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Conserved domains on  [gi|242090617|ref|XP_002441141|]
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potassium channel AKT2 [Sorghum bicolor]

Protein Classification

ion transporter; cyclic nucleotide-gated ion channel family protein( domain architecture ID 11477558)

ion transporter such as a voltage-gated cation channel, which enables the selective translocation of cations such as sodium, calcium, or potassium, across cell membranes; cyclic nucleotide-gated ion channel is a nonselective channel that is opened by the direct binding of cyclic nucleotides, cAMP and cGMP

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 24-828 0e+00

Voltage-dependent potassium channel; Provisional


:

Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 1639.59  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617  24 FNLRNLSKVILPPLGGPSgQSQSHGGSDKWVISPLDSRYRWWDTLMVVLVAYSAWVYPFEVAFMNASPKGGLEVADIVVD 103
Cdd:PLN03192  24 LSLRNLSKVILPPLGVPS-YNQNHIGSDGWIISPMDSRYRWWETLMVVLVAYSAWVYPFEVAFLNASPKRGLEIADNVVD 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617 104 LFFAVDIVLTFFVAYIDHRTQLLVRDRRKITLRYLSTFFIMDVASTIPFQGLAYLVTGEVRENAAYSMLGVLRLWRLRRV 183
Cdd:PLN03192 103 LFFAVDIVLTFFVAYIDPRTQLLVRDRKKIAVRYLSTWFLMDVASTIPFQALAYLITGTVKLNLSYSLLGLLRFWRLRRV 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617 184 KQFFTRLEKDIRFSYFWIRCARLVAVTLFLVHCAGCLYYLIADRYPHREKTWIGAVIPNFRQASLRIRYISSIYWSITTM 263
Cdd:PLN03192 183 KQLFTRLEKDIRFSYFWIRCARLLSVTLFLVHCAGCLYYLIADRYPHQGKTWIGAVIPNFRETSLWIRYISAIYWSITTM 262

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617 264 TTVGYGDLHAENTVEMIFNIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIRAASSFVGRNHLPPRLKQQILAYMC 343
Cdd:PLN03192 263 TTVGYGDLHAVNTIEMIFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRLKDQILAYMC 342

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617 344 LKFRAESLNQQQLMDQLPKSICKSICEHLFVPVVKDVYLFNGVSREMLLSLVTKMKPEYIPPKEDVIVQNEAPDDVYVVV 423
Cdd:PLN03192 343 LRFKAESLNQQQLIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVV 422

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617 424 SGEVEVILFNGIDEHVKATLGTRDIFGEVSALSDRAQAFTFRTRTLSQLLRLKQATLKEAMQSRPEDSVVIIKNFLKHQV 503
Cdd:PLN03192 423 SGEVEIIDSEGEKERVVGTLGCGDIFGEVGALCCRPQSFTFRTKTLSQLLRLKTSTLIEAMQTRQEDNVVILKNFLQHHK 502

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617 504 EMHGMKADDLLGDNTGEHDD---DANVLTVAAMGNSGLLEDLLRAGKDADVGDAKGRTALHIAASNGYEDCVLVLLKHAC 580
Cdd:PLN03192 503 ELHDLNVGDLLGDNGGEHDDpnmASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHAC 582

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617 581 NVNIKDAQGNTAMWNAIAAGHHKIFNILYHFARASNPHAGGDVLCFAARRGDLGALRELLKLGLDVDSEDHDGATALRVA 660
Cdd:PLN03192 583 NVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVA 662

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617 661 MAEGHADAARFLIMNGASVDKASLDDDgsgsgaarltMSPTELRELLQKRELGHSITIVDS-PAVIPDGGSSGHSRPGRL 739
Cdd:PLN03192 663 MAEDHVDMVRLLIMNGADVDKANTDDD----------FSPTELRELLQKRELGHSITIVDSvPADEPDLGRDGGSRPGRL 732

                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617 740 QGTSSDNQCWPRVSVYKGHPFLRNR--SSEAGKLINLPGTLEEFKAIVGEKLKVDAKKGLIVNDEGAEIDSIDVIRDNDK 817
Cdd:PLN03192 733 QGTSSDNQCRPRVSIYKGHPLLRNErcCNEAGKLINLPPSLEELKAIAGEKLGFDARKAMVTNEEGAEIDSIEVIRDNDK 812

                        810
                 ....*....|.
gi 242090617 818 LFVVTEEDLRR 828
Cdd:PLN03192 813 LFVVEDEDSRR 823
 
Name Accession Description Interval E-value
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 24-828 0e+00

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 1639.59  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617  24 FNLRNLSKVILPPLGGPSgQSQSHGGSDKWVISPLDSRYRWWDTLMVVLVAYSAWVYPFEVAFMNASPKGGLEVADIVVD 103
Cdd:PLN03192  24 LSLRNLSKVILPPLGVPS-YNQNHIGSDGWIISPMDSRYRWWETLMVVLVAYSAWVYPFEVAFLNASPKRGLEIADNVVD 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617 104 LFFAVDIVLTFFVAYIDHRTQLLVRDRRKITLRYLSTFFIMDVASTIPFQGLAYLVTGEVRENAAYSMLGVLRLWRLRRV 183
Cdd:PLN03192 103 LFFAVDIVLTFFVAYIDPRTQLLVRDRKKIAVRYLSTWFLMDVASTIPFQALAYLITGTVKLNLSYSLLGLLRFWRLRRV 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617 184 KQFFTRLEKDIRFSYFWIRCARLVAVTLFLVHCAGCLYYLIADRYPHREKTWIGAVIPNFRQASLRIRYISSIYWSITTM 263
Cdd:PLN03192 183 KQLFTRLEKDIRFSYFWIRCARLLSVTLFLVHCAGCLYYLIADRYPHQGKTWIGAVIPNFRETSLWIRYISAIYWSITTM 262

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617 264 TTVGYGDLHAENTVEMIFNIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIRAASSFVGRNHLPPRLKQQILAYMC 343
Cdd:PLN03192 263 TTVGYGDLHAVNTIEMIFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRLKDQILAYMC 342

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617 344 LKFRAESLNQQQLMDQLPKSICKSICEHLFVPVVKDVYLFNGVSREMLLSLVTKMKPEYIPPKEDVIVQNEAPDDVYVVV 423
Cdd:PLN03192 343 LRFKAESLNQQQLIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVV 422

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617 424 SGEVEVILFNGIDEHVKATLGTRDIFGEVSALSDRAQAFTFRTRTLSQLLRLKQATLKEAMQSRPEDSVVIIKNFLKHQV 503
Cdd:PLN03192 423 SGEVEIIDSEGEKERVVGTLGCGDIFGEVGALCCRPQSFTFRTKTLSQLLRLKTSTLIEAMQTRQEDNVVILKNFLQHHK 502

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617 504 EMHGMKADDLLGDNTGEHDD---DANVLTVAAMGNSGLLEDLLRAGKDADVGDAKGRTALHIAASNGYEDCVLVLLKHAC 580
Cdd:PLN03192 503 ELHDLNVGDLLGDNGGEHDDpnmASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHAC 582

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617 581 NVNIKDAQGNTAMWNAIAAGHHKIFNILYHFARASNPHAGGDVLCFAARRGDLGALRELLKLGLDVDSEDHDGATALRVA 660
Cdd:PLN03192 583 NVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVA 662

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617 661 MAEGHADAARFLIMNGASVDKASLDDDgsgsgaarltMSPTELRELLQKRELGHSITIVDS-PAVIPDGGSSGHSRPGRL 739
Cdd:PLN03192 663 MAEDHVDMVRLLIMNGADVDKANTDDD----------FSPTELRELLQKRELGHSITIVDSvPADEPDLGRDGGSRPGRL 732

                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617 740 QGTSSDNQCWPRVSVYKGHPFLRNR--SSEAGKLINLPGTLEEFKAIVGEKLKVDAKKGLIVNDEGAEIDSIDVIRDNDK 817
Cdd:PLN03192 733 QGTSSDNQCRPRVSIYKGHPLLRNErcCNEAGKLINLPPSLEELKAIAGEKLGFDARKAMVTNEEGAEIDSIEVIRDNDK 812

                        810
                 ....*....|.
gi 242090617 818 LFVVTEEDLRR 828
Cdd:PLN03192 813 LFVVEDEDSRR 823
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 62-312 3.65e-45

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: 162.44  E-value: 3.65e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617   62 YRWWDTLMVVLVAYSAWVYPFEVAFMNASP-KGGLEVADIVVDLFFAVDIVLTFFVAYIDhrtqllvrdrrkitLRYL-S 139
Cdd:pfam00520   1 SRYFELFILLLILLNTIFLALETYFQPEEPlTTVLEILDYVFTGIFTLEMLLKIIAAGFK--------------KRYFrS 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617  140 TFFIMDVASTIPfqglaYLVTGEVRENAAYSMLGVLRLWRLRRVKQFFTRLEKDIRFSYFWIRCARLVAVTLFLVHCAGC 219
Cdd:pfam00520  67 PWNILDFVVVLP-----SLISLVLSSVGSLSGLRVLRLLRLLRLLRLIRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLF 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617  220 LYYLIADRYPH-REKTWIGAV--IPNFRqaslriRYISSIYWSITTMTTVGYGDLHAENTVEM-------IFNIFYMLFN 289
Cdd:pfam00520 142 IFAIIGYQLFGgKLKTWENPDngRTNFD------NFPNAFLWLFQTMTTEGWGDIMYDTIDGKgefwayiYFVSFIILGG 215

                         250       260
                  ....*....|....*....|...
gi 242090617  290 LGLTAYLIGNMTNLVVEGTRRTM 312
Cdd:pfam00520 216 FLLLNLFIAVIIDNFQELTERTE 238
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
516-712 3.07e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 112.35  E-value: 3.07e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617 516 DNTGEHDDDANVLTVAAMGNSGLLEDLLRAGKDADVGDAKGRTALHIAASNGYEDCVLVLLKHACNVNIKDAQGNTAMWN 595
Cdd:COG0666   80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617 596 AIAAGHHKIFNILyhFARASNPHA----GGDVLCFAARRGDLGALRELLKLGLDVDSEDHDGATALRVAMAEGHADAARF 671
Cdd:COG0666  160 AAANGNLEIVKLL--LEAGADVNArdndGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKL 237

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 242090617 672 LIMNGASVDKASLDDDGSGSGAARLTMSPTELRELLQKREL 712
Cdd:COG0666  238 LLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 382-495 1.12e-21

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: 90.85  E-value: 1.12e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617 382 LFNGVSREMLLSLVTKMKPEYIPPKEDVIVQNEAPDDVYVVVSGEVEVI-LFNGIDEHVKATLGTRDIFGEVSALSDRAQ 460
Cdd:cd00038    1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYkLDEDGREQIVGFLGPGDLFGELALLGNGPR 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 242090617 461 AFTFRTRTLSQLLRLKQATLKEAMQSRPEDSVVII 495
Cdd:cd00038   81 SATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 382-498 2.49e-18

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: 81.68  E-value: 2.49e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617   382 LFNGVSREMLLSLVTKMKPEYIPPKEDVIVQNEAPDDVYVVVSGEVEVI-LFNGIDEHVKATLGTRDIFGEVSALSD--R 458
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYkVLEDGEEQIVGTLGPGDFFGELALLTNsrR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 242090617   459 AQAFTFRTRTLSQLLRLKQATLKEAMQSRPEDSVVIIKNF 498
Cdd:smart00100  81 AASAAAVALELATLLRIDFRDFLQLLPELPQLLLELLLEL 120
 
Name Accession Description Interval E-value
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 24-828 0e+00

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 1639.59  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617  24 FNLRNLSKVILPPLGGPSgQSQSHGGSDKWVISPLDSRYRWWDTLMVVLVAYSAWVYPFEVAFMNASPKGGLEVADIVVD 103
Cdd:PLN03192  24 LSLRNLSKVILPPLGVPS-YNQNHIGSDGWIISPMDSRYRWWETLMVVLVAYSAWVYPFEVAFLNASPKRGLEIADNVVD 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617 104 LFFAVDIVLTFFVAYIDHRTQLLVRDRRKITLRYLSTFFIMDVASTIPFQGLAYLVTGEVRENAAYSMLGVLRLWRLRRV 183
Cdd:PLN03192 103 LFFAVDIVLTFFVAYIDPRTQLLVRDRKKIAVRYLSTWFLMDVASTIPFQALAYLITGTVKLNLSYSLLGLLRFWRLRRV 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617 184 KQFFTRLEKDIRFSYFWIRCARLVAVTLFLVHCAGCLYYLIADRYPHREKTWIGAVIPNFRQASLRIRYISSIYWSITTM 263
Cdd:PLN03192 183 KQLFTRLEKDIRFSYFWIRCARLLSVTLFLVHCAGCLYYLIADRYPHQGKTWIGAVIPNFRETSLWIRYISAIYWSITTM 262

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617 264 TTVGYGDLHAENTVEMIFNIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIRAASSFVGRNHLPPRLKQQILAYMC 343
Cdd:PLN03192 263 TTVGYGDLHAVNTIEMIFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRLKDQILAYMC 342

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617 344 LKFRAESLNQQQLMDQLPKSICKSICEHLFVPVVKDVYLFNGVSREMLLSLVTKMKPEYIPPKEDVIVQNEAPDDVYVVV 423
Cdd:PLN03192 343 LRFKAESLNQQQLIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVV 422

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617 424 SGEVEVILFNGIDEHVKATLGTRDIFGEVSALSDRAQAFTFRTRTLSQLLRLKQATLKEAMQSRPEDSVVIIKNFLKHQV 503
Cdd:PLN03192 423 SGEVEIIDSEGEKERVVGTLGCGDIFGEVGALCCRPQSFTFRTKTLSQLLRLKTSTLIEAMQTRQEDNVVILKNFLQHHK 502

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617 504 EMHGMKADDLLGDNTGEHDD---DANVLTVAAMGNSGLLEDLLRAGKDADVGDAKGRTALHIAASNGYEDCVLVLLKHAC 580
Cdd:PLN03192 503 ELHDLNVGDLLGDNGGEHDDpnmASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHAC 582

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617 581 NVNIKDAQGNTAMWNAIAAGHHKIFNILYHFARASNPHAGGDVLCFAARRGDLGALRELLKLGLDVDSEDHDGATALRVA 660
Cdd:PLN03192 583 NVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVA 662

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617 661 MAEGHADAARFLIMNGASVDKASLDDDgsgsgaarltMSPTELRELLQKRELGHSITIVDS-PAVIPDGGSSGHSRPGRL 739
Cdd:PLN03192 663 MAEDHVDMVRLLIMNGADVDKANTDDD----------FSPTELRELLQKRELGHSITIVDSvPADEPDLGRDGGSRPGRL 732

                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617 740 QGTSSDNQCWPRVSVYKGHPFLRNR--SSEAGKLINLPGTLEEFKAIVGEKLKVDAKKGLIVNDEGAEIDSIDVIRDNDK 817
Cdd:PLN03192 733 QGTSSDNQCRPRVSIYKGHPLLRNErcCNEAGKLINLPPSLEELKAIAGEKLGFDARKAMVTNEEGAEIDSIEVIRDNDK 812

                        810
                 ....*....|.
gi 242090617 818 LFVVTEEDLRR 828
Cdd:PLN03192 813 LFVVEDEDSRR 823
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 62-312 3.65e-45

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: 162.44  E-value: 3.65e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617   62 YRWWDTLMVVLVAYSAWVYPFEVAFMNASP-KGGLEVADIVVDLFFAVDIVLTFFVAYIDhrtqllvrdrrkitLRYL-S 139
Cdd:pfam00520   1 SRYFELFILLLILLNTIFLALETYFQPEEPlTTVLEILDYVFTGIFTLEMLLKIIAAGFK--------------KRYFrS 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617  140 TFFIMDVASTIPfqglaYLVTGEVRENAAYSMLGVLRLWRLRRVKQFFTRLEKDIRFSYFWIRCARLVAVTLFLVHCAGC 219
Cdd:pfam00520  67 PWNILDFVVVLP-----SLISLVLSSVGSLSGLRVLRLLRLLRLLRLIRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLF 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617  220 LYYLIADRYPH-REKTWIGAV--IPNFRqaslriRYISSIYWSITTMTTVGYGDLHAENTVEM-------IFNIFYMLFN 289
Cdd:pfam00520 142 IFAIIGYQLFGgKLKTWENPDngRTNFD------NFPNAFLWLFQTMTTEGWGDIMYDTIDGKgefwayiYFVSFIILGG 215

                         250       260
                  ....*....|....*....|...
gi 242090617  290 LGLTAYLIGNMTNLVVEGTRRTM 312
Cdd:pfam00520 216 FLLLNLFIAVIIDNFQELTERTE 238
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
516-712 3.07e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 112.35  E-value: 3.07e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617 516 DNTGEHDDDANVLTVAAMGNSGLLEDLLRAGKDADVGDAKGRTALHIAASNGYEDCVLVLLKHACNVNIKDAQGNTAMWN 595
Cdd:COG0666   80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617 596 AIAAGHHKIFNILyhFARASNPHA----GGDVLCFAARRGDLGALRELLKLGLDVDSEDHDGATALRVAMAEGHADAARF 671
Cdd:COG0666  160 AAANGNLEIVKLL--LEAGADVNArdndGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKL 237

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 242090617 672 LIMNGASVDKASLDDDGSGSGAARLTMSPTELRELLQKREL 712
Cdd:COG0666  238 LLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
472-688 6.69e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 111.58  E-value: 6.69e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617 472 LLRLKQATLKEAMQSRPEDSVVIIKNFLKHQVEMHGMKADDLLGDNTGEHDDDANVLTVAAMGNSGLLEDLLRAGKDADV 551
Cdd:COG0666    3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617 552 GDAKGRTALHIAASNGYEDCVLVLLKHACNVNIKDAQGNTAMWNAIAAGHHKIFNILYhfARASNPHA----GGDVLCFA 627
Cdd:COG0666   83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLL--EAGADVNAqdndGNTPLHLA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 242090617 628 ARRGDLGALRELLKLGLDVDSEDHDGATALRVAMAEGHADAARFLIMNGASVDKAslDDDG 688
Cdd:COG0666  161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAK--DNDG 219
KHA pfam11834
KHA, dimerization domain of potassium ion channel; KHA is the tetramerization domain of ...
 750-820 5.29e-22

KHA, dimerization domain of potassium ion channel; KHA is the tetramerization domain of eukaryotic voltage-dependent potassium ion-channel proteins. In plants the domain lies at the C-terminus whereas in many chordates it lies at the N-terminus.


Pssm-ID: 463367  Cd Length: 65  Bit Score: 89.82  E-value: 5.29e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 242090617  750 PRVSVykgHPFlRNRSSEAGKLINLPGTLEEFKAIVGEKLKVDAKKglIVNDEGAEIDSIDVIRDNDKLFV 820
Cdd:pfam11834   1 KRVTI---FPN-HDGKRRNGKLIWLPDSLEELLKIASEKFGISATK--ILTEDGAEIDDIDVIRDGDHLYL 65
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 382-495 1.12e-21

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: 90.85  E-value: 1.12e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617 382 LFNGVSREMLLSLVTKMKPEYIPPKEDVIVQNEAPDDVYVVVSGEVEVI-LFNGIDEHVKATLGTRDIFGEVSALSDRAQ 460
Cdd:cd00038    1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYkLDEDGREQIVGFLGPGDLFGELALLGNGPR 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 242090617 461 AFTFRTRTLSQLLRLKQATLKEAMQSRPEDSVVII 495
Cdd:cd00038   81 SATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 382-498 2.49e-18

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: 81.68  E-value: 2.49e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617   382 LFNGVSREMLLSLVTKMKPEYIPPKEDVIVQNEAPDDVYVVVSGEVEVI-LFNGIDEHVKATLGTRDIFGEVSALSD--R 458
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYkVLEDGEEQIVGTLGPGDFFGELALLTNsrR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 242090617   459 AQAFTFRTRTLSQLLRLKQATLKEAMQSRPEDSVVIIKNF 498
Cdd:smart00100  81 AASAAAVALELATLLRIDFRDFLQLLPELPQLLLELLLEL 120
KHA cd17073
KHA, dimerization domain of potassium ion channel, similar to doublecortin-like domain, found ...
 750-822 4.63e-16

KHA, dimerization domain of potassium ion channel, similar to doublecortin-like domain, found in potassium channel tetramerization domain containing 9 (KCTD9) and similar proteins; This family corresponds to KHA, the tetramerization domain of eukaryotic voltage-dependent potassium ion-channel proteins, mainly found in vertebrates KCTD9 and plants AKT proteins. In plants the domain lies at the C-terminus whereas in many chordates it lies at the N-terminus. KHA shows high sequence similarity with doublecortin-like domain, which has a stable ubiquitin-like tertiary fold. KCTD9, also termed BTB/POZ domain-containing protein 9, belongs to the KCTD protein family, which corresponds to potassium channel tetramerization domain proteins, a class of BTB-domain-containing proteins. It is involved in potassium channel formation. Moreover, KCTD9 contributes to liver injury through NK cell activation during hepatitis B virus (HBV)-induced acute-on-chronic liver failure. AKT proteins play crucial roles in K+ uptake and translocation in plant cells.


Pssm-ID: 340593  Cd Length: 65  Bit Score: 73.02  E-value: 4.63e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 242090617 750 PRVSVYkghpflRNRSSEAGKLINLPGTLEEFKAIVGEKLKVDAKKglIVNDEGAEIDSIDVIRDNDKLFVVT 822
Cdd:cd17073    1 KRVTVF------VNGSSSGGKVIALPSTLSELLKIASEKLGIPAKR--LYTGSGGEIDDIALIRDDDVLYVSE 65
Ank_2 pfam12796
Ankyrin repeats (3 copies);
528-610 9.73e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 73.23  E-value: 9.73e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617  528 LTVAAM-GNSGLLEDLLRAGKDADVGDAKGRTALHIAASNGYEDCVLVLLKHAcNVNIKDaQGNTAMWNAIAAGHHKIFN 606
Cdd:pfam12796   1 LHLAAKnGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKD-NGRTALHYAARSGHLEIVK 78


                  ....
gi 242090617  607 ILYH 610
Cdd:pfam12796  79 LLLE 82
Ank_2 pfam12796
Ankyrin repeats (3 copies);
560-650 1.05e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.14  E-value: 1.05e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617  560 LHIAASNGYEDCVLVLLKHACNVNIKDAQGNTAMWNAIAAGHHKIFNILYHFARASNPHAGGDVLCFAARRGDLGALREL 639
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRTALHYAARSGHLEIVKLL 80

                          90
                  ....*....|.
gi 242090617  640 LKLGLDVDSED 650
Cdd:pfam12796  81 LEKGADINVKD 91
Ion_trans_2 pfam07885
Ion channel; This family includes the two membrane helix type ion channels found in bacteria.
 252-306 5.34e-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: 64.98  E-value: 5.34e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 242090617  252 YISSIYWSITTMTTVGYGDLHAENTVEMIFNIFYMLFNLGLTAYLIGNMTNLVVE 306
Cdd:pfam07885  24 FLDALYFSFVTLTTVGYGDIVPLTDAGRLFTIFYILIGIPLFAIFLAVLGRFLTE 78
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 383-506 4.68e-12

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: 66.16  E-value: 4.68e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617 383 FNGVSREMLLSLVTKMKPEYIPPKEDVIVQNEAPDDVYVVVSGEVEV--ILFNGiDEHVKATLGTRDIFGEVSALSDRAQ 460
Cdd:COG0664    1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLyrISEDG-REQILGFLGPGDFFGELSLLGGEPS 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 242090617 461 AFTFRTRTLSQLLRLKQATLKEAMQSRPEDSVVIIKNFLKHQVEMH 506
Cdd:COG0664   80 PATAEALEDSELLRIPREDLEELLERNPELARALLRLLARRLRQLQ 125
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 400-486 9.21e-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: 61.86  E-value: 9.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617  400 PEYIPPKEDVIVQNEAPDDVYVVVSGEVEV--ILFNGiDEHVKATLGTRDIFGEVSALSDRAQAFTFRTRTLSQLLRLKQ 477
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVyrTLEDG-REQILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPR 79


                  ....*....
gi 242090617  478 ATLKEAMQS 486
Cdd:pfam00027  80 EDFLELLER 88
Ank_2 pfam12796
Ankyrin repeats (3 copies);
494-586 1.75e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 52.43  E-value: 1.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617  494 IIKNFLKHQVEMHGMKADDLlgdntgehdddaNVLTVAAMGNSGLLEDLLRAGKDADVGDaKGRTALHIAASNGYEDCVL 573
Cdd:pfam12796  12 LVKLLLENGADANLQDKNGR------------TALHLAAKNGHLEIVKLLLEHADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 242090617  574 VLLKHACNVNIKD 586
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_4 pfam13637
Ankyrin repeats (many copies);
556-608 2.79e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.74  E-value: 2.79e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 242090617  556 GRTALHIAASNGYEDCVLVLLKHACNVNIKDAQGNTAMWNAIAAGHHKIFNIL 608
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank_2 pfam12796
Ankyrin repeats (3 copies);
624-690 3.90e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 51.66  E-value: 3.90e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 242090617  624 LCFAARRGDLGALRELLKLGLDVDSEDHDGATALRVAMAEGHADAARFLImngasvDKASLDDDGSG 690
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL------EHADVNLKDNG 61
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 524-685 6.58e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 55.74  E-value: 6.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617 524 DANVLTVAAMGNSgLLEDLLRAGKDADVGDAKGRTALHIAASNGYEDCVLVLLKHACNVNIKDAQGNTAMWNAIAAGHHK 603
Cdd:PHA02874  93 DTSILPIPCIEKD-MIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFD 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617 604 IFNILYH---FARASNpHAGGDVLCFAARRGDLGALRELLKLGLDVDSEDHDGATALRVAMAegHADAARFLIMNGASVD 680
Cdd:PHA02874 172 IIKLLLEkgaYANVKD-NNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASIN 248


                 ....*
gi 242090617 681 KASLD 685
Cdd:PHA02874 249 DQDID 253
Ank_5 pfam13857
Ankyrin repeats (many copies);
542-593 4.75e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.34  E-value: 4.75e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 242090617  542 LLRAG-KDADVGDAKGRTALHIAASNGYEDCVLVLLKHACNVNIKDAQGNTAM 593
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
Ank_4 pfam13637
Ankyrin repeats (many copies);
620-673 4.53e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 4.53e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 242090617  620 GGDVLCFAARRGDLGALRELLKLGLDVDSEDHDGATALRVAMAEGHADAARFLI 673
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 555-586 7.96e-06

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 43.05  E-value: 7.96e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 242090617  555 KGRTALHIAA-SNGYEDCVLVLLKHACNVNIKD 586
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 525-608 1.28e-05

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.74  E-value: 1.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617 525 ANVLTV-----AAMGNSGLLEDLLRAGKDADVGDAKGRTALHIAASNGYEDCVLVLLKHACNVNIKDAQGNTAMWNAIAA 599
Cdd:PTZ00322  79 AHMLTVelcqlAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEEN 158


                 ....*....
gi 242090617 600 GHHKIFNIL 608
Cdd:PTZ00322 159 GFREVVQLL 167
PHA03095 PHA03095
ankyrin-like protein; Provisional
 535-670 1.42e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 48.48  E-value: 1.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617 535 NSGLLEDLLRAGKDADVGDAKGRTALHIAASN--GYEDCVLVLLKHACNVNIKDAQGNTAMWNAIAAGHHK---IFNILY 609
Cdd:PHA03095 166 NVELLRLLIDAGADVYAVDDRFRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrslVLPLLI 245

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 242090617 610 HFARASNPHAGGDV-LCFAARRGDLGALRELLKLGLDVDSEDHDGATALRVAMAEGHADAAR 670
Cdd:PHA03095 246 AGISINARNRYGQTpLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVR 307
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 624-688 1.67e-05

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.36  E-value: 1.67e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 242090617 624 LCFAARRGDLGALRELLKLGLDVDSEDHDGATALRVAMAEGHADAARFLIMNGAsvDKASLDDDG 688
Cdd:PTZ00322  86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGA--DPTLLDKDG 148
PHA03095 PHA03095
ankyrin-like protein; Provisional
 538-695 2.03e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 48.10  E-value: 2.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617 538 LLEDLLRAGKDADVGDAKGRTALHIAASNGY--EDCVLVLLKHACNVNIKDAQGNTAMW------NA--------IAAGH 601
Cdd:PHA03095  99 VIKLLIKAGADVNAKDKVGRTPLHVYLSGFNinPKVIRLLLRKGADVNALDLYGMTPLAvllksrNAnvellrllIDAGA 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617 602 HKI------FNILYHFARASNPHAG-----GDVLCFAARRGDLGA----------------LRELLKLGLDVDSEDHDGA 654
Cdd:PHA03095 179 DVYavddrfRSLLHHHLQSFKPRARivrelIRAGCDPAATDMLGNtplhsmatgssckrslVLPLLIAGISINARNRYGQ 258

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 242090617 655 TALRVAMAEGHADAARFLIMNGASVDKASLDDDGSGSGAAR 695
Cdd:PHA03095 259 TPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVR 299
PHA03095 PHA03095
ankyrin-like protein; Provisional
 516-649 3.24e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 47.33  E-value: 3.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617 516 DNTGEHDDDANVLTVAAMGNS---GLLEDLLRAGKDADVGDAKGRTALHIAASNGYEDCVLVLLKHACNVNIKDAQGNTA 592
Cdd:PHA03095 214 DPAATDMLGNTPLHSMATGSSckrSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTP 293

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 242090617 593 MWNAIAAGHHKIFNILYH-----------FARASNphAGGDVLCFAARRgdlgALRE-LLKLGLDVDSE 649
Cdd:PHA03095 294 LSLMVRNNNGRAVRAALAknpsaetvaatLNTASV--AGGDIPSDATRL----CVAKvVLRGAFSLLPE 356
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 555-584 4.21e-05

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.03  E-value: 4.21e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 242090617   555 KGRTALHIAASNGYEDCVLVLLKHACNVNI 584
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
526-576 4.65e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.49  E-value: 4.65e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 242090617  526 NVLTVAAM-GNSGLLEDLLRAGKDADVGDAKGRTALHIAASNGYEDCVLVLL 576
Cdd:pfam13637   3 TALHAAAAsGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
573-695 1.78e-04

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 44.56  E-value: 1.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617 573 LVLLKHACNVNIKDAQGNTAMWNAIAAGHHKIFNILYHFARASNPHAGGDVLCFAARRGDLGALRELLKLGLDVDSEDHD 652
Cdd:COG0666    7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 242090617 653 GATALRVAMAEGHADAARFLIMNGASVDKASLDDDGSGSGAAR 695
Cdd:COG0666   87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAY 129
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 555-584 4.81e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.01  E-value: 4.81e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 242090617  555 KGRTALHIAASNGYEDCVLVLLKHACNVNI 584
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 535-645 4.94e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 43.44  E-value: 4.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617 535 NSGLLEDLLRAGKDADVGDAKGRTALHIAASNGYEDCVLVLLKHACNVNIKDAQGNTAMWNAIAAGHHKIFNILyhFARA 614
Cdd:PHA02875 114 KLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKML--LDSG 191

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 242090617 615 SNPH---AGGDV--LCFAARRGDLGALRELLKLGLD 645
Cdd:PHA02875 192 ANIDyfgKNGCVaaLCYAIENNKIDIVRLFIKRGAD 227
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 542-608 5.15e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 43.50  E-value: 5.15e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 242090617 542 LLRAGKDADVGDAKGRTALHIAASNGYEDCVLVLLKHACNVNIKDAQGNTAMWNAIAAGHHKIFNIL 608
Cdd:PHA03100 178 LLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLL 244
PHA03095 PHA03095
ankyrin-like protein; Provisional
 542-679 5.21e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 43.47  E-value: 5.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617 542 LLRAGKDADVGDAKGRTALHIAASNGY-EDCVLVLLKHACNVNIKDAQGNTAMwnaiaaghhkifnilyhfarasnpHAg 620
Cdd:PHA03095  69 LLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGADVNAKDKVGRTPL------------------------HV- 123

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 242090617 621 gdvlCFAARRGDLGALRELLKLGLDVDSEDHDGATALRVAMAEGHADAA--RFLIMNGASV 679
Cdd:PHA03095 124 ----YLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVEllRLLIDAGADV 180
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 536-685 3.63e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 40.82  E-value: 3.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617 536 SGLLEDLLRAGKDADVGDAKGRTALHIAASNGYE-DCVLVLLKHACNVNIKDAQGNTAMWNAIAAGHHK--IFNILYHFA 612
Cdd:PHA02876 287 SRLVPKLLERGADVNAKNIKGETPLYLMAKNGYDtENIRTLIMLGADVNAADRLYITPLHQASTLDRNKdiVITLLELGA 366

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 242090617 613 RA-SNPHAGGDVLCFAARRGDLGALRELLKLGLDVDSEDHDGATALRVAMAEGHA-DAARFLIMNGASVDKASLD 685
Cdd:PHA02876 367 NVnARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPyMSVKTLIDRGANVNSKNKD 441
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 542-687 4.66e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 40.25  E-value: 4.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617 542 LLRAGKDADVGDA-KGRTALHIAASNGYEDCVLVLLKHACNVNIKDAQGNTAMWNAIAAGHHKIFNILYHFARASNPHA- 619
Cdd:PHA02878 153 LLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDk 232

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 242090617 620 -GGDVLCFAARR-GDLGALRELLKLGLDVDSEDH-DGATALRVAMAEghADAARFLIMNGASVDKASLDDD 687
Cdd:PHA02878 233 cGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKL 301
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 446-661 8.21e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 39.48  E-value: 8.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617 446 RDIFGEVSALSDraqAFTFRTRTLSQLLRL------KQATLKEAMQSRPEDSV--VIIKNFLKHQVEMHgMKADDllGDN 517
Cdd:PHA02878  96 CSVFYTLVAIKD---AFNNRNVEIFKIILTnrykniQTIDLVYIDKKSKDDIIeaEITKLLLSYGADIN-MKDRH--KGN 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242090617 518 TGEHDDDANvltvaamGNSGLLEDLLRAGKDADVGDAKGRTALHIAASNGYEDCVLVLLKHACNVNIKDAQGNTAMwnAI 597
Cdd:PHA02878 170 TALHYATEN-------KDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPL--HI 240

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 242090617 598 AAGHHKIFNIL-YHFARASNPHAGGDVLCFAARRGDLGA---LRELLKLGLDVDSEDHDGATALRVAM 661
Cdd:PHA02878 241 SVGYCKDYDILkLLLEHGVDVNAKSYILGLTALHSSIKSerkLKLLLEYGADINSLNSYKLTPLSSAV 308
PRK10537 PRK10537
voltage-gated potassium channel protein;
256-316 8.38e-03

voltage-gated potassium channel protein;


Pssm-ID: 236711 [Multi-domain]  Cd Length: 393  Bit Score: 39.23  E-value: 8.38e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 242090617 256 IYWSITTMTTVGYGDLHAENTVEMIFNIFYMLfnLGLTAY----------LIGNMTNLVVEGTRRTMEFRN 316
Cdd:PRK10537 173 FYFSIVTMSTVGYGDIVPVSESARLFTISVII--LGITVFatsisaifgpVIRGNLKRLVKGRISHMHRKD 241
 
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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