|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
41-298 |
7.00e-36 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 138.16 E-value: 7.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 41 LDARTEADNLRSIIHQSAREGNVNALQEALLKAPLAVNAQDGDFMTPLHYAARYGNYDAVKLLLSKNALPNTKNREGDTP 120
Cdd:COG0666 44 LLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETP 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 121 LHIASKYIYgysdicsiidedqadsarkyntatKKIINALVSENAEIDPVNKYQLTPLHYAAMKSNFSALHALIKLKADV 200
Cdd:COG0666 124 LHLAAYNGN------------------------LEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 201 DAEDDNKMTPLLLACVHGSQEIIQELIKANSNVTKRDQRLNTVFHIVALRGEPEYLEMMmdhdpVEAIKALNLFNNEKKT 280
Cdd:COG0666 180 NARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLL-----LEAGADLNAKDKDGLT 254
|
250
....*....|....*...
gi 212645948 281 PLRMAVEGNHPETLKKIL 298
Cdd:COG0666 255 ALLLAAAAGAALIVKLLL 272
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
453-660 |
2.38e-35 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 136.62 E-value: 2.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 453 NTLRIVSEDVRRTMVNMVDRDQNTPMHIVASNGYLEMMQLLQKHGASITQVNEDEETALHRAAIGGQTGAVRQLLEWDIR 532
Cdd:COG0666 33 LLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGAD 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 533 LLLmKDEMGNSALHLAARSGHDATTKVLLDNGADKEAKNSYQKTPLQVAVDSGKLETCQRLVAKGAQIES-SSDTKTVLH 611
Cdd:COG0666 113 VNA-RDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNArDNDGETPLH 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 212645948 612 TAAFYGNESIVRYFIAEGVTIDRRDEEGKTAFDIACENDHKDVARAFLE 660
Cdd:COG0666 192 LAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
6-276 |
5.57e-35 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 135.47 E-value: 5.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 6 LGLDVRLELEGLISNDDTIRSEKDGRQASIFRVAELDARTEADNLRSIIHQSAREGNVNALqEALLKAPLAVNAQDGDFM 85
Cdd:COG0666 43 ALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIV-KLLLEAGADVNARDKDGE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 86 TPLHYAARYGNYDAVKLLLSKNALPNTKNREGDTPLHIAskyiygysdicsiidedqadsARKYNTatkKIINALVSENA 165
Cdd:COG0666 122 TPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA---------------------AANGNL---EIVKLLLEAGA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 166 EIDPVNKYQLTPLHYAAMKSNFSALHALIKLKADVDAEDDNKMTPLLLACVHGSQEIIQELIKANSNVTKRDQRLNTVFH 245
Cdd:COG0666 178 DVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALL 257
|
250 260 270
....*....|....*....|....*....|.
gi 212645948 246 IVALRGEPEYLEMMMDHDPVEAIKALNLFNN 276
Cdd:COG0666 258 LAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
467-667 |
6.01e-35 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 135.47 E-value: 6.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 467 VNMVDRDQNTPMHIVASNGYLEMMQLLQKHGASITQVNEDEETALHRAAIGGQTGAVRQLLEWDIRLLLmKDEMGNSALH 546
Cdd:COG0666 80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNA-QDNDGNTPLH 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 547 LAARSGHDATTKVLLDNGADKEAKNSYQKTPLQVAVDSGKLETCQRLVAKGAQIE-SSSDTKTVLHTAAFYGNESIVRYF 625
Cdd:COG0666 159 LAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNaKDNDGKTALDLAAENGNLEIVKLL 238
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 212645948 626 IAEGVTIDRRDEEGKTAFDIACENDHKDVARAFLETDQWKNL 667
Cdd:COG0666 239 LEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAA 280
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
266-578 |
5.54e-33 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 129.69 E-value: 5.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 266 EAIKALNLFNNEKKTPLRMAVEGNHPETLKKILQMEKKNSCKWMDREKELIHFAAEKGFLEVLKALVEAGGNKNELNEVK 345
Cdd:COG0666 8 LLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 346 AVPLHVAAQMNQLEVVSYLIEEeKDNIDVVDEQGLTPLMMAVTHDSKKCVEYLIAKKANLTITDKDERTPVFIGAKFNAL 425
Cdd:COG0666 88 NTLLHAAARNGDLEIVKLLLEA-GADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 426 SSVEYILDHlrKKNketersalksptrntlrivsedvrrtmVNMVDRDQNTPMHIVASNGYLEMMQLLQKHGASITQVNE 505
Cdd:COG0666 167 EIVKLLLEA--GAD---------------------------VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 212645948 506 DEETALHRAAIGGQTGAVRQLLEWDIRLLLmKDEMGNSALHLAARSGHDATTKVLLDNGADKEAKNSYQKTPL 578
Cdd:COG0666 218 DGKTALDLAAENGNLEIVKLLLEAGADLNA-KDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
294-643 |
6.18e-32 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 126.61 E-value: 6.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 294 LKKILQMEKKNSCKWMDREKELIHFAAEKGFLEVLKALVEAGGNKNELNEVKAVPLHVAAQMNQLEVVSYLIEEEKDNID 373
Cdd:COG0666 2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 374 VVDEQGLTPLMMAVTHDSKKCVEYLIAKKANltitdkdertpvfigakfnalssveyildhlrkknketersalksptrn 453
Cdd:COG0666 82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGAD------------------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 454 tlrivsedvrrtmVNMVDRDQNTPMHIVASNGYLEMMQLLQKHGASITQVNEDEETALHRAAIGGQTGAVRQLLEWDIRL 533
Cdd:COG0666 113 -------------VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADV 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 534 LLmKDEMGNSALHLAARSGHDATTKVLLDNGADKEAKNSYQKTPLQVAVDSGKLETCQRLVAKGAQIE-SSSDTKTVLHT 612
Cdd:COG0666 180 NA-RDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNaKDKDGLTALLL 258
|
330 340 350
....*....|....*....|....*....|.
gi 212645948 613 AAFYGNESIVRYFIAEGVTIDRRDEEGKTAF 643
Cdd:COG0666 259 AAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
35-346 |
5.34e-30 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 121.21 E-value: 5.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 35 IFRVAELDARTEADNLRSIIHQSAREGNVNALQEALLKAPLAVNAQDGDFMTPLHYAARYGNYDAVKLLLSKNALPNTKN 114
Cdd:COG0666 5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 115 REGDTPLHIASKYiygysdicsiidedqadsarkyntATKKIINALVSENAEIDPVNKYQLTPLHYAAMKSNFSALHALI 194
Cdd:COG0666 85 DGGNTLLHAAARN------------------------GDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 195 KLKADVDAEDDNKMTPLLLACVHGSQEIIQELIKANSNVTKRDQRLNTVFHIVALRGEPEYLEMMMDH--DPveaikalN 272
Cdd:COG0666 141 EAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAgaDV-------N 213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 212645948 273 LFNNEKKTPLRMAVEGNHPETLKKILQMEKKNScKWMDREKELIHFAAEKGFLEVLKALVEAGGNKNELNEVKA 346
Cdd:COG0666 214 AKDNDGKTALDLAAENGNLEIVKLLLEAGADLN-AKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLL 286
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
121-440 |
1.84e-29 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 119.67 E-value: 1.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 121 LHIASKYIYGYSDICSIIDEDQADSARKYNTATKKIINALVSENAEIDPVNKYQLTPLHYAAMKSNFSALHALIKLKADV 200
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 201 DAEDDNKMTPLLLACVHGSQEIIQELIKANSNVTKRDQRLNTVFHIVALRGEPEYLEMMMDH--DPveaikalNLFNNEK 278
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAgaDV-------NAQDNDG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 279 KTPLrmavegnhpetlkkilqmekknsckwmdrekeliHFAAEKGFLEVLKALVEAGGNKNELNEVKAVPLHVAAQMNQL 358
Cdd:COG0666 154 NTPL----------------------------------HLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHL 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 359 EVVSYLIEEEKDnIDVVDEQGLTPLMMAVTHDSKKCVEYLIAKKANLTITDKDERTPVFIGAKFNALSSVEYILDHLRKK 438
Cdd:COG0666 200 EIVKLLLEAGAD-VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278
|
..
gi 212645948 439 NK 440
Cdd:COG0666 279 AA 280
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
455-660 |
3.01e-29 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 118.90 E-value: 3.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 455 LRIVSEDVRRTMVNMVDRDQNTPMHIVASNGYLEMMQLLQKHGASITQVNEDEETALHRAAIGGQTGAVRQLLEWDIRLL 534
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 535 LMKDEMGNSALHLAARSGHDATTKVLLDNGADKEAKNSYQKTPLQVAVDSGKLETCQRLVAKGAQIE-SSSDTKTVLHTA 613
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNaQDNDGNTPLHLA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 212645948 614 AFYGNESIVRYFIAEGVTIDRRDEEGKTAFDIACENDHKDVARAFLE 660
Cdd:COG0666 161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLE 207
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
155-442 |
1.14e-27 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 114.28 E-value: 1.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 155 KIINALVSENAEIDPVNKYQLTPLHYAAMKSNFSALHALIKLKADVDAEDDNKMTPLLLACVHGSQEIIQELIKANSNVT 234
Cdd:COG0666 2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 235 KRDQRLNTVFHIVALRGEPEYLEMMMDHDPveaikALNLFNNEKKTPLrmavegnhpetlkkilqmekknsckwmdreke 314
Cdd:COG0666 82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGA-----DVNARDKDGETPL-------------------------------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 315 liHFAAEKGFLEVLKALVEAGGNKNELNEVKAVPLHVAAQMNQLEVVSYLIEEeKDNIDVVDEQGLTPLMMAVTHDSKKC 394
Cdd:COG0666 125 --HLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARDNDGETPLHLAAENGHLEI 201
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 212645948 395 VEYLIAKKANLTITDKDERTPVFIGAKFNALSSVEYILDHLRKKNKET 442
Cdd:COG0666 202 VKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKD 249
|
|
| Ion_trans |
pfam00520 |
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ... |
814-1080 |
1.75e-22 |
|
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: 97.72 E-value: 1.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 814 YYFALFMYLVFIVSLTQYVrhtkapynvwneesyydSEYFDENETCPQINTTKPDVVWKIIIQTLAVCQILVECFqlfqr 893
Cdd:pfam00520 2 RYFELFILLLILLNTIFLA-----------------LETYFQPEEPLTTVLEILDYVFTGIFTLEMLLKIIAAGF----- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 894 KFAYLVNWENWIDCFIYSTALITVYdFSECSATSGVRQNwqwilaalcIFFGWINLLFMIRKMPRFGIFVVMFVDIVKTF 973
Cdd:pfam00520 60 KKRYFRSPWNILDFVVVLPSLISLV-LSSVGSLSGLRVL---------RLLRLLRLLRLIRRLEGLRTLVNSLIRSLKSL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 974 FRFFPVFVLFIIAFSSSFYVILQ-----------NRPEFSTIFMSPLKTTVMMIGEfEFTGIFHgdETTHAEkmfgpaHT 1042
Cdd:pfam00520 130 GNLLLLLLLFLFIFAIIGYQLFGgklktwenpdnGRTNFDNFPNAFLWLFQTMTTE-GWGDIMY--DTIDGK------GE 200
|
250 260 270
....*....|....*....|....*....|....*...
gi 212645948 1043 AVACALFFFFCIIMTILLMNLLVGLAVDDIKGVQEKAE 1080
Cdd:pfam00520 201 FWAYIYFVSFIILGGFLLLNLFIAVIIDNFQELTERTE 238
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
539-1128 |
1.81e-21 |
|
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: 100.34 E-value: 1.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 539 EMGNSALHLAA---RSGHDATTKVLLD----NGADKEAKNS------YQ-KTPLQVAVDSGKLETCQRLVAKGAQIESSS 604
Cdd:cd21882 24 ATGKTCLHKAAlnlNDGVNEAIMLLLEaapdSGNPKELVNApctdefYQgQTALHIAIENRNLNLVRLLVENGADVSARA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 605 DTKTV--------------LHTAAFYGNESIVRYFIAEG---VTIDRRDEEGKTAFDIACENDHKDVARAFLETDQWKNL 667
Cdd:cd21882 104 TGRFFrkspgnlfyfgelpLSLAACTNQEEIVRLLLENGaqpAALEAQDSLGNTVLHALVLQADNTPENSAFVCQMYNLL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 668 MIpcdvipLDKHRNPVNMKRRTPFRTLLTKFPELAS----FVMDNCIEKSKEETDSTQS---VAYNFEFLDDT-YMMRCV 739
Cdd:cd21882 184 LS------YGAHLDPTQQLEEIPNHQGLTPLKLAAVegkiVMFQHILQREFSGPYQPLSrkfTEWTYGPVTSSlYDLSEI 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 740 sdDGTGEQLIgcksaydedfkLEKDAQSYASnydrvykyhplklmaDAEKLHLLNHPLSKaLLKYKWNRLGRPMYYFALF 819
Cdd:cd21882 258 --DSWEKNSV-----------LELIAFSKKR---------------EARHQMLVQEPLNE-LLQEKWDRYGRPYFCFNFA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 820 MYLVFIVSLTQYVRHTKAPYNVWNEESYydseyfdenetcpqiNTTKPD--VVWKIIIQTLAVCQILVECFQLFQRK-FA 896
Cdd:cd21882 309 CYLLYMIIFTVCAYYRPLKDRPANQEAK---------------ATFGDSirLVGEILTVLGGVYILLGEIPYFFRRRlSR 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 897 YLVNWENWIDCFIYSTALIT----VYDFSEcsatsgvrQNWQWILAALCIFFGWINLLFMIRKMPRFGIFVVMFVD-IVK 971
Cdd:cd21882 374 WFGFLDSYFEILFITQALLVllsmVLRFME--------TEGYVVPLVFSLVLGWCNVLYYTRGFQMLGIYTVMIQKmILR 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 972 TFFRFFPVFVLFIIAFSSSFYVILQ-----NRPEFSTIFMSPLKTtvmmigeFEFT-GIFHGDETTHAEKMFgpahtaVA 1045
Cdd:cd21882 446 DLMRFCWVYLVFLFGFASAFVILFQtedpnKLGEFRDYPDALLEL-------FKFTiGMGDLPFNENVDFPF------VY 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 1046 CALFFFFCIIMTILLMNLLVGLAVDDIKGV-QEKAELKRlamqvdlvLQIEASLhffIQRTKKYATCRYATFPYGKLHKT 1124
Cdd:cd21882 513 LILLLAYVILTYLLLLNMLIALMGETVNRVaQESDEIWK--------LQKAITT---LMLERKYPRCLRKRSREGRLLKV 581
|
....
gi 212645948 1125 GFAG 1128
Cdd:cd21882 582 GCGG 585
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
508-1088 |
3.14e-21 |
|
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: 99.70 E-value: 3.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 508 ETALHRAAIGGQTGAVRQLLEWDIRLLLMKDEMGNSALHLAARSGHDATTKVLLDNGAD--KEAKNS--YQ-KTPLQVAV 582
Cdd:cd22192 18 ESPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElvNEPMTSdlYQgETALHIAV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 583 DSGKLETCQRLVAKGAQIESSSDTKT---------------VLHTAAFYGNESIVRYFIAEGVTIDRRDEEGKTAFDIAC 647
Cdd:cd22192 98 VNQNLNLVRELIARGADVVSPRATGTffrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 648 ENDHKDVARA----FLETDQWKNLMipcdviPLDKHRNPVNMkrrTPFRtlltkfpeLAS----FVMDNCIEKSKEETD- 718
Cdd:cd22192 178 LQPNKTFACQmydlILSYDKEDDLQ------PLDLVPNNQGL---TPFK--------LAAkegnIVMFQHLVQKRRHIQw 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 719 ---STQSVAYNFEFLDdtymmrcvsddgtgeqligcksAYDEDFKLekdaqsyasnydrvykyhpLKLMADAEK---LHL 792
Cdd:cd22192 241 tygPLTSTLYDLTEID----------------------SWGDEQSV-------------------LELIVSSKKreaRKI 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 793 LNHPLSKALLKYKWNRLGRPMYYFALFMYLVFIVSLTQ--YVRHTKAPYNVWNEES---YYDSEYFDENETCPQINTTkp 867
Cdd:cd22192 280 LDVTPVKELVSLKWKRYGRPYFRILALLYLLYIIIFTLccVYRPLKPRPENNTDPRditLYVQKTLQESYVTPKDYLR-- 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 868 dVVWKIIIQTLAVCQILVECFQLFQ----RKFAY--------LVNWenwidCFIYSTALITVYDFSEcsaTSGvrqnwQW 935
Cdd:cd22192 358 -LVGELISVLGAIVILLLEIPDILRvgvkRYFGQtvlggpfhVIII-----TYACLVLLTLVLRLTS---LSG-----EV 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 936 ILAALCIFFGWINLLFMIRKMPRFGIFVVMFVDIV-KTFFRFFPVFVLFIIAFSSSFYVILQNRPEFSTIFMSPLKTTvm 1014
Cdd:cd22192 424 VPMSLALVLGWCNVMYFARGFQMLGPFTIMIQKIIfGDLMKFCWLMFVVILGFSSAFYMIFQTEDPDSLGHFYDFPMT-- 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 1015 MIGEFE-FTGIFHgdetthaekmfGPAHTAV-----ACALFFFFCIIMTILLMNLLVGLAVDDIKGV-QEKAELKRlaMQ 1087
Cdd:cd22192 502 LFSTFElFLGLID-----------GPANYTVdlpfmYKVLYTAFAVIAYLLMLNLLIAMMGDTHWRVaHERDELWR--AQ 568
|
.
gi 212645948 1088 V 1088
Cdd:cd22192 569 V 569
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
26-416 |
1.86e-20 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 96.25 E-value: 1.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 26 SEKDGRQASIFRVAELDARTEADNLRSIIHQSAregNVNalqeallkaplavnaQDGDFM-TPLHYAARYGNY---DAVK 101
Cdd:PHA03095 6 SVDIIMEAALYDYLLNASNVTVEEVRRLLAAGA---DVN---------------FRGEYGkTPLHLYLHYSSEkvkDIVR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 102 LLLSKNALPNTKNREGDTPLHIaskYIYgysdicsiidedqadsarkyNTATKKIINALVSENAEIDPVNKYQLTPLH-Y 180
Cdd:PHA03095 68 LLLEAGADVNAPERCGFTPLHL---YLY--------------------NATTLDVIKLLIKAGADVNAKDKVGRTPLHvY 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 181 AAMKS-NFSALHALIKLKADVDAEDDNKMTPL--LLACVHGSQEIIQELIKANSNVTKRDQRLNTVFHIVAlrgepeyle 257
Cdd:PHA03095 125 LSGFNiNPKVIRLLLRKGADVNALDLYGMTPLavLLKSRNANVELLRLLIDAGADVYAVDDRFRSLLHHHL--------- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 258 mmmdhdpveaikalnlfnnekktplrmavegnhpetlkkilqmekkNSCKwmDREKelihfaaekgfleVLKALVEAGGN 337
Cdd:PHA03095 196 ----------------------------------------------QSFK--PRAR-------------IVRELIRAGCD 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 338 KNELNEVKAVPLHVAAQMNQLE--VVSYLIEEEKDnIDVVDEQGLTPLMMAVTHDSKKCVEYLIAKKANLTITDKDERTP 415
Cdd:PHA03095 215 PAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGIS-INARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTP 293
|
.
gi 212645948 416 V 416
Cdd:PHA03095 294 L 294
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
441-1067 |
9.26e-20 |
|
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: 95.53 E-value: 9.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 441 ETERSALKSPTRNTLRIVS---EDVRRTMVNMVDR-DQNTPMHIVASNGYLEMMQLLQKHGASItqvnEDEETALHRAAI 516
Cdd:TIGR00870 16 DEEKAFLPAAERGDLASVYrdlEEPKKLNINCPDRlGRSALFVAAIENENLELTELLLNLSCRG----AVGDTLLHAISL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 517 GGQtGAVRQLLEW-------DIRLLLMKDEMGN------SALHLAARSGHDATTKVLLDNGADKEAKnsyqktplqvavd 583
Cdd:TIGR00870 92 EYV-DAVEAILLHllaafrkSGPLELANDQYTSeftpgiTALHLAAHRQNYEIVKLLLERGASVPAR------------- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 584 sgkletcqrlvAKGAQIESSSDTKTVLHT------AAFYGNESIVRYFIAEGVTIDRRDEEGKTAFDIA-CENDHKDVAR 656
Cdd:TIGR00870 158 -----------ACGDFFVKSQGVDSFYHGesplnaAACLGSPSIVALLSEDPADILTADSLGNTLLHLLvMENEFKAEYE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 657 AFleTDQWKNLMipcdVIPLDKHRNPV------NMKRRTPFrTLLTK--FPELASFVMDNCIEKSK--EETDSTQSVAyn 726
Cdd:TIGR00870 227 EL--SCQMYNFA----LSLLDKLRDSKelevilNHQGLTPL-KLAAKegRIVLFRLKLAIKYKQKKfvAWPNGQQLLS-- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 727 feflddTYMMRCVsdDGTGEQLIGCKSAydedfklekdaqsyasnydrvyKYHPLKLMADAEKLHLLNHPLSKaLLKYKW 806
Cdd:TIGR00870 298 ------LYWLEEL--DGWRRKQSVLELI----------------------VVFVIGLKFPELSDMYLIAPLSR-LGQFKW 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 807 NRLGRPMYYFALFMYLVFIVSLT--QYVRHTKAPYnvwneesyydseyfdENETCPQINTTKPDVVWKIIIQTLAVCQIL 884
Cdd:TIGR00870 347 KPFIKFIFHSASYLYFLYLIIFTsvAYYRPTRTDL---------------RVTGLQQTPLEMLIVTWVDGLRLGEEKLIW 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 885 VECFQLfqrkfaYLVNWENWIDcFI------------YSTALITVYDFSEcsATSGVR----QNWQWILAALCIFFGWIN 948
Cdd:TIGR00870 412 LGGIFE------YIHQLWNILD-FGmnsfylatfldrPFAILFVTQAFLV--LREHWLrfdpTLIEEALFAFALVLSWLN 482
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 949 LLFMIRKMPRFGIFVVM-----FVDIvktfFRFFPVFVLFIIAFSSSFYVILQ-----NRPEFSTIFMSPLKTTVMMIGE 1018
Cdd:TIGR00870 483 LLYIFRGNQHLGPLQIMigrmiLGDI----LRFLFIYAVVLFGFACGLNQLYQyydelKLNECSNPHARSCEKQGNAYST 558
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 212645948 1019 FEFT------GIFHGDETTHAEKMFGPahtAVACALFFFFCIIMTILLMNLLVGL 1067
Cdd:TIGR00870 559 LFETsqelfwAIIGLGDLLANEHKFTE---FVGLLLFGAYNVIMYILLLNMLIAM 610
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
316-409 |
5.98e-19 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 82.86 E-value: 5.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 316 IHFAAEKGFLEVLKALVEAGGNKNELNEVKAVPLHVAAQMNQLEVVSYLIeeEKDNIDVVDEqGLTPLMMAVTHDSKKCV 395
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL--EHADVNLKDN-GRTALHYAARSGHLEIV 77
|
90
....*....|....
gi 212645948 396 EYLIAKKANLTITD 409
Cdd:pfam12796 78 KLLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
478-571 |
6.36e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 79.77 E-value: 6.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 478 MHIVASNGYLEMMQLLQKHGASITQVNEDEETALHRAAIGGQTGAVRQLLEwdiRLLLMKDEMGNSALHLAARSGHDATT 557
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE---HADVNLKDNGRTALHYAARSGHLEIV 77
|
90
....*....|....
gi 212645948 558 KVLLDNGADKEAKN 571
Cdd:pfam12796 78 KLLLEKGADINVKD 91
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
66-435 |
6.52e-18 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 89.35 E-value: 6.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 66 LQEALLKAPLAVNAQDGDFMTPLHYAARYGNYDAVKLLLSKNALPNTKNREGDTPLHIA--SKYIygySDICSIIDedqa 143
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAvdSKNI---DTIKAIID---- 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 144 dSARKYNTATKKIINALVSENAE-----------IDPVNKYQLTPLHYAAMKSNFSAL-HALIKLKADVDAEDDNKMTPL 211
Cdd:PHA02876 233 -NRSNINKNDLSLLKAIRNEDLEtslllydagfsVNSIDDCKNTPLHHASQAPSLSRLvPKLLERGADVNAKNIKGETPL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 212 LLACVHG-SQEIIQELIKANSNVTKRDQRLNTVFHIVAlrgepeylemMMDHDPVEAIKALNLFNNE------KKTPLRM 284
Cdd:PHA02876 312 YLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQAS----------TLDRNKDIVITLLELGANVnardycDKTPIHY 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 285 AVEGNHPETLKKILQMEKKNSCkWMDREKELIHFA--AEKGFLEVlKALVEAGGNKNELNEVKAVPLHVAAQMN-QLEVV 361
Cdd:PHA02876 382 AAVRNNVVIINTLLDYGADIEA-LSQKIGTALHFAlcGTNPYMSV-KTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVI 459
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 212645948 362 SYLIEEEKDnIDVVDEQGLTPLMMAVTHDSkkCVEYLIAKKANLtitdKDERtpVFIGAKFNALSSVEYILDHL 435
Cdd:PHA02876 460 EMLLDNGAD-VNAINIQNQYPLLIALEYHG--IVNILLHYGAEL----RDSR--VLHKSLNDNMFSFRYIIAHI 524
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
545-636 |
9.34e-17 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 76.31 E-value: 9.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 545 LHLAARSGHDATTKVLLDNGADKEAKNSYQKTPLQVAVDSGKLETCQRLVAKgAQIESSSDTKTVLHTAAFYGNESIVRY 624
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGRTALHYAARSGHLEIVKL 79
|
90
....*....|..
gi 212645948 625 FIAEGVTIDRRD 636
Cdd:pfam12796 80 LLEKGADINVKD 91
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
325-661 |
1.78e-16 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 83.92 E-value: 1.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 325 LEVLKALVEAGGNKNELNEVKAVPLHV---AAQMNQLEVVSYLIEEEKDnIDVVDEQGLTPLMMAVTHDSK-KCVEYLIA 400
Cdd:PHA03095 27 VEEVRRLLAAGADVNFRGEYGKTPLHLylhYSSEKVKDIVRLLLEAGAD-VNAPERCGFTPLHLYLYNATTlDVIKLLIK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 401 KKANLTITDKDERTPVFIgakfnalssveyildHLRKKNketersalksptrntlriVSEDVRRTMVNM------VDRDQ 474
Cdd:PHA03095 106 AGADVNAKDKVGRTPLHV---------------YLSGFN------------------INPKVIRLLLRKgadvnaLDLYG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 475 NTPMHI--VASNGYLEMMQLLQKHGASITQVNEDEETALH--------RAAIggqtgaVRQLLEWDIRLLlMKDEMGNSA 544
Cdd:PHA03095 153 MTPLAVllKSRNANVELLRLLIDAGADVYAVDDRFRSLLHhhlqsfkpRARI------VRELIRAGCDPA-ATDMLGNTP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 545 LHLAARSGHDATTKV--LLDNGADKEAKNSYQKTPLqvavdsgkletcqrlvakgaqiesssdtktvlHTAAFYGNESIV 622
Cdd:PHA03095 226 LHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPL--------------------------------HYAAVFNNPRAC 273
|
330 340 350
....*....|....*....|....*....|....*....
gi 212645948 623 RYFIAEGVTIDRRDEEGKTAFDIACENDHKDVARAFLET 661
Cdd:PHA03095 274 RRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAK 312
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
88-204 |
2.48e-14 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 69.76 E-value: 2.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 88 LHYAARYGNYDAVKLLLSKNALPNTKNREGDTPLHIASKyiYGYSDICSIidedqadsarkyntatkkiinaLVsENAEI 167
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAK--NGHLEIVKL----------------------LL-EHADV 55
|
90 100 110
....*....|....*....|....*....|....*..
gi 212645948 168 DPVNkYQLTPLHYAAMKSNFSALHALIKLKADVDAED 204
Cdd:pfam12796 56 NLKD-NGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
221-660 |
2.71e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 77.80 E-value: 2.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 221 EIIQELIKANSN-VTKRDQRLNTVFHIVALrgEPEYLEMM----MDHDPVEAIKALNLFNNEKKTP------LRMAVEGN 289
Cdd:PHA02876 55 DIVEEIIQQNPElIYITDHKCHSTLHTICI--IPNVMDIVisltLDCDIILDIKYASIILNKHKLDeacihiLKEAISGN 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 290 HpetlkkiLQMEKKN-SCKWMDREKELIhfaaEKGFLEVLKALVEAGGNKNELNEVKAVPLHVAAQMNQLEVVSYLIEEE 368
Cdd:PHA02876 133 D-------IHYDKINeSIEYMKLIKERI----QQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYG 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 369 KDnIDVVDEQGLTPLMMAVTHDSKKCVEYLIAKKANLTITDkdertpvfigakfnaLSSVEYIldhlrkKNKETERSALK 448
Cdd:PHA02876 202 AD-VNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKND---------------LSLLKAI------RNEDLETSLLL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 449 SPTRNTlrivsedvrrtmVNMVDRDQNTPMHIVASNGYLEMM--QLLQKhGASITQVNEDEETALHRAAIGGQTGAvrql 526
Cdd:PHA02876 260 YDAGFS------------VNSIDDCKNTPLHHASQAPSLSRLvpKLLER-GADVNAKNIKGETPLYLMAKNGYDTE---- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 527 lewDIRLLLMK-------DEMGNSALHLAARSGHDATTKV-LLDNGADKEAKNSYQKTPLQVAVDSGKLETCQRLVAKGA 598
Cdd:PHA02876 323 ---NIRTLIMLgadvnaaDRLYITPLHQASTLDRNKDIVItLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGA 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 212645948 599 QIES-SSDTKTVLHTAAFYGNESI-VRYFIAEGVTIDRRDEEGKTAFDIACENDHK-DVARAFLE 660
Cdd:PHA02876 400 DIEAlSQKIGTALHFALCGTNPYMsVKTLIDRGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLD 464
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
69-405 |
3.25e-14 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 76.60 E-value: 3.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 69 ALLKAPLAVNAQDGDFMTPLHYAARYGN-YDAVKLLLSKNALPNTKNREGDTPLHIaskYIYGYSdicsiIDedqadsar 147
Cdd:PHA03095 68 LLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGADVNAKDKVGRTPLHV---YLSGFN-----IN-------- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 148 kyntatKKIINALVSENAEIDPVNKYQLTPLHyAAMKSNfsalhaliklkaDVDAeddnkmtplllacvhgsqEIIQELI 227
Cdd:PHA03095 132 ------PKVIRLLLRKGADVNALDLYGMTPLA-VLLKSR------------NANV------------------ELLRLLI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 228 KANSNVTKRDQRLNTVFHIVA--LRGEPEYLEMMMDH--DPVeaikALNLFNNekkTPLRMavegnhpetlkkilqMEKK 303
Cdd:PHA03095 175 DAGADVYAVDDRFRSLLHHHLqsFKPRARIVRELIRAgcDPA----ATDMLGN---TPLHS---------------MATG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 304 NSCKWMdrekelihfaaekgfleVLKALVEAGGNKNELNEVKAVPLHVAAQMNQLEVVSYLIeEEKDNIDVVDEQGLTPL 383
Cdd:PHA03095 233 SSCKRS-----------------LVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLI-ALGADINAVSSDGNTPL 294
|
330 340
....*....|....*....|..
gi 212645948 384 MMAVTHDSKKCVEYLIAKKANL 405
Cdd:PHA03095 295 SLMVRNNNGRAVRAALAKNPSA 316
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
148-434 |
8.50e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 75.09 E-value: 8.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 148 KYNTATKKIINALVSENAEIDPVNKYQLTPLHYAAMKSNFSALHALIKLKADVDAEDDNKMTPLLLACVHGS-----QEI 222
Cdd:PHA03100 9 KSRIIKVKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 223 IQELIKANSNVTKRDQRLNTVFHIVALR--GEPEYLEMMMDHdpveAIKaLNLFNNEKKTPLRMAVEGNHPEtlkkilqm 300
Cdd:PHA03100 89 VKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDN----GAN-VNIKNSDGENLLHLYLESNKID-------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 301 ekknsckwmdrekelihfaaekgfLEVLKALVEAGGNKNELNEVKavplhvaaqmnqlevvsYLIEEEKDnIDVVDEQGL 380
Cdd:PHA03100 156 ------------------------LKILKLLIDKGVDINAKNRVN-----------------YLLSYGVP-INIKDVYGF 193
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 212645948 381 TPLMMAVTHDSKKCVEYLIAKKANLTITDKDERTPVFIGAKFNALSSVEYILDH 434
Cdd:PHA03100 194 TPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNN 247
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
54-144 |
1.03e-13 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 67.83 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 54 IHQSAREGNVNALQEaLLKAPLAVNAQDGDFMTPLHYAARYGNYDAVKLLLSKNALPNTKNreGDTPLHIASKyiYGYSD 133
Cdd:pfam12796 1 LHLAAKNGNLELVKL-LLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN--GRTALHYAAR--SGHLE 75
|
90
....*....|.
gi 212645948 134 ICSIIDEDQAD 144
Cdd:pfam12796 76 IVKLLLEKGAD 86
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
70-233 |
1.42e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 74.32 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 70 LLKAPLAVNAQDGDFMTPLHYAA--RYGNYDAVKLLLSKNALPNTKNREGDTPLHIASKYIYGYSDICSIIDEdqadsaR 147
Cdd:PHA03100 92 LLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLKILKLLID------K 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 148 KYNTATKKIINALVSENAEIDPVNKYQLTPLHYAAMKSNFSALHALIKLKADVDAEDDNKMTPLLLACVHGSQEIIQELI 227
Cdd:PHA03100 166 GVDINAKNRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLL 245
|
....*.
gi 212645948 228 KANSNV 233
Cdd:PHA03100 246 NNGPSI 251
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
349-439 |
1.99e-13 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 67.06 E-value: 1.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 349 LHVAAQMNQLEVVSYLIEEEKDnIDVVDEQGLTPLMMAVTHDSKKCVEYLIaKKANLTITDKDeRTPVFIGAKFNALSSV 428
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGAD-ANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDNG-RTALHYAARSGHLEIV 77
|
90
....*....|.
gi 212645948 429 EYILDHLRKKN 439
Cdd:pfam12796 78 KLLLEKGADIN 88
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
39-233 |
2.94e-13 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 73.52 E-value: 2.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 39 AELDARTEADnlRSIIHQSAREGNVNA-LQEALLKAPLAVNAQDGDFMTPLHYAARYGNYDA--VKLLLSKNALPNTKNR 115
Cdd:PHA03095 108 ADVNAKDKVG--RTPLHVYLSGFNINPkVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVYAVDD 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 116 EGDTPLHIASKYIYGYSDI--------CSIIDEDQAD-----SARKYNTATKKIINALVSENAEIDPVNKYQLTPLHYAA 182
Cdd:PHA03095 186 RFRSLLHHHLQSFKPRARIvreliragCDPAATDMLGntplhSMATGSSCKRSLVLPLLIAGISINARNRYGQTPLHYAA 265
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 212645948 183 MKSNFSALHALIKLKADVDAEDDNKMTPLLLACVHGSQEIIQELIKANSNV 233
Cdd:PHA03095 266 VFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSA 316
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
156-237 |
1.89e-12 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 64.37 E-value: 1.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 156 IINALVSENAEIDPVNKYQLTPLHYAAMKSNFSALHALIKlKADVDaEDDNKMTPLLLACVHGSQEIIQELIKANSNVTK 235
Cdd:pfam12796 12 LVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVN-LKDNGRTALHYAARSGHLEIVKLLLEKGADINV 89
|
..
gi 212645948 236 RD 237
Cdd:pfam12796 90 KD 91
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
86-289 |
1.91e-12 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 71.58 E-value: 1.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 86 TPLHYAARYGNYDAVK-LLLSKNALPNTKNREGDTPLHIASKYiygysdicsiiDEDQAdsarkyntaTKKIINA---LV 161
Cdd:cd22192 19 SPLLLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALY-----------DNLEA---------AVVLMEAapeLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 162 SENAEIDPvnkYQ-LTPLHYAAMKSNFSALHALIKLKADVDA----------EDDNKM----TPLLLACVHGSQEIIQEL 226
Cdd:cd22192 79 NEPMTSDL---YQgETALHIAVVNQNLNLVRELIARGADVVSpratgtffrpGPKNLIyygeHPLSFAACVGNEEIVRLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 212645948 227 IKANSNVTKRDQRLNTVFHIVALRGEP----EYLEMMMDHDPVEAIKALNLF-NNEKKTPLRMA-VEGN 289
Cdd:cd22192 156 IEHGADIRAQDSLGNTVLHILVLQPNKtfacQMYDLILSYDKEDDLQPLDLVpNNQGLTPFKLAaKEGN 224
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
358-654 |
1.95e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 70.76 E-value: 1.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 358 LEVVSYLIEEEKDNIDVVDEQGLTPLMMAVTHDSKKCVEYLIAKKANLTITDKDERTPVFIGAKFNALSSVEYILDHlrk 437
Cdd:PHA02874 14 IEAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDN--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 438 knkETERSALKSPTRNTLRIVSEDVRRTMVNMVDRDQNTPMHIVASNGYLEMMQLLQKHGASITqvnedeetalhraaig 517
Cdd:PHA02874 91 ---GVDTSILPIPCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVN---------------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 518 gqtgavrqllewdirlllMKDEMGNSALHLAARSGHDATTKVLLDNGADKEAKNSYQKTPLQVAVDSGKLETCQRLVAKG 597
Cdd:PHA02874 152 ------------------IEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHG 213
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 212645948 598 AQIESSSDTK-TVLHTAAFYgNESIVRYFIaEGVTIDRRDEEGKT----AFDIACENDHKDV 654
Cdd:PHA02874 214 NHIMNKCKNGfTPLHNAIIH-NRSAIELLI-NNASINDQDIDGSTplhhAINPPCDIDIIDI 273
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
466-684 |
4.16e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 69.69 E-value: 4.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 466 MVNMVDRDQNTPMHIVASNGYLEMMQLLQKHGASITQVNEDEETALHraaIGGQTGAVRQLLEWDIRLLL-------MKD 538
Cdd:PHA03100 27 LNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLH---YLSNIKYNLTDVKEIVKLLLeyganvnAPD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 539 EMGNSALHLAA--RSGHDATTKVLLDNGADKEAKNSYQKTPLQVAVDSG--KLETCQRLVAKGAQI------------ES 602
Cdd:PHA03100 104 NNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNkiDLKILKLLIDKGVDInaknrvnyllsyGV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 603 SSDTK-----TVLHTAAFYGNESIVRYFIAEGVTIDRRDEEGKTAFDIACENDHKDVARAFLETDQWKNLMIPCdvIPLD 677
Cdd:PHA03100 184 PINIKdvygfTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET--LLYF 261
|
....*..
gi 212645948 678 KHRNPVN 684
Cdd:PHA03100 262 KDKDLNT 268
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
365-601 |
4.66e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 69.69 E-value: 4.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 365 IEEEKDNIDVVDEQGLTPLMMAVTHDSKKCVEYLIAKKANLTITDKDERTPvfigakFNALSSVEYILDHlrkkNKETER 444
Cdd:PHA03100 21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTP------LHYLSNIKYNLTD----VKEIVK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 445 SALKsptrntlrivsedvRRTMVNMVDRDQNTPMHIVASN--GYLEMMQLLQKHGASITQVNEDEETALHRAAIGG---- 518
Cdd:PHA03100 91 LLLE--------------YGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNkidl 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 519 --------------QTGAVRQLLEWDIRLLLmKDEMGNSALHLAARSGHDATTKVLLDNGADKEAKNSYQKTPLQVAVDS 584
Cdd:PHA03100 157 kilkllidkgvdinAKNRVNYLLSYGVPINI-KDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILN 235
|
250
....*....|....*..
gi 212645948 585 GKLETCQRLVAKGAQIE 601
Cdd:PHA03100 236 NNKEIFKLLLNNGPSIK 252
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
339-594 |
5.58e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 69.52 E-value: 5.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 339 NELNEVKAVPLHVAAQMNQLEVVSYLIEEEKdNIDVVDEQGLTPLMMAVTHDSKKCVEYLIAKKanltITDKDERTPVFI 418
Cdd:PHA02878 31 TSASLIPFIPLHQAVEARNLDVVKSLLTRGH-NVNQPDHRDLTPLHIICKEPNKLGMKEMIRSI----NKCSVFYTLVAI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 419 GAKFN--ALSSVEYILDHLRKKNKETERSALKSPTRNTLrIVSEDVRRTM-----VNMVDRDQ-NTPMHIVASNGYLEMM 490
Cdd:PHA02878 106 KDAFNnrNVEIFKIILTNRYKNIQTIDLVYIDKKSKDDI-IEAEITKLLLsygadINMKDRHKgNTALHYATENKDQRLT 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 491 QLLQKHGASITQVNEDEETALHRAA---------IGGQTGA----------------VRQLLEWDIRLLLMKDE------ 539
Cdd:PHA02878 185 ELLLSYGANVNIPDKTNNSPLHHAVkhynkpivhILLENGAstdardkcgntplhisVGYCKDYDILKLLLEHGvdvnak 264
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 212645948 540 ---MGNSALHLAARSghDATTKVLLDNGADKEAKNSYQKTPLQVAVDS-GKLETCQRLV 594
Cdd:PHA02878 265 syiLGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAVKQyLCINIGRILI 321
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
61-422 |
9.90e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 68.45 E-value: 9.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 61 GNVNALQEALLKAPLAVNAQDGDFMTPLHYAARYGNYDAVKLLLSKNALPNTKNREGDTPLHIASKYiyGYSDICSIIDE 140
Cdd:PHA02874 12 GDIEAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKI--GAHDIIKLLID 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 141 DQAD-SARKYNTATKKIINALVSENAEIDPVNKYQLTPLHYAAMKSNFSALHALIKLKADVDAEDDNKMTPLLLACVHGS 219
Cdd:PHA02874 90 NGVDtSILPIPCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNF 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 220 QEIIQELikansnvtkrdqrlntvfhivalrgepeylemmmdhdpVEAIKALNLFNNEKKTPLrmavegnhpetlkkilq 299
Cdd:PHA02874 170 FDIIKLL--------------------------------------LEKGAYANVKDNNGESPL----------------- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 300 mekknsckwmdrekeliHFAAEKGFLEVLKALVEAGGNKNELNEVKAVPLHVAAQMNQlEVVSYLIEEEkdNIDVVDEQG 379
Cdd:PHA02874 195 -----------------HNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLINNA--SINDQDIDG 254
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 212645948 380 LTPLMMAVTHD-SKKCVEYLIAKKANLTITDKDERTPVFIGAKF 422
Cdd:PHA02874 255 STPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAFKY 298
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
578-660 |
2.04e-11 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 61.29 E-value: 2.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 578 LQVAVDSGKLETCQRLVAKGAQIES-SSDTKTVLHTAAFYGNESIVRYFIAEGVTidRRDEEGKTAFDIACENDHKDVAR 656
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLqDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78
|
....
gi 212645948 657 AFLE 660
Cdd:pfam12796 79 LLLE 82
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
222-685 |
3.59e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 67.40 E-value: 3.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 222 IIQELIKANSNVTKRDQRLNTVFHIVALRGEPEYLEMMMDHDpveaiKALNLFNNEKKTPLRMAVEGNHPETLKKILQme 301
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYG-----ADVNIIALDDLSVLECAVDSKNIDTIKAIID-- 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 302 kkNSCKWMDREKELIHfAAEKGFLEVLKALVEAGGNKNELNEVKAVPLHVAAQMNQL-EVVSYLIEEEKDnIDVVDEQGL 380
Cdd:PHA02876 233 --NRSNINKNDLSLLK-AIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGAD-VNAKNIKGE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 381 TPL-MMAVTHDSKKCVEYLIAKKANLTITDKDERTPVFIGAKFNalssveyildhlrkKNKETERSALKSPTRntlrivs 459
Cdd:PHA02876 309 TPLyLMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTLD--------------RNKDIVITLLELGAN------- 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 460 edvrrtmVNMVDRDQNTPMHIVASNGYLEMMQLLQKHGASITQVNEDEETALHRAAIGGQT-GAVRQLLEWDIRLLlMKD 538
Cdd:PHA02876 368 -------VNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPyMSVKTLIDRGANVN-SKN 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 539 EMGNSALHLAARSG-HDATTKVLLDNGADKEAKNSYQKTPLQVAVdsGKLETCQRLVAKGAQIESSSDTKTVLHTAAFYG 617
Cdd:PHA02876 440 KDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGAELRDSRVLHKSLNDNMFSF 517
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 212645948 618 NESIVRYFIAEGVTIDRRDEEGKTAFDIACENDHKDVARAFLETDQ-WKNLMIPCDVIPLDKHRNPVNM 685
Cdd:PHA02876 518 RYIIAHICIQDFIRHDIRNEVNPLKRVPTRFTSLRESFKEIIQSDDtFKRIWLRCKEELKDISKIRINM 586
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
54-287 |
4.30e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 67.40 E-value: 4.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 54 IHQSAREGNVNALQEALLKAPLAVNAQDGDFMTPLHYAARYGnYDA--VKLLLSKNALPNTKNREGDTPLHiaskyiygy 131
Cdd:PHA02876 277 LHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNG-YDTenIRTLIMLGADVNAADRLYITPLH--------- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 132 sdicsiidedQADSARKYntatKKIINALVSENAEIDPVNKYQLTPLHYAAMKSNFSALHALIKLKADVDAEDDNKMTPL 211
Cdd:PHA02876 347 ----------QASTLDRN----KDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTAL 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 212645948 212 LLA-CVHGSQEIIQELIKANSNVTKRDQRLNTVFHIVALRG-EPEYLEMMMDHDpveaiKALNLFNNEKKTPLRMAVE 287
Cdd:PHA02876 413 HFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNG-----ADVNAINIQNQYPLLIALE 485
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
74-124 |
1.14e-10 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 58.13 E-value: 1.14e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 212645948 74 PLAVNAQDGDFMTPLHYAARYGNYDAVKLLLSKNALPNTKNREGDTPLHIA 124
Cdd:pfam13857 6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
54-286 |
1.27e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 65.29 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 54 IHQSAREGNVNALqEALLKAPLAVNAQDGDFMTPLHYAARYGNYDAVKLLLSK-------NALPNTKNREGDTPLHIASK 126
Cdd:PHA02878 41 LHQAVEARNLDVV-KSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSinkcsvfYTLVAIKDAFNNRNVEIFKI 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 127 YIYGYSDICSIIDEDQADSARKYNTATKKIINALVSENAEIDPVNKYQL-TPLHYAAMKSNFSALHALIKLKADVDAEDD 205
Cdd:PHA02878 120 ILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDRHKGnTALHYATENKDQRLTELLLSYGANVNIPDK 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 206 NKMTPLLLACVHGSQEIIQELIKANSNVTKRDQRLNTVFHI-VALRGEPEYLEMMMDHDPVEAIKA-------------- 270
Cdd:PHA02878 200 TNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIsVGYCKDYDILKLLLEHGVDVNAKSyilgltalhssiks 279
|
250 260
....*....|....*....|....*....
gi 212645948 271 -------------LNLFNNEKKTPLRMAV 286
Cdd:PHA02878 280 erklkllleygadINSLNSYKLTPLSSAV 308
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
61-233 |
1.67e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 64.63 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 61 GNVNALQEaLLKAPLAVNAQDGDFMTPLHYAARYGNYDAVKLLLSKNALPNTKNREGDTPLHIAS-----KYIYGYSDIC 135
Cdd:PHA02875 13 GELDIARR-LLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVeegdvKAVEELLDLG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 136 SIIDE---DQADSARKYNTATKK--IINALVSENAEIDPVNKYQLTPLHYAAMKSNFSALHALIKLKADVDAEDDNKMTP 210
Cdd:PHA02875 92 KFADDvfyKDGMTPLHLATILKKldIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTP 171
|
170 180
....*....|....*....|...
gi 212645948 211 LLLACVHGSQEIIQELIKANSNV 233
Cdd:PHA02875 172 LIIAMAKGDIAICKMLLDSGANI 194
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
178-263 |
3.32e-10 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 57.82 E-value: 3.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 178 LHYAAMKSNFSALHALIKLKADVDAEDDNKMTPLLLACVHGSQEIIQELI-KANSNVTKRDqrlNTVFHIVALRGEPEYL 256
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLeHADVNLKDNG---RTALHYAARSGHLEIV 77
|
....*..
gi 212645948 257 EMMMDHD 263
Cdd:pfam12796 78 KLLLEKG 84
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
383-504 |
4.53e-10 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 57.43 E-value: 4.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 383 LMMAVTHDSKKCVEYLIAKKANLTITDKDERTPVFIGAKFNALSSVEYILDHLRKKNKEtersalksptrntlrivsedv 462
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD--------------------- 59
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 212645948 463 rrtmvnmvdrDQNTPMHIVASNGYLEMMQLLQKHGASITQVN 504
Cdd:pfam12796 60 ----------NGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
186-434 |
4.62e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 63.44 E-value: 4.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 186 NFSALHALIKLKAD-VDAEDDNKMTPLLLACVHGSQEIIQELIKANSNV----TKRDQRLNTVFHIvalrGEPEYLEMMM 260
Cdd:PHA02874 13 DIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADInhinTKIPHPLLTAIKI----GAHDIIKLLI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 261 DHDPVEAIKALNLFNNEkktplrmavegnhpeTLKKILQMEKKNSCKwmDRE-KELIHFAAEKGFLEVLKALVEAGGNKN 339
Cdd:PHA02874 89 DNGVDTSILPIPCIEKD---------------MIKTILDCGIDVNIK--DAElKTFLHYAIKKGDLESIKMLFEYGADVN 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 340 ELNEVKAVPLHVAAQMNQLEVVSYLIEEEKdNIDVVDEQGLTPLMMAVTHDSKKCVEYLIAKKANLTITDKDERTPVFIG 419
Cdd:PHA02874 152 IEDDNGCYPIHIAIKHNFFDIIKLLLEKGA-YANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA 230
|
250
....*....|....*
gi 212645948 420 AKFNAlSSVEYILDH 434
Cdd:PHA02874 231 IIHNR-SAIELLINN 244
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
113-504 |
5.04e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 63.93 E-value: 5.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 113 KNREGDTPLHIASKYIYGYSdicsiIDEDQADSARKYNTATKK--------IINALVSENAEIDPVNKYQLTPLHYAAMK 184
Cdd:PHA02876 114 KHKLDEACIHILKEAISGND-----IHYDKINESIEYMKLIKEriqqdellIAEMLLEGGADVNAKDIYCITPIHYAAER 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 185 SNFSALHALIKLKADVDAEDDNKMTPLLLACVHGSQEIIQELIKANSNVTKRDQRLntvfhIVALRGEPEYLEMMMdhdp 264
Cdd:PHA02876 189 GNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDLSL-----LKAIRNEDLETSLLL---- 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 265 VEAIKALNLFNNEKKTPLRMAVEGNH-----PETLKKILQMEKKNSckwmdREKELIHFAAEKGF-LEVLKALVEAGGNK 338
Cdd:PHA02876 260 YDAGFSVNSIDDCKNTPLHHASQAPSlsrlvPKLLERGADVNAKNI-----KGETPLYLMAKNGYdTENIRTLIMLGADV 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 339 NELNEVKAVPLHVAAQMNQLEVVSYLIEEEKDNIDVVDEQGLTPLMMAVTHDSKKCVEYLIAKKANLTITDKDERTPV-F 417
Cdd:PHA02876 335 NAADRLYITPLHQASTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALhF 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 418 IGAKFNALSSVEYILDhlrkknketersalksptrntlrivsedvRRTMVNMVDRDQNTPMHIVA-SNGYLEMMQLLQKH 496
Cdd:PHA02876 415 ALCGTNPYMSVKTLID-----------------------------RGANVNSKNKDLSTPLHYACkKNCKLDVIEMLLDN 465
|
....*...
gi 212645948 497 GASITQVN 504
Cdd:PHA02876 466 GADVNAIN 473
|
|
| TRPV1-4 |
cd22193 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ... |
792-1128 |
8.10e-10 |
|
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: 62.89 E-value: 8.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 792 LLNHPLSKaLLKYKWNRLGRPMYYFALFMYLVFIVSLTQYvrhtkapynvwneeSYYDSEyfDENETCPQINTTKPD--- 868
Cdd:cd22193 287 LTLEPLNT-LLQDKWDKFAKYMFFFSFCFYLFYMIIFTLV--------------AYYRPR--EDEPPPPLAKTTKMDymr 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 869 VVWKIIIQTLAVCQILVECFQLFQRKfayLVNWENWIDC------FIYS--TALITVYDFSEcsatsgvrqnWQWILAAL 940
Cdd:cd22193 350 LLGEILVLLGGVYFFVKEIAYFLLRR---SDLQSSFSDSyfeilfFVQAvlVILSVVLYLFA----------YKEYLACL 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 941 --CIFFGWINLLFMIRKMPRFGIFVVMFVD-IVKTFFRFFPVFVLFIIAFSSSFYVILQ--NRPEFSTIFMSPLKTTVMM 1015
Cdd:cd22193 417 vlALALGWANMLYYTRGFQSMGIYSVMIQKvILRDLLRFLFVYLLFLFGFAVALVSLIEkcSSDKKDCSSYGSFSDAVLE 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 1016 IgeFEFTgIFHGDETTHAEKMFgpahTAVACALFFFFCIIMTILLMNLLVGLAVDDIKGV-QEKAELKRLAMQVDlVLQI 1094
Cdd:cd22193 497 L--FKLT-IGMGDLEFQENSTY----PAVFLILLLTYVILTFVLLLNMLIALMGETVNNVsKESKRIWKLQRAIT-ILEF 568
|
330 340 350
....*....|....*....|....*....|....
gi 212645948 1095 EaslhffiqrtKKYATCRYATFPYGKLHKTGFAG 1128
Cdd:cd22193 569 E----------KSFPECMRKAFRSGRLLKVGLCK 592
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
42-114 |
1.49e-09 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 55.89 E-value: 1.49e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 212645948 42 DARTEADNLRSIIHQSAREGNVNALQEALLKAplAVNAQDGDfMTPLHYAARYGNYDAVKLLLSKNALPNTKN 114
Cdd:pfam12796 22 DANLQDKNGRTALHLAAKNGHLEIVKLLLEHA--DVNLKDNG-RTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
174-227 |
2.85e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 53.82 E-value: 2.85e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 212645948 174 QLTPLHYAAMKSNFSALHALIKLKADVDAEDDNKMTPLLLACVHGSQEIIQELI 227
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
51-104 |
1.52e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 51.89 E-value: 1.52e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 212645948 51 RSIIHQSAREGNVNALQeALLKAPLAVNAQDGDFMTPLHYAARYGNYDAVKLLL 104
Cdd:pfam13637 2 LTALHAAAASGHLELLR-LLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
85-126 |
2.21e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 51.51 E-value: 2.21e-08
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 212645948 85 MTPLHYAARYGNYDAVKLLLSKNALPNTKNREGDTPLHIASK 126
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAAS 43
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
538-656 |
3.09e-08 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 57.96 E-value: 3.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 538 DEMGNSALHLAARSGHDATTKVLLDNGADKEAKNSYQKTPLQVAVDSGKLETCQRLVakgaQIESSSDTKT---VLHTAA 614
Cdd:PLN03192 555 DSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY----HFASISDPHAagdLLCTAA 630
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 212645948 615 FYGNESIVRYFIAEGVTIDRRDEEGKTAFDIACENDHKDVAR 656
Cdd:PLN03192 631 KRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVR 672
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
211-299 |
3.66e-08 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 52.04 E-value: 3.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 211 LLLACVHGSQEIIQELIKANSNVTKRDQRLNTVFHIVALRGEPEYLEMMMDHDPVEAikalnlfNNEKKTPLRMAVEGNH 290
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL-------KDNGRTALHYAARSGH 73
|
....*....
gi 212645948 291 PETLKKILQ 299
Cdd:pfam12796 74 LEIVKLLLE 82
|
|
| TRPV1 |
cd22196 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ... |
792-1098 |
5.14e-08 |
|
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: 57.12 E-value: 5.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 792 LLNHPLSKaLLKYKWNRLGRPMYYFALFMYLVFIVSLT--QYVRHTKAPYNVWNEESYydSEYFdenETCPQINTTKPDV 869
Cdd:cd22196 305 LLVEPLNK-LLQDKWDKFVKRIFYFNFFVYFIYMIIFTlaAYYRPVNKTPPFPIENTT--GEYL---RLTGEIISVSGGV 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 870 VWKII-IQTLavcqilvecfqLFQRKFAYLVNWENWIDCFIYSTALI----TVYDFSecsatsgvRQNWQWILAALCIFF 944
Cdd:cd22196 379 YFFFRgIQYF-----------LQRRPSLKKLIVDSYCEILFFVQSLFllasTVLYFC--------GRNEYVAFMVISLAL 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 945 GWINLLFMIRKMPRFGIFVVMFVD-IVKTFFRFFPVFVLFIIAFSSSFYVILQNRPE----------------------- 1000
Cdd:cd22196 440 GWANVLYYTRGFQQMGIYSVMIQKmILRDICRFLFVYLVFLFGFSAALVTLIEDGPPkgdvntsqkecvcksgynsynsl 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 1001 FSTiFMSPLKTTVMMiGEFEFTGIFHgdetthaekmfgpaHTAVACALFFFFCIIMTILLMNLLVGLAVDDIKGV-QEKA 1079
Cdd:cd22196 520 YST-CLELFKFTIGM-GDLEFTENYK--------------FKEVFIFLLISYVILTYILLLNMLIALMGETVSKIaQESK 583
|
330
....*....|....*....
gi 212645948 1080 ELKRLAMQVDlVLQIEASL 1098
Cdd:cd22196 584 NIWKLQRAIT-ILDLEKSL 601
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
348-399 |
7.08e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 49.97 E-value: 7.08e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 212645948 348 PLHVAAQMNQLEVVSYLIEEEKDnIDVVDEQGLTPLMMAVTHDSKKCVEYLI 399
Cdd:pfam13637 4 ALHAAAASGHLELLRLLLEKGAD-INAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
608-659 |
7.73e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 49.97 E-value: 7.73e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 212645948 608 TVLHTAAFYGNESIVRYFIAEGVTIDRRDEEGKTAFDIACENDHKDVARAFL 659
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| TRPV2 |
cd22197 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ... |
796-1107 |
1.12e-07 |
|
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: 56.02 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 796 PLSKaLLKYKWNRLGrPMYYFALFMYLVFIVSLTQYVRHTKApynvwneesyydseyfDENETCPQINTTKPD---VVWK 872
Cdd:cd22197 307 PLNK-LLQEKWDRLV-SRFYFNFLCYLVYMFIFTVVAYHQPL----------------LDQPPIPPLKATAGGsmlLLGH 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 873 IIIQT----LAVCQILvecFQLFQRKFAYLVNWENWIDCFIYSTALITVYDFSECSATSgvrqNWQWILAALCIFFGWIN 948
Cdd:cd22197 369 ILILLggiyLLLGQLW---YFWRRRLFIWISFMDSYFEILFLLQALLTVLSQVLYFMGS----EWYLPLLVFSLVLGWLN 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 949 LLFMIRKMPRFGIFVVMFVD-IVKTFFRFFPVFVLFIIAFSSSFYVILQNRPEFSTIfMSPLKTTVMMIGE--------- 1018
Cdd:cd22197 442 LLYYTRGFQHTGIYSVMIQKvILRDLLRFLLVYLVFLFGFAVALVSLSREAPSPKAP-EDNNSTVTEQPTVgqeeepapy 520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 1019 ----------FEFTgIFHGDETTHAEKMFgpahTAVACALFFFFCIIMTILLMNLLVGLAVDDIKGVQEKA----ELKRL 1084
Cdd:cd22197 521 rsildaslelFKFT-IGMGELAFQEQLRF----RGVVLLLLLAYVLLTYVLLLNMLIALMSETVNHVADNSwsiwKLQKA 595
|
330 340
....*....|....*....|...
gi 212645948 1085 AMqvdlVLQIEASLHFFIQRTKK 1107
Cdd:cd22197 596 IS----VLEMENGYWWCRRKKQR 614
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
347-598 |
1.27e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 55.38 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 347 VPLHVAAQMNQLEVVSYLIEEEKD-NIDVVDeqGLTPLMMAVTHDSKKCVEYLIAKKANLTITDKDERTPVFIGAKFNAL 425
Cdd:PHA02875 4 VALCDAILFGELDIARRLLDIGINpNFEIYD--GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 426 SSVEYILDhlrkknketersalksptrntLRIVSEDVrrtmvnmVDRDQNTPMHIVASNGYLEMMQLLQKHGASITQVNE 505
Cdd:PHA02875 82 KAVEELLD---------------------LGKFADDV-------FYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNT 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 506 DEETALHRAAIGGQTGAVRQLLEWDIRLLLmKDEMGNSALHLAARSGHDATTKVLLDNGADkeaKNSYQKTP----LQVA 581
Cdd:PHA02875 134 DKFSPLHLAVMMGDIKGIELLIDHKACLDI-EDCCGCTPLIIAMAKGDIAICKMLLDSGAN---IDYFGKNGcvaaLCYA 209
|
250
....*....|....*..
gi 212645948 582 VDSGKLETCQRLVAKGA 598
Cdd:PHA02875 210 IENNKIDIVRLFIKRGA 226
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
39-214 |
1.74e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 55.27 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 39 AELDARTEaDNLRSIIHQSAREGNVNaLQEALLKAPLAVNAQDGDFMTPLHYAARYGNYDAVKLLLSKNALPNTKNREGD 118
Cdd:PHA02878 158 ADINMKDR-HKGNTALHYATENKDQR-LTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGN 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 119 TPLHIASKYIYGYsDICSIIDEDQADSarkynTATKKIINalvsenaeidpvnkyqLTPLHyAAMKSNfSALHALIKLKA 198
Cdd:PHA02878 236 TPLHISVGYCKDY-DILKLLLEHGVDV-----NAKSYILG----------------LTALH-SSIKSE-RKLKLLLEYGA 291
|
170
....*....|....*.
gi 212645948 199 DVDAEDDNKMTPLLLA 214
Cdd:PHA02878 292 DINSLNSYKLTPLSSA 307
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
49-233 |
2.71e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 54.61 E-value: 2.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 49 NLRSIIHQSAREGNVNALQEALLKAPLAVNAQDGDFMTPLHYAARYGNYDAVKLLLSKNALPNTKNREGDTPLHIAskyi 128
Cdd:PHA02875 67 DIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLA---- 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 129 ygysdicsIIDEDqadsarkyntatKKIINALVSENAEIDPVNKYQLTPLHYAAMKSNFSALHALIKLKADVDAEDDNKM 208
Cdd:PHA02875 143 --------VMMGD------------IKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGC 202
|
170 180
....*....|....*....|....*...
gi 212645948 209 TPLLLACVHGSQ-EIIQELIK--ANSNV 233
Cdd:PHA02875 203 VAALCYAIENNKiDIVRLFIKrgADCNI 230
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
471-604 |
2.96e-07 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 54.87 E-value: 2.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 471 DRDQNTPMHIVASNGYLEMMQLLQKHGASITQVNEDEETALHRAAIGGQTGAVRQLLEWDirlLLMKDEMGNSALHLAAR 550
Cdd:PLN03192 555 DSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFA---SISDPHAAGDLLCTAAK 631
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 212645948 551 SGHDATTKVLLDNGADKEAKNSYQKTPLQVAVDSGKLETCQRLVAKGAQIESSS 604
Cdd:PLN03192 632 RNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
62-131 |
4.47e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 53.90 E-value: 4.47e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 212645948 62 NVNALQ--EALLKAPLAVNAQDGDFMTPLHYAARYGNYDAVKLLLSKNALPNTKNREGDTPLHIASKYIYGY 131
Cdd:PHA03100 168 DINAKNrvNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKE 239
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
293-508 |
4.73e-07 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 54.10 E-value: 4.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 293 TLKKILQMEKKNSCKWMdreKELIHFAAEKGFLEVLKALVEAGGNKNelNEVKAVPLHVAAQMNQLEVVSYLIEEEKDNi 372
Cdd:PLN03192 478 TLIEAMQTRQEDNVVIL---KNFLQHHKELHDLNVGDLLGDNGGEHD--DPNMASNLLTVASTGNAALLEELLKAKLDP- 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 373 DVVDEQGLTPLMMAVTHDSKKCVEYLIAKKANLTITDKDERTpvfigAKFNALSSVEY----ILDHL-RKKNKETERSAL 447
Cdd:PLN03192 552 DIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNT-----ALWNAISAKHHkifrILYHFaSISDPHAAGDLL 626
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 212645948 448 -KSPTRNTLRIVSEDVRRTM-VNMVDRDQNTPMHIVASNGYLEMMQLLQKHGASITQVNEDEE 508
Cdd:PLN03192 627 cTAAKRNDLTAMKELLKQGLnVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDD 689
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
480-712 |
6.04e-07 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 53.49 E-value: 6.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 480 IVASNGYLEMMQLLQKHGASITQVNEDEETALH---RAAIGGQTGAVRQLLEWDIRLLLmKDEMGNSALHLAARSghdAT 556
Cdd:PHA03095 20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHlylHYSSEKVKDIVRLLLEAGADVNA-PERCGFTPLHLYLYN---AT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 557 T----KVLLDNGADKEAKNSYQKTPLQV-----AVDSGKLETcqrLVAKGAQIEsssDTKTVLHT--AAFYGNE----SI 621
Cdd:PHA03095 96 TldviKLLIKAGADVNAKDKVGRTPLHVylsgfNINPKVIRL---LLRKGADVN---ALDLYGMTplAVLLKSRnanvEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 622 VRYFIAEGVTIDRRDEEGKTAFDIACENDHKDvARAFLEtdqwkNLMIPCDVIPLDKHRNpvnmkrrTPFRTLLTKFPEL 701
Cdd:PHA03095 170 LRLLIDAGADVYAVDDRFRSLLHHHLQSFKPR-ARIVRE-----LIRAGCDPAATDMLGN-------TPLHSMATGSSCK 236
|
250
....*....|.
gi 212645948 702 ASfVMDNCIEK 712
Cdd:PHA03095 237 RS-LVLPLLIA 246
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
154-401 |
6.58e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 53.35 E-value: 6.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 154 KKIINALVSENAEIDPVNKYQLTPLHYAAMKSNFSALHALIKLKADVDAEDDNKMTPLLLACVHGSQEIIQELIkanSNV 233
Cdd:PHA02878 17 LKYIEYIDHTENYSTSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMI---RSI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 234 TKRD-----QRLNTVFHivalrgepeylemmmdHDPVEAIKAL--NLFNNEKKTPLRMAVEGNH-----PETLKKILQME 301
Cdd:PHA02878 94 NKCSvfytlVAIKDAFN----------------NRNVEIFKIIltNRYKNIQTIDLVYIDKKSKddiieAEITKLLLSYG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 302 KKNSCKWMDREKELIHFAAEKGFLEVLKALVEAGGNKNELNEVKAVPLHVAAQMNQLEVVSYLIEEEKdNIDVVDEQGLT 381
Cdd:PHA02878 158 ADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA-STDARDKCGNT 236
|
250 260
....*....|....*....|
gi 212645948 382 PLMMAVTHdskkCVEYLIAK 401
Cdd:PHA02878 237 PLHISVGY----CKDYDILK 252
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
474-527 |
8.46e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 46.88 E-value: 8.46e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 212645948 474 QNTPMHIVASNGYLEMMQLLQKHGASITQVNEDEETALHRAAIGGQTGAVRQLL 527
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
576-626 |
1.19e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 46.50 E-value: 1.19e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 212645948 576 TPLQVAVDSGKLETCQRLVAKGAQI-ESSSDTKTVLHTAAFYGNESIVRYFI 626
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADInAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
314-365 |
1.26e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 46.50 E-value: 1.26e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 212645948 314 ELIHFAAEKGFLEVLKALVEAGGNKNELNEVKAVPLHVAAQMNQLEVVSYLI 365
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
58-235 |
1.64e-06 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 52.56 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 58 AREGNvNALQEALLKAPLAVNAQDGDFMTPLHYAARYGNYDAVKLLLSKNALPNTKNREGDTPL--HIASKYiygysdic 135
Cdd:PLN03192 533 ASTGN-AALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnAISAKH-------- 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 136 siidedqadsarkyntatKKIINALVSENAEIDPVNKYQLtpLHYAAMKSNFSALHALIKLKADVDAEDDNKMTPLLLAC 215
Cdd:PLN03192 604 ------------------HKIFRILYHFASISDPHAAGDL--LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAM 663
|
170 180
....*....|....*....|
gi 212645948 216 VHGSQEIIQELIKANSNVTK 235
Cdd:PLN03192 664 AEDHVDMVRLLIMNGADVDK 683
|
|
| TRPV4 |
cd22195 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed ... |
801-1104 |
4.29e-06 |
|
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: 51.01 E-value: 4.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 801 LLKYKWNRLGRPMYYFALFMYLV--FIVSLTQYVRHT--KAPYNVWNEESYYDseyfdenetcpqinttkpdVVWKIIIQ 876
Cdd:cd22195 357 LLRDKWRKFGAVSFYISVVSYLVamIIFTLIAYYRPMegTPPYPYRTTVDYLR-------------------LAGEIITL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 877 TLAVCQILVECFQLFQRKF----AYLVNWENWIDCFIYSTALITvydfSECSATSGVRQNWQWILAALCIffGWINLLFM 952
Cdd:cd22195 418 LTGIFFFFTNIKDLFMKKCpgvnSLFIDGSFQLLYFIYSVLVIV----TAALYLAGIEAYLAVMVFALVL--GWMNALYF 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 953 IRKMPRFGIFVVMFVDI-VKTFFRFFPVFVLFIIAFSSSFYVILQ---------------NRPE---------FSTIFMS 1007
Cdd:cd22195 492 TRGLKLTGTYSIMIQKIlFKDLFRFLLVYLLFMIGYASALVSLLNpcptketckedstncTVPTypscrdsntFSKFLLD 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 1008 PLKTTVMMigefeftgifhGDetthAEKMFGPAHTAVACALFFFFCIIMTILLMNLLVGLAVDDIKGVQEKAELKRLAMQ 1087
Cdd:cd22195 572 LFKLTIGM-----------GD----LEMLNSAKYPAVFIILLVTYIILTFVLLLNMLIALMGETVGQVSKESKQIWKLQW 636
|
330
....*....|....*..
gi 212645948 1088 VDLVLQIEASLHFFIQR 1104
Cdd:cd22195 637 ATTILDIERSFPVFLRK 653
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
280-433 |
4.88e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 50.37 E-value: 4.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 280 TPLRMAVEGNHPETLKKILQMEKKNSCKWMDREKELiHFAAEKGFLEVLKALVEAGGNKNELNEVKA-VPLHVAAQMNQL 358
Cdd:PHA02875 37 SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESEL-HDAVEEGDVKAVEELLDLGKFADDVFYKDGmTPLHLATILKKL 115
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 212645948 359 EVVSYLIEEEKDNiDVVDEQGLTPLMMAVTHDSKKCVEYLIAKKANLTITDKDERTPVFIGAKFNALSSVEYILD 433
Cdd:PHA02875 116 DIMKLLIARGADP-DIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLD 189
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
289-432 |
2.48e-05 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411978 [Multi-domain] Cd Length: 680 Bit Score: 48.60 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 289 NHPETLKKILQMEKKNSC--KWMDREKE--------LIHFAAEKGFLEVLKALVEAGGN--------------KNELNEV 344
Cdd:cd22194 108 NTKEIVRILLAFAEENGIldRFINAEYTeeayegqtALNIAIERRQGDIVKLLIAKGADvnahakgvffnpkyKHEGFYF 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 345 KAVPLHVAAQMNQLEVVSYLIEEEKDNIDVVDEQGLTPL--MMAVTHDSKKCVEYLI---------AKKANL-TITDKDE 412
Cdd:cd22194 188 GETPLALAACTNQPEIVQLLMEKESTDITSQDSRGNTVLhaLVTVAEDSKTQNDFVKrmydmillkSENKNLeTIRNNEG 267
|
170 180
....*....|....*....|
gi 212645948 413 RTPVFIGAKFNALSSVEYIL 432
Cdd:cd22194 268 LTPLQLAAKMGKAEILKYIL 287
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
541-594 |
2.68e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 42.65 E-value: 2.68e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 212645948 541 GNSALHLAARSGHDATTKVLLDNGADKEAKNSYQKTPLQVAVDSGKLETCQRLV 594
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
467-514 |
3.05e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 42.72 E-value: 3.05e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 212645948 467 VNMVDRDQNTPMHIVASNGYLEMMQLLQKHGASITQVNEDEETALHRA 514
Cdd:pfam13857 9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
608-646 |
3.93e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 42.33 E-value: 3.93e-05
10 20 30
....*....|....*....|....*....|....*....
gi 212645948 608 TVLHTAAFYGNESIVRYFIAEGVTIDRRDEEGKTAFDIA 646
Cdd:pfam13857 18 TPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
83-111 |
4.56e-05 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 41.42 E-value: 4.56e-05
10 20
....*....|....*....|....*....
gi 212645948 83 DFMTPLHYAARYGNYDAVKLLLSKNALPN 111
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
85-115 |
4.62e-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: 41.51 E-value: 4.62e-05
10 20 30
....*....|....*....|....*....|..
gi 212645948 85 MTPLHYAA-RYGNYDAVKLLLSKNALPNTKNR 115
Cdd:pfam00023 3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
57-303 |
4.82e-05 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 47.77 E-value: 4.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 57 SAREGNVNALQEALLKA-PLAVNAQDGDFMTPLHYAARYG-NYDAVKLLLSKNALPntknREGDTPLHIASKyiyGYSDI 134
Cdd:TIGR00870 24 AAERGDLASVYRDLEEPkKLNINCPDRLGRSALFVAAIENeNLELTELLLNLSCRG----AVGDTLLHAISL---EYVDA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 135 CSIIDEDQADSARKYNTATKKIINALVSENAEIdpvnkyqlTPLHYAAMKSNFSALHALIKLKADVDAE---DDNKMTPL 211
Cdd:TIGR00870 97 VEAILLHLLAAFRKSGPLELANDQYTSEFTPGI--------TALHLAAHRQNYEIVKLLLERGASVPARacgDFFVKSQG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 212 ------------LLACVhGSQEIIQELIKANSNVTKRDQRLNTVFHIVALRGE--PEYLEMMMD------------HDPV 265
Cdd:TIGR00870 169 vdsfyhgesplnAAACL-GSPSIVALLSEDPADILTADSLGNTLLHLLVMENEfkAEYEELSCQmynfalslldklRDSK 247
|
250 260 270
....*....|....*....|....*....|....*...
gi 212645948 266 EAIKALnlfNNEKKTPLRMAVEGNHPETLKKILQMEKK 303
Cdd:TIGR00870 248 ELEVIL---NHQGLTPLKLAAKEGRIVLFRLKLAIKYK 282
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
68-238 |
5.54e-05 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 46.97 E-value: 5.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 68 EALLKAPLAVNAQDGDFMTPLHYAARYGNYDAVKLLLSKNALPNTKNREGDTPLHiaskYIYGYSD-------------- 133
Cdd:PHA02946 56 EELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLY----YLSGTDDevierinllvqyga 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 134 -ICSIIDEDQADSARKYNTATKKIINALVSENAEIDPVNKYQLTPLHYAAMKSN--FSALHALIKLKADVDAEDDNKMTP 210
Cdd:PHA02946 132 kINNSVDEEGCGPLLACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNpkASTISWMMKLGISPSKPDHDGNTP 211
|
170 180
....*....|....*....|....*....
gi 212645948 211 LLLACVHGSQEI-IQELIKANSNVTKRDQ 238
Cdd:PHA02946 212 LHIVCSKTVKNVdIINLLLPSTDVNKQNK 240
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
379-432 |
8.46e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 41.49 E-value: 8.46e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 212645948 379 GLTPLMMAVTHDSKKCVEYLIAKKANLTITDKDERTPVFIGAKFNALSSVEYIL 432
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
796-1080 |
1.18e-04 |
|
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: 46.29 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 796 PLsKALLKYKWNRLGRPMYYFALFMYLVFIVSLTQYvrhtkapynvwneeSYYDseyfdenetcPQINTTKPDVV----- 870
Cdd:cd22194 350 PL-HTLLHMKWKKFARYMFFISFLFYFFYNITLTLV--------------SYYR----------PREDEDPPHPLalshk 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 871 ---WKIIIQTL----AVCQIL---VECFQLFQRKFAYLVNwENWIDCFIYSTALITVydFSECSATSGVRQNWQWILAAL 940
Cdd:cd22194 405 mgwLQLLGQMFvliwATCLSVkegIAIFLLRPSDLKSILS-DAWFHILFFIQAVLVI--VSVFLYLFAYKEYLACLVLAM 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 941 CIffGWINLLFMIRKMPRFGIFVVMFVD-IVKTFFRFFPVFVLFIIAFSSSFYVILQNRPEFSTIF-MSPLKTTVMMIge 1018
Cdd:cd22194 482 AL--GWANMLYYTRGFQSLGIYSVMIQKvILNDVLKFLLVYILFLLGFGVALASLIEDCPDDSECSsYGSFSDAVLEL-- 557
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 212645948 1019 FEFTgIFHGDETTHAEkmfgPAHTAVACALFFFFCIIMTILLMNLLVGLAVDDIKGVQEKAE 1080
Cdd:cd22194 558 FKLT-IGLGDLEIQQN----SKYPILFLLLLITYVILTFVLLLNMLIALMGETVENVSKESE 614
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
526-581 |
1.23e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 40.79 E-value: 1.23e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 212645948 526 LLEWDIRLLLMKDEMGNSALHLAARSGHDATTKVLLDNGADKEAKNSYQKTPLQVA 581
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PKD_channel |
pfam08016 |
Polycystin cation channel; This family contains the cation channel region from group II of ... |
936-1067 |
1.55e-04 |
|
Polycystin cation channel; This family contains the cation channel region from group II of Transient receptor potential (TRP) channels, the TRPP subfamily, including PKD1, PKD2, PKD2L and mucolipin proteins.
Pssm-ID: 462341 [Multi-domain] Cd Length: 225 Bit Score: 44.57 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 936 ILAALCIFFGWINLLFMIRKMPRFGIFVVMFVDIVKTFFRFFPVFVLFIIAFSSSFYVIL-QNRPEFSTIFMSPLKTTVM 1014
Cdd:pfam08016 98 IILAFLVFLTWLKLFKVLRFNKTMSLFTKTLSRAWKDLAGFALMFVIFFFAYAQFGYLLFgTQAPNFSNFVKSILTLFRT 177
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 212645948 1015 MIGEFEFTGIFHGDetthaeKMFGPahtavacALFFFFCIIMTILLMNLLVGL 1067
Cdd:pfam08016 178 ILGDFGYNEIFSGN------RVLGP-------LLFLTFVFLVIFILLNLFLAI 217
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
531-593 |
2.62e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 45.27 E-value: 2.62e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 531 IRLLLM-------KDEMGNSALHLAARSGHDATTKVLLDNGADKEAKNSYQKTPLQVAVDSGKLETCQRL 593
Cdd:PTZ00322 98 ARILLTggadpncRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
85-112 |
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 212645948 85 MTPLHYAARYGNYDAVKLLLSKNALPNT 112
Cdd:pfam13606 3 NTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
541-571 |
4.01e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 38.81 E-value: 4.01e-04
10 20 30
....*....|....*....|....*....|..
gi 212645948 541 GNSALHLAA-RSGHDATTKVLLDNGADKEAKN 571
Cdd:pfam00023 2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
488-661 |
5.54e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 43.83 E-value: 5.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 488 EMMQLLQKHGASITQVNEDEETALHRAAIGGQTGAVRQLLEWD--IRLLLMKDemGNSALHLAARSGHDATTKVLLDNGA 565
Cdd:PHA02875 49 EAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGkfADDVFYKD--GMTPLHLATILKKLDIMKLLIARGA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 566 DKEAknsyqktplqvavdsgkletcqrlvakgaqieSSSDTKTVLHTAAFYGNESIVRYFIAEGVTIDRRDEEGKTAFDI 645
Cdd:PHA02875 127 DPDI--------------------------------PNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLII 174
|
170
....*....|....*.
gi 212645948 646 ACENDHKDVARAFLET 661
Cdd:PHA02875 175 AMAKGDIAICKMLLDS 190
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
546-659 |
1.31e-03 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 42.96 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 546 HLAArSGHDATTKVLLDNGADKEAKNSYQKTPLqvavdsgkletcqrlvakgaqiesssdtktvlHTAAFYGNESIVRYF 625
Cdd:PTZ00322 88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPL--------------------------------HIACANGHVQVVRVL 134
|
90 100 110
....*....|....*....|....*....|....
gi 212645948 626 IAEGVTIDRRDEEGKTAFDIACENDHKDVARAFL 659
Cdd:PTZ00322 135 LEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
364-416 |
1.40e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 38.10 E-value: 1.40e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 212645948 364 LIEEEKDNIDVVDEQGLTPLMMAVTHDSKKCVEYLIAKKANLTITDKDERTPV 416
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
378-410 |
1.51e-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: 37.27 E-value: 1.51e-03
10 20 30
....*....|....*....|....*....|....
gi 212645948 378 QGLTPLMMAVTH-DSKKCVEYLIAKKANLTITDK 410
Cdd:pfam00023 1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
155-194 |
1.60e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 37.64 E-value: 1.60e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 212645948 155 KIINALVSENAEIDPVNKYQLTPLHYAAMKSNFSALHALI 194
Cdd:pfam13637 15 ELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
509-561 |
1.72e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 37.64 E-value: 1.72e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 212645948 509 TALHRAAIGGQTGAVRQLLE--WDIRlllMKDEMGNSALHLAARSGHDATTKVLL 561
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEkgADIN---AVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
256-404 |
2.13e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 41.90 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 256 LEMMMDHDPVEAIKAL---NLFNNEK----KTPLRMAVEGNHPETLKKILQMEKKNSCKWMDREKELIHFAAEKGFLEVL 328
Cdd:PHA02875 39 IKLAMKFRDSEAIKLLmkhGAIPDVKypdiESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIM 118
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 212645948 329 KALVEAGGNKNELNEVKAVPLHVAAQMNQLEVVSYLIEEeKDNIDVVDEQGLTPLMMAVTHDSKKCVEYLIAKKAN 404
Cdd:PHA02875 119 KLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDH-KACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGAN 193
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
174-365 |
2.85e-03 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 41.78 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 174 QLTPLHYAAMKSNFSALHALIK------LKADVDAEDDNKMTP--LLLACVHGSQEIIQELIKANSNVTKRDQRLNTVFH 245
Cdd:PLN03192 484 QTRQEDNVVILKNFLQHHKELHdlnvgdLLGDNGGEHDDPNMAsnLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLH 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 246 IVALRGEPEYLEMMMDHDPVEAIKALNlfnneKKTPLRMAVEGNHPETLKKILQMEKKNSCKwmdREKELIHFAAEKGFL 325
Cdd:PLN03192 564 IAASKGYEDCVLVLLKHACNVHIRDAN-----GNTALWNAISAKHHKIFRILYHFASISDPH---AAGDLLCTAAKRNDL 635
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 212645948 326 EVLKALVEAGGNKNELNEVKAVPLHVAAQMNQLEVVSYLI 365
Cdd:PLN03192 636 TAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLI 675
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
468-527 |
3.10e-03 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 41.81 E-value: 3.10e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 468 NMVDRDQNTPMHIVASNGYLEMMQLLQKHGASITQVNEDEETALhRAAIGGQTGAVRQLL 527
Cdd:PTZ00322 109 NCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPL-ELAEENGFREVVQLL 167
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
76-138 |
3.47e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 41.49 E-value: 3.47e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 212645948 76 AVNAQDGDFMTPLHYAARYG-NYDAVKLLLSKNALPNTKNREGDTPLHIASKYIYGYSDICSII 138
Cdd:PHA02874 246 SINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAFKYINKDPVIKDII 309
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
540-569 |
3.72e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 36.03 E-value: 3.72e-03
10 20 30
....*....|....*....|....*....|
gi 212645948 540 MGNSALHLAARSGHDATTKVLLDNGADKEA 569
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
541-566 |
4.07e-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: 36.08 E-value: 4.07e-03
10 20
....*....|....*....|....*.
gi 212645948 541 GNSALHLAARSGHDATTKVLLDNGAD 566
Cdd:pfam13606 2 GNTPLHLAARNGRLEIVKLLLENGAD 27
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
538-605 |
4.17e-03 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 41.19 E-value: 4.17e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 538 DEMGNSALHLAARSGHDATTKVLLDNGADKEAKNSYQKTPLQV--AVDSGKLETCQRLVAKGAQIESSSD 605
Cdd:PHA02946 69 DDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYlsGTDDEVIERINLLVQYGAKINNSVD 138
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
473-501 |
4.27e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 36.03 E-value: 4.27e-03
10 20
....*....|....*....|....*....
gi 212645948 473 DQNTPMHIVASNGYLEMMQLLQKHGASIT 501
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
150-303 |
5.22e-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: 40.90 E-value: 5.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 150 NTATKKIINALVS-----------ENAEIDPVNKYQLTPLHYAAMKSNFSALHALIKLKADVDA-------EDDNKM--- 208
Cdd:cd22194 106 NENTKEIVRILLAfaeengildrfINAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAhakgvffNPKYKHegf 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 209 ----TPLLLACVHGSQEIIQELI-KANSNVTKRDQRLNTVFH---IVALRGEPE-------YLEMMMDHD--PVEAIKal 271
Cdd:cd22194 186 yfgeTPLALAACTNQPEIVQLLMeKESTDITSQDSRGNTVLHalvTVAEDSKTQndfvkrmYDMILLKSEnkNLETIR-- 263
|
170 180 190
....*....|....*....|....*....|..
gi 212645948 272 nlfNNEKKTPLRMAVEGNHPETLKKILQMEKK 303
Cdd:cd22194 264 ---NNEGLTPLQLAAKMGKAEILKYILSREIK 292
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
378-407 |
5.67e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 35.64 E-value: 5.67e-03
10 20 30
....*....|....*....|....*....|
gi 212645948 378 QGLTPLMMAVTHDSKKCVEYLIAKKANLTI 407
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
412-493 |
6.00e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 36.10 E-value: 6.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 412 ERTPVFIGAKFNALSSVEYILDHlrkknketersalksptrntlrivsedvrRTMVNMVDRDQNTPMHIVASNGYLEMMQ 491
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEK-----------------------------GADINAVDGNGETALHFAASNGNVEVLK 51
|
..
gi 212645948 492 LL 493
Cdd:pfam13637 52 LL 53
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
557-646 |
8.00e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 40.25 E-value: 8.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645948 557 TKVLLDNGADKEAKNSYQ-KTPLQVAVDSGKLETCQRLVAKGAQIESSSDT-KTVLHTAAFYGNESIVRYFIAEGVTIDR 634
Cdd:PHA02878 150 TKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTnNSPLHHAVKHYNKPIVHILLENGASTDA 229
|
90
....*....|..
gi 212645948 635 RDEEGKTAFDIA 646
Cdd:PHA02878 230 RDKCGNTPLHIS 241
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
492-548 |
8.92e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 35.79 E-value: 8.92e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 212645948 492 LLQKHGASITQVNEDEETALHRAAIGGQTGAVRQLLEWDIrLLLMKDEMGNSALHLA 548
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGV-DLNLKDEEGLTALDLA 56
|
|
| |
