|
Name |
Accession |
Description |
Interval |
E-value |
| PGG |
pfam13962 |
Domain of unknown function; The PGG domain is named for the highly conserved sequence motif ... |
462-568 |
5.95e-24 |
|
Domain of unknown function; The PGG domain is named for the highly conserved sequence motif found at the startt of the domain. The function is not known.
Pssm-ID: 433609 Cd Length: 114 Bit Score: 96.85 E-value: 5.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 462 TSTGTVASVLIATVTFAAALTVPGGYVADD-HPNAGTAASAGRFAFRAFAVSDTMAFLCSIVGTCLLVVGEAREVRPSRG 540
Cdd:pfam13962 8 RNTLLLVATLIATVTFAAGFTPPGGYWQDDdGPHAGKPILAKNPAFKAFVISNAIAFFASLVAVVLLLSIVSDFLRSLPR 87
|
90 100
....*....|....*....|....*...
gi 2756276124 541 RLRAyqgSAWALVTAGAqFMVAAFAFGL 568
Cdd:pfam13962 88 KLRI---GLKLLWVALL-SMLVAFAAGS 111
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
168-426 |
1.83e-19 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 89.24 E-value: 1.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 168 LMAEAPELASVANDGGVSPLYLAATVGSVDIVRALLHPLPDGTPSPASAAGPDGRTALHSAATTSKEIAREILDwkpEGR 247
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLL---AAG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 248 TLLTKADSSGRTPLHFAISSqiERFDVFQLFLDAEPSLALVcDIQGSFPLHVAAVMGSVRIVVELIQKCPNNynDLVDDR 327
Cdd:COG0666 78 ADINAKDDGGNTLLHAAARN--GDLEIVKLLLEAGADVNAR-DKDGETPLHLAAYNGNLEIVKLLLEAGADV--NAQDND 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 328 GRNFLHCAVEHNKESIVRYICRddrFGILMNAMDNEGNTPLHLAAEYGHPRMVSLLLETmSVDVAITNRDGLTAADLAYR 407
Cdd:COG0666 153 GNTPLHLAAANGNLEIVKLLLE---AGADVNARDNDGETPLHLAAENGHLEIVKLLLEA-GADVNAKDNDGKTALDLAAE 228
|
250
....*....|....*....
gi 2756276124 408 HLQPGLHYFLNPRAVVKNL 426
Cdd:COG0666 229 NGNLEIVKLLLEAGADLNA 247
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
38-287 |
3.47e-16 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 79.61 E-value: 3.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 38 GHSLSQVAIRVDDDDDGRAPAGASRLLGVTTGNGNTALHVAATRGHAALAALVCAtAPALAATRNRFLDTPLHCAAKSGH 117
Cdd:COG0666 54 GALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLE-AGADVNARDKDGETPLHLAAYNGN 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 118 RDVAACLLsemlrAGGAASAalplrrATNCLGATALHEAVRNGHAGVVALLMaEAPELASVANDGGVSPLYLAATVGSVD 197
Cdd:COG0666 133 LEIVKLLL-----EAGADVN------AQDNDGNTPLHLAAANGNLEIVKLLL-EAGADVNARDNDGETPLHLAAENGHLE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 198 IVRALLhplpdgtpspasAAGPD-------GRTALHSAAttsKEIAREILDWKPEGRTLLTKADSSGRTPLHFAISSQIE 270
Cdd:COG0666 201 IVKLLL------------EAGADvnakdndGKTALDLAA---ENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAA 265
|
250
....*....|....*..
gi 2756276124 271 RFDVFQLFLDAEPSLAL 287
Cdd:COG0666 266 LIVKLLLLALLLLAAAL 282
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
297-385 |
6.21e-13 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 64.75 E-value: 6.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 297 LHVAAVMGSVRIVVELIQKCPNNynDLVDDRGRNFLHCAVEHNKESIVRYICRDDRFGilmnaMDNEGNTPLHLAAEYGH 376
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADA--NLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN-----LKDNGRTALHYAARSGH 73
|
....*....
gi 2756276124 377 PRMVSLLLE 385
Cdd:pfam12796 74 LEIVKLLLE 82
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
141-450 |
3.00e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 69.22 E-value: 3.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 141 LRRATNCLG------ATALHEAVRNGHAGVVALLMAEAPELASVaNDGGVSPLYLAATVGSVDIVRALLHPLPDGTPSPA 214
Cdd:PHA02874 21 IKNKGNCINisvdetTTPLIDAIRSGDAKIVELFIKHGADINHI-NTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSILPI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 215 saagPDgrtalhsaatTSKEIAREILDwkpEGRTLLTKaDSSGRTPLHFAISSQieRFDVFQLFLDAEPSLAlVCDIQGS 294
Cdd:PHA02874 100 ----PC----------IEKDMIKTILD---CGIDVNIK-DAELKTFLHYAIKKG--DLESIKMLFEYGADVN-IEDDNGC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 295 FPLHVAAVMGSVRIVVELIQKcpNNYNDLVDDRGRNFLHCAVEHNKESIVRYICrdDRFGILMNAMDNeGNTPLHLAAEY 374
Cdd:PHA02874 159 YPIHIAIKHNFFDIIKLLLEK--GAYANVKDNNGESPLHNAAEYGDYACIKLLI--DHGNHIMNKCKN-GFTPLHNAIIH 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2756276124 375 GHpRMVSLLLETMSVDVaiTNRDGLTAadlayrhlqpgLHYFLNP---RAVVKNLFYcTRAPVTLEGDHARTGIPSAME 450
Cdd:PHA02874 234 NR-SAIELLINNASIND--QDIDGSTP-----------LHHAINPpcdIDIIDILLY-HKADISIKDNKGENPIDTAFK 297
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
109-208 |
8.12e-11 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 58.97 E-value: 8.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 109 LHCAAKSGHRDVAACLLSEMLRAGgaasaalplrrATNCLGATALHEAVRNGHAGVVALLMAEApelASVANDGGVSPLY 188
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADAN-----------LQDKNGRTALHLAAKNGHLEIVKLLLEHA---DVNLKDNGRTALH 66
|
90 100
....*....|....*....|
gi 2756276124 189 LAATVGSVDIVRALLHPLPD 208
Cdd:pfam12796 67 YAARSGHLEIVKLLLEKGAD 86
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
103-315 |
4.57e-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: 59.64 E-value: 4.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 103 RFLDTPLHCAAKSGhrDVAAclLSEMLRAggaaSAALPLRRATncLGATALHEAVRNGHAGVVALLMAEAPELASVANDG 182
Cdd:cd22192 15 RISESPLLLAAKEN--DVQA--IKKLLKC----PSCDLFQRGA--LGETALHVAALYDNLEAAVVLMEAAPELVNEPMTS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 183 ----GVSPLYLAATVGSVDIVRALLHPLPD-GTPSPASAAGPDGRTAL-----H----SAATTSKEIAREILDwkpegRT 248
Cdd:cd22192 85 dlyqGETALHIAVVNQNLNLVRELIARGADvVSPRATGTFFRPGPKNLiyygeHplsfAACVGNEEIVRLLIE-----HG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2756276124 249 LLTKA-DSSGRTPLHFAISSQIERF--DVFQLFLDAEP-----SLALVCDIQGSFPLHVAAVMGSVRIVVELIQK 315
Cdd:cd22192 160 ADIRAqDSLGNTVLHILVLQPNKTFacQMYDLILSYDKeddlqPLDLVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
71-180 |
3.09e-04 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 43.86 E-value: 3.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 71 GNTALHVAATRGHAALAALVcataPALAA-----TRNRFLDTPLHCAAKSGHRDVAACLlsemLRAGGAASAalplrrAT 145
Cdd:PHA03095 222 GNTPLHSMATGSSCKRSLVL----PLLIAgisinARNRYGQTPLHYAAVFNNPRACRRL----IALGADINA------VS 287
|
90 100 110
....*....|....*....|....*....|....*
gi 2756276124 146 NClGATALHEAVRNGHAGVVALLMAEAPELASVAN 180
Cdd:PHA03095 288 SD-GNTPLSLMVRNNNGRAVRAALAKNPSAETVAA 321
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
363-385 |
8.22e-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: 37.18 E-value: 8.22e-04
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PGG |
pfam13962 |
Domain of unknown function; The PGG domain is named for the highly conserved sequence motif ... |
462-568 |
5.95e-24 |
|
Domain of unknown function; The PGG domain is named for the highly conserved sequence motif found at the startt of the domain. The function is not known.
Pssm-ID: 433609 Cd Length: 114 Bit Score: 96.85 E-value: 5.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 462 TSTGTVASVLIATVTFAAALTVPGGYVADD-HPNAGTAASAGRFAFRAFAVSDTMAFLCSIVGTCLLVVGEAREVRPSRG 540
Cdd:pfam13962 8 RNTLLLVATLIATVTFAAGFTPPGGYWQDDdGPHAGKPILAKNPAFKAFVISNAIAFFASLVAVVLLLSIVSDFLRSLPR 87
|
90 100
....*....|....*....|....*...
gi 2756276124 541 RLRAyqgSAWALVTAGAqFMVAAFAFGL 568
Cdd:pfam13962 88 KLRI---GLKLLWVALL-SMLVAFAAGS 111
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
168-426 |
1.83e-19 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 89.24 E-value: 1.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 168 LMAEAPELASVANDGGVSPLYLAATVGSVDIVRALLHPLPDGTPSPASAAGPDGRTALHSAATTSKEIAREILDwkpEGR 247
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLL---AAG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 248 TLLTKADSSGRTPLHFAISSqiERFDVFQLFLDAEPSLALVcDIQGSFPLHVAAVMGSVRIVVELIQKCPNNynDLVDDR 327
Cdd:COG0666 78 ADINAKDDGGNTLLHAAARN--GDLEIVKLLLEAGADVNAR-DKDGETPLHLAAYNGNLEIVKLLLEAGADV--NAQDND 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 328 GRNFLHCAVEHNKESIVRYICRddrFGILMNAMDNEGNTPLHLAAEYGHPRMVSLLLETmSVDVAITNRDGLTAADLAYR 407
Cdd:COG0666 153 GNTPLHLAAANGNLEIVKLLLE---AGADVNARDNDGETPLHLAAENGHLEIVKLLLEA-GADVNAKDNDGKTALDLAAE 228
|
250
....*....|....*....
gi 2756276124 408 HLQPGLHYFLNPRAVVKNL 426
Cdd:COG0666 229 NGNLEIVKLLLEAGADLNA 247
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
150-426 |
1.27e-18 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 86.93 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 150 ATALHEAVRNGHAGVVALLMAEAPELASVANDGGVSPLYLAATVGSVDIVRALLHPLPDgtpspASAAGPDGRTALHSAA 229
Cdd:COG0666 21 LALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGAD-----INAKDDGGNTLLHAAA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 230 TT-SKEIAREILDWKPEgrtlLTKADSSGRTPLHFAISSqiERFDVFQLFLDAEPSLALVcDIQGSFPLHVAAVMGSVRI 308
Cdd:COG0666 96 RNgDLEIVKLLLEAGAD----VNARDKDGETPLHLAAYN--GNLEIVKLLLEAGADVNAQ-DNDGNTPLHLAAANGNLEI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 309 VVELIQKCPNNynDLVDDRGRNFLHCAVEHNKESIVRYICRddrFGILMNAMDNEGNTPLHLAAEYGHPRMVSLLLETMS 388
Cdd:COG0666 169 VKLLLEAGADV--NARDNDGETPLHLAAENGHLEIVKLLLE---AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
|
250 260 270
....*....|....*....|....*....|....*...
gi 2756276124 389 vDVAITNRDGLTAADLAYRHLQPGLHYFLNPRAVVKNL 426
Cdd:COG0666 244 -DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAA 280
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
70-401 |
1.98e-17 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 83.46 E-value: 1.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 70 NGNTALHVAATRGHAALAALVCATAPALAATRNRFLDTPLHCAAKSGHRDVAACLLsemlraggaasAALPLRRATNCLG 149
Cdd:COG0666 19 LLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLL-----------AAGADINAKDDGG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 150 ATALHEAVRNGHAGVVALLMAEAPELASVANDGGvSPLYLAATVGSVDIVRALLhplpdgtpspasAAGPDgrtalhsaa 229
Cdd:COG0666 88 NTLLHAAARNGDLEIVKLLLEAGADVNARDKDGE-TPLHLAAYNGNLEIVKLLL------------EAGAD--------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 230 ttskeiareildwkpegrtlLTKADSSGRTPLHFAISSQieRFDVFQLFLDAEPSLALVcDIQGSFPLHVAAVMGSVRIV 309
Cdd:COG0666 146 --------------------VNAQDNDGNTPLHLAAANG--NLEIVKLLLEAGADVNAR-DNDGETPLHLAAENGHLEIV 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 310 VELIQKCPNnyNDLVDDRGRNFLHCAVEHNKESIVRYIcrdDRFGILMNAMDNEGNTPLHLAAEYGHPRMVSLLLETMSV 389
Cdd:COG0666 203 KLLLEAGAD--VNAKDNDGKTALDLAAENGNLEIVKLL---LEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLL 277
|
330
....*....|..
gi 2756276124 390 DVAITNRDGLTA 401
Cdd:COG0666 278 LAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
38-287 |
3.47e-16 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 79.61 E-value: 3.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 38 GHSLSQVAIRVDDDDDGRAPAGASRLLGVTTGNGNTALHVAATRGHAALAALVCAtAPALAATRNRFLDTPLHCAAKSGH 117
Cdd:COG0666 54 GALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLE-AGADVNARDKDGETPLHLAAYNGN 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 118 RDVAACLLsemlrAGGAASAalplrrATNCLGATALHEAVRNGHAGVVALLMaEAPELASVANDGGVSPLYLAATVGSVD 197
Cdd:COG0666 133 LEIVKLLL-----EAGADVN------AQDNDGNTPLHLAAANGNLEIVKLLL-EAGADVNARDNDGETPLHLAAENGHLE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 198 IVRALLhplpdgtpspasAAGPD-------GRTALHSAAttsKEIAREILDWKPEGRTLLTKADSSGRTPLHFAISSQIE 270
Cdd:COG0666 201 IVKLLL------------EAGADvnakdndGKTALDLAA---ENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAA 265
|
250
....*....|....*..
gi 2756276124 271 RFDVFQLFLDAEPSLAL 287
Cdd:COG0666 266 LIVKLLLLALLLLAAAL 282
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
297-385 |
6.21e-13 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 64.75 E-value: 6.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 297 LHVAAVMGSVRIVVELIQKCPNNynDLVDDRGRNFLHCAVEHNKESIVRYICRDDRFGilmnaMDNEGNTPLHLAAEYGH 376
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADA--NLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN-----LKDNGRTALHYAARSGH 73
|
....*....
gi 2756276124 377 PRMVSLLLE 385
Cdd:pfam12796 74 LEIVKLLLE 82
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
141-450 |
3.00e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 69.22 E-value: 3.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 141 LRRATNCLG------ATALHEAVRNGHAGVVALLMAEAPELASVaNDGGVSPLYLAATVGSVDIVRALLHPLPDGTPSPA 214
Cdd:PHA02874 21 IKNKGNCINisvdetTTPLIDAIRSGDAKIVELFIKHGADINHI-NTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSILPI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 215 saagPDgrtalhsaatTSKEIAREILDwkpEGRTLLTKaDSSGRTPLHFAISSQieRFDVFQLFLDAEPSLAlVCDIQGS 294
Cdd:PHA02874 100 ----PC----------IEKDMIKTILD---CGIDVNIK-DAELKTFLHYAIKKG--DLESIKMLFEYGADVN-IEDDNGC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 295 FPLHVAAVMGSVRIVVELIQKcpNNYNDLVDDRGRNFLHCAVEHNKESIVRYICrdDRFGILMNAMDNeGNTPLHLAAEY 374
Cdd:PHA02874 159 YPIHIAIKHNFFDIIKLLLEK--GAYANVKDNNGESPLHNAAEYGDYACIKLLI--DHGNHIMNKCKN-GFTPLHNAIIH 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2756276124 375 GHpRMVSLLLETMSVDVaiTNRDGLTAadlayrhlqpgLHYFLNP---RAVVKNLFYcTRAPVTLEGDHARTGIPSAME 450
Cdd:PHA02874 234 NR-SAIELLINNASIND--QDIDGSTP-----------LHHAINPpcdIDIIDILLY-HKADISIKDNKGENPIDTAFK 297
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
109-208 |
8.12e-11 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 58.97 E-value: 8.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 109 LHCAAKSGHRDVAACLLSEMLRAGgaasaalplrrATNCLGATALHEAVRNGHAGVVALLMAEApelASVANDGGVSPLY 188
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADAN-----------LQDKNGRTALHLAAKNGHLEIVKLLLEHA---DVNLKDNGRTALH 66
|
90 100
....*....|....*....|
gi 2756276124 189 LAATVGSVDIVRALLHPLPD 208
Cdd:pfam12796 67 YAARSGHLEIVKLLLEKGAD 86
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
103-315 |
4.57e-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: 59.64 E-value: 4.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 103 RFLDTPLHCAAKSGhrDVAAclLSEMLRAggaaSAALPLRRATncLGATALHEAVRNGHAGVVALLMAEAPELASVANDG 182
Cdd:cd22192 15 RISESPLLLAAKEN--DVQA--IKKLLKC----PSCDLFQRGA--LGETALHVAALYDNLEAAVVLMEAAPELVNEPMTS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 183 ----GVSPLYLAATVGSVDIVRALLHPLPD-GTPSPASAAGPDGRTAL-----H----SAATTSKEIAREILDwkpegRT 248
Cdd:cd22192 85 dlyqGETALHIAVVNQNLNLVRELIARGADvVSPRATGTFFRPGPKNLiyygeHplsfAACVGNEEIVRLLIE-----HG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2756276124 249 LLTKA-DSSGRTPLHFAISSQIERF--DVFQLFLDAEP-----SLALVCDIQGSFPLHVAAVMGSVRIVVELIQK 315
Cdd:cd22192 160 ADIRAqDSLGNTVLHILVLQPNKTFacQMYDLILSYDKeddlqPLDLVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
332-405 |
8.27e-09 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 53.20 E-value: 8.27e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2756276124 332 LHCAVEHNKESIVRYICRddrFGILMNAMDNEGNTPLHLAAEYGHPRMVSLLLETMSVDVaitNRDGLTAADLA 405
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLE---NGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL---KDNGRTALHYA 68
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
75-175 |
8.86e-08 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 50.11 E-value: 8.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 75 LHVAATRGHAALA-ALVcaTAPALAATRNRFLDTPLHCAAKSGHRDVAACLLSEMlraggaasaalplRRATNCLGATAL 153
Cdd:pfam12796 1 LHLAAKNGNLELVkLLL--ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-------------DVNLKDNGRTAL 65
|
90 100
....*....|....*....|..
gi 2756276124 154 HEAVRNGHAGVVALLMAEAPEL 175
Cdd:pfam12796 66 HYAARSGHLEIVKLLLEKGADI 87
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
187-280 |
9.96e-08 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 50.11 E-value: 9.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 187 LYLAATVGSVDIVRALLHPLPDgtpspASAAGPDGRTALHSAATT-SKEIAREILDwkpegrTLLTKADSSGRTPLHFAI 265
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGAD-----ANLQDKNGRTALHLAAKNgHLEIVKLLLE------HADVNLKDNGRTALHYAA 69
|
90
....*....|....*
gi 2756276124 266 SSQieRFDVFQLFLD 280
Cdd:pfam12796 70 RSG--HLEIVKLLLE 82
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
288-400 |
1.54e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 54.29 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 288 VCDIQGSFPLHVAAV--MGSVRIVVELIQkcpNNYN-DLVDDRGRNFLHCAVE--HNKESIVRY----------ICRDDR 352
Cdd:PHA03100 101 APDNNGITPLLYAISkkSNSYSIVEYLLD---NGANvNIKNSDGENLLHLYLEsnKIDLKILKLlidkgvdinaKNRVNY 177
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2756276124 353 F---GILMNAMDNEGNTPLHLAAEYGHPRMVSLLLEtMSVDVAITNRDGLT 400
Cdd:PHA03100 178 LlsyGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLD-LGANPNLVNKYGDT 227
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
162-408 |
2.33e-07 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 53.88 E-value: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 162 AGVVALLMAEApelASVANDG--GVSPL--YLAATVG-SVDIVRALLhplpdgtpspasAAGPD-------GRTALHSAA 229
Cdd:PHA03095 27 VEEVRRLLAAG---ADVNFRGeyGKTPLhlYLHYSSEkVKDIVRLLL------------EAGADvnapercGFTPLHLYL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 230 TTSKEIarEILDwkpegrtLLTKA-------DSSGRTPLHFAISSQIERFDVFQLFLDAEPSLAlVCDIQGSFPLHVaaV 302
Cdd:PHA03095 92 YNATTL--DVIK-------LLIKAgadvnakDKVGRTPLHVYLSGFNINPKVIRLLLRKGADVN-ALDLYGMTPLAV--L 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 303 MGSVRIVVE----LIQKCPNNYNdlVDDRGRNFLH--CAVEHNKESIVRYICR-------DDRF---------------- 353
Cdd:PHA03095 160 LKSRNANVEllrlLIDAGADVYA--VDDRFRSLLHhhLQSFKPRARIVRELIRagcdpaaTDMLgntplhsmatgssckr 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2756276124 354 ---------GILMNAMDNEGNTPLHLAAEYGHPRMVSLLLEtMSVDVAITNRDGLTAADLAYRH 408
Cdd:PHA03095 238 slvlplliaGISINARNRYGQTPLHYAAVFNNPRACRRLIA-LGADINAVSSDGNTPLSLMVRN 300
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
184-385 |
3.38e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 53.13 E-value: 3.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 184 VSPLYLAATVGSVDIVRALLHplpDGTPSPASAAgpDGRTALHSAA------TTSKEIAREILdwkpEGRTLLTKADSSG 257
Cdd:PHA03100 36 VLPLYLAKEARNIDVVKILLD---NGADINSSTK--NNSTPLHYLSnikynlTDVKEIVKLLL----EYGANVNAPDNNG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 258 RTPLHFAISSQIERFDVFQLFLDAEPSLALVCDIQGSfPLHVAAVMGSVRI-VVELIQKcpNNYN--------------- 321
Cdd:PHA03100 107 ITPLLYAISKKSNSYSIVEYLLDNGANVNIKNSDGEN-LLHLYLESNKIDLkILKLLID--KGVDinaknrvnyllsygv 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2756276124 322 --DLVDDRGRNFLHCAVEHNKESIVRYICRddrFGILMNAMDNEGNTPLHLAAEYGHPRMVSLLLE 385
Cdd:PHA03100 184 piNIKDVYGFTPLHYAVYNNNPEFVKYLLD---LGANPNLVNKYGDTPLHIAILNNNKEIFKLLLN 246
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
261-348 |
3.79e-07 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 48.57 E-value: 3.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 261 LHFAISSqiERFDVFQLFLDAEPSlALVCDIQGSFPLHVAAVMGSVRIVVELIQKCPNNyndlVDDRGRNFLHCAVEHNK 340
Cdd:pfam12796 1 LHLAAKN--GNLELVKLLLENGAD-ANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN----LKDNGRTALHYAARSGH 73
|
....*...
gi 2756276124 341 ESIVRYIC 348
Cdd:pfam12796 74 LEIVKLLL 81
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
351-405 |
4.71e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 46.96 E-value: 4.71e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2756276124 351 DRFGILMNAMDNEGNTPLHLAAEYGHPRMVSLLLEtMSVDVAITNRDGLTAADLA 405
Cdd:pfam13857 3 EHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLA-YGVDLNLKDEEGLTALDLA 56
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
104-386 |
7.91e-07 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 51.95 E-value: 7.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 104 FLDTPLHCAAKSGHRDVAACLLSeMLRAGGAASAAlplrraTNClGATALHEAVRNGH-AGVVALLMAEAPELaSVANDG 182
Cdd:PHA03095 46 YGKTPLHLYLHYSSEKVKDIVRL-LLEAGADVNAP------ERC-GFTPLHLYLYNATtLDVIKLLIKAGADV-NAKDKV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 183 GVSPLYLAATVGSVD--IVRALLHPLPDgtpspASAAGPDGRTALHsAATTSKEIAREILdwkpegRTLLTK------AD 254
Cdd:PHA03095 117 GRTPLHVYLSGFNINpkVIRLLLRKGAD-----VNALDLYGMTPLA-VLLKSRNANVELL------RLLIDAgadvyaVD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 255 SSGRTPLH-FAISSQiERFDVFQLFLDAEPSLALVcDIQGSFPLHVAAVMGSVR--IVVELIQKcpNNYNDLVDDRGRNF 331
Cdd:PHA03095 185 DRFRSLLHhHLQSFK-PRARIVRELIRAGCDPAAT-DMLGNTPLHSMATGSSCKrsLVLPLLIA--GISINARNRYGQTP 260
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2756276124 332 LHCAVEHNKESIVRYICRddrFGILMNAMDNEGNTPLHLAAEYGHPRMVSLLLET 386
Cdd:PHA03095 261 LHYAAVFNNPRACRRLIA---LGADINAVSSDGNTPLSLMVRNNNGRAVRAALAK 312
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
65-126 |
1.09e-06 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 47.03 E-value: 1.09e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2756276124 65 GVTTGNGNTALHVAATRGHAALAALVCATAPALAATRNRfldTPLHCAAKSGHRDVAACLLS 126
Cdd:pfam12796 24 NLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR---TALHYAARSGHLEIVKLLLE 82
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
328-384 |
2.24e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 44.96 E-value: 2.24e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2756276124 328 GRNFLHCAVEHNKESIVRYiCRDdrFGILMNAMDNEGNTPLHLAAEYGHPRMVSLLL 384
Cdd:pfam13637 1 ELTALHAAAASGHLELLRL-LLE--KGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
221-385 |
1.22e-05 |
|
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: 48.60 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 221 GRTALHSA----ATTSKEIAREILDWKPEGRTL-------LTKADSSGRTPLHFAIssqiER--FDVFQLFLDA------ 281
Cdd:cd22194 94 GKTCLMKAllniNENTKEIVRILLAFAEENGILdrfinaeYTEEAYEGQTALNIAI----ERrqGDIVKLLIAKgadvna 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 282 -------EPSLALVCDIQGSFPLHVAAVMGSVRIVVELIQKCPNNYNdLVDDRGRNFLHCAV------EHNKESIVRY-- 346
Cdd:cd22194 170 hakgvffNPKYKHEGFYFGETPLALAACTNQPEIVQLLMEKESTDIT-SQDSRGNTVLHALVtvaedsKTQNDFVKRMyd 248
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2756276124 347 -ICRDDRFGILMNAMDNEGNTPLHLAAEYGHPRMVSLLLE 385
Cdd:cd22194 249 mILLKSENKNLETIRNNEGLTPLQLAAKMGKAEILKYILS 288
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
259-405 |
2.43e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 47.75 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 259 TPLHFAIssQIERFDVFQLFLDAEPSLALVCDIQGSFPLHVAAVMGSVR-IVVELIQKCP------------NNY----- 320
Cdd:PHA02876 43 TAIHQAL--QLRQIDIVEEIIQQNPELIYITDHKCHSTLHTICIIPNVMdIVISLTLDCDiildikyasiilNKHkldea 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 321 -----------NDLVDDRgrnfLHCAVEHNKeSIVRYICRDD--------RFGILMNAMDNEGNTPLHLAAEYGHPRMVS 381
Cdd:PHA02876 121 cihilkeaisgNDIHYDK----INESIEYMK-LIKERIQQDElliaemllEGGADVNAKDIYCITPIHYAAERGNAKMVN 195
|
170 180
....*....|....*....|....
gi 2756276124 382 LLLeTMSVDVAITNRDGLTAADLA 405
Cdd:PHA02876 196 LLL-SYGADVNIIALDDLSVLECA 218
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
358-452 |
3.34e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 47.20 E-value: 3.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 358 NAMDNEGNTPLHLAAEYGHPRMVSLLLEtMSVDVAITNRDGLTAADLAYRHlqpglhyflNPRAVVKNLFYCTRAPVTLE 437
Cdd:PTZ00322 109 NCRDYDGRTPLHIACANGHVQVVRVLLE-FGADPTLLDKDGKTPLELAEEN---------GFREVVQLLSRHSQCHFELG 178
|
90
....*....|....*...
gi 2756276124 438 GDHAR---TGIPSAMEDA 452
Cdd:PTZ00322 179 ANAKPdsfTGKPPSLEDS 196
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
66-182 |
6.74e-05 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 45.33 E-value: 6.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 66 VTTGNGNTALHVAATRGHAALAALVCAtAPALAATRNRFLDTPLHCAAKSGHRDVAACLLsemlraggaasAALPLRRAT 145
Cdd:COG0666 181 ARDNDGETPLHLAAENGHLEIVKLLLE-AGADVNAKDNDGKTALDLAAENGNLEIVKLLL-----------EAGADLNAK 248
|
90 100 110
....*....|....*....|....*....|....*..
gi 2756276124 146 NCLGATALHEAVRNGHAGVVALLMAEAPELASVANDG 182
Cdd:COG0666 249 DKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
185-405 |
1.69e-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: 44.62 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 185 SPLYLAATVGSVDIVRALLhplpdGTPS-PASAAGPDGRTALHSAATTSK-EIAREILDWKPEgrtLLTKADSSgrtplh 262
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLL-----KCPScDLFQRGALGETALHVAALYDNlEAAVVLMEAAPE---LVNEPMTS------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 263 faissqierfdvfQLFldaepslalvcdiQGSFPLHVAAVMGSVRIVVELIQKCPnnynDLVDDR--------------- 327
Cdd:cd22192 85 -------------DLY-------------QGETALHIAVVNQNLNLVRELIARGA----DVVSPRatgtffrpgpknliy 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 328 -GRNFLHCAVEHNKESIVRYICRDdrfGILMNAMDNEGNTPLH---------LAAEyghprMVSLLL------ETMSVDV 391
Cdd:cd22192 135 yGEHPLSFAACVGNEEIVRLLIEH---GADIRAQDSLGNTVLHilvlqpnktFACQ-----MYDLILsydkedDLQPLDL 206
|
250
....*....|....
gi 2756276124 392 aITNRDGLTAADLA 405
Cdd:cd22192 207 -VPNNQGLTPFKLA 219
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
71-125 |
2.12e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 39.57 E-value: 2.12e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2756276124 71 GNTALHVAATRGH-AALAALVCATAPALAatRNRFLDTPLHCAAKSGHRDVAACLL 125
Cdd:pfam13637 1 ELTALHAAAASGHlELLRLLLEKGADINA--VDGNGETALHFAASNGNVEVLKLLL 54
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
107-315 |
3.04e-04 |
|
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: 44.10 E-value: 3.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 107 TPLHCAAKSGHRDVAACLLSeMLRAGGAASAALPLRRATnCL-----GATALHEAVRNGHAGVVALLMAEAPELASVAND 181
Cdd:cd21882 28 TCLHKAALNLNDGVNEAIML-LLEAAPDSGNPKELVNAP-CTdefyqGQTALHIAIENRNLNLVRLLVENGADVSARATG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 182 G------------GVSPLYLAATVGSVDIVRALLHPLPDgtpsPASAAGPD--GRTALHsaattskeIAREILDWKPEGR 247
Cdd:cd21882 106 RffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQ----PAALEAQDslGNTVLH--------ALVLQADNTPENS 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2756276124 248 TLLTKadssgrtpLHFAISSQIERFDVFQlfldaepSLALVCDIQGSFPLHVAAVMGSVRIVVELIQK 315
Cdd:cd21882 174 AFVCQ--------MYNLLLSYGAHLDPTQ-------QLEEIPNHQGLTPLKLAAVEGKIVMFQHILQR 226
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
71-180 |
3.09e-04 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 43.86 E-value: 3.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 71 GNTALHVAATRGHAALAALVcataPALAA-----TRNRFLDTPLHCAAKSGHRDVAACLlsemLRAGGAASAalplrrAT 145
Cdd:PHA03095 222 GNTPLHSMATGSSCKRSLVL----PLLIAgisinARNRYGQTPLHYAAVFNNPRACRRL----IALGADINA------VS 287
|
90 100 110
....*....|....*....|....*....|....*
gi 2756276124 146 NClGATALHEAVRNGHAGVVALLMAEAPELASVAN 180
Cdd:PHA03095 288 SD-GNTPLSLMVRNNNGRAVRAALAKNPSAETVAA 321
|
|
| PHA02741 |
PHA02741 |
hypothetical protein; Provisional |
249-396 |
6.58e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 165108 [Multi-domain] Cd Length: 169 Bit Score: 41.18 E-value: 6.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 249 LLTKADSSGRTPLHFAISSQ----IERFDVFqLFLDAEPSLALVCDIQGSFPLHVAAVMGSVRIVVELIQKCPN-----N 319
Cdd:PHA02741 13 MIAEKNSEGENFFHEAARCGcfdiIARFTPF-IRGDCHAAALNATDDAGQMCIHIAAEKHEAQLAAEIIDHLIElgadiN 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2756276124 320 YNDLVDdrGRNFLHCAVEHNKESIVRYICRDDRFGILMNAMDNEgnTPLHLAAEYGHPRMVSLLLETMSVDVAITNR 396
Cdd:PHA02741 92 AQEMLE--GDTALHLAAHRRDHDLAEWLCCQPGIDLHFCNADNK--SPFELAIDNEDVAMMQILREIVATSRGFSNE 164
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
363-385 |
8.22e-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: 37.18 E-value: 8.22e-04
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
363-396 |
9.01e-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: 37.27 E-value: 9.01e-04
10 20 30
....*....|....*....|....*....|....*
gi 2756276124 363 EGNTPLHLAA-EYGHPRMVSLLLEtMSVDVAITNR 396
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLS-KGADVNARDK 34
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
153-395 |
9.14e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 42.29 E-value: 9.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 153 LHEAVRNGHAGVVALLMAEAPELASVANDGGVSPLYLAATVGSVDIVRALLhplpdgtpspASAAGPDgrtalhsAATTS 232
Cdd:PHA02875 72 LHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLI----------ARGADPD-------IPNTD 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 233 KEiareildwkpegrtlltkadssgrTPLHFAISSQieRFDVFQLFLDAEPSLALVcDIQGSFPLHVAAVMGSVRIVVEL 312
Cdd:PHA02875 135 KF------------------------SPLHLAVMMG--DIKGIELLIDHKACLDIE-DCCGCTPLIIAMAKGDIAICKML 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 313 IQKCPNnyNDLVDDRGRNFLHC-AVEHNKESIVRYICRDDRFGILMNAMDNEGNTPLHLAAEYghprmvSLLLETMSVDV 391
Cdd:PHA02875 188 LDSGAN--IDYFGKNGCVAALCyAIENNKIDIVRLFIKRGADCNIMFMIEGEECTILDMICNM------CTNLESEAIDA 259
|
....
gi 2756276124 392 AITN 395
Cdd:PHA02875 260 LIAD 263
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
363-393 |
1.06e-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.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 36.85 E-value: 1.06e-03
10 20 30
....*....|....*....|....*....|.
gi 2756276124 363 EGNTPLHLAAEYGHPRMVSLLLEtMSVDVAI 393
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLE-NGADINA 30
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
292-407 |
1.35e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 41.79 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 292 QGSFPLHVAAVMGSVRIVVELIQKC--PNnyndlVDDRGRNF-LHCAVEHNKESIVRYICRDdrfGILMNAMDNEGNTPL 368
Cdd:PHA02878 167 KGNTALHYATENKDQRLTELLLSYGanVN-----IPDKTNNSpLHHAVKHYNKPIVHILLEN---GASTDARDKCGNTPL 238
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2756276124 369 HLAAEY-GHPRMVSLLLET-MSVDVAITNRdGLTAADLAYR 407
Cdd:PHA02878 239 HISVGYcKDYDILKLLLEHgVDVNAKSYIL-GLTALHSSIK 278
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
149-282 |
1.46e-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: 41.67 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 149 GATALHEAVRNGHAGVVALLMAEAPELASVA----------NDG---GVSPLYLAATVGSVDIVRALLhplpDGTPSPAS 215
Cdd:cd22194 141 GQTALNIAIERRQGDIVKLLIAKGADVNAHAkgvffnpkykHEGfyfGETPLALAACTNQPEIVQLLM----EKESTDIT 216
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2756276124 216 AAGPDGRTALHSAATTS----------KEIAREILDwKPEGRTLLTKADSSGRTPLHFAisSQIERFDVFQLFLDAE 282
Cdd:cd22194 217 SQDSRGNTVLHALVTVAedsktqndfvKRMYDMILL-KSENKNLETIRNNEGLTPLQLA--AKMGKAEILKYILSRE 290
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
364-417 |
1.56e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 36.87 E-value: 1.56e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2756276124 364 GNTPLHLAAEYGHPRMVSLLLETmSVDVAITNRDGLTAADLAYRHLQPG-LHYFL 417
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEK-GADINAVDGNGETALHFAASNGNVEvLKLLL 54
|
|
| PHA02741 |
PHA02741 |
hypothetical protein; Provisional |
297-405 |
2.49e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 165108 [Multi-domain] Cd Length: 169 Bit Score: 39.26 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756276124 297 LHVAAVMGSVRIVVELIQKCPNNYN----DLVDDRGRNFLH-CAVEHNKESIVRYICRDDRFGILMNAMDN-EGNTPLHL 370
Cdd:PHA02741 25 FHEAARCGCFDIIARFTPFIRGDCHaaalNATDDAGQMCIHiAAEKHEAQLAAEIIDHLIELGADINAQEMlEGDTALHL 104
|
90 100 110
....*....|....*....|....*....|....*
gi 2756276124 371 AAEYGHPRMVSLLLETMSVDVAITNRDGLTAADLA 405
Cdd:PHA02741 105 AAHRRDHDLAEWLCCQPGIDLHFCNADNKSPFELA 139
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
254-315 |
2.52e-03 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 37.40 E-value: 2.52e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2756276124 254 DSSGRTPLHFAISSQieRFDVFQLFLDaepSLALVCDIQGSFPLHVAAVMGSVRIVVELIQK 315
Cdd:pfam12796 27 DKNGRTALHLAAKNG--HLEIVKLLLE---HADVNLKDNGRTALHYAARSGHLEIVKLLLEK 83
|
|
|