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Conserved domains on  [gi|442616378|ref|NP_001259557|]
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ether a go-go, isoform F [Drosophila melanogaster]

Protein Classification

potassium voltage-gated channel protein; ion transporter( domain architecture ID 12140962)

potassium voltage-gated channel protein similar to members from Homo sapiens potassium voltage-gated channel subfamilies (F, G, and V)| ion transporter such as a voltage-gated cation channel, which enables the selective translocation of cations such as sodium, calcium, or potassium, across cell membranes

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 228-489 1.60e-31

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: 121.99  E-value: 1.60e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616378  228 IWDWVILCLTFYTAIMVPYNVAFKNKTSEDVSLLVVDSIVDVIFFIDIVLNFHTTFvgpggevvsdpkvIRMNYLKS-WF 306
Cdd:pfam00520   3 YFELFILLLILLNTIFLALETYFQPEEPLTTVLEILDYVFTGIFTLEMLLKIIAAG-------------FKKRYFRSpWN 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616378  307 IIDLLSCLPYDVfnAFDRDEDGIGSLFSALKVVRLLRLGRVVRKLD--RYLEYGAAMLILLLCFYMLVAHWLACIWYSIG 384
Cdd:pfam00520  70 ILDFVVVLPSLI--SLVLSSVGSLSGLRVLRLLRLLRLLRLIRRLEglRTLVNSLIRSLKSLGNLLLLLLLFLFIFAIIG 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616378  385 rsdadngiqYSWLWKLANVTQSPYSYIWSNDTgpelvngpsrksmYVTALYFTMTCMTSVGFGNVAAETDNEK------- 457
Cdd:pfam00520 148 ---------YQLFGGKLKTWENPDNGRTNFDN-------------FPNAFLWLFQTMTTEGWGDIMYDTIDGKgefwayi 205

                         250       260       270
                  ....*....|....*....|....*....|..
gi 442616378  458 VFTICMMIIAALLYATIFGHVTTIIQQMTSAT 489
Cdd:pfam00520 206 YFVSFIILGGFLLLNLFIAVIIDNFQELTERT 237
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
 40-138 1.18e-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: 86.75  E-value: 1.18e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616378   40 DFPIVYCNESFCKISGYNRAEVMQKSCRYVCGfmygeltDKETVGRLEYTLEN-QQQDQFEILLYKKNKTPLWLLLQVAP 118
Cdd:pfam13426   1 DGRIIYVNDAALRLLGYTREELLGKSITDLFA-------EPEDSERLREALREgKAVREFEVVLYRKDGEPFPVLVSLAP 73

                          90       100
                  ....*....|....*....|
gi 442616378  119 IRNERDLVVLFLLTFRDITA 138
Cdd:pfam13426  74 IRDDGGELVGIIAILRDITE 93
 
Name Accession Description Interval E-value
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 228-489 1.60e-31

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: 121.99  E-value: 1.60e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616378  228 IWDWVILCLTFYTAIMVPYNVAFKNKTSEDVSLLVVDSIVDVIFFIDIVLNFHTTFvgpggevvsdpkvIRMNYLKS-WF 306
Cdd:pfam00520   3 YFELFILLLILLNTIFLALETYFQPEEPLTTVLEILDYVFTGIFTLEMLLKIIAAG-------------FKKRYFRSpWN 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616378  307 IIDLLSCLPYDVfnAFDRDEDGIGSLFSALKVVRLLRLGRVVRKLD--RYLEYGAAMLILLLCFYMLVAHWLACIWYSIG 384
Cdd:pfam00520  70 ILDFVVVLPSLI--SLVLSSVGSLSGLRVLRLLRLLRLLRLIRRLEglRTLVNSLIRSLKSLGNLLLLLLLFLFIFAIIG 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616378  385 rsdadngiqYSWLWKLANVTQSPYSYIWSNDTgpelvngpsrksmYVTALYFTMTCMTSVGFGNVAAETDNEK------- 457
Cdd:pfam00520 148 ---------YQLFGGKLKTWENPDNGRTNFDN-------------FPNAFLWLFQTMTTEGWGDIMYDTIDGKgefwayi 205

                         250       260       270
                  ....*....|....*....|....*....|..
gi 442616378  458 VFTICMMIIAALLYATIFGHVTTIIQQMTSAT 489
Cdd:pfam00520 206 YFVSFIILGGFLLLNLFIAVIIDNFQELTERT 237
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 229-520 5.26e-29

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 121.90  E-value: 5.26e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616378 229 WDWVILCLTFYTAIMVPYNVAFKNkTSEDVSLLVVDSIVDVIFFIDIVLNFHTTFVGPGGEV-VSDPKVIRMNYLKSWFI 307
Cdd:PLN03192  64 WETLMVVLVAYSAWVYPFEVAFLN-ASPKRGLEIADNVVDLFFAVDIVLTFFVAYIDPRTQLlVRDRKKIAVRYLSTWFL 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616378 308 IDLLSCLPYDVFNAFDRDEDGIGSLFSALKVVRLLRLGRVVRKLDRyLE------YGAAMLILLLCFYMLVAHWLACIWY 381
Cdd:PLN03192 143 MDVASTIPFQALAYLITGTVKLNLSYSLLGLLRFWRLRRVKQLFTR-LEkdirfsYFWIRCARLLSVTLFLVHCAGCLYY 221

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616378 382 SIgrsdADNGIQYSWLWKLANVTQSPYSYIWSNdtgpelvngpsrksmYVTALYFTMTCMTSVGFGNVAAETDNEKVFTI 461
Cdd:PLN03192 222 LI----ADRYPHQGKTWIGAVIPNFRETSLWIR---------------YISAIYWSITTMTTVGYGDLHAVNTIEMIFII 282

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 442616378 462 CMMIIAALLYATIFGHVTTIIQQMTSATAKYHDMLNNVREFMKLHEVPKALSERVMDYV 520
Cdd:PLN03192 283 FYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRLKDQILAYM 341
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
 40-138 1.18e-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: 86.75  E-value: 1.18e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616378   40 DFPIVYCNESFCKISGYNRAEVMQKSCRYVCGfmygeltDKETVGRLEYTLEN-QQQDQFEILLYKKNKTPLWLLLQVAP 118
Cdd:pfam13426   1 DGRIIYVNDAALRLLGYTREELLGKSITDLFA-------EPEDSERLREALREgKAVREFEVVLYRKDGEPFPVLVSLAP 73

                          90       100
                  ....*....|....*....|
gi 442616378  119 IRNERDLVVLFLLTFRDITA 138
Cdd:pfam13426  74 IRDDGGELVGIIAILRDITE 93
PAS COG2202
PAS domain [Signal transduction mechanisms];
40-141 3.73e-18

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 84.31  E-value: 3.73e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616378  40 DFPIVYCNESFCKISGYNRAEVMQKSCRyvcgFMYGELTDKETVGRLEYTLENQQQDQFEILLYKKNKTPLWLLLQVAPI 119
Cdd:COG2202   30 DGRILYVNPAFERLTGYSAEELLGKTLR----DLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGSLFWVELSISPV 105

                         90       100
                 ....*....|....*....|..
gi 442616378 120 RNERDLVVLFLLTFRDITALKQ 141
Cdd:COG2202  106 RDEDGEITGFVGIARDITERKR 127
PRK13558 PRK13558
bacterio-opsin activator; Provisional
 33-141 1.74e-14

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 76.41  E-value: 1.74e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616378  33 LANAQIVDFPIVYCNESFCKISGYNRAEVMQKSCRyvcgFMYGELTDKETVGRLEYTLENQQQDQFEILLYKKNKTPLWL 112
Cdd:PRK13558 163 IADATLPDEPLIYINDAFERITGYSPDEVLGRNCR----FLQGEDTNEERVAELREAIDEERPTSVELRNYRKDGSTFWN 238

                         90       100       110
                 ....*....|....*....|....*....|
gi 442616378 113 LLQVAPIRNErDLVVLFLLTFR-DITALKQ 141
Cdd:PRK13558 239 QVDIAPIRDE-DGTVTHYVGFQtDVTERKE 267
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 40-136 2.51e-09

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 54.56  E-value: 2.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616378  40 DFPIVYCNESFCKISGYNRAEVMQKSCRYVcgFMYGELTDKETvgRLEYTLENQQQDQFEILLYKKNKTPLWLLLQVAPI 119
Cdd:cd00130   11 DGRILYANPAAEQLLGYSPEELIGKSLLDL--IHPEDREELRE--RLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLTPI 86

                         90
                 ....*....|....*..
gi 442616378 120 RNERDLVVLFLLTFRDI 136
Cdd:cd00130   87 RDEGGEVIGLLGVVRDI 103
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
 43-141 2.55e-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: 49.60  E-value: 2.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616378   43 IVYCNESFCKISGYNRAEVMQKSCRYvcgFMYGELTDkETVGRLEYTLENQQQDQFEILLYK-KNKTPLWLLLQVAPIRN 121
Cdd:TIGR00229  25 ILYVNPAFEEIFGYSAEELIGRNVLE---LIPEEDRE-EVRERIERRLEGEPEPVSEERRVRrKDGSEIWVEVSVSPIRT 100

                          90       100
                  ....*....|....*....|
gi 442616378  122 ERDlVVLFLLTFRDITALKQ 141
Cdd:TIGR00229 101 NGG-ELGVVGIVRDITERKE 119
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
 97-139 1.89e-06

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: 44.48  E-value: 1.89e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 442616378    97 QFEILLYKKNKTPLWLLLQVAPIRNERDLVVLFLLTFRDITAL 139
Cdd:smart00086   1 TVEYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITER 43
 
Name Accession Description Interval E-value
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 228-489 1.60e-31

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: 121.99  E-value: 1.60e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616378  228 IWDWVILCLTFYTAIMVPYNVAFKNKTSEDVSLLVVDSIVDVIFFIDIVLNFHTTFvgpggevvsdpkvIRMNYLKS-WF 306
Cdd:pfam00520   3 YFELFILLLILLNTIFLALETYFQPEEPLTTVLEILDYVFTGIFTLEMLLKIIAAG-------------FKKRYFRSpWN 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616378  307 IIDLLSCLPYDVfnAFDRDEDGIGSLFSALKVVRLLRLGRVVRKLD--RYLEYGAAMLILLLCFYMLVAHWLACIWYSIG 384
Cdd:pfam00520  70 ILDFVVVLPSLI--SLVLSSVGSLSGLRVLRLLRLLRLLRLIRRLEglRTLVNSLIRSLKSLGNLLLLLLLFLFIFAIIG 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616378  385 rsdadngiqYSWLWKLANVTQSPYSYIWSNDTgpelvngpsrksmYVTALYFTMTCMTSVGFGNVAAETDNEK------- 457
Cdd:pfam00520 148 ---------YQLFGGKLKTWENPDNGRTNFDN-------------FPNAFLWLFQTMTTEGWGDIMYDTIDGKgefwayi 205

                         250       260       270
                  ....*....|....*....|....*....|..
gi 442616378  458 VFTICMMIIAALLYATIFGHVTTIIQQMTSAT 489
Cdd:pfam00520 206 YFVSFIILGGFLLLNLFIAVIIDNFQELTERT 237
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 229-520 5.26e-29

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 121.90  E-value: 5.26e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616378 229 WDWVILCLTFYTAIMVPYNVAFKNkTSEDVSLLVVDSIVDVIFFIDIVLNFHTTFVGPGGEV-VSDPKVIRMNYLKSWFI 307
Cdd:PLN03192  64 WETLMVVLVAYSAWVYPFEVAFLN-ASPKRGLEIADNVVDLFFAVDIVLTFFVAYIDPRTQLlVRDRKKIAVRYLSTWFL 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616378 308 IDLLSCLPYDVFNAFDRDEDGIGSLFSALKVVRLLRLGRVVRKLDRyLE------YGAAMLILLLCFYMLVAHWLACIWY 381
Cdd:PLN03192 143 MDVASTIPFQALAYLITGTVKLNLSYSLLGLLRFWRLRRVKQLFTR-LEkdirfsYFWIRCARLLSVTLFLVHCAGCLYY 221

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616378 382 SIgrsdADNGIQYSWLWKLANVTQSPYSYIWSNdtgpelvngpsrksmYVTALYFTMTCMTSVGFGNVAAETDNEKVFTI 461
Cdd:PLN03192 222 LI----ADRYPHQGKTWIGAVIPNFRETSLWIR---------------YISAIYWSITTMTTVGYGDLHAVNTIEMIFII 282

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 442616378 462 CMMIIAALLYATIFGHVTTIIQQMTSATAKYHDMLNNVREFMKLHEVPKALSERVMDYV 520
Cdd:PLN03192 283 FYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRLKDQILAYM 341
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
 40-138 1.18e-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: 86.75  E-value: 1.18e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616378   40 DFPIVYCNESFCKISGYNRAEVMQKSCRYVCGfmygeltDKETVGRLEYTLEN-QQQDQFEILLYKKNKTPLWLLLQVAP 118
Cdd:pfam13426   1 DGRIIYVNDAALRLLGYTREELLGKSITDLFA-------EPEDSERLREALREgKAVREFEVVLYRKDGEPFPVLVSLAP 73

                          90       100
                  ....*....|....*....|
gi 442616378  119 IRNERDLVVLFLLTFRDITA 138
Cdd:pfam13426  74 IRDDGGELVGIIAILRDITE 93
PAS COG2202
PAS domain [Signal transduction mechanisms];
40-141 3.73e-18

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 84.31  E-value: 3.73e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616378  40 DFPIVYCNESFCKISGYNRAEVMQKSCRyvcgFMYGELTDKETVGRLEYTLENQQQDQFEILLYKKNKTPLWLLLQVAPI 119
Cdd:COG2202   30 DGRILYVNPAFERLTGYSAEELLGKTLR----DLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGSLFWVELSISPV 105

                         90       100
                 ....*....|....*....|..
gi 442616378 120 RNERDLVVLFLLTFRDITALKQ 141
Cdd:COG2202  106 RDEDGEITGFVGIARDITERKR 127
PRK13558 PRK13558
bacterio-opsin activator; Provisional
 33-141 1.74e-14

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 76.41  E-value: 1.74e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616378  33 LANAQIVDFPIVYCNESFCKISGYNRAEVMQKSCRyvcgFMYGELTDKETVGRLEYTLENQQQDQFEILLYKKNKTPLWL 112
Cdd:PRK13558 163 IADATLPDEPLIYINDAFERITGYSPDEVLGRNCR----FLQGEDTNEERVAELREAIDEERPTSVELRNYRKDGSTFWN 238

                         90       100       110
                 ....*....|....*....|....*....|
gi 442616378 113 LLQVAPIRNErDLVVLFLLTFR-DITALKQ 141
Cdd:PRK13558 239 QVDIAPIRDE-DGTVTHYVGFQtDVTERKE 267
PRK13559 PRK13559
hypothetical protein; Provisional
 33-137 2.57e-13

hypothetical protein; Provisional


Pssm-ID: 237427 [Multi-domain]  Cd Length: 361  Bit Score: 71.39  E-value: 2.57e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616378  33 LANAQIVDFPIVYCNESFCKISGYNRAEVMQKSCRyvcgFMYGELTDKETVGRLEYTLENQQQDQFEILLYKKNKTPLWL 112
Cdd:PRK13559  58 ITDPHQPDLPIVLANQAFLDLTGYAAEEVVGRNCR----FLQGAATDPIAVAKIRAAIAAEREIVVELLNYRKDGEPFWN 133

                         90       100
                 ....*....|....*....|....*
gi 442616378 113 LLQVAPIRNERDLVVLFLLTFRDIT 137
Cdd:PRK13559 134 ALHLGPVYGEDGRLLYFFGSQWDVT 158
PRK13557 PRK13557
histidine kinase; Provisional
 40-129 9.71e-11

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 64.31  E-value: 9.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616378  40 DFPIVYCNESFCKISGYNRAEVMQKSCRyvcgFMYGELTDKETVGRLEYTLENQQQDQFEILLYKKNKTPLWLLLQVAPI 119
Cdd:PRK13557  52 DNPIVFANRAFLEMTGYAAEEIIGNNCR----FLQGPETDRATVAEVRDAIAERREIATEILNYRKDGSSFWNALFVSPV 127

                         90
                 ....*....|.
gi 442616378 120 RNER-DLVVLF 129
Cdd:PRK13557 128 YNDAgDLVYFF 138
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 43-136 2.83e-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 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: 57.81  E-value: 2.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616378   43 IVYCNESFCKISGYNRAEVMQKScryvcgfMYGEL---TDKETVGRLEYTLENQQQDQ-FEILLYKKNKTPLWLLLQVAP 118
Cdd:pfam00989  23 ILYVNAAAEELLGLSREEVIGKS-------LLDLIpeeDDAEVAELLRQALLQGEESRgFEVSFRVPDGRPRHVEVRASP 95

                          90
                  ....*....|....*...
gi 442616378  119 IRNERDLVVLFLLTFRDI 136
Cdd:pfam00989  96 VRDAGGEILGFLGVLRDI 113
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
43-141 1.71e-09

Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 59.47  E-value: 1.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616378  43 IVYCNESFCKISGYNRAEVMQKSCRYVCGFmygeltDKETVGRLEYTLENQQQ-DQFEILLYKKNKTPLWLLLQVAPIRN 121
Cdd:COG3852   29 ITYVNPAAERLLGLSAEELLGRPLAELFPE------DSPLRELLERALAEGQPvTEREVTLRRKDGEERPVDVSVSPLRD 102

                         90       100
                 ....*....|....*....|
gi 442616378 122 ErDLVVLFLLTFRDITALKQ 141
Cdd:COG3852  103 A-EGEGGVLLVLRDITERKR 121
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 40-136 2.51e-09

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 54.56  E-value: 2.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616378  40 DFPIVYCNESFCKISGYNRAEVMQKSCRYVcgFMYGELTDKETvgRLEYTLENQQQDQFEILLYKKNKTPLWLLLQVAPI 119
Cdd:cd00130   11 DGRILYANPAAEQLLGYSPEELIGKSLLDL--IHPEDREELRE--RLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLTPI 86

                         90
                 ....*....|....*..
gi 442616378 120 RNERDLVVLFLLTFRDI 136
Cdd:cd00130   87 RDEGGEVIGLLGVVRDI 103
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 43-140 2.87e-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: 59.22  E-value: 2.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616378  43 IVYCNESFCKISGYNRAEVMQKSCRYVCGFMYgeltDKETVGRLEYTLENQQQDQFEILLYKKNKTPLWLLLQVAPIRNE 122
Cdd:COG5809   37 ILKVNPAAERIFGYTEDELLGTNILDFLHPDD----EKELREILKLLKEGESRDELEFELRHKNGKRLEFSSKLSPIFDQ 112

                         90
                 ....*....|....*...
gi 442616378 123 RDLVVLFLLTFRDITALK 140
Cdd:COG5809  113 NGDIEGMLAISRDITERK 130
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
 43-141 2.55e-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: 49.60  E-value: 2.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616378   43 IVYCNESFCKISGYNRAEVMQKSCRYvcgFMYGELTDkETVGRLEYTLENQQQDQFEILLYK-KNKTPLWLLLQVAPIRN 121
Cdd:TIGR00229  25 ILYVNPAFEEIFGYSAEELIGRNVLE---LIPEEDRE-EVRERIERRLEGEPEPVSEERRVRrKDGSEIWVEVSVSPIRT 100

                          90       100
                  ....*....|....*....|
gi 442616378  122 ERDlVVLFLLTFRDITALKQ 141
Cdd:TIGR00229 101 NGG-ELGVVGIVRDITERKE 119
Ion_trans_2 pfam07885
Ion channel; This family includes the two membrane helix type ion channels found in bacteria.
 430-484 6.03e-07

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: 47.26  E-value: 6.03e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 442616378  430 YVTALYFTMTCMTSVGFGNVAAETDNEKVFTICMMIIAALLYATIFGHVTTIIQQ 484
Cdd:pfam07885  24 FLDALYFSFVTLTTVGYGDIVPLTDAGRLFTIFYILIGIPLFAIFLAVLGRFLTE 78
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
 97-139 1.89e-06

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: 44.48  E-value: 1.89e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 442616378    97 QFEILLYKKNKTPLWLLLQVAPIRNERDLVVLFLLTFRDITAL 139
Cdd:smart00086   1 TVEYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITER 43
PAS COG2202
PAS domain [Signal transduction mechanisms];
16-141 2.23e-06

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 49.25  E-value: 2.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616378  16 LENIIRRSNSQPDSSFLLANAQIV----DFPIVYCNESFCKISGYNRAEVMQKSCRYVcgfmYGELTDKETVGRLEYTLE 91
Cdd:COG2202  128 AEEALRESEERLRLLVENAPDGIFvldlDGRILYVNPAAEELLGYSPEELLGKSLLDL----LHPEDRERLLELLRRLLE 203

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 442616378  92 NQQQdQFEILLYKKNKTPLWLLLQVAPIRNE-RDLVVLFLLTFRDITALKQ 141
Cdd:COG2202  204 GGRE-SYELELRLKDGDGRWVWVEASAVPLRdGGEVIGVLGIVRDITERKR 253
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 40-141 1.21e-04

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain is associated to signalling systems and works as a signal sensor domain. It recognizes differently substituted aromatic hydrocarbons, oxygen, different dodecanoic acids, autoinducers, 3,5-dimethyl-pyrazin-2-ol and N-alanyl-aminoacetone (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 312075 [Multi-domain]  Cd Length: 110  Bit Score: 41.63  E-value: 1.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616378   40 DFPIVYCNESFCKISGYNRAEVMQKSCRyvcgfmygELTDKETVGRLEYTL-----ENQQQDQFEILLYkkNKTPLWLLL 114
Cdd:pfam08448  14 DGRVRYANAAAAELFGLPPEELLGKTLA--------ELLPPEDAARLERALrraleGEEPIDFLEELLL--NGEERHYEL 83

                          90       100
                  ....*....|....*....|....*..
gi 442616378  115 QVAPIRNERDLVVLFLLTFRDITALKQ 141
Cdd:pfam08448  84 RLTPLRDPDGEVIGVLVISRDITERRR 110
PRK10537 PRK10537
voltage-gated potassium channel protein;
431-478 1.56e-04

voltage-gated potassium channel protein;


Pssm-ID: 236711 [Multi-domain]  Cd Length: 393  Bit Score: 44.24  E-value: 1.56e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 442616378 431 VTALYFTMTCMTSVGFGNVAAETDNEKVFTICMMIIAALLYAT----IFGHV 478
Cdd:PRK10537 170 STAFYFSIVTMSTVGYGDIVPVSESARLFTISVIILGITVFATsisaIFGPV 221
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 43-141 1.60e-04

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 44.38  E-value: 1.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616378  43 IVYCNESFCKISGYNRAEVMQKScryVCGFMYGELTDKETVGRLEYTLENQQQDQFEILLYKKNKTPLWLLLQVAPIRNE 122
Cdd:PRK11359 158 IVQCNRAFTEMFGYCISEASGMQ---PDTLLNIPEFPADNRIRLQQLLWKTARDQDEFLLLTRTGEKIWIKASISPVYDV 234

                         90
                 ....*....|....*....
gi 442616378 123 RDLVVLFLLTFRDITALKQ 141
Cdd:PRK11359 235 LAHLQNLVMTFSDITEERQ 253
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 40-141 3.37e-04

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: 43.42  E-value: 3.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616378  40 DFPIVYCNESFCKISGYNRAEVMQKSCRYVCGFMYGELTDKetvgRLEYTLENQQQDQFEILLYKKNKTPLWLLLQVAPI 119
Cdd:COG5809  160 DGRIIYANPAACKLLGISIEELIGKSILELIHSDDQENVAA----FISQLLKDGGIAQGEVRFWTKDGRWRLLEASGAPI 235

                         90       100
                 ....*....|....*....|..
gi 442616378 120 rNERDLVVLFLLTFRDITALKQ 141
Cdd:COG5809  236 -KKNGEVDGIVIIFRDITERKK 256
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
 12-141 2.45e-03

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: 40.33  E-value: 2.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616378  12 QNTFLENIIRRSnsqpDSSFLLANAqivDFPIVYCNESFCKISGYNRAEVMQKSCRYVcgfmygeLTDKETVGRLEYTLE 91
Cdd:COG5000   88 RRRYLETILENL----PAGVIVLDA---DGRITLANPAAERLLGIPLEELIGKPLEEL-------LPELDLAELLREALE 153

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 442616378  92 NQQQDQFEIllykKNKTPLWLLLQVAPIRNERdlvvlFLLTFRDITALKQ 141
Cdd:COG5000  154 RGWQEEIEL----TRDGRRTLLVRASPLRDDG-----YVIVFDDITELLR 194
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
 43-141 3.43e-03

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: 40.14  E-value: 3.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616378  43 IVYCNESFCKISGYNRAEVMQKSCRYVcgfmYGELTDKETVgrleytlenQQQDQFEILLYKKNKTPLWLLLQVAPIRnE 122
Cdd:COG3829   33 ITYVNRAAERILGLPREEVIGKNVTEL----IPNSPLLEVL---------KTGKPVTGVIQKTGGKGKTVIVTAIPIF-E 98

                         90
                 ....*....|....*....
gi 442616378 123 RDLVVLFLLTFRDITALKQ 141
Cdd:COG3829   99 DGEVIGAVETFRDITELKR 117
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 15-95 6.61e-03

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.


Pssm-ID: 214512  Cd Length: 67  Bit Score: 35.45  E-value: 6.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616378    15 FLENIIrrsNSQPDSSFLLANaqivDFPIVYCNESFCKISGYNRAEVMQKScryvcgfmYGELTDKETVGRLEYTLENQQ 94
Cdd:smart00091   2 RLRAIL---ESLPDGIFVLDL----DGRILYANPAAEELLGYSPEELIGKS--------LLELIHPEDRERVQEALQRLL 66


                   .
gi 442616378    95 Q 95
Cdd:smart00091  67 S 67
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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