....*..
gi 221040866 122 D-VVLFLASFKDITDTK 137
Cdd:COG2202 236 GeVIGVLGIVRDITERK 252
|
|
| KinA |
COG5805 |
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ... |
42-137 |
1.56e-04 |
|
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: 44.34 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221040866 42 IVYCSDGFCELAGFARTEVMQKSCSckFLFGVETNEQLMLQIEKSLEEKTEFKGEIMFYKKNGSPFWCLLDIVPIKNEKG 121
Cdd:COG5805 179 ILFINESIERLFGAPREELIGKNLL--ELLHPCDKEEFKERIESITEVWQEFIIEREIITKDGRIRYFEAVIVPLIDTDG 256
|
90
....*....|....*.
gi 221040866 122 DVVLFLASFKDITDTK 137
Cdd:COG5805 257 SVKGILVILRDITEKK 272
|
|
| |
