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Conserved domains on  [gi|13540549|ref|NP_110406|]
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potassium voltage-gated channel subfamily H member 6 isoform 1 [Homo sapiens]

Protein Classification

PAS domain-containing protein( domain architecture ID 13822714)

PAS domain-containing protein

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
259-698 1.95e-36

Voltage-dependent potassium channel; Provisional


The actual alignment was detected with superfamily member PLN03192:

Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 148.48  E-value: 1.95e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540549  259 WDWLILLLVIYTAVFTPYSAAFLLSdqdesrrgacsytcSP---LTVVDLIVDIMFVVDIVINFRTTYVNTNDEV-VSHP 334
Cdd:PLN03192  64 WETLMVVLVAYSAWVYPFEVAFLNA--------------SPkrgLEIADNVVDLFFAVDIVLTFFVAYIDPRTQLlVRDR 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540549  335 RRIAVHYFKGWFLIDMVAAIPFDLL-IFRTGS---DETTTLIGLLKTARLLRLVRVARKLD---RYSEYGAAVLFLLMCT 407
Cdd:PLN03192 130 KKIAVRYLSTWFLMDVASTIPFQALaYLITGTvklNLSYSLLGLLRFWRLRRVKQLFTRLEkdiRFSYFWIRCARLLSVT 209
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540549  408 FALIaHWLACIWYAIGNvERPYLEHKigWLDSLGVQLGKryngsdpasgPSVQDKYVTALYFTFSSLTSVGFGNVSPNTN 487
Cdd:PLN03192 210 LFLV-HCAGCLYYLIAD-RYPHQGKT--WIGAVIPNFRE----------TSLWIRYISAIYWSITTMTTVGYGDLHAVNT 275
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540549  488 SEKVFSICVMLIGSLMYASIFGNVSAIIQRLYSGTARYHTQMLRVKEFIRFHQIPNPLRQRLEEYFQHAWSYTNgIDMNA 567
Cdd:PLN03192 276 IEMIFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRLKDQILAYMCLRFKAES-LNQQQ 354
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540549  568 VLKGFPECLQADICLHLHRALLQHCPAFSGAGKGCLRALAVKFKTTHAPPGDTLVHLGDVLSTLYFISRGSIEIL----R 643
Cdd:PLN03192 355 LIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEIIdsegE 434
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 13540549  644 DDVVVAILGKNDIFGEPVSLHAQPgkSSADVRALTYCDLHKIQRADLLEVLDMYP 698
Cdd:PLN03192 435 KERVVGTLGCGDIFGEVGALCCRP--QSFTFRTKTLSQLLRLKTSTLIEAMQTRQ 487
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
38-132 7.71e-19

PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


:

Pssm-ID: 463873 [Multi-domain]  Cd Length: 93  Bit Score: 82.12  E-value: 7.71e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540549    38 NCAIIYCNDGFCELFGYSRVEVMQQPCTCDFltgpnTPSSAVSRLAQAL-LGAEECKVDILYYRKDASSFRCLVDVVPVK 116
Cdd:pfam13426   1 DGRIIYVNDAALRLLGYTREELLGKSITDLF-----AEPEDSERLREALrEGKAVREFEVVLYRKDGEPFPVLVSLAPIR 75
                          90
                  ....*....|....*.
gi 13540549   117 NEDGAVIMFILNFEDL 132
Cdd:pfam13426  76 DDGGELVGIIAILRDI 91
 
Name Accession Description Interval E-value
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
259-698 1.95e-36

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 148.48  E-value: 1.95e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540549  259 WDWLILLLVIYTAVFTPYSAAFLLSdqdesrrgacsytcSP---LTVVDLIVDIMFVVDIVINFRTTYVNTNDEV-VSHP 334
Cdd:PLN03192  64 WETLMVVLVAYSAWVYPFEVAFLNA--------------SPkrgLEIADNVVDLFFAVDIVLTFFVAYIDPRTQLlVRDR 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540549  335 RRIAVHYFKGWFLIDMVAAIPFDLL-IFRTGS---DETTTLIGLLKTARLLRLVRVARKLD---RYSEYGAAVLFLLMCT 407
Cdd:PLN03192 130 KKIAVRYLSTWFLMDVASTIPFQALaYLITGTvklNLSYSLLGLLRFWRLRRVKQLFTRLEkdiRFSYFWIRCARLLSVT 209
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540549  408 FALIaHWLACIWYAIGNvERPYLEHKigWLDSLGVQLGKryngsdpasgPSVQDKYVTALYFTFSSLTSVGFGNVSPNTN 487
Cdd:PLN03192 210 LFLV-HCAGCLYYLIAD-RYPHQGKT--WIGAVIPNFRE----------TSLWIRYISAIYWSITTMTTVGYGDLHAVNT 275
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540549  488 SEKVFSICVMLIGSLMYASIFGNVSAIIQRLYSGTARYHTQMLRVKEFIRFHQIPNPLRQRLEEYFQHAWSYTNgIDMNA 567
Cdd:PLN03192 276 IEMIFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRLKDQILAYMCLRFKAES-LNQQQ 354
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540549  568 VLKGFPECLQADICLHLHRALLQHCPAFSGAGKGCLRALAVKFKTTHAPPGDTLVHLGDVLSTLYFISRGSIEIL----R 643
Cdd:PLN03192 355 LIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEIIdsegE 434
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 13540549  644 DDVVVAILGKNDIFGEPVSLHAQPgkSSADVRALTYCDLHKIQRADLLEVLDMYP 698
Cdd:PLN03192 435 KERVVGTLGCGDIFGEVGALCCRP--QSFTFRTKTLSQLLRLKTSTLIEAMQTRQ 487
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
258-520 8.03e-36

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: 135.86  E-value: 8.03e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540549   258 VWDWLILLLVIYTAVFTPYSAAFLLSDQdesrrgacsyTCSPLTVVDLIVDIMFVVDIVINFRTTYVNtndevvshprri 337
Cdd:pfam00520   3 YFELFILLLILLNTIFLALETYFQPEEP----------LTTVLEILDYVFTGIFTLEMLLKIIAAGFK------------ 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540549   338 aVHYFK-GWFLIDMVAAIPFDLLIFRTGSdETTTLIGLLKTARLLRLVRVARKLDRYSEYGAAVL--FLLMCTFALIAHW 414
Cdd:pfam00520  61 -KRYFRsPWNILDFVVVLPSLISLVLSSV-GSLSGLRVLRLLRLLRLLRLIRRLEGLRTLVNSLIrsLKSLGNLLLLLLL 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540549   415 LACIWYAIgnverpylehkigwldslGVQL--GKRYNGSDPASGPSVQDKYVTALYFTFSSLTSVGFGNVSPNTNSEK-- 490
Cdd:pfam00520 139 FLFIFAII------------------GYQLfgGKLKTWENPDNGRTNFDNFPNAFLWLFQTMTTEGWGDIMYDTIDGKge 200
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 13540549   491 -----VFSICVMLIGSLMYASIFGNVSAIIQRLYS 520
Cdd:pfam00520 201 fwayiYFVSFIILGGFLLLNLFIAVIIDNFQELTE 235
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
594-705 2.29e-23

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: 95.86  E-value: 2.29e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540549 594 AFSGAGKGCLRALAVKFKTTHAPPGDTLVHLGDVLSTLYFISRGSIEILRDD-----VVVAILGKNDIFGEPVSLHAQPg 668
Cdd:cd00038   1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDedgreQIVGFLGPGDLFGELALLGNGP- 79
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 13540549 669 kSSADVRALTYCDLHKIQRADLLEVLDMYPAFAESFW 705
Cdd:cd00038  80 -RSATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
595-694 2.26e-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: 84.76  E-value: 2.26e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540549    595 FSGAGKGCLRALAVKFKTTHAPPGDTLVHLGDVLSTLYFISRGSIEILRD-----DVVVAILGKNDIFGEPVSLHAQPGK 669
Cdd:smart00100   2 FKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVledgeEQIVGTLGPGDFFGELALLTNSRRA 81
                           90       100
                   ....*....|....*....|....*
gi 13540549    670 SSADVRALTYCDLHKIQRADLLEVL 694
Cdd:smart00100  82 ASAAAVALELATLLRIDFRDFLQLL 106
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
38-132 7.71e-19

PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 463873 [Multi-domain]  Cd Length: 93  Bit Score: 82.12  E-value: 7.71e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540549    38 NCAIIYCNDGFCELFGYSRVEVMQQPCTCDFltgpnTPSSAVSRLAQAL-LGAEECKVDILYYRKDASSFRCLVDVVPVK 116
Cdd:pfam13426   1 DGRIIYVNDAALRLLGYTREELLGKSITDLF-----AEPEDSERLREALrEGKAVREFEVVLYRKDGEPFPVLVSLAPIR 75
                          90
                  ....*....|....*.
gi 13540549   117 NEDGAVIMFILNFEDL 132
Cdd:pfam13426  76 DDGGELVGIIAILRDI 91
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
603-709 3.47e-16

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: 78.10  E-value: 3.47e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540549 603 LRALAVKFKTTHAPPGDTLVHLGDVLSTLYFISRGSIEILR-----DDVVVAILGKNDIFGEPVSLHAQPgkSSADVRAL 677
Cdd:COG0664   9 LEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRisedgREQILGFLGPGDFFGELSLLGGEP--SPATAEAL 86
                        90       100       110
                ....*....|....*....|....*....|..
gi 13540549 678 TYCDLHKIQRADLLEVLDMYPAFAESFWSKLE 709
Cdd:COG0664  87 EDSELLRIPREDLEELLERNPELARALLRLLA 118
PRK13559 PRK13559
hypothetical protein; Provisional
31-125 1.96e-15

hypothetical protein; Provisional


Pssm-ID: 237427 [Multi-domain]  Cd Length: 361  Bit Score: 79.09  E-value: 1.96e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540549   31 IANAQMENCAIIYCNDGFCELFGYSRVEVMQQpcTCDFLTGPNTPSSAVSRLAQALLGAEECKVDILYYRKDASSFRCLV 110
Cdd:PRK13559  58 ITDPHQPDLPIVLANQAFLDLTGYAAEEVVGR--NCRFLQGAATDPIAVAKIRAAIAAEREIVVELLNYRKDGEPFWNAL 135
                         90
                 ....*....|....*
gi 13540549  111 DVVPVKNEDGAVIMF 125
Cdd:PRK13559 136 HLGPVYGEDGRLLYF 150
PAS COG2202
PAS domain [Signal transduction mechanisms];
41-131 6.79e-14

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 72.75  E-value: 6.79e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540549  41 IIYCNDGFCELFGYSRVEVMQQpcTCDFLTGPNTPSSAVSRLAQALLGAEECKVDILYYRKDASSFRCLVDVVPVKNEDG 120
Cdd:COG2202  33 ILYVNPAFERLTGYSAEELLGK--TLRDLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGSLFWVELSISPVRDEDG 110
                        90
                ....*....|.
gi 13540549 121 AVIMFILNFED 131
Cdd:COG2202 111 EITGFVGIARD 121
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
41-132 9.14e-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: 53.79  E-value: 9.14e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540549  41 IIYCNDGFCELFGYSRVEVMQQPctCDFLTGPNTPSSAVSRLAQALLGAEECKVDILYYRKDASSFRCLVDVVPVKNEDG 120
Cdd:cd00130  14 ILYANPAAEQLLGYSPEELIGKS--LLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLTPIRDEGG 91
                        90
                ....*....|..
gi 13540549 121 AVIMFILNFEDL 132
Cdd:cd00130  92 EVIGLLGVVRDI 103
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
37-63 4.44e-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: 36.61  E-value: 4.44e-03
                           10        20
                   ....*....|....*....|....*..
gi 13540549     37 ENCAIIYCNDGFCELFGYSRVEVMQQP 63
Cdd:smart00091  19 LDGRILYANPAAEELLGYSPEELIGKS 45
 
Name Accession Description Interval E-value
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
259-698 1.95e-36

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 148.48  E-value: 1.95e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540549  259 WDWLILLLVIYTAVFTPYSAAFLLSdqdesrrgacsytcSP---LTVVDLIVDIMFVVDIVINFRTTYVNTNDEV-VSHP 334
Cdd:PLN03192  64 WETLMVVLVAYSAWVYPFEVAFLNA--------------SPkrgLEIADNVVDLFFAVDIVLTFFVAYIDPRTQLlVRDR 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540549  335 RRIAVHYFKGWFLIDMVAAIPFDLL-IFRTGS---DETTTLIGLLKTARLLRLVRVARKLD---RYSEYGAAVLFLLMCT 407
Cdd:PLN03192 130 KKIAVRYLSTWFLMDVASTIPFQALaYLITGTvklNLSYSLLGLLRFWRLRRVKQLFTRLEkdiRFSYFWIRCARLLSVT 209
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540549  408 FALIaHWLACIWYAIGNvERPYLEHKigWLDSLGVQLGKryngsdpasgPSVQDKYVTALYFTFSSLTSVGFGNVSPNTN 487
Cdd:PLN03192 210 LFLV-HCAGCLYYLIAD-RYPHQGKT--WIGAVIPNFRE----------TSLWIRYISAIYWSITTMTTVGYGDLHAVNT 275
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540549  488 SEKVFSICVMLIGSLMYASIFGNVSAIIQRLYSGTARYHTQMLRVKEFIRFHQIPNPLRQRLEEYFQHAWSYTNgIDMNA 567
Cdd:PLN03192 276 IEMIFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRLKDQILAYMCLRFKAES-LNQQQ 354
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540549  568 VLKGFPECLQADICLHLHRALLQHCPAFSGAGKGCLRALAVKFKTTHAPPGDTLVHLGDVLSTLYFISRGSIEIL----R 643
Cdd:PLN03192 355 LIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEIIdsegE 434
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 13540549  644 DDVVVAILGKNDIFGEPVSLHAQPgkSSADVRALTYCDLHKIQRADLLEVLDMYP 698
Cdd:PLN03192 435 KERVVGTLGCGDIFGEVGALCCRP--QSFTFRTKTLSQLLRLKTSTLIEAMQTRQ 487
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
258-520 8.03e-36

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: 135.86  E-value: 8.03e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540549   258 VWDWLILLLVIYTAVFTPYSAAFLLSDQdesrrgacsyTCSPLTVVDLIVDIMFVVDIVINFRTTYVNtndevvshprri 337
Cdd:pfam00520   3 YFELFILLLILLNTIFLALETYFQPEEP----------LTTVLEILDYVFTGIFTLEMLLKIIAAGFK------------ 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540549   338 aVHYFK-GWFLIDMVAAIPFDLLIFRTGSdETTTLIGLLKTARLLRLVRVARKLDRYSEYGAAVL--FLLMCTFALIAHW 414
Cdd:pfam00520  61 -KRYFRsPWNILDFVVVLPSLISLVLSSV-GSLSGLRVLRLLRLLRLLRLIRRLEGLRTLVNSLIrsLKSLGNLLLLLLL 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540549   415 LACIWYAIgnverpylehkigwldslGVQL--GKRYNGSDPASGPSVQDKYVTALYFTFSSLTSVGFGNVSPNTNSEK-- 490
Cdd:pfam00520 139 FLFIFAII------------------GYQLfgGKLKTWENPDNGRTNFDNFPNAFLWLFQTMTTEGWGDIMYDTIDGKge 200
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 13540549   491 -----VFSICVMLIGSLMYASIFGNVSAIIQRLYS 520
Cdd:pfam00520 201 fwayiYFVSFIILGGFLLLNLFIAVIIDNFQELTE 235
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
594-705 2.29e-23

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: 95.86  E-value: 2.29e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540549 594 AFSGAGKGCLRALAVKFKTTHAPPGDTLVHLGDVLSTLYFISRGSIEILRDD-----VVVAILGKNDIFGEPVSLHAQPg 668
Cdd:cd00038   1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDedgreQIVGFLGPGDLFGELALLGNGP- 79
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 13540549 669 kSSADVRALTYCDLHKIQRADLLEVLDMYPAFAESFW 705
Cdd:cd00038  80 -RSATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
595-694 2.26e-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: 84.76  E-value: 2.26e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540549    595 FSGAGKGCLRALAVKFKTTHAPPGDTLVHLGDVLSTLYFISRGSIEILRD-----DVVVAILGKNDIFGEPVSLHAQPGK 669
Cdd:smart00100   2 FKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVledgeEQIVGTLGPGDFFGELALLTNSRRA 81
                           90       100
                   ....*....|....*....|....*
gi 13540549    670 SSADVRALTYCDLHKIQRADLLEVL 694
Cdd:smart00100  82 ASAAAVALELATLLRIDFRDFLQLL 106
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
38-132 7.71e-19

PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 463873 [Multi-domain]  Cd Length: 93  Bit Score: 82.12  E-value: 7.71e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540549    38 NCAIIYCNDGFCELFGYSRVEVMQQPCTCDFltgpnTPSSAVSRLAQAL-LGAEECKVDILYYRKDASSFRCLVDVVPVK 116
Cdd:pfam13426   1 DGRIIYVNDAALRLLGYTREELLGKSITDLF-----AEPEDSERLREALrEGKAVREFEVVLYRKDGEPFPVLVSLAPIR 75
                          90
                  ....*....|....*.
gi 13540549   117 NEDGAVIMFILNFEDL 132
Cdd:pfam13426  76 DDGGELVGIIAILRDI 91
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
603-709 3.47e-16

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: 78.10  E-value: 3.47e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540549 603 LRALAVKFKTTHAPPGDTLVHLGDVLSTLYFISRGSIEILR-----DDVVVAILGKNDIFGEPVSLHAQPgkSSADVRAL 677
Cdd:COG0664   9 LEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRisedgREQILGFLGPGDFFGELSLLGGEP--SPATAEAL 86
                        90       100       110
                ....*....|....*....|....*....|..
gi 13540549 678 TYCDLHKIQRADLLEVLDMYPAFAESFWSKLE 709
Cdd:COG0664  87 EDSELLRIPREDLEELLERNPELARALLRLLA 118
PRK13559 PRK13559
hypothetical protein; Provisional
31-125 1.96e-15

hypothetical protein; Provisional


Pssm-ID: 237427 [Multi-domain]  Cd Length: 361  Bit Score: 79.09  E-value: 1.96e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540549   31 IANAQMENCAIIYCNDGFCELFGYSRVEVMQQpcTCDFLTGPNTPSSAVSRLAQALLGAEECKVDILYYRKDASSFRCLV 110
Cdd:PRK13559  58 ITDPHQPDLPIVLANQAFLDLTGYAAEEVVGR--NCRFLQGAATDPIAVAKIRAAIAAEREIVVELLNYRKDGEPFWNAL 135
                         90
                 ....*....|....*
gi 13540549  111 DVVPVKNEDGAVIMF 125
Cdd:PRK13559 136 HLGPVYGEDGRLLYF 150
PRK13558 PRK13558
bacterio-opsin activator; Provisional
31-149 5.11e-15

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 79.50  E-value: 5.11e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540549   31 IANAQMENCAIIYCNDGFCELFGYSRVEVMQQpcTCDFLTGPNTPSSAVSRLAQALLGAEECKVDILYYRKDASSFRCLV 110
Cdd:PRK13558 163 IADATLPDEPLIYINDAFERITGYSPDEVLGR--NCRFLQGEDTNEERVAELREAIDEERPTSVELRNYRKDGSTFWNQV 240
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 13540549  111 DVVPVKNEDGAVIMFILNFEDL-----AQLLAKCSSRSLsQRLL 149
Cdd:PRK13558 241 DIAPIRDEDGTVTHYVGFQTDVterkeAELALQRERRKL-QRLL 283
PAS COG2202
PAS domain [Signal transduction mechanisms];
41-131 6.79e-14

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 72.75  E-value: 6.79e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540549  41 IIYCNDGFCELFGYSRVEVMQQpcTCDFLTGPNTPSSAVSRLAQALLGAEECKVDILYYRKDASSFRCLVDVVPVKNEDG 120
Cdd:COG2202  33 ILYVNPAFERLTGYSAEELLGK--TLRDLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGSLFWVELSISPVRDEDG 110
                        90
                ....*....|.
gi 13540549 121 AVIMFILNFED 131
Cdd:COG2202 111 EITGFVGIARD 121
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
614-697 2.96e-13

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://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 459637 [Multi-domain]  Cd Length: 89  Bit Score: 66.09  E-value: 2.96e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540549   614 HAPPGDTLVHLGDVLSTLYFISRGSIEILRDD-----VVVAILGKNDIFGEPVSLHAQPgkSSADVRALTYCDLHKIQRA 688
Cdd:pfam00027   3 SYKAGEVIFREGDPADSLYIVLSGKVKVYRTLedgreQILAVLGPGDFFGELALLGGEP--RSATVVALTDSELLVIPRE 80

                  ....*....
gi 13540549   689 DLLEVLDMY 697
Cdd:pfam00027  81 DFLELLERD 89
Ion_trans_2 pfam07885
Ion channel; This family includes the two membrane helix type ion channels found in bacteria.
463-517 1.23e-10

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: 58.43  E-value: 1.23e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 13540549   463 YVTALYFTFSSLTSVGFGNVSPNTNSEKVFSICVMLIGSLMYASIFGNVSAIIQR 517
Cdd:pfam07885  24 FLDALYFSFVTLTTVGYGDIVPLTDAGRLFTIFYILIGIPLFAIFLAVLGRFLTE 78
PRK13557 PRK13557
histidine kinase; Provisional
41-125 1.46e-10

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 65.08  E-value: 1.46e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540549   41 IIYCNDGFCELFGYSRVEVMQQpcTCDFLTGPNTPSSAVSRLAQALLGAEECKVDILYYRKDASSFRCLVDVVPVKNEDG 120
Cdd:PRK13557  55 IVFANRAFLEMTGYAAEEIIGN--NCRFLQGPETDRATVAEVRDAIAERREIATEILNYRKDGSSFWNALFVSPVYNDAG 132

                 ....*
gi 13540549  121 AVIMF 125
Cdd:PRK13557 133 DLVYF 137
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
41-131 5.07e-09

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: 55.12  E-value: 5.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540549    41 IIYCNDGFCELFGYSRVEVMQQPcTCDFLTgPNTPSSAVSRLAQALLGAEECK-VDILYYRKDASSFRCLVDVVPVKNED 119
Cdd:pfam00989  23 ILYVNAAAEELLGLSREEVIGKS-LLDLIP-EEDDAEVAELLRQALLQGEESRgFEVSFRVPDGRPRHVEVRASPVRDAG 100
                          90
                  ....*....|..
gi 13540549   120 GAVIMFILNFED 131
Cdd:pfam00989 101 GEILGFLGVLRD 112
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
616-698 6.18e-09

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 57.30  E-value: 6.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540549  616 PPGDTLVHLGDVLSTLYFISRGSIEILRDD-----VVVAILGKNDIFGEpVSLHAQPGKSSADVRALTYCDLHKIQRADL 690
Cdd:PRK11753  26 PAKSTLIHAGEKAETLYYIVKGSVAVLIKDeegkeMILSYLNQGDFIGE-LGLFEEGQERSAWVRAKTACEVAEISYKKF 104

                 ....*...
gi 13540549  691 LEVLDMYP 698
Cdd:PRK11753 105 RQLIQVNP 112
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
41-132 9.14e-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: 53.79  E-value: 9.14e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540549  41 IIYCNDGFCELFGYSRVEVMQQPctCDFLTGPNTPSSAVSRLAQALLGAEECKVDILYYRKDASSFRCLVDVVPVKNEDG 120
Cdd:cd00130  14 ILYANPAAEQLLGYSPEELIGKS--LLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLTPIRDEGG 91
                        90
                ....*....|..
gi 13540549 121 AVIMFILNFEDL 132
Cdd:cd00130  92 EVIGLLGVVRDI 103
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
37-136 5.28e-06

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 49.84  E-value: 5.28e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540549  37 ENCAIIYCNDGFCELFGYSRVEVMQQPCTcDFLTGPNTPSSAVSRLAQAllGAEECKVDILYYRKDASSFRCLVDVVPVK 116
Cdd:COG3852  25 ADGRITYVNPAAERLLGLSAEELLGRPLA-ELFPEDSPLRELLERALAE--GQPVTEREVTLRRKDGEERPVDVSVSPLR 101
                        90       100
                ....*....|....*....|
gi 13540549 117 NEDGAvIMFILNFEDLAQLL 136
Cdd:COG3852 102 DAEGE-GGVLLVLRDITERK 120
PRK10537 PRK10537
voltage-gated potassium channel protein;
334-536 1.15e-04

voltage-gated potassium channel protein;


Pssm-ID: 236711 [Multi-domain]  Cd Length: 393  Bit Score: 45.78  E-value: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540549  334 PRRIAVHYFKGWfLIDMVAAIPFDLLI----FRTGSDETTTLIGLLKTAR-------LLRLVRVARKLDRYSEYGAAVLF 402
Cdd:PRK10537  35 YGMAALNLFDIW-HIKALSALDLSLLAnapqFMLGVFLVLMAIGLLFRARlawaisiLLLLAALAITLHFYPWLKFLIGY 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540549  403 LLMCTFALIAHW-------LAC--IWYAIGnverpylehkIGWLDSLGVqLGKRYNGSDPAsgPSVQDkYVTALYFTFSS 473
Cdd:PRK10537 114 CIVLLVALLIYRrdfdrssLAAgtLFAVIS----------ITSLLFYST-FGALYLGDGFS--PPIES-LSTAFYFSIVT 179
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13540549  474 LTSVGFGNVSPNTNSEKVFSICVMLIGSLMYA----SIFGNV-SAIIQRLYSGtaRYHTqMLRVKEFI 536
Cdd:PRK10537 180 MSTVGYGDIVPVSESARLFTISVIILGITVFAtsisAIFGPViRGNLKRLVKG--RISH-MHRKDHFI 244
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
37-146 1.23e-04

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 45.92  E-value: 1.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540549   37 ENCAIIYCNDGFCELFGYSRVEVM-QQPCTcdFLTGPNTPSSAVSRLAQALLGAEECKVDILYYRKDASSFRCLVDVVPV 115
Cdd:PRK11359 154 PERRIVQCNRAFTEMFGYCISEASgMQPDT--LLNIPEFPADNRIRLQQLLWKTARDQDEFLLLTRTGEKIWIKASISPV 231
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 13540549  116 KNEDGAVIMFILNFEDLAQ-----------LLAKCSSRSLSQ 146
Cdd:PRK11359 232 YDVLAHLQNLVMTFSDITEerqirqlegniLAAMCSSPPFHE 273
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
41-135 3.54e-04

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: 44.38  E-value: 3.54e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540549  41 IIYCNDGFCELFGYSRVEVMQQPCTcDFLTGpntpssavSRLAQALlgAEECKVDILYYRKDASSFRCLVDVVPVKnEDG 120
Cdd:COG3829  33 ITYVNRAAERILGLPREEVIGKNVT-ELIPN--------SPLLEVL--KTGKPVTGVIQKTGGKGKTVIVTAIPIF-EDG 100
                        90
                ....*....|....*
gi 13540549 121 AVIMFILNFEDLAQL 135
Cdd:COG3829 101 EVIGAVETFRDITEL 115
PAS COG2202
PAS domain [Signal transduction mechanisms];
41-132 2.35e-03

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 40.78  E-value: 2.35e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540549  41 IIYCNDGFCELFGYSRVEVMQQpcTCDFLTGPNTPSSAVSRLAQALLGAEEcKVDILYYRKDASSFRCLVDVVPVKNEDG 120
Cdd:COG2202 159 ILYVNPAAEELLGYSPEELLGK--SLLDLLHPEDRERLLELLRRLLEGGRE-SYELELRLKDGDGRWVWVEASAVPLRDG 235
                        90
                ....*....|...
gi 13540549 121 A-VIMFILNFEDL 132
Cdd:COG2202 236 GeVIGVLGIVRDI 248
PLN02868 PLN02868
acyl-CoA thioesterase family protein
588-692 2.43e-03

acyl-CoA thioesterase family protein


Pssm-ID: 178459 [Multi-domain]  Cd Length: 413  Bit Score: 41.63  E-value: 2.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540549  588 LLQHCPAFSgagkgcLRALAVKFKTTHAPPGDTLVHLGDVLSTLYFISRGSIEILR----DDVVVAILGKNDIFGEPV-- 661
Cdd:PLN02868  15 LLQRLPSSS------LKKIAEVVVPKRYGKGEYVVREGEPGDGLYFIWKGEAEVSGpaeeESRPEFLLKRYDYFGYGLsg 88
                         90       100       110
                 ....*....|....*....|....*....|...
gi 13540549  662 SLHaqpgksSADVRALT--YCDLHKIQRADLLE 692
Cdd:PLN02868  89 SVH------SADVVAVSelTCLVLPHEHCHLLS 115
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
37-63 4.44e-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: 36.61  E-value: 4.44e-03
                           10        20
                   ....*....|....*....|....*..
gi 13540549     37 ENCAIIYCNDGFCELFGYSRVEVMQQP 63
Cdd:smart00091  19 LDGRILYANPAAEELLGYSPEELIGKS 45
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
19-132 7.49e-03

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: 39.96  E-value: 7.49e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540549  19 IRKFEGQSRKflIANAQMENCA-------IIYCNDGFCELFGYSRVEVMQQPCTcDFLtGPNTPSSAVSRLAQALLGAEE 91
Cdd:COG5809 136 LRESEEKFRL--IFNHSPDGIIvtdldgrIIYANPAACKLLGISIEELIGKSIL-ELI-HSDDQENVAAFISQLLKDGGI 211
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 13540549  92 CKVDILYYRKDASSFRCLVDVVPVkNEDGAVIMFILNFEDL 132
Cdd:COG5809 212 AQGEVRFWTKDGRWRLLEASGAPI-KKNGEVDGIVIIFRDI 251
 
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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