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Conserved domains on  [gi|241946430|gb|EES19575|]
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hypothetical protein SORBI_3009G147500 [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
 30-824 0e+00

Voltage-dependent potassium channel; Provisional


:

Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 1563.32  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241946430  30 LSLRYLSKIILPPLGGPPgQSQSHGGSDKWVISPLDSRYRWWDTLMVVLVAYSAWVYLFEVAFMNASPKGGLEVADIVVD 109
Cdd:PLN03192  24 LSLRNLSKVILPPLGVPS-YNQNHIGSDGWIISPMDSRYRWWETLMVVLVAYSAWVYPFEVAFLNASPKRGLEIADNVVD 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241946430 110 LFFAVDIVLTFFVAYIDPRTQLLIRDRKKITFRYLSTFFIMDVASTVPFQALAYFITGEVRENGAYSVLGLLRLWRLRRV 189
Cdd:PLN03192 103 LFFAVDIVLTFFVAYIDPRTQLLVRDRKKIAVRYLSTWFLMDVASTIPFQALAYLITGTVKLNLSYSLLGLLRFWRLRRV 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241946430 190 NQFFTRLEKDIRFSYFWIRCARLVAVTLFVVHSAGCLYYLIADRYPHPEKTWIGDVIPNFRQVSVWIRYITSVYWSITTM 269
Cdd:PLN03192 183 KQLFTRLEKDIRFSYFWIRCARLLSVTLFLVHCAGCLYYLIADRYPHQGKTWIGAVIPNFRETSLWIRYISAIYWSITTM 262

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241946430 270 TTVGYGDLHARNTVEMIFNIFYMLFNLGLTAYLIGNMTNLVVEGTHRTMEFRNSIRAATSFVGRNHLPPRLKQQILAYMC 349
Cdd:PLN03192 263 TTVGYGDLHAVNTIEMIFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRLKDQILAYMC 342

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241946430 350 LKFRAESLNQQQLMDQLPKSICKSICDHLFVPVVKDVYLFNGVSREMLLSLVTKMKPEYIPPREDVIVQNEAPDDVYVVV 429
Cdd:PLN03192 343 LRFKAESLNQQQLIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVV 422

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241946430 430 SGEVEVILFNGINERVEATLGTRDIFGEVSALSDRAQAFTFRTRTLSQLLRLKQATLKEAMQSRPEDNVVVIKNFLKHQV 509
Cdd:PLN03192 423 SGEVEIIDSEGEKERVVGTLGCGDIFGEVGALCCRPQSFTFRTKTLSQLLRLKTSTLIEAMQTRQEDNVVILKNFLQHHK 502

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241946430 510 EMHGMEVEDLLGDNTGEHDN---DANVLTAAMMGNSGLLEDLLRAGKDADVGDATGRTALHIAAAKVYEDCVLVLLKHAC 586
Cdd:PLN03192 503 ELHDLNVGDLLGDNGGEHDDpnmASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHAC 582

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241946430 587 NVNIEDAQGNTAMWNAIAAGHHRIFNILYQFSRASNPHAGGDVLCLAARRGDLGMLRELLKLGLDVDSEDHDGATALRVA 666
Cdd:PLN03192 583 NVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVA 662

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241946430 667 MAEGHADVARFLIMNGASVDKASLDDDgsgsgtarrtMSSTELRELLQKRELGHSITIVDSPAVI-----------PDRL 735
Cdd:PLN03192 663 MAEDHVDMVRLLIMNGADVDKANTDDD----------FSPTELRELLQKRELGHSITIVDSVPADepdlgrdggsrPGRL 732

                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241946430 736 QSTGSNQQRWPRVSIYNGHPFLRNR--SYEAGKLINLPGTMEEFIATVGEKLKVDAEKVLIVNDEGAEIDSIDVIRDNDK 813
Cdd:PLN03192 733 QGTSSDNQCRPRVSIYKGHPLLRNErcCNEAGKLINLPPSLEELKAIAGEKLGFDARKAMVTNEEGAEIDSIEVIRDNDK 812

                        810
                 ....*....|.
gi 241946430 814 LFVVTGEDMRQ 824
Cdd:PLN03192 813 LFVVEDEDSRR 823
 
Name Accession Description Interval E-value
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 30-824 0e+00

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 1563.32  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241946430  30 LSLRYLSKIILPPLGGPPgQSQSHGGSDKWVISPLDSRYRWWDTLMVVLVAYSAWVYLFEVAFMNASPKGGLEVADIVVD 109
Cdd:PLN03192  24 LSLRNLSKVILPPLGVPS-YNQNHIGSDGWIISPMDSRYRWWETLMVVLVAYSAWVYPFEVAFLNASPKRGLEIADNVVD 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241946430 110 LFFAVDIVLTFFVAYIDPRTQLLIRDRKKITFRYLSTFFIMDVASTVPFQALAYFITGEVRENGAYSVLGLLRLWRLRRV 189
Cdd:PLN03192 103 LFFAVDIVLTFFVAYIDPRTQLLVRDRKKIAVRYLSTWFLMDVASTIPFQALAYLITGTVKLNLSYSLLGLLRFWRLRRV 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241946430 190 NQFFTRLEKDIRFSYFWIRCARLVAVTLFVVHSAGCLYYLIADRYPHPEKTWIGDVIPNFRQVSVWIRYITSVYWSITTM 269
Cdd:PLN03192 183 KQLFTRLEKDIRFSYFWIRCARLLSVTLFLVHCAGCLYYLIADRYPHQGKTWIGAVIPNFRETSLWIRYISAIYWSITTM 262

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241946430 270 TTVGYGDLHARNTVEMIFNIFYMLFNLGLTAYLIGNMTNLVVEGTHRTMEFRNSIRAATSFVGRNHLPPRLKQQILAYMC 349
Cdd:PLN03192 263 TTVGYGDLHAVNTIEMIFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRLKDQILAYMC 342

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241946430 350 LKFRAESLNQQQLMDQLPKSICKSICDHLFVPVVKDVYLFNGVSREMLLSLVTKMKPEYIPPREDVIVQNEAPDDVYVVV 429
Cdd:PLN03192 343 LRFKAESLNQQQLIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVV 422

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241946430 430 SGEVEVILFNGINERVEATLGTRDIFGEVSALSDRAQAFTFRTRTLSQLLRLKQATLKEAMQSRPEDNVVVIKNFLKHQV 509
Cdd:PLN03192 423 SGEVEIIDSEGEKERVVGTLGCGDIFGEVGALCCRPQSFTFRTKTLSQLLRLKTSTLIEAMQTRQEDNVVILKNFLQHHK 502

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241946430 510 EMHGMEVEDLLGDNTGEHDN---DANVLTAAMMGNSGLLEDLLRAGKDADVGDATGRTALHIAAAKVYEDCVLVLLKHAC 586
Cdd:PLN03192 503 ELHDLNVGDLLGDNGGEHDDpnmASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHAC 582

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241946430 587 NVNIEDAQGNTAMWNAIAAGHHRIFNILYQFSRASNPHAGGDVLCLAARRGDLGMLRELLKLGLDVDSEDHDGATALRVA 666
Cdd:PLN03192 583 NVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVA 662

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241946430 667 MAEGHADVARFLIMNGASVDKASLDDDgsgsgtarrtMSSTELRELLQKRELGHSITIVDSPAVI-----------PDRL 735
Cdd:PLN03192 663 MAEDHVDMVRLLIMNGADVDKANTDDD----------FSPTELRELLQKRELGHSITIVDSVPADepdlgrdggsrPGRL 732

                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241946430 736 QSTGSNQQRWPRVSIYNGHPFLRNR--SYEAGKLINLPGTMEEFIATVGEKLKVDAEKVLIVNDEGAEIDSIDVIRDNDK 813
Cdd:PLN03192 733 QGTSSDNQCRPRVSIYKGHPLLRNErcCNEAGKLINLPPSLEELKAIAGEKLGFDARKAMVTNEEGAEIDSIEVIRDNDK 812

                        810
                 ....*....|.
gi 241946430 814 LFVVTGEDMRQ 824
Cdd:PLN03192 813 LFVVEDEDSRR 823
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 68-318 1.98e-33

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: 128.92  E-value: 1.98e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241946430   68 YRWWDTLMVVLVAYSAWVYLFEVAFMNASP-KGGLEVADIVVDLFFAVDIVLTFFVAYIDprtqllirdrkkitFRYL-S 145
Cdd:pfam00520   1 SRYFELFILLLILLNTIFLALETYFQPEEPlTTVLEILDYVFTGIFTLEMLLKIIAAGFK--------------KRYFrS 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241946430  146 TFFIMDVASTVPFqalayFITGEVRENGAYSVLGLLRLWRLRRVNQFFTRLEKDIRFSYFWIRCARLVAVTLFVVHSAGC 225
Cdd:pfam00520  67 PWNILDFVVVLPS-----LISLVLSSVGSLSGLRVLRLLRLLRLLRLIRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLF 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241946430  226 LYYLIADRYPHP-EKTWIG--DVIPNFRqvsvwiRYITSVYWSITTMTTVGYGDLHARNTVEM-------IFNIFYMLFN 295
Cdd:pfam00520 142 IFAIIGYQLFGGkLKTWENpdNGRTNFD------NFPNAFLWLFQTMTTEGWGDIMYDTIDGKgefwayiYFVSFIILGG 215

                         250       260
                  ....*....|....*....|...
gi 241946430  296 LGLTAYLIGNMTNLVVEGTHRTM 318
Cdd:pfam00520 216 FLLLNLFIAVIIDNFQELTERTE 238
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
522-693 1.47e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 110.43  E-value: 1.47e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241946430 522 DNTGEHDNDANVLTAAMMGNSGLLEDLLRAGKDADVGDATGRTALHIAAAKVYEDCVLVLLKHACNVNIEDAQGNTAMWN 601
Cdd:COG0666   80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241946430 602 AIAAGHHRIFNILYQfsrasnphAGGDV----------LCLAARRGDLGMLRELLKLGLDVDSEDHDGATALRVAMAEGH 671
Cdd:COG0666  160 AAANGNLEIVKLLLE--------AGADVnardndgetpLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGN 231

                        170       180
                 ....*....|....*....|..
gi 241946430 672 ADVARFLIMNGASVDKASLDDD 693
Cdd:COG0666  232 LEIVKLLLEAGADLNAKDKDGL 253
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 388-501 2.77e-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: 89.69  E-value: 2.77e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241946430 388 LFNGVSREMLLSLVTKMKPEYIPPREDVIVQNEAPDDVYVVVSGEVEVI-LFNGINERVEATLGTRDIFGEVSALSDRAQ 466
Cdd:cd00038    1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYkLDEDGREQIVGFLGPGDLFGELALLGNGPR 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 241946430 467 AFTFRTRTLSQLLRLKQATLKEAMQSRPEDNVVVI 501
Cdd:cd00038   81 SATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 388-504 1.11e-17

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: 79.75  E-value: 1.11e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241946430   388 LFNGVSREMLLSLVTKMKPEYIPPREDVIVQNEAPDDVYVVVSGEVEVI-LFNGINERVEATLGTRDIFGEVSALSD--R 464
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYkVLEDGEEQIVGTLGPGDFFGELALLTNsrR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 241946430   465 AQAFTFRTRTLSQLLRLKQATLKEAMQSRPEDNVVVIKNF 504
Cdd:smart00100  81 AASAAAVALELATLLRIDFRDFLQLLPELPQLLLELLLEL 120
 
Name Accession Description Interval E-value
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 30-824 0e+00

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 1563.32  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241946430  30 LSLRYLSKIILPPLGGPPgQSQSHGGSDKWVISPLDSRYRWWDTLMVVLVAYSAWVYLFEVAFMNASPKGGLEVADIVVD 109
Cdd:PLN03192  24 LSLRNLSKVILPPLGVPS-YNQNHIGSDGWIISPMDSRYRWWETLMVVLVAYSAWVYPFEVAFLNASPKRGLEIADNVVD 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241946430 110 LFFAVDIVLTFFVAYIDPRTQLLIRDRKKITFRYLSTFFIMDVASTVPFQALAYFITGEVRENGAYSVLGLLRLWRLRRV 189
Cdd:PLN03192 103 LFFAVDIVLTFFVAYIDPRTQLLVRDRKKIAVRYLSTWFLMDVASTIPFQALAYLITGTVKLNLSYSLLGLLRFWRLRRV 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241946430 190 NQFFTRLEKDIRFSYFWIRCARLVAVTLFVVHSAGCLYYLIADRYPHPEKTWIGDVIPNFRQVSVWIRYITSVYWSITTM 269
Cdd:PLN03192 183 KQLFTRLEKDIRFSYFWIRCARLLSVTLFLVHCAGCLYYLIADRYPHQGKTWIGAVIPNFRETSLWIRYISAIYWSITTM 262

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241946430 270 TTVGYGDLHARNTVEMIFNIFYMLFNLGLTAYLIGNMTNLVVEGTHRTMEFRNSIRAATSFVGRNHLPPRLKQQILAYMC 349
Cdd:PLN03192 263 TTVGYGDLHAVNTIEMIFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRLKDQILAYMC 342

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241946430 350 LKFRAESLNQQQLMDQLPKSICKSICDHLFVPVVKDVYLFNGVSREMLLSLVTKMKPEYIPPREDVIVQNEAPDDVYVVV 429
Cdd:PLN03192 343 LRFKAESLNQQQLIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVV 422

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241946430 430 SGEVEVILFNGINERVEATLGTRDIFGEVSALSDRAQAFTFRTRTLSQLLRLKQATLKEAMQSRPEDNVVVIKNFLKHQV 509
Cdd:PLN03192 423 SGEVEIIDSEGEKERVVGTLGCGDIFGEVGALCCRPQSFTFRTKTLSQLLRLKTSTLIEAMQTRQEDNVVILKNFLQHHK 502

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241946430 510 EMHGMEVEDLLGDNTGEHDN---DANVLTAAMMGNSGLLEDLLRAGKDADVGDATGRTALHIAAAKVYEDCVLVLLKHAC 586
Cdd:PLN03192 503 ELHDLNVGDLLGDNGGEHDDpnmASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHAC 582

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241946430 587 NVNIEDAQGNTAMWNAIAAGHHRIFNILYQFSRASNPHAGGDVLCLAARRGDLGMLRELLKLGLDVDSEDHDGATALRVA 666
Cdd:PLN03192 583 NVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVA 662

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241946430 667 MAEGHADVARFLIMNGASVDKASLDDDgsgsgtarrtMSSTELRELLQKRELGHSITIVDSPAVI-----------PDRL 735
Cdd:PLN03192 663 MAEDHVDMVRLLIMNGADVDKANTDDD----------FSPTELRELLQKRELGHSITIVDSVPADepdlgrdggsrPGRL 732

                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241946430 736 QSTGSNQQRWPRVSIYNGHPFLRNR--SYEAGKLINLPGTMEEFIATVGEKLKVDAEKVLIVNDEGAEIDSIDVIRDNDK 813
Cdd:PLN03192 733 QGTSSDNQCRPRVSIYKGHPLLRNErcCNEAGKLINLPPSLEELKAIAGEKLGFDARKAMVTNEEGAEIDSIEVIRDNDK 812

                        810
                 ....*....|.
gi 241946430 814 LFVVTGEDMRQ 824
Cdd:PLN03192 813 LFVVEDEDSRR 823
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 68-318 1.98e-33

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: 128.92  E-value: 1.98e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241946430   68 YRWWDTLMVVLVAYSAWVYLFEVAFMNASP-KGGLEVADIVVDLFFAVDIVLTFFVAYIDprtqllirdrkkitFRYL-S 145
Cdd:pfam00520   1 SRYFELFILLLILLNTIFLALETYFQPEEPlTTVLEILDYVFTGIFTLEMLLKIIAAGFK--------------KRYFrS 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241946430  146 TFFIMDVASTVPFqalayFITGEVRENGAYSVLGLLRLWRLRRVNQFFTRLEKDIRFSYFWIRCARLVAVTLFVVHSAGC 225
Cdd:pfam00520  67 PWNILDFVVVLPS-----LISLVLSSVGSLSGLRVLRLLRLLRLLRLIRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLF 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241946430  226 LYYLIADRYPHP-EKTWIG--DVIPNFRqvsvwiRYITSVYWSITTMTTVGYGDLHARNTVEM-------IFNIFYMLFN 295
Cdd:pfam00520 142 IFAIIGYQLFGGkLKTWENpdNGRTNFD------NFPNAFLWLFQTMTTEGWGDIMYDTIDGKgefwayiYFVSFIILGG 215

                         250       260
                  ....*....|....*....|...
gi 241946430  296 LGLTAYLIGNMTNLVVEGTHRTM 318
Cdd:pfam00520 216 FLLLNLFIAVIIDNFQELTERTE 238
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
522-693 1.47e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 110.43  E-value: 1.47e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241946430 522 DNTGEHDNDANVLTAAMMGNSGLLEDLLRAGKDADVGDATGRTALHIAAAKVYEDCVLVLLKHACNVNIEDAQGNTAMWN 601
Cdd:COG0666   80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241946430 602 AIAAGHHRIFNILYQfsrasnphAGGDV----------LCLAARRGDLGMLRELLKLGLDVDSEDHDGATALRVAMAEGH 671
Cdd:COG0666  160 AAANGNLEIVKLLLE--------AGADVnardndgetpLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGN 231

                        170       180
                 ....*....|....*....|..
gi 241946430 672 ADVARFLIMNGASVDKASLDDD 693
Cdd:COG0666  232 LEIVKLLLEAGADLNAKDKDGL 253
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
478-694 2.88e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 109.66  E-value: 2.88e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241946430 478 LLRLKQATLKEAMQSRPEDNVVVIKNFLKHQVEMHGMEVEDLLGDNTGEHDNDANVLTAAMMGNSGLLEDLLRAGKDADV 557
Cdd:COG0666    3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241946430 558 GDATGRTALHIAAAKVYEDCVLVLLKHACNVNIEDAQGNTAMWNAIAAGHHRIFNILYQfsrasnphAGGDV-------- 629
Cdd:COG0666   83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLE--------AGADVnaqdndgn 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 241946430 630 --LCLAARRGDLGMLRELLKLGLDVDSEDHDGATALRVAMAEGHADVARFLIMNGASVDKAslDDDG 694
Cdd:COG0666  155 tpLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAK--DNDG 219
KHA pfam11834
KHA, dimerization domain of potassium ion channel; KHA is the tetramerization domain of ...
 746-816 2.28e-21

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: 88.28  E-value: 2.28e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 241946430  746 PRVSIyngHPFlRNRSYEAGKLINLPGTMEEFIATVGEKLKVDAEKVLivNDEGAEIDSIDVIRDNDKLFV 816
Cdd:pfam11834   1 KRVTI---FPN-HDGKRRNGKLIWLPDSLEELLKIASEKFGISATKIL--TEDGAEIDDIDVIRDGDHLYL 65
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 388-501 2.77e-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: 89.69  E-value: 2.77e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241946430 388 LFNGVSREMLLSLVTKMKPEYIPPREDVIVQNEAPDDVYVVVSGEVEVI-LFNGINERVEATLGTRDIFGEVSALSDRAQ 466
Cdd:cd00038    1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYkLDEDGREQIVGFLGPGDLFGELALLGNGPR 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 241946430 467 AFTFRTRTLSQLLRLKQATLKEAMQSRPEDNVVVI 501
Cdd:cd00038   81 SATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 388-504 1.11e-17

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: 79.75  E-value: 1.11e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241946430   388 LFNGVSREMLLSLVTKMKPEYIPPREDVIVQNEAPDDVYVVVSGEVEVI-LFNGINERVEATLGTRDIFGEVSALSD--R 464
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYkVLEDGEEQIVGTLGPGDFFGELALLTNsrR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 241946430   465 AQAFTFRTRTLSQLLRLKQATLKEAMQSRPEDNVVVIKNF 504
Cdd:smart00100  81 AASAAAVALELATLLRIDFRDFLQLLPELPQLLLELLLEL 120
KHA cd17073
KHA, dimerization domain of potassium ion channel, similar to doublecortin-like domain, found ...
 746-818 1.57e-14

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: 68.78  E-value: 1.57e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 241946430 746 PRVSIYnghpflRNRSYEAGKLINLPGTMEEFIATVGEKLKVDAEKVLivNDEGAEIDSIDVIRDNDKLFVVT 818
Cdd:cd17073    1 KRVTVF------VNGSSSGGKVIALPSTLSELLKIASEKLGIPAKRLY--TGSGGEIDDIALIRDDDVLYVSE 65
Ank_2 pfam12796
Ankyrin repeats (3 copies);
536-614 6.03e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.14  E-value: 6.03e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 241946430  536 AAMMGNSGLLEDLLRAGKDADVGDATGRTALHIAAAKVYEDCVLVLLKHAcNVNIEDaQGNTAMWNAIAAGHHRIFNIL 614
Cdd:pfam12796   4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKD-NGRTALHYAARSGHLEIVKLL 80
Ank_2 pfam12796
Ankyrin repeats (3 copies);
566-656 1.04e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 64.37  E-value: 1.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241946430  566 LHIAAAKVYEDCVLVLLKHACNVNIEDAQGNTAMWNAIAAGHHRIFNILYQFSRASNPHAGGDVLCLAARRGDLGMLREL 645
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRTALHYAARSGHLEIVKLL 80

                          90
                  ....*....|.
gi 241946430  646 LKLGLDVDSED 656
Cdd:pfam12796  81 LEKGADINVKD 91
Ion_trans_2 pfam07885
Ion channel; This family includes the two membrane helix type ion channels found in bacteria.
 258-312 1.32e-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: 63.83  E-value: 1.32e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 241946430  258 YITSVYWSITTMTTVGYGDLHARNTVEMIFNIFYMLFNLGLTAYLIGNMTNLVVE 312
Cdd:pfam07885  24 FLDALYFSFVTLTTVGYGDIVPLTDAGRLFTIFYILIGIPLFAIFLAVLGRFLTE 78
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 406-492 1.18e-11

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


Pssm-ID: 459637 [Multi-domain]  Cd Length: 89  Bit Score: 61.47  E-value: 1.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241946430  406 PEYIPPREDVIVQNEAPDDVYVVVSGEVEV--ILFNGiNERVEATLGTRDIFGEVSALSDRAQAFTFRTRTLSQLLRLKQ 483
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVyrTLEDG-REQILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPR 79


                  ....*....
gi 241946430  484 ATLKEAMQS 492
Cdd:pfam00027  80 EDFLELLER 88
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 389-517 2.25e-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: 63.85  E-value: 2.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241946430 389 FNGVSREMLLSLVTKMKPEYIPPREDVIVQNEAPDDVYVVVSGEVEV--ILFNGiNERVEATLGTRDIFGEVSALSDRAQ 466
Cdd:COG0664    1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLyrISEDG-REQILGFLGPGDFFGELSLLGGEPS 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 241946430 467 AFTFRTRTLSQLLRLKQATLKEAMQSRPEDNVVVIKNFLKHQVEMHGMEVE 517
Cdd:COG0664   80 PATAEALEDSELLRIPREDLEELLERNPELARALLRLLARRLRQLQERLVS 130
Ank_2 pfam12796
Ankyrin repeats (3 copies);
630-696 1.11e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 53.20  E-value: 1.11e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 241946430  630 LCLAARRGDLGMLRELLKLGLDVDSEDHDGATALRVAMAEGHADVARFLImngasvDKASLDDDGSG 696
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL------EHADVNLKDNG 61
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
536-614 9.21e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 54.57  E-value: 9.21e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 241946430 536 AAMMGNSGLLEDLLRAGKDADVGDATGRTALHIAAAKVYEDCVLVLLKHACNVNIEDAQGNTAMWNAIAAGHHRIFNIL 614
Cdd:COG0666  193 AAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLL 271
Ank_4 pfam13637
Ankyrin repeats (many copies);
562-614 1.18e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.11  E-value: 1.18e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 241946430  562 GRTALHIAAAKVYEDCVLVLLKHACNVNIEDAQGNTAMWNAIAAGHHRIFNIL 614
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 630-746 1.59e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.82  E-value: 1.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241946430 630 LCLAARRGDLGMLRELLKLGLDVDSEDHDGATALRVAMAEGHADVARFLIMNGAsvDKASLDDDGSgsgTARRTMSSTEL 709
Cdd:PTZ00322  86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGA--DPTLLDKDGK---TPLELAEENGF 160

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 241946430 710 RELLQKReLGHSITIVDSPA-VIPDRLQSTGSNQQRWP 746
Cdd:PTZ00322 161 REVVQLL-SRHSQCHFELGAnAKPDSFTGKPPSLEDSP 197
Ank_2 pfam12796
Ankyrin repeats (3 copies);
516-592 2.57e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 46.26  E-value: 2.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241946430  516 VEDLLGDNTGEHDNDANVLT----AAMMGNSGLLEdLLRAGKDADVGDAtGRTALHIAAAKVYEDCVLVLLKHACNVNIE 591
Cdd:pfam12796  13 VKLLLENGADANLQDKNGRTalhlAAKNGHLEIVK-LLLEHADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVK 90


                  .
gi 241946430  592 D 592
Cdd:pfam12796  91 D 91
Ank_4 pfam13637
Ankyrin repeats (many copies);
626-679 3.79e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 3.79e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 241946430  626 GGDVLCLAARRGDLGMLRELLKLGLDVDSEDHDGATALRVAMAEGHADVARFLI 679
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 522-655 2.27e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 47.71  E-value: 2.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241946430 522 DNTGEHDNDANVLTAAMMGNS---GLLEDLLRAGKDADVGDATGRTALHIAAAKVYEDCVLVLLKHACNVNIEDAQGNTA 598
Cdd:PHA03095 214 DPAATDMLGNTPLHSMATGSSckrSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTP 293

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 241946430 599 MWNAIAAGHHRIFN-----------ILYQFSRASNphAGGDVLCLAARrgdLGMLRELLKLGLDVDSE 655
Cdd:PHA03095 294 LSLMVRNNNGRAVRaalaknpsaetVAATLNTASV--AGGDIPSDATR---LCVAKVVLRGAFSLLPE 356
PHA03095 PHA03095
ankyrin-like protein; Provisional
 524-685 3.21e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 47.33  E-value: 3.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241946430 524 TGEHDNDAnvLTAAMMGNSGLLED----LLRAGKDADVGDATGRTALH--IAAAKVyEDCVLVLLKHACNVNIEDAQGNT 597
Cdd:PHA03095  43 RGEYGKTP--LHLYLHYSSEKVKDivrlLLEAGADVNAPERCGFTPLHlyLYNATT-LDVIKLLIKAGADVNAKDKVGRT 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241946430 598 AMwnaiaaghhrifnilyqfsrasnpHAggdvlCLAARRGDLGMLRELLKLGLDVDSEDHDGATALRVAMAEGHADVA-- 675
Cdd:PHA03095 120 PL------------------------HV-----YLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVEll 170

                        170
                 ....*....|
gi 241946430 676 RFLIMNGASV 685
Cdd:PHA03095 171 RLLIDAGADV 180
Ank_5 pfam13857
Ankyrin repeats (many copies);
548-599 7.98e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.18  E-value: 7.98e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 241946430  548 LLRAG-KDADVGDATGRTALHIAAAKVYEDCVLVLLKHACNVNIEDAQGNTAM 599
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 541-691 8.66e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 45.72  E-value: 8.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241946430 541 NSGLLEDLLRAGKDADVGDATGRTALHIAAAKVYEDCVLVLLKHACNVNIEDAQGNTAMWNAIAAGHHRIFNILYQFSRA 620
Cdd:PHA02874 103 EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY 182

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 241946430 621 SN--PHAGGDVLCLAARRGDLGMLRELLKLGLDVDSEDHDGATALRVAMAEGHADVArfLIMNGASVDKASLD 691
Cdd:PHA02874 183 ANvkDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIE--LLINNASINDQDID 253
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 562-592 1.50e-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. 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: 39.58  E-value: 1.50e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 241946430  562 GRTALHIAAAKV-YEDCVLVLLKHACNVNIED 592
Cdd:pfam00023   2 GNTPLHLAAGRRgNLEIVKLLLSKGADVNARD 33
PHA03095 PHA03095
ankyrin-like protein; Provisional
 541-678 3.29e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 44.25  E-value: 3.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241946430 541 NSGLLEDLLRAGKDADVGDATGRTALHIAA--AKVYEDCVLVLLKHACNVNIEDAQGNTAMWNAIAAGHHR---IFNILY 615
Cdd:PHA03095 166 NVELLRLLIDAGADVYAVDDRFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrslVLPLLI 245

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 241946430 616 QFSRASNPHAGGDV-LCLAARRGDLGMLRELLKLGLDVDSEDHDGATALRVAMAEGHAD-VARFL 678
Cdd:PHA03095 246 AGISINARNRYGQTpLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRaVRAAL 310
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 562-590 7.77e-04

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: 37.57  E-value: 7.77e-04
                           10        20
                   ....*....|....*....|....*....
gi 241946430   562 GRTALHIAAAKVYEDCVLVLLKHACNVNI 590
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
536-582 3.10e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.48  E-value: 3.10e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 241946430  536 AAMMGNSGLLEDLLRAGKDADVGDATGRTALHIAAAKVYEDCVLVLL 582
Cdd:pfam13637   8 AAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PRK10537 PRK10537
voltage-gated potassium channel protein;
260-334 3.40e-03

voltage-gated potassium channel protein;


Pssm-ID: 236711 [Multi-domain]  Cd Length: 393  Bit Score: 40.78  E-value: 3.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241946430 260 TSVYWSITTMTTVGYGDLHARNTVEMIFNIFYMLfnLGLTAY----------LIGNMTNLVVEGTHRTMEFRNS-IRAAT 328
Cdd:PRK10537 171 TAFYFSIVTMSTVGYGDIVPVSESARLFTISVII--LGITVFatsisaifgpVIRGNLKRLVKGRISHMHRKDHfIICGH 248


                 ....*.
gi 241946430 329 SFVGRN 334
Cdd:PRK10537 249 SPLAIN 254
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 548-628 5.00e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 40.27  E-value: 5.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241946430 548 LLRAGKDADVGDATGRTALHIAAAKVYEDCVLVLLKHACNVNIEDAQGNTAMWNAIAAGHHRIFNILyqfSRASNPHAGG 627
Cdd:PTZ00322 101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL---SRHSQCHFEL 177


                 .
gi 241946430 628 D 628
Cdd:PTZ00322 178 G 178
 
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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