|
Name |
Accession |
Description |
Interval |
E-value |
| PGG |
pfam13962 |
Domain of unknown function; The PGG domain is named for the highly conserved sequence motif ... |
500-606 |
5.16e-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: 97.24 E-value: 5.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 500 TSTGTVASVLIATVTFAAALTVPGGYVADD-HPNAGTAASAGRFAFRAFAVSDTMAFLCSIVGTCLLVVGEAREVRPSRG 578
Cdd:pfam13962 8 RNTLLLVATLIATVTFAAGFTPPGGYWQDDdGPHAGKPILAKNPAFKAFVISNAIAFFASLVAVVLLLSIVSDFLRSLPR 87
|
90 100
....*....|....*....|....*...
gi 1443089275 579 RLRAyqgSAWALVTAGAqFMVAAFAFGL 606
Cdd:pfam13962 88 KLRI---GLKLLWVALL-SMLVAFAAGS 111
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
206-464 |
8.81e-20 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 90.40 E-value: 8.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 206 LMAEAPELASVANDGGVSPLYLAATVGSVDIVRALLHPLPDGTPSPASAAGPDGRTALHSAATTSKEIAREILDwkpEGR 285
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLL---AAG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 286 TLLTKADSSGRTPLHFAISSqiERFDVFQLFLDAEPSLALVcDIQGSFPLHVAAVMGSVRIVVELIQKCPNNynDLVDDR 365
Cdd:COG0666 78 ADINAKDDGGNTLLHAAARN--GDLEIVKLLLEAGADVNAR-DKDGETPLHLAAYNGNLEIVKLLLEAGADV--NAQDND 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 366 GRNFLHCAVEHNKESIVRYICRddrFGILMNAMDNEGNTPLHLAAEYGHPRMVSLLLETmSVDVAITNRDGLTAADLAYR 445
Cdd:COG0666 153 GNTPLHLAAANGNLEIVKLLLE---AGADVNARDNDGETPLHLAAENGHLEIVKLLLEA-GADVNAKDNDGKTALDLAAE 228
|
250
....*....|....*....
gi 1443089275 446 HLQPGLHYFLNPRAVVKNL 464
Cdd:COG0666 229 NGNLEIVKLLLEAGADLNA 247
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
76-325 |
1.56e-16 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 80.77 E-value: 1.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 76 GHSLSQVAIRVDDDDDGRAPAGASRLLGVTTGNGNTALHVAATRGHAALAALVCAtAPALAATRNRFLDTPLHCAAKSGH 155
Cdd:COG0666 54 GALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLE-AGADVNARDKDGETPLHLAAYNGN 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 156 RDVAACLLsemlrAGGAASAalplrrATNCLGATALHEAVRNGHAGVVALLMaEAPELASVANDGGVSPLYLAATVGSVD 235
Cdd:COG0666 133 LEIVKLLL-----EAGADVN------AQDNDGNTPLHLAAANGNLEIVKLLL-EAGADVNARDNDGETPLHLAAENGHLE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 236 IVRALLhplpdgtpspasAAGPD-------GRTALHSAAttsKEIAREILDWKPEGRTLLTKADSSGRTPLHFAISSQIE 308
Cdd:COG0666 201 IVKLLL------------EAGADvnakdndGKTALDLAA---ENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAA 265
|
250
....*....|....*..
gi 1443089275 309 RFDVFQLFLDAEPSLAL 325
Cdd:COG0666 266 LIVKLLLLALLLLAAAL 282
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
335-423 |
4.25e-13 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 65.52 E-value: 4.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 335 LHVAAVMGSVRIVVELIQKCPNNynDLVDDRGRNFLHCAVEHNKESIVRYICRDDRFGilmnaMDNEGNTPLHLAAEYGH 414
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADA--NLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN-----LKDNGRTALHYAARSGH 73
|
....*....
gi 1443089275 415 PRMVSLLLE 423
Cdd:pfam12796 74 LEIVKLLLE 82
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
179-488 |
3.27e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 69.22 E-value: 3.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 179 LRRATNCLG------ATALHEAVRNGHAGVVALLMAEAPELASVaNDGGVSPLYLAATVGSVDIVRALLHPLPDGTPSPA 252
Cdd:PHA02874 21 IKNKGNCINisvdetTTPLIDAIRSGDAKIVELFIKHGADINHI-NTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSILPI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 253 saagPDgrtalhsaatTSKEIAREILDwkpEGRTLLTKaDSSGRTPLHFAISSQieRFDVFQLFLDAEPSLAlVCDIQGS 332
Cdd:PHA02874 100 ----PC----------IEKDMIKTILD---CGIDVNIK-DAELKTFLHYAIKKG--DLESIKMLFEYGADVN-IEDDNGC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 333 FPLHVAAVMGSVRIVVELIQKcpNNYNDLVDDRGRNFLHCAVEHNKESIVRYICrdDRFGILMNAMDNeGNTPLHLAAEY 412
Cdd:PHA02874 159 YPIHIAIKHNFFDIIKLLLEK--GAYANVKDNNGESPLHNAAEYGDYACIKLLI--DHGNHIMNKCKN-GFTPLHNAIIH 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1443089275 413 GHpRMVSLLLETMSVDVaiTNRDGLTAadlayrhlqpgLHYFLNP---RAVVKNLFYcTRAPVTLEGDHARTGIPSAME 488
Cdd:PHA02874 234 NR-SAIELLINNASIND--QDIDGSTP-----------LHHAINPpcdIDIIDILLY-HKADISIKDNKGENPIDTAFK 297
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
147-246 |
6.30e-11 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 59.36 E-value: 6.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 147 LHCAAKSGHRDVAACLLSEMLRAGgaasaalplrrATNCLGATALHEAVRNGHAGVVALLMAEApelASVANDGGVSPLY 226
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADAN-----------LQDKNGRTALHLAAKNGHLEIVKLLLEHA---DVNLKDNGRTALH 66
|
90 100
....*....|....*....|
gi 1443089275 227 LAATVGSVDIVRALLHPLPD 246
Cdd:pfam12796 67 YAARSGHLEIVKLLLEKGAD 86
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
141-353 |
4.33e-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: 4.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 141 RFLDTPLHCAAKSGhrDVAAclLSEMLRAggaaSAALPLRRATncLGATALHEAVRNGHAGVVALLMAEAPELASVANDG 220
Cdd:cd22192 15 RISESPLLLAAKEN--DVQA--IKKLLKC----PSCDLFQRGA--LGETALHVAALYDNLEAAVVLMEAAPELVNEPMTS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 221 ----GVSPLYLAATVGSVDIVRALLHPLPD-GTPSPASAAGPDGRTAL-----H----SAATTSKEIAREILDwkpegRT 286
Cdd:cd22192 85 dlyqGETALHIAVVNQNLNLVRELIARGADvVSPRATGTFFRPGPKNLiyygeHplsfAACVGNEEIVRLLIE-----HG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1443089275 287 LLTKA-DSSGRTPLHFAISSQIERF--DVFQLFLDAEP-----SLALVCDIQGSFPLHVAAVMGSVRIVVELIQK 353
Cdd:cd22192 160 ADIRAqDSLGNTVLHILVLQPNKTFacQMYDLILSYDKeddlqPLDLVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
109-218 |
1.86e-04 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 44.63 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 109 GNTALHVAATRGHAALAALVcataPALAA-----TRNRFLDTPLHCAAKSGHRDVAACLlsemLRAGGAASAalplrrAT 183
Cdd:PHA03095 222 GNTPLHSMATGSSCKRSLVL----PLLIAgisinARNRYGQTPLHYAAVFNNPRACRRL----IALGADINA------VS 287
|
90 100 110
....*....|....*....|....*....|....*
gi 1443089275 184 NClGATALHEAVRNGHAGVVALLMAEAPELASVAN 218
Cdd:PHA03095 288 SD-GNTPLSLMVRNNNGRAVRAALAKNPSAETVAA 321
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
401-423 |
6.86e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 37.57 E-value: 6.86e-04
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PGG |
pfam13962 |
Domain of unknown function; The PGG domain is named for the highly conserved sequence motif ... |
500-606 |
5.16e-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: 97.24 E-value: 5.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 500 TSTGTVASVLIATVTFAAALTVPGGYVADD-HPNAGTAASAGRFAFRAFAVSDTMAFLCSIVGTCLLVVGEAREVRPSRG 578
Cdd:pfam13962 8 RNTLLLVATLIATVTFAAGFTPPGGYWQDDdGPHAGKPILAKNPAFKAFVISNAIAFFASLVAVVLLLSIVSDFLRSLPR 87
|
90 100
....*....|....*....|....*...
gi 1443089275 579 RLRAyqgSAWALVTAGAqFMVAAFAFGL 606
Cdd:pfam13962 88 KLRI---GLKLLWVALL-SMLVAFAAGS 111
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
206-464 |
8.81e-20 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 90.40 E-value: 8.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 206 LMAEAPELASVANDGGVSPLYLAATVGSVDIVRALLHPLPDGTPSPASAAGPDGRTALHSAATTSKEIAREILDwkpEGR 285
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLL---AAG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 286 TLLTKADSSGRTPLHFAISSqiERFDVFQLFLDAEPSLALVcDIQGSFPLHVAAVMGSVRIVVELIQKCPNNynDLVDDR 365
Cdd:COG0666 78 ADINAKDDGGNTLLHAAARN--GDLEIVKLLLEAGADVNAR-DKDGETPLHLAAYNGNLEIVKLLLEAGADV--NAQDND 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 366 GRNFLHCAVEHNKESIVRYICRddrFGILMNAMDNEGNTPLHLAAEYGHPRMVSLLLETmSVDVAITNRDGLTAADLAYR 445
Cdd:COG0666 153 GNTPLHLAAANGNLEIVKLLLE---AGADVNARDNDGETPLHLAAENGHLEIVKLLLEA-GADVNAKDNDGKTALDLAAE 228
|
250
....*....|....*....
gi 1443089275 446 HLQPGLHYFLNPRAVVKNL 464
Cdd:COG0666 229 NGNLEIVKLLLEAGADLNA 247
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
188-464 |
5.19e-19 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 88.09 E-value: 5.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 188 ATALHEAVRNGHAGVVALLMAEAPELASVANDGGVSPLYLAATVGSVDIVRALLHPLPDgtpspASAAGPDGRTALHSAA 267
Cdd:COG0666 21 LALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGAD-----INAKDDGGNTLLHAAA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 268 TT-SKEIAREILDWKPEgrtlLTKADSSGRTPLHFAISSqiERFDVFQLFLDAEPSLALVcDIQGSFPLHVAAVMGSVRI 346
Cdd:COG0666 96 RNgDLEIVKLLLEAGAD----VNARDKDGETPLHLAAYN--GNLEIVKLLLEAGADVNAQ-DNDGNTPLHLAAANGNLEI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 347 VVELIQKCPNNynDLVDDRGRNFLHCAVEHNKESIVRYICRddrFGILMNAMDNEGNTPLHLAAEYGHPRMVSLLLETMS 426
Cdd:COG0666 169 VKLLLEAGADV--NARDNDGETPLHLAAENGHLEIVKLLLE---AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
|
250 260 270
....*....|....*....|....*....|....*...
gi 1443089275 427 vDVAITNRDGLTAADLAYRHLQPGLHYFLNPRAVVKNL 464
Cdd:COG0666 244 -DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAA 280
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
108-439 |
7.71e-18 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 84.62 E-value: 7.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 108 NGNTALHVAATRGHAALAALVCATAPALAATRNRFLDTPLHCAAKSGHRDVAACLLsemlraggaasAALPLRRATNCLG 187
Cdd:COG0666 19 LLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLL-----------AAGADINAKDDGG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 188 ATALHEAVRNGHAGVVALLMAEAPELASVANDGGvSPLYLAATVGSVDIVRALLhplpdgtpspasAAGPDgrtalhsaa 267
Cdd:COG0666 88 NTLLHAAARNGDLEIVKLLLEAGADVNARDKDGE-TPLHLAAYNGNLEIVKLLL------------EAGAD--------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 268 ttskeiareildwkpegrtlLTKADSSGRTPLHFAISSQieRFDVFQLFLDAEPSLALVcDIQGSFPLHVAAVMGSVRIV 347
Cdd:COG0666 146 --------------------VNAQDNDGNTPLHLAAANG--NLEIVKLLLEAGADVNAR-DNDGETPLHLAAENGHLEIV 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 348 VELIQKCPNnyNDLVDDRGRNFLHCAVEHNKESIVRYIcrdDRFGILMNAMDNEGNTPLHLAAEYGHPRMVSLLLETMSV 427
Cdd:COG0666 203 KLLLEAGAD--VNAKDNDGKTALDLAAENGNLEIVKLL---LEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLL 277
|
330
....*....|..
gi 1443089275 428 DVAITNRDGLTA 439
Cdd:COG0666 278 LAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
76-325 |
1.56e-16 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 80.77 E-value: 1.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 76 GHSLSQVAIRVDDDDDGRAPAGASRLLGVTTGNGNTALHVAATRGHAALAALVCAtAPALAATRNRFLDTPLHCAAKSGH 155
Cdd:COG0666 54 GALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLE-AGADVNARDKDGETPLHLAAYNGN 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 156 RDVAACLLsemlrAGGAASAalplrrATNCLGATALHEAVRNGHAGVVALLMaEAPELASVANDGGVSPLYLAATVGSVD 235
Cdd:COG0666 133 LEIVKLLL-----EAGADVN------AQDNDGNTPLHLAAANGNLEIVKLLL-EAGADVNARDNDGETPLHLAAENGHLE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 236 IVRALLhplpdgtpspasAAGPD-------GRTALHSAAttsKEIAREILDWKPEGRTLLTKADSSGRTPLHFAISSQIE 308
Cdd:COG0666 201 IVKLLL------------EAGADvnakdndGKTALDLAA---ENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAA 265
|
250
....*....|....*..
gi 1443089275 309 RFDVFQLFLDAEPSLAL 325
Cdd:COG0666 266 LIVKLLLLALLLLAAAL 282
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
335-423 |
4.25e-13 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 65.52 E-value: 4.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 335 LHVAAVMGSVRIVVELIQKCPNNynDLVDDRGRNFLHCAVEHNKESIVRYICRDDRFGilmnaMDNEGNTPLHLAAEYGH 414
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADA--NLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN-----LKDNGRTALHYAARSGH 73
|
....*....
gi 1443089275 415 PRMVSLLLE 423
Cdd:pfam12796 74 LEIVKLLLE 82
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
179-488 |
3.27e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 69.22 E-value: 3.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 179 LRRATNCLG------ATALHEAVRNGHAGVVALLMAEAPELASVaNDGGVSPLYLAATVGSVDIVRALLHPLPDGTPSPA 252
Cdd:PHA02874 21 IKNKGNCINisvdetTTPLIDAIRSGDAKIVELFIKHGADINHI-NTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSILPI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 253 saagPDgrtalhsaatTSKEIAREILDwkpEGRTLLTKaDSSGRTPLHFAISSQieRFDVFQLFLDAEPSLAlVCDIQGS 332
Cdd:PHA02874 100 ----PC----------IEKDMIKTILD---CGIDVNIK-DAELKTFLHYAIKKG--DLESIKMLFEYGADVN-IEDDNGC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 333 FPLHVAAVMGSVRIVVELIQKcpNNYNDLVDDRGRNFLHCAVEHNKESIVRYICrdDRFGILMNAMDNeGNTPLHLAAEY 412
Cdd:PHA02874 159 YPIHIAIKHNFFDIIKLLLEK--GAYANVKDNNGESPLHNAAEYGDYACIKLLI--DHGNHIMNKCKN-GFTPLHNAIIH 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1443089275 413 GHpRMVSLLLETMSVDVaiTNRDGLTAadlayrhlqpgLHYFLNP---RAVVKNLFYcTRAPVTLEGDHARTGIPSAME 488
Cdd:PHA02874 234 NR-SAIELLINNASIND--QDIDGSTP-----------LHHAINPpcdIDIIDILLY-HKADISIKDNKGENPIDTAFK 297
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
147-246 |
6.30e-11 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 59.36 E-value: 6.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 147 LHCAAKSGHRDVAACLLSEMLRAGgaasaalplrrATNCLGATALHEAVRNGHAGVVALLMAEApelASVANDGGVSPLY 226
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADAN-----------LQDKNGRTALHLAAKNGHLEIVKLLLEHA---DVNLKDNGRTALH 66
|
90 100
....*....|....*....|
gi 1443089275 227 LAATVGSVDIVRALLHPLPD 246
Cdd:pfam12796 67 YAARSGHLEIVKLLLEKGAD 86
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
141-353 |
4.33e-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: 4.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 141 RFLDTPLHCAAKSGhrDVAAclLSEMLRAggaaSAALPLRRATncLGATALHEAVRNGHAGVVALLMAEAPELASVANDG 220
Cdd:cd22192 15 RISESPLLLAAKEN--DVQA--IKKLLKC----PSCDLFQRGA--LGETALHVAALYDNLEAAVVLMEAAPELVNEPMTS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 221 ----GVSPLYLAATVGSVDIVRALLHPLPD-GTPSPASAAGPDGRTAL-----H----SAATTSKEIAREILDwkpegRT 286
Cdd:cd22192 85 dlyqGETALHIAVVNQNLNLVRELIARGADvVSPRATGTFFRPGPKNLiyygeHplsfAACVGNEEIVRLLIE-----HG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1443089275 287 LLTKA-DSSGRTPLHFAISSQIERF--DVFQLFLDAEP-----SLALVCDIQGSFPLHVAAVMGSVRIVVELIQK 353
Cdd:cd22192 160 ADIRAqDSLGNTVLHILVLQPNKTFacQMYDLILSYDKeddlqPLDLVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
370-443 |
6.11e-09 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 53.58 E-value: 6.11e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1443089275 370 LHCAVEHNKESIVRYICRddrFGILMNAMDNEGNTPLHLAAEYGHPRMVSLLLETMSVDVaitNRDGLTAADLA 443
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLE---NGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL---KDNGRTALHYA 68
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
113-213 |
6.74e-08 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 50.50 E-value: 6.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 113 LHVAATRGHAALA-ALVcaTAPALAATRNRFLDTPLHCAAKSGHRDVAACLLSEMlraggaasaalplRRATNCLGATAL 191
Cdd:pfam12796 1 LHLAAKNGNLELVkLLL--ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-------------DVNLKDNGRTAL 65
|
90 100
....*....|....*....|..
gi 1443089275 192 HEAVRNGHAGVVALLMAEAPEL 213
Cdd:pfam12796 66 HYAARSGHLEIVKLLLEKGADI 87
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
225-318 |
7.43e-08 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 50.50 E-value: 7.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 225 LYLAATVGSVDIVRALLHPLPDgtpspASAAGPDGRTALHSAATT-SKEIAREILDwkpegrTLLTKADSSGRTPLHFAI 303
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGAD-----ANLQDKNGRTALHLAAKNgHLEIVKLLLE------HADVNLKDNGRTALHYAA 69
|
90
....*....|....*
gi 1443089275 304 SSQieRFDVFQLFLD 318
Cdd:pfam12796 70 RSG--HLEIVKLLLE 82
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
200-446 |
8.20e-08 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 55.42 E-value: 8.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 200 AGVVALLMAEApelASVANDG--GVSPL--YLAATVG-SVDIVRALLhplpdgtpspasAAGPD-------GRTALHSAA 267
Cdd:PHA03095 27 VEEVRRLLAAG---ADVNFRGeyGKTPLhlYLHYSSEkVKDIVRLLL------------EAGADvnapercGFTPLHLYL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 268 TTSKEIarEILDwkpegrtLLTKA-------DSSGRTPLHFAISSQIERFDVFQLFLDAEPSLAlVCDIQGSFPLHVaaV 340
Cdd:PHA03095 92 YNATTL--DVIK-------LLIKAgadvnakDKVGRTPLHVYLSGFNINPKVIRLLLRKGADVN-ALDLYGMTPLAV--L 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 341 MGSVRIVVE----LIQKCPNNYNdlVDDRGRNFLH--CAVEHNKESIVRYICR-------DDRF---------------- 391
Cdd:PHA03095 160 LKSRNANVEllrlLIDAGADVYA--VDDRFRSLLHhhLQSFKPRARIVRELIRagcdpaaTDMLgntplhsmatgssckr 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1443089275 392 ---------GILMNAMDNEGNTPLHLAAEYGHPRMVSLLLEtMSVDVAITNRDGLTAADLAYRH 446
Cdd:PHA03095 238 slvlplliaGISINARNRYGQTPLHYAAVFNNPRACRRLIA-LGADINAVSSDGNTPLSLMVRN 300
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
326-438 |
1.66e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 54.29 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 326 VCDIQGSFPLHVAAV--MGSVRIVVELIQkcpNNYN-DLVDDRGRNFLHCAVE--HNKESIVRY----------ICRDDR 390
Cdd:PHA03100 101 APDNNGITPLLYAISkkSNSYSIVEYLLD---NGANvNIKNSDGENLLHLYLEsnKIDLKILKLlidkgvdinaKNRVNY 177
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1443089275 391 F---GILMNAMDNEGNTPLHLAAEYGHPRMVSLLLEtMSVDVAITNRDGLT 438
Cdd:PHA03100 178 LlsyGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLD-LGANPNLVNKYGDT 227
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
299-386 |
2.72e-07 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 48.96 E-value: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 299 LHFAISSqiERFDVFQLFLDAEPSlALVCDIQGSFPLHVAAVMGSVRIVVELIQKCPNNyndlVDDRGRNFLHCAVEHNK 378
Cdd:pfam12796 1 LHLAAKN--GNLELVKLLLENGAD-ANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN----LKDNGRTALHYAARSGH 73
|
....*...
gi 1443089275 379 ESIVRYIC 386
Cdd:pfam12796 74 LEIVKLLL 81
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
142-424 |
3.21e-07 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 53.49 E-value: 3.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 142 FLDTPLHCAAKSGHRDVAACLLSeMLRAGGAASAAlplrraTNClGATALHEAVRNGH-AGVVALLMAEAPELaSVANDG 220
Cdd:PHA03095 46 YGKTPLHLYLHYSSEKVKDIVRL-LLEAGADVNAP------ERC-GFTPLHLYLYNATtLDVIKLLIKAGADV-NAKDKV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 221 GVSPLYLAATVGSVD--IVRALLHPLPDgtpspASAAGPDGRTALHsAATTSKEIAREILdwkpegRTLLTK------AD 292
Cdd:PHA03095 117 GRTPLHVYLSGFNINpkVIRLLLRKGAD-----VNALDLYGMTPLA-VLLKSRNANVELL------RLLIDAgadvyaVD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 293 SSGRTPLH-FAISSQiERFDVFQLFLDAEPSLALVcDIQGSFPLHVAAVMGSVR--IVVELIQKcpNNYNDLVDDRGRNF 369
Cdd:PHA03095 185 DRFRSLLHhHLQSFK-PRARIVRELIRAGCDPAAT-DMLGNTPLHSMATGSSCKrsLVLPLLIA--GISINARNRYGQTP 260
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1443089275 370 LHCAVEHNKESIVRYICRddrFGILMNAMDNEGNTPLHLAAEYGHPRMVSLLLET 424
Cdd:PHA03095 261 LHYAAVFNNPRACRRLIA---LGADINAVSSDGNTPLSLMVRNNNGRAVRAALAK 312
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
389-443 |
3.39e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 47.34 E-value: 3.39e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1443089275 389 DRFGILMNAMDNEGNTPLHLAAEYGHPRMVSLLLEtMSVDVAITNRDGLTAADLA 443
Cdd:pfam13857 3 EHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLA-YGVDLNLKDEEGLTALDLA 56
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
222-423 |
3.65e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 53.13 E-value: 3.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 222 VSPLYLAATVGSVDIVRALLHplpDGTPSPASAAgpDGRTALHSAA------TTSKEIAREILdwkpEGRTLLTKADSSG 295
Cdd:PHA03100 36 VLPLYLAKEARNIDVVKILLD---NGADINSSTK--NNSTPLHYLSnikynlTDVKEIVKLLL----EYGANVNAPDNNG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 296 RTPLHFAISSQIERFDVFQLFLDAEPSLALVCDIQGSfPLHVAAVMGSVRI-VVELIQKcpNNYN--------------- 359
Cdd:PHA03100 107 ITPLLYAISKKSNSYSIVEYLLDNGANVNIKNSDGEN-LLHLYLESNKIDLkILKLLID--KGVDinaknrvnyllsygv 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1443089275 360 --DLVDDRGRNFLHCAVEHNKESIVRYICRddrFGILMNAMDNEGNTPLHLAAEYGHPRMVSLLLE 423
Cdd:PHA03100 184 piNIKDVYGFTPLHYAVYNNNPEFVKYLLD---LGANPNLVNKYGDTPLHIAILNNNKEIFKLLLN 246
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
103-164 |
8.78e-07 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 47.42 E-value: 8.78e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1443089275 103 GVTTGNGNTALHVAATRGHAALAALVCATAPALAATRNRfldTPLHCAAKSGHRDVAACLLS 164
Cdd:pfam12796 24 NLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR---TALHYAARSGHLEIVKLLLE 82
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
366-422 |
2.10e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 45.34 E-value: 2.10e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1443089275 366 GRNFLHCAVEHNKESIVRYiCRDdrFGILMNAMDNEGNTPLHLAAEYGHPRMVSLLL 422
Cdd:pfam13637 1 ELTALHAAAASGHLELLRL-LLE--KGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
259-423 |
1.31e-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: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 259 GRTALHSA----ATTSKEIAREILDWKPEGRTL-------LTKADSSGRTPLHFAIssqiER--FDVFQLFLDA------ 319
Cdd:cd22194 94 GKTCLMKAllniNENTKEIVRILLAFAEENGILdrfinaeYTEEAYEGQTALNIAI----ERrqGDIVKLLIAKgadvna 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 320 -------EPSLALVCDIQGSFPLHVAAVMGSVRIVVELIQKCPNNYNdLVDDRGRNFLHCAV------EHNKESIVRY-- 384
Cdd:cd22194 170 hakgvffNPKYKHEGFYFGETPLALAACTNQPEIVQLLMEKESTDIT-SQDSRGNTVLHALVtvaedsKTQNDFVKRMyd 248
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1443089275 385 -ICRDDRFGILMNAMDNEGNTPLHLAAEYGHPRMVSLLLE 423
Cdd:cd22194 249 mILLKSENKNLETIRNNEGLTPLQLAAKMGKAEILKYILS 288
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
297-443 |
2.62e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 47.75 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 297 TPLHFAIssQIERFDVFQLFLDAEPSLALVCDIQGSFPLHVAAVMGSVR-IVVELIQKCP------------NNY----- 358
Cdd:PHA02876 43 TAIHQAL--QLRQIDIVEEIIQQNPELIYITDHKCHSTLHTICIIPNVMdIVISLTLDCDiildikyasiilNKHkldea 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 359 -----------NDLVDDRgrnfLHCAVEHNKeSIVRYICRDD--------RFGILMNAMDNEGNTPLHLAAEYGHPRMVS 419
Cdd:PHA02876 121 cihilkeaisgNDIHYDK----INESIEYMK-LIKERIQQDElliaemllEGGADVNAKDIYCITPIHYAAERGNAKMVN 195
|
170 180
....*....|....*....|....
gi 1443089275 420 LLLeTMSVDVAITNRDGLTAADLA 443
Cdd:PHA02876 196 LLL-SYGADVNIIALDDLSVLECA 218
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
396-490 |
3.28e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 47.20 E-value: 3.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 396 NAMDNEGNTPLHLAAEYGHPRMVSLLLEtMSVDVAITNRDGLTAADLAYRHlqpglhyflNPRAVVKNLFYCTRAPVTLE 475
Cdd:PTZ00322 109 NCRDYDGRTPLHIACANGHVQVVRVLLE-FGADPTLLDKDGKTPLELAEEN---------GFREVVQLLSRHSQCHFELG 178
|
90
....*....|....*...
gi 1443089275 476 GDHAR---TGIPSAMEDA 490
Cdd:PTZ00322 179 ANAKPdsfTGKPPSLEDS 196
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
104-220 |
4.80e-05 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 45.72 E-value: 4.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 104 VTTGNGNTALHVAATRGHAALAALVCAtAPALAATRNRFLDTPLHCAAKSGHRDVAACLLsemlraggaasAALPLRRAT 183
Cdd:COG0666 181 ARDNDGETPLHLAAENGHLEIVKLLLE-AGADVNAKDNDGKTALDLAAENGNLEIVKLLL-----------EAGADLNAK 248
|
90 100 110
....*....|....*....|....*....|....*..
gi 1443089275 184 NCLGATALHEAVRNGHAGVVALLMAEAPELASVANDG 220
Cdd:COG0666 249 DKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
223-443 |
1.55e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 45.00 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 223 SPLYLAATVGSVDIVRALLhplpdGTPS-PASAAGPDGRTALHSAATTSK-EIAREILDWKPEgrtLLTKADSSgrtplh 300
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLL-----KCPScDLFQRGALGETALHVAALYDNlEAAVVLMEAAPE---LVNEPMTS------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 301 faissqierfdvfQLFldaepslalvcdiQGSFPLHVAAVMGSVRIVVELIQKCPnnynDLVDDR--------------- 365
Cdd:cd22192 85 -------------DLY-------------QGETALHIAVVNQNLNLVRELIARGA----DVVSPRatgtffrpgpknliy 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 366 -GRNFLHCAVEHNKESIVRYICRDdrfGILMNAMDNEGNTPLH---------LAAEyghprMVSLLL------ETMSVDV 429
Cdd:cd22192 135 yGEHPLSFAACVGNEEIVRLLIEH---GADIRAQDSLGNTVLHilvlqpnktFACQ-----MYDLILsydkedDLQPLDL 206
|
250
....*....|....
gi 1443089275 430 aITNRDGLTAADLA 443
Cdd:cd22192 207 -VPNNQGLTPFKLA 219
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
109-163 |
1.86e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 39.57 E-value: 1.86e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1443089275 109 GNTALHVAATRGH-AALAALVCATAPALAatRNRFLDTPLHCAAKSGHRDVAACLL 163
Cdd:pfam13637 1 ELTALHAAAASGHlELLRLLLEKGADINA--VDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
109-218 |
1.86e-04 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 44.63 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 109 GNTALHVAATRGHAALAALVcataPALAA-----TRNRFLDTPLHCAAKSGHRDVAACLlsemLRAGGAASAalplrrAT 183
Cdd:PHA03095 222 GNTPLHSMATGSSCKRSLVL----PLLIAgisinARNRYGQTPLHYAAVFNNPRACRRL----IALGADINA------VS 287
|
90 100 110
....*....|....*....|....*....|....*
gi 1443089275 184 NClGATALHEAVRNGHAGVVALLMAEAPELASVAN 218
Cdd:PHA03095 288 SD-GNTPLSLMVRNNNGRAVRAALAKNPSAETVAA 321
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
145-353 |
3.18e-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: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 145 TPLHCAAKSGHRDVAACLLSeMLRAGGAASAALPLRRATnCL-----GATALHEAVRNGHAGVVALLMAEAPELASVAND 219
Cdd:cd21882 28 TCLHKAALNLNDGVNEAIML-LLEAAPDSGNPKELVNAP-CTdefyqGQTALHIAIENRNLNLVRLLVENGADVSARATG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 220 G------------GVSPLYLAATVGSVDIVRALL-HPlpdgtPSPASAAGPD--GRTALHsaattskeIAREILDWKPEG 284
Cdd:cd21882 106 RffrkspgnlfyfGELPLSLAACTNQEEIVRLLLeNG-----AQPAALEAQDslGNTVLH--------ALVLQADNTPEN 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1443089275 285 RTLLTKadssgrtpLHFAISSQIERFDVFQlfldaepSLALVCDIQGSFPLHVAAVMGSVRIVVELIQK 353
Cdd:cd21882 173 SAFVCQ--------MYNLLLSYGAHLDPTQ-------QLEEIPNHQGLTPLKLAAVEGKIVMFQHILQR 226
|
|
| PHA02741 |
PHA02741 |
hypothetical protein; Provisional |
287-434 |
6.57e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 165108 [Multi-domain] Cd Length: 169 Bit Score: 41.18 E-value: 6.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 287 LLTKADSSGRTPLHFAISSQ----IERFDVFqLFLDAEPSLALVCDIQGSFPLHVAAVMGSVRIVVELIQKCPN-----N 357
Cdd:PHA02741 13 MIAEKNSEGENFFHEAARCGcfdiIARFTPF-IRGDCHAAALNATDDAGQMCIHIAAEKHEAQLAAEIIDHLIElgadiN 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1443089275 358 YNDLVDdrGRNFLHCAVEHNKESIVRYICRDDRFGILMNAMDNEgnTPLHLAAEYGHPRMVSLLLETMSVDVAITNR 434
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 ... |
401-423 |
6.86e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 37.57 E-value: 6.86e-04
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
401-434 |
7.23e-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: 7.23e-04
10 20 30
....*....|....*....|....*....|....*
gi 1443089275 401 EGNTPLHLAA-EYGHPRMVSLLLEtMSVDVAITNR 434
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLS-KGADVNARDK 34
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
401-431 |
9.13e-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: 37.24 E-value: 9.13e-04
10 20 30
....*....|....*....|....*....|.
gi 1443089275 401 EGNTPLHLAAEYGHPRMVSLLLEtMSVDVAI 431
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLE-NGADINA 30
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
191-433 |
9.80e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 42.29 E-value: 9.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 191 LHEAVRNGHAGVVALLMAEAPELASVANDGGVSPLYLAATVGSVDIVRALLhplpdgtpspASAAGPDgrtalhsAATTS 270
Cdd:PHA02875 72 LHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLI----------ARGADPD-------IPNTD 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 271 KEiareildwkpegrtlltkadssgrTPLHFAISSQieRFDVFQLFLDAEPSLALVcDIQGSFPLHVAAVMGSVRIVVEL 350
Cdd:PHA02875 135 KF------------------------SPLHLAVMMG--DIKGIELLIDHKACLDIE-DCCGCTPLIIAMAKGDIAICKML 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 351 IQKCPNnyNDLVDDRGRNFLHC-AVEHNKESIVRYICRDDRFGILMNAMDNEGNTPLHLAAEYghprmvSLLLETMSVDV 429
Cdd:PHA02875 188 LDSGAN--IDYFGKNGCVAALCyAIENNKIDIVRLFIKRGADCNIMFMIEGEECTILDMICNM------CTNLESEAIDA 259
|
....
gi 1443089275 430 AITN 433
Cdd:PHA02875 260 LIAD 263
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
402-455 |
1.37e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 37.25 E-value: 1.37e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1443089275 402 GNTPLHLAAEYGHPRMVSLLLETmSVDVAITNRDGLTAADLAYRHLQPG-LHYFL 455
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEK-GADINAVDGNGETALHFAASNGNVEvLKLLL 54
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
330-445 |
1.44e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 41.79 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 330 QGSFPLHVAAVMGSVRIVVELIQKC--PNnyndlVDDRGRNF-LHCAVEHNKESIVRYICRDdrfGILMNAMDNEGNTPL 406
Cdd:PHA02878 167 KGNTALHYATENKDQRLTELLLSYGanVN-----IPDKTNNSpLHHAVKHYNKPIVHILLEN---GASTDARDKCGNTPL 238
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1443089275 407 HLAAEY-GHPRMVSLLLET-MSVDVAITNRdGLTAADLAYR 445
Cdd:PHA02878 239 HISVGYcKDYDILKLLLEHgVDVNAKSYIL-GLTALHSSIK 278
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
187-320 |
1.56e-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: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 187 GATALHEAVRNGHAGVVALLMAEAPELASVA----------NDG---GVSPLYLAATVGSVDIVRALLhplpDGTPSPAS 253
Cdd:cd22194 141 GQTALNIAIERRQGDIVKLLIAKGADVNAHAkgvffnpkykHEGfyfGETPLALAACTNQPEIVQLLM----EKESTDIT 216
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1443089275 254 AAGPDGRTALHSAATTS----------KEIAREILDwKPEGRTLLTKADSSGRTPLHFAisSQIERFDVFQLFLDAE 320
Cdd:cd22194 217 SQDSRGNTVLHALVTVAedsktqndfvKRMYDMILL-KSENKNLETIRNNEGLTPLQLA--AKMGKAEILKYILSRE 290
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
292-353 |
1.97e-03 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 37.79 E-value: 1.97e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1443089275 292 DSSGRTPLHFAISSQieRFDVFQLFLDaepSLALVCDIQGSFPLHVAAVMGSVRIVVELIQK 353
Cdd:pfam12796 27 DKNGRTALHLAAKNG--HLEIVKLLLE---HADVNLKDNGRTALHYAARSGHLEIVKLLLEK 83
|
|
| PHA02741 |
PHA02741 |
hypothetical protein; Provisional |
335-443 |
2.33e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 165108 [Multi-domain] Cd Length: 169 Bit Score: 39.64 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 335 LHVAAVMGSVRIVVELIQKCPNNYN----DLVDDRGRNFLH-CAVEHNKESIVRYICRDDRFGILMNAMDN-EGNTPLHL 408
Cdd:PHA02741 25 FHEAARCGCFDIIARFTPFIRGDCHaaalNATDDAGQMCIHiAAEKHEAQLAAEIIDHLIELGADINAQEMlEGDTALHL 104
|
90 100 110
....*....|....*....|....*....|....*
gi 1443089275 409 AAEYGHPRMVSLLLETMSVDVAITNRDGLTAADLA 443
Cdd:PHA02741 105 AAHRRDHDLAEWLCCQPGIDLHFCNADNKSPFELA 139
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
334-384 |
9.36e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 34.94 E-value: 9.36e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1443089275 334 PLHVAAVMGSVRIVVELIQKcPNNYNDlVDDRGRNFLHCAVEHNKESIVRY 384
Cdd:pfam13637 4 ALHAAAASGHLELLRLLLEK-GADINA-VDGNGETALHFAASNGNVEVLKL 52
|
|
|