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Conserved domains on  [gi|13929046|ref|NP_113930|]
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potassium voltage-gated channel subfamily H member 1 [Rattus norvegicus]

Protein Classification

PAS and CAP_ED domain-containing protein( domain architecture ID 13822798)

protein containing domains PAS, CAP_ED, and PRK11753

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN03192 super family cl33658
Voltage-dependent potassium channel; Provisional
 220-620 3.29e-37

Voltage-dependent potassium channel; Provisional


The actual alignment was detected with superfamily member PLN03192:

Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 150.79  E-value: 3.29e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929046  220 WDWIILILTFYTAILVPYNVSFKTRQNNVAWLVVDSIVDVIFLVDIVLNFHTTFVGPAGEV-ISDPKLIRMNYLKTWFVI 298
Cdd:PLN03192  64 WETLMVVLVAYSAWVYPFEVAFLNASPKRGLEIADNVVDLFFAVDIVLTFFVAYIDPRTQLlVRDRKKIAVRYLSTWFLM 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929046  299 DLLSCLPYDVINAFENVDEGISSLFSSLKVVRLLRLGRVAR---KLDHYIEYGAAVL--VLLVCVFGLAAHWMACIWYSI 373
Cdd:PLN03192 144 DVASTIPFQALAYLITGTVKLNLSYSLLGLLRFWRLRRVKQlftRLEKDIRFSYFWIrcARLLSVTLFLVHCAGCLYYLI 223

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929046  374 GDYEIFDEDT---KTIRNnswLYQLALDIGtpyqfngsgsgkweggpsknsvYISSLYFTMTSLTSVGFGNIAPSTDIEK 450
Cdd:PLN03192 224 ADRYPHQGKTwigAVIPN---FRETSLWIR----------------------YISAIYWSITTMTTVGYGDLHAVNTIEM 278

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929046  451 IFAVAIMMIGSLLYATIFGNVTTIFQQmyaNTNRYHEMLNSVR---DFLKLYQVPKGLSERVMDYIVSTWSmSRGIDTEK 527
Cdd:PLN03192 279 IFIIFYMLFNLGLTAYLIGNMTNLVVE---GTRRTMEFRNSIEaasNFVGRNRLPPRLKDQILAYMCLRFK-AESLNQQQ 354

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929046  528 VLQICPKDMRADICVHLNRKVFKEHPAFRLASDGCLRALAMEFQTVHCAPGDLIYHAGESVDSLCFVVSGSLEVI----Q 603
Cdd:PLN03192 355 LIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEIIdsegE 434

                        410
                 ....*....|....*..
gi 13929046  604 DDEVVAILGKGDVFGDV 620
Cdd:PLN03192 435 KERVVGTLGCGDIFGEV 451
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
 41-135 2.13e-16

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://0-doi-org.brum.beds.ac.uk/10.1093/femsre/fuab043).


:

Pssm-ID: 463873 [Multi-domain]  Cd Length: 93  Bit Score: 75.19  E-value: 2.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929046    41 PIVYSNDGFCKLSGYHRAEVMQKSsaCSFMYGeltDKDTVEKVRQTFENYEMN-SFEILMYKKNRTPVWFFVKIAPIRNE 119
Cdd:pfam13426   3 RIIYVNDAALRLLGYTREELLGKS--ITDLFA---EPEDSERLREALREGKAVrEFEVVLYRKDGEPFPVLVSLAPIRDD 77

                          90
                  ....*....|....*.
gi 13929046   120 QDKVVLFLCTFSDITA 135
Cdd:pfam13426  78 GGELVGIIAILRDITE 93
PRK11753 super family cl36052
cAMP-activated global transcriptional regulator CRP;
581-685 8.78e-07

cAMP-activated global transcriptional regulator CRP;


The actual alignment was detected with superfamily member PRK11753:

Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 50.75  E-value: 8.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929046  581 IYHAGESVDSLCFVVSGSLEVIQDDE-----VVAILGKGDVFGDVFWKEATLAQScANVRALTYCDLHVIKRDALQKVLE 655
Cdd:PRK11753  31 LIHAGEKAETLYYIVKGSVAVLIKDEegkemILSYLNQGDFIGELGLFEEGQERS-AWVRAKTACEVAEISYKKFRQLIQ 109

                         90       100       110
                 ....*....|....*....|....*....|
gi 13929046  656 FYTAFSHSFSRNLIltynLRKRIVFRKISD 685
Cdd:PRK11753 110 VNPDILMALSAQMA----RRLQNTSRKVGD 135
 
Name Accession Description Interval E-value
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 220-620 3.29e-37

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 150.79  E-value: 3.29e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929046  220 WDWIILILTFYTAILVPYNVSFKTRQNNVAWLVVDSIVDVIFLVDIVLNFHTTFVGPAGEV-ISDPKLIRMNYLKTWFVI 298
Cdd:PLN03192  64 WETLMVVLVAYSAWVYPFEVAFLNASPKRGLEIADNVVDLFFAVDIVLTFFVAYIDPRTQLlVRDRKKIAVRYLSTWFLM 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929046  299 DLLSCLPYDVINAFENVDEGISSLFSSLKVVRLLRLGRVAR---KLDHYIEYGAAVL--VLLVCVFGLAAHWMACIWYSI 373
Cdd:PLN03192 144 DVASTIPFQALAYLITGTVKLNLSYSLLGLLRFWRLRRVKQlftRLEKDIRFSYFWIrcARLLSVTLFLVHCAGCLYYLI 223

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929046  374 GDYEIFDEDT---KTIRNnswLYQLALDIGtpyqfngsgsgkweggpsknsvYISSLYFTMTSLTSVGFGNIAPSTDIEK 450
Cdd:PLN03192 224 ADRYPHQGKTwigAVIPN---FRETSLWIR----------------------YISAIYWSITTMTTVGYGDLHAVNTIEM 278

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929046  451 IFAVAIMMIGSLLYATIFGNVTTIFQQmyaNTNRYHEMLNSVR---DFLKLYQVPKGLSERVMDYIVSTWSmSRGIDTEK 527
Cdd:PLN03192 279 IFIIFYMLFNLGLTAYLIGNMTNLVVE---GTRRTMEFRNSIEaasNFVGRNRLPPRLKDQILAYMCLRFK-AESLNQQQ 354

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929046  528 VLQICPKDMRADICVHLNRKVFKEHPAFRLASDGCLRALAMEFQTVHCAPGDLIYHAGESVDSLCFVVSGSLEVI----Q 603
Cdd:PLN03192 355 LIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEIIdsegE 434

                        410
                 ....*....|....*..
gi 13929046  604 DDEVVAILGKGDVFGDV 620
Cdd:PLN03192 435 KERVVGTLGCGDIFGEV 451
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 220-483 1.18e-33

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: 129.69  E-value: 1.18e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929046   220 WDWIILILTFYTAILVPYNVSFKTRQ-NNVAWLVVDSIVDVIFLVDIVLNFHTTFvgpagevisdpklIRMNYLKT-WFV 297
Cdd:pfam00520   4 FELFILLLILLNTIFLALETYFQPEEpLTTVLEILDYVFTGIFTLEMLLKIIAAG-------------FKKRYFRSpWNI 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929046   298 IDLLSCLPYDVInaFENVDEGISSLFSSLKVVRLLRLGRVARKLDHYIEYGAAVL--VLLVCVFGLAAHWMACIWYSIGd 375
Cdd:pfam00520  71 LDFVVVLPSLIS--LVLSSVGSLSGLRVLRLLRLLRLLRLIRRLEGLRTLVNSLIrsLKSLGNLLLLLLLFLFIFAIIG- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929046   376 yeifdedtktirnnswlyqlaldigtpYQFNGSGSGKWEGGPSKNSV---YISSLYFTMTSLTSVGFGNIAPSTDIEK-- 450
Cdd:pfam00520 148 ---------------------------YQLFGGKLKTWENPDNGRTNfdnFPNAFLWLFQTMTTEGWGDIMYDTIDGKge 200

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 13929046   451 -----IFAVAIMMIGSLLYATIFGNVTTIFQQMYANTN 483
Cdd:pfam00520 201 fwayiYFVSFIILGGFLLLNLFIAVIIDNFQELTERTE 238
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 554-664 2.19e-24

effector domain of the CAP family of transcription factors; members include CAP (or cAMP receptor protein (CRP)), which binds cAMP, FNR (fumarate and nitrate reduction), which uses an iron-sulfur cluster to sense oxygen) and CooA, a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. Cyclic nucleotide-binding domain similar to CAP are also present in cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) and vertebrate cyclic nucleotide-gated ion-channels. Cyclic nucleotide-monophosphate binding domain; proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural domain of about 120 residues; the best studied is the prokaryotic catabolite gene activator, CAP, where such a domain is known to be composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure; three conserved glycine residues are thought to be essential for maintenance of the structural integrity of the beta-barrel; CooA is a homodimeric transcription factor that belongs to CAP family; cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) contain two tandem copies of the cyclic nucleotide-binding domain; cAPK's are composed of two different subunits, a catalytic chain and a regulatory chain, which contains both copies of the domain; cGPK's are single chain enzymes that include the two copies of the domain in their N-terminal section; also found in vertebrate cyclic nucleotide-gated ion-channels


Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 98.94  E-value: 2.19e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929046 554 AFRLASDGCLRALAMEFQTVHCAPGDLIYHAGESVDSLCFVVSGSLEVIQDDE-----VVAILGKGDVFGDVFWkeATLA 628
Cdd:cd00038   1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEdgreqIVGFLGPGDLFGELAL--LGNG 78

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 13929046 629 QSCANVRALTYCDLHVIKRDALQKVLEFYTAFSHSF 664
Cdd:cd00038  79 PRSATVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 555-671 1.16e-19

Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a prokaryotic homologue of eukaryotic cNMP-binding domains, present in ion channels, and cNMP-dependent kinases.


Pssm-ID: 197516 [Multi-domain]  Cd Length: 120  Bit Score: 85.53  E-value: 1.16e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929046    555 FRLASDGCLRALAMEFQTVHCAPGDLIYHAGESVDSLCFVVSGSLEVIQDDE-----VVAILGKGDVFGDvfwkEATLAQ 629
Cdd:smart00100   2 FKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEdgeeqIVGTLGPGDFFGE----LALLTN 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 13929046    630 --SCANVRALTYCdLHVIKRDALQKVLEFYTAFSHSFSRNLILT 671
Cdd:smart00100  78 srRAASAAAVALE-LATLLRIDFRDFLQLLPELPQLLLELLLEL 120
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
 41-135 2.13e-16

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://0-doi-org.brum.beds.ac.uk/10.1093/femsre/fuab043).


Pssm-ID: 463873 [Multi-domain]  Cd Length: 93  Bit Score: 75.19  E-value: 2.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929046    41 PIVYSNDGFCKLSGYHRAEVMQKSsaCSFMYGeltDKDTVEKVRQTFENYEMN-SFEILMYKKNRTPVWFFVKIAPIRNE 119
Cdd:pfam13426   3 RIIYVNDAALRLLGYTREELLGKS--ITDLFA---EPEDSERLREALREGKAVrEFEVVLYRKDGEPFPVLVSLAPIRDD 77

                          90
                  ....*....|....*.
gi 13929046   120 QDKVVLFLCTFSDITA 135
Cdd:pfam13426  78 GGELVGIIAILRDITE 93
PAS COG2202
PAS domain [Signal transduction mechanisms];
39-138 7.51e-16

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 78.53  E-value: 7.51e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929046  39 DWPIVYSNDGFCKLSGYHRAEVMQKSsaCSFMYGELTDKDTVEKVRQTFENYEMNSFEILMYKKNRTPVWFFVKIAPIRN 118
Cdd:COG2202  30 DGRILYVNPAFERLTGYSAEELLGKT--LRDLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGSLFWVELSISPVRD 107

                        90       100
                ....*....|....*....|
gi 13929046 119 EQDKVVLFLCTFSDITAFKQ 138
Cdd:COG2202 108 EDGEITGFVGIARDITERKR 127
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 555-668 8.86e-15

cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal transduction mechanisms];


Pssm-ID: 440428 [Multi-domain]  Cd Length: 207  Bit Score: 74.25  E-value: 8.86e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929046 555 FRLASDGCLRALAMEFQTVHCAPGDLIYHAGESVDSLCFVVSGSLEVIQDDE-----VVAILGKGDVFGDVFWKEATLAQ 629
Cdd:COG0664   1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEdgreqILGFLGPGDFFGELSLLGGEPSP 80

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 13929046 630 scANVRALTYCDLHVIKRDALQKVLEFYTAFSHSFSRNL 668
Cdd:COG0664  81 --ATAEALEDSELLRIPREDLEELLERNPELARALLRLL 117
PRK13558 PRK13558
bacterio-opsin activator; Provisional
 39-138 1.34e-13

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 74.87  E-value: 1.34e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929046   39 DWPIVYSNDGFCKLSGYHRAEVMQKSsaCSFMYGELTDKDTVEKVRQTFENYEMNSFEILMYKKNRTPVWFFVKIAPIRN 118
Cdd:PRK13558 170 DEPLIYINDAFERITGYSPDEVLGRN--CRFLQGEDTNEERVAELREAIDEERPTSVELRNYRKDGSTFWNQVDIAPIRD 247

                         90       100
                 ....*....|....*....|
gi 13929046  119 EQDKVVLFLCTFSDITAFKQ 138
Cdd:PRK13558 248 EDGTVTHYVGFQTDVTERKE 267
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 39-133 1.02e-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: 56.49  E-value: 1.02e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929046  39 DWPIVYSNDGFCKLSGYHRAEVMQKSsacsfmYGELTDKDTVEKVRQTFENY----EMNSFEILMYKKNRTPVWFFVKIA 114
Cdd:cd00130  11 DGRILYANPAAEQLLGYSPEELIGKS------LLDLIHPEDREELRERLENLlsggEPVTLEVRLRRKDGSVIWVLVSLT 84

                        90
                ....*....|....*....
gi 13929046 115 PIRNEQDKVVLFLCTFSDI 133
Cdd:cd00130  85 PIRDEGGEVIGLLGVVRDI 103
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
 94-135 3.04e-07

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: 47.56  E-value: 3.04e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 13929046     94 SFEILMYKKNRTPVWFFVKIAPIRNEQDKVVLFLCTFSDITA 135
Cdd:smart00086   1 TVEYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITE 42
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
581-685 8.78e-07

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 50.75  E-value: 8.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929046  581 IYHAGESVDSLCFVVSGSLEVIQDDE-----VVAILGKGDVFGDVFWKEATLAQScANVRALTYCDLHVIKRDALQKVLE 655
Cdd:PRK11753  31 LIHAGEKAETLYYIVKGSVAVLIKDEegkemILSYLNQGDFIGELGLFEEGQERS-AWVRAKTACEVAEISYKKFRQLIQ 109

                         90       100       110
                 ....*....|....*....|....*....|
gi 13929046  656 FYTAFSHSFSRNLIltynLRKRIVFRKISD 685
Cdd:PRK11753 110 VNPDILMALSAQMA----RRLQNTSRKVGD 135
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
 16-138 2.00e-05

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: 44.97  E-value: 2.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929046    16 TFLENIVRRSNDTNFVLG-NAQIVDWpivysNDGFCKLSGYHRAEVMQKSSAcsfmygELTDKDTVEKVRQTFENYEM-- 92
Cdd:TIGR00229   3 ERYRAIFESSPDAIIVIDlEGNILYV-----NPAFEEIFGYSAEELIGRNVL------ELIPEEDREEVRERIERRLEge 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 13929046    93 ---NSFEILMYKKNRTPVWFFVKIAPIRnEQDKVVLFLCTFSDITAFKQ 138
Cdd:TIGR00229  72 pepVSEERRVRRKDGSEIWVEVSVSPIR-TNGGELGVVGIVRDITERKE 119
 
Name Accession Description Interval E-value
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 220-620 3.29e-37

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 150.79  E-value: 3.29e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929046  220 WDWIILILTFYTAILVPYNVSFKTRQNNVAWLVVDSIVDVIFLVDIVLNFHTTFVGPAGEV-ISDPKLIRMNYLKTWFVI 298
Cdd:PLN03192  64 WETLMVVLVAYSAWVYPFEVAFLNASPKRGLEIADNVVDLFFAVDIVLTFFVAYIDPRTQLlVRDRKKIAVRYLSTWFLM 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929046  299 DLLSCLPYDVINAFENVDEGISSLFSSLKVVRLLRLGRVAR---KLDHYIEYGAAVL--VLLVCVFGLAAHWMACIWYSI 373
Cdd:PLN03192 144 DVASTIPFQALAYLITGTVKLNLSYSLLGLLRFWRLRRVKQlftRLEKDIRFSYFWIrcARLLSVTLFLVHCAGCLYYLI 223

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929046  374 GDYEIFDEDT---KTIRNnswLYQLALDIGtpyqfngsgsgkweggpsknsvYISSLYFTMTSLTSVGFGNIAPSTDIEK 450
Cdd:PLN03192 224 ADRYPHQGKTwigAVIPN---FRETSLWIR----------------------YISAIYWSITTMTTVGYGDLHAVNTIEM 278

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929046  451 IFAVAIMMIGSLLYATIFGNVTTIFQQmyaNTNRYHEMLNSVR---DFLKLYQVPKGLSERVMDYIVSTWSmSRGIDTEK 527
Cdd:PLN03192 279 IFIIFYMLFNLGLTAYLIGNMTNLVVE---GTRRTMEFRNSIEaasNFVGRNRLPPRLKDQILAYMCLRFK-AESLNQQQ 354

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929046  528 VLQICPKDMRADICVHLNRKVFKEHPAFRLASDGCLRALAMEFQTVHCAPGDLIYHAGESVDSLCFVVSGSLEVI----Q 603
Cdd:PLN03192 355 LIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEIIdsegE 434

                        410
                 ....*....|....*..
gi 13929046  604 DDEVVAILGKGDVFGDV 620
Cdd:PLN03192 435 KERVVGTLGCGDIFGEV 451
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 220-483 1.18e-33

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: 129.69  E-value: 1.18e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929046   220 WDWIILILTFYTAILVPYNVSFKTRQ-NNVAWLVVDSIVDVIFLVDIVLNFHTTFvgpagevisdpklIRMNYLKT-WFV 297
Cdd:pfam00520   4 FELFILLLILLNTIFLALETYFQPEEpLTTVLEILDYVFTGIFTLEMLLKIIAAG-------------FKKRYFRSpWNI 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929046   298 IDLLSCLPYDVInaFENVDEGISSLFSSLKVVRLLRLGRVARKLDHYIEYGAAVL--VLLVCVFGLAAHWMACIWYSIGd 375
Cdd:pfam00520  71 LDFVVVLPSLIS--LVLSSVGSLSGLRVLRLLRLLRLLRLIRRLEGLRTLVNSLIrsLKSLGNLLLLLLLFLFIFAIIG- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929046   376 yeifdedtktirnnswlyqlaldigtpYQFNGSGSGKWEGGPSKNSV---YISSLYFTMTSLTSVGFGNIAPSTDIEK-- 450
Cdd:pfam00520 148 ---------------------------YQLFGGKLKTWENPDNGRTNfdnFPNAFLWLFQTMTTEGWGDIMYDTIDGKge 200

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 13929046   451 -----IFAVAIMMIGSLLYATIFGNVTTIFQQMYANTN 483
Cdd:pfam00520 201 fwayiYFVSFIILGGFLLLNLFIAVIIDNFQELTERTE 238
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 554-664 2.19e-24

effector domain of the CAP family of transcription factors; members include CAP (or cAMP receptor protein (CRP)), which binds cAMP, FNR (fumarate and nitrate reduction), which uses an iron-sulfur cluster to sense oxygen) and CooA, a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. Cyclic nucleotide-binding domain similar to CAP are also present in cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) and vertebrate cyclic nucleotide-gated ion-channels. Cyclic nucleotide-monophosphate binding domain; proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural domain of about 120 residues; the best studied is the prokaryotic catabolite gene activator, CAP, where such a domain is known to be composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure; three conserved glycine residues are thought to be essential for maintenance of the structural integrity of the beta-barrel; CooA is a homodimeric transcription factor that belongs to CAP family; cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) contain two tandem copies of the cyclic nucleotide-binding domain; cAPK's are composed of two different subunits, a catalytic chain and a regulatory chain, which contains both copies of the domain; cGPK's are single chain enzymes that include the two copies of the domain in their N-terminal section; also found in vertebrate cyclic nucleotide-gated ion-channels


Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 98.94  E-value: 2.19e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929046 554 AFRLASDGCLRALAMEFQTVHCAPGDLIYHAGESVDSLCFVVSGSLEVIQDDE-----VVAILGKGDVFGDVFWkeATLA 628
Cdd:cd00038   1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEdgreqIVGFLGPGDLFGELAL--LGNG 78

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 13929046 629 QSCANVRALTYCDLHVIKRDALQKVLEFYTAFSHSF 664
Cdd:cd00038  79 PRSATVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 555-671 1.16e-19

Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a prokaryotic homologue of eukaryotic cNMP-binding domains, present in ion channels, and cNMP-dependent kinases.


Pssm-ID: 197516 [Multi-domain]  Cd Length: 120  Bit Score: 85.53  E-value: 1.16e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929046    555 FRLASDGCLRALAMEFQTVHCAPGDLIYHAGESVDSLCFVVSGSLEVIQDDE-----VVAILGKGDVFGDvfwkEATLAQ 629
Cdd:smart00100   2 FKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEdgeeqIVGTLGPGDFFGE----LALLTN 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 13929046    630 --SCANVRALTYCdLHVIKRDALQKVLEFYTAFSHSFSRNLILT 671
Cdd:smart00100  78 srRAASAAAVALE-LATLLRIDFRDFLQLLPELPQLLLELLLEL 120
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
 41-135 2.13e-16

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://0-doi-org.brum.beds.ac.uk/10.1093/femsre/fuab043).


Pssm-ID: 463873 [Multi-domain]  Cd Length: 93  Bit Score: 75.19  E-value: 2.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929046    41 PIVYSNDGFCKLSGYHRAEVMQKSsaCSFMYGeltDKDTVEKVRQTFENYEMN-SFEILMYKKNRTPVWFFVKIAPIRNE 119
Cdd:pfam13426   3 RIIYVNDAALRLLGYTREELLGKS--ITDLFA---EPEDSERLREALREGKAVrEFEVVLYRKDGEPFPVLVSLAPIRDD 77

                          90
                  ....*....|....*.
gi 13929046   120 QDKVVLFLCTFSDITA 135
Cdd:pfam13426  78 GGELVGIIAILRDITE 93
PAS COG2202
PAS domain [Signal transduction mechanisms];
39-138 7.51e-16

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 78.53  E-value: 7.51e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929046  39 DWPIVYSNDGFCKLSGYHRAEVMQKSsaCSFMYGELTDKDTVEKVRQTFENYEMNSFEILMYKKNRTPVWFFVKIAPIRN 118
Cdd:COG2202  30 DGRILYVNPAFERLTGYSAEELLGKT--LRDLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGSLFWVELSISPVRD 107

                        90       100
                ....*....|....*....|
gi 13929046 119 EQDKVVLFLCTFSDITAFKQ 138
Cdd:COG2202 108 EDGEITGFVGIARDITERKR 127
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 555-668 8.86e-15

cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal transduction mechanisms];


Pssm-ID: 440428 [Multi-domain]  Cd Length: 207  Bit Score: 74.25  E-value: 8.86e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929046 555 FRLASDGCLRALAMEFQTVHCAPGDLIYHAGESVDSLCFVVSGSLEVIQDDE-----VVAILGKGDVFGDVFWKEATLAQ 629
Cdd:COG0664   1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEdgreqILGFLGPGDFFGELSLLGGEPSP 80

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 13929046 630 scANVRALTYCDLHVIKRDALQKVLEFYTAFSHSFSRNL 668
Cdd:COG0664  81 --ATAEALEDSELLRIPREDLEELLERNPELARALLRLL 117
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 573-655 7.59e-14

Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, oxygen and 2-oxoglutarate (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://0-doi-org.brum.beds.ac.uk/10.1093/femsre/fuab043).


Pssm-ID: 459637 [Multi-domain]  Cd Length: 89  Bit Score: 67.63  E-value: 7.59e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929046   573 VHCAPGDLIYHAGESVDSLCFVVSGSLEVIQDDE-----VVAILGKGDVFGDVfwkeATLAQSC--ANVRALTYCDLHVI 645
Cdd:pfam00027   2 RSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEdgreqILAVLGPGDFFGEL----ALLGGEPrsATVVALTDSELLVI 77

                          90
                  ....*....|
gi 13929046   646 KRDALQKVLE 655
Cdd:pfam00027  78 PREDFLELLE 87
PRK13558 PRK13558
bacterio-opsin activator; Provisional
 39-138 1.34e-13

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 74.87  E-value: 1.34e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929046   39 DWPIVYSNDGFCKLSGYHRAEVMQKSsaCSFMYGELTDKDTVEKVRQTFENYEMNSFEILMYKKNRTPVWFFVKIAPIRN 118
Cdd:PRK13558 170 DEPLIYINDAFERITGYSPDEVLGRN--CRFLQGEDTNEERVAELREAIDEERPTSVELRNYRKDGSTFWNQVDIAPIRD 247

                         90       100
                 ....*....|....*....|
gi 13929046  119 EQDKVVLFLCTFSDITAFKQ 138
Cdd:PRK13558 248 EDGTVTHYVGFQTDVTERKE 267
Ion_trans_2 pfam07885
Ion channel; This family includes the two membrane helix type ion channels found in bacteria.
 423-477 4.60e-12

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: 62.28  E-value: 4.60e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 13929046   423 YISSLYFTMTSLTSVGFGNIAPSTDIEKIFAVAIMMIGSLLYATIFGNVTTIFQQ 477
Cdd:pfam07885  24 FLDALYFSFVTLTTVGYGDIVPLTDAGRLFTIFYILIGIPLFAIFLAVLGRFLTE 78
PRK13559 PRK13559
hypothetical protein; Provisional
 31-137 6.16e-11

hypothetical protein; Provisional


Pssm-ID: 237427 [Multi-domain]  Cd Length: 361  Bit Score: 65.23  E-value: 6.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929046   31 VLGNAQIVDWPIVYSNDGFCKLSGYHRAEVMQKSsaCSFMYGELTDKDTVEKVRQTFENYEMNSFEILMYKKNRTPVWFF 110
Cdd:PRK13559  57 CITDPHQPDLPIVLANQAFLDLTGYAAEEVVGRN--CRFLQGAATDPIAVAKIRAAIAAEREIVVELLNYRKDGEPFWNA 134

                         90       100
                 ....*....|....*....|....*..
gi 13929046  111 VKIAPIRNEQDKVVLFLCTFSDITAFK 137
Cdd:PRK13559 135 LHLGPVYGEDGRLLYFFGSQWDVTDIR 161
PRK13557 PRK13557
histidine kinase; Provisional
 39-134 1.37e-10

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 65.08  E-value: 1.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929046   39 DWPIVYSNDGFCKLSGYHRAEVMqkSSACSFMYGELTDKDTVEKVRQTFENYEMNSFEILMYKKNRTPVWFFVKIAPIRN 118
Cdd:PRK13557  52 DNPIVFANRAFLEMTGYAAEEII--GNNCRFLQGPETDRATVAEVRDAIAERREIATEILNYRKDGSSFWNALFVSPVYN 129

                         90
                 ....*....|....*.
gi 13929046  119 EQDKVVLFLCTFSDIT 134
Cdd:PRK13557 130 DAGDLVYFFGSQLDVS 145
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 39-133 1.02e-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: 56.49  E-value: 1.02e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929046  39 DWPIVYSNDGFCKLSGYHRAEVMQKSsacsfmYGELTDKDTVEKVRQTFENY----EMNSFEILMYKKNRTPVWFFVKIA 114
Cdd:cd00130  11 DGRILYANPAAEQLLGYSPEELIGKS------LLDLIHPEDREELRERLENLlsggEPVTLEVRLRRKDGSVIWVLVSLT 84

                        90
                ....*....|....*....
gi 13929046 115 PIRNEQDKVVLFLCTFSDI 133
Cdd:cd00130  85 PIRDEGGEVIGLLGVVRDI 103
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
 94-135 3.04e-07

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: 47.56  E-value: 3.04e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 13929046     94 SFEILMYKKNRTPVWFFVKIAPIRNEQDKVVLFLCTFSDITA 135
Cdd:smart00086   1 TVEYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITE 42
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
581-685 8.78e-07

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 50.75  E-value: 8.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929046  581 IYHAGESVDSLCFVVSGSLEVIQDDE-----VVAILGKGDVFGDVFWKEATLAQScANVRALTYCDLHVIKRDALQKVLE 655
Cdd:PRK11753  31 LIHAGEKAETLYYIVKGSVAVLIKDEegkemILSYLNQGDFIGELGLFEEGQERS-AWVRAKTACEVAEISYKKFRQLIQ 109

                         90       100       110
                 ....*....|....*....|....*....|
gi 13929046  656 FYTAFSHSFSRNLIltynLRKRIVFRKISD 685
Cdd:PRK11753 110 VNPDILMALSAQMA----RRLQNTSRKVGD 135
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 42-133 5.74e-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://0-doi-org.brum.beds.ac.uk/10.1093/femsre/fuab043).


Pssm-ID: 395786 [Multi-domain]  Cd Length: 113  Bit Score: 46.26  E-value: 5.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929046    42 IVYSNDGFCKLSGYHRAEVMQKSsacsfMYGEL---TDKDTVEKVRQTFENYEMN-SFEILMYKKNRTPVWFFVKIAPIR 117
Cdd:pfam00989  23 ILYVNAAAEELLGLSREEVIGKS-----LLDLIpeeDDAEVAELLRQALLQGEESrGFEVSFRVPDGRPRHVEVRASPVR 97

                          90
                  ....*....|....*.
gi 13929046   118 NEQDKVVLFLCTFSDI 133
Cdd:pfam00989  98 DAGGEILGFLGVLRDI 113
PAS COG2202
PAS domain [Signal transduction mechanisms];
14-138 1.05e-05

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 48.10  E-value: 1.05e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929046  14 QNTFLENIVRRSNDTNFVLGNAQIvdwpIVYSNDGFCKLSGYHRAEVMQKSSAcsfmygELTDKDTVEKVRQTFENY--- 90
Cdd:COG2202 135 SEERLRLLVENAPDGIFVLDLDGR----ILYVNPAAEELLGYSPEELLGKSLL------DLLHPEDRERLLELLRRLleg 204

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 13929046  91 EMNSFEILMYKKNRTPVWFFVKIAPIRNE-QDKVVLFLCTFSDITAFKQ 138
Cdd:COG2202 205 GRESYELELRLKDGDGRWVWVEASAVPLRdGGEVIGVLGIVRDITERKR 253
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
 16-138 2.00e-05

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: 44.97  E-value: 2.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929046    16 TFLENIVRRSNDTNFVLG-NAQIVDWpivysNDGFCKLSGYHRAEVMQKSSAcsfmygELTDKDTVEKVRQTFENYEM-- 92
Cdd:TIGR00229   3 ERYRAIFESSPDAIIVIDlEGNILYV-----NPAFEEIFGYSAEELIGRNVL------ELIPEEDREEVRERIERRLEge 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 13929046    93 ---NSFEILMYKKNRTPVWFFVKIAPIRnEQDKVVLFLCTFSDITAFKQ 138
Cdd:TIGR00229  72 pepVSEERRVRRKDGSEIWVEVSVSPIR-TNGGELGVVGIVRDITERKE 119
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
42-138 7.78e-05

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 45.99  E-value: 7.78e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929046  42 IVYSNDGFCKLSGYHRAEVMQKSsACSFMYGELTDKDTVEKVRQtfENYEMNSFEILMYKKNRTPVWFFVKIAPIRNEQD 121
Cdd:COG3852  29 ITYVNPAAERLLGLSAEELLGRP-LAELFPEDSPLRELLERALA--EGQPVTEREVTLRRKDGEERPVDVSVSPLRDAEG 105

                        90
                ....*....|....*..
gi 13929046 122 KvVLFLCTFSDITAFKQ 138
Cdd:COG3852 106 E-GGVLLVLRDITERKR 121
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 42-129 1.70e-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.


Pssm-ID: 430001 [Multi-domain]  Cd Length: 89  Bit Score: 41.17  E-value: 1.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929046    42 IVYSNDGFCKLSGYHRAEVMQKSSAC-SFMYGEltdkDtVEKVRQTFENYEMN----SFEILMYKKNRTPVWFFVKIAPI 116
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELLGKGESWlDLVHPD----D-RERVREALWEALKGgepySGEYRIRRKDGEYRWVEARARPI 75

                          90
                  ....*....|...
gi 13929046   117 RNEQDKVVLFLCT 129
Cdd:pfam08447  76 RDENGKPVRVIGV 88
PRK10537 PRK10537
voltage-gated potassium channel protein;
427-471 2.01e-03

voltage-gated potassium channel protein;


Pssm-ID: 236711 [Multi-domain]  Cd Length: 393  Bit Score: 41.55  E-value: 2.01e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 13929046  427 LYFTMTSLTSVGFGNIAPSTDIEKIFAVAIMMIGSLLYAT----IFGNV 471
Cdd:PRK10537 173 FYFSIVTMSTVGYGDIVPVSESARLFTISVIILGITVFATsisaIFGPV 221
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 42-138 5.47e-03

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 40.52  E-value: 5.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929046   42 IVYSNDGFCKLSGYHRAEVMQKSSAcSFMYGELTDKDTVEKVRQTFENYEMNSFEILMYKKNRTPVWFFVKIAPIRNEQD 121
Cdd:PRK11359 158 IVQCNRAFTEMFGYCISEASGMQPD-TLLNIPEFPADNRIRLQQLLWKTARDQDEFLLLTRTGEKIWIKASISPVYDVLA 236

                         90
                 ....*....|....*..
gi 13929046  122 KVVLFLCTFSDITAFKQ 138
Cdd:PRK11359 237 HLQNLVMTFSDITEERQ 253
 
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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