|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
72-371 |
5.27e-38 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 144.33 E-value: 5.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 72 LQNFNKQKKLKRCDDMDTFFLHYAAAEGQIELMEKITRDSSLEVLHEMDDYGNTPLHCAVEKNQIESVKFLLSRGANPNL 151
Cdd:COG0666 3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 152 RNFNMMAPLHIAVQGMNNEVMKVLLEHRtIDVNLEGENGNTAVIIACTTNNSEALQILLKKGAKPCKSNKWGCFPIHQAA 231
Cdd:COG0666 83 KDDGGNTLLHAAARNGDLEIVKLLLEAG-ADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 232 FSGSKECMEIILrfgeEHGysrqLHINFMNNGKATPLHLAVQNGDLEMIKMCLDNGAQIDPVEKGRCTAIHFAATQGATE 311
Cdd:COG0666 162 ANGNLEIVKLLL----EAG----ADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLE 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 312 IVKLMISSYsgsvDIVNTTDGCHETMLHRASLFDHHELADYLISVGADINKIDSEGRSPL 371
Cdd:COG0666 234 IVKLLLEAG----ADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
254-544 |
5.65e-34 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 132.77 E-value: 5.65e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 254 QLHINFMNNGKATPLHLAVQNGDLEMIKMCLDNGAQIDPVEKGRCTAIHFAATQGATEIVKLMISSYsgsvDIVNTTDGC 333
Cdd:COG0666 44 LLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAG----ADVNARDKD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 334 HETMLHRASLFDHHELADYLISVGADINKIDSEGRSPLILATASASWNIVNLLLSKGAQVDIKDNFGRnflhltvqqpyg 413
Cdd:COG0666 120 GETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGE------------ 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 414 lknlrpefmqmqqikelvmdedndgcTPLHYACRQGGPGSVNNLLGFNVSIHSKSKDKKSPLHFAASYGRINTCQRLLQD 493
Cdd:COG0666 188 --------------------------TPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 767952011 494 ISDtrlLNEGDLHGMTPLHLAAKNGHDKVVQLLLKKGALFLSDHNGWTALH 544
Cdd:COG0666 242 GAD---LNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
255-606 |
1.50e-33 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 131.23 E-value: 1.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 255 LHINFMNNGKATPLHLAVQNGDLEMIKMCLDNGAQIDPVEKGRCTAIHFAATQGATEIVKLMISSysgsVDIVNTTDGCH 334
Cdd:COG0666 12 LAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAA----GADINAKDDGG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 335 ETMLHRASLFDHHELADYLISVGADINKIDSEGRSPLILATASASWNIVNLLLSKGAQVDIKDNFGRnflhltvqqpygl 414
Cdd:COG0666 88 NTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGN------------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 415 knlrpefmqmqqikelvmdedndgctplhyacrqggpgsvnnllgfnvsihskskdkkSPLHFAASYGRINTCQRLLQ-- 492
Cdd:COG0666 155 ----------------------------------------------------------TPLHLAAANGNLEIVKLLLEag 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 493 -DIsdtrllNEGDLHGMTPLHLAAKNGHDKVVQLLLKKGA-LFLSDHNGWTALHHASMGGYTQTMKVILDTNLKCTDRlD 570
Cdd:COG0666 177 aDV------NARDNDGETPLHLAAENGHLEIVKLLLEAGAdVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAK-D 249
|
330 340 350
....*....|....*....|....*....|....*.
gi 767952011 571 EDGNTALHFAAREGHAKAVALLLSHNADIVLNKQQA 606
Cdd:COG0666 250 KDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
347-640 |
3.88e-33 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 130.07 E-value: 3.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 347 HELADYLISVGADINKIDSEGRSPLILATASASWNIVNLLLSKGAQVDIKDNFGRNFLHLTVqqpygLKNLRPEFMQMQQ 426
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAA-----LAGDLLVALLLLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 427 IKELVMDEDNDGCTPLHYACRQGGPGSVNNLLGFNVSIHSKSKDKKSPLHFAASYGRINTCQRLLQ---DIsdtrllNEG 503
Cdd:COG0666 76 AGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEagaDV------NAQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 504 DLHGMTPLHLAAKNGHDKVVQLLLKKGA-LFLSDHNGWTALHHASMGGYTQTMKVILDTNLKCTDRlDEDGNTALHFAAR 582
Cdd:COG0666 150 DNDGNTPLHLAAANGNLEIVKLLLEAGAdVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAK-DNDGKTALDLAAE 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 767952011 583 EGHAKAVALLLSHNADIVL-NKQQASFLHLALHNKRKEVVLTIIRSKRWDECLKIFSHN 640
Cdd:COG0666 229 NGNLEIVKLLLEAGADLNAkDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
511-602 |
1.04e-20 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 87.86 E-value: 1.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 511 LHLAAKNGHDKVVQLLLKKGA-LFLSDHNGWTALHHASMGGYTQTMKVILDTNLKctdRLDEDGNTALHFAAREGHAKAV 589
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGAdANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV---NLKDNGRTALHYAARSGHLEIV 77
|
90
....*....|...
gi 767952011 590 ALLLSHNADIVLN 602
Cdd:pfam12796 78 KLLLEKGADINVK 90
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
105-399 |
1.99e-20 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 95.50 E-value: 1.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 105 EKITRDSSLEVLHEMDDYGN-------TPLHCAVEKNQIESVKFLLSRGANPNLRNFNMMAPLHIAVQGMNNEvmkvlle 177
Cdd:PHA03100 10 SRIIKVKNIKYIIMEDDLNDysykkpvLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNL------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 178 hrtidvnlegengntaviiactTNNSEALQILLKKGAKPCKSNKWGCFPIHQAAfSGSKECMEIIlrfgeEHGYSRQLHI 257
Cdd:PHA03100 83 ----------------------TDVKEIVKLLLEYGANVNAPDNNGITPLLYAI-SKKSNSYSIV-----EYLLDNGANV 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 258 NFMNNGKATPLHLAVQNG--DLEMIKMCLDNGAQIDpvekgrctaihfaatqgATEIVKLMISSysgSVDIvNTTDGCHE 335
Cdd:PHA03100 135 NIKNSDGENLLHLYLESNkiDLKILKLLIDKGVDIN-----------------AKNRVNYLLSY---GVPI-NIKDVYGF 193
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767952011 336 TMLHRASLFDHHELADYLISVGADINKIDSEGRSPLILATASASWNIVNLLLSKGAQVDIKDNF 399
Cdd:PHA03100 194 TPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
120-389 |
8.10e-19 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 90.85 E-value: 8.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 120 DDYGNTPLH----CAVEKNQiESVKFLLSRGANPNLRNFNMMAPLHIAVQGMNNE-VMKVLLEHRTiDVNLEGENGNTAV 194
Cdd:PHA03095 44 GEYGKTPLHlylhYSSEKVK-DIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAGA-DVNAKDKVGRTPL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 195 IIACTTNNSEA--LQILLKKGAKPCKSNKWGCFPIHqaAFSGSKECMEIILRFGEEHGYSRQLHINFMNngkaTPLHLAV 272
Cdd:PHA03095 122 HVYLSGFNINPkvIRLLLRKGADVNALDLYGMTPLA--VLLKSRNANVELLRLLIDAGADVYAVDDRFR----SLLHHHL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 273 QN--GDLEMIKMCLDNGAQIDPVEKGRCTAIHFAATQG---ATEIVKLMISSYSgsvdiVNTTDGCHETMLHRASLFDHH 347
Cdd:PHA03095 196 QSfkPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSsckRSLVLPLLIAGIS-----INARNRYGQTPLHYAAVFNNP 270
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 767952011 348 ELADYLISVGADINKIDSEGRSPLILATASASWNIVNLLLSK 389
Cdd:PHA03095 271 RACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAK 312
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
258-532 |
2.97e-18 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 88.87 E-value: 2.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 258 NFMN---NGKATPLHLAVQNGDLEMIKMCLDNGAQIDPVEKGRCTAIHFAATQGATEIVKLMISSysgSVDI-------- 326
Cdd:PHA02874 26 NCINisvDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDN---GVDTsilpipci 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 327 --------------VNTTDGCHETMLHRASLFDHHELADYLISVGADINKIDSEGRSPLILATASASWNIVNLLLSKGAQ 392
Cdd:PHA02874 103 ekdmiktildcgidVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 393 VDIKDNFGRNFLHLTVQqpYGlknlrpefmQMQQIKEL------VMDEDNDGCTPLHYACRQGgpGSVNNLLGFNVSIHS 466
Cdd:PHA02874 183 ANVKDNNGESPLHNAAE--YG---------DYACIKLLidhgnhIMNKCKNGFTPLHNAIIHN--RSAIELLINNASIND 249
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767952011 467 KSKDKKSPLHFAASYgrinTCQRllqDISDTRLLNEGDL-----HGMTPLHLAAKN-GHDKVVQLLLKKGAL 532
Cdd:PHA02874 250 QDIDGSTPLHHAINP----PCDI---DIIDILLYHKADIsikdnKGENPIDTAFKYiNKDPVIKDIIANAVL 314
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
442-531 |
7.80e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 79.39 E-value: 7.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 442 LHYACRQGGPGSVNNLLGFNVSIHSKSKDKKSPLHFAASYGRINTCQRLLQDISdtrllNEGDLHGMTPLHLAAKNGHDK 521
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD-----VNLKDNGRTALHYAARSGHLE 75
|
90
....*....|
gi 767952011 522 VVQLLLKKGA 531
Cdd:pfam12796 76 IVKLLLEKGA 85
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
327-601 |
1.13e-17 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 87.39 E-value: 1.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 327 VNTTDGCHETMLHRASLFDHHELAD---YLISVGADINKIDSEGRSPLIL-ATASASWNIVNLLLSKGAQVDIKDNFGRN 402
Cdd:PHA03095 40 VNFRGEYGKTPLHLYLHYSSEKVKDivrLLLEAGADVNAPERCGFTPLHLyLYNATTLDVIKLLIKAGADVNAKDKVGRT 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 403 FLH--LTVqqpyglKNLRPEFmqmqqIKEL------VMDEDNDGCTPLHYACRQGG--PGSVNNLLGFNVSIHSKSKDKK 472
Cdd:PHA03095 120 PLHvyLSG------FNINPKV-----IRLLlrkgadVNALDLYGMTPLAVLLKSRNanVELLRLLIDAGADVYAVDDRFR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 473 SPLHFAASYGRINTC--QRLLQDISDTRLLNegdLHGMTPLHLAAKNGHDK---VVQLLLKKGALFLSDHNGWTALHHAS 547
Cdd:PHA03095 189 SLLHHHLQSFKPRARivRELIRAGCDPAATD---MLGNTPLHSMATGSSCKrslVLPLLIAGISINARNRYGQTPLHYAA 265
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 767952011 548 mgGYTQTM---KVI-LDTNLKCTdrlDEDGNTALHFAAREGHAKAVALLLSHNADIVL 601
Cdd:PHA03095 266 --VFNNPRacrRLIaLGADINAV---SSDGNTPLSLMVRNNNGRAVRAALAKNPSAET 318
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
99-374 |
2.00e-17 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 86.17 E-value: 2.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 99 GQIELMEKITRDSSlEVLHEMDDYGNTPLHCAVEKNQIESVKFLLSRGANPNLRNFNMMAPLHIAVQGMNNEVMKVLLEH 178
Cdd:PHA02874 12 GDIEAIEKIIKNKG-NCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 179 RT----------------------IDVNLEGENGNTAVIIACTTNNSEALQILLKKGAKPCKSNKWGCFPIHQAAFSGSK 236
Cdd:PHA02874 91 GVdtsilpipciekdmiktildcgIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFF 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 237 ECMEIILRFGEehgysrqlHINFMNNGKATPLHLAVQNGDLEMIKMCLDNGAQIDPVEKGRCTAIHFAATQGATeIVKLM 316
Cdd:PHA02874 171 DIIKLLLEKGA--------YANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRS-AIELL 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 767952011 317 ISSYSgsvdiVNTTDGCHETMLHRASLFD-HHELADYLISVGADINKIDSEGRSPLILA 374
Cdd:PHA02874 242 INNAS-----INDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTA 295
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
92-502 |
3.57e-17 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 86.66 E-value: 3.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 92 LHYAAAEGQIELM----EKITRDSSL--EVLHE-------MDDYGNTPLHCAVEKNQIESVKFLLSRGANPNLRNFNMMA 158
Cdd:PHA02876 134 IHYDKINESIEYMklikERIQQDELLiaEMLLEggadvnaKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLS 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 159 PLHIAVQGMNNEVMKVLLEHRTidvNLegeNGNTAVIIACTTNNSEALQILLkkgakpcksnkwgcfpiHQAAFSgskec 238
Cdd:PHA02876 214 VLECAVDSKNIDTIKAIIDNRS---NI---NKNDLSLLKAIRNEDLETSLLL-----------------YDAGFS----- 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 239 meiilrfgeehgysrqlhINFMNNGKATPLHLAVQNGDL-EMIKMCLDNGAQIDPVEKGRCTAIHFAATQG-ATEIVKLM 316
Cdd:PHA02876 266 ------------------VNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTL 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 317 ISSYSGsvdiVNTTDGCHETMLHRASLFDHH-ELADYLISVGADINKIDSEGRSPLILATASASWNIVNLLLSKGAQVDI 395
Cdd:PHA02876 328 IMLGAD----VNAADRLYITPLHQASTLDRNkDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEA 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 396 KDNFGRNFLHltvqqpYGLKNLRPeFMQMQQIKEL---VMDEDNDGCTPLHYACRQG-GPGSVNNLLGFNVSIHSKSKDK 471
Cdd:PHA02876 404 LSQKIGTALH------FALCGTNP-YMSVKTLIDRganVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQN 476
|
410 420 430
....*....|....*....|....*....|..
gi 767952011 472 KSPLHFAASY-GRINTCQRLLQDISDTRLLNE 502
Cdd:PHA02876 477 QYPLLIALEYhGIVNILLHYGAELRDSRVLHK 508
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
268-364 |
6.91e-17 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 76.69 E-value: 6.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 268 LHLAVQNGDLEMIKMCLDNGAQIDPVEKGRCTAIHFAATQGATEIVKLMISsysgSVDIVNTTDGchETMLHRASLFDHH 347
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE----HADVNLKDNG--RTALHYAARSGHL 74
|
90
....*....|....*..
gi 767952011 348 ELADYLISVGADINKID 364
Cdd:pfam12796 75 EIVKLLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
127-220 |
8.39e-17 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 76.69 E-value: 8.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 127 LHCAVEKNQIESVKFLLSRGANPNLRNFNMMAPLHIAVQGMNNEVMKVLLEHRTIDVNlegENGNTAVIIACTTNNSEAL 206
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLK---DNGRTALHYAARSGHLEIV 77
|
90
....*....|....
gi 767952011 207 QILLKKGAKPCKSN 220
Cdd:pfam12796 78 KLLLEKGADINVKD 91
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
123-338 |
2.44e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 82.73 E-value: 2.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 123 GNTPLHCAVEKNQIESVKFLLSRGANPNLRNFNMMAPLHIAVQGMNNEVMKVLLEHRTIDVNLEGENGNTAVIIACTTNN 202
Cdd:PHA02875 35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKK 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 203 SEALQILLKKGAKPCKSNKWGCFPIHQAAFSGSKECMEIILRfgeehgysRQLHINFMNNGKATPLHLAVQNGDLEMIKM 282
Cdd:PHA02875 115 LDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLID--------HKACLDIEDCCGCTPLIIAMAKGDIAICKM 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 767952011 283 CLDNGAQIDPVEKGRC-TAIHFAATQGATEIVKLMISSYSGSvDIVNTTDGCHETML 338
Cdd:PHA02875 187 LLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADC-NIMFMIEGEECTIL 242
|
|
| Ion_trans |
pfam00520 |
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ... |
821-997 |
5.33e-16 |
|
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This family is 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some sub-families (e.g. Na channels) the domain is repeated four times, whereas in others (e.g. K channels) the protein forms as a tetramer in the membrane.
Pssm-ID: 459842 [Multi-domain] Cd Length: 238 Bit Score: 78.85 E-value: 5.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 821 KRNYFMDISNVLEWIIyttgiifVLPLFVEIPAHLQWQCGAIAV--YFYWMNFLLYLQRFENCGIFIVMLEVILKTLLRS 898
Cdd:pfam00520 60 KKRYFRSPWNILDFVV-------VLPSLISLVLSSVGSLSGLRVlrLLRLLRLLRLIRRLEGLRTLVNSLIRSLKSLGNL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 899 TVVFIFLLLAFGLSFYILL-----NLQDP------FSSPLLSIIQTFSMMLGdINYRESFLEPYLRNelaHPVLSFAQLV 967
Cdd:pfam00520 133 LLLLLLFLFIFAIIGYQLFggklkTWENPdngrtnFDNFPNAFLWLFQTMTT-EGWGDIMYDTIDGK---GEFWAYIYFV 208
|
170 180 190
....*....|....*....|....*....|
gi 767952011 968 SFTIFVPIVLMNLLIGLAVGDIAEVQKHAS 997
Cdd:pfam00520 209 SFIILGGFLLLNLFIAVIIDNFQELTERTE 238
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
207-531 |
1.80e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 81.26 E-value: 1.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 207 QILLKKGAKPCKSNKWGCFPIHQAAFSGSKECMEIILRFGEEhgysrqlhINFMNNGKATPLHLAVQNGDLEMIKMCLDN 286
Cdd:PHA02876 162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGAD--------VNIIALDDLSVLECAVDSKNIDTIKAIIDN 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 287 GAQIDPVEKGRCTAIhfAATQGATEIVkLMISSYSgsvdiVNTTDGCHETMLHRASLFDH-HELADYLISVGADINKIDS 365
Cdd:PHA02876 234 RSNINKNDLSLLKAI--RNEDLETSLL-LYDAGFS-----VNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNI 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 366 EGRSPLILaTASASWNIVNL--LLSKGAQVDIKDNFGRNFLHltvqQPYGLKNLRPEFMQMQQIKELVMDEDNDGCTPLH 443
Cdd:PHA02876 306 KGETPLYL-MAKNGYDTENIrtLIMLGADVNAADRLYITPLH----QASTLDRNKDIVITLLELGANVNARDYCDKTPIH 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 444 YACRQGGPGSVNNLLGFNVSIHSKSKDKKSPLHFAASYGRINTCQRLLQDISDTrlLNEGDLHGMTPLHLAAKNG-HDKV 522
Cdd:PHA02876 381 YAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMSVKTLIDRGAN--VNSKNKDLSTPLHYACKKNcKLDV 458
|
....*....
gi 767952011 523 VQLLLKKGA 531
Cdd:PHA02876 459 IEMLLDNGA 467
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
130-361 |
7.91e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 78.11 E-value: 7.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 130 AVEKNQIESVKFLLSRGANPNLRNFNMMAPLHIAVQGMNNEVMKVLLEHRTI-DVNLEG---------ENGNTAVIIACT 199
Cdd:PHA02875 9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIpDVKYPDieselhdavEEGDVKAVEELL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 200 TNNSEALQILLKKGAKpcksnkwgcfPIHQAAFSGSKECMEIILRFGEEHGYSrqlhinfmNNGKATPLHLAVQNGDLEM 279
Cdd:PHA02875 89 DLGKFADDVFYKDGMT----------PLHLATILKKLDIMKLLIARGADPDIP--------NTDKFSPLHLAVMMGDIKG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 280 IKMCLDNGAQIDPVEKGRCTAIHFAATQGATEIVKLMISSySGSVDIVnTTDGChETMLHRASLFDHHELADYLISVGAD 359
Cdd:PHA02875 151 IELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDS-GANIDYF-GKNGC-VAALCYAIENNKIDIVRLFIKRGAD 227
|
..
gi 767952011 360 IN 361
Cdd:PHA02875 228 CN 229
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
372-652 |
3.41e-14 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 76.60 E-value: 3.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 372 ILATASASWNIVNLLLSKGAQVDIKDNFGRNFLHLtvqqpYGLKNLRPEfmqmQQIKELVMDEDND-------GCTPLH- 443
Cdd:PHA03095 19 LLNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHL-----YLHYSSEKV----KDIVRLLLEAGADvnapercGFTPLHl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 444 YACRQGGPGSVNNLLGFNVSIHSKSKDKKSPLHFAASYGRINTCQRLLqdisdtrLLNEG------DLHGMTPLH--LAA 515
Cdd:PHA03095 90 YLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVYLSGFNINPKVIRL-------LLRKGadvnalDLYGMTPLAvlLKS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 516 KNGHDKVVQLLLKKGA-LFLSDHNGWTALHHasMGGYTQTMKVILDTN--LKCTDR-LDEDGNTALHFAAREGHAKA--V 589
Cdd:PHA03095 163 RNANVELLRLLIDAGAdVYAVDDRFRSLLHH--HLQSFKPRARIVRELirAGCDPAaTDMLGNTPLHSMATGSSCKRslV 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767952011 590 ALLLSHNADI-VLNKQQASFLHLAlhnkrkevvlTIIRSKR-WDECLKI---FSHNSPGNKCPITEMI 652
Cdd:PHA03095 241 LPLLIAGISInARNRYGQTPLHYA----------AVFNNPRaCRRLIALgadINAVSSDGNTPLSLMV 298
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
277-531 |
4.94e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 75.47 E-value: 4.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 277 LEMIKMCLDNGAQIDPVEKGRCTAIHFAATQGATEIVKLMISSysgSVDIVNTTDGcHETMLHRASLFDHH-----ELAD 351
Cdd:PHA03100 15 VKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDN---GADINSSTKN-NSTPLHYLSNIKYNltdvkEIVK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 352 YLISVGADINKIDSEGRSPLILA--TASASWNIVNLLLSKGAQVDIKDNFGRNFLHLTVQQPYGLKNlrpefmqmqqIKE 429
Cdd:PHA03100 91 LLLEYGANVNAPDNNGITPLLYAisKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLK----------ILK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 430 LVMDE--DNDGCTplhyacrqggpgSVNNLLGFNVSIHSKSKDKKSPLHFAASYGRINTCQRLLQDISDTRLLNEgdlHG 507
Cdd:PHA03100 161 LLIDKgvDINAKN------------RVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNK---YG 225
|
250 260
....*....|....*....|....
gi 767952011 508 MTPLHLAAKNGHDKVVQLLLKKGA 531
Cdd:PHA03100 226 DTPLHIAILNNNKEIFKLLLNNGP 249
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
195-291 |
1.74e-13 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 67.06 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 195 IIACTTNNSEALQILLKKGAKPCKSNKWGCFPIHQAAFSGSKECMEIILRFGeehgysrqlHINFMNNGKaTPLHLAVQN 274
Cdd:pfam12796 2 HLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA---------DVNLKDNGR-TALHYAARS 71
|
90
....*....|....*..
gi 767952011 275 GDLEMIKMCLDNGAQID 291
Cdd:pfam12796 72 GHLEIVKLLLEKGADIN 88
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
463-1022 |
2.40e-13 |
|
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: 74.15 E-value: 2.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 463 SIHSKSKDKKSPLHFAASY--GRINTCQRLLQDI-----SDTRLLNEGDL----HGMTPLHLAAKNGHDKVVQLLLKKGA 531
Cdd:cd21882 18 SAYQRGATGKTCLHKAALNlnDGVNEAIMLLLEAapdsgNPKELVNAPCTdefyQGQTALHIAIENRNLNLVRLLVENGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 532 LFLSDHNGWTALHHASMGGYTqtmkvildtnlkctdrldedGNTALHFAAREGHAKAVALLLSHNADIVLNKQQASF--- 608
Cdd:cd21882 98 DVSARATGRFFRKSPGNLFYF--------------------GELPLSLAACTNQEEIVRLLLENGAQPAALEAQDSLgnt 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 609 -LHLALHNKRKEVVLTIIRSKRWDECLKIFSHNSPgnkcpiTEMIEYLPEcMKVLLDFcMLHSTEDKSCRDYYI---EYN 684
Cdd:cd21882 158 vLHALVLQADNTPENSAFVCQMYNLLLSYGAHLDP------TQQLEEIPN-HQGLTPL-KLAAVEGKIVMFQHIlqrEFS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 685 FKYLQCPLEFTKKT--PTQDVIYEpLTALNAMVQNNRIE--------------LLNHPVcKEYLLMKWLAYGFRAHMMNL 748
Cdd:cd21882 230 GPYQPLSRKFTEWTygPVTSSLYD-LSEIDSWEKNSVLEliafskkrearhqmLVQEPL-NELLQEKWDRYGRPYFCFNF 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 749 GSYCLGLIPMTILVVNiKPgmafnstgiINETSDHSEILDTTNSYLIKTCMILVFLSSIFGYCKEAGQIFQQKRNYFMDI 828
Cdd:cd21882 308 ACYLLYMIIFTVCAYY-RP---------LKDRPANQEAKATFGDSIRLVGEILTVLGGVYILLGEIPYFFRRRLSRWFGF 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 829 SNVLEWIIYTTGIIFVLPLFVEIPAHLQWQCGAI--AVYFYWMNFLLYLQRFENCGIFIVMLE-VILKTLLRSTVVFIFL 905
Cdd:cd21882 378 LDSYFEILFITQALLVLLSMVLRFMETEGYVVPLvfSLVLGWCNVLYYTRGFQMLGIYTVMIQkMILRDLMRFCWVYLVF 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 906 LLAFGLSFYILLNLQDP-----FSSPLLSIIQTFSMMLG--DINYRESflepylrneLAHPVLSFAQLVSFTIFVPIVLM 978
Cdd:cd21882 458 LFGFASAFVILFQTEDPnklgeFRDYPDALLELFKFTIGmgDLPFNEN---------VDFPFVYLILLLAYVILTYLLLL 528
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 767952011 979 NLLIGL---AVGDIAEVQKHA-SLKRIAMQVElhtsLEKKLPlWFLRK 1022
Cdd:cd21882 529 NMLIALmgeTVNRVAQESDEIwKLQKAITTLM----LERKYP-RCLRK 571
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
126-492 |
3.32e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 73.38 E-value: 3.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 126 PLHCAVEKNQIESVKFLLSRGANPNLRNFNMMAPLHIAVQGMNNEVMKVLLEHRTIDvnlegENGNTAVII--ACTTNNS 203
Cdd:PHA02878 40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKC-----SVFYTLVAIkdAFNNRNV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 204 EALQILLkkgakpcksnkwgcfpihqaaFSGSKECMEIILRFGEEHGYSRQLhinfmnngkatplhlavqngDLEMIKMC 283
Cdd:PHA02878 115 EIFKIIL---------------------TNRYKNIQTIDLVYIDKKSKDDII--------------------EAEITKLL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 284 LDNGAQIDPVEKGR-CTAIHFAATQGATEIVKLMIsSYSGSvdiVNTTDGCHETMLHRASLFDHHELADYLISVGADINK 362
Cdd:PHA02878 154 LSYGADINMKDRHKgNTALHYATENKDQRLTELLL-SYGAN---VNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 363 IDSEGRSPLILATASA-SWNIVNLLLSKGAQVDIKDNFgRNF--LHLTVQQPYGLKNLrpefmqmQQIKELVMDEDNDGC 439
Cdd:PHA02878 230 RDKCGNTPLHISVGYCkDYDILKLLLEHGVDVNAKSYI-LGLtaLHSSIKSERKLKLL-------LEYGADINSLNSYKL 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 767952011 440 TPLHYACRQGGPGSVNNLLGFNVSIHS-KSKDKKSPLHFAASYGRINTCQRLLQ 492
Cdd:PHA02878 302 TPLSSAVKQYLCINIGRILISNICLLKrIKPDIKNSEGFIDNMDCITSNKRLNQ 355
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
717-1022 |
3.71e-13 |
|
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: 74.02 E-value: 3.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 717 NNRIELLNHPVCKEYLLMKWLAygFRAHMMNLgSYCLGLIPMTILVVnikpgMAFNSTGIiNETSDHSEILDTTNSYLIK 796
Cdd:cd22194 340 DNRHEMLTLEPLHTLLHMKWKK--FARYMFFI-SFLFYFFYNITLTL-----VSYYRPRE-DEDPPHPLALSHKMGWLQL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 797 TCMILVFLSSIFGYCKEAGQIFQQKRNyfmDISNVLEwIIYTTGIIFVLPLFVEIPAHLQWQ-------CGAIAVYFYWM 869
Cdd:cd22194 411 LGQMFVLIWATCLSVKEGIAIFLLRPS---DLKSILS-DAWFHILFFIQAVLVIVSVFLYLFaykeylaCLVLAMALGWA 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 870 NFLLYLQRFENCGIFIVMLE-VILKTLLRSTVVFIFLLLAFGLSFYILLN-LQD-----PFSSPLLSIIQTFSMM--LGD 940
Cdd:cd22194 487 NMLYYTRGFQSLGIYSVMIQkVILNDVLKFLLVYILFLLGFGVALASLIEdCPDdsecsSYGSFSDAVLELFKLTigLGD 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 941 INyresflepyLRNELAHPVLSFAQLVSFTIFVPIVLMNLLIGLAVGDIAEVQKHAS----LKRiAMQVelhTSLEKKLP 1016
Cdd:cd22194 567 LE---------IQQNSKYPILFLLLLITYVILTFVLLLNMLIALMGETVENVSKESEriwrLQR-ARTI---LEFEKSLP 633
|
....*.
gi 767952011 1017 LWFLRK 1022
Cdd:cd22194 634 EWLRKR 639
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
301-397 |
4.43e-13 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 65.91 E-value: 4.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 301 IHFAATQGATEIVKLMISSYSGsvdiVNTTDGCHETMLHRASLFDHHELADYLISVgADINKIDsEGRSPLILATASASW 380
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGAD----ANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHL 74
|
90
....*....|....*..
gi 767952011 381 NIVNLLLSKGAQVDIKD 397
Cdd:pfam12796 75 EIVKLLLEKGADINVKD 91
|
|
| TRPV1-4 |
cd22193 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ... |
698-1022 |
7.82e-13 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411977 [Multi-domain] Cd Length: 607 Bit Score: 72.52 E-value: 7.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 698 TPTQDVIYEpLTALNAMVQNNRIELLNHPVcKEYLLMKWLAYGFRAHMMNLGSYCLGLIPMTiLVVNIKPgmafnstgiI 777
Cdd:cd22193 264 TCEKNSVLE-IIVYNSKIDNRHEMLTLEPL-NTLLQDKWDKFAKYMFFFSFCFYLFYMIIFT-LVAYYRP---------R 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 778 NETSDHSEILDTTNSYLIKTCMILVFLSSIFGYCKEAgQIFQQKR----NYFMDISNVLEWIIYTTGIIFVLPL-FVEIP 852
Cdd:cd22193 332 EDEPPPPLAKTTKMDYMRLLGEILVLLGGVYFFVKEI-AYFLLRRsdlqSSFSDSYFEILFFVQAVLVILSVVLyLFAYK 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 853 AHLQwqCGAIAVYFYWMNFLLYLQRFENCGIFIVMLE-VILKTLLRSTVVFIFLLLAFGLSFYILLN-------LQDPFS 924
Cdd:cd22193 411 EYLA--CLVLALALGWANMLYYTRGFQSMGIYSVMIQkVILRDLLRFLFVYLLFLFGFAVALVSLIEkcssdkkDCSSYG 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 925 SPLLSIIQTFSMM--LGDINYRESflepylrneLAHPVLSFAQLVSFTIFVPIVLMNLLIGLAVGDIAEVQKHAslKRIA 1002
Cdd:cd22193 489 SFSDAVLELFKLTigMGDLEFQEN---------STYPAVFLILLLTYVILTFVLLLNMLIALMGETVNNVSKES--KRIW 557
|
330 340
....*....|....*....|.
gi 767952011 1003 MQVELHTSLE-KKLPLWFLRK 1022
Cdd:cd22193 558 KLQRAITILEfEKSFPECMRK 578
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
345-664 |
1.64e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 71.63 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 345 DHHELADYLISVGADINKIDSEGRSPLILATASASWNIVNLLLSKGAQVDIKDNFGRNFLHLTVQQpyglKNLrpefmqm 424
Cdd:PHA02876 156 DELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDS----KNI------- 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 425 QQIKELVMDEDNDGCTPLHYACRQGGPGSVNNLLGFNVSIHSKSKD--KKSPLHFAA---SYGRIntCQRLLQDISDtrl 499
Cdd:PHA02876 225 DTIKAIIDNRSNINKNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDdcKNTPLHHASqapSLSRL--VPKLLERGAD--- 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 500 LNEGDLHGMTPLHLAAKNGHD-KVVQLLLKKGA-LFLSDHNGWTALHHAS-MGGYTQTMKVILD--TNLKCTDRLDEdgn 574
Cdd:PHA02876 300 VNAKNIKGETPLYLMAKNGYDtENIRTLIMLGAdVNAADRLYITPLHQAStLDRNKDIVITLLElgANVNARDYCDK--- 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 575 TALHFAAREGHAKAVALLLSHNADI-VLNKQQASFLHLALH--NKRKEVVLTIIRSKRWDECLKIFS---HNSPGNKCPi 648
Cdd:PHA02876 377 TPIHYAAVRNNVVIINTLLDYGADIeALSQKIGTALHFALCgtNPYMSVKTLIDRGANVNSKNKDLStplHYACKKNCK- 455
|
330
....*....|....*.
gi 767952011 649 temieylPECMKVLLD 664
Cdd:PHA02876 456 -------LDVIEMLLD 464
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
440-1018 |
2.39e-12 |
|
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: 71.20 E-value: 2.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 440 TPLHYACRQGGPGSVNNLLGFN-VSIHSKSKDKKSPLHFAASYGRINTCQRLLQdiSDTRLLNE---GDLH-GMTPLHLA 514
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLLKCPsCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNEpmtSDLYqGETALHIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 515 AKNGHDKVVQLLLKKGALFLSDHNGWTALHhasmggytqtmkvildtnlKCTDRLDEDGNTALHFAAREGHAKAVALLLS 594
Cdd:cd22192 97 VVNQNLNLVRELIARGADVVSPRATGTFFR-------------------PGPKNLIYYGEHPLSFAACVGNEEIVRLLIE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 595 HNADIvlnKQQASF----LH-LALHNKRK------EVVLTIIRSKRwDECLKIFSHN---SP-------GNkcpiTEMIE 653
Cdd:cd22192 158 HGADI---RAQDSLgntvLHiLVLQPNKTfacqmyDLILSYDKEDD-LQPLDLVPNNqglTPfklaakeGN----IVMFQ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 654 YLpecMKvlldfcmlhstedkscRDYYIEYNFKYLQCPLEFTKKTPTQDviyEPLTALNAMVQNNRIELLN----HPVcK 729
Cdd:cd22192 230 HL---VQ----------------KRRHIQWTYGPLTSTLYDLTEIDSWG---DEQSVLELIVSSKKREARKildvTPV-K 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 730 EYLLMKWLAYGFRAHMMNLGSYCLGLIPMTILVVN----IKPGMAFNSTGI---INETSDHSEIldTTNSYLIKTCMILV 802
Cdd:cd22192 287 ELVSLKWKRYGRPYFRILALLYLLYIIIFTLCCVYrplkPRPENNTDPRDItlyVQKTLQESYV--TPKDYLRLVGELIS 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 803 FLSSIFGYCKEAGQIFQ--QKRnYFMD--ISNVLEWIIYTTGI-IFVLPLFVEIPAHLQWQCGAIAVYFYWMNFLLYLQR 877
Cdd:cd22192 365 VLGAIVILLLEIPDILRvgVKR-YFGQtvLGGPFHVIIITYAClVLLTLVLRLTSLSGEVVPMSLALVLGWCNVMYFARG 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 878 FENCGIFIVMLE-VILKTLLRSTVVFIFLLLAFGLSFYILLNLQDP-----FSSPLLSIIQTFSMMLGDINYresflepY 951
Cdd:cd22192 444 FQMLGPFTIMIQkIIFGDLMKFCWLMFVVILGFSSAFYMIFQTEDPdslghFYDFPMTLFSTFELFLGLIDG-------P 516
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767952011 952 LRNELAHPVLSFAQLVSFTIFVPIVLMNLLIGLaVGDiaevqkhaSLKRIA--------MQVELHT-SLEKKLP--LW 1018
Cdd:cd22192 517 ANYTVDLPFMYKVLYTAFAVIAYLLMLNLLIAM-MGD--------THWRVAherdelwrAQVVATTlMLERRLPrcLW 585
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
370-599 |
3.43e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 66.61 E-value: 3.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 370 PLILATASASWNIVNLLLSKGAQVDIKDNFGRNFLHLTVQQPYGLKNLRPEFMQMQQIKELVMDEDNDGCTPLHYA--CR 447
Cdd:PHA03100 38 PLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAisKK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 448 QGGPGSVNNLLGFNVSIHSKSKDKKSPLHFAASYGRINT--CQRLLQDISD----TRL---------LNEGDLHGMTPLH 512
Cdd:PHA03100 118 SNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkiLKLLIDKGVDinakNRVnyllsygvpINIKDVYGFTPLH 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 513 LAAKNGHDKVVQLLLKKGAlflsdhngwtalhhasmggytqtmkvilDTNLKctdrlDEDGNTALHFAAREGHAKAVALL 592
Cdd:PHA03100 198 YAVYNNNPEFVKYLLDLGA----------------------------NPNLV-----NKYGDTPLHIAILNNNKEIFKLL 244
|
....*..
gi 767952011 593 LSHNADI 599
Cdd:PHA03100 245 LNNGPSI 251
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
160-248 |
5.85e-11 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 59.74 E-value: 5.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 160 LHIAVQGMNNEVMKVLLEHRTiDVNLEGENGNTAVIIACTTNNSEALQILLKKGAKPCKSNkwGCFPIHQAAFSGSKECM 239
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGA-DANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN--GRTALHYAARSGHLEIV 77
|
....*....
gi 767952011 240 EIILRFGEE 248
Cdd:pfam12796 78 KLLLEKGAD 86
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
92-185 |
6.70e-11 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 59.74 E-value: 6.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 92 LHYAAAEGQIELMEKItrdssLEVLHEM---DDYGNTPLHCAVEKNQIESVKFLLSRgANPNLRNFNmMAPLHIAVQGMN 168
Cdd:pfam12796 1 LHLAAKNGNLELVKLL-----LENGADAnlqDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG-RTALHYAARSGH 73
|
90
....*....|....*..
gi 767952011 169 NEVMKVLLEHrTIDVNL 185
Cdd:pfam12796 74 LEIVKLLLEK-GADINV 89
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
338-467 |
3.45e-10 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 57.82 E-value: 3.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 338 LHRASLFDHHELADYLISVGADINKIDSEGRSPLILATASASWNIVNLLLSKGAQvdikdnfgrnflhltvqqpyglknl 417
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV------------------------- 55
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 767952011 418 rpefmqmqqikelvmDEDNDGCTPLHYACRQGGPGSVNNLLGFNVSIHSK 467
Cdd:pfam12796 56 ---------------NLKDNGRTALHYAARSGHLEIVKLLLEKGADINVK 90
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
120-191 |
6.26e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 62.76 E-value: 6.26e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767952011 120 DDYGNTPLHCAVEKNQIESVKFLLSRGANPNLRNFNMMAPLHIAVQGMNNEVMKVLLEHR----TIDVNLEGENGN 191
Cdd:PHA03100 189 DVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGpsikTIIETLLYFKDK 264
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
121-272 |
6.57e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 62.98 E-value: 6.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 121 DYGNTPLHCAVEKNQIESVKFLLSRGANPNLRNFNMMAPLHIAVQGMNNEVMKVLLEHRTiDVNLEGENGNTAVIIACTT 200
Cdd:PHA02878 166 HKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA-STDARDKCGNTPLHISVGY 244
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767952011 201 -NNSEALQILLKKGAK-PCKSNKWGCFPIHQAAFSGSKecMEIILRFGEEhgysrqlhINFMNNGKATPLHLAV 272
Cdd:PHA02878 245 cKDYDILKLLLEHGVDvNAKSYILGLTALHSSIKSERK--LKLLLEYGAD--------INSLNSYKLTPLSSAV 308
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
92-153 |
9.99e-10 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 56.28 E-value: 9.99e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767952011 92 LHYAAAEGQIE----LMEKITRDsslevlheMDDYGNTPLHCAVEKNQIESVKFLLSRGANPNLRN 153
Cdd:pfam12796 34 LHLAAKNGHLEivklLLEHADVN--------LKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
334-531 |
4.27e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 60.00 E-value: 4.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 334 HETMLHRASLFDHHELADYLISVGADINKIDSEGRSPLILATASASWNIVNLLLSKGAQVDIKDNFGRNFLHLTVQQPyg 413
Cdd:PHA02875 2 DQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEG-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 414 lknlrpefmQMQQIKELVMDED-------NDGCTPLHYACRQGGPGSVNNLLGFNVSIHSKSKDKKSPLHFAASYGRINT 486
Cdd:PHA02875 80 ---------DVKAVEELLDLGKfaddvfyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKG 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 767952011 487 CQRLLQDISDTRLlneGDLHGMTPLHLAAKNGHDKVVQLLLKKGA 531
Cdd:PHA02875 151 IELLIDHKACLDI---EDCCGCTPLIIAMAKGDIAICKMLLDSGA 192
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
359-984 |
4.72e-09 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 60.48 E-value: 4.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 359 DINKIDSEGRSPLILAtASASWN--IVNLLLSKGAQVDIkdnfGRNFLHLTVQQPYGLKN---LRPEFMQMQQIK-ELVM 432
Cdd:TIGR00870 44 NINCPDRLGRSALFVA-AIENENleLTELLLNLSCRGAV----GDTLLHAISLEYVDAVEailLHLLAAFRKSGPlELAN 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 433 DEDND----GCTPLHYACRQGGPGSVNNLL--GFNVSIHSKSKD-KKSPLHFAASYGRintcqrllqdisdtrllnegdl 505
Cdd:TIGR00870 119 DQYTSeftpGITALHLAAHRQNYEIVKLLLerGASVPARACGDFfVKSQGVDSFYHGE---------------------- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 506 hgmTPLHLAAKNGHDKVVQLLLKKGALFLS-DHNGWTALHHASM--------GGYTQTMK---VILDTNLKCTDRLDE-- 571
Cdd:TIGR00870 177 ---SPLNAAACLGSPSIVALLSEDPADILTaDSLGNTLLHLLVMenefkaeyEELSCQMYnfaLSLLDKLRDSKELEVil 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 572 --DGNTALHFAAREGhakavalllshnadivlnKQQASFLHLALHNKRKEVVltiirskrwdeclkiFSHNSPgnkcpit 649
Cdd:TIGR00870 254 nhQGLTPLKLAAKEG------------------RIVLFRLKLAIKYKQKKFV---------------AWPNGQ------- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 650 emieylpecmkvlldfcMLHSTEDKSCRDyyieynfkylqcplEFTKKTPTQDVIyePLTALNAMVQNNRIELLNHPvCK 729
Cdd:TIGR00870 294 -----------------QLLSLYWLEELD--------------GWRRKQSVLELI--VVFVIGLKFPELSDMYLIAP-LS 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 730 EYLLMKWLAYGFRAHMMNLGSYCLGLIPMTILVVnIKPGMAFNSTGIINETSDHSEILdTTNSYLIKTCMILVFLSSIFG 809
Cdd:TIGR00870 340 RLGQFKWKPFIKFIFHSASYLYFLYLIIFTSVAY-YRPTRTDLRVTGLQQTPLEMLIV-TWVDGLRLGEEKLIWLGGIFE 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 810 YCKEAGQIFQQKRNYFMDISNVL---EWIIYTTGIIFVLPLFVEIPAHLqWQCG--AIAVYFYWMNFLLYLQRFENCGIF 884
Cdd:TIGR00870 418 YIHQLWNILDFGMNSFYLATFLDrpfAILFVTQAFLVLREHWLRFDPTL-IEEAlfAFALVLSWLNLLYIFRGNQHLGPL 496
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 885 IVMLE-VILKTLLRSTVVFIFLLLAFGLSFYILLNLQDPFSSPLLS---------IIQTFSMMLgdinyrESFLE----- 949
Cdd:TIGR00870 497 QIMIGrMILGDILRFLFIYAVVLFGFACGLNQLYQYYDELKLNECSnpharscekQGNAYSTLF------ETSQElfwai 570
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 767952011 950 ----PYLRNELAH-PVLSFAQLVSFTIFVPIVLMNLLIGL 984
Cdd:TIGR00870 571 iglgDLLANEHKFtEFVGLLLFGAYNVIMYILLLNMLIAM 610
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
360-624 |
9.01e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 59.21 E-value: 9.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 360 INKIDSEGRSPLILATASASWNIVNLLLSKGAQVDikdnfgrnflHLTVQQPYGLknLRPEFMQMQQIKELVMDEDNDgC 439
Cdd:PHA02874 28 INISVDETTTPLIDAIRSGDAKIVELFIKHGADIN----------HINTKIPHPL--LTAIKIGAHDIIKLLIDNGVD-T 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 440 TPLHYACRQGGpgSVNNLLGFNVSIHSKSKDKKSPLHFAASYGRINTCQRLLQDISDtrlLNEGDLHGMTPLHLAAKNGH 519
Cdd:PHA02874 95 SILPIPCIEKD--MIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGAD---VNIEDDNGCYPIHIAIKHNF 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 520 DKVVQLLLKKGALflsdhngwtalhhasmggytqtmkvildTNLKctdrlDEDGNTALHFAAREGHAKAVALLLSHNADI 599
Cdd:PHA02874 170 FDIIKLLLEKGAY----------------------------ANVK-----DNNGESPLHNAAEYGDYACIKLLIDHGNHI 216
|
250 260
....*....|....*....|....*..
gi 767952011 600 vLNKQQASF--LHLALHNKRKEVVLTI 624
Cdd:PHA02874 217 -MNKCKNGFtpLHNAIIHNRSAIELLI 242
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
91-243 |
1.04e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 58.82 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 91 FLHYAAAEGQIELMEKITR---DSSLEvlhemDDYGNTPLHCAVEKNQIESVKFLLSRGANPNLRNFNMMAPLHIAVQGM 167
Cdd:PHA02874 127 FLHYAIKKGDLESIKMLFEygaDVNIE-----DDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYG 201
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767952011 168 NNEVMKVLLEHrTIDVNLEGENGNTAVIIACTTNNSeALQILLKKgAKPCKSNKWGCFPIHQA-AFSGSKECMEIIL 243
Cdd:PHA02874 202 DYACIKLLIDH-GNHIMNKCKNGFTPLHNAIIHNRS-AIELLINN-ASINDQDIDGSTPLHHAiNPPCDIDIIDILL 275
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
507-559 |
1.68e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 51.89 E-value: 1.68e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 767952011 507 GMTPLHLAAKNGHDKVVQLLLKKGA-LFLSDHNGWTALHHASMGGYTQTMKVIL 559
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGAdINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
539-593 |
3.05e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 51.12 E-value: 3.05e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 767952011 539 GWTALHHASMGGYTQTMKVILDTNLKCtDRLDEDGNTALHFAAREGHAKAVALLL 593
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADI-NAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
266-317 |
4.65e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 50.35 E-value: 4.65e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 767952011 266 TPLHLAVQNGDLEMIKMCLDNGAQIDPVEKGRCTAIHFAATQGATEIVKLMI 317
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
503-600 |
7.39e-08 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 56.80 E-value: 7.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 503 GDLHGMTPLHLAAKNGHDKVVQLLLKKGA-LFLSDHNGWTAL-------HH------------------------ASMGG 550
Cdd:PLN03192 554 GDSKGRTPLHIAASKGYEDCVLVLLKHACnVHIRDANGNTALwnaisakHHkifrilyhfasisdphaagdllctAAKRN 633
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 767952011 551 YTQTMKVILDTNLKcTDRLDEDGNTALHFAAREGHAKAVALLLSHNADIV 600
Cdd:PLN03192 634 DLTAMKELLKQGLN-VDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVD 682
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
130-452 |
1.35e-07 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 55.86 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 130 AVEKNQIESVKfllSRGANPNLRNFNMMAPL------HIAVQGMNNEVMKVLLEHrtidvNLEGENGNTAVIIACTT--- 200
Cdd:TIGR00870 24 AAERGDLASVY---RDLEEPKKLNINCPDRLgrsalfVAAIENENLELTELLLNL-----SCRGAVGDTLLHAISLEyvd 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 201 NNSEALQILLKKGAKpcksnkwGCFPIHQAAFSGSkecmeiilRFGEEHgysrqlhinfmnngkaTPLHLAVQNGDLEMI 280
Cdd:TIGR00870 96 AVEAILLHLLAAFRK-------SGPLELANDQYTS--------EFTPGI----------------TALHLAAHRQNYEIV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 281 KMCLDNGAQIdPVekgRCTAIHFAATQGATeivklmissysgsvdivnttdgchetmlhrasLFDHheladylisvgadi 360
Cdd:TIGR00870 145 KLLLERGASV-PA---RACGDFFVKSQGVD--------------------------------SFYH-------------- 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 361 nkidseGRSPLILATASASWNIVNLLLSKGAQVDIKDNFGRNFLHLTVQQPyGLKNLRPEF-MQMQQI-----------K 428
Cdd:TIGR00870 175 ------GESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVMEN-EFKAEYEELsCQMYNFalslldklrdsK 247
|
330 340
....*....|....*....|....
gi 767952011 429 ELVMDEDNDGCTPLHYACRQGGPG 452
Cdd:TIGR00870 248 ELEVILNHQGLTPLKLAAKEGRIV 271
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
266-411 |
1.42e-07 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 55.79 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 266 TPLHLAVQNGDLEMIKMCLDNgAQIDPVEKGRC--TAIHFAATQGATEIVKLMISSYSGSVDIVNTTD---GchETMLHR 340
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLLKC-PSCDLFQRGALgeTALHVAALYDNLEAAVVLMEAAPELVNEPMTSDlyqG--ETALHI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 341 ASLFDHHELADYLISVGADINKIDSEG--------------RSPLILATASASWNIVNLLLSKGAQVDIKDNFGRNFLHL 406
Cdd:cd22192 96 AVVNQNLNLVRELIARGADVVSPRATGtffrpgpknliyygEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175
|
....*
gi 767952011 407 TVQQP 411
Cdd:cd22192 176 LVLQP 180
|
|
| TRPV4 |
cd22195 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed ... |
702-1038 |
2.93e-07 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed broadly in neuronal and non-neuronal cells. It is activated by various stimuli, including hypo-osmolarity, warm temperature, and chemical ligands. TRPV4 acts in physiological functions such as osmoregulation and thermoregulation. It also has a role in mechanosensation in the vascular endothelium and urinary tract, and in cell barrier formation in vascular and epidermal tissues. Knockout mice studies suggested the functional importance of TRPV4 in the central nervous system, nociception, and bone formation. TRPV4 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411979 [Multi-domain] Cd Length: 733 Bit Score: 54.86 E-value: 2.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 702 DVIYEPLTALNAMVQN----NRIELLNHPVCKEYLLMKWLAYGFRAHMMNLGSYCLGLIPMTILV----VNIKPGMAFNs 773
Cdd:cd22195 324 DTCGEEVSVLEILVYNskieNRHEMLAVEPINELLRDKWRKFGAVSFYISVVSYLVAMIIFTLIAyyrpMEGTPPYPYR- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 774 tgiinetsdhseildTTNSYLIKTCMILVFLSSIFGYCKEAGQIFQQK----RNYFMDISNVLEWIIYTTGIIFVLPLFV 849
Cdd:cd22195 403 ---------------TTVDYLRLAGEIITLLTGIFFFFTNIKDLFMKKcpgvNSLFIDGSFQLLYFIYSVLVIVTAALYL 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 850 E-IPAHLQWQcgAIAVYFYWMNFLLYLQRFENCGIFIVMLEVIL-KTLLRSTVVFIFLLLAFGLSFYILLNL-------- 919
Cdd:cd22195 468 AgIEAYLAVM--VFALVLGWMNALYFTRGLKLTGTYSIMIQKILfKDLFRFLLVYLLFMIGYASALVSLLNPcptketck 545
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 920 --QDPFSSPLLSII---QTFSMMLGDInYRESF----LEpyLRNELAHPVLSFAQLVSFTIFVPIVLMNLLIGL---AVG 987
Cdd:cd22195 546 edSTNCTVPTYPSCrdsNTFSKFLLDL-FKLTIgmgdLE--MLNSAKYPAVFIILLVTYIILTFVLLLNMLIALmgeTVG 622
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 767952011 988 DIAEVQKHASLKRIAMQVelhTSLEKKLPLwFLRKVDQKSTIVYPNKPRSG 1038
Cdd:cd22195 623 QVSKESKQIWKLQWATTI---LDIERSFPV-FLRKAFRSGEMVTVGKNLDG 669
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
267-546 |
3.03e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 54.50 E-value: 3.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 267 PLHLAVQNGDLEMIKMCLDNGAQIDPVEKGRCTAIHFAATQGATEIVKLMISSY---SGSVDIVNTTDGCHETMLHRASL 343
Cdd:PHA02878 40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSInkcSVFYTLVAIKDAFNNRNVEIFKI 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 344 FdhheLADYLISV-GADINKIDSEGRSPLILAtasaswNIVNLLLSKGAQVDIKDnfgrnflhltvqqpyglknlrpefm 422
Cdd:PHA02878 120 I----LTNRYKNIqTIDLVYIDKKSKDDIIEA------EITKLLLSYGADINMKD------------------------- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 423 qmqqikelvmdeDNDGCTPLHYACRQGGPGSVNNLLGFNVSIHSKSKDKKSPLHFAASYGRINTCQRLLQDISDTrllNE 502
Cdd:PHA02878 165 ------------RHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAST---DA 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 767952011 503 GDLHGMTPLHLAAKNGHD-KVVQLLLKKGALF--LSDHNGWTALHHA 546
Cdd:PHA02878 230 RDKCGNTPLHISVGYCKDyDILKLLLEHGVDVnaKSYILGLTALHSS 276
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
118-295 |
3.16e-07 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 54.26 E-value: 3.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 118 EMDDYGNTPLHCAVEKNQ--IESVKFLLSRGANPNLRNFNMMAPLHIAVQGM--NNEVMKVLLEhRTIDVNLEGENGNTA 193
Cdd:PHA03095 147 ALDLYGMTPLAVLLKSRNanVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFkpRARIVRELIR-AGCDPAATDMLGNTP 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 194 VIIACTTNNSEALQI--LLKKGAKPCKSNKWGCFPIHQAAFSGSKECMEIILRFGEEhgysrqlhINFMNNGKATPLHLA 271
Cdd:PHA03095 226 LHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGAD--------INAVSSDGNTPLSLM 297
|
170 180
....*....|....*....|....
gi 767952011 272 VQNGDLEMIKMCLDNGAQIDPVEK 295
Cdd:PHA03095 298 VRNNNGRAVRAALAKNPSAETVAA 321
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
245-400 |
3.84e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 53.84 E-value: 3.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 245 FGEEHGYSRQLHI----NFMNNGKATPLHLAVQNGDLEMIKMCLDNGAQIDPVEKGRCTAIHFAATQGATEIVKLMISSY 320
Cdd:PHA02875 12 FGELDIARRLLDIginpNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 321 SGSVDIVnTTDGchETMLHRASLFDHHELADYLISVGADINKIDSEGRSPLILATASASWNIVNLLLSKGAQVDIKDNFG 400
Cdd:PHA02875 92 KFADDVF-YKDG--MTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCG 168
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
473-527 |
5.61e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 47.27 E-value: 5.61e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 767952011 473 SPLHFAASYGRINTCQRLLQDISDtrlLNEGDLHGMTPLHLAAKNGHDKVVQLLL 527
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGAD---INAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
122-153 |
7.68e-07 |
|
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: 46.51 E-value: 7.68e-07
10 20 30
....*....|....*....|....*....|...
gi 767952011 122 YGNTPLHCAVEK-NQIESVKFLLSRGANPNLRN 153
Cdd:pfam00023 1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
496-546 |
9.54e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 46.96 E-value: 9.54e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 767952011 496 DTRLLNEGDLHGMTPLHLAAKNGHDKVVQLLLKKGA-LFLSDHNGWTALHHA 546
Cdd:pfam13857 5 GPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVdLNLKDEEGLTALDLA 56
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
123-176 |
1.44e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 46.11 E-value: 1.44e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 767952011 123 GNTPLHCAVEKNQIESVKFLLSRGANPNLRNFNMMAPLHIAVQGMNNEVMKVLL 176
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
171-340 |
2.18e-06 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 52.18 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 171 VMKVLLEH--RTIDVNLE-------GENGNTA----VIIACTTNNSEALQILLKKGAKPCKSNKWGCFPIHQAAFSGSKE 237
Cdd:PLN03192 493 ILKNFLQHhkELHDLNVGdllgdngGEHDDPNmasnLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYED 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 238 CMEIILRFG-----------------EEHGYSRQLHINFMNNGKATP------LHLAVQNGDLEMIKMCLDNGAQIDPVE 294
Cdd:PLN03192 573 CVLVLLKHAcnvhirdangntalwnaISAKHHKIFRILYHFASISDPhaagdlLCTAAKRNDLTAMKELLKQGLNVDSED 652
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 767952011 295 KGRCTAIHFAATQGATEIVKLMISSySGSVDIVNTTDGCHETMLHR 340
Cdd:PLN03192 653 HQGATALQVAMAEDHVDMVRLLIMN-GADVDKANTDDDFSPTELRE 697
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
122-151 |
6.31e-06 |
|
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: 43.73 E-value: 6.31e-06
10 20 30
....*....|....*....|....*....|
gi 767952011 122 YGNTPLHCAVEKNQIESVKFLLSRGANPNL 151
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
437-597 |
6.80e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 49.99 E-value: 6.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 437 DGCTPLHYACRQGGPGSVNNLLGFNVSIHSKSKDKKSPLHFAASYGRINTCQRLLqdISDTRLLNEGDLHGMTPLHLAAK 516
Cdd:PHA02875 34 DGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL--DLGKFADDVFYKDGMTPLHLATI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 517 NGHDKVVQLLLKKGAlflsdhngwtalhhasmggytqtmkvilDTNLKCTDRLdedgnTALHFAAREGHAKAVALLLSHN 596
Cdd:PHA02875 112 LKKLDIMKLLIARGA----------------------------DPDIPNTDKF-----SPLHLAVMMGDIKGIELLIDHK 158
|
.
gi 767952011 597 A 597
Cdd:PHA02875 159 A 159
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
120-163 |
7.72e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 44.26 E-value: 7.72e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 767952011 120 DDYGNTPLHCAVEKNQIESVKFLLSRGANPNLRNFNMMAPLHIA 163
Cdd:pfam13857 13 DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
299-354 |
8.50e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 44.19 E-value: 8.50e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 767952011 299 TAIHFAATQGATEIVKLMISSysgSVDIvNTTDGCHETMLHRASLFDHHELADYLI 354
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEK---GADI-NAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
142-291 |
1.71e-05 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 49.10 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 142 LLSRGANPNLRNFNMMAPLHIAVQGMNNEVMKVLLEHrTIDVNLEGENGNTAVIIACTTNNSEALQIL--LKKGAKPCKS 219
Cdd:PLN03192 544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKH-ACNVHIRDANGNTALWNAISAKHHKIFRILyhFASISDPHAA 622
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767952011 220 NKWGCFpihqAAFSGSKECMEIILRFGeehgysrqLHINFMNNGKATPLHLAVQNGDLEMIKMCLDNGAQID 291
Cdd:PLN03192 623 GDLLCT----AAKRNDLTAMKELLKQG--------LNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVD 682
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
244-602 |
1.89e-05 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 48.51 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 244 RFGEE---HGYSRqlhiNFMNNGKATPLHLAVQNGDLEMIKMCLDNGAQIDPVEKGRCTAIHFAAtqgateivklmissy 320
Cdd:PHA02946 53 RFVEEllhRGYSP----NETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLS--------------- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 321 sgsvdivnttdGCHETMLHRASLfdhheladyLISVGADINK-IDSEGRSPLiLATASASWNIVNLLLSKGAQVDIKDNF 399
Cdd:PHA02946 114 -----------GTDDEVIERINL---------LVQYGAKINNsVDEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKF 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 400 GRNFLHltvqqpYGLKNLRPEFMQMQQIKELVMD---EDNDGCTPLHYACRQGGPG-SVNNLLGFNVSIHSKSKDKKSPL 475
Cdd:PHA02946 173 GKNHIH------RHLMSDNPKASTISWMMKLGISpskPDHDGNTPLHIVCSKTVKNvDIINLLLPSTDVNKQNKFGDSPL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 476 HFaasygrintcqrLLQDISDTRLLNE----GDLHGMTPLHLAAKNGHDKVVQLLLKKGALFLSdhngwTALHHASMGGY 551
Cdd:PHA02946 247 TL------------LIKTLSPAHLINKllstSNVITDQTVNICIFYDRDDVLEIINDKGKQYDS-----TDFKMAVEVGS 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 767952011 552 TQTMKVILDTNLKCTDrldedgntALHFAAREGHAKAV-ALLLSH-NADIVLN 602
Cdd:PHA02946 310 IRCVKYLLDNDIICED--------AMYYAVLSEYETMVdYLLFNHfSVDSVVN 354
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
506-531 |
2.35e-05 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 42.28 E-value: 2.35e-05
10 20
....*....|....*....|....*..
gi 767952011 506 HGMTPLHLAA-KNGHDKVVQLLLKKGA 531
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGA 27
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
92-143 |
2.43e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 42.65 E-value: 2.43e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 767952011 92 LHYAAAEGQIELMeKITRDSSLEVlHEMDDYGNTPLHCAVEKNQIESVKFLL 143
Cdd:pfam13637 5 LHAAAASGHLELL-RLLLEKGADI-NAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
506-531 |
2.61e-05 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 42.19 E-value: 2.61e-05
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
476-595 |
2.86e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 48.36 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 476 HFAASyGRINTCQRLLQDISDTrllNEGDLHGMTPLHLAAKNGHDKVVQLLLKKGAlflsdhngwtalhhasmggytqtm 555
Cdd:PTZ00322 88 QLAAS-GDAVGARILLTGGADP---NCRDYDGRTPLHIACANGHVQVVRVLLEFGA------------------------ 139
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 767952011 556 kvilDTNLkctdrLDEDGNTALHFAAREGHAKAVALLLSH 595
Cdd:PTZ00322 140 ----DPTL-----LDKDGKTPLELAEENGFREVVQLLSRH 170
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
431-618 |
2.99e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 47.95 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 431 VMDEDNDGCTPLHYACRQggpgsvNNLLGFNVSIHSKSKDKKS----PLHFAASYGRINTCQRLL-------QDISD--- 496
Cdd:PHA02878 63 VNQPDHRDLTPLHIICKE------PNKLGMKEMIRSINKCSVFytlvAIKDAFNNRNVEIFKIILtnrykniQTIDLvyi 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 497 -------------TRLL-------NEGDLH-GMTPLHLAAKNGHDKVVQLLLKKGA-LFLSDHNGWTALHHAsMGGYTQT 554
Cdd:PHA02878 137 dkkskddiieaeiTKLLlsygadiNMKDRHkGNTALHYATENKDQRLTELLLSYGAnVNIPDKTNNSPLHHA-VKHYNKP 215
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767952011 555 MKVILDTNLKCTDRLDEDGNTALHFA-AREGHAKAVALLLSHNADIvlNKQQA----SFLHLALHNKRK 618
Cdd:PHA02878 216 IVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDV--NAKSYilglTALHSSIKSERK 282
|
|
| TRPV1 |
cd22196 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ... |
717-1030 |
3.41e-05 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411980 [Multi-domain] Cd Length: 649 Bit Score: 47.88 E-value: 3.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 717 NNRIELLNHPVCKeYLLMKWLAYGFRAHMMNLGSYCLGLIPMTILVVNIKPGMafnstgiinetSDHSEILDTTNSYLIK 796
Cdd:cd22196 300 NRHEMLLVEPLNK-LLQDKWDKFVKRIFYFNFFVYFIYMIIFTLAAYYRPVNK-----------TPPFPIENTTGEYLRL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 797 TCMILVFLSSIFGYCKeAGQIFQQKRNYFMDIsnvlewII--YTTGIIFVLPLFVEIPAHLQW-------QCGAIAVYFY 867
Cdd:cd22196 368 TGEIISVSGGVYFFFR-GIQYFLQRRPSLKKL------IVdsYCEILFFVQSLFLLASTVLYFcgrneyvAFMVISLALG 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 868 WMNFLLYLQRFENCGIFIVMLE-VILKTLLRSTVVFIFLLLAFGLSFYILL---------------NLQDPFSSPLLSII 931
Cdd:cd22196 441 WANVLYYTRGFQQMGIYSVMIQkMILRDICRFLFVYLVFLFGFSAALVTLIedgppkgdvntsqkeCVCKSGYNSYNSLY 520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 932 QT------FSMMLGDINYRESFlepylrneLAHPVLSFAqLVSFTIFVPIVLMNLLIGL---AVGDIAEVQKHA-SLKRi 1001
Cdd:cd22196 521 STclelfkFTIGMGDLEFTENY--------KFKEVFIFL-LISYVILTYILLLNMLIALmgeTVSKIAQESKNIwKLQR- 590
|
330 340
....*....|....*....|....*....
gi 767952011 1002 AMQVelhTSLEKKLPLWFLRKVDQKSTIV 1030
Cdd:cd22196 591 AITI---LDLEKSLLRCLRDRFRSGKSVL 616
|
|
| PHA02741 |
PHA02741 |
hypothetical protein; Provisional |
91-222 |
3.57e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 165108 [Multi-domain] Cd Length: 169 Bit Score: 45.42 E-value: 3.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 91 FLHYAAAEGQIELMEKIT----RDSSLEVLHEMDDYGNTPLHCAVEKNQ----IESVKFLLSRGANPNLRN-FNMMAPLH 161
Cdd:PHA02741 24 FFHEAARCGCFDIIARFTpfirGDCHAAALNATDDAGQMCIHIAAEKHEaqlaAEIIDHLIELGADINAQEmLEGDTALH 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767952011 162 IAVQGMNNEVMKVLLEHRTIDVNLEGENGNTAVIIACTTNNSEALQILLKKGAKPCK-SNKW 222
Cdd:PHA02741 104 LAAHRRDHDLAEWLCCQPGIDLHFCNADNKSPFELAIDNEDVAMMQILREIVATSRGfSNEN 165
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
103-211 |
3.67e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 47.97 E-value: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 103 LMEKITR-DSSLEVLHEMDDYGNTPLH---------------CAVEKNQIES------VKFLLSRGANPNLRNFNMMAPL 160
Cdd:PTZ00322 40 IQEEIARiDTHLEALEATENKDATPDHnltteevidpvvahmLTVELCQLAAsgdavgARILLTGGADPNCRDYDGRTPL 119
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 767952011 161 HIAVQGMNNEVMKVLLEHRTiDVNLEGENGNTAVIIACTTNNSEALQILLK 211
Cdd:PTZ00322 120 HIACANGHVQVVRVLLEFGA-DPTLLDKDGKTPLELAEENGFREVVQLLSR 169
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
507-616 |
5.03e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 47.29 E-value: 5.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 507 GMTPLHLAAKNGHDKVVQLLLKKGALFLSDHNGW-TALHHASMGGYTQTMKVILDTNLKCTDRLDEDGNTALHFAAREGH 585
Cdd:PHA02875 35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIeSELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKK 114
|
90 100 110
....*....|....*....|....*....|..
gi 767952011 586 AKAVALLLSHNADI-VLNKQQASFLHLALHNK 616
Cdd:PHA02875 115 LDIMKLLIARGADPdIPNTDKFSPLHLAVMMG 146
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
334-387 |
7.91e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 41.49 E-value: 7.91e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 767952011 334 HETMLHRASLFDHHELADYLISVGADINKIDSEGRSPLILATASASWNIVNLLL 387
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
572-599 |
9.67e-05 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 40.35 E-value: 9.67e-05
10 20
....*....|....*....|....*....
gi 767952011 572 DGNTALHFAA-REGHAKAVALLLSHNADI 599
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGADV 29
|
|
| PHA02989 |
PHA02989 |
ankyrin repeat protein; Provisional |
135-387 |
2.01e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222954 [Multi-domain] Cd Length: 494 Bit Score: 45.50 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 135 QIESVKFLLSRGANPNLRNFnMMAPLHIAVQGMN------NEVMKVLLEHrTIDVNLEGENGNTAV---IIACTTNNSEA 205
Cdd:PHA02989 49 KIKIVKLLIDNGADVNYKGY-IETPLCAVLRNREitsnkiKKIVKLLLKF-GADINLKTFNGVSPIvcfIYNSNINNCDM 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 206 LQILLKKGA--KPCKSNK-WGCFPIHQAAFSGSKECMEIILRFGEEHGYSRQLHinfmnngKATPLHLAVQNG----DLE 278
Cdd:PHA02989 127 LRFLLSKGInvNDVKNSRgYNLLHMYLESFSVKKDVIKILLSFGVNLFEKTSLY-------GLTPMNIYLRNDidviSIK 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 279 MIKMCLDNGAQIDPVEKGRCTAIH-FAATQGATEIVKLMISSYSGSVDIVNTTDGCHETMLHRASLFDHHELADYLISVG 357
Cdd:PHA02989 200 VIKYLIKKGVNIETNNNGSESVLEsFLDNNKILSKKEFKVLNFILKYIKINKKDKKGFNPLLISAKVDNYEAFNYLLKLG 279
|
250 260 270
....*....|....*....|....*....|
gi 767952011 358 ADINKIDSEGRSPLILATASASWNIVNLLL 387
Cdd:PHA02989 280 DDIYNVSKDGDTVLTYAIKHGNIDMLNRIL 309
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
190-243 |
2.29e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 39.95 E-value: 2.29e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 767952011 190 GNTAVIIACTTNNSEALQILLKKGAKPCKSNKWGCFPIHQAAFSGSKECMEIIL 243
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02791 |
PHA02791 |
ankyrin-like protein; Provisional |
483-615 |
2.35e-04 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165154 [Multi-domain] Cd Length: 284 Bit Score: 44.26 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 483 RINTCQ-RLLQDISDTRLLNEGDLHGMTPLHLAAKNGHDKVVQLLLKKGALFLSDHNGWtALHHASMGGYTQTMKVILDT 561
Cdd:PHA02791 5 RINTWKsKQLKSFLSSKDAFKADVHGHSALYYAIADNNVRLVCTLLNAGALKNLLENEF-PLHQAATLEDTKIVKILLFS 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 767952011 562 NLKcTDRLDEDGNTALHFAAREGHAKAVALLLSHNADIVLNKQ---QASFLHLALHN 615
Cdd:PHA02791 84 GMD-DSQFDDKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKtgwKTSFYHAVMLN 139
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
142-197 |
2.36e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 40.02 E-value: 2.36e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 767952011 142 LLSRG-ANPNLRNFNMMAPLHIAVQGMNNEVMKVLLEHRtIDVNLEGENGNTAVIIA 197
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYG-VDLNLKDEEGLTALDLA 56
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
122-150 |
2.41e-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: 39.16 E-value: 2.41e-04
10 20
....*....|....*....|....*....
gi 767952011 122 YGNTPLHCAVEKNQIESVKFLLSRGANPN 150
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
114-257 |
2.98e-04 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 44.66 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 114 EVLH------EMDDYGNTPLHCAVEKNQIESVKFLLSRGANPNLRNFNMMAPLHIaVQGMNNEVMKV--LLEHRTIDVNL 185
Cdd:PHA02946 57 ELLHrgyspnETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYY-LSGTDDEVIERinLLVQYGAKINN 135
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767952011 186 EGENGNTAVIIACTTNNSEALQILLKKGAKPCKSNKWGCFPIHQAAFSGSKECMEI--ILRFG-----EEHGYSRQLHI 257
Cdd:PHA02946 136 SVDEEGCGPLLACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNPKASTIswMMKLGispskPDHDGNTPLHI 214
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
573-621 |
3.16e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 39.57 E-value: 3.16e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 767952011 573 GNTALHFAAREGHAKAVALLLSHNADI-VLNKQQASFLHLALHNKRKEVV 621
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADInAVDGNGETALHFAASNGNVEVL 50
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
226-282 |
3.26e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 39.57 E-value: 3.26e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 767952011 226 PIHQAAFSGSKECMEIILrfgeEHGysrqLHINFMNNGKATPLHLAVQNGDLEMIKM 282
Cdd:pfam13637 4 ALHAAAASGHLELLRLLL----EKG----ADINAVDGNGETALHFAASNGNVEVLKL 52
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
506-531 |
3.26e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 38.78 E-value: 3.26e-04
10 20
....*....|....*....|....*.
gi 767952011 506 HGMTPLHLAAKNGHDKVVQLLLKKGA 531
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGA 26
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
466-528 |
3.36e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 44.89 E-value: 3.36e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767952011 466 SKSKDKKSPLHFAASYGRINTCQRLLQDISDTRLLnegDLHGMTPLHLAAKNGHDKVVQLLLK 528
Cdd:PTZ00322 110 CRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLL---DKDGKTPLELAEENGFREVVQLLSR 169
|
|
| PHA02736 |
PHA02736 |
Viral ankyrin protein; Provisional |
92-215 |
3.63e-04 |
|
Viral ankyrin protein; Provisional
Pssm-ID: 165103 [Multi-domain] Cd Length: 154 Bit Score: 42.17 E-value: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 92 LHYAAAEGQI-ELM--EKITRDSSLEVLHEMDDYGNTPLHCAVEKNQI---ESVKFLLSRGANPNLRN-FNMMAPLHIAV 164
Cdd:PHA02736 21 LHYLCRNGGVtDLLafKNAISDENRYLVLEYNRHGKQCVHIVSNPDKAdpqEKLKLLMEWGADINGKErVFGNTPLHIAV 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 767952011 165 QGMNNEVMKVLLEHRTIDVNLEGENGNTAVIIACTTNNSEALQILLKKGAK 215
Cdd:PHA02736 101 YTQNYELATWLCNQPGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGAQ 151
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
266-291 |
4.20e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 38.72 E-value: 4.20e-04
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
429-478 |
4.56e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 39.25 E-value: 4.56e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 767952011 429 ELVMDEDNDGCTPLHYACRQGGPGSVNNLLGFNVSIHSKSKDKKSPLHFA 478
Cdd:pfam13857 7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
572-599 |
4.78e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 38.34 E-value: 4.78e-04
10 20
....*....|....*....|....*...
gi 767952011 572 DGNTALHFAAREGHAKAVALLLSHNADI 599
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
79-279 |
6.07e-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: 43.85 E-value: 6.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 79 KKLKRCDDMDTF--------FLHYAAAEGQIE----LMEKITRDSSLEVLHEMddY-GNTPLHCAVEKNQIESVKFLLSR 145
Cdd:cd22192 34 KKLLKCPSCDLFqrgalgetALHVAALYDNLEaavvLMEAAPELVNEPMTSDL--YqGETALHIAVVNQNLNLVRELIAR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 146 GA---NPNlrnfnmmaplhiaVQGMnnevmkVLLEHRTidvNL--EGENgntAVIIACTTNNSEALQILLKKGAKPCKSN 220
Cdd:cd22192 112 GAdvvSPR-------------ATGT------FFRPGPK---NLiyYGEH---PLSFAACVGNEEIVRLLIEHGADIRAQD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767952011 221 KWGCFPIH----QAAFSGSKECMEIILRFGEEHGYSRQLHInfMNNGKATPLHLAVQNGDLEM 279
Cdd:cd22192 167 SLGNTVLHilvlQPNKTFACQMYDLILSYDKEDDLQPLDLV--PNNQGLTPFKLAAKEGNIVM 227
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
159-317 |
7.98e-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: 43.46 E-value: 7.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 159 PLHIAVQGMNNEVMKVLLEHRTIDVNLEGENGNTAVIIACTTNNSEALQILLKkgAKPCKSNKwgcfPIHQAAFSGSkec 238
Cdd:cd22192 20 PLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNE----PMTSDLYQGE--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 239 meiilrfgeehgysrqlhinfmnngkaTPLHLAVQNGDLEMIKMCLDNGAQidpVEKGRCTAIHF--------------- 303
Cdd:cd22192 91 ---------------------------TALHIAVVNQNLNLVRELIARGAD---VVSPRATGTFFrpgpknliyygehpl 140
|
170
....*....|....*.
gi 767952011 304 --AATQGATEIVKLMI 317
Cdd:cd22192 141 sfAACVGNEEIVRLLI 156
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
175-214 |
8.31e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 38.48 E-value: 8.31e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 767952011 175 LLEHRTIDVNLEGENGNTAVIIACTTNNSEALQILLKKGA 214
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGV 40
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
92-210 |
1.03e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 43.06 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 92 LHYAAAEGQIELMEKITRDSSLEVLHemDDYGNTPLHCAVEKNQIESVKFLLSRGANPNLRNFN-MMAPLHIAVQGMNNE 170
Cdd:PHA02875 139 LHLAVMMGDIKGIELLIDHKACLDIE--DCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNgCVAALCYAIENNKID 216
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 767952011 171 VMKVLLEhRTIDVNL----EGENGNTAVIIA--CTTNNSEALQILL 210
Cdd:PHA02875 217 IVRLFIK-RGADCNImfmiEGEECTILDMICnmCTNLESEAIDALI 261
|
|
| TRPV2 |
cd22197 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ... |
789-1022 |
1.15e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411981 [Multi-domain] Cd Length: 640 Bit Score: 42.92 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 789 TTNSYLIKTCMILVFLSSIFGYCkeaGQI--FQQKR----NYFMD-----------ISNVLEWIIYTTGIIFVLPLFVei 851
Cdd:cd22197 358 TAGGSMLLLGHILILLGGIYLLL---GQLwyFWRRRlfiwISFMDsyfeilfllqaLLTVLSQVLYFMGSEWYLPLLV-- 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 852 pahlqwqcgaIAVYFYWMNFLLYLQRFENCGIFIVMLE-VILKTLLRSTVVFIFLLLAFGLSFYIL-------------- 916
Cdd:cd22197 433 ----------FSLVLGWLNLLYYTRGFQHTGIYSVMIQkVILRDLLRFLLVYLVFLFGFAVALVSLsreapspkapednn 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 917 -------LNLQDPFSSPLLSIIQT------FSMMLGDINYRESFlepylrnELAHPVLSFaqLVSFTIFVPIVLMNLLIG 983
Cdd:cd22197 503 stvteqpTVGQEEEPAPYRSILDAslelfkFTIGMGELAFQEQL-------RFRGVVLLL--LLAYVLLTYVLLLNMLIA 573
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 767952011 984 LAVGDIAEVQKHA----SLKRIAMQVELHTSLekklpLWFLRK 1022
Cdd:cd22197 574 LMSETVNHVADNSwsiwKLQKAISVLEMENGY-----WWCRRK 611
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
261-304 |
1.20e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 38.10 E-value: 1.20e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 767952011 261 NNGKATPLHLAVQNGDLEMIKMCLDNGAQIDPVEKGRCTAIHFA 304
Cdd:pfam13857 13 DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
327-374 |
1.23e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 38.10 E-value: 1.23e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 767952011 327 VNTTDGCHETMLHRASLFDHHELADYLISVGADINKIDSEGRSPLILA 374
Cdd:pfam13857 9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
543-626 |
1.29e-03 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 42.96 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 543 LHHASMGGYTQTMKVILDTNLKCTDRlDEDGNTALHFAAREGHAKAVALLLSHNADI-VLNKQQASFLHLALHNKRKEVV 621
Cdd:PTZ00322 86 LCQLAASGDAVGARILLTGGADPNCR-DYDGRTPLHIACANGHVQVVRVLLEFGADPtLLDKDGKTPLELAEENGFREVV 164
|
....*
gi 767952011 622 LTIIR 626
Cdd:PTZ00322 165 QLLSR 169
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
119-184 |
1.79e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 42.17 E-value: 1.79e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767952011 119 MDDYGNTPLHCAVEK-NQIESVKFLLSRGANPNLRNFNM-MAPLHIAVQgmNNEVMKVLLEHRTiDVN 184
Cdd:PHA02878 230 RDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYILgLTALHSSIK--SERKLKLLLEYGA-DIN 294
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
266-291 |
1.80e-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: 1.80e-03
10 20
....*....|....*....|....*.
gi 767952011 266 TPLHLAVQNGDLEMIKMCLDNGAQID 291
Cdd:pfam13606 4 TPLHLAARNGRLEIVKLLLENGADIN 29
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
572-599 |
1.89e-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: 1.89e-03
10 20
....*....|....*....|....*...
gi 767952011 572 DGNTALHFAAREGHAKAVALLLSHNADI 599
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
123-243 |
2.67e-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: 42.05 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 123 GNTPLHCAVEKNQIESVKFLLSRGANPNLRN----FNMM----------APLHIAVQGMNNEVMKVLLEHRTIDVNLEGE 188
Cdd:cd22194 141 GQTALNIAIERRQGDIVKLLIAKGADVNAHAkgvfFNPKykhegfyfgeTPLALAACTNQPEIVQLLMEKESTDITSQDS 220
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 189 NGNTA----VIIActtNNSEAL---------QILLKKGAKPCK--SNKWGCFPIHQAAFSGSKECMEIIL 243
Cdd:cd22194 221 RGNTVlhalVTVA---EDSKTQndfvkrmydMILLKSENKNLEtiRNNEGLTPLQLAAKMGKAEILKYIL 287
|
|
| PLN03223 |
PLN03223 |
Polycystin cation channel protein; Provisional |
865-1014 |
2.74e-03 |
|
Polycystin cation channel protein; Provisional
Pssm-ID: 215637 [Multi-domain] Cd Length: 1634 Bit Score: 42.24 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 865 YFYW------MNFLLYLQRFENCGIFIVMLEVILKTLLRST-------VVFIFLLLAFGLSFYILLNLQDP-FSSPLLSI 930
Cdd:PLN03223 1287 YFQWymtlsgINIILLLGRILKLMDFQPRLGVITRTLWLAGadlmhffVIFGMVFVGYAFIGHVIFGNASVhFSDMTDSI 1366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 931 IQTFSMMLGDINYresFLEPyLRNelAHPVLSFAQLV---SFTIFVPIVLMNLLIGLAVGDIAEVQKHASlKRIAMQVEL 1007
Cdd:PLN03223 1367 NSLFENLLGDITY---FNED-LKN--LTGLQFVVGMIyfySYNIFVFMILFNFLLAIICDAFGEVKANAA-ETVSVHTEL 1439
|
....*..
gi 767952011 1008 HTSLEKK 1014
Cdd:PLN03223 1440 FPMLRDK 1446
|
|
| TRPV2 |
cd22197 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ... |
120-244 |
3.28e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411981 [Multi-domain] Cd Length: 640 Bit Score: 41.38 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 120 DDY--GNTPLHCAVEKNQIESVKFLLSRGANPNLRN--------------FNMMaPLHIAVQGMNNEVMKVLLEHRTIDV 183
Cdd:cd22197 89 DEYyrGHSALHIAIEKRSLQCVKLLVENGADVHARAcgrffqkkqgtcfyFGEL-PLSLAACTKQWDVVNYLLENPHQPA 167
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767952011 184 NLEGEN--GNTA----VIIACTTNNSEALQI-----LLKKGAKPCK-------SNKWGCFPIHQAAFSGSKECMEIILR 244
Cdd:cd22197 168 SLQAQDslGNTVlhalVMIADNSPENSALVIkmydgLLQAGARLCPtvqleeiSNHEGLTPLKLAAKEGKIEIFRHILQ 246
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
121-186 |
3.72e-03 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 41.42 E-value: 3.72e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767952011 121 DY-GNTPLHCAVEKNQIESVKFLLSRGANPNLRNFNMMAPLHIAVQGMNNEVMKVLLEHRTIDVNLE 186
Cdd:PTZ00322 112 DYdGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELG 178
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
321-388 |
4.05e-03 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 41.42 E-value: 4.05e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767952011 321 SGSVDiVNTTDGCHETMLHRASLFDHHELADYLISVGADINKIDSEGRSPLILATASASWNIVNLLLS 388
Cdd:PTZ00322 103 TGGAD-PNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
484-620 |
4.76e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 40.80 E-value: 4.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 484 INTCQRLLQDISDTRLLNEGDL------HGMTPLHLAAKNGHDKVVQLLLKKGA-LFLSDHNGWTALHHASMGGYTQTMK 556
Cdd:PHA03100 6 VLTKSRIIKVKNIKYIIMEDDLndysykKPVLPLYLAKEARNIDVVKILLDNGAdINSSTKNNSTPLHYLSNIKYNLTDV 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767952011 557 V----ILDTNLKCTDRLDEDGNTALHFAARE--GHAKAVALLLSHNADI-VLNKQQASFLHLALHNKRKEV 620
Cdd:PHA03100 86 KeivkLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVnIKNSDGENLLHLYLESNKIDL 156
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
440-491 |
5.61e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 36.10 E-value: 5.61e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 767952011 440 TPLHYACRQGGPGSVNNLLGFNVSIHSKSKDKKSPLHFAASYGRINTCQRLL 491
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
266-291 |
6.45e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 35.34 E-value: 6.45e-03
10 20
....*....|....*....|....*..
gi 767952011 266 TPLHLAV-QNGDLEMIKMCLDNGAQID 291
Cdd:pfam00023 4 TPLHLAAgRRGNLEIVKLLLSKGADVN 30
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
244-405 |
9.79e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 38.65 E-value: 9.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 244 RFGEEHGYSRQlhINFMNNGKATPLHLAVQNGDLEMIK--MCLDNGAQiDPVEkgrcTAIHFAATQ--GATEIVKLMISS 319
Cdd:PHA02859 3 KLCSEYDYNDF--TDYLFYRYCNPLFYYVEKDDIEGVKkwIKFVNDCN-DLYE----TPIFSCLEKdkVNVEILKFLIEN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952011 320 YSgsvDIVNTTDGCHETMLHRASLFDHH---ELADYLISVGADINKIDSEGRSPL--ILATASASWNIVNLLLSKGAQVD 394
Cdd:PHA02859 76 GA---DVNFKTRDNNLSALHHYLSFNKNvepEILKILIDSGSSITEEDEDGKNLLhmYMCNFNVRINVIKLLIDSGVSFL 152
|
170
....*....|.
gi 767952011 395 IKDNFGRNFLH 405
Cdd:PHA02859 153 NKDFDNNNILY 163
|
|
| |
