NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|15225768|ref|NP_180233|]
View 

K+ transporter 1 [Arabidopsis thaliana]

Protein Classification

ion transporter( domain architecture ID 1000861)

ion transporter such as a voltage-gated cation channel, which enables the selective translocation of cations such as sodium, calcium, or potassium, across cell membranes

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PLN03192 super family cl33658
Voltage-dependent potassium channel; Provisional
 26-856 0e+00

Voltage-dependent potassium channel; Provisional


The actual alignment was detected with superfamily member PLN03192:

Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 787.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768   26 SLSTGILPSLG--ARSNRRVKLRRFVVSPYDHKYRIWEAFLVVLVVYTAWVSPFEFGFLR-KPRPPLSITDNIVNAFFAI 102
Cdd:PLN03192  28 NLSKVILPPLGvpSYNQNHIGSDGWIISPMDSRYRWWETLMVVLVAYSAWVYPFEVAFLNaSPKRGLEIADNVVDLFFAV 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768  103 DIIMTFFVGYLDKSTYLIVDDRKQIAFKYLRSWFLLDLVSTIPSEA-AMRISSQ-----SYGLFNMLRLWRLRRVGALFA 176
Cdd:PLN03192 108 DIVLTFFVAYIDPRTQLLVRDRKKIAVRYLSTWFLMDVASTIPFQAlAYLITGTvklnlSYSLLGLLRFWRLRRVKQLFT 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768  177 RLEKDRNFNYFWVRCAKLVCVTLFAVHCAACFYYLIAARNSNPAKTWIGANVANFLEESLWMRYVTSMYWSITTLTTVGY 256
Cdd:PLN03192 188 RLEKDIRFSYFWIRCARLLSVTLFLVHCAGCLYYLIADRYPHQGKTWIGAVIPNFRETSLWIRYISAIYWSITTMTTVGY 267

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768  257 GDLHPVNTKEMIFDIFYMLFNLGLTAYLIGNMTNLVVHGTSRTRNFRDTIQAASNFAHRNHLPPRLQDQMLAHLCLKYRt 336
Cdd:PLN03192 268 GDLHAVNTIEMIFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRLKDQILAYMCLRFK- 346

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768  337 dSEGLQQQETLDALPKAIRSSISHFLFYSLMDKVYLFRGVSNDLLFQLVSEMKAEYFPPKEDVILQNEAPTDFYILVNGT 416
Cdd:PLN03192 347 -AESLNQQQLIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVVSGE 425

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768  417 ADLVDVDTGTESIVREVKAGDIIGEIGVLCYRPQLFTVRTKRLCQLLRMNRTTFLNIIQANVGDGTIIMNNLLQHLKEMN 496
Cdd:PLN03192 426 VEIIDSEGEKERVVGTLGCGDIFGEVGALCCRPQSFTFRTKTLSQLLRLKTSTLIEAMQTRQEDNVVILKNFLQHHKELH 505

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768  497 DPVMTNVLleIENMLARGKMDLPLNLCFAAIREDDLLLHQLLKRGLDPNESDNNGRTPLHIAASKGTLNCVLLLLEYHAD 576
Cdd:PLN03192 506 DLNVGDLL--GDNGGEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACN 583

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768  577 PNCRDAEGSVPLWEAMVEGHEKVVKVLLEHGSTIDAGDVGHFACTAAEQGNLKLLKEIVLHGGDVTRPRATGTSALHTAV 656
Cdd:PLN03192 584 VHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAM 663

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768  657 CEENIEMVKYLLEQGADVNKQDMH-GWTPRDLaeqqghedikalfREKLHERRvhietsssvpilktgirfLGRFTSEPN 735
Cdd:PLN03192 664 AEDHVDMVRLLIMNGADVDKANTDdDFSPTEL-------------RELLQKRE------------------LGHSITIVD 712

                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768  736 IRPASREVSFRIRETRARRKTNNFDNslfgilaNQSVPKNGLatvdegRTGNP-VRVTISCAEkddiAGKLVLLPGSFKE 814
Cdd:PLN03192 713 SVPADEPDLGRDGGSRPGRLQGTSSD-------NQCRPRVSI------YKGHPlLRNERCCNE----AGKLINLPPSLEE 775

                        810       820       830       840
                 ....*....|....*....|....*....|....*....|...
gi 15225768  815 LLELGSNKFGIVATKVM-NKDNNAEIDDVDVIRDGDHLIFATD 856
Cdd:PLN03192 776 LKAIAGEKLGFDARKAMvTNEEGAEIDSIEVIRDNDKLFVVED 818
 
Name Accession Description Interval E-value
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 26-856 0e+00

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 787.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768   26 SLSTGILPSLG--ARSNRRVKLRRFVVSPYDHKYRIWEAFLVVLVVYTAWVSPFEFGFLR-KPRPPLSITDNIVNAFFAI 102
Cdd:PLN03192  28 NLSKVILPPLGvpSYNQNHIGSDGWIISPMDSRYRWWETLMVVLVAYSAWVYPFEVAFLNaSPKRGLEIADNVVDLFFAV 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768  103 DIIMTFFVGYLDKSTYLIVDDRKQIAFKYLRSWFLLDLVSTIPSEA-AMRISSQ-----SYGLFNMLRLWRLRRVGALFA 176
Cdd:PLN03192 108 DIVLTFFVAYIDPRTQLLVRDRKKIAVRYLSTWFLMDVASTIPFQAlAYLITGTvklnlSYSLLGLLRFWRLRRVKQLFT 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768  177 RLEKDRNFNYFWVRCAKLVCVTLFAVHCAACFYYLIAARNSNPAKTWIGANVANFLEESLWMRYVTSMYWSITTLTTVGY 256
Cdd:PLN03192 188 RLEKDIRFSYFWIRCARLLSVTLFLVHCAGCLYYLIADRYPHQGKTWIGAVIPNFRETSLWIRYISAIYWSITTMTTVGY 267

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768  257 GDLHPVNTKEMIFDIFYMLFNLGLTAYLIGNMTNLVVHGTSRTRNFRDTIQAASNFAHRNHLPPRLQDQMLAHLCLKYRt 336
Cdd:PLN03192 268 GDLHAVNTIEMIFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRLKDQILAYMCLRFK- 346

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768  337 dSEGLQQQETLDALPKAIRSSISHFLFYSLMDKVYLFRGVSNDLLFQLVSEMKAEYFPPKEDVILQNEAPTDFYILVNGT 416
Cdd:PLN03192 347 -AESLNQQQLIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVVSGE 425

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768  417 ADLVDVDTGTESIVREVKAGDIIGEIGVLCYRPQLFTVRTKRLCQLLRMNRTTFLNIIQANVGDGTIIMNNLLQHLKEMN 496
Cdd:PLN03192 426 VEIIDSEGEKERVVGTLGCGDIFGEVGALCCRPQSFTFRTKTLSQLLRLKTSTLIEAMQTRQEDNVVILKNFLQHHKELH 505

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768  497 DPVMTNVLleIENMLARGKMDLPLNLCFAAIREDDLLLHQLLKRGLDPNESDNNGRTPLHIAASKGTLNCVLLLLEYHAD 576
Cdd:PLN03192 506 DLNVGDLL--GDNGGEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACN 583

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768  577 PNCRDAEGSVPLWEAMVEGHEKVVKVLLEHGSTIDAGDVGHFACTAAEQGNLKLLKEIVLHGGDVTRPRATGTSALHTAV 656
Cdd:PLN03192 584 VHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAM 663

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768  657 CEENIEMVKYLLEQGADVNKQDMH-GWTPRDLaeqqghedikalfREKLHERRvhietsssvpilktgirfLGRFTSEPN 735
Cdd:PLN03192 664 AEDHVDMVRLLIMNGADVDKANTDdDFSPTEL-------------RELLQKRE------------------LGHSITIVD 712

                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768  736 IRPASREVSFRIRETRARRKTNNFDNslfgilaNQSVPKNGLatvdegRTGNP-VRVTISCAEkddiAGKLVLLPGSFKE 814
Cdd:PLN03192 713 SVPADEPDLGRDGGSRPGRLQGTSSD-------NQCRPRVSI------YKGHPlLRNERCCNE----AGKLINLPPSLEE 775

                        810       820       830       840
                 ....*....|....*....|....*....|....*....|...
gi 15225768  815 LLELGSNKFGIVATKVM-NKDNNAEIDDVDVIRDGDHLIFATD 856
Cdd:PLN03192 776 LKAIAGEKLGFDARKAMvTNEEGAEIDSIEVIRDNDKLFVVED 818
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 57-300 7.57e-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: 161.67  E-value: 7.57e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768    57 YRIWEAFLVVLVVYTAWVSPFEFGFLRKPRP--PLSITDNIVNAFFAIDIIMTFFVGYLDKstylivddrkqiafKYLRS 134
Cdd:pfam00520   1 SRYFELFILLLILLNTIFLALETYFQPEEPLttVLEILDYVFTGIFTLEMLLKIIAAGFKK--------------RYFRS 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768   135 -WFLLDLVSTIPSEAAMRISSQ-SYGLFNMLRLWRLRRVGALFARLEKDRNFNYFWVRCAKLVCVTLFAVHCAACFYYLI 212
Cdd:pfam00520  67 pWNILDFVVVLPSLISLVLSSVgSLSGLRVLRLLRLLRLLRLIRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLFIFAII 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768   213 A-ARNSNPAKTWIGANVANFleesLWMRYVTSMYWSITTLTTVGYGDLHPVNTKEM-------IFDIFYMLFNLGLTAYL 284
Cdd:pfam00520 147 GyQLFGGKLKTWENPDNGRT----NFDNFPNAFLWLFQTMTTEGWGDIMYDTIDGKgefwayiYFVSFIILGGFLLLNLF 222

                         250
                  ....*....|....*.
gi 15225768   285 IGNMTNLVVHGTSRTR 300
Cdd:pfam00520 223 IAVIIDNFQELTERTE 238
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
471-704 1.83e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 150.87  E-value: 1.83e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768 471 LNIIQANVGDGTIIMNNLLQHLKEMNDPVMTNVLLEIENMLARGKMDLPLNLCFAAIREDDLLLHQLLKRGLDPNESDNN 550
Cdd:COG0666   7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768 551 GRTPLHIAASKGTLNCVLLLLEYHADPNCRDAEGSVPLWEAMVEGHEKVVKVLLEHGSTIDAGDVG-----HFactAAEQ 625
Cdd:COG0666  87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDgntplHL---AAAN 163

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15225768 626 GNLKLLKEIVLHGGDVTRPRATGTSALHTAVCEENIEMVKYLLEQGADVNKQDMHGWTPRDLAEQQGHEDIKALFREKL 704
Cdd:COG0666 164 GNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 372-477 1.25e-24

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: 99.32  E-value: 1.25e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768 372 LFRGVSNDLLFQLVSEMKAEYFPPKEDVILQNEAPTDFYILVNGTADLV-DVDTGTESIVREVKAGDIIGEIGVLCYRPQ 450
Cdd:cd00038   1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYkLDEDGREQIVGFLGPGDLFGELALLGNGPR 80

                        90       100
                ....*....|....*....|....*..
gi 15225768 451 LFTVRTKRLCQLLRMNRTTFLNIIQAN 477
Cdd:cd00038  81 SATVRALTDSELLVLPRSDFRRLLQEY 107
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 372-488 7.19e-22

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: 91.69  E-value: 7.19e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768    372 LFRGVSNDLLFQLVSEMKAEYFPPKEDVILQNEAPTDFYILVNGTADLV-DVDTGTESIVREVKAGDIIGEIGVL--CYR 448
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYkVLEDGEEQIVGTLGPGDFFGELALLtnSRR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 15225768    449 PQLFTVRTKRLCQLLRMNRTTFLNIIQANVGDGTIIMNNL 488
Cdd:smart00100  81 AASAAAVALELATLLRIDFRDFLQLLPELPQLLLELLLEL 120
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 576-675 3.69e-04

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 44.30  E-value: 3.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768   576 DPNCRDAEGSVPLWEAMVEG-HEKVVKVLLEHGSTIDAGDVGHFACTAAEQGNLKLLKEIVL--HGGDVTRPRAT----- 647
Cdd:TIGR00870  44 NINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAVGDTLLHAISLEYVDAVEAILLHLLaaFRKSGPLELANdqyts 123

                          90       100       110
                  ....*....|....*....|....*....|..
gi 15225768   648 ----GTSALHTAVCEENIEMVKYLLEQGADVN 675
Cdd:TIGR00870 124 eftpGITALHLAAHRQNYEIVKLLLERGASVP 155
 
Name Accession Description Interval E-value
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 26-856 0e+00

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 787.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768   26 SLSTGILPSLG--ARSNRRVKLRRFVVSPYDHKYRIWEAFLVVLVVYTAWVSPFEFGFLR-KPRPPLSITDNIVNAFFAI 102
Cdd:PLN03192  28 NLSKVILPPLGvpSYNQNHIGSDGWIISPMDSRYRWWETLMVVLVAYSAWVYPFEVAFLNaSPKRGLEIADNVVDLFFAV 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768  103 DIIMTFFVGYLDKSTYLIVDDRKQIAFKYLRSWFLLDLVSTIPSEA-AMRISSQ-----SYGLFNMLRLWRLRRVGALFA 176
Cdd:PLN03192 108 DIVLTFFVAYIDPRTQLLVRDRKKIAVRYLSTWFLMDVASTIPFQAlAYLITGTvklnlSYSLLGLLRFWRLRRVKQLFT 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768  177 RLEKDRNFNYFWVRCAKLVCVTLFAVHCAACFYYLIAARNSNPAKTWIGANVANFLEESLWMRYVTSMYWSITTLTTVGY 256
Cdd:PLN03192 188 RLEKDIRFSYFWIRCARLLSVTLFLVHCAGCLYYLIADRYPHQGKTWIGAVIPNFRETSLWIRYISAIYWSITTMTTVGY 267

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768  257 GDLHPVNTKEMIFDIFYMLFNLGLTAYLIGNMTNLVVHGTSRTRNFRDTIQAASNFAHRNHLPPRLQDQMLAHLCLKYRt 336
Cdd:PLN03192 268 GDLHAVNTIEMIFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRLKDQILAYMCLRFK- 346

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768  337 dSEGLQQQETLDALPKAIRSSISHFLFYSLMDKVYLFRGVSNDLLFQLVSEMKAEYFPPKEDVILQNEAPTDFYILVNGT 416
Cdd:PLN03192 347 -AESLNQQQLIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVVSGE 425

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768  417 ADLVDVDTGTESIVREVKAGDIIGEIGVLCYRPQLFTVRTKRLCQLLRMNRTTFLNIIQANVGDGTIIMNNLLQHLKEMN 496
Cdd:PLN03192 426 VEIIDSEGEKERVVGTLGCGDIFGEVGALCCRPQSFTFRTKTLSQLLRLKTSTLIEAMQTRQEDNVVILKNFLQHHKELH 505

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768  497 DPVMTNVLleIENMLARGKMDLPLNLCFAAIREDDLLLHQLLKRGLDPNESDNNGRTPLHIAASKGTLNCVLLLLEYHAD 576
Cdd:PLN03192 506 DLNVGDLL--GDNGGEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACN 583

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768  577 PNCRDAEGSVPLWEAMVEGHEKVVKVLLEHGSTIDAGDVGHFACTAAEQGNLKLLKEIVLHGGDVTRPRATGTSALHTAV 656
Cdd:PLN03192 584 VHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAM 663

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768  657 CEENIEMVKYLLEQGADVNKQDMH-GWTPRDLaeqqghedikalfREKLHERRvhietsssvpilktgirfLGRFTSEPN 735
Cdd:PLN03192 664 AEDHVDMVRLLIMNGADVDKANTDdDFSPTEL-------------RELLQKRE------------------LGHSITIVD 712

                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768  736 IRPASREVSFRIRETRARRKTNNFDNslfgilaNQSVPKNGLatvdegRTGNP-VRVTISCAEkddiAGKLVLLPGSFKE 814
Cdd:PLN03192 713 SVPADEPDLGRDGGSRPGRLQGTSSD-------NQCRPRVSI------YKGHPlLRNERCCNE----AGKLINLPPSLEE 775

                        810       820       830       840
                 ....*....|....*....|....*....|....*....|...
gi 15225768  815 LLELGSNKFGIVATKVM-NKDNNAEIDDVDVIRDGDHLIFATD 856
Cdd:PLN03192 776 LKAIAGEKLGFDARKAMvTNEEGAEIDSIEVIRDNDKLFVVED 818
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 57-300 7.57e-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: 161.67  E-value: 7.57e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768    57 YRIWEAFLVVLVVYTAWVSPFEFGFLRKPRP--PLSITDNIVNAFFAIDIIMTFFVGYLDKstylivddrkqiafKYLRS 134
Cdd:pfam00520   1 SRYFELFILLLILLNTIFLALETYFQPEEPLttVLEILDYVFTGIFTLEMLLKIIAAGFKK--------------RYFRS 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768   135 -WFLLDLVSTIPSEAAMRISSQ-SYGLFNMLRLWRLRRVGALFARLEKDRNFNYFWVRCAKLVCVTLFAVHCAACFYYLI 212
Cdd:pfam00520  67 pWNILDFVVVLPSLISLVLSSVgSLSGLRVLRLLRLLRLLRLIRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLFIFAII 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768   213 A-ARNSNPAKTWIGANVANFleesLWMRYVTSMYWSITTLTTVGYGDLHPVNTKEM-------IFDIFYMLFNLGLTAYL 284
Cdd:pfam00520 147 GyQLFGGKLKTWENPDNGRT----NFDNFPNAFLWLFQTMTTEGWGDIMYDTIDGKgefwayiYFVSFIILGGFLLLNLF 222

                         250
                  ....*....|....*.
gi 15225768   285 IGNMTNLVVHGTSRTR 300
Cdd:pfam00520 223 IAVIIDNFQELTERTE 238
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
471-704 1.83e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 150.87  E-value: 1.83e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768 471 LNIIQANVGDGTIIMNNLLQHLKEMNDPVMTNVLLEIENMLARGKMDLPLNLCFAAIREDDLLLHQLLKRGLDPNESDNN 550
Cdd:COG0666   7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768 551 GRTPLHIAASKGTLNCVLLLLEYHADPNCRDAEGSVPLWEAMVEGHEKVVKVLLEHGSTIDAGDVG-----HFactAAEQ 625
Cdd:COG0666  87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDgntplHL---AAAN 163

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15225768 626 GNLKLLKEIVLHGGDVTRPRATGTSALHTAVCEENIEMVKYLLEQGADVNKQDMHGWTPRDLAEQQGHEDIKALFREKL 704
Cdd:COG0666 164 GNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
502-696 7.72e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 120.06  E-value: 7.72e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768 502 NVLLEIENMLARGKMDLPLNLCFAAIREDDLLLHQLLKRGLDPNESDNNGRTPLHIAASKGTLNCVLLLLEYHADPNCRD 581
Cdd:COG0666   5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768 582 AEGSVPLWEAMVEGHEKVVKVLLEHGSTIDAGDVGHFA--CTAAEQGNLKLLKEIVLHGGDVTRPRATGTSALHTAVCEE 659
Cdd:COG0666  85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETplHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANG 164

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 15225768 660 NIEMVKYLLEQGADVNKQDMHGWTPRDLAEQQGHEDI 696
Cdd:COG0666 165 NLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEI 201
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 372-477 1.25e-24

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: 99.32  E-value: 1.25e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768 372 LFRGVSNDLLFQLVSEMKAEYFPPKEDVILQNEAPTDFYILVNGTADLV-DVDTGTESIVREVKAGDIIGEIGVLCYRPQ 450
Cdd:cd00038   1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYkLDEDGREQIVGFLGPGDLFGELALLGNGPR 80

                        90       100
                ....*....|....*....|....*..
gi 15225768 451 LFTVRTKRLCQLLRMNRTTFLNIIQAN 477
Cdd:cd00038  81 SATVRALTDSELLVLPRSDFRRLLQEY 107
KHA pfam11834
KHA, dimerization domain of potassium ion channel; KHA is the tetramerization domain of ...
 790-853 3.55e-23

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: 93.29  E-value: 3.55e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15225768   790 RVTISCAEKD-DIAGKLVLLPGSFKELLELGSNKFGIVATKVMNKDnNAEIDDVDVIRDGDHLIF 853
Cdd:pfam11834   2 RVTIFPNHDGkRRNGKLIWLPDSLEELLKIASEKFGISATKILTED-GAEIDDIDVIRDGDHLYL 65
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 372-488 7.19e-22

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: 91.69  E-value: 7.19e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768    372 LFRGVSNDLLFQLVSEMKAEYFPPKEDVILQNEAPTDFYILVNGTADLV-DVDTGTESIVREVKAGDIIGEIGVL--CYR 448
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYkVLEDGEEQIVGTLGPGDFFGELALLtnSRR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 15225768    449 PQLFTVRTKRLCQLLRMNRTTFLNIIQANVGDGTIIMNNL 488
Cdd:smart00100  81 AASAAAVALELATLLRIDFRDFLQLLPELPQLLLELLLEL 120
Ank_2 pfam12796
Ankyrin repeats (3 copies);
522-614 2.07e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 83.63  E-value: 2.07e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768   522 LCFAAIREDDLLLHQLLKRGLDPNESDNNGRTPLHIAASKGTLNCVLLLLEyHADPNCRDaEGSVPLWEAMVEGHEKVVK 601
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 15225768   602 VLLEHGSTIDAGD 614
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
555-678 9.49e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.00  E-value: 9.49e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768   555 LHIAASKGTLNCVLLLLEYHADPNCRDAEGSVPLWEAMVEGHEKVVKVLLEHGSTidagdvghfactaaeqgnlkllkei 634
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV------------------------- 55

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 15225768   635 vlhggdvtRPRATGTSALHTAVCEENIEMVKYLLEQGADVNKQD 678
Cdd:pfam12796  56 --------NLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 391-477 5.21e-16

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: 73.80  E-value: 5.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768   391 EYFPPKEDVILQNEAPTDFYILVNGTADLVDVDT-GTESIVREVKAGDIIGEIGVLCYRPQLFTVRTKRLCQLLRMNRTT 469
Cdd:pfam00027   2 RSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEdGREQILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPRED 81


                  ....*...
gi 15225768   470 FLNIIQAN 477
Cdd:pfam00027  82 FLELLERD 89
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 537-684 8.59e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 77.40  E-value: 8.59e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768  537 LLKRGLDPNESDNNGRTPLHIAASK--GTLNCVLLLLEYHADPNCRDAEGSVPLWEAMVEGHE--KVVKVLLEHGSTIDA 612
Cdd:PHA03100  92 LLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINA 171

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15225768  613 GDvghfactaaeqgNLKLLKEivlHGGDVTRPRATGTSALHTAVCEENIEMVKYLLEQGADVNKQDMHGWTP 684
Cdd:PHA03100 172 KN------------RVNYLLS---YGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTP 228
Ion_trans_2 pfam07885
Ion channel; This family includes the two membrane helix type ion channels found in bacteria.
 231-293 1.71e-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: 66.14  E-value: 1.71e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15225768   231 FLEESLWMRYVTSMYWSITTLTTVGYGDLHPVNTKEMIFDIFYMLFNLGLTAYLIGNMTNLVV 293
Cdd:pfam07885  15 LLEEGWEWSFLDALYFSFVTLTTVGYGDIVPLTDAGRLFTIFYILIGIPLFAIFLAVLGRFLT 77
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 373-513 1.98e-13

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: 70.02  E-value: 1.98e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768 373 FRGVSNDLLFQLVSEMKAEYFPPKEDVILQNEAPTDFYILVNGTADLVDVD-TGTESIVREVKAGDIIGEIGVLCYRPQL 451
Cdd:COG0664   1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISeDGREQILGFLGPGDFFGELSLLGGEPSP 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15225768 452 FTVRTKRLCQLLRMNRTTFLNIIQANVGDGTIIMNNLLQHLKEMNDPVMTNVLLEIENMLAR 513
Cdd:COG0664  81 ATAEALEDSELLRIPREDLEELLERNPELARALLRLLARRLRQLQERLVSLAFLSAEERLAR 142
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 522-696 2.31e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 73.10  E-value: 2.31e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768  522 LCFAAIREDDLLLHQLLKRGLDPNESDNNGRTPLHIAASKGTLNCVLLLLEYHADPNCRDAEGSVPLWEAMVEGHEKVVK 601
Cdd:PHA02875   6 LCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768  602 VLLEHGSTID-----AGDVGHFACTAAEqgNLKLLKEIVLHGGDVTRPRATGTSALHTAVCEENIEMVKYLLEQGADVNK 676
Cdd:PHA02875  86 ELLDLGKFADdvfykDGMTPLHLATILK--KLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDI 163

                        170       180
                 ....*....|....*....|
gi 15225768  677 QDMHGWTPRDLAEQQGHEDI 696
Cdd:PHA02875 164 EDCCGCTPLIIAMAKGDIAI 183
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 533-684 3.53e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 72.69  E-value: 3.53e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768  533 LLHQLLKRGLDPNESDNNGRTPLHIAASKGTLNCVLLLLEYHADPNCRDAEGSVPLWEAMVEGHEKVVKVLLEHGSTIDA 612
Cdd:PHA02874 106 MIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANV 185

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15225768  613 GDVG-----HFactAAEQGNLKLLKEIVLHGGDVTRPRATGTSALHTAVCeENIEMVKyLLEQGADVNKQDMHGWTP 684
Cdd:PHA02874 186 KDNNgesplHN---AAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII-HNRSAIE-LLINNASINDQDIDGSTP 257
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 537-691 4.18e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 72.61  E-value: 4.18e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768  537 LLKRGLDPNESD-NNGRTPLHIAASKGTLNCVLLLLEYHADPNCRDAEGSVPLWEAMVEGHEKVVKVLLEHGSTIDAGDV 615
Cdd:PHA02878 153 LLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDK 232

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768  616 G-----HFACTAAEqgNLKLLKEIVLHGGDVT-RPRATGTSALHTAVCEEniEMVKYLLEQGADVNKQDMHGWTPRDLAE 689
Cdd:PHA02878 233 CgntplHISVGYCK--DYDILKLLLEHGVDVNaKSYILGLTALHSSIKSE--RKLKLLLEYGADINSLNSYKLTPLSSAV 308


                 ..
gi 15225768  690 QQ 691
Cdd:PHA02878 309 KQ 310
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 527-699 2.55e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 70.48  E-value: 2.55e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768  527 IREDDLLLHQ-LLKRGLDPNESDNNGRTPLHIAASKGTLNCVLLLLEYHADPNCRDAEGSVPLWEAMVEGHEKVVKVLLE 605
Cdd:PHA02876 153 IQQDELLIAEmLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIID 232

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768  606 HGSTIDAGDVGHFACTAAEQGNLKLLkeIVLHGGDVTRPRATGTSALHTAVCEENI-EMVKYLLEQGADVNKQDMHGWTP 684
Cdd:PHA02876 233 NRSNINKNDLSLLKAIRNEDLETSLL--LYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETP 310

                        170
                 ....*....|....*..
gi 15225768  685 RDLAEQQGH--EDIKAL 699
Cdd:PHA02876 311 LYLMAKNGYdtENIRTL 327
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 518-606 4.90e-12

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 69.54  E-value: 4.90e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768  518 LPLNLCFAAIREDDLLLHQLLKRGLDPNESDNNGRTPLHIAASKGTLNCVLLLLEYHADPNCRDAEGSVPLWEAMVEGHE 597
Cdd:PTZ00322  82 LTVELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFR 161


                 ....*....
gi 15225768  598 KVVKVLLEH 606
Cdd:PTZ00322 162 EVVQLLSRH 170
Ank_2 pfam12796
Ankyrin repeats (3 copies);
622-696 5.02e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.44  E-value: 5.02e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15225768   622 AAEQGNLKLLKEIVLHGGDVTRPRATGTSALHTAVCEENIEMVKYLLEQgADVNKQDmHGWTPRDLAEQQGHEDI 696
Cdd:pfam12796   4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEI 76
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 494-675 7.63e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 65.01  E-value: 7.63e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768  494 EMNDPVMTNVLLEIENMLARGKM---------DLPLNLcfAAIREDDLLLHQLLKRGLDPNESDNNGRTPLHIAASKGTL 564
Cdd:PHA02875  71 ELHDAVEEGDVKAVEELLDLGKFaddvfykdgMTPLHL--ATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768  565 NCVLLLLEYHADPNCRDAEGSVPLWEAMVEGHEKVVKVLLEHGSTIDagdvghfactaaeqgnlkllkeIVLHGGDVTrp 644
Cdd:PHA02875 149 KGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANID----------------------YFGKNGCVA-- 204

                        170       180       190
                 ....*....|....*....|....*....|.
gi 15225768  645 ratgtsALHTAVCEENIEMVKYLLEQGADVN 675
Cdd:PHA02875 205 ------ALCYAIENNKIDIVRLFIKRGADCN 229
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 533-678 1.88e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 63.92  E-value: 1.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768  533 LLHQLLKRGLDPNESDNNGRTPLHIAASKGTLNCVLLLLEYHADPNCRDAEGSVPL----WEAMVEGHEK-VVKVLLEHG 607
Cdd:PHA03100  17 NIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLhylsNIKYNLTDVKeIVKLLLEYG 96

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15225768  608 STIDAGDVGH----FACTAAEQGNLKLLKEIVLHGGDVTRPRATGTSALHTAV--CEENIEMVKYLLEQGADVNKQD 678
Cdd:PHA03100  97 ANVNAPDNNGitplLYAISKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLesNKIDLKILKLLIDKGVDINAKN 173
PHA03095 PHA03095
ankyrin-like protein; Provisional
 517-684 2.85e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 63.51  E-value: 2.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768  517 DLPLNLCF-AAIREDdlLLHQLLKRGLDPNESDNNGRTPLHI-AASKGTLNCVL-LLLEYHADPNCRDAEGSVPLwEAMV 593
Cdd:PHA03095  84 FTPLHLYLyNATTLD--VIKLLIKAGADVNAKDKVGRTPLHVyLSGFNINPKVIrLLLRKGADVNALDLYGMTPL-AVLL 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768  594 EGHE---KVVKVLLEHGSTIDAGDVGHFacTAAEQ------GNLKLLKEIVLHGGDVTRPRATGTSALHTAV--CEENIE 662
Cdd:PHA03095 161 KSRNanvELLRLLIDAGADVYAVDDRFR--SLLHHhlqsfkPRARIVRELIRAGCDPAATDMLGNTPLHSMAtgSSCKRS 238

                        170       180
                 ....*....|....*....|..
gi 15225768  663 MVKYLLEQGADVNKQDMHGWTP 684
Cdd:PHA03095 239 LVLPLLIAGISINARNRYGQTP 260
KHA cd17073
KHA, dimerization domain of potassium ion channel, similar to doublecortin-like domain, found ...
 803-855 3.86e-10

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: 56.46  E-value: 3.86e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 15225768 803 GKLVLLPGSFKELLELGSNKFGIVATKVMNKdNNAEIDDVDVIRDGDHLIFAT 855
Cdd:cd17073  14 GKVIALPSTLSELLKIASEKLGIPAKRLYTG-SGGEIDDIALIRDDDVLYVSE 65
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 534-709 4.63e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 63.16  E-value: 4.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768  534 LHQLLKRGLDPNESDNNGRTPLHIAAS-KGTLNCVLLLLEYHADPNCRDAEGSVPLWEAMVEGHEKVVKVLLEHGSTIDA 612
Cdd:PHA02876 324 IRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEA 403

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768  613 -----GDVGHFACTAAEQgnLKLLKEIVLHGGDVTRPRATGTSALHTAvCEEN--IEMVKYLLEQGADVNKQDMHGWTPR 685
Cdd:PHA02876 404 lsqkiGTALHFALCGTNP--YMSVKTLIDRGANVNSKNKDLSTPLHYA-CKKNckLDVIEMLLDNGADVNAINIQNQYPL 480

                        170       180
                 ....*....|....*....|....*
gi 15225768  686 DLA-EQQGHEDIKALFREKLHERRV 709
Cdd:PHA02876 481 LIAlEYHGIVNILLHYGAELRDSRV 505
PHA02946 PHA02946
ankyin-like protein; Provisional
 530-684 9.02e-10

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 61.99  E-value: 9.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768  530 DDLLLHQLLKRGLDPNESDNNGRTPLHIAASKGTLNCVLLLLEYHADPNCRDAEGSVPLWEAMVEGHEKV--VKVLLEHG 607
Cdd:PHA02946  51 DERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIerINLLVQYG 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768  608 STI-----DAGDVGHFACTAAEQgnlKLLKEIVLHGGDVTRPRATGTSALHTAVCEEN--IEMVKYLLEQGADVNKQDMH 680
Cdd:PHA02946 131 AKInnsvdEEGCGPLLACTDPSE---RVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNpkASTISWMMKLGISPSKPDHD 207


                 ....
gi 15225768  681 GWTP 684
Cdd:PHA02946 208 GNTP 211
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 526-688 1.71e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 60.75  E-value: 1.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768  526 AIREDDL-LLHQLLKRGLDPNESDNNGRTPLHIAASKGTLNCVLLLLEYHADPNCRDAEGSVPLWEAMVEGHEKVVKVLL 604
Cdd:PHA02874 131 AIKKGDLeSIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLI 210

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768  605 EHGSTIDAGDVGHFACTAAEQGNLKLLKEIVLHGGDVTRPRATGTSALHTAV---CeeNIEMVKYLLEQGADVNKQDMHG 681
Cdd:PHA02874 211 DHGNHIMNKCKNGFTPLHNAIIHNRSAIELLINNASINDQDIDGSTPLHHAInppC--DIDIIDILLYHKADISIKDNKG 288


                 ....*..
gi 15225768  682 WTPRDLA 688
Cdd:PHA02874 289 ENPIDTA 295
PHA03095 PHA03095
ankyrin-like protein; Provisional
 537-703 2.14e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 60.81  E-value: 2.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768  537 LLKRGLDPNESDNNGRTPLHI-----AASKGTLNcvlLLLEYHADPNCRDAEGSVPLWEAMVEGH--EKVVKVLLEHGST 609
Cdd:PHA03095 138 LLRKGADVNALDLYGMTPLAVllksrNANVELLR---LLIDAGADVYAVDDRFRSLLHHHLQSFKprARIVRELIRAGCD 214

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768  610 IDAGDVG-----HFACTAAEQGNLKLLKeIVLHGGDVTRPRATGTSALHTAVCEENIEMVKYLLEQGADVNKQDMHGWTP 684
Cdd:PHA03095 215 PAATDMLgntplHSMATGSSCKRSLVLP-LLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTP 293

                        170
                 ....*....|....*....
gi 15225768  685 RDLAEQQGHEDIKALFREK 703
Cdd:PHA03095 294 LSLMVRNNNGRAVRAALAK 312
PHA03095 PHA03095
ankyrin-like protein; Provisional
 536-686 2.42e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 60.42  E-value: 2.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768  536 QLLKRGLDPNESDNNGRTPLHIAASKGTLNC---VLLLLEYHADPNCRDAEGSVPLweamvegHekvvkVLLEHGSTIDA 612
Cdd:PHA03095  32 RLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPL-------H-----LYLYNATTLDV 99

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15225768  613 gdvghfactaaeqgnLKLLkeiVLHGGDVTRPRATGTSALHTAVCEENI--EMVKYLLEQGADVNKQDMHGWTPRD 686
Cdd:PHA03095 100 ---------------IKLL---IKAGADVNAKDKVGRTPLHVYLSGFNInpKVIRLLLRKGADVNALDLYGMTPLA 157
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
522-614 3.64e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 58.81  E-value: 3.64e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768 522 LCFAAIREDDLLLHQLLKRGLDPNESDNNGRTPLHIAASKGTLNCVLLLLEYHADPNCRDAEGSVPLWEAMVEGHEKVVK 601
Cdd:COG0666 190 LHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVK 269

                        90
                ....*....|...
gi 15225768 602 VLLEHGSTIDAGD 614
Cdd:COG0666 270 LLLLALLLLAAAL 282
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 537-612 6.21e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 58.91  E-value: 6.21e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15225768  537 LLKRGLDPNESDNNGRTPLHIAASKGTLNCVLLLLEYHADPNCRDAEGSVPLWEAMVEGHEKVVKVLLEHGSTIDA 612
Cdd:PHA03100 178 LLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
Ank_5 pfam13857
Ankyrin repeats (many copies);
537-588 1.06e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 51.96  E-value: 1.06e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 15225768   537 LLKRG-LDPNESDNNGRTPLHIAASKGTLNCVLLLLEYHADPNCRDAEGSVPL 588
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
Ank_4 pfam13637
Ankyrin repeats (many copies);
522-571 1.77e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.12  E-value: 1.77e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 15225768   522 LCFAAIREDDLLLHQLLKRGLDPNESDNNGRTPLHIAASKGTLNCVLLLL 571
Cdd:pfam13637   5 LHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 553-684 3.99e-08

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 56.94  E-value: 3.99e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768 553 TPLHIAASKGTLNCVLLLLEY-HADPNCRDAEGSVPLWEAMVEGHEKVVKVLLEhgstiDAGDVGHFACT---------- 621
Cdd:cd22192  19 SPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLME-----AAPELVNEPMTsdlyqgetal 93

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15225768 622 --AAEQGNLKLLKEIVLHGGDVTRPRATGT--------------SALHTAVCEENIEMVKYLLEQGADVNKQDMHGWTP 684
Cdd:cd22192  94 hiAVVNQNLNLVRELIARGADVVSPRATGTffrpgpknliyygeHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTV 172
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 533-703 1.16e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 54.97  E-value: 1.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768  533 LLHQLLK-RGLDPNESDNNGRTPLHIAASKGTLNCVLLLLEYHADPNCRDAEGSVPLWEAMVEGHEKVVKVLLEHG---S 608
Cdd:PHA02874  16 AIEKIIKnKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGvdtS 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768  609 TIDAGDVghfactaaeqgNLKLLKEIVLHGGDVTRPRATGTSALHTAVCEENIEMVKYLLEQGADVNKQDMHGWTPRDLA 688
Cdd:PHA02874  96 ILPIPCI-----------EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIA 164

                        170
                 ....*....|....*
gi 15225768  689 EQQGHEDIKALFREK 703
Cdd:PHA02874 165 IKHNFFDIIKLLLEK 179
Ank_4 pfam13637
Ankyrin repeats (many copies);
551-604 6.78e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.88  E-value: 6.78e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 15225768   551 GRTPLHIAASKGTLNCVLLLLEYHADPNCRDAEGSVPLWEAMVEGHEKVVKVLL 604
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 551-683 9.00e-07

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 52.71  E-value: 9.00e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768 551 GRTPLHIAASKGTLNCVLLLLEYHADPNCRDAEGSV--------------PLWEAMVEGHEKVVKVLLEHGSTIDAGD-- 614
Cdd:cd22192  89 GETALHIAVVNQNLNLVRELIARGADVVSPRATGTFfrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDsl 168

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15225768 615 ---VGHFACTAAEQGNLKLLKEIVL----HGGDV---TRPRATGTSALHTAVCEENIEMVKYLleqgadVNKQDMHGWT 683
Cdd:cd22192 169 gntVLHILVLQPNKTFACQMYDLILsydkEDDLQpldLVPNNQGLTPFKLAAKEGNIVMFQHL------VQKRRHIQWT 241
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 533-684 1.55e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 51.42  E-value: 1.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768  533 LLHQLLKRGLDPNESDNNGRTPLHIAASKGTLNCV---------------------------------LLLLEYHADPNC 579
Cdd:PHA02878  52 VVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMkemirsinkcsvfytlvaikdafnnrnveifkiILTNRYKNIQTI 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768  580 RDAEGSVPLWEAMVEGheKVVKVLLEHGSTIDAGDVG------HFactAAEQGNLKLLKEIVLHGGDVTRPRATGTSALH 653
Cdd:PHA02878 132 DLVYIDKKSKDDIIEA--EITKLLLSYGADINMKDRHkgntalHY---ATENKDQRLTELLLSYGANVNIPDKTNNSPLH 206

                        170       180       190
                 ....*....|....*....|....*....|.
gi 15225768  654 TAVCEENIEMVKYLLEQGADVNKQDMHGWTP 684
Cdd:PHA02878 207 HAVKHYNKPIVHILLENGASTDARDKCGNTP 237
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 550-581 1.89e-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: 44.97  E-value: 1.89e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 15225768   550 NGRTPLHIAASK-GTLNCVLLLLEYHADPNCRD 581
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 556-614 2.21e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.44  E-value: 2.21e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15225768  556 HIAASKGTLNcVLLLLEYHADPNCRDAEGSVPLWEAMVEGHEKVVKVLLEHGSTIDAGD 614
Cdd:PTZ00322  88 QLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLD 145
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 550-579 1.07e-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: 42.96  E-value: 1.07e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 15225768    550 NGRTPLHIAASKGTLNCVLLLLEYHADPNC 579
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_2 pfam12796
Ankyrin repeats (3 copies);
652-696 1.41e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 44.34  E-value: 1.41e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 15225768   652 LHTAVCEENIEMVKYLLEQGADVNKQDMHGWTPRDLAEQQGHEDI 696
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEI 45
Ank_4 pfam13637
Ankyrin repeats (many copies);
648-696 1.45e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.03  E-value: 1.45e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 15225768   648 GTSALHTAVCEENIEMVKYLLEQGADVNKQDMHGWTPRDLAEQQGHEDI 696
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEV 49
Ank_4 pfam13637
Ankyrin repeats (many copies);
622-668 4.35e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.88  E-value: 4.35e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 15225768   622 AAEQGNLKLLKEIVLHGGDVTRPRATGTSALHTAVCEENIEMVKYLL 668
Cdd:pfam13637   8 AAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 648-678 4.67e-05

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: 41.12  E-value: 4.67e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 15225768   648 GTSALHTAVCEE-NIEMVKYLLEQGADVNKQD 678
Cdd:pfam00023   2 GNTPLHLAAGRRgNLEIVKLLLSKGADVNARD 33
Ank_5 pfam13857
Ankyrin repeats (many copies);
640-688 5.74e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.56  E-value: 5.74e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 15225768   640 DVTRPRATGTSALHTAVCEENIEMVKYLLEQGADVNKQDMHGWTPRDLA 688
Cdd:pfam13857   8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 550-697 7.23e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 46.14  E-value: 7.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768  550 NGRTPLHIAASKGTLNCVLLLLEYHADPNCRDAEGSVPLWEAMVEGHEKVVKVLLEHGSTIDAG--DVGHFACTAAEQGN 627
Cdd:PHA02875   1 MDQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKypDIESELHDAVEEGD 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15225768  628 LKLLKEIVLHG---GDVTRPRatGTSALHTAVCEENIEMVKYLLEQGADVNKQDMHGWTPRDLAEQQGheDIK 697
Cdd:PHA02875  81 VKAVEELLDLGkfaDDVFYKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMG--DIK 149
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 648-676 1.84e-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: 39.11  E-value: 1.84e-04
                           10        20
                   ....*....|....*....|....*....
gi 15225768    648 GTSALHTAVCEENIEMVKYLLEQGADVNK 676
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02798 PHA02798
ankyrin-like protein; Provisional
 537-675 2.02e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 44.83  E-value: 2.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768  537 LLKRGLDPNESDNNGRTPL-----HIAASKGTLNCVLLLLEYHADPNCRDAEGSVPLWeamveghekvvkvLLEHGSTID 611
Cdd:PHA02798  57 FINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLY-------------CLLSNGYIN 123

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15225768  612 agdvghfactaaeqgNLKLLKEIVLHGGDVTRPRATGTSALHTAV---CEENIEMVKYLLEQGADVN 675
Cdd:PHA02798 124 ---------------NLEILLFMIENGADTTLLDKDGFTMLQVYLqsnHHIDIEIIKLLLEKGVDIN 175
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 550-579 2.43e-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: 38.78  E-value: 2.43e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 15225768   550 NGRTPLHIAASKGTLNCVLLLLEYHADPNC 579
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA03095 PHA03095
ankyrin-like protein; Provisional
 483-639 3.14e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 44.25  E-value: 3.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768  483 IIMNNLLQHLKEMNDP----VMTNVLLEIENMLARGKMDLPLNLCFAAIREDDLLLHQLLKRGLDPNESDNNGRTPLHIA 558
Cdd:PHA03095 185 DRFRSLLHHHLQSFKPrariVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVLPLLIAGISINARNRYGQTPLHYA 264

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768  559 ASKGTLNCVLLLLEYHADPNCRDAEGSVPLWEAMVEGHEKVVKVLLE---HGSTID-----AGDVGHFACTAAeqgNLKL 630
Cdd:PHA03095 265 AVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAknpSAETVAatlntASVAGGDIPSDA---TRLC 341


                 ....*....
gi 15225768  631 LKEIVLHGG 639
Cdd:PHA03095 342 VAKVVLRGA 350
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 576-675 3.69e-04

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 44.30  E-value: 3.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768   576 DPNCRDAEGSVPLWEAMVEG-HEKVVKVLLEHGSTIDAGDVGHFACTAAEQGNLKLLKEIVL--HGGDVTRPRAT----- 647
Cdd:TIGR00870  44 NINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAVGDTLLHAISLEYVDAVEAILLHLLaaFRKSGPLELANdqyts 123

                          90       100       110
                  ....*....|....*....|....*....|..
gi 15225768   648 ----GTSALHTAVCEENIEMVKYLLEQGADVN 675
Cdd:TIGR00870 124 eftpGITALHLAAHRQNYEIVKLLLERGASVP 155
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
393-477 8.95e-04

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 41.51  E-value: 8.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225768  393 FPPKEDVILQNEAPTDFYILVNGTAD-LVDVDTGTESIVREVKAGDIIGEIGvlcyrpqLF--------TVRTKRLCQLL 463
Cdd:PRK11753  25 YPAKSTLIHAGEKAETLYYIVKGSVAvLIKDEEGKEMILSYLNQGDFIGELG-------LFeegqersaWVRAKTACEVA 97

                         90
                 ....*....|....
gi 15225768  464 RMNRTTFLNIIQAN 477
Cdd:PRK11753  98 EISYKKFRQLIQVN 111
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 650-676 2.13e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.47  E-value: 2.13e-03
                          10        20
                  ....*....|....*....|....*..
gi 15225768   650 SALHTAVCEENIEMVKYLLEQGADVNK 676
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADINA 30
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 551-612 2.64e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 41.40  E-value: 2.64e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15225768 551 GRTPLHIAASKGTLNCVLLLLEYHADPNCRDAE-------------GSVPLWEAMVEGHEKVVKVLLEHGSTIDA 612
Cdd:cd21882  73 GQTALHIAIENRNLNLVRLLVENGADVSARATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPAA 147
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH