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Conserved domains on  [gi|164607184|ref|NP_291079|]
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B-cell lymphoma 3 protein homolog [Mus musculus]

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];
112-354 8.11e-44

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 155.11  E-value: 8.11e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 112 MEHPLSADIAMATRVDEDGDTPLHIAVVQNNIAAVYRILSLfklGSREVDVHNNLRQTPLHLAVITTLPDMVRLLVTAGA 191
Cdd:COG0666   35 LLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLA---AGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGA 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 192 SPMALDRHGQTAIHLACEHRSPSCLQALLDSatsGsVDLEVRNYEGLTALHVAVNTGCQEAVLLLLERGADIDAVDiKSG 271
Cdd:COG0666  112 DVNARDKDGETPLHLAAYNGNLEIVKLLLEA---G-ADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD-NDG 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 272 RSPLIHAVENNSLNMVQLLLLHGANVNAQMYSGSSALHSASGRGLLPLVRTLVRSGADSGLKNCHNDTPLMVARSRRVID 351
Cdd:COG0666  187 ETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAAL 266


                 ...
gi 164607184 352 ILR 354
Cdd:COG0666  267 IVK 269
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
112-354 8.11e-44

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 155.11  E-value: 8.11e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 112 MEHPLSADIAMATRVDEDGDTPLHIAVVQNNIAAVYRILSLfklGSREVDVHNNLRQTPLHLAVITTLPDMVRLLVTAGA 191
Cdd:COG0666   35 LLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLA---AGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGA 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 192 SPMALDRHGQTAIHLACEHRSPSCLQALLDSatsGsVDLEVRNYEGLTALHVAVNTGCQEAVLLLLERGADIDAVDiKSG 271
Cdd:COG0666  112 DVNARDKDGETPLHLAAYNGNLEIVKLLLEA---G-ADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD-NDG 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 272 RSPLIHAVENNSLNMVQLLLLHGANVNAQMYSGSSALHSASGRGLLPLVRTLVRSGADSGLKNCHNDTPLMVARSRRVID 351
Cdd:COG0666  187 ETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAAL 266


                 ...
gi 164607184 352 ILR 354
Cdd:COG0666  267 IVK 269
Ank_2 pfam12796
Ankyrin repeats (3 copies);
171-267 5.49e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.40  E-value: 5.49e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184  171 LHLAVITTLPDMVRLLVTAGASPMALDRHGQTAIHLACEHRSPSCLQALLDSAtsgsvDLEVRNYeGLTALHVAVNTGCQ 250
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-----DVNLKDN-GRTALHYAARSGHL 74

                          90
                  ....*....|....*..
gi 164607184  251 EAVLLLLERGADIDAVD 267
Cdd:pfam12796  75 EIVKLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 132-329 4.24e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 82.79  E-value: 4.24e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 132 TPLHIAVVQNNIAAVYrilSLFKLGSReVDVHNNLRQTPLHL-----AVITTLPDMVRLLVTAGASPMALDRHGQTAIHL 206
Cdd:PHA03100  37 LPLYLAKEARNIDVVK---ILLDNGAD-INSSTKNNSTPLHYlsnikYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLY 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 207 ACEHR--SPSCLQALLDSATsgsvDLEVRNYEGLTALHVAVNTGCQ--EAVLLLLERGADIDA-------------VDIK 269
Cdd:PHA03100 113 AISKKsnSYSIVEYLLDNGA----NVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAknrvnyllsygvpINIK 188

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164607184 270 S--GRSPLIHAVENNSLNMVQLLLLHGANVNAQMYSGSSALHSASGRGLLPLVRTLVRSGAD 329
Cdd:PHA03100 189 DvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 169-309 1.54e-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: 60.03  E-value: 1.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 169 TPLHLAVITT-LPDMVRLLVTAGASPMALDRHGQTAIHLACEHRSPSCLQALLDSAtSGSVDLEVRN--YEGLTALHVAV 245
Cdd:cd22192   19 SPLLLAAKENdVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAA-PELVNEPMTSdlYQGETALHIAV 97

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164607184 246 NTGCQEAVLLLLERGADIDAVD-------------IKSGRSPLIHAVENNSLNMVQLLLLHGANVNAQMYSGSSALH 309
Cdd:cd22192   98 VNQNLNLVRELIARGADVVSPRatgtffrpgpknlIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 105-309 1.33e-07

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: 53.93  E-value: 1.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184  105 PYSMICPMEHPLSadiamatrvdeDGDTPLHIAVVQNNIAAVYRILSLFKlgSREVDVHNNLRQTPLHLAVITTLP-DMV 183
Cdd:TIGR00870   3 PLDIVPAEESPLS-----------DEEKAFLPAAERGDLASVYRDLEEPK--KLNINCPDRLGRSALFVAAIENENlELT 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184  184 RLLVTAGASPmaldRHGQTAIHLA-------CEhrspSCLQALLDSAtSGSVDLEVRN-------YEGLTALHVAVNTGC 249
Cdd:TIGR00870  70 ELLLNLSCRG----AVGDTLLHAIsleyvdaVE----AILLHLLAAF-RKSGPLELANdqytsefTPGITALHLAAHRQN 140

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164607184  250 QEAVLLLLERGADIDA------------VD-IKSGRSPLIHAVENNSLNMVQLLLLHGANVNAQMYSGSSALH 309
Cdd:TIGR00870 141 YEIVKLLLERGASVPAracgdffvksqgVDsFYHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLH 213
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 271-299 1.98e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.42  E-value: 1.98e-05
                           10        20
                   ....*....|....*....|....*....
gi 164607184   271 GRSPLIHAVENNSLNMVQLLLLHGANVNA 299
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
112-354 8.11e-44

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 155.11  E-value: 8.11e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 112 MEHPLSADIAMATRVDEDGDTPLHIAVVQNNIAAVYRILSLfklGSREVDVHNNLRQTPLHLAVITTLPDMVRLLVTAGA 191
Cdd:COG0666   35 LLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLA---AGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGA 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 192 SPMALDRHGQTAIHLACEHRSPSCLQALLDSatsGsVDLEVRNYEGLTALHVAVNTGCQEAVLLLLERGADIDAVDiKSG 271
Cdd:COG0666  112 DVNARDKDGETPLHLAAYNGNLEIVKLLLEA---G-ADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD-NDG 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 272 RSPLIHAVENNSLNMVQLLLLHGANVNAQMYSGSSALHSASGRGLLPLVRTLVRSGADSGLKNCHNDTPLMVARSRRVID 351
Cdd:COG0666  187 ETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAAL 266


                 ...
gi 164607184 352 ILR 354
Cdd:COG0666  267 IVK 269
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
116-361 1.20e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 149.33  E-value: 1.20e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 116 LSADIAMATRVDEDGDTPLHIAVVQNNIAAVYRILSLFKLgsreVDVHNNLRQTPLHLAVITTLPDMVRLLVTAGASPMA 195
Cdd:COG0666    7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLA----LALADALGALLLLAAALAGDLLVALLLLAAGADINA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 196 LDRHGQTAIHLACEHRSPSCLQALLDSAtsgsVDLEVRNYEGLTALHVAVNTGCQEAVLLLLERGADIDAVDiKSGRSPL 275
Cdd:COG0666   83 KDDGGNTLLHAAARNGDLEIVKLLLEAG----ADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQD-NDGNTPL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 276 IHAVENNSLNMVQLLLLHGANVNAQMYSGSSALHSASGRGLLPLVRTLVRSGADSGLKNCHNDTPLMVARSRRVIDILRG 355
Cdd:COG0666  158 HLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKL 237


                 ....*.
gi 164607184 356 KASRAA 361
Cdd:COG0666  238 LLEAGA 243
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
116-341 5.89e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 147.79  E-value: 5.89e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 116 LSADIAMATRVDEDGDTPLHIAVVQNNIAAVYRILslfKLGSrEVDVHNNLRQTPLHLAVITTLPDMVRLLVTAGASPMA 195
Cdd:COG0666   73 LLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLL---EAGA-DVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNA 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 196 LDRHGQTAIHLACEHRSPSCLQALLDSatsGsVDLEVRNYEGLTALHVAVNTGCQEAVLLLLERGADIDAVDiKSGRSPL 275
Cdd:COG0666  149 QDNDGNTPLHLAAANGNLEIVKLLLEA---G-ADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKD-NDGKTAL 223

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 164607184 276 IHAVENNSLNMVQLLLLHGANVNAQMYSGSSALHSASGRGLLPLVRTLVRSGADSGLKNCHNDTPL 341
Cdd:COG0666  224 DLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
149-354 2.47e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 124.30  E-value: 2.47e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 149 ILSLFKLGSREVDVHNNLRQTPLHLAVITTLPDMVRLLVTAGASPMALDRHGQTAIHLACEHRSPSCLQALLDSatsGSV 228
Cdd:COG0666    2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLA---AGA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 229 DLEVRNYEGLTALHVAVNTGCQEAVLLLLERGADIDAVDiKSGRSPLIHAVENNSLNMVQLLLLHGANVNAQMYSGSSAL 308
Cdd:COG0666   79 DINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARD-KDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPL 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 164607184 309 HSASGRGLLPLVRTLVRSGADSGLKNCHNDTPLMVARSRRVIDILR 354
Cdd:COG0666  158 HLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203
Ank_2 pfam12796
Ankyrin repeats (3 copies);
171-267 5.49e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.40  E-value: 5.49e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184  171 LHLAVITTLPDMVRLLVTAGASPMALDRHGQTAIHLACEHRSPSCLQALLDSAtsgsvDLEVRNYeGLTALHVAVNTGCQ 250
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-----DVNLKDN-GRTALHYAARSGHL 74

                          90
                  ....*....|....*..
gi 164607184  251 EAVLLLLERGADIDAVD 267
Cdd:pfam12796  75 EIVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
204-300 2.57e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.47  E-value: 2.57e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184  204 IHLACEHRSPSCLQALLDSatsgSVDLEVRNYEGLTALHVAVNTGCQEAVLLLLERgADIDAVDikSGRSPLIHAVENNS 283
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLEN----GADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD--NGRTALHYAARSGH 73

                          90
                  ....*....|....*..
gi 164607184  284 LNMVQLLLLHGANVNAQ 300
Cdd:pfam12796  74 LEIVKLLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
241-334 4.04e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.00  E-value: 4.04e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184  241 LHVAVNTGCQEAVLLLLERGADIDAVDiKSGRSPLIHAVENNSLNMVQLLLLHgANVNAQMYsGSSALHSASGRGLLPLV 320
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQD-KNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIV 77

                          90
                  ....*....|....
gi 164607184  321 RTLVRSGADSGLKN 334
Cdd:pfam12796  78 KLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 132-329 4.24e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 82.79  E-value: 4.24e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 132 TPLHIAVVQNNIAAVYrilSLFKLGSReVDVHNNLRQTPLHL-----AVITTLPDMVRLLVTAGASPMALDRHGQTAIHL 206
Cdd:PHA03100  37 LPLYLAKEARNIDVVK---ILLDNGAD-INSSTKNNSTPLHYlsnikYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLY 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 207 ACEHR--SPSCLQALLDSATsgsvDLEVRNYEGLTALHVAVNTGCQ--EAVLLLLERGADIDA-------------VDIK 269
Cdd:PHA03100 113 AISKKsnSYSIVEYLLDNGA----NVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAknrvnyllsygvpINIK 188

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164607184 270 S--GRSPLIHAVENNSLNMVQLLLLHGANVNAQMYSGSSALHSASGRGLLPLVRTLVRSGAD 329
Cdd:PHA03100 189 DvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 129-298 1.81e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 78.11  E-value: 1.81e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 129 DGDTPLHIAVVQNNIAAVYRILSLFKLGSrevDVHNNLRQTPLHLAVITTLPDMVRLLVTAGASPMALDRHGQTAIHLAC 208
Cdd:PHA02875  67 DIESELHDAVEEGDVKAVEELLDLGKFAD---DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAV 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 209 EHRSPSCLQALLDSATSgsvdLEVRNYEGLTALHVAVNTGCQEAVLLLLERGADIDAVDIKSGRSPLIHAVENNSLNMVQ 288
Cdd:PHA02875 144 MMGDIKGIELLIDHKAC----LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVR 219

                        170
                 ....*....|
gi 164607184 289 LLLLHGANVN 298
Cdd:PHA02875 220 LFIKRGADCN 229
PHA03095 PHA03095
ankyrin-like protein; Provisional
 118-354 1.41e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 75.45  E-value: 1.41e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 118 ADIAMATRVdedGDTPLHIAVVQNNIAAVYRILslFKLGSReVDVHNNLRQTPLH--LAVITTLPDMVRLLVTAGASPMA 195
Cdd:PHA03095  74 ADVNAPERC---GFTPLHLYLYNATTLDVIKLL--IKAGAD-VNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNA 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 196 LDRHGQTAIHlaCEHRSPSCLQALLDSATSGSVDLEVRNYEGLTALHV-AVNTGCQEAVL-LLLERGADIDAVDIkSGRS 273
Cdd:PHA03095 148 LDLYGMTPLA--VLLKSRNANVELLRLLIDAGADVYAVDDRFRSLLHHhLQSFKPRARIVrELIRAGCDPAATDM-LGNT 224

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 274 PLIHAVENNSLN--MVQLLLLHGANVNAQMYSGSSALHSASGRGLLPLVRTLVRSGADSGLKNCHNDTPLMVARSRRVID 351
Cdd:PHA03095 225 PLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGR 304


                 ...
gi 164607184 352 ILR 354
Cdd:PHA03095 305 AVR 307
PHA03095 PHA03095
ankyrin-like protein; Provisional
 239-354 2.09e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 75.06  E-value: 2.09e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 239 TALHVAVNTGCQ---EAVLLLLERGADIDAVDIkSGRSPLIHAVENNS-LNMVQLLLLHGANVNAQMYSGSSALHS-ASG 313
Cdd:PHA03095  49 TPLHLYLHYSSEkvkDIVRLLLEAGADVNAPER-CGFTPLHLYLYNATtLDVIKLLIKAGADVNAKDKVGRTPLHVyLSG 127

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 164607184 314 RGLLP-LVRTLVRSGADSGLKNCHNDTPLMVA-RSRRV-IDILR 354
Cdd:PHA03095 128 FNINPkVIRLLLRKGADVNALDLYGMTPLAVLlKSRNAnVELLR 171
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 132-299 2.29e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 74.70  E-value: 2.29e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 132 TPLHIAVVQN-NIAAVYRILS-LFKLGSReVDVHNNLRQTPLHLAVITTL--PDMVRLLVTAGASPMALDRHGQTAIHLA 207
Cdd:PHA03100  70 TPLHYLSNIKyNLTDVKEIVKlLLEYGAN-VNAPDNNGITPLLYAISKKSnsYSIVEYLLDNGANVNIKNSDGENLLHLY 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 208 --CEHRSPSCLQALLDSAT------------SGSVDLEVRNYEGLTALHVAVNTGCQEAVLLLLERGADIDAVDIKsGRS 273
Cdd:PHA03100 149 leSNKIDLKILKLLIDKGVdinaknrvnyllSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKY-GDT 227

                        170       180
                 ....*....|....*....|....*.
gi 164607184 274 PLIHAVENNSLNMVQLLLLHGANVNA 299
Cdd:PHA03100 228 PLHIAILNNNKEIFKLLLNNGPSIKT 253
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 170-354 1.03e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 72.99  E-value: 1.03e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 170 PLHLAVITTLPDMVRLLVTAGASPMALDRHGQTAIHLACEHRSPSCLQALLDSATSGSVDLEV---------RNYEGLTA 240
Cdd:PHA02878  40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFYTLvaikdafnnRNVEIFKI 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 241 LHVAVNTGCQ------------------EAVLLLLERGADIDAVDIKSGRSPLIHAVENNSLNMVQLLLLHGANVNAQMY 302
Cdd:PHA02878 120 ILTNRYKNIQtidlvyidkkskddiieaEITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDK 199

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 164607184 303 SGSSALHSASGRGLLPLVRTLVRSGADSGLKNCHNDTPLMVARSRRV-IDILR 354
Cdd:PHA02878 200 TNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKdYDILK 252
PHA03095 PHA03095
ankyrin-like protein; Provisional
 169-344 2.19e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 71.59  E-value: 2.19e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 169 TPLHLAVITTLP---DMVRLLVTAGASPMALDRHGQTAIHLACEHRSPSCLQALLDSAtsgSVDLEVRNYEGLTALHV-- 243
Cdd:PHA03095  49 TPLHLYLHYSSEkvkDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDVIKLLIKA---GADVNAKDKVGRTPLHVyl 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 244 ---AVNTGcqeAVLLLLERGADIDAVDiKSGRSPLIHAVENN--SLNMVQLLLLHGANVNAQMYSGSSALHS--ASGRGL 316
Cdd:PHA03095 126 sgfNINPK---VIRLLLRKGADVNALD-LYGMTPLAVLLKSRnaNVELLRLLIDAGADVYAVDDRFRSLLHHhlQSFKPR 201

                        170       180
                 ....*....|....*....|....*...
gi 164607184 317 LPLVRTLVRSGADSGLKNCHNDTPLMVA 344
Cdd:PHA03095 202 ARIVRELIRAGCDPAATDMLGNTPLHSM 229
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 128-358 8.68e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 69.61  E-value: 8.68e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 128 EDGDTPLHIAVVQNNIaavyRILSLFKLGSREVDVHNNLRQTPLHLAVITTLPDMVRLLVTAGASpmaldrhgqTAIhLA 207
Cdd:PHA02874  33 DETTTPLIDAIRSGDA----KIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVD---------TSI-LP 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 208 CEHRSPSCLQALLDSAtsgsVDLEVRNYEGLTALHVAVNTGCQEAVLLLLERGADIDAVDIkSGRSPLIHAVENNSLNMV 287
Cdd:PHA02874  99 IPCIEKDMIKTILDCG----IDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDD-NGCYPIHIAIKHNFFDII 173

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 164607184 288 QLLLLHGANVNAQMYSGSSALHSASGRGLLPLVRTLVRSGADSGLKnCHND-TPLMVA--RSRRVIDILRGKAS 358
Cdd:PHA02874 174 KLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNK-CKNGfTPLHNAiiHNRSAIELLINNAS 246
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 125-354 9.43e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 69.91  E-value: 9.43e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 125 RVDEDGDTPLHIAVVQNNIAAVYRILSLF---KLGSREVDVHNNLRQTPLHLAVITTL---------------------- 179
Cdd:PHA02878  65 QPDHRDLTPLHIICKEPNKLGMKEMIRSInkcSVFYTLVAIKDAFNNRNVEIFKIILTnrykniqtidlvyidkkskddi 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 180 --PDMVRLLVTAGASPMALDRH-GQTAIHLACEHRSPSCLQALLDSATSGSVDLEVRNYegltALHVAVNTGCQEAVLLL 256
Cdd:PHA02878 145 ieAEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNS----PLHHAVKHYNKPIVHIL 220

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 257 LERGADIDAVDiKSGRSPLIHAVEN-NSLNMVQLLLLHGANVNAQMY-SGSSALHSA--SGRGLlplvRTLVRSGADSGL 332
Cdd:PHA02878 221 LENGASTDARD-KCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYiLGLTALHSSikSERKL----KLLLEYGADINS 295

                        250       260
                 ....*....|....*....|...
gi 164607184 333 KNCHNDTPL-MVARSRRVIDILR 354
Cdd:PHA02878 296 LNSYKLTPLsSAVKQYLCINIGR 318
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 118-293 5.19e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 67.60  E-value: 5.19e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 118 ADIAMATRvdEDGDTPLHIAVVQNNiaavYRILSLFKLGSREVDVHNNLRQTPLHLAVITTLPDMVRLLVTAGASPMALD 197
Cdd:PHA02878 158 ADINMKDR--HKGNTALHYATENKD----QRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARD 231

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 198 RHGQTAIHLACEH-RSPSCLQALLDSATSGSVDLEVRnyeGLTALHVAVNTgcQEAVLLLLERGADIDAVDIKSgRSPLI 276
Cdd:PHA02878 232 KCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYIL---GLTALHSSIKS--ERKLKLLLEYGADINSLNSYK-LTPLS 305

                        170
                 ....*....|....*...
gi 164607184 277 HAVENNS-LNMVQLLLLH 293
Cdd:PHA02878 306 SAVKQYLcINIGRILISN 323
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 126-344 7.50e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 67.40  E-value: 7.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 126 VDEDGDTPLHIAVvqnNIAAVYRILSlfKLGSREVDVH-NNLR-QTPLHLAVITTL-PDMVRLLVTAGASPMALDRHGQT 202
Cdd:PHA02876 269 IDDCKNTPLHHAS---QAPSLSRLVP--KLLERGADVNaKNIKgETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYIT 343

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 203 AIHLACE-HRSPSCLQALLDSATsgsvDLEVRNYEGLTALHVAVNTGCQEAVLLLLERGADIDAVDIKSGRSPLIHAVEN 281
Cdd:PHA02876 344 PLHQASTlDRNKDIVITLLELGA----NVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGT 419

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 164607184 282 NSLNMVQLLLLHGANVNAQMYSGSSALHSASGRGLLP-LVRTLVRSGADSGLKNCHNDTPLMVA 344
Cdd:PHA02876 420 NPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKLdVIEMLLDNGADVNAINIQNQYPLLIA 483
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 129-329 3.81e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 65.08  E-value: 3.81e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 129 DGDTPLHIAVVQNNIAAVYRIlslfklgsreVDVHNNLRQTPLHL--AVITTLPDMVRLLVTAGASPMALDRHGQTAIHL 206
Cdd:PHA02876 210 DDLSVLECAVDSKNIDTIKAI----------IDNRSNINKNDLSLlkAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHH 279

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 207 ACEhrSPScLQALLDSATSGSVDLEVRNYEGLTALHVAVNTGCQ-EAVLLLLERGADIDAVDiKSGRSPLIHA--VENNS 283
Cdd:PHA02876 280 ASQ--APS-LSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYDtENIRTLIMLGADVNAAD-RLYITPLHQAstLDRNK 355

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 164607184 284 LNMVQLLLLhGANVNAQMYSGSSALHSASGRGLLPLVRTLVRSGAD 329
Cdd:PHA02876 356 DIVITLLEL-GANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGAD 400
Ank_2 pfam12796
Ankyrin repeats (3 copies);
275-354 4.36e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.97  E-value: 4.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184  275 LIHAVENNSLNMVQLLLLHGANVNAQMYSGSSALHSASGRGLLPLVRTLVrSGADSGLKNcHNDTPLMVARSRRVIDILR 354
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 174-354 9.24e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 63.47  E-value: 9.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 174 AVITTLPDMVRLLVTAGASPMALDRHGQTAIHLACEHRSPSCLQALLDSATSGSVdlevrNYEGL-TALHVAVNTGCQEA 252
Cdd:PHA02875   9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDV-----KYPDIeSELHDAVEEGDVKA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 253 VLLLLERGADIDAVDIKSGRSPLIHAVENNSLNMVQLLLLHGANVNAQMYSGSSALHSASGRGLLPLVRTLVRSGADSGL 332
Cdd:PHA02875  84 VEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDI 163

                        170       180
                 ....*....|....*....|..
gi 164607184 333 KNCHNDTPLMVARSRRVIDILR 354
Cdd:PHA02875 164 EDCCGCTPLIIAMAKGDIAICK 185
Ank_4 pfam13637
Ankyrin repeats (many copies);
237-291 1.79e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.13  E-value: 1.79e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 164607184  237 GLTALHVAVNTGCQEAVLLLLERGADIDAVDiKSGRSPLIHAVENNSLNMVQLLL 291
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVD-GNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 159-344 4.52e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 61.13  E-value: 4.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 159 EVDVHNNLRQTPLHLAVITTLPDMVRLLVTAGASPMALDRHGQTAIHLACEHRSPSCLQALLDSATSgsvdLEVRNYEGL 238
Cdd:PHA02874 116 DVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY----ANVKDNNGE 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 239 TALHVAVNTGCQEAVLLLLERGADIdAVDIKSGRSPLIHAVENNslNMVQLLLLHGANVNAQMYSGSSALHSAsgrgLLP 318
Cdd:PHA02874 192 SPLHNAAEYGDYACIKLLIDHGNHI-MNKCKNGFTPLHNAIIHN--RSAIELLINNASINDQDIDGSTPLHHA----INP 264

                        170       180       190
                 ....*....|....*....|....*....|.
gi 164607184 319 -----LVRTLVRSGADSGLKNCHNDTPLMVA 344
Cdd:PHA02874 265 pcdidIIDILLYHKADISIKDNKGENPIDTA 295
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 169-361 6.59e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 60.78  E-value: 6.59e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 169 TPLHLAVITTLPDMVRLLVTAGASPMALDRHGQTAIHLACEHRSPSCLQALLDSATSGSvdlEVRNYEGLTALHVAVNTG 248
Cdd:PHA02875  37 SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAD---DVFYKDGMTPLHLATILK 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 249 CQEAVLLLLERGADIDaVDIKSGRSPLIHAVENNSLNMVQLLLLHGANVNAQMYSGSSALHSASGRGLLPLVRTLVRSGA 328
Cdd:PHA02875 114 KLDIMKLLIARGADPD-IPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGA 192

                        170       180       190
                 ....*....|....*....|....*....|....
gi 164607184 329 DSGLKNCHNDTPLM-VARSRRVIDILRGKASRAA 361
Cdd:PHA02875 193 NIDYFGKNGCVAALcYAIENNKIDIVRLFIKRGA 226
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 148-346 9.80e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 60.85  E-value: 9.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 148 RILSLFKLGSREVDVHNNLRQTPLHLAVITTLPDMVRLLVTAGASPMALDRHGQTAIHLACEHRSPSCLQALLDSATSgs 227
Cdd:PHA02876 159 LIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSN-- 236

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 228 vdlevRNYEGLTALHVAVNTGCqEAVLLLLERGADIDAVDIKSgRSPLIHAVENNSLN-MVQLLLLHGANVNAQMYSGSS 306
Cdd:PHA02876 237 -----INKNDLSLLKAIRNEDL-ETSLLLYDAGFSVNSIDDCK-NTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGET 309

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 164607184 307 ALHSASGRGL-LPLVRTLVRSGADSGLKNCHNDTPLMVARS 346
Cdd:PHA02876 310 PLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQAST 350
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 186-338 1.28e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 60.27  E-value: 1.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 186 LVTAGASPMALDRHGQTAIHLACEHRSPSCLQALLDSAtsgsVDLEVRNYEGLTALHVAVNTGCQEAVLLLLERGAdidA 265
Cdd:PLN03192 544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA----CNVHIRDANGNTALWNAISAKHHKIFRILYHFAS---I 616

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164607184 266 VDIKSGRSPLIHAVENNSLNMVQLLLLHGANVNAQMYSGSSALHSASGRGLLPLVRTLVRSGADSGLKNCHND 338
Cdd:PLN03192 617 SDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDD 689
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 169-309 1.54e-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: 60.03  E-value: 1.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 169 TPLHLAVITT-LPDMVRLLVTAGASPMALDRHGQTAIHLACEHRSPSCLQALLDSAtSGSVDLEVRN--YEGLTALHVAV 245
Cdd:cd22192   19 SPLLLAAKENdVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAA-PELVNEPMTSdlYQGETALHIAV 97

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164607184 246 NTGCQEAVLLLLERGADIDAVD-------------IKSGRSPLIHAVENNSLNMVQLLLLHGANVNAQMYSGSSALH 309
Cdd:cd22192   98 VNQNLNLVRELIARGADVVSPRatgtffrpgpknlIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 127-275 4.40e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 58.05  E-value: 4.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 127 DEDGDTPLHIAVVQNNiaavYRILSLFKLGSREVDVHNNLRQTPLHLAVITTLPDMVRLLVTAGASPMALDRHGQTAIHL 206
Cdd:PHA02874 154 DDNGCYPIHIAIKHNF----FDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHN 229

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 207 ACEHRSpSCLQALLDSATsgsvdLEVRNYEGLTALHVAVNTGCQEAVL-LLLERGADIDAVDIKsGRSPL 275
Cdd:PHA02874 230 AIIHNR-SAIELLINNAS-----INDQDIDGSTPLHHAINPPCDIDIIdILLYHKADISIKDNK-GENPI 292
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 130-248 4.52e-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: 58.49  E-value: 4.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 130 GDTPLHIAVVQNNIAAVYRILSlfklgsREVDVhNNLRQT-----------------PLHLAVITTLPDMVRLLVTAGAS 192
Cdd:cd22192   89 GETALHIAVVNQNLNLVRELIA------RGADV-VSPRATgtffrpgpknliyygehPLSFAACVGNEEIVRLLIEHGAD 161

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164607184 193 PMALDRHGQTAIH-LACE-HRSPSC-----LQALLDSATSGSVDLeVRNYEGLTALHVAVNTG 248
Cdd:cd22192  162 IRAQDSLGNTVLHiLVLQpNKTFACqmydlILSYDKEDDLQPLDL-VPNNQGLTPFKLAAKEG 223
Ank_2 pfam12796
Ankyrin repeats (3 copies);
126-197 2.25e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 51.27  E-value: 2.25e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164607184  126 VDEDGDTPLHIAVVQNNIAAVYRILSLFKLGSRevdvhnNLRQTPLHLAVITTLPDMVRLLVTAGASPMALD 197
Cdd:pfam12796  26 QDKNGRTALHLAAKNGHLEIVKLLLEHADVNLK------DNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 225-312 2.29e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.45  E-value: 2.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 225 SGSVDLEVRNYEGLTALHVAVNTGCQEAVLLLLERGADIDAVDiKSGRSPLIHAVENNSLNMVQLLLLH-------GANV 297
Cdd:PTZ00322 103 TGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLD-KDGKTPLELAEENGFREVVQLLSRHsqchfelGANA 181

                         90
                 ....*....|....*
gi 164607184 298 NAQMYSGSSALHSAS 312
Cdd:PTZ00322 182 KPDSFTGKPPSLEDS 196
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 105-309 1.33e-07

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: 53.93  E-value: 1.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184  105 PYSMICPMEHPLSadiamatrvdeDGDTPLHIAVVQNNIAAVYRILSLFKlgSREVDVHNNLRQTPLHLAVITTLP-DMV 183
Cdd:TIGR00870   3 PLDIVPAEESPLS-----------DEEKAFLPAAERGDLASVYRDLEEPK--KLNINCPDRLGRSALFVAAIENENlELT 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184  184 RLLVTAGASPmaldRHGQTAIHLA-------CEhrspSCLQALLDSAtSGSVDLEVRN-------YEGLTALHVAVNTGC 249
Cdd:TIGR00870  70 ELLLNLSCRG----AVGDTLLHAIsleyvdaVE----AILLHLLAAF-RKSGPLELANdqytsefTPGITALHLAAHRQN 140

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164607184  250 QEAVLLLLERGADIDA------------VD-IKSGRSPLIHAVENNSLNMVQLLLLHGANVNAQMYSGSSALH 309
Cdd:TIGR00870 141 YEIVKLLLERGASVPAracgdffvksqgVDsFYHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLH 213
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 127-267 1.80e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 53.13  E-value: 1.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 127 DEDGDTPLHIAVVqnNIAAVYRILSLFKLGSREVDVHNNLRQTPLHLAVITTLPD--MVRLLVTAGASPMALDR------ 198
Cdd:PHA03100 103 DNNGITPLLYAIS--KKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDINAKNRvnylls 180

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164607184 199 ----------HGQTAIHLACEHRSPSCLQALLDSatsgSVDLEVRNYEGLTALHVAVNTGCQEAVLLLLERGADIDAVD 267
Cdd:PHA03100 181 ygvpinikdvYGFTPLHYAVYNNNPEFVKYLLDL----GANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTII 255
Ank_5 pfam13857
Ankyrin repeats (many copies);
226-278 3.83e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.96  E-value: 3.83e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 164607184  226 GSVDLEVRNYEGLTALHVAVNTGCQEAVLLLLERGADIDAVDiKSGRSPLIHA 278
Cdd:pfam13857   5 GPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKD-EEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
271-324 1.00e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.34  E-value: 1.00e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 164607184  271 GRSPLIHAVENNSLNMVQLLLLHGANVNAQMYSGSSALHSASGRGLLPLVRTLV 324
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 230-329 2.83e-06

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: 49.69  E-value: 2.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184  230 LEVRNYEGLTALHVAVNT---GCQEAVLLLLERGADID----AVDIKSGR-----SPLIHAVENNSLNMVQLLLLHGANV 297
Cdd:TIGR00870  75 LSCRGAVGDTLLHAISLEyvdAVEAILLHLLAAFRKSGplelANDQYTSEftpgiTALHLAAHRQNYEIVKLLLERGASV 154

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 164607184  298 NAQ--------------MYSGSSALHSASGRGLLPLVRTLVRSGAD 329
Cdd:TIGR00870 155 PARacgdffvksqgvdsFYHGESPLNAAACLGSPSIVALLSEDPAD 200
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 200-309 2.96e-06

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: 49.49  E-value: 2.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 200 GQTAIHLAC---EHRSPSCLQALLDSATSGSVDLEVRN-------YEGLTALHVAVNTGCQEAVLLLLERGADIDAVD-- 267
Cdd:cd21882   26 GKTCLHKAAlnlNDGVNEAIMLLLEAAPDSGNPKELVNapctdefYQGQTALHIAIENRNLNLVRLLVENGADVSARAtg 105

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 164607184 268 ----------IKSGRSPLIHAVENNSLNMVQLLLLHG---ANVNAQMYSGSSALH 309
Cdd:cd21882  106 rffrkspgnlFYFGELPLSLAACTNQEEIVRLLLENGaqpAALEAQDSLGNTVLH 160
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 215-310 2.97e-06

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: 49.76  E-value: 2.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 215 CLQALLDSAtsgsvdLEVRNYEGLTALHVAVNTGCQEAVLLLLERGADIDAV-------------DIKSGRSPLIHAVEN 281
Cdd:cd22194  125 ILDRFINAE------YTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHakgvffnpkykheGFYFGETPLALAACT 198

                         90       100       110
                 ....*....|....*....|....*....|
gi 164607184 282 NSLNMVQLLLLHGA-NVNAQMYSGSSALHS 310
Cdd:cd22194  199 NQPEIVQLLMEKEStDITSQDSRGNTVLHA 228
PHA02741 PHA02741
hypothetical protein; Provisional
 233-354 5.42e-06

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 46.57  E-value: 5.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 233 RNYEGLTALHVAVNTGCQEavllLLER----------GADIDAVDIKSGRSPLIHAVENN---SLNMVQLLLLHGANVNA 299
Cdd:PHA02741  17 KNSEGENFFHEAARCGCFD----IIARftpfirgdchAAALNATDDAGQMCIHIAAEKHEaqlAAEIIDHLIELGADINA 92

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 300 Q-MYSGSSALHSASGRGLLPLVRTLVRS-GADSGLKNCHNDTPLMVA---RSRRVIDILR 354
Cdd:PHA02741  93 QeMLEGDTALHLAAHRRDHDLAEWLCCQpGIDLHFCNADNKSPFELAidnEDVAMMQILR 152
Ank_5 pfam13857
Ankyrin repeats (many copies);
152-207 5.63e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.49  E-value: 5.63e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 164607184  152 LFKLGSREVDVHNNLRQTPLHLAVITTLPDMVRLLVTAGASPMALDRHGQTAIHLA 207
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
169-220 1.98e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.88  E-value: 1.98e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 164607184  169 TPLHLAVITTLPDMVRLLVTAGASPMALDRHGQTAIHLACEHRSPSCLQALL 220
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 271-299 1.98e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.42  E-value: 1.98e-05
                           10        20
                   ....*....|....*....|....*....
gi 164607184   271 GRSPLIHAVENNSLNMVQLLLLHGANVNA 299
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 236-267 2.90e-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: 40.74  E-value: 2.90e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 164607184  236 EGLTALHVAV-NTGCQEAVLLLLERGADIDAVD 267
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
Ank_5 pfam13857
Ankyrin repeats (many copies);
185-244 5.67e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.79  E-value: 5.67e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184  185 LLVTAGASPMALDRHGQTAIHLACEHRSPSCLQALLDsatsGSVDLEVRNYEGLTALHVA 244
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLA----YGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
256-311 6.50e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.41  E-value: 6.50e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 164607184  256 LLERG-ADIDAVDiKSGRSPLIHAVENNSLNMVQLLLLHGANVNAQMYSGSSALHSA 311
Cdd:pfam13857   1 LLEHGpIDLNRLD-GEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 130-259 8.43e-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: 45.07  E-value: 8.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184  130 GDTPLHIAVVQNNiaavYRILSLfkLGSREVDVH--------------NNLR--QTPLHLAVITTLPDMVRLLVTAGASP 193
Cdd:TIGR00870 128 GITALHLAAHRQN----YEIVKL--LLERGASVParacgdffvksqgvDSFYhgESPLNAAACLGSPSIVALLSEDPADI 201

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164607184  194 MALDRHGQTAIHLA-------CEHR--SPSCLQALLD--SATSGSVDLE-VRNYEGLTALHVAVNTGCQEAVLLLLER 259
Cdd:TIGR00870 202 LTADSLGNTLLHLLvmenefkAEYEelSCQMYNFALSllDKLRDSKELEvILNHQGLTPLKLAAKEGRIVLFRLKLAI 279
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 271-299 1.81e-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: 38.39  E-value: 1.81e-04
                          10        20
                  ....*....|....*....|....*....
gi 164607184  271 GRSPLIHAVENNSLNMVQLLLLHGANVNA 299
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 287-344 3.28e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.96  E-value: 3.28e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 164607184 287 VQLLLLHGANVNAQMYSGSSALHSASGRGLLPLVRTLVRSGADSGLKNCHNDTPLMVA 344
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA 155
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 271-300 3.59e-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: 3.59e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 164607184  271 GRSPLIHAV-ENNSLNMVQLLLLHGANVNAQ 300
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNAR 32
Ank_4 pfam13637
Ankyrin repeats (many copies);
202-257 4.75e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.02  E-value: 4.75e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 164607184  202 TAIHLACEHRSPSCLQALLDSatsgSVDLEVRNYEGLTALHVAVNTGCQEAVLLLL 257
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEK----GADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 215-329 5.49e-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: 5.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 215 CLQALLDSAtsgSVDLEVRNYEGLTALHVAVNTGCQEAVLLLLERGADIdavdiksgrsplihavennsLNMVqllllhg 294
Cdd:cd22192   32 AIKKLLKCP---SCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPEL--------------------VNEP------- 81

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 164607184 295 anVNAQMYSGSSALHSASGRGLLPLVRTLVRSGAD 329
Cdd:cd22192   82 --MTSDLYQGETALHIAVVNQNLNLVRELIARGAD 114
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 236-265 1.03e-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: 36.41  E-value: 1.03e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 164607184   236 EGLTALHVAVNTGCQEAVLLLLERGADIDA 265
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 235-310 1.26e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong 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: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 41.32  E-value: 1.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 235 YEGLTALHVAVNTGCQEAVLLLLERGADIDAVD-------------IKSGRSPLIHAVENNSLNMVQLLLLHG---ANVN 298
Cdd:cd22193   74 YEGQTALHIAIERRQGDIVALLVENGADVHAHAkgrffqpkyqgegFYFGELPLSLAACTNQPDIVQYLLENEhqpADIE 153

                         90
                 ....*....|..
gi 164607184 299 AQMYSGSSALHS 310
Cdd:cd22193  154 AQDSRGNTVLHA 165
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 168-220 1.58e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.04  E-value: 1.58e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 164607184 168 QTPLHLAVITTLPDMVRLLVTAGASPMALDRHGQTAIHLACEHRSPSCLQALL 220
Cdd:PTZ00322 116 RTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PHA03095 PHA03095
ankyrin-like protein; Provisional
 126-222 1.90e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 40.39  E-value: 1.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 126 VDEDGDTPLHIAVVQNNIAAVYrILSLFKLGSrEVDVHNNLRQTPLHLAVITTLPDMVRLLVTAGASPMALDRHGQTAIH 205
Cdd:PHA03095 218 TDMLGNTPLHSMATGSSCKRSL-VLPLLIAGI-SINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLS 295

                         90
                 ....*....|....*..
gi 164607184 206 LACEHRSPSCLQALLDS 222
Cdd:PHA03095 296 LMVRNNNGRAVRAALAK 312
Ank_5 pfam13857
Ankyrin repeats (many copies);
289-344 2.48e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.17  E-value: 2.48e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 164607184  289 LLLLHGANVNAQMYSGSSALHSASGRGLLPLVRTLVRSGADSGLKNCHNDTPLMVA 344
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 191-331 3.41e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 37.93  E-value: 3.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 191 ASPMALDRHGQTAIHLACEHRSPSCLQALLDSATSGSVDLEVR-NYEGLTALHVAVNTGC---QEAVLLLLERGADIDAV 266
Cdd:PHA02736   8 IFASEPDIEGENILHYLCRNGGVTDLLAFKNAISDENRYLVLEyNRHGKQCVHIVSNPDKadpQEKLKLLMEWGADINGK 87

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 164607184 267 DIKSGRSPLIHAVENNSLNMVQLLLLH-GANVNAQMYSGSSALHSASGRGLLPLVRTLVRSGADSG 331
Cdd:PHA02736  88 ERVFGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGAQCK 153
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 235-310 4.09e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. 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.


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 39.40  E-value: 4.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 235 YEGLTALHVAVNTGCQEAVLLLLERGADIDAV-------DIKS------GRSPLIHAVENNSLNMVQLLL---LHGANVN 298
Cdd:cd22196   92 YKGQTALHIAIERRNMHLVELLVQNGADVHARasgeffkKKKGgpgfyfGELPLSLAACTNQLDIVKFLLenpHSPADIS 171

                         90
                 ....*....|..
gi 164607184 299 AQMYSGSSALHS 310
Cdd:cd22196  172 ARDSMGNTVLHA 183
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 121-259 4.13e-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: 39.74  E-value: 4.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 121 AMATRVDEDGDTPLHIAVVQNNiaavYRILSLFKLGSREVDVHNNLR--------------QTPLHLAVITTLPDMVRLL 186
Cdd:cd22194  132 AEYTEEAYEGQTALNIAIERRQ----GDIVKLLIAKGADVNAHAKGVffnpkykhegfyfgETPLALAACTNQPEIVQLL 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 187 VTAGASPMAL-DRHGQTAIHLACEHRSPSclQALLDSAT---------SGSVDLE-VRNYEGLTALHVAVNTGCQEAVLL 255
Cdd:cd22194  208 MEKESTDITSqDSRGNTVLHALVTVAEDS--KTQNDFVKrmydmillkSENKNLEtIRNNEGLTPLQLAAKMGKAEILKY 285


                 ....
gi 164607184 256 LLER 259
Cdd:cd22194  286 ILSR 289
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 168-198 4.37e-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: 34.57  E-value: 4.37e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 164607184  168 QTPLHLAVITT-LPDMVRLLVTAGASPMALDR 198
Cdd:pfam00023   3 NTPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 118-191 5.32e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 37.55  E-value: 5.32e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 164607184 118 ADIAMATRVDedGDTPLHIAVVQNNiaavYRILS-LFKLGSREVDVHNNLRQTPLHLAVITTLPDMVRLLVTAGA 191
Cdd:PHA02736  82 ADINGKERVF--GNTPLHIAVYTQN----YELATwLCNQPGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGA 150
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 237-335 6.67e-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: 38.71  E-value: 6.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164607184 237 GLTALHVAV---NTGCQEAVLLLLErgadidavdiksgrsplihaVENNSLNMVQLlllhganVNAQM----YSGSSALH 309
Cdd:cd21882   26 GKTCLHKAAlnlNDGVNEAIMLLLE--------------------AAPDSGNPKEL-------VNAPCtdefYQGQTALH 78

                         90       100
                 ....*....|....*....|....*.
gi 164607184 310 SASGRGLLPLVRTLVRSGADSGLKNC 335
Cdd:cd21882   79 IAIENRNLNLVRLLVENGADVSARAT 104
TRPV4 cd22195
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed ...
 235-265 8.22e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed broadly in neuronal and non-neuronal cells. It is activated by various stimuli, including hypo-osmolarity, warm temperature, and chemical ligands. TRPV4 acts in physiological functions such as osmoregulation and thermoregulation. It also has a role in mechanosensation in the vascular endothelium and urinary tract, and in cell barrier formation in vascular and epidermal tissues. Knockout mice studies suggested the functional importance of TRPV4 in the central nervous system, nociception, and bone formation. TRPV4 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 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.


Pssm-ID: 411979 [Multi-domain]  Cd Length: 733  Bit Score: 38.68  E-value: 8.22e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 164607184 235 YEGLTALHVAVNTGCQEAVLLLLERGADIDA 265
Cdd:cd22195  135 YRGQTALHIAIERRCKHYVELLVEKGADVHA 165
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 126-199 8.59e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 38.49  E-value: 8.59e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 164607184 126 VDEDGDTPLHIAVVQNNIAAVYRILslfKLGSrEVDVHNNLRQTPLHLAVITTLPDMVRLLVTAGASPMALDRH 199
Cdd:PHA03100 188 KDVYGFTPLHYAVYNNNPEFVKYLL---DLGA-NPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 169-193 8.93e-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: 33.72  E-value: 8.93e-03
                           10        20
                   ....*....|....*....|....*
gi 164607184   169 TPLHLAVITTLPDMVRLLVTAGASP 193
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADI 28
 
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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