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Conserved domains on  [gi|26051260|ref|NP_004509|]
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potassium voltage-gated channel subfamily KQT member 2 isoform c [Homo sapiens]

Protein Classification

potassium voltage-gated channel subfamily KQT member 2( domain architecture ID 11999099)

potassium voltage-gated channel subfamily KQT member 2 (KCNQ2) associates with KCNQ3 to form a potassium channel with essentially identical properties to the channel underlying the native M-current, a slowly activating and deactivating potassium conductance which plays a critical role in determining the subthreshold electrical excitability of neurons as well as the responsiveness to synaptic inputs

Gene Ontology:  GO:0005249|GO:0034220|GO:0005267
PubMed:  11836519
TCDB:  1.A.1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KCNQ_channel pfam03520
KCNQ voltage-gated potassium channel; This family matches to the C-terminal tail of KCNQ type ...
 438-623 1.44e-121

KCNQ voltage-gated potassium channel; This family matches to the C-terminal tail of KCNQ type potassium channels.


:

Pssm-ID: 460954  Cd Length: 190  Bit Score: 364.47  E-value: 1.44e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051260   438 SPSADQSLEDSPSKVPKSWSFGDRSRARQAFRIKGAASRQNSEEASLPGEDIVDDKSCPCEFVTEDLTPGLKVSIRAVCV 517
Cdd:pfam03520   1 SPSAEDSIEASPSKVQKSWSFNDRTRFRTSLRLKGSASRQSSEEASGPGEEVAEDKGCHCDFLVEDLIPALKTVIRAVRI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051260   518 MRFLVSKRKFKESLRPYDVMDVIEQYSAGHLDMLSRIKSLQSRVDQIVGRGPAITDKD-RTKGPA---EAELPEDPSMMG 593
Cdd:pfam03520  81 MKFLVAKRKFKETLRPYDVKDVIEQYSAGHLDMLCRIKSLQTRVDQIVGRGPPPTDKKkREKGPKvpaEGDLVEDLSMMG 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 26051260   594 RLGKVEKQVLSMEKKLDFLVNIYMQRMGIP 623
Cdd:pfam03520 161 RVVKVEKQVQSIEKKLDFLLDIYSQCLRKG 190
KCNQC3-Ank-G_bd pfam11956
Ankyrin-G binding motif of KCNQ2-3; Interactions with ankyrin-G are crucial to the ...
 740-840 2.52e-59

Ankyrin-G binding motif of KCNQ2-3; Interactions with ankyrin-G are crucial to the localization of voltage-gated sodium channels (VGSCs) at the axon initial segment and for neurons to initiate action potentials. This conserved 9-amino acid motif ((V/A)P(I/L)AXXE(S/D)D) is required for ankyrin-G binding and functions to localize sodium channels to a variety of 'excitable' membrane domains both inside and outside of the nervous system. This motif has also been identified in the potassium channel 6TM proteins KCNQ2 and KCNQ3, that correspond to the M channels that exert a crucial influence over neuronal excitability. KCNQ2/KCNQ3 channels are preferentially localized to the surface of axons both at the axonal initial segment and more distally, and this axonal initial segment targeting of surface KCNQ channels is mediated by these ankyrin-G binding motifs of KCNQ2 and KCNQ3. KCNQ3 is a major determinant of M channel localization to the AIS, rather than KCNQ2. Phylogenetic analysis reveals that anchor motifs evolved sequentially in chordates (NaV channel) and jawed vertebrates (KCNQ2/3).


:

Pssm-ID: 463411  Cd Length: 101  Bit Score: 196.54  E-value: 2.52e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051260   740 QEDTPGCRPPEGNLRDSDTSISIPSVDHEELERSFSGFSISQSKENLDALN-SCYAAVAPCAKVRPYIAEGESDTDSDLC 818
Cdd:pfam11956   1 LQDLSGGRGRTTALRDSDTPLSILSVNHEELERSPSGFSISQSRENLDFLNnGCAAGVAPWTRVRPYLAEGETDTDTDPF 80

                          90       100
                  ....*....|....*....|..
gi 26051260   819 TPCGPPPRSATGEGpFGDVGWA 840
Cdd:pfam11956  81 TPSGPPPLSSTGEG-FGDMGWS 101
KCNQ2_u3 pfam16642
Unstructured region on Potassium channel subunit alpha KvLQT2; KCNQ2_u3 is a region of ...
 637-728 6.06e-52

Unstructured region on Potassium channel subunit alpha KvLQT2; KCNQ2_u3 is a region of natively unstructured sequence on potassium voltage-gated channel subfamily KQT member 2 proteins from higher eukaryotes. It lies between families KCNQ_channel, pfam03520, and KCNQC3-Ank_bd, pfam11956. The function is not known.


:

Pssm-ID: 465213  Cd Length: 98  Bit Score: 176.21  E-value: 6.06e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051260   637 EPAPPYHSPEDSREHVDRHGCIVKIVRSSSSTGQKNFSAPP--AAPPVQCPPSTSWQPQSHPRQG----HGTSPVGDHGS 710
Cdd:pfam16642   1 DPAPPYHSPEDSREHKDKNGCITKIIRSTSSMGQKNFSAPPapAVPHSHCPPSTSWQQQLQHPYGrsmsHGSSPVGDPGS 80

                          90
                  ....*....|....*...
gi 26051260   711 LVRIPPPPAHERSLSAYG 728
Cdd:pfam16642  81 LVRIPPPPAHERSLSAYS 98
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 92-324 7.31e-41

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: 150.11  E-value: 7.31e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051260    92 AFIYHAYVFLLVFSCLVLSVFSTIKEYEKSSEGALYILEIVTIVVFGVEYFVRIWAAGCCCRYrgwrgrlkfARKPFCVI 171
Cdd:pfam00520   1 SRYFELFILLLILLNTIFLALETYFQPEEPLTTVLEILDYVFTGIFTLEMLLKIIAAGFKKRY---------FRSPWNIL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051260   172 DIMVLIASIAVLAAGSQGNVFatsALRSLRFLQILRMIRMDRRGGTWKLLGSVVYAHSKELVTAWYIGFLCLILASFLVY 251
Cdd:pfam00520  72 DFVVVLPSLISLVLSSVGSLS---GLRVLRLLRLLRLLRLIRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLFIFAIIGY 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051260   252 LAEKG----------ENDHFDTYADALWWGLITLTTIGYGDKYPQTWNGR-------LLAATFTLIGVSFFALPAGILGS 314
Cdd:pfam00520 149 QLFGGklktwenpdnGRTNFDNFPNAFLWLFQTMTTEGWGDIMYDTIDGKgefwayiYFVSFIILGGFLLLNLFIAVIID 228

                         250
                  ....*....|
gi 26051260   315 GFALKVQEQH 324
Cdd:pfam00520 229 NFQELTERTE 238
 
Name Accession Description Interval E-value
KCNQ_channel pfam03520
KCNQ voltage-gated potassium channel; This family matches to the C-terminal tail of KCNQ type ...
 438-623 1.44e-121

KCNQ voltage-gated potassium channel; This family matches to the C-terminal tail of KCNQ type potassium channels.


Pssm-ID: 460954  Cd Length: 190  Bit Score: 364.47  E-value: 1.44e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051260   438 SPSADQSLEDSPSKVPKSWSFGDRSRARQAFRIKGAASRQNSEEASLPGEDIVDDKSCPCEFVTEDLTPGLKVSIRAVCV 517
Cdd:pfam03520   1 SPSAEDSIEASPSKVQKSWSFNDRTRFRTSLRLKGSASRQSSEEASGPGEEVAEDKGCHCDFLVEDLIPALKTVIRAVRI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051260   518 MRFLVSKRKFKESLRPYDVMDVIEQYSAGHLDMLSRIKSLQSRVDQIVGRGPAITDKD-RTKGPA---EAELPEDPSMMG 593
Cdd:pfam03520  81 MKFLVAKRKFKETLRPYDVKDVIEQYSAGHLDMLCRIKSLQTRVDQIVGRGPPPTDKKkREKGPKvpaEGDLVEDLSMMG 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 26051260   594 RLGKVEKQVLSMEKKLDFLVNIYMQRMGIP 623
Cdd:pfam03520 161 RVVKVEKQVQSIEKKLDFLLDIYSQCLRKG 190
KCNQC3-Ank-G_bd pfam11956
Ankyrin-G binding motif of KCNQ2-3; Interactions with ankyrin-G are crucial to the ...
 740-840 2.52e-59

Ankyrin-G binding motif of KCNQ2-3; Interactions with ankyrin-G are crucial to the localization of voltage-gated sodium channels (VGSCs) at the axon initial segment and for neurons to initiate action potentials. This conserved 9-amino acid motif ((V/A)P(I/L)AXXE(S/D)D) is required for ankyrin-G binding and functions to localize sodium channels to a variety of 'excitable' membrane domains both inside and outside of the nervous system. This motif has also been identified in the potassium channel 6TM proteins KCNQ2 and KCNQ3, that correspond to the M channels that exert a crucial influence over neuronal excitability. KCNQ2/KCNQ3 channels are preferentially localized to the surface of axons both at the axonal initial segment and more distally, and this axonal initial segment targeting of surface KCNQ channels is mediated by these ankyrin-G binding motifs of KCNQ2 and KCNQ3. KCNQ3 is a major determinant of M channel localization to the AIS, rather than KCNQ2. Phylogenetic analysis reveals that anchor motifs evolved sequentially in chordates (NaV channel) and jawed vertebrates (KCNQ2/3).


Pssm-ID: 463411  Cd Length: 101  Bit Score: 196.54  E-value: 2.52e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051260   740 QEDTPGCRPPEGNLRDSDTSISIPSVDHEELERSFSGFSISQSKENLDALN-SCYAAVAPCAKVRPYIAEGESDTDSDLC 818
Cdd:pfam11956   1 LQDLSGGRGRTTALRDSDTPLSILSVNHEELERSPSGFSISQSRENLDFLNnGCAAGVAPWTRVRPYLAEGETDTDTDPF 80

                          90       100
                  ....*....|....*....|..
gi 26051260   819 TPCGPPPRSATGEGpFGDVGWA 840
Cdd:pfam11956  81 TPSGPPPLSSTGEG-FGDMGWS 101
KCNQ2_u3 pfam16642
Unstructured region on Potassium channel subunit alpha KvLQT2; KCNQ2_u3 is a region of ...
 637-728 6.06e-52

Unstructured region on Potassium channel subunit alpha KvLQT2; KCNQ2_u3 is a region of natively unstructured sequence on potassium voltage-gated channel subfamily KQT member 2 proteins from higher eukaryotes. It lies between families KCNQ_channel, pfam03520, and KCNQC3-Ank_bd, pfam11956. The function is not known.


Pssm-ID: 465213  Cd Length: 98  Bit Score: 176.21  E-value: 6.06e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051260   637 EPAPPYHSPEDSREHVDRHGCIVKIVRSSSSTGQKNFSAPP--AAPPVQCPPSTSWQPQSHPRQG----HGTSPVGDHGS 710
Cdd:pfam16642   1 DPAPPYHSPEDSREHKDKNGCITKIIRSTSSMGQKNFSAPPapAVPHSHCPPSTSWQQQLQHPYGrsmsHGSSPVGDPGS 80

                          90
                  ....*....|....*...
gi 26051260   711 LVRIPPPPAHERSLSAYG 728
Cdd:pfam16642  81 LVRIPPPPAHERSLSAYS 98
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 92-324 7.31e-41

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: 150.11  E-value: 7.31e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051260    92 AFIYHAYVFLLVFSCLVLSVFSTIKEYEKSSEGALYILEIVTIVVFGVEYFVRIWAAGCCCRYrgwrgrlkfARKPFCVI 171
Cdd:pfam00520   1 SRYFELFILLLILLNTIFLALETYFQPEEPLTTVLEILDYVFTGIFTLEMLLKIIAAGFKKRY---------FRSPWNIL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051260   172 DIMVLIASIAVLAAGSQGNVFatsALRSLRFLQILRMIRMDRRGGTWKLLGSVVYAHSKELVTAWYIGFLCLILASFLVY 251
Cdd:pfam00520  72 DFVVVLPSLISLVLSSVGSLS---GLRVLRLLRLLRLLRLIRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLFIFAIIGY 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051260   252 LAEKG----------ENDHFDTYADALWWGLITLTTIGYGDKYPQTWNGR-------LLAATFTLIGVSFFALPAGILGS 314
Cdd:pfam00520 149 QLFGGklktwenpdnGRTNFDNFPNAFLWLFQTMTTEGWGDIMYDTIDGKgefwayiYFVSFIILGGFLLLNLFIAVIID 228

                         250
                  ....*....|
gi 26051260   315 GFALKVQEQH 324
Cdd:pfam00520 229 NFQELTERTE 238
 
Name Accession Description Interval E-value
KCNQ_channel pfam03520
KCNQ voltage-gated potassium channel; This family matches to the C-terminal tail of KCNQ type ...
 438-623 1.44e-121

KCNQ voltage-gated potassium channel; This family matches to the C-terminal tail of KCNQ type potassium channels.


Pssm-ID: 460954  Cd Length: 190  Bit Score: 364.47  E-value: 1.44e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051260   438 SPSADQSLEDSPSKVPKSWSFGDRSRARQAFRIKGAASRQNSEEASLPGEDIVDDKSCPCEFVTEDLTPGLKVSIRAVCV 517
Cdd:pfam03520   1 SPSAEDSIEASPSKVQKSWSFNDRTRFRTSLRLKGSASRQSSEEASGPGEEVAEDKGCHCDFLVEDLIPALKTVIRAVRI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051260   518 MRFLVSKRKFKESLRPYDVMDVIEQYSAGHLDMLSRIKSLQSRVDQIVGRGPAITDKD-RTKGPA---EAELPEDPSMMG 593
Cdd:pfam03520  81 MKFLVAKRKFKETLRPYDVKDVIEQYSAGHLDMLCRIKSLQTRVDQIVGRGPPPTDKKkREKGPKvpaEGDLVEDLSMMG 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 26051260   594 RLGKVEKQVLSMEKKLDFLVNIYMQRMGIP 623
Cdd:pfam03520 161 RVVKVEKQVQSIEKKLDFLLDIYSQCLRKG 190
KCNQC3-Ank-G_bd pfam11956
Ankyrin-G binding motif of KCNQ2-3; Interactions with ankyrin-G are crucial to the ...
 740-840 2.52e-59

Ankyrin-G binding motif of KCNQ2-3; Interactions with ankyrin-G are crucial to the localization of voltage-gated sodium channels (VGSCs) at the axon initial segment and for neurons to initiate action potentials. This conserved 9-amino acid motif ((V/A)P(I/L)AXXE(S/D)D) is required for ankyrin-G binding and functions to localize sodium channels to a variety of 'excitable' membrane domains both inside and outside of the nervous system. This motif has also been identified in the potassium channel 6TM proteins KCNQ2 and KCNQ3, that correspond to the M channels that exert a crucial influence over neuronal excitability. KCNQ2/KCNQ3 channels are preferentially localized to the surface of axons both at the axonal initial segment and more distally, and this axonal initial segment targeting of surface KCNQ channels is mediated by these ankyrin-G binding motifs of KCNQ2 and KCNQ3. KCNQ3 is a major determinant of M channel localization to the AIS, rather than KCNQ2. Phylogenetic analysis reveals that anchor motifs evolved sequentially in chordates (NaV channel) and jawed vertebrates (KCNQ2/3).


Pssm-ID: 463411  Cd Length: 101  Bit Score: 196.54  E-value: 2.52e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051260   740 QEDTPGCRPPEGNLRDSDTSISIPSVDHEELERSFSGFSISQSKENLDALN-SCYAAVAPCAKVRPYIAEGESDTDSDLC 818
Cdd:pfam11956   1 LQDLSGGRGRTTALRDSDTPLSILSVNHEELERSPSGFSISQSRENLDFLNnGCAAGVAPWTRVRPYLAEGETDTDTDPF 80

                          90       100
                  ....*....|....*....|..
gi 26051260   819 TPCGPPPRSATGEGpFGDVGWA 840
Cdd:pfam11956  81 TPSGPPPLSSTGEG-FGDMGWS 101
KCNQ2_u3 pfam16642
Unstructured region on Potassium channel subunit alpha KvLQT2; KCNQ2_u3 is a region of ...
 637-728 6.06e-52

Unstructured region on Potassium channel subunit alpha KvLQT2; KCNQ2_u3 is a region of natively unstructured sequence on potassium voltage-gated channel subfamily KQT member 2 proteins from higher eukaryotes. It lies between families KCNQ_channel, pfam03520, and KCNQC3-Ank_bd, pfam11956. The function is not known.


Pssm-ID: 465213  Cd Length: 98  Bit Score: 176.21  E-value: 6.06e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051260   637 EPAPPYHSPEDSREHVDRHGCIVKIVRSSSSTGQKNFSAPP--AAPPVQCPPSTSWQPQSHPRQG----HGTSPVGDHGS 710
Cdd:pfam16642   1 DPAPPYHSPEDSREHKDKNGCITKIIRSTSSMGQKNFSAPPapAVPHSHCPPSTSWQQQLQHPYGrsmsHGSSPVGDPGS 80

                          90
                  ....*....|....*...
gi 26051260   711 LVRIPPPPAHERSLSAYG 728
Cdd:pfam16642  81 LVRIPPPPAHERSLSAYS 98
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 92-324 7.31e-41

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: 150.11  E-value: 7.31e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051260    92 AFIYHAYVFLLVFSCLVLSVFSTIKEYEKSSEGALYILEIVTIVVFGVEYFVRIWAAGCCCRYrgwrgrlkfARKPFCVI 171
Cdd:pfam00520   1 SRYFELFILLLILLNTIFLALETYFQPEEPLTTVLEILDYVFTGIFTLEMLLKIIAAGFKKRY---------FRSPWNIL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051260   172 DIMVLIASIAVLAAGSQGNVFatsALRSLRFLQILRMIRMDRRGGTWKLLGSVVYAHSKELVTAWYIGFLCLILASFLVY 251
Cdd:pfam00520  72 DFVVVLPSLISLVLSSVGSLS---GLRVLRLLRLLRLLRLIRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLFIFAIIGY 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051260   252 LAEKG----------ENDHFDTYADALWWGLITLTTIGYGDKYPQTWNGR-------LLAATFTLIGVSFFALPAGILGS 314
Cdd:pfam00520 149 QLFGGklktwenpdnGRTNFDNFPNAFLWLFQTMTTEGWGDIMYDTIDGKgefwayiYFVSFIILGGFLLLNLFIAVIID 228

                         250
                  ....*....|
gi 26051260   315 GFALKVQEQH 324
Cdd:pfam00520 229 NFQELTERTE 238
Ion_trans_2 pfam07885
Ion channel; This family includes the two membrane helix type ion channels found in bacteria.
 240-314 1.34e-14

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: 69.60  E-value: 1.34e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26051260   240 FLCLILASFLVYLAEKGENDHFDtyadALWWGLITLTTIGYGDKYPQTWNGRLLAATFTLIGVSFFALPAGILGS 314
Cdd:pfam07885   4 LLVLIFGTVYYLLEEGWEWSFLD----ALYFSFVTLTTVGYGDIVPLTDAGRLFTIFYILIGIPLFAIFLAVLGR 74
 
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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