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Conserved domains on  [gi|4557729|ref|NP_000229|]
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voltage-gated inwardly rectifying potassium channel KCNH2 isoform a [Homo sapiens]

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 ...
409-668 1.47e-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: 1.47e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557729     409 VWDWLILLLVIYTAVFTPYSAAFLLKEteegppatecgYACQPLAVVDLIVDIMFIVDILINFRTTYVNaneevvshpgr 488
Cdd:pfam00520    3 YFELFILLLILLNTIFLALETYFQPEE-----------PLTTVLEILDYVFTGIFTLEMLLKIIAAGFK----------- 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557729     489 iaVHYFK-GWFLIDMVAAIPFDLLIFGSGSEELIGL--LKTARLLRLVRVARKLDRYSEYGAAVL--FLLMCTFALIAHW 563
Cdd:pfam00520   61 --KRYFRsPWNILDFVVVLPSLISLVLSSVGSLSGLrvLRLLRLLRLLRLIRRLEGLRTLVNSLIrsLKSLGNLLLLLLL 138
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557729     564 LACIWYAIGnMEQPHmdsriGWLHNLGDQIGKPYNSsglggpsikDKYVTALYFTFSSLTSVGFGNVSPNTNSEK----- 638
Cdd:pfam00520  139 FLFIFAIIG-YQLFG-----GKLKTWENPDNGRTNF---------DNFPNAFLWLFQTMTTEGWGDIMYDTIDGKgefwa 203
                          250       260       270
                   ....*....|....*....|....*....|..
gi 4557729     639 --IFSICVMLIGSLMYASIFGNVSAIIQRLYS 668
Cdd:pfam00520  204 yiYFVSFIILGGFLLLNLFIAVIIDNFQELTE 235
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
742-853 5.37e-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: 97.78  E-value: 5.37e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557729   742 PFRGATKGCLRALAMKFKTTHAPPGDTLVHAGDLLTALYFISRGSIEILRGD-----VVVAILGKNDIFGEPLNLYARPg 816
Cdd:cd00038    1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDedgreQIVGFLGPGDLFGELALLGNGP- 79
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 4557729   817 kSNGDVRALTYCDLHKIHRDDLLEVLDMYPEFSDHFW 853
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 ...
38-130 5.49e-17

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: 77.12  E-value: 5.49e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557729      38 NCAVIYCNDGFCELCGYSRAEVMQRPCTCDFLHGPRTQRRAAAQIaqalLGAEERKVEIAFYRKDGSCFLCLVDVVPVKN 117
Cdd:pfam13426    1 DGRIIYVNDAALRLLGYTREELLGKSITDLFAEPEDSERLREALR----EGKAVREFEVVLYRKDGEPFPVLVSLAPIRD 76
                           90
                   ....*....|...
gi 4557729     118 EDGAVIMFILNFE 130
Cdd:pfam13426   77 DGGELVGIIAILR 89
 
Name Accession Description Interval E-value
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
409-668 1.47e-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: 1.47e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557729     409 VWDWLILLLVIYTAVFTPYSAAFLLKEteegppatecgYACQPLAVVDLIVDIMFIVDILINFRTTYVNaneevvshpgr 488
Cdd:pfam00520    3 YFELFILLLILLNTIFLALETYFQPEE-----------PLTTVLEILDYVFTGIFTLEMLLKIIAAGFK----------- 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557729     489 iaVHYFK-GWFLIDMVAAIPFDLLIFGSGSEELIGL--LKTARLLRLVRVARKLDRYSEYGAAVL--FLLMCTFALIAHW 563
Cdd:pfam00520   61 --KRYFRsPWNILDFVVVLPSLISLVLSSVGSLSGLrvLRLLRLLRLLRLIRRLEGLRTLVNSLIrsLKSLGNLLLLLLL 138
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557729     564 LACIWYAIGnMEQPHmdsriGWLHNLGDQIGKPYNSsglggpsikDKYVTALYFTFSSLTSVGFGNVSPNTNSEK----- 638
Cdd:pfam00520  139 FLFIFAIIG-YQLFG-----GKLKTWENPDNGRTNF---------DNFPNAFLWLFQTMTTEGWGDIMYDTIDGKgefwa 203
                          250       260       270
                   ....*....|....*....|....*....|..
gi 4557729     639 --IFSICVMLIGSLMYASIFGNVSAIIQRLYS 668
Cdd:pfam00520  204 yiYFVSFIILGGFLLLNLFIAVIIDNFQELTE 235
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
410-847 6.40e-34

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 141.16  E-value: 6.40e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557729    410 WDWLILLLVIYTAVFTPYSAAFLLKETEEGppatecgyacqpLAVVDLIVDIMFIVDILINFRTTYVNANEEV-VSHPGR 488
Cdd:PLN03192   64 WETLMVVLVAYSAWVYPFEVAFLNASPKRG------------LEIADNVVDLFFAVDIVLTFFVAYIDPRTQLlVRDRKK 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557729    489 IAVHYFKGWFLIDMVAAIPFD---LLIFGS----GSEELIGLLKTARLLRLVRVARKLD---RYSEYGAAVLFLLMCTFA 558
Cdd:PLN03192  132 IAVRYLSTWFLMDVASTIPFQalaYLITGTvklnLSYSLLGLLRFWRLRRVKQLFTRLEkdiRFSYFWIRCARLLSVTLF 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557729    559 LIaHWLACIWYAIGNmEQPHMDSRigWLhnlGDQIgkpynsSGLGGPSIKDKYVTALYFTFSSLTSVGFGNVSPNTNSEK 638
Cdd:PLN03192  212 LV-HCAGCLYYLIAD-RYPHQGKT--WI---GAVI------PNFRETSLWIRYISAIYWSITTMTTVGYGDLHAVNTIEM 278
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557729    639 IFSICVMLIGSLMYASIFGNVSAIIQRLYSGTARYHTQMLRVREFIRFHQIPNPLRQRLEEYFQHAWSYTNgIDMNAVLK 718
Cdd:PLN03192  279 IFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRLKDQILAYMCLRFKAES-LNQQQLID 357
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557729    719 GFPECLQADICLHLNRSLLQHCKPFRGATKGCLRALAMKFKTTHAPPGDTLVHAGDLLTALYFISRGSIEILRGDV---- 794
Cdd:PLN03192  358 QLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEIIDSEGeker 437
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 4557729    795 VVAILGKNDIFGEPLNLYARPGKSNGDVRALTycDLHKIHRDDLLEVLDMYPE 847
Cdd:PLN03192  438 VVGTLGCGDIFGEVGALCCRPQSFTFRTKTLS--QLLRLKTSTLIEAMQTRQE 488
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
742-853 5.37e-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: 97.78  E-value: 5.37e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557729   742 PFRGATKGCLRALAMKFKTTHAPPGDTLVHAGDLLTALYFISRGSIEILRGD-----VVVAILGKNDIFGEPLNLYARPg 816
Cdd:cd00038    1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDedgreQIVGFLGPGDLFGELALLGNGP- 79
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 4557729   817 kSNGDVRALTYCDLHKIHRDDLLEVLDMYPEFSDHFW 853
Cdd:cd00038   80 -RSATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
742-859 8.09e-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: 8.09e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557729      742 PFRGATKGCLRALAMKFKTTHAPPGDTLVHAGDLLTALYFISRGSIEILR-----GDVVVAILGKNDIFGEPLNLYARPG 816
Cdd:smart00100    1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKvledgEEQIVGTLGPGDFFGELALLTNSRR 80
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 4557729      817 KSNGDVRALTYCdlhKIHRDDLLEVLDMYPEFSDHFWSSLEIT 859
Cdd:smart00100   81 AASAAAVALELA---TLLRIDFRDFLQLLPELPQLLLELLLEL 120
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
38-130 5.49e-17

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: 77.12  E-value: 5.49e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557729      38 NCAVIYCNDGFCELCGYSRAEVMQRPCTCDFLHGPRTQRRAAAQIaqalLGAEERKVEIAFYRKDGSCFLCLVDVVPVKN 117
Cdd:pfam13426    1 DGRIIYVNDAALRLLGYTREELLGKSITDLFAEPEDSERLREALR----EGKAVREFEVVLYRKDGEPFPVLVSLAPIRD 76
                           90
                   ....*....|...
gi 4557729     118 EDGAVIMFILNFE 130
Cdd:pfam13426   77 DGGELVGIIAILR 89
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
751-857 6.47e-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: 77.72  E-value: 6.47e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557729   751 LRALAMKFKTTHAPPGDTLVHAGDLLTALYFISRGSIEILRGD-----VVVAILGKNDIFGEPLNLYARPgkSNGDVRAL 825
Cdd:COG0664    9 LEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISedgreQILGFLGPGDFFGELSLLGGEP--SPATAEAL 86
                         90       100       110
                 ....*....|....*....|....*....|..
gi 4557729   826 TYCDLHKIHRDDLLEVLDMYPEFSDHFWSSLE 857
Cdd:COG0664   87 EDSELLRIPREDLEELLERNPELARALLRLLA 118
PAS COG2202
PAS domain [Signal transduction mechanisms];
41-126 8.49e-13

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 69.67  E-value: 8.49e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557729    41 VIYCNDGFCELCGYSRAEVMQRpcTCDFLHGPRTQRRAAAQIAQALLGAEERKVEIAFYRKDGSCFLCLVDVVPVKNEDG 120
Cdd:COG2202   33 ILYVNPAFERLTGYSAEELLGK--TLRDLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGSLFWVELSISPVRDEDG 110

                 ....*.
gi 4557729   121 AVIMFI 126
Cdd:COG2202  111 EITGFV 116
PRK13559 PRK13559
hypothetical protein; Provisional
30-125 4.11e-12

hypothetical protein; Provisional


Pssm-ID: 237427 [Multi-domain]  Cd Length: 361  Bit Score: 69.08  E-value: 4.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557729     30 IIANARVENCAVIYCNDGFCELCGYSRAEVMQRpcTCDFLHGPRTQRRAAAQIAQALLGAEERKVEIAFYRKDGSCFLCL 109
Cdd:PRK13559   57 CITDPHQPDLPIVLANQAFLDLTGYAAEEVVGR--NCRFLQGAATDPIAVAKIRAAIAAEREIVVELLNYRKDGEPFWNA 134
                          90
                  ....*....|....*.
gi 4557729    110 VDVVPVKNEDGAVIMF 125
Cdd:PRK13559  135 LHLGPVYGEDGRLLYF 150
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
762-845 2.76e-11

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: 60.70  E-value: 2.76e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557729     762 HAPPGDTLVHAGDLLTALYFISRGSIEILR-----GDVVVAILGKNDIFGEPLNLYARPgkSNGDVRALTYCDLHKIHRD 836
Cdd:pfam00027    3 SYKAGEVIFREGDPADSLYIVLSGKVKVYRtledgREQILAVLGPGDFFGELALLGGEP--RSATVVALTDSELLVIPRE 80

                   ....*....
gi 4557729     837 DLLEVLDMY 845
Cdd:pfam00027   81 DFLELLERD 89
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
41-132 2.96e-08

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: 52.64  E-value: 2.96e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557729    41 VIYCNDGFCELCGYSRAEVMQRPCTcDFLHgPRTQRRAAAQIAQALLGAEERKVEIAFYRKDGSCFLCLVDVVPVKNEDG 120
Cdd:cd00130   14 ILYANPAAEQLLGYSPEELIGKSLL-DLIH-PEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLTPIRDEGG 91
                         90
                 ....*....|..
gi 4557729   121 AVIMFILNFEVV 132
Cdd:cd00130   92 EVIGLLGVVRDI 103
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
764-866 3.39e-08

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 55.37  E-value: 3.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557729    764 PPGDTLVHAGDLLTALYFISRGSIEILRGD-----VVVAILGKNDIFGEpLNLYARPGKSNGDVRALTYCDLHKIHRDDL 838
Cdd:PRK11753   26 PAKSTLIHAGEKAETLYYIVKGSVAVLIKDeegkeMILSYLNQGDFIGE-LGLFEEGQERSAWVRAKTACEVAEISYKKF 104
                          90       100
                  ....*....|....*....|....*...
gi 4557729    839 LEVLDMYPEFSdhFWSSLEITFNLRDTN 866
Cdd:PRK11753  105 RQLIQVNPDIL--MALSAQMARRLQNTS 130
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
93-135 1.22e-04

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: 40.63  E-value: 1.22e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 4557729       93 KVEIAFYRKDGSCFLCLVDVVPVKNEDGAVIMFILNFEVVMEK 135
Cdd:smart00086    1 TVEYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITER 43
 
Name Accession Description Interval E-value
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
409-668 1.47e-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: 1.47e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557729     409 VWDWLILLLVIYTAVFTPYSAAFLLKEteegppatecgYACQPLAVVDLIVDIMFIVDILINFRTTYVNaneevvshpgr 488
Cdd:pfam00520    3 YFELFILLLILLNTIFLALETYFQPEE-----------PLTTVLEILDYVFTGIFTLEMLLKIIAAGFK----------- 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557729     489 iaVHYFK-GWFLIDMVAAIPFDLLIFGSGSEELIGL--LKTARLLRLVRVARKLDRYSEYGAAVL--FLLMCTFALIAHW 563
Cdd:pfam00520   61 --KRYFRsPWNILDFVVVLPSLISLVLSSVGSLSGLrvLRLLRLLRLLRLIRRLEGLRTLVNSLIrsLKSLGNLLLLLLL 138
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557729     564 LACIWYAIGnMEQPHmdsriGWLHNLGDQIGKPYNSsglggpsikDKYVTALYFTFSSLTSVGFGNVSPNTNSEK----- 638
Cdd:pfam00520  139 FLFIFAIIG-YQLFG-----GKLKTWENPDNGRTNF---------DNFPNAFLWLFQTMTTEGWGDIMYDTIDGKgefwa 203
                          250       260       270
                   ....*....|....*....|....*....|..
gi 4557729     639 --IFSICVMLIGSLMYASIFGNVSAIIQRLYS 668
Cdd:pfam00520  204 yiYFVSFIILGGFLLLNLFIAVIIDNFQELTE 235
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
410-847 6.40e-34

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 141.16  E-value: 6.40e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557729    410 WDWLILLLVIYTAVFTPYSAAFLLKETEEGppatecgyacqpLAVVDLIVDIMFIVDILINFRTTYVNANEEV-VSHPGR 488
Cdd:PLN03192   64 WETLMVVLVAYSAWVYPFEVAFLNASPKRG------------LEIADNVVDLFFAVDIVLTFFVAYIDPRTQLlVRDRKK 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557729    489 IAVHYFKGWFLIDMVAAIPFD---LLIFGS----GSEELIGLLKTARLLRLVRVARKLD---RYSEYGAAVLFLLMCTFA 558
Cdd:PLN03192  132 IAVRYLSTWFLMDVASTIPFQalaYLITGTvklnLSYSLLGLLRFWRLRRVKQLFTRLEkdiRFSYFWIRCARLLSVTLF 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557729    559 LIaHWLACIWYAIGNmEQPHMDSRigWLhnlGDQIgkpynsSGLGGPSIKDKYVTALYFTFSSLTSVGFGNVSPNTNSEK 638
Cdd:PLN03192  212 LV-HCAGCLYYLIAD-RYPHQGKT--WI---GAVI------PNFRETSLWIRYISAIYWSITTMTTVGYGDLHAVNTIEM 278
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557729    639 IFSICVMLIGSLMYASIFGNVSAIIQRLYSGTARYHTQMLRVREFIRFHQIPNPLRQRLEEYFQHAWSYTNgIDMNAVLK 718
Cdd:PLN03192  279 IFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRLKDQILAYMCLRFKAES-LNQQQLID 357
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557729    719 GFPECLQADICLHLNRSLLQHCKPFRGATKGCLRALAMKFKTTHAPPGDTLVHAGDLLTALYFISRGSIEILRGDV---- 794
Cdd:PLN03192  358 QLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEIIDSEGeker 437
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 4557729    795 VVAILGKNDIFGEPLNLYARPGKSNGDVRALTycDLHKIHRDDLLEVLDMYPE 847
Cdd:PLN03192  438 VVGTLGCGDIFGEVGALCCRPQSFTFRTKTLS--QLLRLKTSTLIEAMQTRQE 488
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
742-853 5.37e-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: 97.78  E-value: 5.37e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557729   742 PFRGATKGCLRALAMKFKTTHAPPGDTLVHAGDLLTALYFISRGSIEILRGD-----VVVAILGKNDIFGEPLNLYARPg 816
Cdd:cd00038    1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDedgreQIVGFLGPGDLFGELALLGNGP- 79
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 4557729   817 kSNGDVRALTYCDLHKIHRDDLLEVLDMYPEFSDHFW 853
Cdd:cd00038   80 -RSATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
742-859 8.09e-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: 8.09e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557729      742 PFRGATKGCLRALAMKFKTTHAPPGDTLVHAGDLLTALYFISRGSIEILR-----GDVVVAILGKNDIFGEPLNLYARPG 816
Cdd:smart00100    1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKvledgEEQIVGTLGPGDFFGELALLTNSRR 80
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 4557729      817 KSNGDVRALTYCdlhKIHRDDLLEVLDMYPEFSDHFWSSLEIT 859
Cdd:smart00100   81 AASAAAVALELA---TLLRIDFRDFLQLLPELPQLLLELLLEL 120
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
38-130 5.49e-17

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: 77.12  E-value: 5.49e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557729      38 NCAVIYCNDGFCELCGYSRAEVMQRPCTCDFLHGPRTQRRAAAQIaqalLGAEERKVEIAFYRKDGSCFLCLVDVVPVKN 117
Cdd:pfam13426    1 DGRIIYVNDAALRLLGYTREELLGKSITDLFAEPEDSERLREALR----EGKAVREFEVVLYRKDGEPFPVLVSLAPIRD 76
                           90
                   ....*....|...
gi 4557729     118 EDGAVIMFILNFE 130
Cdd:pfam13426   77 DGGELVGIIAILR 89
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
751-857 6.47e-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: 77.72  E-value: 6.47e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557729   751 LRALAMKFKTTHAPPGDTLVHAGDLLTALYFISRGSIEILRGD-----VVVAILGKNDIFGEPLNLYARPgkSNGDVRAL 825
Cdd:COG0664    9 LEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISedgreQILGFLGPGDFFGELSLLGGEP--SPATAEAL 86
                         90       100       110
                 ....*....|....*....|....*....|..
gi 4557729   826 TYCDLHKIHRDDLLEVLDMYPEFSDHFWSSLE 857
Cdd:COG0664   87 EDSELLRIPREDLEELLERNPELARALLRLLA 118
PAS COG2202
PAS domain [Signal transduction mechanisms];
41-126 8.49e-13

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 69.67  E-value: 8.49e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557729    41 VIYCNDGFCELCGYSRAEVMQRpcTCDFLHGPRTQRRAAAQIAQALLGAEERKVEIAFYRKDGSCFLCLVDVVPVKNEDG 120
Cdd:COG2202   33 ILYVNPAFERLTGYSAEELLGK--TLRDLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGSLFWVELSISPVRDEDG 110

                 ....*.
gi 4557729   121 AVIMFI 126
Cdd:COG2202  111 EITGFV 116
PRK13559 PRK13559
hypothetical protein; Provisional
30-125 4.11e-12

hypothetical protein; Provisional


Pssm-ID: 237427 [Multi-domain]  Cd Length: 361  Bit Score: 69.08  E-value: 4.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557729     30 IIANARVENCAVIYCNDGFCELCGYSRAEVMQRpcTCDFLHGPRTQRRAAAQIAQALLGAEERKVEIAFYRKDGSCFLCL 109
Cdd:PRK13559   57 CITDPHQPDLPIVLANQAFLDLTGYAAEEVVGR--NCRFLQGAATDPIAVAKIRAAIAAEREIVVELLNYRKDGEPFWNA 134
                          90
                  ....*....|....*.
gi 4557729    110 VDVVPVKNEDGAVIMF 125
Cdd:PRK13559  135 LHLGPVYGEDGRLLYF 150
PRK13558 PRK13558
bacterio-opsin activator; Provisional
31-126 4.83e-12

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 70.25  E-value: 4.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557729     31 IANARVENCAVIYCNDGFCELCGYSRAEVMQRpcTCDFLHGPRTQRRAAAQIAQALLGAEERKVEIAFYRKDGSCFLCLV 110
Cdd:PRK13558  163 IADATLPDEPLIYINDAFERITGYSPDEVLGR--NCRFLQGEDTNEERVAELREAIDEERPTSVELRNYRKDGSTFWNQV 240
                          90
                  ....*....|....*.
gi 4557729    111 DVVPVKNEDGAVIMFI 126
Cdd:PRK13558  241 DIAPIRDEDGTVTHYV 256
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
762-845 2.76e-11

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: 60.70  E-value: 2.76e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557729     762 HAPPGDTLVHAGDLLTALYFISRGSIEILR-----GDVVVAILGKNDIFGEPLNLYARPgkSNGDVRALTYCDLHKIHRD 836
Cdd:pfam00027    3 SYKAGEVIFREGDPADSLYIVLSGKVKVYRtledgREQILAVLGPGDFFGELALLGGEP--RSATVVALTDSELLVIPRE 80

                   ....*....
gi 4557729     837 DLLEVLDMY 845
Cdd:pfam00027   81 DFLELLERD 89
Ion_trans_2 pfam07885
Ion channel; This family includes the two membrane helix type ion channels found in bacteria.
611-665 6.84e-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: 59.20  E-value: 6.84e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 4557729     611 YVTALYFTFSSLTSVGFGNVSPNTNSEKIFSICVMLIGSLMYASIFGNVSAIIQR 665
Cdd:pfam07885   24 FLDALYFSFVTLTTVGYGDIVPLTDAGRLFTIFYILIGIPLFAIFLAVLGRFLTE 78
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
41-132 2.96e-08

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: 52.64  E-value: 2.96e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557729    41 VIYCNDGFCELCGYSRAEVMQRPCTcDFLHgPRTQRRAAAQIAQALLGAEERKVEIAFYRKDGSCFLCLVDVVPVKNEDG 120
Cdd:cd00130   14 ILYANPAAEQLLGYSPEELIGKSLL-DLIH-PEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLTPIRDEGG 91
                         90
                 ....*....|..
gi 4557729   121 AVIMFILNFEVV 132
Cdd:cd00130   92 EVIGLLGVVRDI 103
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
764-866 3.39e-08

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 55.37  E-value: 3.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557729    764 PPGDTLVHAGDLLTALYFISRGSIEILRGD-----VVVAILGKNDIFGEpLNLYARPGKSNGDVRALTYCDLHKIHRDDL 838
Cdd:PRK11753   26 PAKSTLIHAGEKAETLYYIVKGSVAVLIKDeegkeMILSYLNQGDFIGE-LGLFEEGQERSAWVRAKTACEVAEISYKKF 104
                          90       100
                  ....*....|....*....|....*...
gi 4557729    839 LEVLDMYPEFSdhFWSSLEITFNLRDTN 866
Cdd:PRK11753  105 RQLIQVNPDIL--MALSAQMARRLQNTS 130
PRK13557 PRK13557
histidine kinase; Provisional
41-125 1.17e-07

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 55.83  E-value: 1.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557729     41 VIYCNDGFCELCGYSRAEVMQRpcTCDFLHGPRTQRRAAAQIAQALLGAEERKVEIAFYRKDGSCFLCLVDVVPVKNEDG 120
Cdd:PRK13557   55 IVFANRAFLEMTGYAAEEIIGN--NCRFLQGPETDRATVAEVRDAIAERREIATEILNYRKDGSSFWNALFVSPVYNDAG 132

                  ....*
gi 4557729    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 ...
41-132 2.19e-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. 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: 50.49  E-value: 2.19e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557729      41 VIYCNDGFCELCGYSRAEVMQRPcTCDFLHGPRTQRRAAAQIAQALLGAEERKVEIAFYRKDGSCFLCLVDVVPVKNEDG 120
Cdd:pfam00989   23 ILYVNAAAEELLGLSREEVIGKS-LLDLIPEEDDAEVAELLRQALLQGEESRGFEVSFRVPDGRPRHVEVRASPVRDAGG 101
                           90
                   ....*....|..
gi 4557729     121 AVIMFILNFEVV 132
Cdd:pfam00989  102 EILGFLGVLRDI 113
PRK10537 PRK10537
voltage-gated potassium channel protein;
497-684 8.58e-06

voltage-gated potassium channel protein;


Pssm-ID: 236711 [Multi-domain]  Cd Length: 393  Bit Score: 49.63  E-value: 8.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557729    497 WFLIDMVAAIPFDLLIFGSGSEELIGLLKTARLLRLVRVARKLDRYSeYGAAVLFLLMCTFALIAhwlaciwYAIgnmeq 576
Cdd:PRK10537   86 WAISILLLLAALAITLHFYPWLKFLIGYCIVLLVALLIYRRDFDRSS-LAAGTLFAVISITSLLF-------YST----- 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557729    577 phmdsrIGWLHnLGDQIGkpynssglggPSIKDkYVTALYFTFSSLTSVGFGNVSPNTNSEKIFSICVMLIGSLMYA--- 653
Cdd:PRK10537  153 ------FGALY-LGDGFS----------PPIES-LSTAFYFSIVTMSTVGYGDIVPVSESARLFTISVIILGITVFAtsi 214
                         170       180       190
                  ....*....|....*....|....*....|...
gi 4557729    654 -SIFGNV-SAIIQRLYSGtaRYHTqMLRVREFI 684
Cdd:PRK10537  215 sAIFGPViRGNLKRLVKG--RISH-MHRKDHFI 244
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
93-135 1.22e-04

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: 40.63  E-value: 1.22e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 4557729       93 KVEIAFYRKDGSCFLCLVDVVPVKNEDGAVIMFILNFEVVMEK 135
Cdd:smart00086    1 TVEYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITER 43
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
37-125 2.11e-04

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 44.84  E-value: 2.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557729    37 ENCAVIYCNDGFCELCGYSRAEVMQRPCTcDFLHGPRTQRRAAAQIAQAllGAEERKVEIAFYRKDGSCFLCLVDVVPVK 116
Cdd:COG3852   25 ADGRITYVNPAAERLLGLSAEELLGRPLA-ELFPEDSPLRELLERALAE--GQPVTEREVTLRRKDGEERPVDVSVSPLR 101
                         90
                 ....*....|..
gi 4557729   117 NEDG---AVIMF 125
Cdd:COG3852  102 DAEGeggVLLVL 113
PAS COG2202
PAS domain [Signal transduction mechanisms];
41-127 4.00e-03

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 40.39  E-value: 4.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557729    41 VIYCNDGFCELCGYSRAEVMQRPCTcDFLHGPRtqRRAAAQIAQALLGAEERKVEIAFYRKDGSCFLCLVDVVPVKNEDG 120
Cdd:COG2202  159 ILYVNPAAEELLGYSPEELLGKSLL-DLLHPED--RERLLELLRRLLEGGRESYELELRLKDGDGRWVWVEASAVPLRDG 235

                 ....*..
gi 4557729   121 AVIMFIL 127
Cdd:COG2202  236 GEVIGVL 242
 
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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