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Conserved domains on  [gi|1046856974|ref|XP_017454422|]
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potassium voltage-gated channel subfamily H member 1 isoform X1 [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
 220-647 2.00e-34

Voltage-dependent potassium channel; Provisional


The actual alignment was detected with superfamily member PLN03192:

Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 142.31  E-value: 2.00e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046856974 220 WDWIILILTFYTAILVPYNVSFKTRQNNVAWLVVDSIVDVIFLVDIVLNFHTTFVGPAGEV-ISDPKLIRMNYLKTWFVI 298
Cdd:PLN03192   64 WETLMVVLVAYSAWVYPFEVAFLNASPKRGLEIADNVVDLFFAVDIVLTFFVAYIDPRTQLlVRDRKKIAVRYLSTWFLM 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046856974 299 DLLSCLPYDVINAFenvdevsafmgdpgkigfadqipppLEGRESQGISslFSSLKVVRLLRLGRVAR---KLDHYIEYG 375
Cdd:PLN03192  144 DVASTIPFQALAYL-------------------------ITGTVKLNLS--YSLLGLLRFWRLRRVKQlftRLEKDIRFS 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046856974 376 AAVL--VLLVCVFGLAAHWMACIWYSIGDYEIFDEDT---KTIRNnswLYQLALDIGtpyqfngsgsgkweggpsknsvY 450
Cdd:PLN03192  197 YFWIrcARLLSVTLFLVHCAGCLYYLIADRYPHQGKTwigAVIPN---FRETSLWIR----------------------Y 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046856974 451 ISSLYFTMTSLTSVGFGNIAPSTDIEKIFAVAIMMIGSLLYATIFGNVTTIFQQmyaNTNRYHEMLNSVR---DFLKLYQ 527
Cdd:PLN03192  252 ISAIYWSITTMTTVGYGDLHAVNTIEMIFIIFYMLFNLGLTAYLIGNMTNLVVE---GTRRTMEFRNSIEaasNFVGRNR 328

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046856974 528 VPKGLSERVMDYIVSTWSmSRGIDTEKVLQICPKDMRADICVHLNRKVFKEHPAFRLASDGCLRALAMEFQTVHCAPGDL 607
Cdd:PLN03192  329 LPPRLKDQILAYMCLRFK-AESLNQQQLIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPRED 407

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 1046856974 608 IYHAGESVDSLCFVVSGSLEVI----QDDEVVAILGKGDVFGDV 647
Cdd:PLN03192  408 VIMQNEAPDDVYIVVSGEVEIIdsegEKERVVGTLGCGDIFGEV 451
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
 41-135 2.05e-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: 2.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046856974  41 PIVYSNDGFCKLSGYHRAEVMQKSsaCSFMYGeltDKDTVEKVRQTFENYEMN-SFEILMYKKNRTPVWFFVKIAPIRNE 119
Cdd:pfam13426   3 RIIYVNDAALRLLGYTREELLGKS--ITDLFA---EPEDSERLREALREGKAVrEFEVVLYRKDGEPFPVLVSLAPIRDD 77

                          90
                  ....*....|....*.
gi 1046856974 120 QDKVVLFLCTFSDITA 135
Cdd:pfam13426  78 GGELVGIIAILRDITE 93
PRK11753 super family cl36052
cAMP-activated global transcriptional regulator CRP;
608-712 9.06e-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: 9.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046856974 608 IYHAGESVDSLCFVVSGSLEVIQDDE-----VVAILGKGDVFGDVFWKEATLAQScANVRALTYCDLHVIKRDALQKVLE 682
Cdd:PRK11753   31 LIHAGEKAETLYYIVKGSVAVLIKDEegkemILSYLNQGDFIGELGLFEEGQERS-AWVRAKTACEVAEISYKKFRQLIQ 109

                          90       100       110
                  ....*....|....*....|....*....|
gi 1046856974 683 FYTAFSHSFSRNLIltynLRKRIVFRKISD 712
Cdd:PRK11753  110 VNPDILMALSAQMA----RRLQNTSRKVGD 135
 
Name Accession Description Interval E-value
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 220-647 2.00e-34

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 142.31  E-value: 2.00e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046856974 220 WDWIILILTFYTAILVPYNVSFKTRQNNVAWLVVDSIVDVIFLVDIVLNFHTTFVGPAGEV-ISDPKLIRMNYLKTWFVI 298
Cdd:PLN03192   64 WETLMVVLVAYSAWVYPFEVAFLNASPKRGLEIADNVVDLFFAVDIVLTFFVAYIDPRTQLlVRDRKKIAVRYLSTWFLM 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046856974 299 DLLSCLPYDVINAFenvdevsafmgdpgkigfadqipppLEGRESQGISslFSSLKVVRLLRLGRVAR---KLDHYIEYG 375
Cdd:PLN03192  144 DVASTIPFQALAYL-------------------------ITGTVKLNLS--YSLLGLLRFWRLRRVKQlftRLEKDIRFS 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046856974 376 AAVL--VLLVCVFGLAAHWMACIWYSIGDYEIFDEDT---KTIRNnswLYQLALDIGtpyqfngsgsgkweggpsknsvY 450
Cdd:PLN03192  197 YFWIrcARLLSVTLFLVHCAGCLYYLIADRYPHQGKTwigAVIPN---FRETSLWIR----------------------Y 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046856974 451 ISSLYFTMTSLTSVGFGNIAPSTDIEKIFAVAIMMIGSLLYATIFGNVTTIFQQmyaNTNRYHEMLNSVR---DFLKLYQ 527
Cdd:PLN03192  252 ISAIYWSITTMTTVGYGDLHAVNTIEMIFIIFYMLFNLGLTAYLIGNMTNLVVE---GTRRTMEFRNSIEaasNFVGRNR 328

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046856974 528 VPKGLSERVMDYIVSTWSmSRGIDTEKVLQICPKDMRADICVHLNRKVFKEHPAFRLASDGCLRALAMEFQTVHCAPGDL 607
Cdd:PLN03192  329 LPPRLKDQILAYMCLRFK-AESLNQQQLIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPRED 407

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 1046856974 608 IYHAGESVDSLCFVVSGSLEVI----QDDEVVAILGKGDVFGDV 647
Cdd:PLN03192  408 VIMQNEAPDDVYIVVSGEVEIIdsegEKERVVGTLGCGDIFGEV 451
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 220-510 1.61e-30

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: 120.83  E-value: 1.61e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046856974 220 WDWIILILTFYTAILVPYNVSFKTRQ-NNVAWLVVDSIVDVIFLVDIVLNFHTTFvgpagevisdpklIRMNYLKT-WFV 297
Cdd:pfam00520   4 FELFILLLILLNTIFLALETYFQPEEpLTTVLEILDYVFTGIFTLEMLLKIIAAG-------------FKKRYFRSpWNI 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046856974 298 IDLLSCLPYDVINAFENVDEVSAFmgdpgkigfadqippplegresqgisSLFSSLKVVRLLRLGRVARKLDHYIeYGAA 377
Cdd:pfam00520  71 LDFVVVLPSLISLVLSSVGSLSGL--------------------------RVLRLLRLLRLLRLIRRLEGLRTLV-NSLI 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046856974 378 VLVLLVCVFGLAAHWMACIWYSIGdyeifdedtktirnnswlyqlaldigtpYQFNGSGSGKWEGGPSKNSV---YISSL 454
Cdd:pfam00520 124 RSLKSLGNLLLLLLLFLFIFAIIG----------------------------YQLFGGKLKTWENPDNGRTNfdnFPNAF 175

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046856974 455 YFTMTSLTSVGFGNIAPSTDIEK-------IFAVAIMMIGSLLYATIFGNVTTIFQQMYANTN 510
Cdd:pfam00520 176 LWLFQTMTTEGWGDIMYDTIDGKgefwayiYFVSFIILGGFLLLNLFIAVIIDNFQELTERTE 238
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 581-691 2.15e-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: 2.15e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046856974 581 AFRLASDGCLRALAMEFQTVHCAPGDLIYHAGESVDSLCFVVSGSLEVIQDDE-----VVAILGKGDVFGDVFWkeATLA 655
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEdgreqIVGFLGPGDLFGELAL--LGNG 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1046856974 656 QSCANVRALTYCDLHVIKRDALQKVLEFYTAFSHSF 691
Cdd:cd00038    79 PRSATVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 582-698 1.15e-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: 1.15e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046856974  582 FRLASDGCLRALAMEFQTVHCAPGDLIYHAGESVDSLCFVVSGSLEVIQDDE-----VVAILGKGDVFGDvfwkEATLAQ 656
Cdd:smart00100   2 FKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEdgeeqIVGTLGPGDFFGE----LALLTN 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1046856974  657 --SCANVRALTYCdLHVIKRDALQKVLEFYTAFSHSFSRNLILT 698
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 2.05e-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: 2.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046856974  41 PIVYSNDGFCKLSGYHRAEVMQKSsaCSFMYGeltDKDTVEKVRQTFENYEMN-SFEILMYKKNRTPVWFFVKIAPIRNE 119
Cdd:pfam13426   3 RIIYVNDAALRLLGYTREELLGKS--ITDLFA---EPEDSERLREALREGKAVrEFEVVLYRKDGEPFPVLVSLAPIRDD 77

                          90
                  ....*....|....*.
gi 1046856974 120 QDKVVLFLCTFSDITA 135
Cdd:pfam13426  78 GGELVGIIAILRDITE 93
PAS COG2202
PAS domain [Signal transduction mechanisms];
39-138 6.75e-16

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 78.91  E-value: 6.75e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046856974  39 DWPIVYSNDGFCKLSGYHRAEVMQKSsaCSFMYGELTDKDTVEKVRQTFENYEMNSFEILMYKKNRTPVWFFVKIAPIRN 118
Cdd:COG2202    30 DGRILYVNPAFERLTGYSAEELLGKT--LRDLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGSLFWVELSISPVRD 107

                          90       100
                  ....*....|....*....|
gi 1046856974 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 ...
 582-695 8.56e-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: 8.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046856974 582 FRLASDGCLRALAMEFQTVHCAPGDLIYHAGESVDSLCFVVSGSLEVIQDDE-----VVAILGKGDVFGDVFWKEATLAQ 656
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEdgreqILGFLGPGDFFGELSLLGGEPSP 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1046856974 657 scANVRALTYCDLHVIKRDALQKVLEFYTAFSHSFSRNL 695
Cdd:COG0664    81 --ATAEALEDSELLRIPREDLEELLERNPELARALLRLL 117
PRK13558 PRK13558
bacterio-opsin activator; Provisional
 39-138 1.39e-13

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 74.87  E-value: 1.39e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046856974  39 DWPIVYSNDGFCKLSGYHRAEVMQKSsaCSFMYGELTDKDTVEKVRQTFENYEMNSFEILMYKKNRTPVWFFVKIAPIRN 118
Cdd:PRK13558  170 DEPLIYINDAFERITGYSPDEVLGRN--CRFLQGEDTNEERVAELREAIDEERPTSVELRNYRKDGSTFWNQVDIAPIRD 247

                          90       100
                  ....*....|....*....|
gi 1046856974 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 9.98e-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: 56.49  E-value: 9.98e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046856974  39 DWPIVYSNDGFCKLSGYHRAEVMQKSsacsfmYGELTDKDTVEKVRQTFENY----EMNSFEILMYKKNRTPVWFFVKIA 114
Cdd:cd00130    11 DGRILYANPAAEQLLGYSPEELIGKS------LLDLIHPEDREELRERLENLlsggEPVTLEVRLRRKDGSVIWVLVSLT 84

                          90
                  ....*....|....*....
gi 1046856974 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 2.89e-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: 2.89e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1046856974   94 SFEILMYKKNRTPVWFFVKIAPIRNEQDKVVLFLCTFSDITA 135
Cdd:smart00086   1 TVEYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITE 42
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
608-712 9.06e-07

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 50.75  E-value: 9.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046856974 608 IYHAGESVDSLCFVVSGSLEVIQDDE-----VVAILGKGDVFGDVFWKEATLAQScANVRALTYCDLHVIKRDALQKVLE 682
Cdd:PRK11753   31 LIHAGEKAETLYYIVKGSVAVLIKDEegkemILSYLNQGDFIGELGLFEEGQERS-AWVRAKTACEVAEISYKKFRQLIQ 109

                          90       100       110
                  ....*....|....*....|....*....|
gi 1046856974 683 FYTAFSHSFSRNLIltynLRKRIVFRKISD 712
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 2.02e-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: 2.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046856974  16 TFLENIVRRSNDTNFVLG-NAQIVDWpivysNDGFCKLSGYHRAEVMQKSSAcsfmygELTDKDTVEKVRQTFENYEM-- 92
Cdd:TIGR00229   3 ERYRAIFESSPDAIIVIDlEGNILYV-----NPAFEEIFGYSAEELIGRNVL------ELIPEEDREEVRERIERRLEge 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1046856974  93 ---NSFEILMYKKNRTPVWFFVKIAPIRnEQDKVVLFLCTFSDITAFKQ 138
Cdd:TIGR00229  72 pepVSEERRVRRKDGSEIWVEVSVSPIR-TNGGELGVVGIVRDITERKE 119
 
Name Accession Description Interval E-value
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 220-647 2.00e-34

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 142.31  E-value: 2.00e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046856974 220 WDWIILILTFYTAILVPYNVSFKTRQNNVAWLVVDSIVDVIFLVDIVLNFHTTFVGPAGEV-ISDPKLIRMNYLKTWFVI 298
Cdd:PLN03192   64 WETLMVVLVAYSAWVYPFEVAFLNASPKRGLEIADNVVDLFFAVDIVLTFFVAYIDPRTQLlVRDRKKIAVRYLSTWFLM 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046856974 299 DLLSCLPYDVINAFenvdevsafmgdpgkigfadqipppLEGRESQGISslFSSLKVVRLLRLGRVAR---KLDHYIEYG 375
Cdd:PLN03192  144 DVASTIPFQALAYL-------------------------ITGTVKLNLS--YSLLGLLRFWRLRRVKQlftRLEKDIRFS 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046856974 376 AAVL--VLLVCVFGLAAHWMACIWYSIGDYEIFDEDT---KTIRNnswLYQLALDIGtpyqfngsgsgkweggpsknsvY 450
Cdd:PLN03192  197 YFWIrcARLLSVTLFLVHCAGCLYYLIADRYPHQGKTwigAVIPN---FRETSLWIR----------------------Y 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046856974 451 ISSLYFTMTSLTSVGFGNIAPSTDIEKIFAVAIMMIGSLLYATIFGNVTTIFQQmyaNTNRYHEMLNSVR---DFLKLYQ 527
Cdd:PLN03192  252 ISAIYWSITTMTTVGYGDLHAVNTIEMIFIIFYMLFNLGLTAYLIGNMTNLVVE---GTRRTMEFRNSIEaasNFVGRNR 328

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046856974 528 VPKGLSERVMDYIVSTWSmSRGIDTEKVLQICPKDMRADICVHLNRKVFKEHPAFRLASDGCLRALAMEFQTVHCAPGDL 607
Cdd:PLN03192  329 LPPRLKDQILAYMCLRFK-AESLNQQQLIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPRED 407

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 1046856974 608 IYHAGESVDSLCFVVSGSLEVI----QDDEVVAILGKGDVFGDV 647
Cdd:PLN03192  408 VIMQNEAPDDVYIVVSGEVEIIdsegEKERVVGTLGCGDIFGEV 451
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 220-510 1.61e-30

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: 120.83  E-value: 1.61e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046856974 220 WDWIILILTFYTAILVPYNVSFKTRQ-NNVAWLVVDSIVDVIFLVDIVLNFHTTFvgpagevisdpklIRMNYLKT-WFV 297
Cdd:pfam00520   4 FELFILLLILLNTIFLALETYFQPEEpLTTVLEILDYVFTGIFTLEMLLKIIAAG-------------FKKRYFRSpWNI 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046856974 298 IDLLSCLPYDVINAFENVDEVSAFmgdpgkigfadqippplegresqgisSLFSSLKVVRLLRLGRVARKLDHYIeYGAA 377
Cdd:pfam00520  71 LDFVVVLPSLISLVLSSVGSLSGL--------------------------RVLRLLRLLRLLRLIRRLEGLRTLV-NSLI 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046856974 378 VLVLLVCVFGLAAHWMACIWYSIGdyeifdedtktirnnswlyqlaldigtpYQFNGSGSGKWEGGPSKNSV---YISSL 454
Cdd:pfam00520 124 RSLKSLGNLLLLLLLFLFIFAIIG----------------------------YQLFGGKLKTWENPDNGRTNfdnFPNAF 175

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046856974 455 YFTMTSLTSVGFGNIAPSTDIEK-------IFAVAIMMIGSLLYATIFGNVTTIFQQMYANTN 510
Cdd:pfam00520 176 LWLFQTMTTEGWGDIMYDTIDGKgefwayiYFVSFIILGGFLLLNLFIAVIIDNFQELTERTE 238
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 581-691 2.15e-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: 2.15e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046856974 581 AFRLASDGCLRALAMEFQTVHCAPGDLIYHAGESVDSLCFVVSGSLEVIQDDE-----VVAILGKGDVFGDVFWkeATLA 655
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEdgreqIVGFLGPGDLFGELAL--LGNG 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1046856974 656 QSCANVRALTYCDLHVIKRDALQKVLEFYTAFSHSF 691
Cdd:cd00038    79 PRSATVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 582-698 1.15e-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: 1.15e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046856974  582 FRLASDGCLRALAMEFQTVHCAPGDLIYHAGESVDSLCFVVSGSLEVIQDDE-----VVAILGKGDVFGDvfwkEATLAQ 656
Cdd:smart00100   2 FKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEdgeeqIVGTLGPGDFFGE----LALLTN 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1046856974  657 --SCANVRALTYCdLHVIKRDALQKVLEFYTAFSHSFSRNLILT 698
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 2.05e-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: 2.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046856974  41 PIVYSNDGFCKLSGYHRAEVMQKSsaCSFMYGeltDKDTVEKVRQTFENYEMN-SFEILMYKKNRTPVWFFVKIAPIRNE 119
Cdd:pfam13426   3 RIIYVNDAALRLLGYTREELLGKS--ITDLFA---EPEDSERLREALREGKAVrEFEVVLYRKDGEPFPVLVSLAPIRDD 77

                          90
                  ....*....|....*.
gi 1046856974 120 QDKVVLFLCTFSDITA 135
Cdd:pfam13426  78 GGELVGIIAILRDITE 93
PAS COG2202
PAS domain [Signal transduction mechanisms];
39-138 6.75e-16

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 78.91  E-value: 6.75e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046856974  39 DWPIVYSNDGFCKLSGYHRAEVMQKSsaCSFMYGELTDKDTVEKVRQTFENYEMNSFEILMYKKNRTPVWFFVKIAPIRN 118
Cdd:COG2202    30 DGRILYVNPAFERLTGYSAEELLGKT--LRDLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGSLFWVELSISPVRD 107

                          90       100
                  ....*....|....*....|
gi 1046856974 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 ...
 582-695 8.56e-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: 8.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046856974 582 FRLASDGCLRALAMEFQTVHCAPGDLIYHAGESVDSLCFVVSGSLEVIQDDE-----VVAILGKGDVFGDVFWKEATLAQ 656
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEdgreqILGFLGPGDFFGELSLLGGEPSP 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1046856974 657 scANVRALTYCDLHVIKRDALQKVLEFYTAFSHSFSRNL 695
Cdd:COG0664    81 --ATAEALEDSELLRIPREDLEELLERNPELARALLRLL 117
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 600-682 7.81e-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: 7.81e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046856974 600 VHCAPGDLIYHAGESVDSLCFVVSGSLEVIQDDE-----VVAILGKGDVFGDVfwkeATLAQSC--ANVRALTYCDLHVI 672
Cdd:pfam00027   2 RSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEdgreqILAVLGPGDFFGEL----ALLGGEPrsATVVALTDSELLVI 77

                          90
                  ....*....|
gi 1046856974 673 KRDALQKVLE 682
Cdd:pfam00027  78 PREDFLELLE 87
PRK13558 PRK13558
bacterio-opsin activator; Provisional
 39-138 1.39e-13

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 74.87  E-value: 1.39e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046856974  39 DWPIVYSNDGFCKLSGYHRAEVMQKSsaCSFMYGELTDKDTVEKVRQTFENYEMNSFEILMYKKNRTPVWFFVKIAPIRN 118
Cdd:PRK13558  170 DEPLIYINDAFERITGYSPDEVLGRN--CRFLQGEDTNEERVAELREAIDEERPTSVELRNYRKDGSTFWNQVDIAPIRD 247

                          90       100
                  ....*....|....*....|
gi 1046856974 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.
 450-504 4.29e-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: 62.67  E-value: 4.29e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1046856974 450 YISSLYFTMTSLTSVGFGNIAPSTDIEKIFAVAIMMIGSLLYATIFGNVTTIFQQ 504
Cdd:pfam07885  24 FLDALYFSFVTLTTVGYGDIVPLTDAGRLFTIFYILIGIPLFAIFLAVLGRFLTE 78
PRK13559 PRK13559
hypothetical protein; Provisional
 31-137 6.38e-11

hypothetical protein; Provisional


Pssm-ID: 237427 [Multi-domain]  Cd Length: 361  Bit Score: 65.23  E-value: 6.38e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046856974  31 VLGNAQIVDWPIVYSNDGFCKLSGYHRAEVMQKSsaCSFMYGELTDKDTVEKVRQTFENYEMNSFEILMYKKNRTPVWFF 110
Cdd:PRK13559   57 CITDPHQPDLPIVLANQAFLDLTGYAAEEVVGRN--CRFLQGAATDPIAVAKIRAAIAAEREIVVELLNYRKDGEPFWNA 134

                          90       100
                  ....*....|....*....|....*..
gi 1046856974 111 VKIAPIRNEQDKVVLFLCTFSDITAFK 137
Cdd:PRK13559  135 LHLGPVYGEDGRLLYFFGSQWDVTDIR 161
PRK13557 PRK13557
histidine kinase; Provisional
 39-134 1.42e-10

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 65.08  E-value: 1.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046856974  39 DWPIVYSNDGFCKLSGYHRAEVMqkSSACSFMYGELTDKDTVEKVRQTFENYEMNSFEILMYKKNRTPVWFFVKIAPIRN 118
Cdd:PRK13557   52 DNPIVFANRAFLEMTGYAAEEII--GNNCRFLQGPETDRATVAEVRDAIAERREIATEILNYRKDGSSFWNALFVSPVYN 129

                          90
                  ....*....|....*.
gi 1046856974 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 9.98e-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: 56.49  E-value: 9.98e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046856974  39 DWPIVYSNDGFCKLSGYHRAEVMQKSsacsfmYGELTDKDTVEKVRQTFENY----EMNSFEILMYKKNRTPVWFFVKIA 114
Cdd:cd00130    11 DGRILYANPAAEQLLGYSPEELIGKS------LLDLIHPEDREELRERLENLlsggEPVTLEVRLRRKDGSVIWVLVSLT 84

                          90
                  ....*....|....*....
gi 1046856974 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 2.89e-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: 2.89e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1046856974   94 SFEILMYKKNRTPVWFFVKIAPIRNEQDKVVLFLCTFSDITA 135
Cdd:smart00086   1 TVEYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITE 42
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
608-712 9.06e-07

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 50.75  E-value: 9.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046856974 608 IYHAGESVDSLCFVVSGSLEVIQDDE-----VVAILGKGDVFGDVFWKEATLAQScANVRALTYCDLHVIKRDALQKVLE 682
Cdd:PRK11753   31 LIHAGEKAETLYYIVKGSVAVLIKDEegkemILSYLNQGDFIGELGLFEEGQERS-AWVRAKTACEVAEISYKKFRQLIQ 109

                          90       100       110
                  ....*....|....*....|....*....|
gi 1046856974 683 FYTAFSHSFSRNLIltynLRKRIVFRKISD 712
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 5.63e-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: 5.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046856974  42 IVYSNDGFCKLSGYHRAEVMQKSsacsfMYGEL---TDKDTVEKVRQTFENYEMN-SFEILMYKKNRTPVWFFVKIAPIR 117
Cdd:pfam00989  23 ILYVNAAAEELLGLSREEVIGKS-----LLDLIpeeDDAEVAELLRQALLQGEESrGFEVSFRVPDGRPRHVEVRASPVR 97

                          90
                  ....*....|....*.
gi 1046856974 118 NEQDKVVLFLCTFSDI 133
Cdd:pfam00989  98 DAGGEILGFLGVLRDI 113
PAS COG2202
PAS domain [Signal transduction mechanisms];
14-138 1.02e-05

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 48.10  E-value: 1.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046856974  14 QNTFLENIVRRSNDTNFVLGNAQIvdwpIVYSNDGFCKLSGYHRAEVMQKSSAcsfmygELTDKDTVEKVRQTFENY--- 90
Cdd:COG2202   135 SEERLRLLVENAPDGIFVLDLDGR----ILYVNPAAEELLGYSPEELLGKSLL------DLLHPEDRERLLELLRRLleg 204

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1046856974  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 2.02e-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: 2.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046856974  16 TFLENIVRRSNDTNFVLG-NAQIVDWpivysNDGFCKLSGYHRAEVMQKSSAcsfmygELTDKDTVEKVRQTFENYEM-- 92
Cdd:TIGR00229   3 ERYRAIFESSPDAIIVIDlEGNILYV-----NPAFEEIFGYSAEELIGRNVL------ELIPEEDREEVRERIERRLEge 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1046856974  93 ---NSFEILMYKKNRTPVWFFVKIAPIRnEQDKVVLFLCTFSDITAFKQ 138
Cdd:TIGR00229  72 pepVSEERRVRRKDGSEIWVEVSVSPIR-TNGGELGVVGIVRDITERKE 119
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
42-138 8.04e-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: 8.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046856974  42 IVYSNDGFCKLSGYHRAEVMQKSsACSFMYGELTDKDTVEKVRQtfENYEMNSFEILMYKKNRTPVWFFVKIAPIRNEQD 121
Cdd:COG3852    29 ITYVNPAAERLLGLSAEELLGRP-LAELFPEDSPLRELLERALA--EGQPVTEREVTLRRKDGEERPVDVSVSPLRDAEG 105

                          90
                  ....*....|....*..
gi 1046856974 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 1.66e-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: 1.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046856974  42 IVYSNDGFCKLSGYHRAEVMQKSSAC-SFMYGEltdkDtVEKVRQTFENYEMN----SFEILMYKKNRTPVWFFVKIAPI 116
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELLGKGESWlDLVHPD----D-RERVREALWEALKGgepySGEYRIRRKDGEYRWVEARARPI 75

                          90
                  ....*....|...
gi 1046856974 117 RNEQDKVVLFLCT 129
Cdd:pfam08447  76 RDENGKPVRVIGV 88
PRK10537 PRK10537
voltage-gated potassium channel protein;
454-498 2.02e-03

voltage-gated potassium channel protein;


Pssm-ID: 236711 [Multi-domain]  Cd Length: 393  Bit Score: 41.55  E-value: 2.02e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1046856974 454 LYFTMTSLTSVGFGNIAPSTDIEKIFAVAIMMIGSLLYAT----IFGNV 498
Cdd:PRK10537  173 FYFSIVTMSTVGYGDIVPVSESARLFTISVIILGITVFATsisaIFGPV 221
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 42-138 5.75e-03

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 40.52  E-value: 5.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046856974  42 IVYSNDGFCKLSGYHRAEVMQKSSAcSFMYGELTDKDTVEKVRQTFENYEMNSFEILMYKKNRTPVWFFVKIAPIRNEQD 121
Cdd:PRK11359  158 IVQCNRAFTEMFGYCISEASGMQPD-TLLNIPEFPADNRIRLQQLLWKTARDQDEFLLLTRTGEKIWIKASISPVYDVLA 236

                          90
                  ....*....|....*..
gi 1046856974 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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