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Conserved domains on  [gi|1950166796|gb|KAG0518192|]
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hypothetical protein BDA96_09G154400 [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
 24-828 0e+00

Voltage-dependent potassium channel; Provisional


:

Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 1634.96  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950166796  24 FHLRNLSKVILPPLGGPSgQSQSHGGSDKWVISPLDSRYRWWDTLMVVLVAYSAWVYPFEVAFMNASPKGGLEVADIVVD 103
Cdd:PLN03192   24 LSLRNLSKVILPPLGVPS-YNQNHIGSDGWIISPMDSRYRWWETLMVVLVAYSAWVYPFEVAFLNASPKRGLEIADNVVD 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950166796 104 LFFAVDIVLTFFVAYIDHRTQLLVRDRRKITLRYLSTFFIMDVASTIPFQGLAYLVTGEVRENAAYSMLGVLRLWRLRRV 183
Cdd:PLN03192  103 LFFAVDIVLTFFVAYIDPRTQLLVRDRKKIAVRYLSTWFLMDVASTIPFQALAYLITGTVKLNLSYSLLGLLRFWRLRRV 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950166796 184 KQFFTRLEKDIRFSYFWIRCARLVAVTLFLVHCAGCLYYLIADRYPHREKTWIGAVIPNFRQASLRIRYISSIYWSITTM 263
Cdd:PLN03192  183 KQLFTRLEKDIRFSYFWIRCARLLSVTLFLVHCAGCLYYLIADRYPHQGKTWIGAVIPNFRETSLWIRYISAIYWSITTM 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950166796 264 TTVGYGDLHAENTVEMIFNIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIRAASSFVGRNHLPPRLKQQILAYMC 343
Cdd:PLN03192  263 TTVGYGDLHAVNTIEMIFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRLKDQILAYMC 342

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950166796 344 LKFRAESLNQQQLMDQLPKSICKSICEHLFVPVVKDVYLFNGVSREMLLSLVTKMKPEYIPPKEDVIVQNEAPDDVYVVV 423
Cdd:PLN03192  343 LRFKAESLNQQQLIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVV 422

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950166796 424 SGEVEVILFNGIDEHVKATLGTRDIFGEVSALSDRAQAFTFRTRTLSQLLRLKQATLKEAMQSRPEDSVVIIKNFLKHQV 503
Cdd:PLN03192  423 SGEVEIIDSEGEKERVVGTLGCGDIFGEVGALCCRPQSFTFRTKTLSQLLRLKTSTLIEAMQTRQEDNVVILKNFLQHHK 502

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950166796 504 EMHGMKADDLLGDNTGEHDD---DANVLTVAAMGNSGLLEDLLRAGKDADVGDAKGRTALHIAASYGYEDCVLVLLKHAC 580
Cdd:PLN03192  503 ELHDLNVGDLLGDNGGEHDDpnmASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHAC 582

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950166796 581 NVNIKDAQGNTAMWNAIAAGHHKIFNILYHFARASNPHAGGDVLCFAARRGDLGALRELLKLGLDVDSEDHDGATALRVA 660
Cdd:PLN03192  583 NVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVA 662

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950166796 661 MAEGHADAARFLIMNGASVDKASLDDDgsgsgaarltMSPTELRELLQKRELGHSITIVDS-PAVIPDGGSSGHSRPGRL 739
Cdd:PLN03192  663 MAEDHVDMVRLLIMNGADVDKANTDDD----------FSPTELRELLQKRELGHSITIVDSvPADEPDLGRDGGSRPGRL 732

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950166796 740 QGTSSDNQCWPRVSVYKGHPFLRNR--SSEAGKLINLPGTLEEFKAIVGEKLKVDAKKGLIVNDEGAEIDSIDVIRDNDK 817
Cdd:PLN03192  733 QGTSSDNQCRPRVSIYKGHPLLRNErcCNEAGKLINLPPSLEELKAIAGEKLGFDARKAMVTNEEGAEIDSIEVIRDNDK 812

                         810
                  ....*....|.
gi 1950166796 818 LFVVTEEDLRR 828
Cdd:PLN03192  813 LFVVEDEDSRR 823
 
Name Accession Description Interval E-value
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 24-828 0e+00

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 1634.96  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950166796  24 FHLRNLSKVILPPLGGPSgQSQSHGGSDKWVISPLDSRYRWWDTLMVVLVAYSAWVYPFEVAFMNASPKGGLEVADIVVD 103
Cdd:PLN03192   24 LSLRNLSKVILPPLGVPS-YNQNHIGSDGWIISPMDSRYRWWETLMVVLVAYSAWVYPFEVAFLNASPKRGLEIADNVVD 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950166796 104 LFFAVDIVLTFFVAYIDHRTQLLVRDRRKITLRYLSTFFIMDVASTIPFQGLAYLVTGEVRENAAYSMLGVLRLWRLRRV 183
Cdd:PLN03192  103 LFFAVDIVLTFFVAYIDPRTQLLVRDRKKIAVRYLSTWFLMDVASTIPFQALAYLITGTVKLNLSYSLLGLLRFWRLRRV 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950166796 184 KQFFTRLEKDIRFSYFWIRCARLVAVTLFLVHCAGCLYYLIADRYPHREKTWIGAVIPNFRQASLRIRYISSIYWSITTM 263
Cdd:PLN03192  183 KQLFTRLEKDIRFSYFWIRCARLLSVTLFLVHCAGCLYYLIADRYPHQGKTWIGAVIPNFRETSLWIRYISAIYWSITTM 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950166796 264 TTVGYGDLHAENTVEMIFNIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIRAASSFVGRNHLPPRLKQQILAYMC 343
Cdd:PLN03192  263 TTVGYGDLHAVNTIEMIFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRLKDQILAYMC 342

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950166796 344 LKFRAESLNQQQLMDQLPKSICKSICEHLFVPVVKDVYLFNGVSREMLLSLVTKMKPEYIPPKEDVIVQNEAPDDVYVVV 423
Cdd:PLN03192  343 LRFKAESLNQQQLIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVV 422

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950166796 424 SGEVEVILFNGIDEHVKATLGTRDIFGEVSALSDRAQAFTFRTRTLSQLLRLKQATLKEAMQSRPEDSVVIIKNFLKHQV 503
Cdd:PLN03192  423 SGEVEIIDSEGEKERVVGTLGCGDIFGEVGALCCRPQSFTFRTKTLSQLLRLKTSTLIEAMQTRQEDNVVILKNFLQHHK 502

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950166796 504 EMHGMKADDLLGDNTGEHDD---DANVLTVAAMGNSGLLEDLLRAGKDADVGDAKGRTALHIAASYGYEDCVLVLLKHAC 580
Cdd:PLN03192  503 ELHDLNVGDLLGDNGGEHDDpnmASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHAC 582

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950166796 581 NVNIKDAQGNTAMWNAIAAGHHKIFNILYHFARASNPHAGGDVLCFAARRGDLGALRELLKLGLDVDSEDHDGATALRVA 660
Cdd:PLN03192  583 NVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVA 662

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950166796 661 MAEGHADAARFLIMNGASVDKASLDDDgsgsgaarltMSPTELRELLQKRELGHSITIVDS-PAVIPDGGSSGHSRPGRL 739
Cdd:PLN03192  663 MAEDHVDMVRLLIMNGADVDKANTDDD----------FSPTELRELLQKRELGHSITIVDSvPADEPDLGRDGGSRPGRL 732

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950166796 740 QGTSSDNQCWPRVSVYKGHPFLRNR--SSEAGKLINLPGTLEEFKAIVGEKLKVDAKKGLIVNDEGAEIDSIDVIRDNDK 817
Cdd:PLN03192  733 QGTSSDNQCRPRVSIYKGHPLLRNErcCNEAGKLINLPPSLEELKAIAGEKLGFDARKAMVTNEEGAEIDSIEVIRDNDK 812

                         810
                  ....*....|.
gi 1950166796 818 LFVVTEEDLRR 828
Cdd:PLN03192  813 LFVVEDEDSRR 823
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 62-312 3.91e-45

Ion transport protein; This family contains sodium, potassium and calcium ion channels. This family is 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some sub-families (e.g. Na channels) the domain is repeated four times, whereas in others (e.g. K channels) the protein forms as a tetramer in the membrane.


Pssm-ID: 459842 [Multi-domain]  Cd Length: 238  Bit Score: 162.44  E-value: 3.91e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950166796  62 YRWWDTLMVVLVAYSAWVYPFEVAFMNASP-KGGLEVADIVVDLFFAVDIVLTFFVAYIDhrtqllvrdrrkitLRYL-S 139
Cdd:pfam00520   1 SRYFELFILLLILLNTIFLALETYFQPEEPlTTVLEILDYVFTGIFTLEMLLKIIAAGFK--------------KRYFrS 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950166796 140 TFFIMDVASTIPfqglaYLVTGEVRENAAYSMLGVLRLWRLRRVKQFFTRLEKDIRFSYFWIRCARLVAVTLFLVHCAGC 219
Cdd:pfam00520  67 PWNILDFVVVLP-----SLISLVLSSVGSLSGLRVLRLLRLLRLLRLIRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLF 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950166796 220 LYYLIADRYPH-REKTWIGAV--IPNFRqaslriRYISSIYWSITTMTTVGYGDLHAENTVEM-------IFNIFYMLFN 289
Cdd:pfam00520 142 IFAIIGYQLFGgKLKTWENPDngRTNFD------NFPNAFLWLFQTMTTEGWGDIMYDTIDGKgefwayiYFVSFIILGG 215

                         250       260
                  ....*....|....*....|...
gi 1950166796 290 LGLTAYLIGNMTNLVVEGTRRTM 312
Cdd:pfam00520 216 FLLLNLFIAVIIDNFQELTERTE 238
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
516-712 3.32e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 112.35  E-value: 3.32e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950166796 516 DNTGEHDDDANVLTVAAMGNSGLLEDLLRAGKDADVGDAKGRTALHIAASYGYEDCVLVLLKHACNVNIKDAQGNTAMWN 595
Cdd:COG0666    80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950166796 596 AIAAGHHKIFNILyhFARASNPHA----GGDVLCFAARRGDLGALRELLKLGLDVDSEDHDGATALRVAMAEGHADAARF 671
Cdd:COG0666   160 AAANGNLEIVKLL--LEAGADVNArdndGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKL 237

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1950166796 672 LIMNGASVDKASLDDDGSGSGAARLTMSPTELRELLQKREL 712
Cdd:COG0666   238 LLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 382-495 1.29e-21

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


Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 90.85  E-value: 1.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950166796 382 LFNGVSREMLLSLVTKMKPEYIPPKEDVIVQNEAPDDVYVVVSGEVEVI-LFNGIDEHVKATLGTRDIFGEVSALSDRAQ 460
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYkLDEDGREQIVGFLGPGDLFGELALLGNGPR 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1950166796 461 AFTFRTRTLSQLLRLKQATLKEAMQSRPEDSVVII 495
Cdd:cd00038    81 SATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 382-498 2.61e-18

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


Pssm-ID: 197516 [Multi-domain]  Cd Length: 120  Bit Score: 81.29  E-value: 2.61e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950166796  382 LFNGVSREMLLSLVTKMKPEYIPPKEDVIVQNEAPDDVYVVVSGEVEVI-LFNGIDEHVKATLGTRDIFGEVSALSD--R 458
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYkVLEDGEEQIVGTLGPGDFFGELALLTNsrR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1950166796  459 AQAFTFRTRTLSQLLRLKQATLKEAMQSRPEDSVVIIKNF 498
Cdd:smart00100  81 AASAAAVALELATLLRIDFRDFLQLLPELPQLLLELLLEL 120
 
Name Accession Description Interval E-value
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 24-828 0e+00

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 1634.96  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950166796  24 FHLRNLSKVILPPLGGPSgQSQSHGGSDKWVISPLDSRYRWWDTLMVVLVAYSAWVYPFEVAFMNASPKGGLEVADIVVD 103
Cdd:PLN03192   24 LSLRNLSKVILPPLGVPS-YNQNHIGSDGWIISPMDSRYRWWETLMVVLVAYSAWVYPFEVAFLNASPKRGLEIADNVVD 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950166796 104 LFFAVDIVLTFFVAYIDHRTQLLVRDRRKITLRYLSTFFIMDVASTIPFQGLAYLVTGEVRENAAYSMLGVLRLWRLRRV 183
Cdd:PLN03192  103 LFFAVDIVLTFFVAYIDPRTQLLVRDRKKIAVRYLSTWFLMDVASTIPFQALAYLITGTVKLNLSYSLLGLLRFWRLRRV 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950166796 184 KQFFTRLEKDIRFSYFWIRCARLVAVTLFLVHCAGCLYYLIADRYPHREKTWIGAVIPNFRQASLRIRYISSIYWSITTM 263
Cdd:PLN03192  183 KQLFTRLEKDIRFSYFWIRCARLLSVTLFLVHCAGCLYYLIADRYPHQGKTWIGAVIPNFRETSLWIRYISAIYWSITTM 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950166796 264 TTVGYGDLHAENTVEMIFNIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIRAASSFVGRNHLPPRLKQQILAYMC 343
Cdd:PLN03192  263 TTVGYGDLHAVNTIEMIFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRLKDQILAYMC 342

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950166796 344 LKFRAESLNQQQLMDQLPKSICKSICEHLFVPVVKDVYLFNGVSREMLLSLVTKMKPEYIPPKEDVIVQNEAPDDVYVVV 423
Cdd:PLN03192  343 LRFKAESLNQQQLIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVV 422

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950166796 424 SGEVEVILFNGIDEHVKATLGTRDIFGEVSALSDRAQAFTFRTRTLSQLLRLKQATLKEAMQSRPEDSVVIIKNFLKHQV 503
Cdd:PLN03192  423 SGEVEIIDSEGEKERVVGTLGCGDIFGEVGALCCRPQSFTFRTKTLSQLLRLKTSTLIEAMQTRQEDNVVILKNFLQHHK 502

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950166796 504 EMHGMKADDLLGDNTGEHDD---DANVLTVAAMGNSGLLEDLLRAGKDADVGDAKGRTALHIAASYGYEDCVLVLLKHAC 580
Cdd:PLN03192  503 ELHDLNVGDLLGDNGGEHDDpnmASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHAC 582

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950166796 581 NVNIKDAQGNTAMWNAIAAGHHKIFNILYHFARASNPHAGGDVLCFAARRGDLGALRELLKLGLDVDSEDHDGATALRVA 660
Cdd:PLN03192  583 NVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVA 662

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950166796 661 MAEGHADAARFLIMNGASVDKASLDDDgsgsgaarltMSPTELRELLQKRELGHSITIVDS-PAVIPDGGSSGHSRPGRL 739
Cdd:PLN03192  663 MAEDHVDMVRLLIMNGADVDKANTDDD----------FSPTELRELLQKRELGHSITIVDSvPADEPDLGRDGGSRPGRL 732

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950166796 740 QGTSSDNQCWPRVSVYKGHPFLRNR--SSEAGKLINLPGTLEEFKAIVGEKLKVDAKKGLIVNDEGAEIDSIDVIRDNDK 817
Cdd:PLN03192  733 QGTSSDNQCRPRVSIYKGHPLLRNErcCNEAGKLINLPPSLEELKAIAGEKLGFDARKAMVTNEEGAEIDSIEVIRDNDK 812

                         810
                  ....*....|.
gi 1950166796 818 LFVVTEEDLRR 828
Cdd:PLN03192  813 LFVVEDEDSRR 823
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 62-312 3.91e-45

Ion transport protein; This family contains sodium, potassium and calcium ion channels. This family is 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some sub-families (e.g. Na channels) the domain is repeated four times, whereas in others (e.g. K channels) the protein forms as a tetramer in the membrane.


Pssm-ID: 459842 [Multi-domain]  Cd Length: 238  Bit Score: 162.44  E-value: 3.91e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950166796  62 YRWWDTLMVVLVAYSAWVYPFEVAFMNASP-KGGLEVADIVVDLFFAVDIVLTFFVAYIDhrtqllvrdrrkitLRYL-S 139
Cdd:pfam00520   1 SRYFELFILLLILLNTIFLALETYFQPEEPlTTVLEILDYVFTGIFTLEMLLKIIAAGFK--------------KRYFrS 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950166796 140 TFFIMDVASTIPfqglaYLVTGEVRENAAYSMLGVLRLWRLRRVKQFFTRLEKDIRFSYFWIRCARLVAVTLFLVHCAGC 219
Cdd:pfam00520  67 PWNILDFVVVLP-----SLISLVLSSVGSLSGLRVLRLLRLLRLLRLIRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLF 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950166796 220 LYYLIADRYPH-REKTWIGAV--IPNFRqaslriRYISSIYWSITTMTTVGYGDLHAENTVEM-------IFNIFYMLFN 289
Cdd:pfam00520 142 IFAIIGYQLFGgKLKTWENPDngRTNFD------NFPNAFLWLFQTMTTEGWGDIMYDTIDGKgefwayiYFVSFIILGG 215

                         250       260
                  ....*....|....*....|...
gi 1950166796 290 LGLTAYLIGNMTNLVVEGTRRTM 312
Cdd:pfam00520 216 FLLLNLFIAVIIDNFQELTERTE 238
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
516-712 3.32e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 112.35  E-value: 3.32e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950166796 516 DNTGEHDDDANVLTVAAMGNSGLLEDLLRAGKDADVGDAKGRTALHIAASYGYEDCVLVLLKHACNVNIKDAQGNTAMWN 595
Cdd:COG0666    80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950166796 596 AIAAGHHKIFNILyhFARASNPHA----GGDVLCFAARRGDLGALRELLKLGLDVDSEDHDGATALRVAMAEGHADAARF 671
Cdd:COG0666   160 AAANGNLEIVKLL--LEAGADVNArdndGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKL 237

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1950166796 672 LIMNGASVDKASLDDDGSGSGAARLTMSPTELRELLQKREL 712
Cdd:COG0666   238 LLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
472-688 8.02e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 111.20  E-value: 8.02e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950166796 472 LLRLKQATLKEAMQSRPEDSVVIIKNFLKHQVEMHGMKADDLLGDNTGEHDDDANVLTVAAMGNSGLLEDLLRAGKDADV 551
Cdd:COG0666     3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950166796 552 GDAKGRTALHIAASYGYEDCVLVLLKHACNVNIKDAQGNTAMWNAIAAGHHKIFNILyhFARASNPHA----GGDVLCFA 627
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLL--LEAGADVNAqdndGNTPLHLA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1950166796 628 ARRGDLGALRELLKLGLDVDSEDHDGATALRVAMAEGHADAARFLIMNGASVDKAslDDDG 688
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAK--DNDG 219
KHA pfam11834
KHA, dimerization domain of potassium ion channel; KHA is the tetramerization domain of ...
 750-820 5.35e-22

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


Pssm-ID: 463367  Cd Length: 65  Bit Score: 89.82  E-value: 5.35e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1950166796 750 PRVSVykgHPFlRNRSSEAGKLINLPGTLEEFKAIVGEKLKVDAKKglIVNDEGAEIDSIDVIRDNDKLFV 820
Cdd:pfam11834   1 KRVTI---FPN-HDGKRRNGKLIWLPDSLEELLKIASEKFGISATK--ILTEDGAEIDDIDVIRDGDHLYL 65
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 382-495 1.29e-21

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


Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 90.85  E-value: 1.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950166796 382 LFNGVSREMLLSLVTKMKPEYIPPKEDVIVQNEAPDDVYVVVSGEVEVI-LFNGIDEHVKATLGTRDIFGEVSALSDRAQ 460
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYkLDEDGREQIVGFLGPGDLFGELALLGNGPR 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1950166796 461 AFTFRTRTLSQLLRLKQATLKEAMQSRPEDSVVII 495
Cdd:cd00038    81 SATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 382-498 2.61e-18

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


Pssm-ID: 197516 [Multi-domain]  Cd Length: 120  Bit Score: 81.29  E-value: 2.61e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950166796  382 LFNGVSREMLLSLVTKMKPEYIPPKEDVIVQNEAPDDVYVVVSGEVEVI-LFNGIDEHVKATLGTRDIFGEVSALSD--R 458
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYkVLEDGEEQIVGTLGPGDFFGELALLTNsrR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1950166796  459 AQAFTFRTRTLSQLLRLKQATLKEAMQSRPEDSVVIIKNF 498
Cdd:smart00100  81 AASAAAVALELATLLRIDFRDFLQLLPELPQLLLELLLEL 120
KHA cd17073
KHA, dimerization domain of potassium ion channel, similar to doublecortin-like domain, found ...
 750-822 4.50e-16

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


Pssm-ID: 340593  Cd Length: 65  Bit Score: 73.02  E-value: 4.50e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1950166796 750 PRVSVYkghpflRNRSSEAGKLINLPGTLEEFKAIVGEKLKVDAKKglIVNDEGAEIDSIDVIRDNDKLFVVT 822
Cdd:cd17073     1 KRVTVF------VNGSSSGGKVIALPSTLSELLKIASEKLGIPAKR--LYTGSGGEIDDIALIRDDDVLYVSE 65
Ank_2 pfam12796
Ankyrin repeats (3 copies);
528-610 2.04e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.07  E-value: 2.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950166796 528 LTVAAM-GNSGLLEDLLRAGKDADVGDAKGRTALHIAASYGYEDCVLVLLKHAcNVNIKDaQGNTAMWNAIAAGHHKIFN 606
Cdd:pfam12796   1 LHLAAKnGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKD-NGRTALHYAARSGHLEIVK 78


                  ....
gi 1950166796 607 ILYH 610
Cdd:pfam12796  79 LLLE 82
Ank_2 pfam12796
Ankyrin repeats (3 copies);
560-650 2.09e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 69.37  E-value: 2.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950166796 560 LHIAASYGYEDCVLVLLKHACNVNIKDAQGNTAMWNAIAAGHHKIFNILYHFARASNPHAGGDVLCFAARRGDLGALREL 639
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRTALHYAARSGHLEIVKLL 80

                          90
                  ....*....|.
gi 1950166796 640 LKLGLDVDSED 650
Cdd:pfam12796  81 LEKGADINVKD 91
Ion_trans_2 pfam07885
Ion channel; This family includes the two membrane helix type ion channels found in bacteria.
 252-306 5.55e-13

Ion channel; This family includes the two membrane helix type ion channels found in bacteria.


Pssm-ID: 462301 [Multi-domain]  Cd Length: 78  Bit Score: 64.98  E-value: 5.55e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1950166796 252 YISSIYWSITTMTTVGYGDLHAENTVEMIFNIFYMLFNLGLTAYLIGNMTNLVVE 306
Cdd:pfam07885  24 FLDALYFSFVTLTTVGYGDIVPLTDAGRLFTIFYILIGIPLFAIFLAVLGRFLTE 78
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 383-506 4.91e-12

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


Pssm-ID: 440428 [Multi-domain]  Cd Length: 207  Bit Score: 65.78  E-value: 4.91e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950166796 383 FNGVSREMLLSLVTKMKPEYIPPKEDVIVQNEAPDDVYVVVSGEVEV--ILFNGiDEHVKATLGTRDIFGEVSALSDRAQ 460
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLyrISEDG-REQILGFLGPGDFFGELSLLGGEPS 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1950166796 461 AFTFRTRTLSQLLRLKQATLKEAMQSRPEDSVVIIKNFLKHQVEMH 506
Cdd:COG0664    80 PATAEALEDSELLRIPREDLEELLERNPELARALLRLLARRLRQLQ 125
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 400-486 9.86e-12

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


Pssm-ID: 459637 [Multi-domain]  Cd Length: 89  Bit Score: 61.47  E-value: 9.86e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950166796 400 PEYIPPKEDVIVQNEAPDDVYVVVSGEVEV--ILFNGiDEHVKATLGTRDIFGEVSALSDRAQAFTFRTRTLSQLLRLKQ 477
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVyrTLEDG-REQILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPR 79


                  ....*....
gi 1950166796 478 ATLKEAMQS 486
Cdd:pfam00027  80 EDFLELLER 88
Ank_4 pfam13637
Ankyrin repeats (many copies);
556-608 1.68e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.51  E-value: 1.68e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1950166796 556 GRTALHIAASYGYEDCVLVLLKHACNVNIKDAQGNTAMWNAIAAGHHKIFNIL 608
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank_2 pfam12796
Ankyrin repeats (3 copies);
494-586 2.67e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 52.04  E-value: 2.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950166796 494 IIKNFLKHQVEMHGMKADDLlgdntgehdddaNVLTVAAMGNSGLLEDLLRAGKDADVGDaKGRTALHIAASYGYEDCVL 573
Cdd:pfam12796  12 LVKLLLENGADANLQDKNGR------------TALHLAAKNGHLEIVKLLLEHADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1950166796 574 VLLKHACNVNIKD 586
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
624-690 3.65e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 51.66  E-value: 3.65e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1950166796 624 LCFAARRGDLGALRELLKLGLDVDSEDHDGATALRVAMAEGHADAARFLImngasvDKASLDDDGSG 690
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL------EHADVNLKDNG 61
Ank_5 pfam13857
Ankyrin repeats (many copies);
542-593 2.26e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.11  E-value: 2.26e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1950166796 542 LLRAG-KDADVGDAKGRTALHIAASYGYEDCVLVLLKHACNVNIKDAQGNTAM 593
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 524-685 5.03e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.04  E-value: 5.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950166796 524 DANVLTVAAMGNSgLLEDLLRAGKDADVGDAKGRTALHIAASYGYEDCVLVLLKHACNVNIKDAQGNTAMWNAIAAGHHK 603
Cdd:PHA02874   93 DTSILPIPCIEKD-MIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFD 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950166796 604 IFNILYH---FARASNpHAGGDVLCFAARRGDLGALRELLKLGLDVDSEDHDGATALRVAMAegHADAARFLIMNGASVD 680
Cdd:PHA02874  172 IIKLLLEkgaYANVKD-NNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASIN 248


                  ....*
gi 1950166796 681 KASLD 685
Cdd:PHA02874  249 DQDID 253
PHA03095 PHA03095
ankyrin-like protein; Provisional
 527-649 3.61e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 50.41  E-value: 3.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950166796 527 VLTVAAMGNS---GLLEDLLRAGKDADVGDAKGRTALHIAASYGYEDCVLVLLKHACNVNIKDAQGNTAMWNAIAAGHHK 603
Cdd:PHA03095  225 PLHSMATGSSckrSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGR 304

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1950166796 604 IFNILYH-----------FARASNphAGGDVLCFAARRgdlgALRE-LLKLGLDVDSE 649
Cdd:PHA03095  305 AVRAALAknpsaetvaatLNTASV--AGGDIPSDATRL----CVAKvVLRGAFSLLPE 356
Ank_4 pfam13637
Ankyrin repeats (many copies);
620-673 4.62e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 4.62e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1950166796 620 GGDVLCFAARRGDLGALRELLKLGLDVDSEDHDGATALRVAMAEGHADAARFLI 673
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 555-586 6.73e-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: 6.73e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1950166796 555 KGRTALHIAA-SYGYEDCVLVLLKHACNVNIKD 586
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA03095 PHA03095
ankyrin-like protein; Provisional
 535-670 7.03e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 49.25  E-value: 7.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950166796 535 NSGLLEDLLRAGKDADVGDAKGRTALHIAASY--GYEDCVLVLLKHACNVNIKDAQGNTAMWNAIAAGHHK---IFNILY 609
Cdd:PHA03095  166 NVELLRLLIDAGADVYAVDDRFRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrslVLPLLI 245

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1950166796 610 HFARASNPHAGGDV-LCFAARRGDLGALRELLKLGLDVDSEDHDGATALRVAMAEGHADAAR 670
Cdd:PHA03095  246 AGISINARNRYGQTpLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVR 307
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 624-688 1.66e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.36  E-value: 1.66e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1950166796 624 LCFAARRGDLGALRELLKLGLDVDSEDHDGATALRVAMAEGHADAARFLIMNGAsvDKASLDDDG 688
Cdd:PTZ00322   86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGA--DPTLLDKDG 148
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 555-584 7.22e-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: 40.26  E-value: 7.22e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 1950166796  555 KGRTALHIAASYGYEDCVLVLLKHACNVNI 584
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 525-608 8.21e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.43  E-value: 8.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950166796 525 ANVLTV-----AAMGNSGLLEDLLRAGKDADVGDAKGRTALHIAASYGYEDCVLVLLKHACNVNIKDAQGNTAMWNAIAA 599
Cdd:PTZ00322   79 AHMLTVelcqlAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEEN 158


                  ....*....
gi 1950166796 600 GHHKIFNIL 608
Cdd:PTZ00322  159 GFREVVQLL 167
PHA03095 PHA03095
ankyrin-like protein; Provisional
 538-695 1.77e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.02  E-value: 1.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950166796 538 LLEDLLRAGKDADVGDAKGRTALHIAASyGY---EDCVLVLLKHACNVNIKDAQGNTAMW------NA--------IAAG 600
Cdd:PHA03095   99 VIKLLIKAGADVNAKDKVGRTPLHVYLS-GFninPKVIRLLLRKGADVNALDLYGMTPLAvllksrNAnvellrllIDAG 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950166796 601 HHKI------FNILYHFARASNPHAG-----GDVLCFAARRGDLGA----------------LRELLKLGLDVDSEDHDG 653
Cdd:PHA03095  178 ADVYavddrfRSLLHHHLQSFKPRARivrelIRAGCDPAATDMLGNtplhsmatgssckrslVLPLLIAGISINARNRYG 257

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1950166796 654 ATALRVAMAEGHADAARFLIMNGASVDKASLDDDGSGSGAAR 695
Cdd:PHA03095  258 QTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVR 299
Ank_4 pfam13637
Ankyrin repeats (many copies);
526-576 2.47e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.57  E-value: 2.47e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1950166796 526 NVLTVAAM-GNSGLLEDLLRAGKDADVGDAKGRTALHIAASYGYEDCVLVLL 576
Cdd:pfam13637   3 TALHAAAAsGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 542-608 4.11e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 43.50  E-value: 4.11e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1950166796 542 LLRAGKDADVGDAKGRTALHIAASYGYEDCVLVLLKHACNVNIKDAQGNTAMWNAIAAGHHKIFNIL 608
Cdd:PHA03100  178 LLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLL 244
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 555-584 4.77e-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: 4.77e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1950166796 555 KGRTALHIAASYGYEDCVLVLLKHACNVNI 584
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 535-645 6.41e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 43.06  E-value: 6.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950166796 535 NSGLLEDLLRAGKDADVGDAKGRTALHIAASYGYEDCVLVLLKHACNVNIKDAQGNTAMWNAIAAGHHKIFNILyhFARA 614
Cdd:PHA02875  114 KLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKML--LDSG 191

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1950166796 615 SNPH---AGGDV--LCFAARRGDLGALRELLKLGLD 645
Cdd:PHA02875  192 ANIDyfgKNGCVaaLCYAIENNKIDIVRLFIKRGAD 227
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 446-661 6.62e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 39.86  E-value: 6.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950166796 446 RDIFGEVSALSDraqAFTFRTRTLSQLLRL------KQATLKEAMQSRPEDSV--VIIKNFLKHQVEMHgMKADDllGDN 517
Cdd:PHA02878   96 CSVFYTLVAIKD---AFNNRNVEIFKIILTnrykniQTIDLVYIDKKSKDDIIeaEITKLLLSYGADIN-MKDRH--KGN 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950166796 518 TGEHDDDANvltvaamGNSGLLEDLLRAGKDADVGDAKGRTALHIAASYGYEDCVLVLLKHACNVNIKDAQGNTAMwnAI 597
Cdd:PHA02878  170 TALHYATEN-------KDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPL--HI 240

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1950166796 598 AAGHHKIFNIL-YHFARASNPHAGGDVLCFAARRGDLGA---LRELLKLGLDVDSEDHDGATALRVAM 661
Cdd:PHA02878  241 SVGYCKDYDILkLLLEHGVDVNAKSYILGLTALHSSIKSerkLKLLLEYGADINSLNSYKLTPLSSAV 308
PRK10537 PRK10537
voltage-gated potassium channel protein;
256-316 8.45e-03

voltage-gated potassium channel protein;


Pssm-ID: 236711 [Multi-domain]  Cd Length: 393  Bit Score: 39.23  E-value: 8.45e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1950166796 256 IYWSITTMTTVGYGDLHAENTVEMIFNIFYMLfnLGLTAY----------LIGNMTNLVVEGTRRTMEFRN 316
Cdd:PRK10537  173 FYFSIVTMSTVGYGDIVPVSESARLFTISVII--LGITVFatsisaifgpVIRGNLKRLVKGRISHMHRKD 241
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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