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Conserved domains on  [gi|1034558428|ref|XP_016856735|]
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potassium voltage-gated channel subfamily H member 1 isoform X2 [Homo sapiens]

Protein Classification

cyclic nucleotide-gated ion channel( domain architecture ID 13328258)

cyclic nucleotide-gated ion channel is a nonselective channel that is opened by the direct binding of cyclic nucleotides, cAMP and cGMP

CATH:  2.60.120.10
Gene Ontology:  GO:0016020|GO:0030551|GO:0005216|GO:0006811|GO:0022832
PubMed:  12087135|17601606
SCOP:  4000272
TCDB:  1.A.1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 189-299 9.67e-25

effector domain of the CAP family of transcription factors; members include CAP (or cAMP receptor protein (CRP)), which binds cAMP, FNR (fumarate and nitrate reduction), which uses an iron-sulfur cluster to sense oxygen) and CooA, a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. Cyclic nucleotide-binding domain similar to CAP are also present in cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) and vertebrate cyclic nucleotide-gated ion-channels. Cyclic nucleotide-monophosphate binding domain; proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural domain of about 120 residues; the best studied is the prokaryotic catabolite gene activator, CAP, where such a domain is known to be composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure; three conserved glycine residues are thought to be essential for maintenance of the structural integrity of the beta-barrel; CooA is a homodimeric transcription factor that belongs to CAP family; cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) contain two tandem copies of the cyclic nucleotide-binding domain; cAPK's are composed of two different subunits, a catalytic chain and a regulatory chain, which contains both copies of the domain; cGPK's are single chain enzymes that include the two copies of the domain in their N-terminal section; also found in vertebrate cyclic nucleotide-gated ion-channels


:

Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 98.94  E-value: 9.67e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558428 189 AFRLASDGCLRALAMEFQTVHCAPGDLIYHAGESVDSLCFVVSGSLEVIQDDE-----VVAILGKGDVFGDVFWkeATLA 263
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEdgreqIVGFLGPGDLFGELAL--LGNG 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1034558428 264 QSCANVRALTYCDLHVIKRDALQKVLEFYTAFSHSF 299
Cdd:cd00038    79 PRSATVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
PLN03192 super family cl33658
Voltage-dependent potassium channel; Provisional
 58-255 5.10e-18

Voltage-dependent potassium channel; Provisional


The actual alignment was detected with superfamily member PLN03192:

Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 88.00  E-value: 5.10e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558428  58 YISSLYFTMTSLTSVGFGNIAPSTDIEKIFAVAIMMIGSLLYATIFGNVTTIFQQmyaNTNRYHEMLNSVR---DFLKLY 134
Cdd:PLN03192  251 YISAIYWSITTMTTVGYGDLHAVNTIEMIFIIFYMLFNLGLTAYLIGNMTNLVVE---GTRRTMEFRNSIEaasNFVGRN 327

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558428 135 QVPKGLSERVMDYIVSTWSmSRGIDTEKVLQICPKDMRADICVHLNRKVFKEHPAFRLASDGCLRALAMEFQTVHCAPGD 214
Cdd:PLN03192  328 RLPPRLKDQILAYMCLRFK-AESLNQQQLIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPRE 406

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1034558428 215 LIYHAGESVDSLCFVVSGSLEVI----QDDEVVAILGKGDVFGDV 255
Cdd:PLN03192  407 DVIMQNEAPDDVYIVVSGEVEIIdsegEKERVVGTLGCGDIFGEV 451
 
Name Accession Description Interval E-value
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 189-299 9.67e-25

effector domain of the CAP family of transcription factors; members include CAP (or cAMP receptor protein (CRP)), which binds cAMP, FNR (fumarate and nitrate reduction), which uses an iron-sulfur cluster to sense oxygen) and CooA, a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. Cyclic nucleotide-binding domain similar to CAP are also present in cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) and vertebrate cyclic nucleotide-gated ion-channels. Cyclic nucleotide-monophosphate binding domain; proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural domain of about 120 residues; the best studied is the prokaryotic catabolite gene activator, CAP, where such a domain is known to be composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure; three conserved glycine residues are thought to be essential for maintenance of the structural integrity of the beta-barrel; CooA is a homodimeric transcription factor that belongs to CAP family; cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) contain two tandem copies of the cyclic nucleotide-binding domain; cAPK's are composed of two different subunits, a catalytic chain and a regulatory chain, which contains both copies of the domain; cGPK's are single chain enzymes that include the two copies of the domain in their N-terminal section; also found in vertebrate cyclic nucleotide-gated ion-channels


Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 98.94  E-value: 9.67e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558428 189 AFRLASDGCLRALAMEFQTVHCAPGDLIYHAGESVDSLCFVVSGSLEVIQDDE-----VVAILGKGDVFGDVFWkeATLA 263
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEdgreqIVGFLGPGDLFGELAL--LGNG 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1034558428 264 QSCANVRALTYCDLHVIKRDALQKVLEFYTAFSHSF 299
Cdd:cd00038    79 PRSATVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 190-306 8.10e-20

Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a prokaryotic homologue of eukaryotic cNMP-binding domains, present in ion channels, and cNMP-dependent kinases.


Pssm-ID: 197516 [Multi-domain]  Cd Length: 120  Bit Score: 85.15  E-value: 8.10e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558428  190 FRLASDGCLRALAMEFQTVHCAPGDLIYHAGESVDSLCFVVSGSLEVIQDDE-----VVAILGKGDVFGDvfwkEATLAQ 264
Cdd:smart00100   2 FKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEdgeeqIVGTLGPGDFFGE----LALLTN 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1034558428  265 --SCANVRALTYCdLHVIKRDALQKVLEFYTAFSHSFSRNLILT 306
Cdd:smart00100  78 srRAASAAAVALE-LATLLRIDFRDFLQLLPELPQLLLELLLEL 120
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 58-255 5.10e-18

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 88.00  E-value: 5.10e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558428  58 YISSLYFTMTSLTSVGFGNIAPSTDIEKIFAVAIMMIGSLLYATIFGNVTTIFQQmyaNTNRYHEMLNSVR---DFLKLY 134
Cdd:PLN03192  251 YISAIYWSITTMTTVGYGDLHAVNTIEMIFIIFYMLFNLGLTAYLIGNMTNLVVE---GTRRTMEFRNSIEaasNFVGRN 327

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558428 135 QVPKGLSERVMDYIVSTWSmSRGIDTEKVLQICPKDMRADICVHLNRKVFKEHPAFRLASDGCLRALAMEFQTVHCAPGD 214
Cdd:PLN03192  328 RLPPRLKDQILAYMCLRFK-AESLNQQQLIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPRE 406

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1034558428 215 LIYHAGESVDSLCFVVSGSLEVI----QDDEVVAILGKGDVFGDV 255
Cdd:PLN03192  407 DVIMQNEAPDDVYIVVSGEVEIIdsegEKERVVGTLGCGDIFGEV 451
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 190-303 8.04e-15

cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal transduction mechanisms];


Pssm-ID: 440428 [Multi-domain]  Cd Length: 207  Bit Score: 73.48  E-value: 8.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558428 190 FRLASDGCLRALAMEFQTVHCAPGDLIYHAGESVDSLCFVVSGSLEVIQDDE-----VVAILGKGDVFGDVFWKEATLAQ 264
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEdgreqILGFLGPGDFFGELSLLGGEPSP 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1034558428 265 scANVRALTYCDLHVIKRDALQKVLEFYTAFSHSFSRNL 303
Cdd:COG0664    81 --ATAEALEDSELLRIPREDLEELLERNPELARALLRLL 117
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 208-290 4.60e-14

Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, oxygen and 2-oxoglutarate (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 459637 [Multi-domain]  Cd Length: 89  Bit Score: 67.63  E-value: 4.60e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558428 208 VHCAPGDLIYHAGESVDSLCFVVSGSLEVIQDDE-----VVAILGKGDVFGDVfwkeATLAQSC--ANVRALTYCDLHVI 280
Cdd:pfam00027   2 RSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEdgreqILAVLGPGDFFGEL----ALLGGEPrsATVVALTDSELLVI 77

                          90
                  ....*....|
gi 1034558428 281 KRDALQKVLE 290
Cdd:pfam00027  78 PREDFLELLE 87
Ion_trans_2 pfam07885
Ion channel; This family includes the two membrane helix type ion channels found in bacteria.
 58-112 6.17e-13

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: 64.21  E-value: 6.17e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1034558428  58 YISSLYFTMTSLTSVGFGNIAPSTDIEKIFAVAIMMIGSLLYATIFGNVTTIFQQ 112
Cdd:pfam07885  24 FLDALYFSFVTLTTVGYGDIVPLTDAGRLFTIFYILIGIPLFAIFLAVLGRFLTE 78
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
216-320 4.95e-07

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 50.75  E-value: 4.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558428 216 IYHAGESVDSLCFVVSGSLEVIQDDE-----VVAILGKGDVFGDVFWKEATLAQScANVRALTYCDLHVIKRDALQKVLE 290
Cdd:PRK11753   31 LIHAGEKAETLYYIVKGSVAVLIKDEegkemILSYLNQGDFIGELGLFEEGQERS-AWVRAKTACEVAEISYKKFRQLIQ 109

                          90       100       110
                  ....*....|....*....|....*....|
gi 1034558428 291 FYTAFSHSFSRNLIltynLRKRIVFRKISD 320
Cdd:PRK11753  110 VNPDILMALSAQMA----RRLQNTSRKVGD 135
 
Name Accession Description Interval E-value
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 189-299 9.67e-25

effector domain of the CAP family of transcription factors; members include CAP (or cAMP receptor protein (CRP)), which binds cAMP, FNR (fumarate and nitrate reduction), which uses an iron-sulfur cluster to sense oxygen) and CooA, a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. Cyclic nucleotide-binding domain similar to CAP are also present in cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) and vertebrate cyclic nucleotide-gated ion-channels. Cyclic nucleotide-monophosphate binding domain; proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural domain of about 120 residues; the best studied is the prokaryotic catabolite gene activator, CAP, where such a domain is known to be composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure; three conserved glycine residues are thought to be essential for maintenance of the structural integrity of the beta-barrel; CooA is a homodimeric transcription factor that belongs to CAP family; cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) contain two tandem copies of the cyclic nucleotide-binding domain; cAPK's are composed of two different subunits, a catalytic chain and a regulatory chain, which contains both copies of the domain; cGPK's are single chain enzymes that include the two copies of the domain in their N-terminal section; also found in vertebrate cyclic nucleotide-gated ion-channels


Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 98.94  E-value: 9.67e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558428 189 AFRLASDGCLRALAMEFQTVHCAPGDLIYHAGESVDSLCFVVSGSLEVIQDDE-----VVAILGKGDVFGDVFWkeATLA 263
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEdgreqIVGFLGPGDLFGELAL--LGNG 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1034558428 264 QSCANVRALTYCDLHVIKRDALQKVLEFYTAFSHSF 299
Cdd:cd00038    79 PRSATVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 190-306 8.10e-20

Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a prokaryotic homologue of eukaryotic cNMP-binding domains, present in ion channels, and cNMP-dependent kinases.


Pssm-ID: 197516 [Multi-domain]  Cd Length: 120  Bit Score: 85.15  E-value: 8.10e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558428  190 FRLASDGCLRALAMEFQTVHCAPGDLIYHAGESVDSLCFVVSGSLEVIQDDE-----VVAILGKGDVFGDvfwkEATLAQ 264
Cdd:smart00100   2 FKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEdgeeqIVGTLGPGDFFGE----LALLTN 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1034558428  265 --SCANVRALTYCdLHVIKRDALQKVLEFYTAFSHSFSRNLILT 306
Cdd:smart00100  78 srRAASAAAVALE-LATLLRIDFRDFLQLLPELPQLLLELLLEL 120
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 58-255 5.10e-18

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 88.00  E-value: 5.10e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558428  58 YISSLYFTMTSLTSVGFGNIAPSTDIEKIFAVAIMMIGSLLYATIFGNVTTIFQQmyaNTNRYHEMLNSVR---DFLKLY 134
Cdd:PLN03192  251 YISAIYWSITTMTTVGYGDLHAVNTIEMIFIIFYMLFNLGLTAYLIGNMTNLVVE---GTRRTMEFRNSIEaasNFVGRN 327

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558428 135 QVPKGLSERVMDYIVSTWSmSRGIDTEKVLQICPKDMRADICVHLNRKVFKEHPAFRLASDGCLRALAMEFQTVHCAPGD 214
Cdd:PLN03192  328 RLPPRLKDQILAYMCLRFK-AESLNQQQLIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPRE 406

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1034558428 215 LIYHAGESVDSLCFVVSGSLEVI----QDDEVVAILGKGDVFGDV 255
Cdd:PLN03192  407 DVIMQNEAPDDVYIVVSGEVEIIdsegEKERVVGTLGCGDIFGEV 451
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 190-303 8.04e-15

cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal transduction mechanisms];


Pssm-ID: 440428 [Multi-domain]  Cd Length: 207  Bit Score: 73.48  E-value: 8.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558428 190 FRLASDGCLRALAMEFQTVHCAPGDLIYHAGESVDSLCFVVSGSLEVIQDDE-----VVAILGKGDVFGDVFWKEATLAQ 264
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEdgreqILGFLGPGDFFGELSLLGGEPSP 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1034558428 265 scANVRALTYCDLHVIKRDALQKVLEFYTAFSHSFSRNL 303
Cdd:COG0664    81 --ATAEALEDSELLRIPREDLEELLERNPELARALLRLL 117
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 208-290 4.60e-14

Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, oxygen and 2-oxoglutarate (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 459637 [Multi-domain]  Cd Length: 89  Bit Score: 67.63  E-value: 4.60e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558428 208 VHCAPGDLIYHAGESVDSLCFVVSGSLEVIQDDE-----VVAILGKGDVFGDVfwkeATLAQSC--ANVRALTYCDLHVI 280
Cdd:pfam00027   2 RSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEdgreqILAVLGPGDFFGEL----ALLGGEPrsATVVALTDSELLVI 77

                          90
                  ....*....|
gi 1034558428 281 KRDALQKVLE 290
Cdd:pfam00027  78 PREDFLELLE 87
Ion_trans_2 pfam07885
Ion channel; This family includes the two membrane helix type ion channels found in bacteria.
 58-112 6.17e-13

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: 64.21  E-value: 6.17e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1034558428  58 YISSLYFTMTSLTSVGFGNIAPSTDIEKIFAVAIMMIGSLLYATIFGNVTTIFQQ 112
Cdd:pfam07885  24 FLDALYFSFVTLTTVGYGDIVPLTDAGRLFTIFYILIGIPLFAIFLAVLGRFLTE 78
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
216-320 4.95e-07

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 50.75  E-value: 4.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558428 216 IYHAGESVDSLCFVVSGSLEVIQDDE-----VVAILGKGDVFGDVFWKEATLAQScANVRALTYCDLHVIKRDALQKVLE 290
Cdd:PRK11753   31 LIHAGEKAETLYYIVKGSVAVLIKDEegkemILSYLNQGDFIGELGLFEEGQERS-AWVRAKTACEVAEISYKKFRQLIQ 109

                          90       100       110
                  ....*....|....*....|....*....|
gi 1034558428 291 FYTAFSHSFSRNLIltynLRKRIVFRKISD 320
Cdd:PRK11753  110 VNPDILMALSAQMA----RRLQNTSRKVGD 135
PRK10537 PRK10537
voltage-gated potassium channel protein;
62-106 8.61e-04

voltage-gated potassium channel protein;


Pssm-ID: 236711 [Multi-domain]  Cd Length: 393  Bit Score: 41.93  E-value: 8.61e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1034558428  62 LYFTMTSLTSVGFGNIAPSTDIEKIFAVAIMMIGSLLYAT----IFGNV 106
Cdd:PRK10537  173 FYFSIVTMSTVGYGDIVPVSESARLFTISVIILGITVFATsisaIFGPV 221
 
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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