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Conserved domains on  [gi|1205980162|ref|XP_021302967|]
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potassium channel AKT2 [Sorghum bicolor]

Protein Classification

PLN03192 family protein( domain architecture ID 11477558)

PLN03192 family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 28-833 0e+00

Voltage-dependent potassium channel; Provisional


:

Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 1572.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162  28 FNLRNLSKVILPPLGGPSagQSPNNGGSDKWVISPLDSRYRWWDTLMVVMVAYSAWVYLFEVAFMNASPKGGLEVADIVV 107
Cdd:PLN03192   24 LSLRNLSKVILPPLGVPS--YNQNHIGSDGWIISPMDSRYRWWETLMVVLVAYSAWVYPFEVAFLNASPKRGLEIADNVV 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 108 DLFFAVDIVLTFFVAYIDPRSQLLVCDRKKITFRYLSTFFIMDVASSIPFQAFAYFITGEVREDAVYSVLGLLRLWRLRR 187
Cdd:PLN03192  102 DLFFAVDIVLTFFVAYIDPRTQLLVRDRKKIAVRYLSTWFLMDVASTIPFQALAYLITGTVKLNLSYSLLGLLRFWRLRR 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 188 VNQFFTRLEKDIRFSYFWIRSARLVAVTLFVVHCAGCLYYLIADRYPHSEKTWIGAVIPNFRQASLGIRYITAIYWSITT 267
Cdd:PLN03192  182 VKQLFTRLEKDIRFSYFWIRCARLLSVTLFLVHCAGCLYYLIADRYPHQGKTWIGAVIPNFRETSLWIRYISAIYWSITT 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 268 MTTVGYGDLCARNTIEMIFNIFYMFFNLGLTSYLIGNMTNLVVEGTGRTMEFRSSIRAASSFVGRNHLPPRLKQQILAHM 347
Cdd:PLN03192  262 MTTVGYGDLHAVNTIEMIFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRLKDQILAYM 341

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 348 CLKFRVENLNQQQLLDELPKPIYKSICEHLFVPVVKDVYLFNGVSREMLLSLVTKMRPEYIPPKEEVIVQNEAPDDVYVV 427
Cdd:PLN03192  342 CLRFKAESLNQQQLIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIV 421

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 428 VSGEVEVILFDGIDERVEATLGTRDIFGEVSALSDRAQAFTFRTRTLSQLLRLKQATLKEAMQNRPEDSVVVIKNFLKHH 507
Cdd:PLN03192  422 VSGEVEIIDSEGEKERVVGTLGCGDIFGEVGALCCRPQSFTFRTKTLSQLLRLKTSTLIEAMQTRQEDNVVILKNFLQHH 501

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 508 VEMHGINVEDLLIDNIGEHDD---DANVLTVAAMGNSGLLEDLLRAGKDADVGDAKGRTALHIAASNGYEDCVLVLLKHA 584
Cdd:PLN03192  502 KELHDLNVGDLLGDNGGEHDDpnmASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA 581

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 585 CNVNIKDAQGNTAMWNAIAAGHHKIFNILYQFAHASNPHAGGDVLCLAARRGDLDALRELLKLGLDVDSEDHDGATALRV 664
Cdd:PLN03192  582 CNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQV 661

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 665 AMANGHVDVARFLIMNGASVDKANLDDDgssaarltMSPTELRELLQKRELGHSITIVDSSPAVVPDGGSSGHSRPGRLQ 744
Cdd:PLN03192  662 AMAEDHVDMVRLLIMNGADVDKANTDDD--------FSPTELRELLQKRELGHSITIVDSVPADEPDLGRDGGSRPGRLQ 733

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 745 STSSDNQRSPRVSLYKGHPSLRNR--SSEAGKLINLrEATMGEFKAIIGEKLKVDAEKALIVNDEGAEIDSIDVIRDNDK 822
Cdd:PLN03192  734 GTSSDNQCRPRVSIYKGHPLLRNErcCNEAGKLINL-PPSLEELKAIAGEKLGFDARKAMVTNEEGAEIDSIEVIRDNDK 812

                         810
                  ....*....|.
gi 1205980162 823 LFVVTQEDLRR 833
Cdd:PLN03192  813 LFVVEDEDSRR 823
 
Name Accession Description Interval E-value
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 28-833 0e+00

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 1572.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162  28 FNLRNLSKVILPPLGGPSagQSPNNGGSDKWVISPLDSRYRWWDTLMVVMVAYSAWVYLFEVAFMNASPKGGLEVADIVV 107
Cdd:PLN03192   24 LSLRNLSKVILPPLGVPS--YNQNHIGSDGWIISPMDSRYRWWETLMVVLVAYSAWVYPFEVAFLNASPKRGLEIADNVV 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 108 DLFFAVDIVLTFFVAYIDPRSQLLVCDRKKITFRYLSTFFIMDVASSIPFQAFAYFITGEVREDAVYSVLGLLRLWRLRR 187
Cdd:PLN03192  102 DLFFAVDIVLTFFVAYIDPRTQLLVRDRKKIAVRYLSTWFLMDVASTIPFQALAYLITGTVKLNLSYSLLGLLRFWRLRR 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 188 VNQFFTRLEKDIRFSYFWIRSARLVAVTLFVVHCAGCLYYLIADRYPHSEKTWIGAVIPNFRQASLGIRYITAIYWSITT 267
Cdd:PLN03192  182 VKQLFTRLEKDIRFSYFWIRCARLLSVTLFLVHCAGCLYYLIADRYPHQGKTWIGAVIPNFRETSLWIRYISAIYWSITT 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 268 MTTVGYGDLCARNTIEMIFNIFYMFFNLGLTSYLIGNMTNLVVEGTGRTMEFRSSIRAASSFVGRNHLPPRLKQQILAHM 347
Cdd:PLN03192  262 MTTVGYGDLHAVNTIEMIFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRLKDQILAYM 341

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 348 CLKFRVENLNQQQLLDELPKPIYKSICEHLFVPVVKDVYLFNGVSREMLLSLVTKMRPEYIPPKEEVIVQNEAPDDVYVV 427
Cdd:PLN03192  342 CLRFKAESLNQQQLIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIV 421

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 428 VSGEVEVILFDGIDERVEATLGTRDIFGEVSALSDRAQAFTFRTRTLSQLLRLKQATLKEAMQNRPEDSVVVIKNFLKHH 507
Cdd:PLN03192  422 VSGEVEIIDSEGEKERVVGTLGCGDIFGEVGALCCRPQSFTFRTKTLSQLLRLKTSTLIEAMQTRQEDNVVILKNFLQHH 501

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 508 VEMHGINVEDLLIDNIGEHDD---DANVLTVAAMGNSGLLEDLLRAGKDADVGDAKGRTALHIAASNGYEDCVLVLLKHA 584
Cdd:PLN03192  502 KELHDLNVGDLLGDNGGEHDDpnmASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA 581

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 585 CNVNIKDAQGNTAMWNAIAAGHHKIFNILYQFAHASNPHAGGDVLCLAARRGDLDALRELLKLGLDVDSEDHDGATALRV 664
Cdd:PLN03192  582 CNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQV 661

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 665 AMANGHVDVARFLIMNGASVDKANLDDDgssaarltMSPTELRELLQKRELGHSITIVDSSPAVVPDGGSSGHSRPGRLQ 744
Cdd:PLN03192  662 AMAEDHVDMVRLLIMNGADVDKANTDDD--------FSPTELRELLQKRELGHSITIVDSVPADEPDLGRDGGSRPGRLQ 733

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 745 STSSDNQRSPRVSLYKGHPSLRNR--SSEAGKLINLrEATMGEFKAIIGEKLKVDAEKALIVNDEGAEIDSIDVIRDNDK 822
Cdd:PLN03192  734 GTSSDNQCRPRVSIYKGHPLLRNErcCNEAGKLINL-PPSLEELKAIAGEKLGFDARKAMVTNEEGAEIDSIEVIRDNDK 812

                         810
                  ....*....|.
gi 1205980162 823 LFVVTQEDLRR 833
Cdd:PLN03192  813 LFVVEDEDSRR 823
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 67-317 1.55e-32

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: 126.23  E-value: 1.55e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162  67 YRWWDTLMVVMVAYSAWVYLFEVAFMNASP-KGGLEVADIVVDLFFAVDIVLTFFVAYIDprsqllvcdrkkitFRYL-S 144
Cdd:pfam00520   1 SRYFELFILLLILLNTIFLALETYFQPEEPlTTVLEILDYVFTGIFTLEMLLKIIAAGFK--------------KRYFrS 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 145 TFFIMDVASSIPFqaFAYFITGEVREDAVYSVLGLlrlWRLRRVNQFFTRLEKDIRFSYFWIRSARLVAVTLFVVHCAGC 224
Cdd:pfam00520  67 PWNILDFVVVLPS--LISLVLSSVGSLSGLRVLRL---LRLLRLLRLIRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLF 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 225 LYYLIADRYPH-SEKTWIGAV--IPNFRqaslgiRYITAIYWSITTMTTVGYGDLCARNTIEM-------IFNIFYMFFN 294
Cdd:pfam00520 142 IFAIIGYQLFGgKLKTWENPDngRTNFD------NFPNAFLWLFQTMTTEGWGDIMYDTIDGKgefwayiYFVSFIILGG 215

                         250       260
                  ....*....|....*....|...
gi 1205980162 295 LGLTSYLIGNMTNLVVEGTGRTM 317
Cdd:pfam00520 216 FLLLNLFIAVIIDNFQELTERTE 238
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
477-697 4.42e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 120.83  E-value: 4.42e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 477 LLRLKQATLKEAMQNRPEDSVVVIKNFLKHHVEMHGINVEDLLIDNIGEHDDDANVLTVAAMGNSGLLEDLLRAGKDADV 556
Cdd:COG0666     3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 557 GDAKGRTALHIAASNGYEDCVLVLLKHACNVNIKDAQGNTAMWNAIAAGHHKIFNILyqFAHASNPHA----GGDVLCLA 632
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLL--LEAGADVNAqdndGNTPLHLA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1205980162 633 ARRGDLDALRELLKLGLDVDSEDHDGATALRVAMANGHVDVARFLIMNGASVDkaNLDDDGSSAA 697
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVN--AKDNDGKTAL 223
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 387-500 1.24e-22

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: 93.54  E-value: 1.24e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 387 LFNGVSREMLLSLVTKMRPEYIPPKEEVIVQNEAPDDVYVVVSGEVEVI-LFDGIDERVEATLGTRDIFGEVSALSDRAQ 465
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYkLDEDGREQIVGFLGPGDLFGELALLGNGPR 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1205980162 466 AFTFRTRTLSQLLRLKQATLKEAMQNRPEDSVVVI 500
Cdd:cd00038    81 SATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 387-503 7.87e-19

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: 82.83  E-value: 7.87e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162  387 LFNGVSREMLLSLVTKMRPEYIPPKEEVIVQNEAPDDVYVVVSGEVEVI-LFDGIDERVEATLGTRDIFGEVSALSD--R 463
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYkVLEDGEEQIVGTLGPGDFFGELALLTNsrR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1205980162  464 AQAFTFRTRTLSQLLRLKQATLKEAMQNRPEDSVVVIKNF 503
Cdd:smart00100  81 AASAAAVALELATLLRIDFRDFLQLLPELPQLLLELLLEL 120
 
Name Accession Description Interval E-value
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 28-833 0e+00

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 1572.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162  28 FNLRNLSKVILPPLGGPSagQSPNNGGSDKWVISPLDSRYRWWDTLMVVMVAYSAWVYLFEVAFMNASPKGGLEVADIVV 107
Cdd:PLN03192   24 LSLRNLSKVILPPLGVPS--YNQNHIGSDGWIISPMDSRYRWWETLMVVLVAYSAWVYPFEVAFLNASPKRGLEIADNVV 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 108 DLFFAVDIVLTFFVAYIDPRSQLLVCDRKKITFRYLSTFFIMDVASSIPFQAFAYFITGEVREDAVYSVLGLLRLWRLRR 187
Cdd:PLN03192  102 DLFFAVDIVLTFFVAYIDPRTQLLVRDRKKIAVRYLSTWFLMDVASTIPFQALAYLITGTVKLNLSYSLLGLLRFWRLRR 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 188 VNQFFTRLEKDIRFSYFWIRSARLVAVTLFVVHCAGCLYYLIADRYPHSEKTWIGAVIPNFRQASLGIRYITAIYWSITT 267
Cdd:PLN03192  182 VKQLFTRLEKDIRFSYFWIRCARLLSVTLFLVHCAGCLYYLIADRYPHQGKTWIGAVIPNFRETSLWIRYISAIYWSITT 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 268 MTTVGYGDLCARNTIEMIFNIFYMFFNLGLTSYLIGNMTNLVVEGTGRTMEFRSSIRAASSFVGRNHLPPRLKQQILAHM 347
Cdd:PLN03192  262 MTTVGYGDLHAVNTIEMIFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRLKDQILAYM 341

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 348 CLKFRVENLNQQQLLDELPKPIYKSICEHLFVPVVKDVYLFNGVSREMLLSLVTKMRPEYIPPKEEVIVQNEAPDDVYVV 427
Cdd:PLN03192  342 CLRFKAESLNQQQLIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIV 421

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 428 VSGEVEVILFDGIDERVEATLGTRDIFGEVSALSDRAQAFTFRTRTLSQLLRLKQATLKEAMQNRPEDSVVVIKNFLKHH 507
Cdd:PLN03192  422 VSGEVEIIDSEGEKERVVGTLGCGDIFGEVGALCCRPQSFTFRTKTLSQLLRLKTSTLIEAMQTRQEDNVVILKNFLQHH 501

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 508 VEMHGINVEDLLIDNIGEHDD---DANVLTVAAMGNSGLLEDLLRAGKDADVGDAKGRTALHIAASNGYEDCVLVLLKHA 584
Cdd:PLN03192  502 KELHDLNVGDLLGDNGGEHDDpnmASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA 581

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 585 CNVNIKDAQGNTAMWNAIAAGHHKIFNILYQFAHASNPHAGGDVLCLAARRGDLDALRELLKLGLDVDSEDHDGATALRV 664
Cdd:PLN03192  582 CNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQV 661

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 665 AMANGHVDVARFLIMNGASVDKANLDDDgssaarltMSPTELRELLQKRELGHSITIVDSSPAVVPDGGSSGHSRPGRLQ 744
Cdd:PLN03192  662 AMAEDHVDMVRLLIMNGADVDKANTDDD--------FSPTELRELLQKRELGHSITIVDSVPADEPDLGRDGGSRPGRLQ 733

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 745 STSSDNQRSPRVSLYKGHPSLRNR--SSEAGKLINLrEATMGEFKAIIGEKLKVDAEKALIVNDEGAEIDSIDVIRDNDK 822
Cdd:PLN03192  734 GTSSDNQCRPRVSIYKGHPLLRNErcCNEAGKLINL-PPSLEELKAIAGEKLGFDARKAMVTNEEGAEIDSIEVIRDNDK 812

                         810
                  ....*....|.
gi 1205980162 823 LFVVTQEDLRR 833
Cdd:PLN03192  813 LFVVEDEDSRR 823
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 67-317 1.55e-32

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: 126.23  E-value: 1.55e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162  67 YRWWDTLMVVMVAYSAWVYLFEVAFMNASP-KGGLEVADIVVDLFFAVDIVLTFFVAYIDprsqllvcdrkkitFRYL-S 144
Cdd:pfam00520   1 SRYFELFILLLILLNTIFLALETYFQPEEPlTTVLEILDYVFTGIFTLEMLLKIIAAGFK--------------KRYFrS 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 145 TFFIMDVASSIPFqaFAYFITGEVREDAVYSVLGLlrlWRLRRVNQFFTRLEKDIRFSYFWIRSARLVAVTLFVVHCAGC 224
Cdd:pfam00520  67 PWNILDFVVVLPS--LISLVLSSVGSLSGLRVLRL---LRLLRLLRLIRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLF 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 225 LYYLIADRYPH-SEKTWIGAV--IPNFRqaslgiRYITAIYWSITTMTTVGYGDLCARNTIEM-------IFNIFYMFFN 294
Cdd:pfam00520 142 IFAIIGYQLFGgKLKTWENPDngRTNFD------NFPNAFLWLFQTMTTEGWGDIMYDTIDGKgefwayiYFVSFIILGG 215

                         250       260
                  ....*....|....*....|...
gi 1205980162 295 LGLTSYLIGNMTNLVVEGTGRTM 317
Cdd:pfam00520 216 FLLLNLFIAVIIDNFQELTERTE 238
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
477-697 4.42e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 120.83  E-value: 4.42e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 477 LLRLKQATLKEAMQNRPEDSVVVIKNFLKHHVEMHGINVEDLLIDNIGEHDDDANVLTVAAMGNSGLLEDLLRAGKDADV 556
Cdd:COG0666     3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 557 GDAKGRTALHIAASNGYEDCVLVLLKHACNVNIKDAQGNTAMWNAIAAGHHKIFNILyqFAHASNPHA----GGDVLCLA 632
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLL--LEAGADVNAqdndGNTPLHLA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1205980162 633 ARRGDLDALRELLKLGLDVDSEDHDGATALRVAMANGHVDVARFLIMNGASVDkaNLDDDGSSAA 697
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVN--AKDNDGKTAL 223
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
504-715 2.60e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 118.52  E-value: 2.60e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 504 LKHHVEMHGINVEDLLIDNIGEHDDDANVLTVAAMGNSGLLEDLLRAGKDADVGDAKGRTALHIAASNGYEDCVLVLLKH 583
Cdd:COG0666    63 LAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 584 ACNVNIKDAQGNTAMWNAIAAGHHKIFNILyqFAHASNPHA----GGDVLCLAARRGDLDALRELLKLGLDVDSEDHDGA 659
Cdd:COG0666   143 GADVNAQDNDGNTPLHLAAANGNLEIVKLL--LEAGADVNArdndGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGK 220

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1205980162 660 TALRVAMANGHVDVARFLIMNGASVDKANLDDDGSSAARLTMSPTELRELLQKREL 715
Cdd:COG0666   221 TALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALL 276
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 387-500 1.24e-22

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: 93.54  E-value: 1.24e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 387 LFNGVSREMLLSLVTKMRPEYIPPKEEVIVQNEAPDDVYVVVSGEVEVI-LFDGIDERVEATLGTRDIFGEVSALSDRAQ 465
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYkLDEDGREQIVGFLGPGDLFGELALLGNGPR 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1205980162 466 AFTFRTRTLSQLLRLKQATLKEAMQNRPEDSVVVI 500
Cdd:cd00038    81 SATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 387-503 7.87e-19

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: 82.83  E-value: 7.87e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162  387 LFNGVSREMLLSLVTKMRPEYIPPKEEVIVQNEAPDDVYVVVSGEVEVI-LFDGIDERVEATLGTRDIFGEVSALSD--R 463
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYkVLEDGEEQIVGTLGPGDFFGELALLTNsrR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1205980162  464 AQAFTFRTRTLSQLLRLKQATLKEAMQNRPEDSVVVIKNF 503
Cdd:smart00100  81 AASAAAVALELATLLRIDFRDFLQLLPELPQLLLELLLEL 120
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
511-662 3.28e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 83.08  E-value: 3.28e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 511 HGINVEdlLIDNIGEhdddaNVLTVAAM-GNSGLLEDLLRAGKDADVGDAKGRTALHIAASNGYEDCVLVLLKHACNVNI 589
Cdd:COG0666   142 AGADVN--AQDNDGN-----TPLHLAAAnGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNA 214

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1205980162 590 KDAQGNTAMWNAIAAGHHKIFNILYQFAHASNP--HAGGDVLCLAARRGDLDALRELLKLGLDVDSEDHDGATAL 662
Cdd:COG0666   215 KDNDGKTALDLAAENGNLEIVKLLLEAGADLNAkdKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
565-655 1.24e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.54  E-value: 1.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 565 LHIAASNGYEDCVLVLLKHACNVNIKDAQGNTAMWNAIAAGHHKIFNILYQFAHASNPHAGGDVLCLAARRGDLDALREL 644
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRTALHYAARSGHLEIVKLL 80

                          90
                  ....*....|.
gi 1205980162 645 LKLGLDVDSED 655
Cdd:pfam12796  81 LEKGADINVKD 91
KHA pfam11834
KHA, dimerization domain of potassium ion channel; KHA is the tetramerization domain of ...
 754-825 1.99e-16

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: 74.03  E-value: 1.99e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1205980162 754 PRVSLYKGHpslrNRSSEAGKLINLrEATMGEFKAIIGEKLKVDAEKalIVNDEGAEIDSIDVIRDNDKLFV 825
Cdd:pfam11834   1 KRVTIFPNH----DGKRRNGKLIWL-PDSLEELLKIASEKFGISATK--ILTEDGAEIDDIDVIRDGDHLYL 65
Ank_2 pfam12796
Ankyrin repeats (3 copies);
533-613 1.25e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.84  E-value: 1.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 533 LTVAAM-GNSGLLEDLLRAGKDADVGDAKGRTALHIAASNGYEDCVLVLLKHAcNVNIKDaQGNTAMWNAIAAGHHKIFN 611
Cdd:pfam12796   1 LHLAAKnGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKD-NGRTALHYAARSGHLEIVK 78


                  ..
gi 1205980162 612 IL 613
Cdd:pfam12796  79 LL 80
KHA cd17073
KHA, dimerization domain of potassium ion channel, similar to doublecortin-like domain, found ...
 754-827 4.99e-13

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: 64.54  E-value: 4.99e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1205980162 754 PRVSLYkghpslRNRSSEAGKLINLREaTMGEFKAIIGEKLKVDAEKalIVNDEGAEIDSIDVIRDNDKLFVVT 827
Cdd:cd17073     1 KRVTVF------VNGSSSGGKVIALPS-TLSELLKIASEKLGIPAKR--LYTGSGGEIDDIALIRDDDVLYVSE 65
Ion_trans_2 pfam07885
Ion channel; This family includes the two membrane helix type ion channels found in bacteria.
 257-311 2.90e-12

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: 62.67  E-value: 2.90e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1205980162 257 YITAIYWSITTMTTVGYGDLCARNTIEMIFNIFYMFFNLGLTSYLIGNMTNLVVE 311
Cdd:pfam07885  24 FLDALYFSFVTLTTVGYGDIVPLTDAGRLFTIFYILIGIPLFAIFLAVLGRFLTE 78
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 405-491 5.74e-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: 62.24  E-value: 5.74e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 405 PEYIPPKEEVIVQNEAPDDVYVVVSGEVEV--ILFDGiDERVEATLGTRDIFGEVSALSDRAQAFTFRTRTLSQLLRLKQ 482
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVyrTLEDG-REQILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPR 79


                  ....*....
gi 1205980162 483 ATLKEAMQN 491
Cdd:pfam00027  80 EDFLELLER 88
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 388-511 1.45e-11

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: 64.62  E-value: 1.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 388 FNGVSREMLLSLVTKMRPEYIPPKEEVIVQNEAPDDVYVVVSGEVEV--ILFDGiDERVEATLGTRDIFGEVSALSDRAQ 465
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLyrISEDG-REQILGFLGPGDFFGELSLLGGEPS 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1205980162 466 AFTFRTRTLSQLLRLKQATLKEAMQNRPEDSVVVIKNFLKHHVEMH 511
Cdd:COG0664    80 PATAEALEDSELLRIPREDLEELLERNPELARALLRLLARRLRQLQ 125
Ank_2 pfam12796
Ankyrin repeats (3 copies);
629-696 1.63e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.20  E-value: 1.63e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1205980162 629 LCLAARRGDLDALRELLKLGLDVDSEDHDGATALRVAMANGHVDVARFLImngaSVDKANLDDDGSSA 696
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL----EHADVNLKDNGRTA 64
Ank_2 pfam12796
Ankyrin repeats (3 copies);
488-591 5.41e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 53.97  E-value: 5.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 488 AMQNRPEdsvvVIKNFLKHHVEMHGINvedllidnigehDDDANVLTVAAMGNSGLLEDLLRAGKDADVGDaKGRTALHI 567
Cdd:pfam12796   5 AKNGNLE----LVKLLLENGADANLQD------------KNGRTALHLAAKNGHLEIVKLLLEHADVNLKD-NGRTALHY 67

                          90       100
                  ....*....|....*....|....
gi 1205980162 568 AASNGYEDCVLVLLKHACNVNIKD 591
Cdd:pfam12796  68 AARSGHLEIVKLLLEKGADINVKD 91
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 629-746 8.17e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 59.14  E-value: 8.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 629 LCLAARRGDLDALRELLKLGLDVDSEDHDGATALRVAMANGHVDVARFLIMNGAsvDKANLDDDGSSAARLTMSpTELRE 708
Cdd:PTZ00322   86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGA--DPTLLDKDGKTPLELAEE-NGFRE 162

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1205980162 709 LLQKReLGHSITIVDSSPAVVPDggsSGHSRPGRLQST 746
Cdd:PTZ00322  163 VVQLL-SRHSQCHFELGANAKPD---SFTGKPPSLEDS 196
Ank_4 pfam13637
Ankyrin repeats (many copies);
625-678 1.47e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.51  E-value: 1.47e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1205980162 625 GGDVLCLAARRGDLDALRELLKLGLDVDSEDHDGATALRVAMANGHVDVARFLI 678
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
561-613 2.09e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.12  E-value: 2.09e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1205980162 561 GRTALHIAASNGYEDCVLVLLKHACNVNIKDAQGNTAMWNAIAAGHHKIFNIL 613
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 518-690 9.13e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 55.35  E-value: 9.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 518 LLIDNigehDDDANVLTVAAMGNSgLLEDLLRAGKDADVGDAKGRTALHIAASNGYEDCVLVLLKHACNVNIKDAQGNTA 597
Cdd:PHA02874   86 LLIDN----GVDTSILPIPCIEKD-MIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYP 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 598 MWNAIAAGHHKIFNILYQF-AHAS-NPHAGGDVLCLAARRGDLDALRELLKLGLDVDSEDHDGATALRVAMANGHVDVAr 675
Cdd:PHA02874  161 IHIAIKHNFFDIIKLLLEKgAYANvKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIE- 239

                         170
                  ....*....|....*
gi 1205980162 676 fLIMNGASVDKANLD 690
Cdd:PHA02874  240 -LLINNASINDQDID 253
Ank_5 pfam13857
Ankyrin repeats (many copies);
547-598 4.92e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.34  E-value: 4.92e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1205980162 547 LLRAG-KDADVGDAKGRTALHIAASNGYEDCVLVLLKHACNVNIKDAQGNTAM 598
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PHA03095 PHA03095
ankyrin-like protein; Provisional
 547-696 1.30e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 51.95  E-value: 1.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 547 LLRAGKDADVGDAKGRTALHIAASNGY-EDCVLVLLKHACNVNIKDAQGNTAMwnaiaaghhkifnilyqfahasnpHAg 625
Cdd:PHA03095   69 LLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGADVNAKDKVGRTPL------------------------HV- 123

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1205980162 626 gdvlCLAARRGDLDALRELLKLGLDVDSEDHDGATALRVAMANGHVDVA--RFLIMNGASVdkANLDDDGSSA 696
Cdd:PHA03095  124 ----YLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVEllRLLIDAGADV--YAVDDRFRSL 190
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 560-591 7.25e-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: 43.43  E-value: 7.25e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1205980162 560 KGRTALHIAA-SNGYEDCVLVLLKHACNVNIKD 591
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 530-626 8.07e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.51  E-value: 8.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 530 ANVLTV-----AAMGNSGLLEDLLRAGKDADVGDAKGRTALHIAASNGYEDCVLVLLKHACNVNIKDAQGNTAMWNAIAA 604
Cdd:PTZ00322   79 AHMLTVelcqlAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEEN 158

                          90       100
                  ....*....|....*....|..
gi 1205980162 605 GHHKIFNILyqFAHASNPHAGG 626
Cdd:PTZ00322  159 GFREVVQLL--SRHSQCHFELG 178
PHA03095 PHA03095
ankyrin-like protein; Provisional
 511-677 1.25e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 48.48  E-value: 1.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 511 HGINVEDLliDNIGEHDDDANVLTVAAmgNSGLLEDLLRAGKDADVGDAKGRTALHIAASN--GYEDCVLVLLKHACNVN 588
Cdd:PHA03095  141 KGADVNAL--DLYGMTPLAVLLKSRNA--NVELLRLLIDAGADVYAVDDRFRSLLHHHLQSfkPRARIVRELIRAGCDPA 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 589 IKDAQGNTAMWNAIAAGHHKIFNILYQFAHASNPHA----GGDVLCLAARRGDLDALRELLKLGLDVDSEDHDGATALRV 664
Cdd:PHA03095  217 ATDMLGNTPLHSMATGSSCKRSLVLPLLIAGISINArnryGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSL 296

                         170
                  ....*....|....
gi 1205980162 665 AMANGHVD-VARFL 677
Cdd:PHA03095  297 MVRNNNGRaVRAAL 310
Ank_4 pfam13637
Ankyrin repeats (many copies);
531-581 3.58e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.88  E-value: 3.58e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1205980162 531 NVLTVAAM-GNSGLLEDLLRAGKDADVGDAKGRTALHIAASNGYEDCVLVLL 581
Cdd:pfam13637   3 TALHAAAAsGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 560-589 4.76e-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: 4.76e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 1205980162  560 KGRTALHIAASNGYEDCVLVLLKHACNVNI 589
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 547-692 4.79e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 46.80  E-value: 4.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 547 LLRAGKDADVGDA-KGRTALHIAASNGYEDCVLVLLKHACNVNIKDAQGNTAMWNAIAAGHHKIFNILYQFAHASNPHA- 624
Cdd:PHA02878  153 LLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDk 232

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1205980162 625 -GGDVLCLAARR-GDLDALRELLKLGLDVDSEDH-DGATALRVAMANGhvDVARFLIMNGASVDKANLDDD 692
Cdd:PHA02878  233 cGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSE--RKLKLLLEYGADINSLNSYKL 301
PHA03095 PHA03095
ankyrin-like protein; Provisional
 532-654 5.24e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.56  E-value: 5.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 532 VLTVAAMGNS---GLLEDLLRAGKDADVGDAKGRTALHIAASNGYEDCVLVLLKHACNVNIKDAQGNTAMWNAIAAGHHK 608
Cdd:PHA03095  225 PLHSMATGSSckrSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGR 304

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1205980162 609 IFN-----------ILYQFAHASNphAGGDVLCLAARRgdldALRE-LLKLGLDVDSE 654
Cdd:PHA03095  305 AVRaalaknpsaetVAATLNTASV--AGGDIPSDATRL----CVAKvVLRGAFSLLPE 356
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 485-650 6.21e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 46.14  E-value: 6.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 485 LKEAMQNRpedSVVVIKNFLKHHV-----------EMHG-------INVEDLL-----IDNIGEHDDDANVLTVAAMGNS 541
Cdd:PHA02875   39 IKLAMKFR---DSEAIKLLMKHGAipdvkypdiesELHDaveegdvKAVEELLdlgkfADDVFYKDGMTPLHLATILKKL 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 542 GLLEDLLRAGKDADVGDAKGRTALHIAASNGYEDCVLVLLKHACNVNIKDAQGNTAMWNAIAAGHHKIFNILyqFAHASN 621
Cdd:PHA02875  116 DIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKML--LDSGAN 193

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1205980162 622 PH---AGGDV--LCLAARRGDLDALRELLKLGLD 650
Cdd:PHA02875  194 IDyfgKNGCVaaLCYAIENNKIDIVRLFIKRGAD 227
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 541-691 3.40e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 44.28  E-value: 3.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 541 SGLLEDLLRAGKDADVGDAKGRTALHIAASNGYE-----------------------------------DCVLVLLKHAC 585
Cdd:PHA02876  287 SRLVPKLLERGADVNAKNIKGETPLYLMAKNGYDtenirtlimlgadvnaadrlyitplhqastldrnkDIVITLLELGA 366

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 586 NVNIKDAQGNTAMWNAIAAGHHKIFNILYQFahasnphaGGDVLCLAARRGDL-----------DALRELLKLGLDVDSE 654
Cdd:PHA02876  367 NVNARDYCDKTPIHYAAVRNNVVIINTLLDY--------GADIEALSQKIGTAlhfalcgtnpyMSVKTLIDRGANVNSK 438

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1205980162 655 DHDGATALRVAMANG-HVDVARFLIMNGASVDKANLDD 691
Cdd:PHA02876  439 NKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQN 476
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 547-692 3.82e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 43.89  E-value: 3.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 547 LLRAGKDADVGDAKGRTALHIAASN--GYEDCVLVLLKHACNVNIKDAQGntamwnaiaaghhkiFNILYQFAhaSNPHA 624
Cdd:PHA03100   92 LLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDG---------------ENLLHLYL--ESNKI 154

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1205980162 625 GGDVLCLAARRG-DLDALRE---LLKLGLDVDSEDHDGATALRVAMANGHVDVARFLIMNGASVDKANLDDD 692
Cdd:PHA03100  155 DLKILKLLIDKGvDINAKNRvnyLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGD 226
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 560-589 4.79e-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: 4.79e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1205980162 560 KGRTALHIAASNGYEDCVLVLLKHACNVNI 589
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 522-680 7.11e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 42.95  E-value: 7.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 522 NIGEHDDDANVLTVAAMG-NSGLLEDLLRAGKDADVGDAKGRTALHIAASNGYEDCVLVLLKHACNVNIKDAQGNTAMwn 600
Cdd:PHA02878  161 NMKDRHKGNTALHYATENkDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPL-- 238

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 601 AIAAGHHKIFNIL-YQFAHASNPHAGGDVLCLAARRGDL---DALRELLKLGLDVDSEDHDGATALRVAMANGH-VDVAR 675
Cdd:PHA02878  239 HISVGYCKDYDILkLLLEHGVDVNAKSYILGLTALHSSIkseRKLKLLLEYGADINSLNSYKLTPLSSAVKQYLcINIGR 318


                  ....*
gi 1205980162 676 FLIMN 680
Cdd:PHA02878  319 ILISN 323
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 547-613 9.90e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 42.34  E-value: 9.90e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1205980162 547 LLRAGKDADVGDAKGRTALHIAASNGYEDCVLVLLKHACNVNIKDAQGNTAMWNAIAAGHHKIFNIL 613
Cdd:PHA03100  178 LLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLL 244
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 540-685 2.85e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.13  E-value: 2.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 540 NSGLLEDLLRAGKDADVGDAKGRTALHIAASNGYEDCVLVLL---KHACNVNIKDaqGNTAMWNAIAAGHHKIFNILyqF 616
Cdd:PHA02875   47 DSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLdlgKFADDVFYKD--GMTPLHLATILKKLDIMKLL--I 122

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1205980162 617 AHASNPHAGG----DVLCLAARRGDLDALRELLKLGLDVDSEDHDGATALRVAMANGHVDVARFLIMNGASVD 685
Cdd:PHA02875  123 ARGADPDIPNtdkfSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANID 195
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 657-688 4.61e-03

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: 35.34  E-value: 4.61e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1205980162 657 DGATALRVAMA-NGHVDVARFLIMNGASVDKAN 688
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
PRK10537 PRK10537
voltage-gated potassium channel protein;
259-318 8.14e-03

voltage-gated potassium channel protein;


Pssm-ID: 236711 [Multi-domain]  Cd Length: 393  Bit Score: 39.62  E-value: 8.14e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205980162 259 TAIYWSITTMTTVGYGDLCARNTIEMIFNIFYMFfnLGLTSY----------LIGNMTNLVVEGTGRTME 318
Cdd:PRK10537  171 TAFYFSIVTMSTVGYGDIVPVSESARLFTISVII--LGITVFatsisaifgpVIRGNLKRLVKGRISHMH 238
 
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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