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Conserved domains on  [gi|161078304|ref|NP_001097796|]
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uncharacterized protein Dmel_CG6966, isoform B [Drosophila melanogaster]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 11429852)

ankyrin repeat domain-containing protein; ANK proteins mediate specific protein-protein interactions without necessarily recognizing specific primary sequences which allows for one ankyrin repeat domain to recognize and bind to a variety of intracellular substrates and may be involved in a wide array of functions

Gene Ontology:  GO:0005515
PubMed:  17176038
SCOP:  4000366

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
2-236 6.14e-41

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 150.87  E-value: 6.14e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304   2 DYKFIVFNAARDNNLAQLKATLYNKSSVEVGSLISAKVN-------GATPLVISCRNGHYDIVEYLLTKcRANVEQVGSv 74
Cdd:COG0666   41 LLALLALALADALGALLLLAAALAGDLLVALLLLAAGADinakddgGNTLLHAAARNGDLEIVKLLLEA-GADVNARDK- 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304  75 sfdgepiEDAPPLWCAAAAGHLGIVKMLVRRGANVNSTTRTNSTPLRAACFDGHYEIVKYLVHHGADFEVANRHGHTCLM 154
Cdd:COG0666  119 -------DGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLH 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304 155 IACYKGHFRIAQYLLSLNADVNRCSVKGNTALHDCAESGSLQILQLLLKHGATMD-VDYYGMTPLLAASVTGHMPIVEHL 233
Cdd:COG0666  192 LAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNaKDKDGLTALLLAAAAGAALIVKLL 271


                 ...
gi 161078304 234 ITL 236
Cdd:COG0666  272 LLA 274
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
525-612 3.01e-10

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 61.89  E-value: 3.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304 525 VRVRFDRTALHYACYREgtlagrypscqfpSVTLAKALLEVGADPNAIDEAGNTPLHLATMQPYVEpLSHILLEGGAHLD 604
Cdd:COG0666  115 ARDKDGETPLHLAAYNG-------------NLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLE-IVKLLLEAGADVN 180


                 ....*...
gi 161078304 605 TKNYAGET 612
Cdd:COG0666  181 ARDNDGET 188
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
2-236 6.14e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 150.87  E-value: 6.14e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304   2 DYKFIVFNAARDNNLAQLKATLYNKSSVEVGSLISAKVN-------GATPLVISCRNGHYDIVEYLLTKcRANVEQVGSv 74
Cdd:COG0666   41 LLALLALALADALGALLLLAAALAGDLLVALLLLAAGADinakddgGNTLLHAAARNGDLEIVKLLLEA-GADVNARDK- 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304  75 sfdgepiEDAPPLWCAAAAGHLGIVKMLVRRGANVNSTTRTNSTPLRAACFDGHYEIVKYLVHHGADFEVANRHGHTCLM 154
Cdd:COG0666  119 -------DGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLH 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304 155 IACYKGHFRIAQYLLSLNADVNRCSVKGNTALHDCAESGSLQILQLLLKHGATMD-VDYYGMTPLLAASVTGHMPIVEHL 233
Cdd:COG0666  192 LAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNaKDKDGLTALLLAAAAGAALIVKLL 271


                 ...
gi 161078304 234 ITL 236
Cdd:COG0666  272 LLA 274
Ank_2 pfam12796
Ankyrin repeats (3 copies);
120-206 9.27e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.40  E-value: 9.27e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304  120 LRAACFDGHYEIVKYLVHHGADFEVANRHGHTCLMIACYKGHFRIAQYLLSlNADVNRCSvKGNTALHDCAESGSLQILQ 199
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78


                  ....*..
gi 161078304  200 LLLKHGA 206
Cdd:pfam12796  79 LLLEKGA 85
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 98-234 2.26e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 85.10  E-value: 2.26e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304  98 IVKMLVRRGANVNSTTRTNSTPLRAACFDGHY-----EIVKYLVHHGADFEVANRHGHTCLMIACYK--GHFRIAQYLLS 170
Cdd:PHA03100  50 VVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLD 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304 171 LNADVNRCSVKGNTALHDCAESGS--LQILQLLLKHGATMD----VDY-------------YGMTPLLAASVTGHMPIVE 231
Cdd:PHA03100 130 NGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINaknrVNYllsygvpinikdvYGFTPLHYAVYNNNPEFVK 209


                 ...
gi 161078304 232 HLI 234
Cdd:PHA03100 210 YLL 212
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
525-612 3.01e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 61.89  E-value: 3.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304 525 VRVRFDRTALHYACYREgtlagrypscqfpSVTLAKALLEVGADPNAIDEAGNTPLHLATMQPYVEpLSHILLEGGAHLD 604
Cdd:COG0666  115 ARDKDGETPLHLAAYNG-------------NLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLE-IVKLLLEAGADVN 180


                 ....*...
gi 161078304 605 TKNYAGET 612
Cdd:COG0666  181 ARDNDGET 188
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 7-234 6.25e-09

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: 58.87  E-value: 6.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304   7 VFNAARDNNLAQLKATLYNKSS--VEVGSLisakvnGATPLVISCRNGHYDIVEYLLTKCRANV-EQVGSVSFDGEPied 83
Cdd:cd22192   21 LLLAAKENDVQAIKKLLKCPSCdlFQRGAL------GETALHVAALYDNLEAAVVLMEAAPELVnEPMTSDLYQGET--- 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304  84 apPLWCAAAAGHLGIVKMLVRRGANVnSTTRTNSTPLR----------------AACFdGHYEIVKYLVHHGADFEVANR 147
Cdd:cd22192   92 --ALHIAVVNQNLNLVRELIARGADV-VSPRATGTFFRpgpknliyygehplsfAACV-GNEEIVRLLIEHGADIRAQDS 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304 148 HGHTCLMIacykghfriaqylLSLNADVNRcsvkgntalhdcaesgSLQILQLLL---KHGATMDVD----YYGMTPLLA 220
Cdd:cd22192  168 LGNTVLHI-------------LVLQPNKTF----------------ACQMYDLILsydKEDDLQPLDlvpnNQGLTPFKL 218

                        250
                 ....*....|....
gi 161078304 221 ASVTGHMPIVEHLI 234
Cdd:cd22192  219 AAKEGNIVMFQHLV 232
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 471-637 1.25e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 54.58  E-value: 1.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304 471 HQHDCNHDPNALSRTMISAIHIGC------LLSSLLDTDALS-PEMRRQVMGALYRLN-RLKVRVRFDRTALHYACyREG 542
Cdd:PHA02874  57 HGADINHINTKIPHPLLTAIKIGAhdiiklLIDNGVDTSILPiPCIEKDMIKTILDCGiDVNIKDAELKTFLHYAI-KKG 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304 543 TLAgrypscqfpsvtLAKALLEVGADPNAIDEAGNTPLHLATMQPYVEPLShILLEGGAHLDTKNYAGEtfesllapTPM 622
Cdd:PHA02874 136 DLE------------SIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIK-LLLEKGAYANVKDNNGE--------SPL 194

                        170
                 ....*....|....*
gi 161078304 623 HkiiDPMKYTTLACL 637
Cdd:PHA02874 195 H---NAAEYGDYACI 206
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 8-202 5.69e-05

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: 46.23  E-value: 5.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304    8 FNAARDNNLAQLKATL-YNKSSVEVG-SLISAkvngatplvisCRNGHYDIVEYLLTKCRANVEQVGSVSF-----DGEP 80
Cdd:TIGR00870  57 FVAAIENENLELTELLlNLSCRGAVGdTLLHA-----------ISLEYVDAVEAILLHLLAAFRKSGPLELandqyTSEF 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304   81 IEDAPPLWCAAAAGHLGIVKMLVRRGANVN---------STTRTNS-----TPLR-AACFdGHYEIVKYLVHHGAD---- 141
Cdd:TIGR00870 126 TPGITALHLAAHRQNYEIVKLLLERGASVParacgdffvKSQGVDSfyhgeSPLNaAACL-GSPSIVALLSEDPADilta 204

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161078304  142 FEVANRHGHTCLMIACYK---GHFRIAQYLLSLNADVNRCSVK---------GNTALHDCAESGSLQILQLLL 202
Cdd:TIGR00870 205 DSLGNTLLHLLVMENEFKaeyEELSCQMYNFALSLLDKLRDSKelevilnhqGLTPLKLAAKEGRIVLFRLKL 277
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 148-176 2.90e-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: 38.34  E-value: 2.90e-04
                           10        20
                   ....*....|....*....|....*....
gi 161078304   148 HGHTCLMIACYKGHFRIAQYLLSLNADVN 176
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank_4 pfam13637
Ankyrin repeats (many copies);
531-585 1.02e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.64  E-value: 1.02e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 161078304  531 RTALHYACYRegtlaGRYPSCQFpsvtlakaLLEVGADPNAIDEAGNTPLHLATM 585
Cdd:pfam13637   2 LTALHAAAAS-----GHLELLRL--------LLEKGADINAVDGNGETALHFAAS 43
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
2-236 6.14e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 150.87  E-value: 6.14e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304   2 DYKFIVFNAARDNNLAQLKATLYNKSSVEVGSLISAKVN-------GATPLVISCRNGHYDIVEYLLTKcRANVEQVGSv 74
Cdd:COG0666   41 LLALLALALADALGALLLLAAALAGDLLVALLLLAAGADinakddgGNTLLHAAARNGDLEIVKLLLEA-GADVNARDK- 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304  75 sfdgepiEDAPPLWCAAAAGHLGIVKMLVRRGANVNSTTRTNSTPLRAACFDGHYEIVKYLVHHGADFEVANRHGHTCLM 154
Cdd:COG0666  119 -------DGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLH 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304 155 IACYKGHFRIAQYLLSLNADVNRCSVKGNTALHDCAESGSLQILQLLLKHGATMD-VDYYGMTPLLAASVTGHMPIVEHL 233
Cdd:COG0666  192 LAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNaKDKDGLTALLLAAAAGAALIVKLL 271


                 ...
gi 161078304 234 ITL 236
Cdd:COG0666  272 LLA 274
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-234 6.04e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 148.18  E-value: 6.04e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304   1 MDYKFIVFNAARDNNLAQLKATLYNKSSVEVGSLISAKVNGATPLVISCRNGHYDIVEYLLTKCRANVeqvgsvsfDGEP 80
Cdd:COG0666   13 AALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI--------NAKD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304  81 IEDAPPLWCAAAAGHLGIVKMLVRRGANVNSTTRTNSTPLRAACFDGHYEIVKYLVHHGADFEVANRHGHTCLMIACYKG 160
Cdd:COG0666   85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANG 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 161078304 161 HFRIAQYLLSLNADVNRCSVKGNTALHDCAESGSLQILQLLLKHGATMDV-DYYGMTPLLAASVTGHMPIVEHLI 234
Cdd:COG0666  165 NLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAkDNDGKTALDLAAENGNLEIVKLLL 239
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
8-206 8.46e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 130.84  E-value: 8.46e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304   8 FNAARDNNLAQLKATLYNKSSVEVGSLisakvNGATPLVISCRNGHYDIVEYLLTKcRANVEQVGSvsfdgepiEDAPPL 87
Cdd:COG0666   92 HAAARNGDLEIVKLLLEAGADVNARDK-----DGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDN--------DGNTPL 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304  88 WCAAAAGHLGIVKMLVRRGANVNSTTRTNSTPLRAACFDGHYEIVKYLVHHGADFEVANRHGHTCLMIACYKGHFRIAQY 167
Cdd:COG0666  158 HLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKL 237

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 161078304 168 LLSLNADVNRCSVKGNTALHDCAESGSLQILQLLLKHGA 206
Cdd:COG0666  238 LLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALL 276
Ank_2 pfam12796
Ankyrin repeats (3 copies);
120-206 9.27e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.40  E-value: 9.27e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304  120 LRAACFDGHYEIVKYLVHHGADFEVANRHGHTCLMIACYKGHFRIAQYLLSlNADVNRCSvKGNTALHDCAESGSLQILQ 199
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78


                  ....*..
gi 161078304  200 LLLKHGA 206
Cdd:pfam12796  79 LLLEKGA 85
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
40-186 1.11e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 90.01  E-value: 1.11e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304  40 NGATPLVISCRNGHYDIVEYLLtKCRANVEQVGSvsfdgepiEDAPPLWCAAAAGHLGIVKMLVRRGANVNSTTRTNSTP 119
Cdd:COG0666  152 DGNTPLHLAAANGNLEIVKLLL-EAGADVNARDN--------DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTA 222

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 161078304 120 LRAACFDGHYEIVKYLVHHGADFEVANRHGHTCLMIACYKGHFRIAQYLLSLNADVNRCSVKGNTAL 186
Cdd:COG0666  223 LDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
87-177 2.36e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 83.24  E-value: 2.36e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304   87 LWCAAAAGHLGIVKMLVRRGANVNSTTRTNSTPLRAACFDGHYEIVKYLVHHgADFEVANrHGHTCLMIACYKGHFRIAQ 166
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|.
gi 161078304  167 YLLSLNADVNR 177
Cdd:pfam12796  79 LLLEKGADINV 89
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 98-234 2.26e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 85.10  E-value: 2.26e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304  98 IVKMLVRRGANVNSTTRTNSTPLRAACFDGHY-----EIVKYLVHHGADFEVANRHGHTCLMIACYK--GHFRIAQYLLS 170
Cdd:PHA03100  50 VVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLD 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304 171 LNADVNRCSVKGNTALHDCAESGS--LQILQLLLKHGATMD----VDY-------------YGMTPLLAASVTGHMPIVE 231
Cdd:PHA03100 130 NGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINaknrVNYllsygvpinikdvYGFTPLHYAVYNNNPEFVK 209


                 ...
gi 161078304 232 HLI 234
Cdd:PHA03100 210 YLL 212
Ank_2 pfam12796
Ankyrin repeats (3 copies);
153-234 1.01e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.54  E-value: 1.01e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304  153 LMIACYKGHFRIAQYLLSLNADVNRCSVKGNTALHDCAESGSLQILQLLLKHGATmDVDYYGMTPLLAASVTGHMPIVEH 232
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV-NLKDNGRTALHYAARSGHLEIVKL 79


                  ..
gi 161078304  233 LI 234
Cdd:pfam12796  80 LL 81
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 98-234 8.03e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 77.01  E-value: 8.03e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304  98 IVKMLVRRGANVNSTTRTNSTPLRAACFD--GHYEIVKYLVHHGADFEVANRHGHTCLMIA--CYKGHFRIAQYLLSLNA 173
Cdd:PHA03100  88 IVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYleSNKIDLKILKLLIDKGV 167

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 161078304 174 DVN-RCSVK---------------GNTALHDCAESGSLQILQLLLKHGA-TMDVDYYGMTPLLAASVTGHMPIVEHLI 234
Cdd:PHA03100 168 DINaKNRVNyllsygvpinikdvyGFTPLHYAVYNNNPEFVKYLLDLGAnPNLVNKYGDTPLHIAILNNNKEIFKLLL 245
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 40-210 9.86e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 76.63  E-value: 9.86e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304  40 NGATPL--VISCRNGHYDIVEYLLTKcRANVEqvgSVSFDGEPIedappLWCAAAAGH--LGIVKMLVRRGANVNSTTRt 115
Cdd:PHA03100 105 NGITPLlyAISKKSNSYSIVEYLLDN-GANVN---IKNSDGENL-----LHLYLESNKidLKILKLLIDKGVDINAKNR- 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304 116 nstplraacfdghyeiVKYLVHHGADFEVANRHGHTCLMIACYKGHFRIAQYLLSLNADVNRCSVKGNTALHDCAESGSL 195
Cdd:PHA03100 175 ----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNK 238

                        170
                 ....*....|....*
gi 161078304 196 QILQLLLKHGATMDV 210
Cdd:PHA03100 239 EIFKLLLNNGPSIKT 253
Ank_2 pfam12796
Ankyrin repeats (3 copies);
45-146 3.96e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.52  E-value: 3.96e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304   45 LVISCRNGHYDIVEYLLTkcraNVEQVGSVSFDGEPiedapPLWCAAAAGHLGIVKMLVRRgANVNSTTRTNsTPLRAAC 124
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLE----NGADANLQDKNGRT-----ALHLAAKNGHLEIVKLLLEH-ADVNLKDNGR-TALHYAA 69

                          90       100
                  ....*....|....*....|..
gi 161078304  125 FDGHYEIVKYLVHHGADFEVAN 146
Cdd:pfam12796  70 RSGHLEIVKLLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 19-235 4.29e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 71.92  E-value: 4.29e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304  19 LKATLYNKSSVEVGSLISAKVN--------GATPLVISCRNGHYDIVEyLLTKCRANVEQVGSvsfdgepieDAP-PLWC 89
Cdd:PHA02874   5 LRMCIYSGDIEAIEKIIKNKGNcinisvdeTTTPLIDAIRSGDAKIVE-LFIKHGADINHINT---------KIPhPLLT 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304  90 AAAAGHLGIVKMLVRRGanvnsttrTNSTPLRAACFDGhyEIVKYLVHHGADFEVANRHGHTCLMIACYKGHFRIAQYLL 169
Cdd:PHA02874  75 AIKIGAHDIIKLLIDNG--------VDTSILPIPCIEK--DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLF 144

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 161078304 170 SLNADVNRCSVKGNTALHDCAESGSLQILQLLLKHGATMDV-DYYGMTPLLAASVTGHMPIVEHLIT 235
Cdd:PHA02874 145 EYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVkDNNGESPLHNAAEYGDYACIKLLID 211
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
96-234 4.05e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 67.29  E-value: 4.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304  96 LGIVKMLVRRGANVNSTTRTNSTPLRAACFDGHYEIVKYLVHHGADFEVANRHGHTCLMIACYKGHFRIAQYLLSLNADV 175
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304 176 NRCSVKGNTALHDCAESGSLQILQLLLKHGATMDV-DYYGMTPLLAASVTGHMPIVEHLI 234
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNArDKDGETPLHLAAYNGNLEIVKLLL 140
Ank_2 pfam12796
Ankyrin repeats (3 copies);
10-112 6.07e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.06  E-value: 6.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304   10 AARDNNLAQLKATLYNKSSVEVGSLisakvNGATPLVISCRNGHYDIVEYLLTKCRANVEQVGSvsfdgepiedaPPLWC 89
Cdd:pfam12796   4 AAKNGNLELVKLLLENGADANLQDK-----NGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR-----------TALHY 67

                          90       100
                  ....*....|....*....|...
gi 161078304   90 AAAAGHLGIVKMLVRRGANVNST 112
Cdd:pfam12796  68 AARSGHLEIVKLLLEKGADINVK 90
PHA03095 PHA03095
ankyrin-like protein; Provisional
 96-218 1.18e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 67.36  E-value: 1.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304  96 LGIVKMLVRRGANVNSTTRTNSTPLraaCFDGHY------EIVKYLVHHGADFEVANRHGHTCL-MIACYKGHFRIAQYL 168
Cdd:PHA03095  27 VEEVRRLLAAGADVNFRGEYGKTPL---HLYLHYssekvkDIVRLLLEAGADVNAPERCGFTPLhLYLYNATTLDVIKLL 103

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 161078304 169 LSLNADVNRCSVKGNTALHDCAESGSLQ--ILQLLLKHGATM-DVDYYGMTPL 218
Cdd:PHA03095 104 IKAGADVNAKDKVGRTPLHVYLSGFNINpkVIRLLLRKGADVnALDLYGMTPL 156
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 83-221 1.47e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 64.13  E-value: 1.47e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304  83 DAPPLWCAAAAGHLGIVKMLVRRGANVNSTTRTNSTPLRAACFDGHYEIVKYLVHHGADFEVANRHGHTCLMIAC-YKGH 161
Cdd:PHA02878 168 GNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVgYCKD 247

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161078304 162 FRIAQYLLSLNADVN-RCSVKGNTALHDCAESGslQILQLLLKHGATMD-VDYYGMTPLLAA 221
Cdd:PHA02878 248 YDILKLLLEHGVDVNaKSYILGLTALHSSIKSE--RKLKLLLEYGADINsLNSYKLTPLSSA 307
Ank_4 pfam13637
Ankyrin repeats (many copies);
116-169 3.01e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.13  E-value: 3.01e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 161078304  116 NSTPLRAACFDGHYEIVKYLVHHGADFEVANRHGHTCLMIACYKGHFRIAQYLL 169
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
525-612 3.01e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 61.89  E-value: 3.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304 525 VRVRFDRTALHYACYREgtlagrypscqfpSVTLAKALLEVGADPNAIDEAGNTPLHLATMQPYVEpLSHILLEGGAHLD 604
Cdd:COG0666  115 ARDKDGETPLHLAAYNG-------------NLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLE-IVKLLLEAGADVN 180


                 ....*...
gi 161078304 605 TKNYAGET 612
Cdd:COG0666  181 ARDNDGET 188
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
531-627 1.25e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 59.97  E-value: 1.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304 531 RTALHYACYREgtlagrypscqfpSVTLAKALLEVGADPNAIDEAGNTPLHLATMQPYVEpLSHILLEGGAHLDTKNYAG 610
Cdd:COG0666  154 NTPLHLAAANG-------------NLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLE-IVKLLLEAGADVNAKDNDG 219

                         90
                 ....*....|....*..
gi 161078304 611 ETFESLLAPTPMHKIID 627
Cdd:COG0666  220 KTALDLAAENGNLEIVK 236
PHA03095 PHA03095
ankyrin-like protein; Provisional
 29-236 1.26e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 60.81  E-value: 1.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304  29 VEVGSLISAK-VNGATPLVISCRNGH-YDIVEyLLTKCRANVEQVGSVSFDgepiedapPL--WCAAAAGHLGIVKMLVR 104
Cdd:PHA03095  70 LEAGADVNAPeRCGFTPLHLYLYNATtLDVIK-LLIKAGADVNAKDKVGRT--------PLhvYLSGFNINPKVIRLLLR 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304 105 RGANVNSTTRTNSTPLraACF----DGHYEIVKYLVHHGAD-FEVANRhGHTCLMIAC--YKGHFRIAQYLLSLNADVNR 177
Cdd:PHA03095 141 KGADVNALDLYGMTPL--AVLlksrNANVELLRLLIDAGADvYAVDDR-FRSLLHHHLqsFKPRARIVRELIRAGCDPAA 217

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161078304 178 CSVKGNTALHDCAESGS---LQILQLLLKhGATMDV-DYYGMTPLLAASVTGHMPIVEHLITL 236
Cdd:PHA03095 218 TDMLGNTPLHSMATGSSckrSLVLPLLIA-GISINArNRYGQTPLHYAAVFNNPRACRRLIAL 279
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 86-218 2.94e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 59.89  E-value: 2.94e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304  86 PLWCAAAAGHLGIVKMLVRRGANVNSTTRTNSTPLRAAC----------------------------------------- 124
Cdd:PHA02878  40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICkepnklgmkemirsinkcsvfytlvaikdafnnrnveifki 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304 125 -----FDGHY------------------EIVKYLVHHGADFEVANRH-GHTCLMIACYKGHFRIAQYLLSLNADVNRCSV 180
Cdd:PHA02878 120 iltnrYKNIQtidlvyidkkskddiieaEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDK 199

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 161078304 181 KGNTALHDCAESGSLQILQLLLKHGATMDV-DYYGMTPL 218
Cdd:PHA02878 200 TNNSPLHHAVKHYNKPIVHILLENGASTDArDKCGNTPL 238
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 43-234 3.04e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 59.59  E-value: 3.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304  43 TPLVISCRNGHYDIVEYLLtKCRANVeqvgsvsfDGEPIEDAPPLWCAAAAGHLGIVKMLVRRGANVNSTTRTNSTPLRA 122
Cdd:PHA02874 126 TFLHYAIKKGDLESIKMLF-EYGADV--------NIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304 123 ACFDGHYEIVKYLVHHGADFEVANRHGHTCLMIACYkgHFRIAQYLLSLNADVNRCSVKGNTALHDCAE-SGSLQILQLL 201
Cdd:PHA02874 197 AAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAINpPCDIDIIDIL 274

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 161078304 202 LKHGATMDV-DYYGMTPL-LAASVTGHMPIVEHLI 234
Cdd:PHA02874 275 LYHKADISIkDNKGENPIdTAFKYINKDPVIKDII 309
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 77-235 5.73e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 59.50  E-value: 5.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304  77 DGEPIEDAPPLwCAAAAGHLGIVKMLVRRGANVNSTTRTNSTPLRAACFDGHYEIVKYLVHHGADFEVANRHGHTCLMIA 156
Cdd:PLN03192 520 HDDPNMASNLL-TVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNA 598

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304 157 CYKGHFRIAQYLLSLNADVNRCSvkGNTALHDCAESGSLQILQLLLKHGATMDV-DYYGMTPLLAASVTGHMPIVEHLIT 235
Cdd:PLN03192 599 ISAKHHKIFRILYHFASISDPHA--AGDLLCTAAKRNDLTAMKELLKQGLNVDSeDHQGATALQVAMAEDHVDMVRLLIM 676
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 7-234 6.25e-09

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: 58.87  E-value: 6.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304   7 VFNAARDNNLAQLKATLYNKSS--VEVGSLisakvnGATPLVISCRNGHYDIVEYLLTKCRANV-EQVGSVSFDGEPied 83
Cdd:cd22192   21 LLLAAKENDVQAIKKLLKCPSCdlFQRGAL------GETALHVAALYDNLEAAVVLMEAAPELVnEPMTSDLYQGET--- 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304  84 apPLWCAAAAGHLGIVKMLVRRGANVnSTTRTNSTPLR----------------AACFdGHYEIVKYLVHHGADFEVANR 147
Cdd:cd22192   92 --ALHIAVVNQNLNLVRELIARGADV-VSPRATGTFFRpgpknliyygehplsfAACV-GNEEIVRLLIEHGADIRAQDS 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304 148 HGHTCLMIacykghfriaqylLSLNADVNRcsvkgntalhdcaesgSLQILQLLL---KHGATMDVD----YYGMTPLLA 220
Cdd:cd22192  168 LGNTVLHI-------------LVLQPNKTF----------------ACQMYDLILsydKEDDLQPLDlvpnNQGLTPFKL 218

                        250
                 ....*....|....
gi 161078304 221 ASVTGHMPIVEHLI 234
Cdd:cd22192  219 AAKEGNIVMFQHLV 232
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 86-210 9.41e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.08  E-value: 9.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304  86 PLWCAAAAGHLGIVKMLVRRGANVNSTTRTNSTPLRAACFDGHYEIVKYLVHHGADFEVANRHGHTCLMIACYKGHFRIA 165
Cdd:PHA02875 105 PLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAIC 184

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 161078304 166 QYLLSLNADVNRCSVKGN-TALHDCAESGSLQILQLLLKHGATMDV 210
Cdd:PHA02875 185 KMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADCNI 230
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 98-218 1.41e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 57.58  E-value: 1.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304  98 IVKMLVRRGANVNSTTR-TNSTPLRAACFDGHYEIVKYLVHHGADFEVANRHGHTCLMIACYKGHFRIAQYLLSLNADVN 176
Cdd:PHA02878 149 ITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTD 228

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 161078304 177 RCSVKGNTALHdcAESGSL---QILQLLLKHGATMDVDYY--GMTPL 218
Cdd:PHA02878 229 ARDKCGNTPLH--ISVGYCkdyDILKLLLEHGVDVNAKSYilGLTAL 273
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 87-238 1.56e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 57.28  E-value: 1.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304  87 LWCAAAAGHLGIVKMLVRRGANVNSTTRTNSTPLRAACFDGHYEIVKYLVHHGADFEVANRHGHTCLMIACYKGHFRIAQ 166
Cdd:PHA02874 128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIK 207

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161078304 167 YLLSLNADV-NRCSvKGNTALHDcAESGSLQILQLLLKHGATMDVDYYGMTPLlaasvtghmpivEHLITLPC 238
Cdd:PHA02874 208 LLIDHGNHImNKCK-NGFTPLHN-AIIHNRSAIELLINNASINDQDIDGSTPL------------HHAINPPC 266
Ank_4 pfam13637
Ankyrin repeats (many copies);
149-202 1.66e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.12  E-value: 1.66e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 161078304  149 GHTCLMIACYKGHFRIAQYLLSLNADVNRCSVKGNTALHDCAESGSLQILQLLL 202
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 29-245 1.85e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 57.77  E-value: 1.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304  29 VEVGSLISAK-VNGATPLVISCRNGhYDiVEYLLTKCRANVEQVGSVSFDGEPIEDAPPLwcaaaAGHLGIVKMLVRRGA 107
Cdd:PHA02876 294 LERGADVNAKnIKGETPLYLMAKNG-YD-TENIRTLIMLGADVNAADRLYITPLHQASTL-----DRNKDIVITLLELGA 366

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304 108 NVNSTTRTNSTPLRAACFDGHYEIVKYLVHHGADFEVANRHGHTCLMIACYKGH-FRIAQYLLSLNADVNRCSVKGNTAL 186
Cdd:PHA02876 367 NVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNpYMSVKTLIDRGANVNSKNKDLSTPL 446

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161078304 187 H-DCAESGSLQILQLLLKHGATMD-VDYYGMTPLLAAsvTGHMPIVEHLITLPCVSRESRI 245
Cdd:PHA02876 447 HyACKKNCKLDVIEMLLDNGADVNaINIQNQYPLLIA--LEYHGIVNILLHYGAELRDSRV 505
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 471-637 1.25e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 54.58  E-value: 1.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304 471 HQHDCNHDPNALSRTMISAIHIGC------LLSSLLDTDALS-PEMRRQVMGALYRLN-RLKVRVRFDRTALHYACyREG 542
Cdd:PHA02874  57 HGADINHINTKIPHPLLTAIKIGAhdiiklLIDNGVDTSILPiPCIEKDMIKTILDCGiDVNIKDAELKTFLHYAI-KKG 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304 543 TLAgrypscqfpsvtLAKALLEVGADPNAIDEAGNTPLHLATMQPYVEPLShILLEGGAHLDTKNYAGEtfesllapTPM 622
Cdd:PHA02874 136 DLE------------SIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIK-LLLEKGAYANVKDNNGE--------SPL 194

                        170
                 ....*....|....*
gi 161078304 623 HkiiDPMKYTTLACL 637
Cdd:PHA02874 195 H---NAAEYGDYACI 206
Ank_4 pfam13637
Ankyrin repeats (many copies);
85-136 3.05e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.65  E-value: 3.05e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 161078304   85 PPLWCAAAAGHLGIVKMLVRRGANVNSTTRTNSTPLRAACFDGHYEIVKYLV 136
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
499-612 3.31e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 52.26  E-value: 3.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304 499 LLDTDALSPEMRRQVMGALYRLNRLKVRVRFDRTALHYACyREGTLAgrypscqfpsvtLAKALLEVGADPNAIDEAGNT 578
Cdd:COG0666   56 LLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAA-RNGDLE------------IVKLLLEAGADVNARDKDGET 122

                         90       100       110
                 ....*....|....*....|....*....|....
gi 161078304 579 PLHLATMQPYVEpLSHILLEGGAHLDTKNYAGET 612
Cdd:COG0666  123 PLHLAAYNGNLE-IVKLLLEAGADVNAQDNDGNT 155
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
525-631 3.93e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 52.26  E-value: 3.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304 525 VRVRFDRTALHYACYREgtlagrypscqfpSVTLAKALLEVGADPNAIDEAGNTPLHLATMQPYVEPLsHILLEGGAHLD 604
Cdd:COG0666  181 ARDNDGETPLHLAAENG-------------HLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIV-KLLLEAGADLN 246

                         90       100
                 ....*....|....*....|....*..
gi 161078304 605 TKNYAGETFESLLAPTPMHKIIDPMKY 631
Cdd:COG0666  247 AKDKDGLTALLLAAAAGAALIVKLLLL 273
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 7-179 4.50e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 53.33  E-value: 4.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304   7 VFNAARDNNLAQLKATLYNKSSVEVGSlisAKvnGATPLVISCRNGHYDIVEYLLTK-CRANVEQVGSVSfdgepiedap 85
Cdd:PLN03192 529 LLTVASTGNAALLEELLKAKLDPDIGD---SK--GRTPLHIAASKGYEDCVLVLLKHaCNVHIRDANGNT---------- 593

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304  86 PLWCAAAAGHLGIVKMLVRRGANvnSTTRTNSTPLRAACFDGHYEIVKYLVHHGADFEVANRHGHTCLMIACYKGHFRIA 165
Cdd:PLN03192 594 ALWNAISAKHHKIFRILYHFASI--SDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMV 671

                        170
                 ....*....|....
gi 161078304 166 QYLLSLNADVNRCS 179
Cdd:PLN03192 672 RLLIMNGADVDKAN 685
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 99-234 5.05e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 52.69  E-value: 5.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304  99 VKMLVRRGANVNSTTRTNSTPLRAACFDGHYEIVKYLVHHG--ADfEVANRHGHTCLMIACYKGHFRIAQYLLSLNADVN 176
Cdd:PHA02875  51 IKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGkfAD-DVFYKDGMTPLHLATILKKLDIMKLLIARGADPD 129

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 161078304 177 RCSVKGNTALHDCAESGSLQILQLLLKHGATMDV-DYYGMTPLLAASVTGHMPIVEHLI 234
Cdd:PHA02875 130 IPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIeDCCGCTPLIIAMAKGDIAICKMLL 188
Ank_4 pfam13637
Ankyrin repeats (many copies);
182-234 1.08e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.11  E-value: 1.08e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 161078304  182 GNTALHDCAESGSLQILQLLLKHGATMD-VDYYGMTPLLAASVTGHMPIVEHLI 234
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINaVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 132-204 1.90e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.05  E-value: 1.90e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161078304 132 VKYLVHHGADFEVANRHGHTCLMIACYKGHFRIAQYLLSLNADVNRCSVKGNTALHDCAESGSLQILQLLLKH 204
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 530-612 4.29e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 49.88  E-value: 4.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304 530 DRTALHYACyregtlagrypscQFPSVTLAKALLEVGADPNAIDEAGNTPLHLAtMQPYVEPLSHILLEGGAHLDTKNYA 609
Cdd:PHA02878 168 GNTALHYAT-------------ENKDQRLTELLLSYGANVNIPDKTNNSPLHHA-VKHYNKPIVHILLENGASTDARDKC 233


                 ...
gi 161078304 610 GET 612
Cdd:PHA02878 234 GNT 236
Ank_5 pfam13857
Ankyrin repeats (many copies);
134-187 9.02e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.49  E-value: 9.02e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 161078304  134 YLVHHGADFEVANRHGHTCLMIACYKGHFRIAQYLLSLNADVNRCSVKGNTALH 187
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
PHA02798 PHA02798
ankyrin-like protein; Provisional
 96-205 1.15e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 48.29  E-value: 1.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304  96 LGIVKMLVRRGANVNSTTRTNSTPLraaC--------FDGHYEIVKYLVHHGADFEVANRHGHT---CLMIACYKGHFRI 164
Cdd:PHA02798  51 TDIVKLFINLGANVNGLDNEYSTPL---CtilsnikdYKHMLDIVKILIENGADINKKNSDGETplyCLLSNGYINNLEI 127

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 161078304 165 AQYLLSLNADVNRCSVKGNTALHDCAESG---SLQILQLLLKHG 205
Cdd:PHA02798 128 LLFMIENGADTTLLDKDGFTMLQVYLQSNhhiDIEIIKLLLEKG 171
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 91-170 1.75e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.97  E-value: 1.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304  91 AAAGHLGIVKMLVRRGANVNSTTRTNSTPLRAACFDGHYEIVKYLVHHGADFEVANRHGHTCLMIACYKGHFRIAQYLLS 170
Cdd:PTZ00322  90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 532-607 1.92e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 47.35  E-value: 1.92e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 161078304 532 TALHYACYregtlagrypscqFPSVTLAKALLEVGADPNAIDEAGNTPLHLAtMQPYVEPLSHILLEGGAHLDTKN 607
Cdd:PHA03100 194 TPLHYAVY-------------NNNPEFVKYLLDLGANPNLVNKYGDTPLHIA-ILNNNKEIFKLLLNNGPSIKTII 255
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 8-202 5.69e-05

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: 46.23  E-value: 5.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304    8 FNAARDNNLAQLKATL-YNKSSVEVG-SLISAkvngatplvisCRNGHYDIVEYLLTKCRANVEQVGSVSF-----DGEP 80
Cdd:TIGR00870  57 FVAAIENENLELTELLlNLSCRGAVGdTLLHA-----------ISLEYVDAVEAILLHLLAAFRKSGPLELandqyTSEF 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304   81 IEDAPPLWCAAAAGHLGIVKMLVRRGANVN---------STTRTNS-----TPLR-AACFdGHYEIVKYLVHHGAD---- 141
Cdd:TIGR00870 126 TPGITALHLAAHRQNYEIVKLLLERGASVParacgdffvKSQGVDSfyhgeSPLNaAACL-GSPSIVALLSEDPADilta 204

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161078304  142 FEVANRHGHTCLMIACYK---GHFRIAQYLLSLNADVNRCSVK---------GNTALHDCAESGSLQILQLLL 202
Cdd:TIGR00870 205 DSLGNTLLHLLVMENEFKaeyEELSCQMYNFALSLLDKLRDSKelevilnhqGLTPLKLAAKEGRIVLFRLKL 277
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 86-209 6.72e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 46.01  E-value: 6.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304  86 PLWCAAAAGHLGIVKMLVRRGANVNSTTRTNSTPLRAACFDGHYEIVKYLVHHGAdfeVANRH-GHTCLMIACYKGHFRI 164
Cdd:PLN03192 561 PLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFAS---ISDPHaAGDLLCTAAKRNDLTA 637

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 161078304 165 AQYLLSLNADVNRCSVKGNTALHDCAESGSLQILQLLLKHGATMD 209
Cdd:PLN03192 638 MKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVD 682
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 86-221 8.79e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 45.37  E-value: 8.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304  86 PLWCAAAAGHLGIVKMLVRRGANVNSTT-RTNSTPLRAACFDGHYEIVKYLVHHGADFEVANRHGHTCLMIACYKGHFRI 164
Cdd:PHA02875  71 ELHDAVEEGDVKAVEELLDLGKFADDVFyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKG 150

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 161078304 165 AQYLLSLNADVNRCSVKGNTALHDCAESGSLQILQLLLKHGAtmDVDYYGMTPLLAA 221
Cdd:PHA02875 151 IELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGA--NIDYFGKNGCVAA 205
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 86-209 1.30e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.05  E-value: 1.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304  86 PLWCAAAAGHLG-IVKMLVRRGANVNSTTRTNSTPLRAACFDGH-YEIVKYLVHHGADFEVANRHGHTCLMIACYKGHFR 163
Cdd:PHA02876 276 PLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDRNK 355

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 161078304 164 -IAQYLLSLNADVNRCSVKGNTALHDCAESGSLQILQLLLKHGATMD 209
Cdd:PHA02876 356 dIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIE 402
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 562-618 1.89e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 44.67  E-value: 1.89e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 161078304 562 LLEVGADPNAIDEAGNTPLHLATMQPYVEPLSHILLEGGAHLDTKNYAGETFESLLA 618
Cdd:PHA02876 259 LYDAGFSVNSIDDCKNTPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMA 315
PHA03095 PHA03095
ankyrin-like protein; Provisional
 97-186 2.01e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 44.25  E-value: 2.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304  97 GIVKMLVRRGANVNSTTRTNSTPLRAACFDGHYE--IVKYLVHHGADFEVANRHGHTCLMIACYKGHFRIAQYLLSLNAD 174
Cdd:PHA03095 203 RIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGAD 282

                         90
                 ....*....|..
gi 161078304 175 VNRCSVKGNTAL 186
Cdd:PHA03095 283 INAVSSDGNTPL 294
PHA03095 PHA03095
ankyrin-like protein; Provisional
 503-612 2.05e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 44.25  E-value: 2.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304 503 DALSPEMRRQVMGALYR--LNRLKVRVR-----------------FDRTALHYAcyregtlaGRYPSCQFPSVTlaKALL 563
Cdd:PHA03095   1 DEEDESVDIIMEAALYDylLNASNVTVEevrrllaagadvnfrgeYGKTPLHLY--------LHYSSEKVKDIV--RLLL 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 161078304 564 EVGADPNAIDEAGNTPLHLATMQPYVEPLSHILLEGGAHLDTKNYAGET 612
Cdd:PHA03095  71 EAGADVNAPERCGFTPLHLYLYNATTLDVIKLLIKAGADVNAKDKVGRT 119
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 531-623 2.74e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.12  E-value: 2.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304 531 RTALHYACyregtLAGRypscqfpsVTLAKALLEVGADPNAIDEAGNTPLHLATMQPY---VEPLS---HILLEGGAHLD 604
Cdd:PTZ00322 116 RTPLHIAC-----ANGH--------VQVVRVLLEFGADPTLLDKDGKTPLELAEENGFrevVQLLSrhsQCHFELGANAK 182

                         90
                 ....*....|....*....
gi 161078304 605 TKNYAGETFESLLAPTPMH 623
Cdd:PTZ00322 183 PDSFTGKPPSLEDSPISSH 201
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 148-176 2.90e-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: 38.34  E-value: 2.90e-04
                           10        20
                   ....*....|....*....|....*....
gi 161078304   148 HGHTCLMIACYKGHFRIAQYLLSLNADVN 176
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 562-653 4.56e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 43.12  E-value: 4.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304 562 LLEVGADPNAIDEAGNTPLHLATMQPYVEPLSHiLLEGGAHLDTKNYAGET-------------FESLLAPTPMHKIIDP 628
Cdd:PHA03100 178 LLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKY-LLDLGANPNLVNKYGDTplhiailnnnkeiFKLLLNNGPSIKTIIE 256

                         90       100
                 ....*....|....*....|....*....
gi 161078304 629 -MKYTTLACLAARTIKK---HDIRYEGTV 653
Cdd:PHA03100 257 tLLYFKDKDLNTITKIKmlkKSIMYMFLL 285
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 148-176 6.02e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 37.65  E-value: 6.02e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 161078304  148 HGHTCLMIACYK-GHFRIAQYLLSLNADVN 176
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVN 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 181-210 6.49e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.57  E-value: 6.49e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 161078304   181 KGNTALHDCAESGSLQILQLLLKHGATMDV 210
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 106-254 8.55e-04

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: 42.31  E-value: 8.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304 106 GANVNSTTRTNSTPLRAACFDGHYEIVK-YLVHHGADFEVANRHGHTCLMIACYKGHFRIAQYLLS-----LNADVNRCS 179
Cdd:cd22192    7 ELHLLQQKRISESPLLLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEaapelVNEPMTSDL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304 180 VKGNTALHDCAESGSLQILQLLLKHGAtmDVD-----------------YYGMTPLLAASVTGHMPIVEHLItlpcvSRE 242
Cdd:cd22192   87 YQGETALHIAVVNQNLNLVRELIARGA--DVVspratgtffrpgpknliYYGEHPLSFAACVGNEEIVRLLI-----EHG 159

                        170
                 ....*....|..
gi 161078304 243 SRIHALELLGAT 254
Cdd:cd22192  160 ADIRAQDSLGNT 171
Ank_5 pfam13857
Ankyrin repeats (many copies);
101-156 9.16e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.71  E-value: 9.16e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 161078304  101 MLVRRGANVNSTTRTNSTPLRAACFDGHYEIVKYLVHHGADFEVANRHGHTCLMIA 156
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
531-585 1.02e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.64  E-value: 1.02e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 161078304  531 RTALHYACYRegtlaGRYPSCQFpsvtlakaLLEVGADPNAIDEAGNTPLHLATM 585
Cdd:pfam13637   2 LTALHAAAAS-----GHLELLRL--------LLEKGADINAVDGNGETALHFAAS 43
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 96-266 1.13e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.97  E-value: 1.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304  96 LGIVKMLVRRGANVNSTTRTNSTPLRAACFDGHYEIVKYLVHHGADFEVANRHGHTCLMIACYKGHF-----------RI 164
Cdd:PHA02876 158 LLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIdtikaiidnrsNI 237

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304 165 AQYLLSL-----NAD-------------VNRCSVKGNTALHDCAESGSL-QILQLLLKHGATMDV-DYYGMTPLLAASVT 224
Cdd:PHA02876 238 NKNDLSLlkairNEDletslllydagfsVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAkNIKGETPLYLMAKN 317

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 161078304 225 GH-MPIVEHLITLPC-VSRESRIHALELLGATYVDRKRDMAAAL 266
Cdd:PHA02876 318 GYdTENIRTLIMLGAdVNAADRLYITPLHQASTLDRNKDIVITL 361
Ank_2 pfam12796
Ankyrin repeats (3 copies);
551-598 1.17e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 38.56  E-value: 1.17e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 161078304  551 CQFPSVTLAKALLEVGADPNAIDEAGNTPLHLATMQPYVEPLShILLE 598
Cdd:pfam12796   5 AKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVK-LLLE 51
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 559-601 1.45e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.81  E-value: 1.45e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 161078304 559 AKALLEVGADPNAIDEAGNTPLHLATMQPYVEpLSHILLEGGA 601
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQ-VVRVLLEFGA 139
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 98-182 1.69e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 40.19  E-value: 1.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304  98 IVKMLVRRGANVNSTTRTNSTPL-RAAC-FDGHYEIVKYLVHHGADFEVANRHG----HTCLMiacYKGHFRIAQYLLSL 171
Cdd:PHA02859 105 ILKILIDSGSSITEEDEDGKNLLhMYMCnFNVRINVIKLLIDSGVSFLNKDFDNnnilYSYIL---FHSDKKIFDFLTSL 181

                         90
                 ....*....|.
gi 161078304 172 NADVNRCSVKG 182
Cdd:PHA02859 182 GIDINETNKSG 192
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 73-138 1.81e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.42  E-value: 1.81e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 161078304  73 SVSFDGEPiedapPLWCAAAAGHLGIVKMLVRRGANVNSTTRTNSTPLRAACFDGHYEIVKYLVHH 138
Cdd:PTZ00322 110 CRDYDGRT-----PLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 86-114 1.83e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.11  E-value: 1.83e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 161078304   86 PLWCAAA-AGHLGIVKMLVRRGANVNSTTR 114
Cdd:pfam00023   5 PLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 148-176 1.90e-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: 36.08  E-value: 1.90e-03
                          10        20
                  ....*....|....*....|....*....
gi 161078304  148 HGHTCLMIACYKGHFRIAQYLLSLNADVN 176
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
Ank_2 pfam12796
Ankyrin repeats (3 copies);
529-607 2.21e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 37.79  E-value: 2.21e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 161078304  529 FDRTALHYACYREgtlagrypscqfpSVTLAKALLEVgADPNAIDEaGNTPLHLATMQPYVEpLSHILLEGGAHLDTKN 607
Cdd:pfam12796  29 NGRTALHLAAKNG-------------HLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLE-IVKLLLEKGADINVKD 91
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 86-110 2.50e-03

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: 35.64  E-value: 2.50e-03
                           10        20
                   ....*....|....*....|....*
gi 161078304    86 PLWCAAAAGHLGIVKMLVRRGANVN 110
Cdd:smart00248   5 PLHLAAENGNLEVVKLLLDKGADIN 29
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 531-574 4.06e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.34  E-value: 4.06e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 161078304  531 RTALHYACYREGtlagrypscqfpSVTLAKALLEVGADPNAIDE 574
Cdd:pfam00023   3 NTPLHLAAGRRG------------NLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 118-144 4.73e-03

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: 34.87  E-value: 4.73e-03
                           10        20
                   ....*....|....*....|....*..
gi 161078304   118 TPLRAACFDGHYEIVKYLVHHGADFEV 144
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 118-147 4.75e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.96  E-value: 4.75e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 161078304  118 TPL-RAACFDGHYEIVKYLVHHGADFEVANR 147
Cdd:pfam00023   4 TPLhLAAGRRGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
528-583 5.09e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.79  E-value: 5.09e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 161078304  528 RFDRTALHYACYRegtlagrypscqfPSVTLAKALLEVGADPNAIDEAGNTPLHLA 583
Cdd:pfam13857  14 GEGYTPLHVAAKY-------------GALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 181-210 5.35e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.96  E-value: 5.35e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 161078304  181 KGNTALHDCAES-GSLQILQLLLKHGATMDV 210
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNA 31
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 149-248 8.10e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all 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.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 39.36  E-value: 8.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078304 149 GHTCLMIACY---KGHFRIAQYLLS-----------LNADVNRCSVKGNTALHDCAESGSLQILQLLLKHGATMDVD--- 211
Cdd:cd22194   94 GKTCLMKALLninENTKEIVRILLAfaeengildrfINAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHakg 173

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 161078304 212 ------------YYGMTPLLAASVTGHMPIVEHLI---TLPCVSRESR----IHAL 248
Cdd:cd22194  174 vffnpkykhegfYFGETPLALAACTNQPEIVQLLMekeSTDITSQDSRgntvLHAL 229
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 560-634 9.91e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 39.09  E-value: 9.91e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 161078304 560 KALLEVGADPNAIDEAGNTPLHLATMQPYVEPLSHILLEGGAHLDTKNYagetfesLLAPTPMH-KIIDPMKYTTL 634
Cdd:PHA02878 218 HILLENGASTDARDKCGNTPLHISVGYCKDYDILKLLLEHGVDVNAKSY-------ILGLTALHsSIKSERKLKLL 286
 
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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