|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
47-343 |
7.03e-38 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 143.94 E-value: 7.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 47 LQNFNKQKKLKRCDDMDTFFLHYAAAEGQIELMEKITRDSSLEVLHEMDDYGNTPLHCAVEKNQIESVKFLLSRGANPNL 126
Cdd:COG0666 3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 127 RNFNMMAPLHIAVQGMNNEVMKVLLEHRtIDVNLEGENGNTAVIIACTTNNSEALQILLKKGAKPCKSNKWGCFPIHQAA 206
Cdd:COG0666 83 KDDGGNTLLHAAARNGDLEIVKLLLEAG-ADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 207 FSGSKECMEIILrfgeEHGysrqLHINFMNNGKATPLHLAVQNGDLEMIKMCLDNGAQIDPVEKGRCTAIHFAATQGATE 286
Cdd:COG0666 162 ANGNLEIVKLLL----EAG----ADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLE 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 116534990 287 IVKLMISSYsgsvDIVNTTDGCHETMLHRASLFDHHELADYLISVGADINKIDSEGR 343
Cdd:COG0666 234 IVKLLLEAG----ADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLL 286
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
229-519 |
7.68e-34 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 132.39 E-value: 7.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 229 QLHINFMNNGKATPLHLAVQNGDLEMIKMCLDNGAQIDPVEKGRCTAIHFAATQGATEIVKLMISSYsgsvDIVNTTDGC 308
Cdd:COG0666 44 LLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAG----ADVNARDKD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 309 HETMLHRASLFDHHELADYLISVGADINKIDSEGRSPLILATASASWNIVNLLLSKGAQVDIKDNFGRnflhltvqqpyg 388
Cdd:COG0666 120 GETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGE------------ 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 389 lknlrpefmqmqqikelvmdedndgcTPLHYACRQGGPGSVNNLLGFNVSIHSKSKDKKSPLHFAASYGRINTCQRLLQD 468
Cdd:COG0666 188 --------------------------TPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 116534990 469 ISDtrlLNEGDLHGMTPLHLAAKNGHDKVVQLLLKKGALFLSDHNGWTALH 519
Cdd:COG0666 242 GAD---LNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
230-581 |
2.17e-33 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 130.84 E-value: 2.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 230 LHINFMNNGKATPLHLAVQNGDLEMIKMCLDNGAQIDPVEKGRCTAIHFAATQGATEIVKLMISSysgsVDIVNTTDGCH 309
Cdd:COG0666 12 LAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAA----GADINAKDDGG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 310 ETMLHRASLFDHHELADYLISVGADINKIDSEGRSPLILATASASWNIVNLLLSKGAQVDIKDNFGRnflhltvqqpygl 389
Cdd:COG0666 88 NTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGN------------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 390 knlrpefmqmqqikelvmdedndgctplhyacrqggpgsvnnllgfnvsihskskdkkSPLHFAASYGRINTCQRLLQ-- 467
Cdd:COG0666 155 ----------------------------------------------------------TPLHLAAANGNLEIVKLLLEag 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 468 -DIsdtrllNEGDLHGMTPLHLAAKNGHDKVVQLLLKKGA-LFLSDHNGWTALHHASMGGYTQTMKVILDTNLKCTDRlD 545
Cdd:COG0666 177 aDV------NARDNDGETPLHLAAENGHLEIVKLLLEAGAdVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAK-D 249
|
330 340 350
....*....|....*....|....*....|....*.
gi 116534990 546 EDGNTALHFAAREGHAKAVALLLSHNADIVLNKQQA 581
Cdd:COG0666 250 KDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
322-615 |
5.80e-33 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 129.69 E-value: 5.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 322 HELADYLISVGADINKIDSEGRSPLILATASASWNIVNLLLSKGAQVDIKDNFGRNFLHLTVqqpygLKNLRPEFMQMQQ 401
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAA-----LAGDLLVALLLLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 402 IKELVMDEDNDGCTPLHYACRQGGPGSVNNLLGFNVSIHSKSKDKKSPLHFAASYGRINTCQRLLQ---DIsdtrllNEG 478
Cdd:COG0666 76 AGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEagaDV------NAQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 479 DLHGMTPLHLAAKNGHDKVVQLLLKKGA-LFLSDHNGWTALHHASMGGYTQTMKVILDTNLKCTDRlDEDGNTALHFAAR 557
Cdd:COG0666 150 DNDGNTPLHLAAANGNLEIVKLLLEAGAdVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAK-DNDGKTALDLAAE 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 116534990 558 EGHAKAVALLLSHNADIVL-NKQQASFLHLALHNKRKEVVLTIIRSKRWDECLKIFSHN 615
Cdd:COG0666 229 NGNLEIVKLLLEAGADLNAkDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
67-235 |
3.90e-24 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 103.88 E-value: 3.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 67 LHYAAAEGQIELMEK-ITRDSSLEVLhemDDYGNTPLHCAVEKNQIESVKFLLSRGANPNLRNFNMMAPLHIAVQGMNNE 145
Cdd:COG0666 124 LHLAAYNGNLEIVKLlLEAGADVNAQ---DNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLE 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 146 VMKVLLEHRtIDVNLEGENGNTAVIIACTTNNSEALQILLKKGAKPCKSNKWGCFPIHQAAFSGSKECMEIILRFGEEHG 225
Cdd:COG0666 201 IVKLLLEAG-ADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLA 279
|
170
....*....|
gi 116534990 226 YSRQLHINFM 235
Cdd:COG0666 280 AALLDLLTLL 289
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
486-577 |
1.24e-20 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 87.48 E-value: 1.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 486 LHLAAKNGHDKVVQLLLKKGA-LFLSDHNGWTALHHASMGGYTQTMKVILDTNLKctdRLDEDGNTALHFAAREGHAKAV 564
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGAdANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV---NLKDNGRTALHYAARSGHLEIV 77
|
90
....*....|...
gi 116534990 565 ALLLSHNADIVLN 577
Cdd:pfam12796 78 KLLLEKGADINVK 90
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
80-374 |
4.58e-20 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 94.35 E-value: 4.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 80 EKITRDSSLEVLHEMDDYGN-------TPLHCAVEKNQIESVKFLLSRGANPNLRNFNMMAPLHIAVQGMNNEvmkvlle 152
Cdd:PHA03100 10 SRIIKVKNIKYIIMEDDLNDysykkpvLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNL------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 153 hrtidvnlegengntaviiactTNNSEALQILLKKGAKPCKSNKWGCFPIHQAAfSGSKECMEIIlrfgeEHGYSRQLHI 232
Cdd:PHA03100 83 ----------------------TDVKEIVKLLLEYGANVNAPDNNGITPLLYAI-SKKSNSYSIV-----EYLLDNGANV 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 233 NFMNNGKATPLHLAVQNG--DLEMIKMCLDNGAQIDpvekgrctaihfaatqgATEIVKLMISSysgSVDIvNTTDGCHE 310
Cdd:PHA03100 135 NIKNSDGENLLHLYLESNkiDLKILKLLIDKGVDIN-----------------AKNRVNYLLSY---GVPI-NIKDVYGF 193
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116534990 311 TMLHRASLFDHHELADYLISVGADINKIDSEGRSPLILATASASWNIVNLLLSKGAQVDIKDNF 374
Cdd:PHA03100 194 TPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
95-364 |
9.39e-19 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 90.85 E-value: 9.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 95 DDYGNTPLH----CAVEKNQiESVKFLLSRGANPNLRNFNMMAPLHIAVQGMNNE-VMKVLLEHRTiDVNLEGENGNTAV 169
Cdd:PHA03095 44 GEYGKTPLHlylhYSSEKVK-DIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAGA-DVNAKDKVGRTPL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 170 IIACTTNNSEA--LQILLKKGAKPCKSNKWGCFPIHqaAFSGSKECMEIILRFGEEHGYSRQLHINFMNngkaTPLHLAV 247
Cdd:PHA03095 122 HVYLSGFNINPkvIRLLLRKGADVNALDLYGMTPLA--VLLKSRNANVELLRLLIDAGADVYAVDDRFR----SLLHHHL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 248 QN--GDLEMIKMCLDNGAQIDPVEKGRCTAIHFAATQG---ATEIVKLMISSYSgsvdiVNTTDGCHETMLHRASLFDHH 322
Cdd:PHA03095 196 QSfkPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSsckRSLVLPLLIAGIS-----INARNRYGQTPLHYAAVFNNP 270
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 116534990 323 ELADYLISVGADINKIDSEGRSPLILATASASWNIVNLLLSK 364
Cdd:PHA03095 271 RACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAK 312
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
233-507 |
4.35e-18 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 88.48 E-value: 4.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 233 NFMN---NGKATPLHLAVQNGDLEMIKMCLDNGAQIDPVEKGRCTAIHFAATQGATEIVKLMISSysgSVDI-------- 301
Cdd:PHA02874 26 NCINisvDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDN---GVDTsilpipci 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 302 --------------VNTTDGCHETMLHRASLFDHHELADYLISVGADINKIDSEGRSPLILATASASWNIVNLLLSKGAQ 367
Cdd:PHA02874 103 ekdmiktildcgidVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 368 VDIKDNFGRNFLHLTVQqpYGlknlrpefmQMQQIKEL------VMDEDNDGCTPLHYACRQGgpGSVNNLLGFNVSIHS 441
Cdd:PHA02874 183 ANVKDNNGESPLHNAAE--YG---------DYACIKLLidhgnhIMNKCKNGFTPLHNAIIHN--RSAIELLINNASIND 249
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116534990 442 KSKDKKSPLHFAASYgrinTCQRllqDISDTRLLNEGDL-----HGMTPLHLAAKN-GHDKVVQLLLKKGAL 507
Cdd:PHA02874 250 QDIDGSTPLHHAINP----PCDI---DIIDILLYHKADIsikdnKGENPIDTAFKYiNKDPVIKDIIANAVL 314
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
417-506 |
9.00e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 79.39 E-value: 9.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 417 LHYACRQGGPGSVNNLLGFNVSIHSKSKDKKSPLHFAASYGRINTCQRLLQDISdtrllNEGDLHGMTPLHLAAKNGHDK 496
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD-----VNLKDNGRTALHYAARSGHLE 75
|
90
....*....|
gi 116534990 497 VVQLLLKKGA 506
Cdd:pfam12796 76 IVKLLLEKGA 85
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
302-576 |
1.25e-17 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 87.39 E-value: 1.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 302 VNTTDGCHETMLHRASLFDHHELAD---YLISVGADINKIDSEGRSPLIL-ATASASWNIVNLLLSKGAQVDIKDNFGRN 377
Cdd:PHA03095 40 VNFRGEYGKTPLHLYLHYSSEKVKDivrLLLEAGADVNAPERCGFTPLHLyLYNATTLDVIKLLIKAGADVNAKDKVGRT 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 378 FLH--LTVqqpyglKNLRPEFmqmqqIKEL------VMDEDNDGCTPLHYACRQGG--PGSVNNLLGFNVSIHSKSKDKK 447
Cdd:PHA03095 120 PLHvyLSG------FNINPKV-----IRLLlrkgadVNALDLYGMTPLAVLLKSRNanVELLRLLIDAGADVYAVDDRFR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 448 SPLHFAASYGRINTC--QRLLQDISDTRLLNegdLHGMTPLHLAAKNGHDK---VVQLLLKKGALFLSDHNGWTALHHAS 522
Cdd:PHA03095 189 SLLHHHLQSFKPRARivRELIRAGCDPAATD---MLGNTPLHSMATGSSCKrslVLPLLIAGISINARNRYGQTPLHYAA 265
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 116534990 523 mgGYTQTM---KVI-LDTNLKCTdrlDEDGNTALHFAAREGHAKAVALLLSHNADIVL 576
Cdd:PHA03095 266 --VFNNPRacrRLIaLGADINAV---SSDGNTPLSLMVRNNNGRAVRAALAKNPSAET 318
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
74-349 |
2.88e-17 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 85.79 E-value: 2.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 74 GQIELMEKITRDSSlEVLHEMDDYGNTPLHCAVEKNQIESVKFLLSRGANPNLRNFNMMAPLHIAVQGMNNEVMKVLLEH 153
Cdd:PHA02874 12 GDIEAIEKIIKNKG-NCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 154 RT----------------------IDVNLEGENGNTAVIIACTTNNSEALQILLKKGAKPCKSNKWGCFPIHQAAFSGSK 211
Cdd:PHA02874 91 GVdtsilpipciekdmiktildcgIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFF 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 212 ECMEIILRFGEehgysrqlHINFMNNGKATPLHLAVQNGDLEMIKMCLDNGAQIDPVEKGRCTAIHFAATQGATeIVKLM 291
Cdd:PHA02874 171 DIIKLLLEKGA--------YANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRS-AIELL 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 116534990 292 ISSYSgsvdiVNTTDGCHETMLHRASLFD-HHELADYLISVGADINKIDSEGRSPLILA 349
Cdd:PHA02874 242 INNAS-----INDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTA 295
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
67-477 |
5.69e-17 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 86.27 E-value: 5.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 67 LHYAAAEGQIELM----EKITRDSSL--EVLHE-------MDDYGNTPLHCAVEKNQIESVKFLLSRGANPNLRNFNMMA 133
Cdd:PHA02876 134 IHYDKINESIEYMklikERIQQDELLiaEMLLEggadvnaKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLS 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 134 PLHIAVQGMNNEVMKVLLEHRTidvNLegeNGNTAVIIACTTNNSEALQILLkkgakpcksnkwgcfpiHQAAFSgskec 213
Cdd:PHA02876 214 VLECAVDSKNIDTIKAIIDNRS---NI---NKNDLSLLKAIRNEDLETSLLL-----------------YDAGFS----- 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 214 meiilrfgeehgysrqlhINFMNNGKATPLHLAVQNGDL-EMIKMCLDNGAQIDPVEKGRCTAIHFAATQG-ATEIVKLM 291
Cdd:PHA02876 266 ------------------VNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTL 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 292 ISSYSGsvdiVNTTDGCHETMLHRASLFDHH-ELADYLISVGADINKIDSEGRSPLILATASASWNIVNLLLSKGAQVDI 370
Cdd:PHA02876 328 IMLGAD----VNAADRLYITPLHQASTLDRNkDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEA 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 371 KDNFGRNFLHltvqqpYGLKNLRPeFMQMQQIKEL---VMDEDNDGCTPLHYACRQG-GPGSVNNLLGFNVSIHSKSKDK 446
Cdd:PHA02876 404 LSQKIGTALH------FALCGTNP-YMSVKTLIDRganVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQN 476
|
410 420 430
....*....|....*....|....*....|..
gi 116534990 447 KSPLHFAASY-GRINTCQRLLQDISDTRLLNE 477
Cdd:PHA02876 477 QYPLLIALEYhGIVNILLHYGAELRDSRVLHK 508
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
243-339 |
7.96e-17 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 76.69 E-value: 7.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 243 LHLAVQNGDLEMIKMCLDNGAQIDPVEKGRCTAIHFAATQGATEIVKLMISsysgSVDIVNTTDGchETMLHRASLFDHH 322
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE----HADVNLKDNG--RTALHYAARSGHL 74
|
90
....*....|....*..
gi 116534990 323 ELADYLISVGADINKID 339
Cdd:pfam12796 75 EIVKLLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
102-195 |
9.68e-17 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 76.31 E-value: 9.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 102 LHCAVEKNQIESVKFLLSRGANPNLRNFNMMAPLHIAVQGMNNEVMKVLLEHRTIDVNlegENGNTAVIIACTTNNSEAL 181
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLK---DNGRTALHYAARSGHLEIV 77
|
90
....*....|....
gi 116534990 182 QILLKKGAKPCKSN 195
Cdd:pfam12796 78 KLLLEKGADINVKD 91
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
98-313 |
2.83e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 82.35 E-value: 2.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 98 GNTPLHCAVEKNQIESVKFLLSRGANPNLRNFNMMAPLHIAVQGMNNEVMKVLLEHRTIDVNLEGENGNTAVIIACTTNN 177
Cdd:PHA02875 35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKK 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 178 SEALQILLKKGAKPCKSNKWGCFPIHQAAFSGSKECMEIILRfgeehgysRQLHINFMNNGKATPLHLAVQNGDLEMIKM 257
Cdd:PHA02875 115 LDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLID--------HKACLDIEDCCGCTPLIIAMAKGDIAICKM 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 116534990 258 CLDNGAQIDPVEKGRC-TAIHFAATQGATEIVKLMISSYSGSvDIVNTTDGCHETML 313
Cdd:PHA02875 187 LLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADC-NIMFMIEGEECTIL 242
|
|
| Ion_trans |
pfam00520 |
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ... |
796-972 |
7.59e-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: 78.08 E-value: 7.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 796 KRNYFMDISNVLEWIIyttgiifVLPLFVEIPAHLQWQCGAIAV--YFYWMNFLLYLQRFENCGIFIVMLEVILKTLLRS 873
Cdd:pfam00520 60 KKRYFRSPWNILDFVV-------VLPSLISLVLSSVGSLSGLRVlrLLRLLRLLRLIRRLEGLRTLVNSLIRSLKSLGNL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 874 TVVFIFLLLAFGLSFYILL-----NLQDP------FSSPLLSIIQTFSMMLGdINYRESFLEPYLRNelaHPVLSFAQLV 942
Cdd:pfam00520 133 LLLLLLFLFIFAIIGYQLFggklkTWENPdngrtnFDNFPNAFLWLFQTMTT-EGWGDIMYDTIDGK---GEFWAYIYFV 208
|
170 180 190
....*....|....*....|....*....|
gi 116534990 943 SFTIFVPIVLMNLLIGLAVGDIAEVQKHAS 972
Cdd:pfam00520 209 SFIILGGFLLLNLFIAVIIDNFQELTERTE 238
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
182-506 |
2.58e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 80.88 E-value: 2.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 182 QILLKKGAKPCKSNKWGCFPIHQAAFSGSKECMEIILRFGEEhgysrqlhINFMNNGKATPLHLAVQNGDLEMIKMCLDN 261
Cdd:PHA02876 162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGAD--------VNIIALDDLSVLECAVDSKNIDTIKAIIDN 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 262 GAQIDPVEKGRCTAIhfAATQGATEIVkLMISSYSgsvdiVNTTDGCHETMLHRASLFDH-HELADYLISVGADINKIDS 340
Cdd:PHA02876 234 RSNINKNDLSLLKAI--RNEDLETSLL-LYDAGFS-----VNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNI 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 341 EGRSPLILaTASASWNIVNL--LLSKGAQVDIKDNFGRNFLHltvqQPYGLKNLRPEFMQMQQIKELVMDEDNDGCTPLH 418
Cdd:PHA02876 306 KGETPLYL-MAKNGYDTENIrtLIMLGADVNAADRLYITPLH----QASTLDRNKDIVITLLELGANVNARDYCDKTPIH 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 419 YACRQGGPGSVNNLLGFNVSIHSKSKDKKSPLHFAASYGRINTCQRLLQDISDTrlLNEGDLHGMTPLHLAAKNG-HDKV 497
Cdd:PHA02876 381 YAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMSVKTLIDRGAN--VNSKNKDLSTPLHYACKKNcKLDV 458
|
....*....
gi 116534990 498 VQLLLKKGA 506
Cdd:PHA02876 459 IEMLLDNGA 467
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
105-336 |
9.69e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 77.72 E-value: 9.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 105 AVEKNQIESVKFLLSRGANPNLRNFNMMAPLHIAVQGMNNEVMKVLLEHRTI-DVNLEG---------ENGNTAVIIACT 174
Cdd:PHA02875 9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIpDVKYPDieselhdavEEGDVKAVEELL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 175 TNNSEALQILLKKGAKpcksnkwgcfPIHQAAFSGSKECMEIILRFGEEHGYSrqlhinfmNNGKATPLHLAVQNGDLEM 254
Cdd:PHA02875 89 DLGKFADDVFYKDGMT----------PLHLATILKKLDIMKLLIARGADPDIP--------NTDKFSPLHLAVMMGDIKG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 255 IKMCLDNGAQIDPVEKGRCTAIHFAATQGATEIVKLMISSySGSVDIVnTTDGChETMLHRASLFDHHELADYLISVGAD 334
Cdd:PHA02875 151 IELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDS-GANIDYF-GKNGC-VAALCYAIENNKIDIVRLFIKRGAD 227
|
..
gi 116534990 335 IN 336
Cdd:PHA02875 228 CN 229
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
347-627 |
4.06e-14 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 76.22 E-value: 4.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 347 ILATASASWNIVNLLLSKGAQVDIKDNFGRNFLHLtvqqpYGLKNLRPEfmqmQQIKELVMDEDND-------GCTPLH- 418
Cdd:PHA03095 19 LLNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHL-----YLHYSSEKV----KDIVRLLLEAGADvnapercGFTPLHl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 419 YACRQGGPGSVNNLLGFNVSIHSKSKDKKSPLHFAASYGRINTCQRLLqdisdtrLLNEG------DLHGMTPLH--LAA 490
Cdd:PHA03095 90 YLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVYLSGFNINPKVIRL-------LLRKGadvnalDLYGMTPLAvlLKS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 491 KNGHDKVVQLLLKKGA-LFLSDHNGWTALHHasMGGYTQTMKVILDTN--LKCTDR-LDEDGNTALHFAAREGHAKA--V 564
Cdd:PHA03095 163 RNANVELLRLLIDAGAdVYAVDDRFRSLLHH--HLQSFKPRARIVRELirAGCDPAaTDMLGNTPLHSMATGSSCKRslV 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116534990 565 ALLLSHNADI-VLNKQQASFLHLAlhnkrkevvlTIIRSKR-WDECLKI---FSHNSPGNKCPITEMI 627
Cdd:PHA03095 241 LPLLIAGISInARNRYGQTPLHYA----------AVFNNPRaCRRLIALgadINAVSSDGNTPLSLMV 298
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
252-506 |
8.39e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 75.09 E-value: 8.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 252 LEMIKMCLDNGAQIDPVEKGRCTAIHFAATQGATEIVKLMISSysgSVDIVNTTDGcHETMLHRASLFDHH-----ELAD 326
Cdd:PHA03100 15 VKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDN---GADINSSTKN-NSTPLHYLSNIKYNltdvkEIVK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 327 YLISVGADINKIDSEGRSPLILA--TASASWNIVNLLLSKGAQVDIKDNFGRNFLHLTVQQPYGLKNlrpefmqmqqIKE 404
Cdd:PHA03100 91 LLLEYGANVNAPDNNGITPLLYAisKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLK----------ILK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 405 LVMDE--DNDGCTplhyacrqggpgSVNNLLGFNVSIHSKSKDKKSPLHFAASYGRINTCQRLLQDISDTRLLNEgdlHG 482
Cdd:PHA03100 161 LLIDKgvDINAKN------------RVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNK---YG 225
|
250 260
....*....|....*....|....
gi 116534990 483 MTPLHLAAKNGHDKVVQLLLKKGA 506
Cdd:PHA03100 226 DTPLHIAILNNNKEIFKLLLNNGP 249
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
170-266 |
1.98e-13 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 67.06 E-value: 1.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 170 IIACTTNNSEALQILLKKGAKPCKSNKWGCFPIHQAAFSGSKECMEIILRFGeehgysrqlHINFMNNGKaTPLHLAVQN 249
Cdd:pfam12796 2 HLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA---------DVNLKDNGR-TALHYAARS 71
|
90
....*....|....*..
gi 116534990 250 GDLEMIKMCLDNGAQID 266
Cdd:pfam12796 72 GHLEIVKLLLEKGADIN 88
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
438-997 |
3.29e-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: 73.76 E-value: 3.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 438 SIHSKSKDKKSPLHFAASY--GRINTCQRLLQDI-----SDTRLLNEGDL----HGMTPLHLAAKNGHDKVVQLLLKKGA 506
Cdd:cd21882 18 SAYQRGATGKTCLHKAALNlnDGVNEAIMLLLEAapdsgNPKELVNAPCTdefyQGQTALHIAIENRNLNLVRLLVENGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 507 LFLSDHNGWTALHHASMGGYTqtmkvildtnlkctdrldedGNTALHFAAREGHAKAVALLLSHNADIVLNKQQASF--- 583
Cdd:cd21882 98 DVSARATGRFFRKSPGNLFYF--------------------GELPLSLAACTNQEEIVRLLLENGAQPAALEAQDSLgnt 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 584 -LHLALHNKRKEVVLTIIRSKRWDECLKIFSHNSPgnkcpiTEMIEYLPEcMKVLLDFcMLHSTEDKSCRDYYI---EYN 659
Cdd:cd21882 158 vLHALVLQADNTPENSAFVCQMYNLLLSYGAHLDP------TQQLEEIPN-HQGLTPL-KLAAVEGKIVMFQHIlqrEFS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 660 FKYLQCPLEFTKKT--PTQDVIYEpLTALNAMVQNNRIE--------------LLNHPVcKEYLLMKWLAYGFRAHMMNL 723
Cdd:cd21882 230 GPYQPLSRKFTEWTygPVTSSLYD-LSEIDSWEKNSVLEliafskkrearhqmLVQEPL-NELLQEKWDRYGRPYFCFNF 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 724 GSYCLGLIPMTILVVNiKPgmafnstgiINETSDHSEILDTTNSYLIKTCMILVFLSSIFGYCKEAGQIFQQKRNYFMDI 803
Cdd:cd21882 308 ACYLLYMIIFTVCAYY-RP---------LKDRPANQEAKATFGDSIRLVGEILTVLGGVYILLGEIPYFFRRRLSRWFGF 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 804 SNVLEWIIYTTGIIFVLPLFVEIPAHLQWQCGAI--AVYFYWMNFLLYLQRFENCGIFIVMLE-VILKTLLRSTVVFIFL 880
Cdd:cd21882 378 LDSYFEILFITQALLVLLSMVLRFMETEGYVVPLvfSLVLGWCNVLYYTRGFQMLGIYTVMIQkMILRDLMRFCWVYLVF 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 881 LLAFGLSFYILLNLQDP-----FSSPLLSIIQTFSMMLG--DINYRESflepylrneLAHPVLSFAQLVSFTIFVPIVLM 953
Cdd:cd21882 458 LFGFASAFVILFQTEDPnklgeFRDYPDALLELFKFTIGmgDLPFNEN---------VDFPFVYLILLLAYVILTYLLLL 528
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 116534990 954 NLLIGL---AVGDIAEVQKHA-SLKRIAMQVElhtsLEKKLPlWFLRK 997
Cdd:cd21882 529 NMLIALmgeTVNRVAQESDEIwKLQKAITTLM----LERKYP-RCLRK 571
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
692-997 |
4.16e-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: 73.64 E-value: 4.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 692 NNRIELLNHPVCKEYLLMKWLAygFRAHMMNLgSYCLGLIPMTILVVnikpgMAFNSTGIiNETSDHSEILDTTNSYLIK 771
Cdd:cd22194 340 DNRHEMLTLEPLHTLLHMKWKK--FARYMFFI-SFLFYFFYNITLTL-----VSYYRPRE-DEDPPHPLALSHKMGWLQL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 772 TCMILVFLSSIFGYCKEAGQIFQQKRNyfmDISNVLE--WIIYTTGIIFVLPLFVEIPAHLQWQ----CGAIAVYFYWMN 845
Cdd:cd22194 411 LGQMFVLIWATCLSVKEGIAIFLLRPS---DLKSILSdaWFHILFFIQAVLVIVSVFLYLFAYKeylaCLVLAMALGWAN 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 846 FLLYLQRFENCGIFIVMLE-VILKTLLRSTVVFIFLLLAFGLSFYILLN-LQD-----PFSSPLLSIIQTFSMM--LGDI 916
Cdd:cd22194 488 MLYYTRGFQSLGIYSVMIQkVILNDVLKFLLVYILFLLGFGVALASLIEdCPDdsecsSYGSFSDAVLELFKLTigLGDL 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 917 NyresflepyLRNELAHPVLSFAQLVSFTIFVPIVLMNLLIGLAVGDIAEVQKHAS----LKRiAMQVelhTSLEKKLPL 992
Cdd:cd22194 568 E---------IQQNSKYPILFLLLLITYVILTFVLLLNMLIALMGETVENVSKESEriwrLQR-ARTI---LEFEKSLPE 634
|
....*
gi 116534990 993 WFLRK 997
Cdd:cd22194 635 WLRKR 639
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
101-467 |
4.53e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 72.99 E-value: 4.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 101 PLHCAVEKNQIESVKFLLSRGANPNLRNFNMMAPLHIAVQGMNNEVMKVLLEHRTIDvnlegENGNTAVII--ACTTNNS 178
Cdd:PHA02878 40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKC-----SVFYTLVAIkdAFNNRNV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 179 EALQILLkkgakpcksnkwgcfpihqaaFSGSKECMEIILRFGEEHGYSRQLhinfmnngkatplhlavqngDLEMIKMC 258
Cdd:PHA02878 115 EIFKIIL---------------------TNRYKNIQTIDLVYIDKKSKDDII--------------------EAEITKLL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 259 LDNGAQIDPVEKGR-CTAIHFAATQGATEIVKLMIsSYSGSvdiVNTTDGCHETMLHRASLFDHHELADYLISVGADINK 337
Cdd:PHA02878 154 LSYGADINMKDRHKgNTALHYATENKDQRLTELLL-SYGAN---VNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 338 IDSEGRSPLILATASA-SWNIVNLLLSKGAQVDIKDNFgRNF--LHLTVQQPYGLKNLrpefmqmQQIKELVMDEDNDGC 414
Cdd:PHA02878 230 RDKCGNTPLHISVGYCkDYDILKLLLEHGVDVNAKSYI-LGLtaLHSSIKSERKLKLL-------LEYGADINSLNSYKL 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 116534990 415 TPLHYACRQGGPGSVNNLLGFNVSIHS-KSKDKKSPLHFAASYGRINTCQRLLQ 467
Cdd:PHA02878 302 TPLSSAVKQYLCINIGRILISNICLLKrIKPDIKNSEGFIDNMDCITSNKRLNQ 355
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
276-372 |
5.26e-13 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 65.91 E-value: 5.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 276 IHFAATQGATEIVKLMISSYSGsvdiVNTTDGCHETMLHRASLFDHHELADYLISVgADINKIDsEGRSPLILATASASW 355
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGAD----ANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHL 74
|
90
....*....|....*..
gi 116534990 356 NIVNLLLSKGAQVDIKD 372
Cdd:pfam12796 75 EIVKLLLEKGADINVKD 91
|
|
| TRPV1-4 |
cd22193 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ... |
673-997 |
1.02e-12 |
|
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: 72.14 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 673 TPTQDVIYEpLTALNAMVQNNRIELLNHPVcKEYLLMKWLAYGFRAHMMNLGSYCLGLIPMTiLVVNIKPgmafnstgiI 752
Cdd:cd22193 264 TCEKNSVLE-IIVYNSKIDNRHEMLTLEPL-NTLLQDKWDKFAKYMFFFSFCFYLFYMIIFT-LVAYYRP---------R 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 753 NETSDHSEILDTTNSYLIKTCMILVFLSSIFGYCKEAgQIFQQKR----NYFMDISNVLEWIIYTTGIIFVLPL-FVEIP 827
Cdd:cd22193 332 EDEPPPPLAKTTKMDYMRLLGEILVLLGGVYFFVKEI-AYFLLRRsdlqSSFSDSYFEILFFVQAVLVILSVVLyLFAYK 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 828 AHLQwqCGAIAVYFYWMNFLLYLQRFENCGIFIVMLE-VILKTLLRSTVVFIFLLLAFGLSFYILLN-------LQDPFS 899
Cdd:cd22193 411 EYLA--CLVLALALGWANMLYYTRGFQSMGIYSVMIQkVILRDLLRFLFVYLLFLFGFAVALVSLIEkcssdkkDCSSYG 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 900 SPLLSIIQTFSMM--LGDINYRESflepylrneLAHPVLSFAQLVSFTIFVPIVLMNLLIGLAVGDIAEVQKHAslKRIA 977
Cdd:cd22193 489 SFSDAVLELFKLTigMGDLEFQEN---------STYPAVFLILLLTYVILTFVLLLNMLIALMGETVNNVSKES--KRIW 557
|
330 340
....*....|....*....|.
gi 116534990 978 MQVELHTSLE-KKLPLWFLRK 997
Cdd:cd22193 558 KLQRAITILEfEKSFPECMRK 578
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
320-639 |
2.34e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 71.25 E-value: 2.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 320 DHHELADYLISVGADINKIDSEGRSPLILATASASWNIVNLLLSKGAQVDIKDNFGRNFLHLTVQQpyglKNLrpefmqm 399
Cdd:PHA02876 156 DELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDS----KNI------- 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 400 QQIKELVMDEDNDGCTPLHYACRQGGPGSVNNLLGFNVSIHSKSKD--KKSPLHFAA---SYGRIntCQRLLQDISDtrl 474
Cdd:PHA02876 225 DTIKAIIDNRSNINKNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDdcKNTPLHHASqapSLSRL--VPKLLERGAD--- 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 475 LNEGDLHGMTPLHLAAKNGHD-KVVQLLLKKGA-LFLSDHNGWTALHHAS-MGGYTQTMKVILD--TNLKCTDRLDEdgn 549
Cdd:PHA02876 300 VNAKNIKGETPLYLMAKNGYDtENIRTLIMLGAdVNAADRLYITPLHQAStLDRNKDIVITLLElgANVNARDYCDK--- 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 550 TALHFAAREGHAKAVALLLSHNADI-VLNKQQASFLHLALH--NKRKEVVLTIIRSKRWDECLKIFS---HNSPGNKCPi 623
Cdd:PHA02876 377 TPIHYAAVRNNVVIINTLLDYGADIeALSQKIGTALHFALCgtNPYMSVKTLIDRGANVNSKNKDLStplHYACKKNCK- 455
|
330
....*....|....*.
gi 116534990 624 temieylPECMKVLLD 639
Cdd:PHA02876 456 -------LDVIEMLLD 464
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
415-993 |
3.16e-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: 70.81 E-value: 3.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 415 TPLHYACRQGGPGSVNNLLGFN-VSIHSKSKDKKSPLHFAASYGRINTCQRLLQdiSDTRLLNE---GDLH-GMTPLHLA 489
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLLKCPsCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNEpmtSDLYqGETALHIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 490 AKNGHDKVVQLLLKKGALFLSDHNGWTALHhasmggytqtmkvildtnlKCTDRLDEDGNTALHFAAREGHAKAVALLLS 569
Cdd:cd22192 97 VVNQNLNLVRELIARGADVVSPRATGTFFR-------------------PGPKNLIYYGEHPLSFAACVGNEEIVRLLIE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 570 HNADIvlnKQQASF----LH-LALHNKRK------EVVLTIIRSKRwDECLKIFSHN---SP-------GNkcpiTEMIE 628
Cdd:cd22192 158 HGADI---RAQDSLgntvLHiLVLQPNKTfacqmyDLILSYDKEDD-LQPLDLVPNNqglTPfklaakeGN----IVMFQ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 629 YLpecMKvlldfcmlhstedkscRDYYIEYNFKYLQCPLEFTKKTPTQDviyEPLTALNAMVQNNRIELLN----HPVcK 704
Cdd:cd22192 230 HL---VQ----------------KRRHIQWTYGPLTSTLYDLTEIDSWG---DEQSVLELIVSSKKREARKildvTPV-K 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 705 EYLLMKWLAYGFRAHMMNLGSYCLGLIPMTILVVN----IKPGMAFNSTGI---INETSDHSEIldTTNSYLIKTCMILV 777
Cdd:cd22192 287 ELVSLKWKRYGRPYFRILALLYLLYIIIFTLCCVYrplkPRPENNTDPRDItlyVQKTLQESYV--TPKDYLRLVGELIS 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 778 FLSSIFGYCKEAGQIFQ--QKRnYFMD--ISNVLEWIIYTTGI-IFVLPLFVEIPAHLQWQCGAIAVYFYWMNFLLYLQR 852
Cdd:cd22192 365 VLGAIVILLLEIPDILRvgVKR-YFGQtvLGGPFHVIIITYAClVLLTLVLRLTSLSGEVVPMSLALVLGWCNVMYFARG 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 853 FENCGIFIVMLE-VILKTLLRSTVVFIFLLLAFGLSFYILLNLQDP-----FSSPLLSIIQTFSMMLGDINYresflepY 926
Cdd:cd22192 444 FQMLGPFTIMIQkIIFGDLMKFCWLMFVVILGFSSAFYMIFQTEDPdslghFYDFPMTLFSTFELFLGLIDG-------P 516
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116534990 927 LRNELAHPVLSFAQLVSFTIFVPIVLMNLLIGLaVGDiaevqkhaSLKRIA--------MQVELHT-SLEKKLP--LW 993
Cdd:cd22192 517 ANYTVDLPFMYKVLYTAFAVIAYLLMLNLLIAM-MGD--------THWRVAherdelwrAQVVATTlMLERRLPrcLW 585
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
345-574 |
5.65e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 65.84 E-value: 5.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 345 PLILATASASWNIVNLLLSKGAQVDIKDNFGRNFLHLTVQQPYGLKNLRPEFMQMQQIKELVMDEDNDGCTPLHYA--CR 422
Cdd:PHA03100 38 PLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAisKK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 423 QGGPGSVNNLLGFNVSIHSKSKDKKSPLHFAASYGRINT--CQRLLQDISD----TRL---------LNEGDLHGMTPLH 487
Cdd:PHA03100 118 SNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkiLKLLIDKGVDinakNRVnyllsygvpINIKDVYGFTPLH 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 488 LAAKNGHDKVVQLLLKKGAlflsdhngwtalhhasmggytqtmkvilDTNLKctdrlDEDGNTALHFAAREGHAKAVALL 567
Cdd:PHA03100 198 YAVYNNNPEFVKYLLDLGA----------------------------NPNLV-----NKYGDTPLHIAILNNNKEIFKLL 244
|
....*..
gi 116534990 568 LSHNADI 574
Cdd:PHA03100 245 LNNGPSI 251
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
135-223 |
6.75e-11 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 59.74 E-value: 6.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 135 LHIAVQGMNNEVMKVLLEHRTiDVNLEGENGNTAVIIACTTNNSEALQILLKKGAKPCKSNkwGCFPIHQAAFSGSKECM 214
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGA-DANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN--GRTALHYAARSGHLEIV 77
|
....*....
gi 116534990 215 EIILRFGEE 223
Cdd:pfam12796 78 KLLLEKGAD 86
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
67-160 |
7.81e-11 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 59.36 E-value: 7.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 67 LHYAAAEGQIELMEKItrdssLEVLHEM---DDYGNTPLHCAVEKNQIESVKFLLSRgANPNLRNFNmMAPLHIAVQGMN 143
Cdd:pfam12796 1 LHLAAKNGNLELVKLL-----LENGADAnlqDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG-RTALHYAARSGH 73
|
90
....*....|....*..
gi 116534990 144 NEVMKVLLEHrTIDVNL 160
Cdd:pfam12796 74 LEIVKLLLEK-GADINV 89
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
313-442 |
3.65e-10 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 57.82 E-value: 3.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 313 LHRASLFDHHELADYLISVGADINKIDSEGRSPLILATASASWNIVNLLLSKGAQvdikdnfgrnflhltvqqpyglknl 392
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV------------------------- 55
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 116534990 393 rpefmqmqqikelvmDEDNDGCTPLHYACRQGGPGSVNNLLGFNVSIHSK 442
Cdd:pfam12796 56 ---------------NLKDNGRTALHYAARSGHLEIVKLLLEKGADINVK 90
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
96-247 |
8.08e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 62.59 E-value: 8.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 96 DYGNTPLHCAVEKNQIESVKFLLSRGANPNLRNFNMMAPLHIAVQGMNNEVMKVLLEHRTiDVNLEGENGNTAVIIACTT 175
Cdd:PHA02878 166 HKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA-STDARDKCGNTPLHISVGY 244
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116534990 176 -NNSEALQILLKKGAK-PCKSNKWGCFPIHQAAFSGSKecMEIILRFGEEhgysrqlhINFMNNGKATPLHLAV 247
Cdd:PHA02878 245 cKDYDILKLLLEHGVDvNAKSYILGLTALHSSIKSERK--LKLLLEYGAD--------INSLNSYKLTPLSSAV 308
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
95-166 |
8.49e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 62.38 E-value: 8.49e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116534990 95 DDYGNTPLHCAVEKNQIESVKFLLSRGANPNLRNFNMMAPLHIAVQGMNNEVMKVLLEHR----TIDVNLEGENGN 166
Cdd:PHA03100 189 DVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGpsikTIIETLLYFKDK 264
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
67-128 |
1.11e-09 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 56.28 E-value: 1.11e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116534990 67 LHYAAAEGQIE----LMEKITRDsslevlheMDDYGNTPLHCAVEKNQIESVKFLLSRGANPNLRN 128
Cdd:pfam12796 34 LHLAAKNGHLEivklLLEHADVN--------LKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
309-506 |
4.99e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 60.00 E-value: 4.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 309 HETMLHRASLFDHHELADYLISVGADINKIDSEGRSPLILATASASWNIVNLLLSKGAQVDIKDNFGRNFLHLTVQQPyg 388
Cdd:PHA02875 2 DQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEG-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 389 lknlrpefmQMQQIKELVMDED-------NDGCTPLHYACRQGGPGSVNNLLGFNVSIHSKSKDKKSPLHFAASYGRINT 461
Cdd:PHA02875 80 ---------DVKAVEELLDLGKfaddvfyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKG 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 116534990 462 CQRLLQDISDTRLlneGDLHGMTPLHLAAKNGHDKVVQLLLKKGA 506
Cdd:PHA02875 151 IELLIDHKACLDI---EDCCGCTPLIIAMAKGDIAICKMLLDSGA 192
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
334-959 |
6.13e-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: 60.09 E-value: 6.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 334 DINKIDSEGRSPLILAtASASWN--IVNLLLSKGAQVDIkdnfGRNFLHLTVQQPYGLKN---LRPEFMQMQQIK-ELVM 407
Cdd:TIGR00870 44 NINCPDRLGRSALFVA-AIENENleLTELLLNLSCRGAV----GDTLLHAISLEYVDAVEailLHLLAAFRKSGPlELAN 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 408 DEDND----GCTPLHYACRQGGPGSVNNLL--GFNVSIHSKSKD-KKSPLHFAASYGRintcqrllqdisdtrllnegdl 480
Cdd:TIGR00870 119 DQYTSeftpGITALHLAAHRQNYEIVKLLLerGASVPARACGDFfVKSQGVDSFYHGE---------------------- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 481 hgmTPLHLAAKNGHDKVVQLLLKKGALFLS-DHNGWTALHHASM--------GGYTQTMK---VILDTNLKCTDRLDE-- 546
Cdd:TIGR00870 177 ---SPLNAAACLGSPSIVALLSEDPADILTaDSLGNTLLHLLVMenefkaeyEELSCQMYnfaLSLLDKLRDSKELEVil 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 547 --DGNTALHFAAREGhakavalllshnadivlnKQQASFLHLALHNKRKEVVltiirskrwdeclkiFSHNSPgnkcpit 624
Cdd:TIGR00870 254 nhQGLTPLKLAAKEG------------------RIVLFRLKLAIKYKQKKFV---------------AWPNGQ------- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 625 emieylpecmkvlldfcMLHSTEDKSCRDyyieynfkylqcplEFTKKTPTQDVIYepLTALNAMVQNNRIELLNHPvCK 704
Cdd:TIGR00870 294 -----------------QLLSLYWLEELD--------------GWRRKQSVLELIV--VFVIGLKFPELSDMYLIAP-LS 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 705 EYLLMKWLAYGFRAHMMNLGSYCLGLIPMTILVVnIKPGMAFNSTGIINETSDHSEILdTTNSYLIKTCMILVFLSSIFG 784
Cdd:TIGR00870 340 RLGQFKWKPFIKFIFHSASYLYFLYLIIFTSVAY-YRPTRTDLRVTGLQQTPLEMLIV-TWVDGLRLGEEKLIWLGGIFE 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 785 YCKEAGQIFQQKRNYFMDISNVL---EWIIYTTGIIFVLPLFVEIPAHLqWQCG--AIAVYFYWMNFLLYLQRFENCGIF 859
Cdd:TIGR00870 418 YIHQLWNILDFGMNSFYLATFLDrpfAILFVTQAFLVLREHWLRFDPTL-IEEAlfAFALVLSWLNLLYIFRGNQHLGPL 496
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 860 IVMLE-VILKTLLRSTVVFIFLLLAFGLSFYILLNLQDPFSSPLLS---------IIQTFSMMLgdinyrESFLE----- 924
Cdd:TIGR00870 497 QIMIGrMILGDILRFLFIYAVVLFGFACGLNQLYQYYDELKLNECSnpharscekQGNAYSTLF------ETSQElfwai 570
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 116534990 925 ----PYLRNELAH-PVLSFAQLVSFTIFVPIVLMNLLIGL 959
Cdd:TIGR00870 571 iglgDLLANEHKFtEFVGLLLFGAYNVIMYILLLNMLIAM 610
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
335-599 |
1.09e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 58.82 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 335 INKIDSEGRSPLILATASASWNIVNLLLSKGAQVDikdnfgrnflHLTVQQPYGLknLRPEFMQMQQIKELVMDEDNDgC 414
Cdd:PHA02874 28 INISVDETTTPLIDAIRSGDAKIVELFIKHGADIN----------HINTKIPHPL--LTAIKIGAHDIIKLLIDNGVD-T 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 415 TPLHYACRQGGpgSVNNLLGFNVSIHSKSKDKKSPLHFAASYGRINTCQRLLQDISDtrlLNEGDLHGMTPLHLAAKNGH 494
Cdd:PHA02874 95 SILPIPCIEKD--MIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGAD---VNIEDDNGCYPIHIAIKHNF 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 495 DKVVQLLLKKGALflsdhngwtalhhasmggytqtmkvildTNLKctdrlDEDGNTALHFAAREGHAKAVALLLSHNADI 574
Cdd:PHA02874 170 FDIIKLLLEKGAY----------------------------ANVK-----DNNGESPLHNAAEYGDYACIKLLIDHGNHI 216
|
250 260
....*....|....*....|....*..
gi 116534990 575 vLNKQQASF--LHLALHNKRKEVVLTI 599
Cdd:PHA02874 217 -MNKCKNGFtpLHNAIIHNRSAIELLI 242
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
66-218 |
1.26e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 58.82 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 66 FLHYAAAEGQIELMEKITR---DSSLEvlhemDDYGNTPLHCAVEKNQIESVKFLLSRGANPNLRNFNMMAPLHIAVQGM 142
Cdd:PHA02874 127 FLHYAIKKGDLESIKMLFEygaDVNIE-----DDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYG 201
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116534990 143 NNEVMKVLLEHrTIDVNLEGENGNTAVIIACTTNNSeALQILLKKgAKPCKSNKWGCFPIHQA-AFSGSKECMEIIL 218
Cdd:PHA02874 202 DYACIKLLIDH-GNHIMNKCKNGFTPLHNAIIHNRS-AIELLINN-ASINDQDIDGSTPLHHAiNPPCDIDIIDILL 275
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
482-534 |
1.83e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 51.51 E-value: 1.83e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 116534990 482 GMTPLHLAAKNGHDKVVQLLLKKGA-LFLSDHNGWTALHHASMGGYTQTMKVIL 534
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGAdINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
514-568 |
3.36e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 50.74 E-value: 3.36e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 116534990 514 GWTALHHASMGGYTQTMKVILDTNLKCtDRLDEDGNTALHFAAREGHAKAVALLL 568
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADI-NAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
241-292 |
4.83e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 50.35 E-value: 4.83e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 116534990 241 TPLHLAVQNGDLEMIKMCLDNGAQIDPVEKGRCTAIHFAATQGATEIVKLMI 292
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
478-575 |
7.51e-08 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 56.80 E-value: 7.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 478 GDLHGMTPLHLAAKNGHDKVVQLLLKKGA-LFLSDHNGWTAL-------HH------------------------ASMGG 525
Cdd:PLN03192 554 GDSKGRTPLHIAASKGYEDCVLVLLKHACnVHIRDANGNTALwnaisakHHkifrilyhfasisdphaagdllctAAKRN 633
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 116534990 526 YTQTMKVILDTNLKcTDRLDEDGNTALHFAAREGHAKAVALLLSHNADIV 575
Cdd:PLN03192 634 DLTAMKELLKQGLN-VDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVD 682
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
241-386 |
1.55e-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: 55.40 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 241 TPLHLAVQNGDLEMIKMCLDNgAQIDPVEKGRC--TAIHFAATQGATEIVKLMISSYSGSVDIVNTTD---GchETMLHR 315
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLLKC-PSCDLFQRGALgeTALHVAALYDNLEAAVVLMEAAPELVNEPMTSDlyqG--ETALHI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 316 ASLFDHHELADYLISVGADINKIDSEG--------------RSPLILATASASWNIVNLLLSKGAQVDIKDNFGRNFLHL 381
Cdd:cd22192 96 AVVNQNLNLVRELIARGADVVSPRATGtffrpgpknliyygEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175
|
....*
gi 116534990 382 TVQQP 386
Cdd:cd22192 176 LVLQP 180
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
105-427 |
1.66e-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: 55.47 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 105 AVEKNQIESVKfllSRGANPNLRNFNMMAPL------HIAVQGMNNEVMKVLLEHrtidvNLEGENGNTAVIIACTT--- 175
Cdd:TIGR00870 24 AAERGDLASVY---RDLEEPKKLNINCPDRLgrsalfVAAIENENLELTELLLNL-----SCRGAVGDTLLHAISLEyvd 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 176 NNSEALQILLKKGAKpcksnkwGCFPIHQAAFSGSkecmeiilRFGEEHgysrqlhinfmnngkaTPLHLAVQNGDLEMI 255
Cdd:TIGR00870 96 AVEAILLHLLAAFRK-------SGPLELANDQYTS--------EFTPGI----------------TALHLAAHRQNYEIV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 256 KMCLDNGAQIdPVekgRCTAIHFAATQGATeivklmissysgsvdivnttdgchetmlhrasLFDHheladylisvgadi 335
Cdd:TIGR00870 145 KLLLERGASV-PA---RACGDFFVKSQGVD--------------------------------SFYH-------------- 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 336 nkidseGRSPLILATASASWNIVNLLLSKGAQVDIKDNFGRNFLHLTVQQPyGLKNLRPEF-MQMQQI-----------K 403
Cdd:TIGR00870 175 ------GESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVMEN-EFKAEYEELsCQMYNFalslldklrdsK 247
|
330 340
....*....|....*....|....
gi 116534990 404 ELVMDEDNDGCTPLHYACRQGGPG 427
Cdd:TIGR00870 248 ELEVILNHQGLTPLKLAAKEGRIV 271
|
|
| TRPV4 |
cd22195 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed ... |
677-1013 |
3.36e-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: 54.47 E-value: 3.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 677 DVIYEPLTALNAMVQN----NRIELLNHPVCKEYLLMKWLAYGFRAHMMNLGSYCLGLIPMTILV----VNIKPGMAFNs 748
Cdd:cd22195 324 DTCGEEVSVLEILVYNskieNRHEMLAVEPINELLRDKWRKFGAVSFYISVVSYLVAMIIFTLIAyyrpMEGTPPYPYR- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 749 tgiinetsdhseildTTNSYLIKTCMILVFLSSIFGYCKEAGQIFQQK----RNYFMDISNVLEWIIYTTGIIFVLPLFV 824
Cdd:cd22195 403 ---------------TTVDYLRLAGEIITLLTGIFFFFTNIKDLFMKKcpgvNSLFIDGSFQLLYFIYSVLVIVTAALYL 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 825 E-IPAHLQWQcgAIAVYFYWMNFLLYLQRFENCGIFIVMLEVIL-KTLLRSTVVFIFLLLAFGLSFYILLNL-------- 894
Cdd:cd22195 468 AgIEAYLAVM--VFALVLGWMNALYFTRGLKLTGTYSIMIQKILfKDLFRFLLVYLLFMIGYASALVSLLNPcptketck 545
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 895 --QDPFSSPLLSII---QTFSMMLGDInYRESF----LEpyLRNELAHPVLSFAQLVSFTIFVPIVLMNLLIGL---AVG 962
Cdd:cd22195 546 edSTNCTVPTYPSCrdsNTFSKFLLDL-FKLTIgmgdLE--MLNSAKYPAVFIILLVTYIILTFVLLLNMLIALmgeTVG 622
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 116534990 963 DIAEVQKHASLKRIAMQVelhTSLEKKLPLwFLRKVDQKSTIVYPNKPRSG 1013
Cdd:cd22195 623 QVSKESKQIWKLQWATTI---LDIERSFPV-FLRKAFRSGEMVTVGKNLDG 669
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
93-270 |
3.36e-07 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 54.26 E-value: 3.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 93 EMDDYGNTPLHCAVEKNQ--IESVKFLLSRGANPNLRNFNMMAPLHIAVQGM--NNEVMKVLLEhRTIDVNLEGENGNTA 168
Cdd:PHA03095 147 ALDLYGMTPLAVLLKSRNanVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFkpRARIVRELIR-AGCDPAATDMLGNTP 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 169 VIIACTTNNSEALQI--LLKKGAKPCKSNKWGCFPIHQAAFSGSKECMEIILRFGEEhgysrqlhINFMNNGKATPLHLA 246
Cdd:PHA03095 226 LHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGAD--------INAVSSDGNTPLSLM 297
|
170 180
....*....|....*....|....
gi 116534990 247 VQNGDLEMIKMCLDNGAQIDPVEK 270
Cdd:PHA03095 298 VRNNNGRAVRAALAKNPSAETVAA 321
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
242-521 |
3.82e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 54.12 E-value: 3.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 242 PLHLAVQNGDLEMIKMCLDNGAQIDPVEKGRCTAIHFAATQGATEIVKLMISSY---SGSVDIVNTTDGCHETMLHRASL 318
Cdd:PHA02878 40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSInkcSVFYTLVAIKDAFNNRNVEIFKI 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 319 FdhheLADYLISV-GADINKIDSEGRSPLILAtasaswNIVNLLLSKGAQVDIKDnfgrnflhltvqqpyglknlrpefm 397
Cdd:PHA02878 120 I----LTNRYKNIqTIDLVYIDKKSKDDIIEA------EITKLLLSYGADINMKD------------------------- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 398 qmqqikelvmdeDNDGCTPLHYACRQGGPGSVNNLLGFNVSIHSKSKDKKSPLHFAASYGRINTCQRLLQDISDTrllNE 477
Cdd:PHA02878 165 ------------RHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAST---DA 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 116534990 478 GDLHGMTPLHLAAKNGHD-KVVQLLLKKGALF--LSDHNGWTALHHA 521
Cdd:PHA02878 230 RDKCGNTPLHISVGYCKDyDILKLLLEHGVDVnaKSYILGLTALHSS 276
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
220-375 |
4.15e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 53.84 E-value: 4.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 220 FGEEHGYSRQLHI----NFMNNGKATPLHLAVQNGDLEMIKMCLDNGAQIDPVEKGRCTAIHFAATQGATEIVKLMISSY 295
Cdd:PHA02875 12 FGELDIARRLLDIginpNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 296 SGSVDIVnTTDGchETMLHRASLFDHHELADYLISVGADINKIDSEGRSPLILATASASWNIVNLLLSKGAQVDIKDNFG 375
Cdd:PHA02875 92 KFADDVF-YKDG--MTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCG 168
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
448-502 |
5.93e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 47.27 E-value: 5.93e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 116534990 448 SPLHFAASYGRINTCQRLLQDISDtrlLNEGDLHGMTPLHLAAKNGHDKVVQLLL 502
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGAD---INAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
97-128 |
7.81e-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: 7.81e-07
10 20 30
....*....|....*....|....*....|...
gi 116534990 97 YGNTPLHCAVEK-NQIESVKFLLSRGANPNLRN 128
Cdd:pfam00023 1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
471-521 |
1.05e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 46.57 E-value: 1.05e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 116534990 471 DTRLLNEGDLHGMTPLHLAAKNGHDKVVQLLLKKGA-LFLSDHNGWTALHHA 521
Cdd:pfam13857 5 GPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVdLNLKDEEGLTALDLA 56
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
98-151 |
1.46e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 46.11 E-value: 1.46e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 116534990 98 GNTPLHCAVEKNQIESVKFLLSRGANPNLRNFNMMAPLHIAVQGMNNEVMKVLL 151
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
146-315 |
2.20e-06 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 51.79 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 146 VMKVLLEH--RTIDVNLE-------GENGNTA----VIIACTTNNSEALQILLKKGAKPCKSNKWGCFPIHQAAFSGSKE 212
Cdd:PLN03192 493 ILKNFLQHhkELHDLNVGdllgdngGEHDDPNmasnLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYED 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 213 CMEIILRFG-----------------EEHGYSRQLHINFMNNGKATP------LHLAVQNGDLEMIKMCLDNGAQIDPVE 269
Cdd:PLN03192 573 CVLVLLKHAcnvhirdangntalwnaISAKHHKIFRILYHFASISDPhaagdlLCTAAKRNDLTAMKELLKQGLNVDSED 652
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 116534990 270 KGRCTAIHFAATQGATEIVKLMISSySGSVDIVNTTDGCHETMLHR 315
Cdd:PLN03192 653 HQGATALQVAMAEDHVDMVRLLIMN-GADVDKANTDDDFSPTELRE 697
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
97-126 |
6.61e-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: 6.61e-06
10 20 30
....*....|....*....|....*....|
gi 116534990 97 YGNTPLHCAVEKNQIESVKFLLSRGANPNL 126
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
412-572 |
7.81e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 49.60 E-value: 7.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 412 DGCTPLHYACRQGGPGSVNNLLGFNVSIHSKSKDKKSPLHFAASYGRINTCQRLLqdISDTRLLNEGDLHGMTPLHLAAK 491
Cdd:PHA02875 34 DGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL--DLGKFADDVFYKDGMTPLHLATI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 492 NGHDKVVQLLLKKGAlflsdhngwtalhhasmggytqtmkvilDTNLKCTDRLdedgnTALHFAAREGHAKAVALLLSHN 571
Cdd:PHA02875 112 LKKLDIMKLLIARGA----------------------------DPDIPNTDKF-----SPLHLAVMMGDIKGIELLIDHK 158
|
.
gi 116534990 572 A 572
Cdd:PHA02875 159 A 159
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
95-138 |
8.41e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 44.26 E-value: 8.41e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 116534990 95 DDYGNTPLHCAVEKNQIESVKFLLSRGANPNLRNFNMMAPLHIA 138
Cdd:pfam13857 13 DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
274-329 |
9.08e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 43.80 E-value: 9.08e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 116534990 274 TAIHFAATQGATEIVKLMISSysgSVDIvNTTDGCHETMLHRASLFDHHELADYLI 329
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEK---GADI-NAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
117-266 |
1.73e-05 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 49.10 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 117 LLSRGANPNLRNFNMMAPLHIAVQGMNNEVMKVLLEHrTIDVNLEGENGNTAVIIACTTNNSEALQIL--LKKGAKPCKS 194
Cdd:PLN03192 544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKH-ACNVHIRDANGNTALWNAISAKHHKIFRILyhFASISDPHAA 622
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116534990 195 NKWGCFpihqAAFSGSKECMEIILRFGeehgysrqLHINFMNNGKATPLHLAVQNGDLEMIKMCLDNGAQID 266
Cdd:PLN03192 623 GDLLCT----AAKRNDLTAMKELLKQG--------LNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVD 682
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
481-506 |
2.37e-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: 2.37e-05
10 20
....*....|....*....|....*..
gi 116534990 481 HGMTPLHLAA-KNGHDKVVQLLLKKGA 506
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGA 27
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
219-577 |
2.45e-05 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 48.13 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 219 RFGEE---HGYSRqlhiNFMNNGKATPLHLAVQNGDLEMIKMCLDNGAQIDPVEKGRCTAIHFAAtqgateivklmissy 295
Cdd:PHA02946 53 RFVEEllhRGYSP----NETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLS--------------- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 296 sgsvdivnttdGCHETMLHRASLfdhheladyLISVGADINK-IDSEGRSPLiLATASASWNIVNLLLSKGAQVDIKDNF 374
Cdd:PHA02946 114 -----------GTDDEVIERINL---------LVQYGAKINNsVDEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKF 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 375 GRNFLHltvqqpYGLKNLRPEFMQMQQIKELVMD---EDNDGCTPLHYACRQGGPG-SVNNLLGFNVSIHSKSKDKKSPL 450
Cdd:PHA02946 173 GKNHIH------RHLMSDNPKASTISWMMKLGISpskPDHDGNTPLHIVCSKTVKNvDIINLLLPSTDVNKQNKFGDSPL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 451 HFaasygrintcqrLLQDISDTRLLNE----GDLHGMTPLHLAAKNGHDKVVQLLLKKGALFLSdhngwTALHHASMGGY 526
Cdd:PHA02946 247 TL------------LIKTLSPAHLINKllstSNVITDQTVNICIFYDRDDVLEIINDKGKQYDS-----TDFKMAVEVGS 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 116534990 527 TQTMKVILDTNLKCTDrldedgntALHFAAREGHAKAV-ALLLSH-NADIVLN 577
Cdd:PHA02946 310 IRCVKYLLDNDIICED--------AMYYAVLSEYETMVdYLLFNHfSVDSVVN 354
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
67-118 |
2.62e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 42.65 E-value: 2.62e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 116534990 67 LHYAAAEGQIELMeKITRDSSLEVlHEMDDYGNTPLHCAVEKNQIESVKFLL 118
Cdd:pfam13637 5 LHAAAASGHLELL-RLLLEKGADI-NAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
451-570 |
2.79e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 48.36 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 451 HFAASyGRINTCQRLLQDISDTrllNEGDLHGMTPLHLAAKNGHDKVVQLLLKKGAlflsdhngwtalhhasmggytqtm 530
Cdd:PTZ00322 88 QLAAS-GDAVGARILLTGGADP---NCRDYDGRTPLHIACANGHVQVVRVLLEFGA------------------------ 139
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 116534990 531 kvilDTNLkctdrLDEDGNTALHFAAREGHAKAVALLLSH 570
Cdd:PTZ00322 140 ----DPTL-----LDKDGKTPLELAEENGFREVVQLLSRH 170
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
481-506 |
2.82e-05 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 41.80 E-value: 2.82e-05
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
406-593 |
3.40e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 47.57 E-value: 3.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 406 VMDEDNDGCTPLHYACRQggpgsvNNLLGFNVSIHSKSKDKKS----PLHFAASYGRINTCQRLL-------QDISD--- 471
Cdd:PHA02878 63 VNQPDHRDLTPLHIICKE------PNKLGMKEMIRSINKCSVFytlvAIKDAFNNRNVEIFKIILtnrykniQTIDLvyi 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 472 -------------TRLL-------NEGDLH-GMTPLHLAAKNGHDKVVQLLLKKGA-LFLSDHNGWTALHHAsMGGYTQT 529
Cdd:PHA02878 137 dkkskddiieaeiTKLLlsygadiNMKDRHkGNTALHYATENKDQRLTELLLSYGAnVNIPDKTNNSPLHHA-VKHYNKP 215
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116534990 530 MKVILDTNLKCTDRLDEDGNTALHFA-AREGHAKAVALLLSHNADIvlNKQQA----SFLHLALHNKRK 593
Cdd:PHA02878 216 IVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDV--NAKSYilglTALHSSIKSERK 282
|
|
| PHA02741 |
PHA02741 |
hypothetical protein; Provisional |
66-197 |
3.55e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 165108 [Multi-domain] Cd Length: 169 Bit Score: 45.42 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 66 FLHYAAAEGQIELMEKIT----RDSSLEVLHEMDDYGNTPLHCAVEKNQ----IESVKFLLSRGANPNLRN-FNMMAPLH 136
Cdd:PHA02741 24 FFHEAARCGCFDIIARFTpfirGDCHAAALNATDDAGQMCIHIAAEKHEaqlaAEIIDHLIELGADINAQEmLEGDTALH 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116534990 137 IAVQGMNNEVMKVLLEHRTIDVNLEGENGNTAVIIACTTNNSEALQILLKKGAKPCK-SNKW 197
Cdd:PHA02741 104 LAAHRRDHDLAEWLCCQPGIDLHFCNADNKSPFELAIDNEDVAMMQILREIVATSRGfSNEN 165
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
78-186 |
3.57e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 47.97 E-value: 3.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 78 LMEKITR-DSSLEVLHEMDDYGNTPLH---------------CAVEKNQIES------VKFLLSRGANPNLRNFNMMAPL 135
Cdd:PTZ00322 40 IQEEIARiDTHLEALEATENKDATPDHnltteevidpvvahmLTVELCQLAAsgdavgARILLTGGADPNCRDYDGRTPL 119
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 116534990 136 HIAVQGMNNEVMKVLLEHRTiDVNLEGENGNTAVIIACTTNNSEALQILLK 186
Cdd:PTZ00322 120 HIACANGHVQVVRVLLEFGA-DPTLLDKDGKTPLELAEENGFREVVQLLSR 169
|
|
| TRPV1 |
cd22196 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ... |
692-990 |
4.14e-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: 4.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 692 NNRIELLNHPVCKeYLLMKWLAYGFRAHMMNLGSYCLGLIPMTILVVNIKPGMafnstgiinetSDHSEILDTTNSYLIK 771
Cdd:cd22196 300 NRHEMLLVEPLNK-LLQDKWDKFVKRIFYFNFFVYFIYMIIFTLAAYYRPVNK-----------TPPFPIENTTGEYLRL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 772 TCMILVFLSSIFGYCKeAGQIFQQKRNYFMDIsnvlewII--YTTGIIFVLPLFVEIPAHLQW-------QCGAIAVYFY 842
Cdd:cd22196 368 TGEIISVSGGVYFFFR-GIQYFLQRRPSLKKL------IVdsYCEILFFVQSLFLLASTVLYFcgrneyvAFMVISLALG 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 843 WMNFLLYLQRFENCGIFIVMLE-VILKTLLRSTVVFIFLLLAFGLSFYILL---------------NLQDPFSSPLLSII 906
Cdd:cd22196 441 WANVLYYTRGFQQMGIYSVMIQkMILRDICRFLFVYLVFLFGFSAALVTLIedgppkgdvntsqkeCVCKSGYNSYNSLY 520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 907 QT------FSMMLGDINYRESFlepylrneLAHPVLSFAqLVSFTIFVPIVLMNLLIGL---AVGDIAEVQKHA-SLKRI 976
Cdd:cd22196 521 STclelfkFTIGMGDLEFTENY--------KFKEVFIFL-LISYVILTYILLLNMLIALmgeTVSKIAQESKNIwKLQRA 591
|
330
....*....|....
gi 116534990 977 AMQVELHTSLEKKL 990
Cdd:cd22196 592 ITILDLEKSLLRCL 605
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
482-591 |
5.48e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 46.91 E-value: 5.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 482 GMTPLHLAAKNGHDKVVQLLLKKGALFLSDHNGW-TALHHASMGGYTQTMKVILDTNLKCTDRLDEDGNTALHFAAREGH 560
Cdd:PHA02875 35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIeSELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKK 114
|
90 100 110
....*....|....*....|....*....|..
gi 116534990 561 AKAVALLLSHNADI-VLNKQQASFLHLALHNK 591
Cdd:PHA02875 115 LDIMKLLIARGADPdIPNTDKFSPLHLAVMMG 146
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
309-362 |
8.04e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 41.11 E-value: 8.04e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 116534990 309 HETMLHRASLFDHHELADYLISVGADINKIDSEGRSPLILATASASWNIVNLLL 362
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
547-574 |
9.84e-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: 9.84e-05
10 20
....*....|....*....|....*....
gi 116534990 547 DGNTALHFAA-REGHAKAVALLLSHNADI 574
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGADV 29
|
|
| PHA02989 |
PHA02989 |
ankyrin repeat protein; Provisional |
110-362 |
2.34e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222954 [Multi-domain] Cd Length: 494 Bit Score: 45.12 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 110 QIESVKFLLSRGANPNLRNFnMMAPLHIAVQGMN------NEVMKVLLEHrTIDVNLEGENGNTAV---IIACTTNNSEA 180
Cdd:PHA02989 49 KIKIVKLLIDNGADVNYKGY-IETPLCAVLRNREitsnkiKKIVKLLLKF-GADINLKTFNGVSPIvcfIYNSNINNCDM 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 181 LQILLKKGA--KPCKSNK-WGCFPIHQAAFSGSKECMEIILRFGEEHGYSRQLHinfmnngKATPLHLAVQNG----DLE 253
Cdd:PHA02989 127 LRFLLSKGInvNDVKNSRgYNLLHMYLESFSVKKDVIKILLSFGVNLFEKTSLY-------GLTPMNIYLRNDidviSIK 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 254 MIKMCLDNGAQIDPVEKGRCTAIH-FAATQGATEIVKLMISSYSGSVDIVNTTDGCHETMLHRASLFDHHELADYLISVG 332
Cdd:PHA02989 200 VIKYLIKKGVNIETNNNGSESVLEsFLDNNKILSKKEFKVLNFILKYIKINKKDKKGFNPLLISAKVDNYEAFNYLLKLG 279
|
250 260 270
....*....|....*....|....*....|
gi 116534990 333 ADINKIDSEGRSPLILATASASWNIVNLLL 362
Cdd:PHA02989 280 DDIYNVSKDGDTVLTYAIKHGNIDMLNRIL 309
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
165-218 |
2.35e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 39.95 E-value: 2.35e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 116534990 165 GNTAVIIACTTNNSEALQILLKKGAKPCKSNKWGCFPIHQAAFSGSKECMEIIL 218
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
117-172 |
2.62e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 40.02 E-value: 2.62e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 116534990 117 LLSRG-ANPNLRNFNMMAPLHIAVQGMNNEVMKVLLEHRtIDVNLEGENGNTAVIIA 172
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYG-VDLNLKDEEGLTALDLA 56
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
97-125 |
2.62e-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: 2.62e-04
10 20
....*....|....*....|....*....
gi 116534990 97 YGNTPLHCAVEKNQIESVKFLLSRGANPN 125
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
|
|
| PHA02791 |
PHA02791 |
ankyrin-like protein; Provisional |
458-590 |
2.64e-04 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165154 [Multi-domain] Cd Length: 284 Bit Score: 44.26 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 458 RINTCQ-RLLQDISDTRLLNEGDLHGMTPLHLAAKNGHDKVVQLLLKKGALFLSDHNGWtALHHASMGGYTQTMKVILDT 536
Cdd:PHA02791 5 RINTWKsKQLKSFLSSKDAFKADVHGHSALYYAIADNNVRLVCTLLNAGALKNLLENEF-PLHQAATLEDTKIVKILLFS 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 116534990 537 NLKcTDRLDEDGNTALHFAAREGHAKAVALLLSHNADIVLNKQ---QASFLHLALHN 590
Cdd:PHA02791 84 GMD-DSQFDDKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKtgwKTSFYHAVMLN 139
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
441-503 |
3.28e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 44.89 E-value: 3.28e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116534990 441 SKSKDKKSPLHFAASYGRINTCQRLLQDISDTRLLnegDLHGMTPLHLAAKNGHDKVVQLLLK 503
Cdd:PTZ00322 110 CRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLL---DKDGKTPLELAEENGFREVVQLLSR 169
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
548-596 |
3.38e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 39.57 E-value: 3.38e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 116534990 548 GNTALHFAAREGHAKAVALLLSHNADI-VLNKQQASFLHLALHNKRKEVV 596
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADInAVDGNGETALHFAASNGNVEVL 50
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
201-257 |
3.48e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 39.57 E-value: 3.48e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 116534990 201 PIHQAAFSGSKECMEIILrfgeEHGysrqLHINFMNNGKATPLHLAVQNGDLEMIKM 257
Cdd:pfam13637 4 ALHAAAASGHLELLRLLL----EKG----ADINAVDGNGETALHFAASNGNVEVLKL 52
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
481-506 |
3.52e-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: 3.52e-04
10 20
....*....|....*....|....*.
gi 116534990 481 HGMTPLHLAAKNGHDKVVQLLLKKGA 506
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGA 26
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
89-232 |
3.57e-04 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 44.27 E-value: 3.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 89 EVLH------EMDDYGNTPLHCAVEKNQIESVKFLLSRGANPNLRNFNMMAPLHIaVQGMNNEVMKV--LLEHRTIDVNL 160
Cdd:PHA02946 57 ELLHrgyspnETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYY-LSGTDDEVIERinLLVQYGAKINN 135
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116534990 161 EGENGNTAVIIACTTNNSEALQILLKKGAKPCKSNKWGCFPIHQAAFSGSKECMEI--ILRFG-----EEHGYSRQLHI 232
Cdd:PHA02946 136 SVDEEGCGPLLACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNPKASTIswMMKLGispskPDHDGNTPLHI 214
|
|
| PHA02736 |
PHA02736 |
Viral ankyrin protein; Provisional |
67-190 |
3.72e-04 |
|
Viral ankyrin protein; Provisional
Pssm-ID: 165103 [Multi-domain] Cd Length: 154 Bit Score: 42.17 E-value: 3.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 67 LHYAAAEGQI-ELM--EKITRDSSLEVLHEMDDYGNTPLHCAVEKNQI---ESVKFLLSRGANPNLRN-FNMMAPLHIAV 139
Cdd:PHA02736 21 LHYLCRNGGVtDLLafKNAISDENRYLVLEYNRHGKQCVHIVSNPDKAdpqEKLKLLMEWGADINGKErVFGNTPLHIAV 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 116534990 140 QGMNNEVMKVLLEHRTIDVNLEGENGNTAVIIACTTNNSEALQILLKKGAK 190
Cdd:PHA02736 101 YTQNYELATWLCNQPGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGAQ 151
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
241-266 |
4.28e-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: 4.28e-04
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
404-453 |
5.07e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 39.25 E-value: 5.07e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 116534990 404 ELVMDEDNDGCTPLHYACRQGGPGSVNNLLGFNVSIHSKSKDKKSPLHFA 453
Cdd:pfam13857 7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
547-574 |
5.16e-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: 5.16e-04
10 20
....*....|....*....|....*...
gi 116534990 547 DGNTALHFAAREGHAKAVALLLSHNADI 574
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
54-254 |
7.08e-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: 7.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 54 KKLKRCDDMDTF--------FLHYAAAEGQIE----LMEKITRDSSLEVLHEMddY-GNTPLHCAVEKNQIESVKFLLSR 120
Cdd:cd22192 34 KKLLKCPSCDLFqrgalgetALHVAALYDNLEaavvLMEAAPELVNEPMTSDL--YqGETALHIAVVNQNLNLVRELIAR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 121 GA---NPNlrnfnmmaplhiaVQGMnnevmkVLLEHRTidvNL--EGENgntAVIIACTTNNSEALQILLKKGAKPCKSN 195
Cdd:cd22192 112 GAdvvSPR-------------ATGT------FFRPGPK---NLiyYGEH---PLSFAACVGNEEIVRLLIEHGADIRAQD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116534990 196 KWGCFPIH----QAAFSGSKECMEIILRFGEEHGYSRQLHInfMNNGKATPLHLAVQNGDLEM 254
Cdd:cd22192 167 SLGNTVLHilvlQPNKTFACQMYDLILSYDKEDDLQPLDLV--PNNQGLTPFKLAAKEGNIVM 227
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
134-292 |
8.84e-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: 8.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 134 PLHIAVQGMNNEVMKVLLEHRTIDVNLEGENGNTAVIIACTTNNSEALQILLKkgAKPCKSNKwgcfPIHQAAFSGSkec 213
Cdd:cd22192 20 PLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNE----PMTSDLYQGE--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 214 meiilrfgeehgysrqlhinfmnngkaTPLHLAVQNGDLEMIKMCLDNGAQidpVEKGRCTAIHF--------------- 278
Cdd:cd22192 91 ---------------------------TALHIAVVNQNLNLVRELIARGAD---VVSPRATGTFFrpgpknliyygehpl 140
|
170
....*....|....*.
gi 116534990 279 --AATQGATEIVKLMI 292
Cdd:cd22192 141 sfAACVGNEEIVRLLI 156
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
150-189 |
8.88e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 38.48 E-value: 8.88e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 116534990 150 LLEHRTIDVNLEGENGNTAVIIACTTNNSEALQILLKKGA 189
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGV 40
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
67-185 |
1.10e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 42.67 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 67 LHYAAAEGQIELMEKITRDSSLEVLHemDDYGNTPLHCAVEKNQIESVKFLLSRGANPNLRNFN-MMAPLHIAVQGMNNE 145
Cdd:PHA02875 139 LHLAVMMGDIKGIELLIDHKACLDIE--DCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNgCVAALCYAIENNKID 216
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 116534990 146 VMKVLLEhRTIDVNL----EGENGNTAVIIA--CTTNNSEALQILL 185
Cdd:PHA02875 217 IVRLFIK-RGADCNImfmiEGEECTILDMICnmCTNLESEAIDALI 261
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
518-601 |
1.26e-03 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 42.96 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 518 LHHASMGGYTQTMKVILDTNLKCTDRlDEDGNTALHFAAREGHAKAVALLLSHNADI-VLNKQQASFLHLALHNKRKEVV 596
Cdd:PTZ00322 86 LCQLAASGDAVGARILLTGGADPNCR-DYDGRTPLHIACANGHVQVVRVLLEFGADPtLLDKDGKTPLELAEENGFREVV 164
|
....*
gi 116534990 597 LTIIR 601
Cdd:PTZ00322 165 QLLSR 169
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
236-279 |
1.27e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 38.10 E-value: 1.27e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 116534990 236 NNGKATPLHLAVQNGDLEMIKMCLDNGAQIDPVEKGRCTAIHFA 279
Cdd:pfam13857 13 DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
302-349 |
1.29e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 38.10 E-value: 1.29e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 116534990 302 VNTTDGCHETMLHRASLFDHHELADYLISVGADINKIDSEGRSPLILA 349
Cdd:pfam13857 9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| TRPV2 |
cd22197 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ... |
764-997 |
1.38e-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: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 764 TTNSYLIKTCMILVFLSSIFGYCkeaGQI--FQQKR----NYFMD-----------ISNVLEWIIYTTGIIFVLPLFVei 826
Cdd:cd22197 358 TAGGSMLLLGHILILLGGIYLLL---GQLwyFWRRRlfiwISFMDsyfeilfllqaLLTVLSQVLYFMGSEWYLPLLV-- 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 827 pahlqwqcgaIAVYFYWMNFLLYLQRFENCGIFIVMLE-VILKTLLRSTVVFIFLLLAFGLSFYIL-------------- 891
Cdd:cd22197 433 ----------FSLVLGWLNLLYYTRGFQHTGIYSVMIQkVILRDLLRFLLVYLVFLFGFAVALVSLsreapspkapednn 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 892 -------LNLQDPFSSPLLSIIQT------FSMMLGDINYRESFlepylrnELAHPVLSFaqLVSFTIFVPIVLMNLLIG 958
Cdd:cd22197 503 stvteqpTVGQEEEPAPYRSILDAslelfkFTIGMGELAFQEQL-------RFRGVVLLL--LLAYVLLTYVLLLNMLIA 573
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 116534990 959 LAVGDIAEVQKHA----SLKRIAMQVELHTSLekklpLWFLRK 997
Cdd:cd22197 574 LMSETVNHVADNSwsiwKLQKAISVLEMENGY-----WWCRRK 611
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
94-159 |
1.88e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 42.17 E-value: 1.88e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116534990 94 MDDYGNTPLHCAVEK-NQIESVKFLLSRGANPNLRNFNM-MAPLHIAVQgmNNEVMKVLLEHRTiDVN 159
Cdd:PHA02878 230 RDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYILgLTALHSSIK--SERKLKLLLEYGA-DIN 294
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
241-266 |
1.93e-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: 1.93e-03
10 20
....*....|....*....|....*.
gi 116534990 241 TPLHLAVQNGDLEMIKMCLDNGAQID 266
Cdd:pfam13606 4 TPLHLAARNGRLEIVKLLLENGADIN 29
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
547-574 |
2.08e-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: 36.47 E-value: 2.08e-03
10 20
....*....|....*....|....*...
gi 116534990 547 DGNTALHFAAREGHAKAVALLLSHNADI 574
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
|
|
| PLN03223 |
PLN03223 |
Polycystin cation channel protein; Provisional |
840-989 |
2.67e-03 |
|
Polycystin cation channel protein; Provisional
Pssm-ID: 215637 [Multi-domain] Cd Length: 1634 Bit Score: 42.24 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 840 YFYW------MNFLLYLQRFENCGIFIVMLEVILKTLLRST-------VVFIFLLLAFGLSFYILLNLQDP-FSSPLLSI 905
Cdd:PLN03223 1287 YFQWymtlsgINIILLLGRILKLMDFQPRLGVITRTLWLAGadlmhffVIFGMVFVGYAFIGHVIFGNASVhFSDMTDSI 1366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 906 IQTFSMMLGDINYresFLEPyLRNelAHPVLSFAQLV---SFTIFVPIVLMNLLIGLAVGDIAEVQKHASlKRIAMQVEL 982
Cdd:PLN03223 1367 NSLFENLLGDITY---FNED-LKN--LTGLQFVVGMIyfySYNIFVFMILFNFLLAIICDAFGEVKANAA-ETVSVHTEL 1439
|
....*..
gi 116534990 983 HTSLEKK 989
Cdd:PLN03223 1440 FPMLRDK 1446
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
98-218 |
2.91e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411978 [Multi-domain] Cd Length: 680 Bit Score: 41.67 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 98 GNTPLHCAVEKNQIESVKFLLSRGANPNLRN----FNMM----------APLHIAVQGMNNEVMKVLLEHRTIDVNLEGE 163
Cdd:cd22194 141 GQTALNIAIERRQGDIVKLLIAKGADVNAHAkgvfFNPKykhegfyfgeTPLALAACTNQPEIVQLLMEKESTDITSQDS 220
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 164 NGNTA----VIIActtNNSEAL---------QILLKKGAKPCK--SNKWGCFPIHQAAFSGSKECMEIIL 218
Cdd:cd22194 221 RGNTVlhalVTVA---EDSKTQndfvkrmydMILLKSENKNLEtiRNNEGLTPLQLAAKMGKAEILKYIL 287
|
|
| TRPV2 |
cd22197 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ... |
95-219 |
3.54e-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: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 95 DDY--GNTPLHCAVEKNQIESVKFLLSRGANPNLRN--------------FNMMaPLHIAVQGMNNEVMKVLLEHRTIDV 158
Cdd:cd22197 89 DEYyrGHSALHIAIEKRSLQCVKLLVENGADVHARAcgrffqkkqgtcfyFGEL-PLSLAACTKQWDVVNYLLENPHQPA 167
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116534990 159 NLEGEN--GNTA----VIIACTTNNSEALQI-----LLKKGAKPCK-------SNKWGCFPIHQAAFSGSKECMEIILR 219
Cdd:cd22197 168 SLQAQDslGNTVlhalVMIADNSPENSALVIkmydgLLQAGARLCPtvqleeiSNHEGLTPLKLAAKEGKIEIFRHILQ 246
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
96-161 |
3.62e-03 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 41.42 E-value: 3.62e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116534990 96 DY-GNTPLHCAVEKNQIESVKFLLSRGANPNLRNFNMMAPLHIAVQGMNNEVMKVLLEHRTIDVNLE 161
Cdd:PTZ00322 112 DYdGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELG 178
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
296-363 |
3.95e-03 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 41.42 E-value: 3.95e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116534990 296 SGSVDiVNTTDGCHETMLHRASLFDHHELADYLISVGADINKIDSEGRSPLILATASASWNIVNLLLS 363
Cdd:PTZ00322 103 TGGAD-PNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
415-466 |
5.88e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 36.10 E-value: 5.88e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 116534990 415 TPLHYACRQGGPGSVNNLLGFNVSIHSKSKDKKSPLHFAASYGRINTCQRLL 466
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
459-595 |
6.01e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 40.42 E-value: 6.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116534990 459 INTCQRLLQDISDTRLLNEGDL------HGMTPLHLAAKNGHDKVVQLLLKKGA-LFLSDHNGWTALHHASMGGYTQTMK 531
Cdd:PHA03100 6 VLTKSRIIKVKNIKYIIMEDDLndysykKPVLPLYLAKEARNIDVVKILLDNGAdINSSTKNNSTPLHYLSNIKYNLTDV 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116534990 532 V----ILDTNLKCTDRLDEDGNTALHFAARE--GHAKAVALLLSHNADI-VLNKQQASFLHLALHNKRKEV 595
Cdd:PHA03100 86 KeivkLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVnIKNSDGENLLHLYLESNKIDL 156
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
241-266 |
6.43e-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: 6.43e-03
10 20
....*....|....*....|....*..
gi 116534990 241 TPLHLAV-QNGDLEMIKMCLDNGAQID 266
Cdd:pfam00023 4 TPLHLAAgRRGNLEIVKLLLSKGADVN 30
|
|
| |
