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Conserved domains on  [gi|229462892|sp|Q9NS40|]
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RecName: Full=Voltage-gated inwardly rectifying potassium channel KCNH7; AltName: Full=Ether-a-go-go-related gene potassium channel 3; Short=ERG-3; Short=Eag-related protein 3; Short=Ether-a-go-go-related protein 3; Short=hERG-3; AltName: Full=Potassium voltage-gated channel subfamily H member 7; AltName: Full=Voltage-gated potassium channel subunit Kv11.3

Protein Classification

potassium voltage-gated channel protein( domain architecture ID 12140963)

potassium voltage-gated channel protein is the pore-forming (alpha) subunit of a voltage-gated potassium channel that mediates the potassium permeability of membranes and may be modulated by cAMP and subunit assembly

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 409-671 1.78e-35

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: 135.47  E-value: 1.78e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462892   409 VWDWLILLLVIYTAIFTPYSAAFLLNDReeqkrrecgySCSPLNVVDLIVDIMFIIDILINFRTTYvnqneevvsdpakI 488
Cdd:pfam00520    3 YFELFILLLILLNTIFLALETYFQPEEP----------LTTVLEILDYVFTGIFTLEMLLKIIAAG-------------F 59

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462892   489 AIHYFK-GWFLIDMVAAIPFDLLIFGSGSdETTTLIGLLKTARLLRLVRVARKLDRYSEYGAAVL--MLLMCIFALIAHW 565
Cdd:pfam00520   60 KKRYFRsPWNILDFVVVLPSLISLVLSSV-GSLSGLRVLRLLRLLRLLRLIRRLEGLRTLVNSLIrsLKSLGNLLLLLLL 138

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462892   566 LACIWYAIGNverpyltdkigwldslgQQIGKRYNDSDSSSGPSIK-DKYVTALYFTFSSLTSVGFGNVSPNTNSEK--- 641
Cdd:pfam00520  139 FLFIFAIIGY-----------------QLFGGKLKTWENPDNGRTNfDNFPNAFLWLFQTMTTEGWGDIMYDTIDGKgef 201

                          250       260       270
                   ....*....|....*....|....*....|....
gi 229462892   642 ----IFSICVMLIGSLMYASIFGNVSAIIQRLYS 671
Cdd:pfam00520  202 wayiYFVSFIILGGFLLLNLFIAVIIDNFQELTE 235
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 745-856 1.40e-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: 96.63  E-value: 1.40e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462892  745 AFRGASKGCLRALAMKFKTTHAPPGDTLVHCGDVLTALYFLSRGSIEILKDD-----IVVAILGKNDIFGEMVHLYAKPg 819
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDedgreQIVGFLGPGDLFGELALLGNGP- 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 229462892  820 kSNADVRALTYCDLHKIQREDLLEVLDMYPEFSDHFL 856
Cdd:cd00038    80 -RSATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
 38-134 1.28e-20

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


:

Pssm-ID: 463873 [Multi-domain]  Cd Length: 93  Bit Score: 87.52  E-value: 1.28e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462892    38 NCAIIYCNDGFCEMTGFSRPDVMQKPCTcDFLHGPETKRHDIAQIAQallGSEERKVEVTYYHKNGSTFICNTHIIPVKN 117
Cdd:pfam13426    1 DGRIIYVNDAALRLLGYTREELLGKSIT-DLFAEPEDSERLREALRE---GKAVREFEVVLYRKDGEPFPVLVSLAPIRD 76

                           90
                   ....*....|....*..
gi 229462892   118 QEGVAMMFIINFEYVTD 134
Cdd:pfam13426   77 DGGELVGIIAILRDITE 93
 
Name Accession Description Interval E-value
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 409-671 1.78e-35

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: 135.47  E-value: 1.78e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462892   409 VWDWLILLLVIYTAIFTPYSAAFLLNDReeqkrrecgySCSPLNVVDLIVDIMFIIDILINFRTTYvnqneevvsdpakI 488
Cdd:pfam00520    3 YFELFILLLILLNTIFLALETYFQPEEP----------LTTVLEILDYVFTGIFTLEMLLKIIAAG-------------F 59

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462892   489 AIHYFK-GWFLIDMVAAIPFDLLIFGSGSdETTTLIGLLKTARLLRLVRVARKLDRYSEYGAAVL--MLLMCIFALIAHW 565
Cdd:pfam00520   60 KKRYFRsPWNILDFVVVLPSLISLVLSSV-GSLSGLRVLRLLRLLRLLRLIRRLEGLRTLVNSLIrsLKSLGNLLLLLLL 138

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462892   566 LACIWYAIGNverpyltdkigwldslgQQIGKRYNDSDSSSGPSIK-DKYVTALYFTFSSLTSVGFGNVSPNTNSEK--- 641
Cdd:pfam00520  139 FLFIFAIIGY-----------------QLFGGKLKTWENPDNGRTNfDNFPNAFLWLFQTMTTEGWGDIMYDTIDGKgef 201

                          250       260       270
                   ....*....|....*....|....*....|....
gi 229462892   642 ----IFSICVMLIGSLMYASIFGNVSAIIQRLYS 671
Cdd:pfam00520  202 wayiYFVSFIILGGFLLLNLFIAVIIDNFQELTE 235
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 410-887 7.83e-35

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 143.86  E-value: 7.83e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462892  410 WDWLILLLVIYTAIFTPYSAAFLlndREEQKRRecgyscspLNVVDLIVDIMFIIDILINFRTTYVNQNEEV-VSDPAKI 488
Cdd:PLN03192   64 WETLMVVLVAYSAWVYPFEVAFL---NASPKRG--------LEIADNVVDLFFAVDIVLTFFVAYIDPRTQLlVRDRKKI 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462892  489 AIHYFKGWFLIDMVAAIPFD---LLIFG-SGSDETTTLIGLLKTARLLRLVRVARKLD---RYSEYGAAVLMLLmCIFAL 561
Cdd:PLN03192  133 AVRYLSTWFLMDVASTIPFQalaYLITGtVKLNLSYSLLGLLRFWRLRRVKQLFTRLEkdiRFSYFWIRCARLL-SVTLF 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462892  562 IAHWLACIWYAIGNverPYLTDKIGWLDSLGQQIGKryndsdsssgPSIKDKYVTALYFTFSSLTSVGFGNVSPNTNSEK 641
Cdd:PLN03192  212 LVHCAGCLYYLIAD---RYPHQGKTWIGAVIPNFRE----------TSLWIRYISAIYWSITTMTTVGYGDLHAVNTIEM 278

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462892  642 IFSICVMLIGSLMYASIFGNVSAIIQRLYSGTARYHMQMLRVKEFIRFHQIPNPLRQRLEEYFQHAWTYTNgIDMNMVLK 721
Cdd:PLN03192  279 IFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRLKDQILAYMCLRFKAES-LNQQQLID 357

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462892  722 GFPECLQADICLHLNQTLLQNCKAFRGASKGCLRALAMKFKTTHAPPGDTLVHCGDVLTALYFLSRGSIEIL----KDDI 797
Cdd:PLN03192  358 QLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEIIdsegEKER 437

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462892  798 VVAILGKNDIFGEMVHLYAKPGKSNADVRALTycDLHKIQREDLLEVLDMYPEFSDHFLTNLeltfnLRHESAKADLLRS 877
Cdd:PLN03192  438 VVGTLGCGDIFGEVGALCCRPQSFTFRTKTLS--QLLRLKTSTLIEAMQTRQEDNVVILKNF-----LQHHKELHDLNVG 510

                         490
                  ....*....|
gi 229462892  878 QSMNDSEGDN 887
Cdd:PLN03192  511 DLLGDNGGEH 520
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 745-856 1.40e-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: 96.63  E-value: 1.40e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462892  745 AFRGASKGCLRALAMKFKTTHAPPGDTLVHCGDVLTALYFLSRGSIEILKDD-----IVVAILGKNDIFGEMVHLYAKPg 819
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDedgreQIVGFLGPGDLFGELALLGNGP- 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 229462892  820 kSNADVRALTYCDLHKIQREDLLEVLDMYPEFSDHFL 856
Cdd:cd00038    80 -RSATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 746-862 7.16e-22

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: 92.08  E-value: 7.16e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462892    746 FRGASKGCLRALAMKFKTTHAPPGDTLVHCGDVLTALYFLSRGSIEILKD-----DIVVAILGKNDIFGEMVHLYAKPGK 820
Cdd:smart00100    2 FKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVledgeEQIVGTLGPGDFFGELALLTNSRRA 81

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|..
gi 229462892    821 SNADVRALTYCDLHKIQREDLLEvldMYPEFSDHFLTNLELT 862
Cdd:smart00100   82 ASAAAVALELATLLRIDFRDFLQ---LLPELPQLLLELLLEL 120
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
 38-134 1.28e-20

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


Pssm-ID: 463873 [Multi-domain]  Cd Length: 93  Bit Score: 87.52  E-value: 1.28e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462892    38 NCAIIYCNDGFCEMTGFSRPDVMQKPCTcDFLHGPETKRHDIAQIAQallGSEERKVEVTYYHKNGSTFICNTHIIPVKN 117
Cdd:pfam13426    1 DGRIIYVNDAALRLLGYTREELLGKSIT-DLFAEPEDSERLREALRE---GKAVREFEVVLYRKDGEPFPVLVSLAPIRD 76

                           90
                   ....*....|....*..
gi 229462892   118 QEGVAMMFIINFEYVTD 134
Cdd:pfam13426   77 DGGELVGIIAILRDITE 93
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 746-880 1.01e-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: 80.03  E-value: 1.01e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462892  746 FRGASKGCLRALAMKFKTTHAPPGDTLVHCGDVLTALYFLSRGSIEILK-----DDIVVAILGKNDIFGEMVHLYAKPgk 820
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRisedgREQILGFLGPGDFFGELSLLGGEP-- 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462892  821 SNADVRALTYCDLHKIQREDLLEVLDMYPEFSDHFLTNLEltFNLRHESAKADLLRSQSM 880
Cdd:COG0664    79 SPATAEALEDSELLRIPREDLEELLERNPELARALLRLLA--RRLRQLQERLVSLAFLSA 136
PAS COG2202
PAS domain [Signal transduction mechanisms];
41-134 2.83e-14

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 74.29  E-value: 2.83e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462892   41 IIYCNDGFCEMTGFSRPDVMQKpcTCDFLHGPETKRHDIAQIAQALLGSEERKVEVTYYHKNGSTFICNTHIIPVKNQEG 120
Cdd:COG2202    33 ILYVNPAFERLTGYSAEELLGK--TLRDLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGSLFWVELSISPVRDEDG 110

                          90
                  ....*....|....
gi 229462892  121 VAMMFIINFEYVTD 134
Cdd:COG2202   111 EITGFVGIARDITE 124
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 765-848 2.05e-12

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: 64.17  E-value: 2.05e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462892   765 HAPPGDTLVHCGDVLTALYFLSRGSIEILKDD-----IVVAILGKNDIFGEMVHLYAKPgkSNADVRALTYCDLHKIQRE 839
Cdd:pfam00027    3 SYKAGEVIFREGDPADSLYIVLSGKVKVYRTLedgreQILAVLGPGDFFGELALLGGEP--RSATVVALTDSELLVIPRE 80


                   ....*....
gi 229462892   840 DLLEVLDMY 848
Cdd:pfam00027   81 DFLELLERD 89
PRK13557 PRK13557
histidine kinase; Provisional
 41-120 8.98e-12

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 69.31  E-value: 8.98e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462892   41 IIYCNDGFCEMTGFSRPDVMQKpcTCDFLHGPETKRHDIAQIAQALLGSEERKVEVTYYHKNGSTFICNTHIIPVKNQEG 120
Cdd:PRK13557   55 IVFANRAFLEMTGYAAEEIIGN--NCRFLQGPETDRATVAEVRDAIAERREIATEILNYRKDGSSFWNALFVSPVYNDAG 132
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 41-130 1.55e-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: 59.18  E-value: 1.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462892   41 IIYCNDGFCEMTGFSRPDVMQKPCTcDFLHGPETKRHdIAQIAQALLGSEERKVEVTYYHKNGSTFICNTHIIPVKNQEG 120
Cdd:cd00130    14 ILYANPAAEQLLGYSPEELIGKSLL-DLIHPEDREEL-RERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLTPIRDEGG 91

                          90
                  ....*....|
gi 229462892  121 VAMMFIINFE 130
Cdd:cd00130    92 EVIGLLGVVR 101
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
767-851 6.32e-09

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 57.30  E-value: 6.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462892  767 PPGDTLVHCGDVLTALYFLSRGSIEIL-KDD----IVVAILGKNDIFGEMvHLYAKPGKSNADVRALTYCDLHKIQREDL 841
Cdd:PRK11753   26 PAKSTLIHAGEKAETLYYIVKGSVAVLiKDEegkeMILSYLNQGDFIGEL-GLFEEGQERSAWVRAKTACEVAEISYKKF 104

                          90
                  ....*....|
gi 229462892  842 LEVLDMYPEF 851
Cdd:PRK11753  105 RQLIQVNPDI 114
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
 41-127 1.97e-04

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: 42.28  E-value: 1.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462892    41 IIYCNDGFCEMTGFSRPDVMQKPCTcDFLHGPETKRHDiaQIAQALLGSEERKV--EVTYYHKNGSTFICNTHIIPV-KN 117
Cdd:TIGR00229   25 ILYVNPAFEEIFGYSAEELIGRNVL-ELIPEEDREEVR--ERIERRLEGEPEPVseERRVRRKDGSEIWVEVSVSPIrTN 101

                           90
                   ....*....|
gi 229462892   118 QEGVAMMFII 127
Cdd:TIGR00229  102 GGELGVVGIV 111
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 41-73 3.58e-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: 36.99  E-value: 3.58e-03
                            10        20        30
                    ....*....|....*....|....*....|...
gi 229462892     41 IIYCNDGFCEMTGFSRPDVMQKPCTcDFLHGPE 73
Cdd:smart00091   23 ILYANPAAEELLGYSPEELIGKSLL-ELIHPED 54
 
Name Accession Description Interval E-value
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 409-671 1.78e-35

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: 135.47  E-value: 1.78e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462892   409 VWDWLILLLVIYTAIFTPYSAAFLLNDReeqkrrecgySCSPLNVVDLIVDIMFIIDILINFRTTYvnqneevvsdpakI 488
Cdd:pfam00520    3 YFELFILLLILLNTIFLALETYFQPEEP----------LTTVLEILDYVFTGIFTLEMLLKIIAAG-------------F 59

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462892   489 AIHYFK-GWFLIDMVAAIPFDLLIFGSGSdETTTLIGLLKTARLLRLVRVARKLDRYSEYGAAVL--MLLMCIFALIAHW 565
Cdd:pfam00520   60 KKRYFRsPWNILDFVVVLPSLISLVLSSV-GSLSGLRVLRLLRLLRLLRLIRRLEGLRTLVNSLIrsLKSLGNLLLLLLL 138

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462892   566 LACIWYAIGNverpyltdkigwldslgQQIGKRYNDSDSSSGPSIK-DKYVTALYFTFSSLTSVGFGNVSPNTNSEK--- 641
Cdd:pfam00520  139 FLFIFAIIGY-----------------QLFGGKLKTWENPDNGRTNfDNFPNAFLWLFQTMTTEGWGDIMYDTIDGKgef 201

                          250       260       270
                   ....*....|....*....|....*....|....
gi 229462892   642 ----IFSICVMLIGSLMYASIFGNVSAIIQRLYS 671
Cdd:pfam00520  202 wayiYFVSFIILGGFLLLNLFIAVIIDNFQELTE 235
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 410-887 7.83e-35

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 143.86  E-value: 7.83e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462892  410 WDWLILLLVIYTAIFTPYSAAFLlndREEQKRRecgyscspLNVVDLIVDIMFIIDILINFRTTYVNQNEEV-VSDPAKI 488
Cdd:PLN03192   64 WETLMVVLVAYSAWVYPFEVAFL---NASPKRG--------LEIADNVVDLFFAVDIVLTFFVAYIDPRTQLlVRDRKKI 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462892  489 AIHYFKGWFLIDMVAAIPFD---LLIFG-SGSDETTTLIGLLKTARLLRLVRVARKLD---RYSEYGAAVLMLLmCIFAL 561
Cdd:PLN03192  133 AVRYLSTWFLMDVASTIPFQalaYLITGtVKLNLSYSLLGLLRFWRLRRVKQLFTRLEkdiRFSYFWIRCARLL-SVTLF 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462892  562 IAHWLACIWYAIGNverPYLTDKIGWLDSLGQQIGKryndsdsssgPSIKDKYVTALYFTFSSLTSVGFGNVSPNTNSEK 641
Cdd:PLN03192  212 LVHCAGCLYYLIAD---RYPHQGKTWIGAVIPNFRE----------TSLWIRYISAIYWSITTMTTVGYGDLHAVNTIEM 278

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462892  642 IFSICVMLIGSLMYASIFGNVSAIIQRLYSGTARYHMQMLRVKEFIRFHQIPNPLRQRLEEYFQHAWTYTNgIDMNMVLK 721
Cdd:PLN03192  279 IFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRLKDQILAYMCLRFKAES-LNQQQLID 357

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462892  722 GFPECLQADICLHLNQTLLQNCKAFRGASKGCLRALAMKFKTTHAPPGDTLVHCGDVLTALYFLSRGSIEIL----KDDI 797
Cdd:PLN03192  358 QLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEIIdsegEKER 437

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462892  798 VVAILGKNDIFGEMVHLYAKPGKSNADVRALTycDLHKIQREDLLEVLDMYPEFSDHFLTNLeltfnLRHESAKADLLRS 877
Cdd:PLN03192  438 VVGTLGCGDIFGEVGALCCRPQSFTFRTKTLS--QLLRLKTSTLIEAMQTRQEDNVVILKNF-----LQHHKELHDLNVG 510

                         490
                  ....*....|
gi 229462892  878 QSMNDSEGDN 887
Cdd:PLN03192  511 DLLGDNGGEH 520
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 745-856 1.40e-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: 96.63  E-value: 1.40e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462892  745 AFRGASKGCLRALAMKFKTTHAPPGDTLVHCGDVLTALYFLSRGSIEILKDD-----IVVAILGKNDIFGEMVHLYAKPg 819
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDedgreQIVGFLGPGDLFGELALLGNGP- 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 229462892  820 kSNADVRALTYCDLHKIQREDLLEVLDMYPEFSDHFL 856
Cdd:cd00038    80 -RSATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 746-862 7.16e-22

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: 92.08  E-value: 7.16e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462892    746 FRGASKGCLRALAMKFKTTHAPPGDTLVHCGDVLTALYFLSRGSIEILKD-----DIVVAILGKNDIFGEMVHLYAKPGK 820
Cdd:smart00100    2 FKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVledgeEQIVGTLGPGDFFGELALLTNSRRA 81

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|..
gi 229462892    821 SNADVRALTYCDLHKIQREDLLEvldMYPEFSDHFLTNLELT 862
Cdd:smart00100   82 ASAAAVALELATLLRIDFRDFLQ---LLPELPQLLLELLLEL 120
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
 38-134 1.28e-20

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


Pssm-ID: 463873 [Multi-domain]  Cd Length: 93  Bit Score: 87.52  E-value: 1.28e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462892    38 NCAIIYCNDGFCEMTGFSRPDVMQKPCTcDFLHGPETKRHDIAQIAQallGSEERKVEVTYYHKNGSTFICNTHIIPVKN 117
Cdd:pfam13426    1 DGRIIYVNDAALRLLGYTREELLGKSIT-DLFAEPEDSERLREALRE---GKAVREFEVVLYRKDGEPFPVLVSLAPIRD 76

                           90
                   ....*....|....*..
gi 229462892   118 QEGVAMMFIINFEYVTD 134
Cdd:pfam13426   77 DGGELVGIIAILRDITE 93
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 746-880 1.01e-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: 80.03  E-value: 1.01e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462892  746 FRGASKGCLRALAMKFKTTHAPPGDTLVHCGDVLTALYFLSRGSIEILK-----DDIVVAILGKNDIFGEMVHLYAKPgk 820
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRisedgREQILGFLGPGDFFGELSLLGGEP-- 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462892  821 SNADVRALTYCDLHKIQREDLLEVLDMYPEFSDHFLTNLEltFNLRHESAKADLLRSQSM 880
Cdd:COG0664    79 SPATAEALEDSELLRIPREDLEELLERNPELARALLRLLA--RRLRQLQERLVSLAFLSA 136
PAS COG2202
PAS domain [Signal transduction mechanisms];
41-134 2.83e-14

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 74.29  E-value: 2.83e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462892   41 IIYCNDGFCEMTGFSRPDVMQKpcTCDFLHGPETKRHDIAQIAQALLGSEERKVEVTYYHKNGSTFICNTHIIPVKNQEG 120
Cdd:COG2202    33 ILYVNPAFERLTGYSAEELLGK--TLRDLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGSLFWVELSISPVRDEDG 110

                          90
                  ....*....|....
gi 229462892  121 VAMMFIINFEYVTD 134
Cdd:COG2202   111 EITGFVGIARDITE 124
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 765-848 2.05e-12

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: 64.17  E-value: 2.05e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462892   765 HAPPGDTLVHCGDVLTALYFLSRGSIEILKDD-----IVVAILGKNDIFGEMVHLYAKPgkSNADVRALTYCDLHKIQRE 839
Cdd:pfam00027    3 SYKAGEVIFREGDPADSLYIVLSGKVKVYRTLedgreQILAVLGPGDFFGELALLGGEP--RSATVVALTDSELLVIPRE 80


                   ....*....
gi 229462892   840 DLLEVLDMY 848
Cdd:pfam00027   81 DFLELLERD 89
PRK13557 PRK13557
histidine kinase; Provisional
 41-120 8.98e-12

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 69.31  E-value: 8.98e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462892   41 IIYCNDGFCEMTGFSRPDVMQKpcTCDFLHGPETKRHDIAQIAQALLGSEERKVEVTYYHKNGSTFICNTHIIPVKNQEG 120
Cdd:PRK13557   55 IVFANRAFLEMTGYAAEEIIGN--NCRFLQGPETDRATVAEVRDAIAERREIATEILNYRKDGSSFWNALFVSPVYNDAG 132
Ion_trans_2 pfam07885
Ion channel; This family includes the two membrane helix type ion channels found in bacteria.
 614-668 5.99e-11

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: 59.59  E-value: 5.99e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 229462892   614 YVTALYFTFSSLTSVGFGNVSPNTNSEKIFSICVMLIGSLMYASIFGNVSAIIQR 668
Cdd:pfam07885   24 FLDALYFSFVTLTTVGYGDIVPLTDAGRLFTIFYILIGIPLFAIFLAVLGRFLTE 78
PRK13559 PRK13559
hypothetical protein; Provisional
 30-125 6.42e-11

hypothetical protein; Provisional


Pssm-ID: 237427 [Multi-domain]  Cd Length: 361  Bit Score: 65.61  E-value: 6.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462892   30 IIANARVQNCAIIYCNDGFCEMTGFSRPDVMQKpcTCDFLHGPETKRHDIAQIAQALLGSEERKVEVTYYHKNGSTFICN 109
Cdd:PRK13559   57 CITDPHQPDLPIVLANQAFLDLTGYAAEEVVGR--NCRFLQGAATDPIAVAKIRAAIAAEREIVVELLNYRKDGEPFWNA 134

                          90
                  ....*....|....*.
gi 229462892  110 THIIPVKNQEGVAMMF 125
Cdd:PRK13559  135 LHLGPVYGEDGRLLYF 150
PRK13558 PRK13558
bacterio-opsin activator; Provisional
 31-120 6.56e-11

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 66.78  E-value: 6.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462892   31 IANARVQNCAIIYCNDGFCEMTGFSRPDVMQKpcTCDFLHGPETKRHDIAQIAQALLGSEERKVEVTYYHKNGSTFICNT 110
Cdd:PRK13558  163 IADATLPDEPLIYINDAFERITGYSPDEVLGR--NCRFLQGEDTNEERVAELREAIDEERPTSVELRNYRKDGSTFWNQV 240

                          90
                  ....*....|
gi 229462892  111 HIIPVKNQEG 120
Cdd:PRK13558  241 DIAPIRDEDG 250
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 41-130 1.55e-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: 59.18  E-value: 1.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462892   41 IIYCNDGFCEMTGFSRPDVMQKPCTcDFLHGPETKRHdIAQIAQALLGSEERKVEVTYYHKNGSTFICNTHIIPVKNQEG 120
Cdd:cd00130    14 ILYANPAAEQLLGYSPEELIGKSLL-DLIHPEDREEL-RERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLTPIRDEGG 91

                          90
                  ....*....|
gi 229462892  121 VAMMFIINFE 130
Cdd:cd00130    92 EVIGLLGVVR 101
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
767-851 6.32e-09

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 57.30  E-value: 6.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462892  767 PPGDTLVHCGDVLTALYFLSRGSIEIL-KDD----IVVAILGKNDIFGEMvHLYAKPGKSNADVRALTYCDLHKIQREDL 841
Cdd:PRK11753   26 PAKSTLIHAGEKAETLYYIVKGSVAVLiKDEegkeMILSYLNQGDFIGEL-GLFEEGQERSAWVRAKTACEVAEISYKKF 104

                          90
                  ....*....|
gi 229462892  842 LEVLDMYPEF 851
Cdd:PRK11753  105 RQLIQVNPDI 114
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 41-120 2.54e-07

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.


Pssm-ID: 430001 [Multi-domain]  Cd Length: 89  Bit Score: 49.64  E-value: 2.54e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462892    41 IIYCNDGFCEMTGFSRPDVMQKPCTC-DFLHgPETKRHDIAQIAQALLGSEERKVEVTYYHKNGSTFICNTHIIPVKNQE 119
Cdd:pfam08447    1 IIYWSPRFEEILGYTPEELLGKGESWlDLVH-PDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDEN 79


                   .
gi 229462892   120 G 120
Cdd:pfam08447   80 G 80
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
41-127 7.29e-07

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 52.93  E-value: 7.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462892   41 IIYCNDGFCEMTGFSRPDVMQKPCTcDFLHGPETKRHDIAQIAQAllGSEERKVEVTYYHKNGSTFICNTHIIPVKNQEG 120
Cdd:COG3852    29 ITYVNPAAERLLGLSAEELLGRPLA-ELFPEDSPLRELLERALAE--GQPVTEREVTLRRKDGEERPVDVSVSPLRDAEG 105


                  ....*..
gi 229462892  121 VAMMFII 127
Cdd:COG3852   106 EGGVLLV 112
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 41-129 2.00e-05

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain 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: 45.10  E-value: 2.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462892    41 IIYCNDGFCEMTGFSRPDVMQKPCTCDFLHGPETKRHDIaqIAQALL-GSEERKVEVTYYHKNGSTFICNTHIIPVKNQE 119
Cdd:pfam00989   23 ILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAEL--LRQALLqGEESRGFEVSFRVPDGRPRHVEVRASPVRDAG 100

                           90
                   ....*....|
gi 229462892   120 GVAMMFIINF 129
Cdd:pfam00989  101 GEILGFLGVL 110
PRK10537 PRK10537
voltage-gated potassium channel protein;
608-687 9.36e-05

voltage-gated potassium channel protein;


Pssm-ID: 236711 [Multi-domain]  Cd Length: 393  Bit Score: 46.17  E-value: 9.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462892  608 PSIKDkYVTALYFTFSSLTSVGFGNVSPNTNSEKIFSICVMLIGSLMYA----SIFGNV-SAIIQRLYSGTARyhmQMLR 682
Cdd:PRK10537  164 PPIES-LSTAFYFSIVTMSTVGYGDIVPVSESARLFTISVIILGITVFAtsisAIFGPViRGNLKRLVKGRIS---HMHR 239


                  ....*
gi 229462892  683 VKEFI 687
Cdd:PRK10537  240 KDHFI 244
PAS COG2202
PAS domain [Signal transduction mechanisms];
41-127 1.37e-04

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 45.02  E-value: 1.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462892   41 IIYCNDGFCEMTGFSRPDVMQKPCTcDFLHgPETKRHDIAQIAQAL-LGSEERKVEVTYYHKNGSTFICNTHIIPVKNQE 119
Cdd:COG2202   159 ILYVNPAAEELLGYSPEELLGKSLL-DLLH-PEDRERLLELLRRLLeGGRESYELELRLKDGDGRWVWVEASAVPLRDGG 236


                  ....*...
gi 229462892  120 GVAMMFII 127
Cdd:COG2202   237 EVIGVLGI 244
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
 41-127 1.97e-04

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: 42.28  E-value: 1.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462892    41 IIYCNDGFCEMTGFSRPDVMQKPCTcDFLHGPETKRHDiaQIAQALLGSEERKV--EVTYYHKNGSTFICNTHIIPV-KN 117
Cdd:TIGR00229   25 ILYVNPAFEEIFGYSAEELIGRNVL-ELIPEEDREEVR--ERIERRLEGEPEPVseERRVRRKDGSEIWVEVSVSPIrTN 101

                           90
                   ....*....|
gi 229462892   118 QEGVAMMFII 127
Cdd:TIGR00229  102 GGELGVVGIV 111
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 41-73 3.58e-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: 36.99  E-value: 3.58e-03
                            10        20        30
                    ....*....|....*....|....*....|...
gi 229462892     41 IIYCNDGFCEMTGFSRPDVMQKPCTcDFLHGPE 73
Cdd:smart00091   23 ILYANPAAEELLGYSPEELIGKSLL-ELIHPED 54
 
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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