|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
81-370 |
2.24e-49 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 177.07 E-value: 2.24e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 81 AEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNV 160
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 161 NVSDRAGRTALHHAAFSGHVEMVSLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVTHGAEVMCKDKKSYTPLHAA 240
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 241 ASSGMISVIKYLLDLGVDMNESNAYGNTPLHVACYNGQDVVVNELIDCGANVNQVNERGFTPLHFAAASTHGALCLELLV 320
Cdd:COG0666 161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1785376409 321 cNGADVNIKSKDGKTPLHMTAIHGRFSRSQIIIQNGAEIDCEDKNGNTPL 370
Cdd:COG0666 241 -AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
27-303 |
9.86e-49 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 175.14 E-value: 9.86e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 27 KILTPPGIVTPPLVQAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLH 106
Cdd:COG0666 13 AALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 107 RAVASCSEDAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHVEMVSLL 186
Cdd:COG0666 93 AAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 187 LSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVTHGAEVMCKDKKSYTPLHAAASSGMISVIKYLLDLGVDMNESNAYG 266
Cdd:COG0666 173 LEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDG 252
|
250 260 270
....*....|....*....|....*....|....*..
gi 1785376409 267 NTPLHVACYNGQDVVVNELIDCGANVNQVNERGFTPL 303
Cdd:COG0666 253 LTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
49-319 |
1.31e-47 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 172.06 E-value: 1.31e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 49 DEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQVLLKHSADVN 128
Cdd:COG0666 2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 129 ARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHVEMVSLLLSRGANINAFDKKDRRAIHWAA 208
Cdd:COG0666 82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 209 YMGHIEVVKLLVTHGAEVMCKDKKSYTPLHAAASSGMISVIKYLLDLGVDMNESNAYGNTPLHVACYNGQDVVVNELIDC 288
Cdd:COG0666 162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
|
250 260 270
....*....|....*....|....*....|.
gi 1785376409 289 GANVNQVNERGFTPLHFAAASTHGALCLELL 319
Cdd:COG0666 242 GADLNAKDKDGLTALLLAAAAGAALIVKLLL 272
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
150-434 |
1.66e-45 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 165.90 E-value: 1.66e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 150 AEALVPLLSNVNVSDRAGRTALHHAAFSGHVEMVSLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVTHGAEVMCK 229
Cdd:COG0666 4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 230 DKKSYTPLHAAASSGMISVIKYLLDLGVDMNESNAYGNTPLHVACYNGQDVVVNELIDCGANVNQVNERGFTPLHFAAAS 309
Cdd:COG0666 84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 310 THGALcLELLVCNGADVNIKSKDGKTPLHMTAIHGRFSRSQIIIQNGAEIDCEDKNGNTPLHIAARYGHELLINTLITSR 389
Cdd:COG0666 164 GNLEI-VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1785376409 390 ADTSKRGIHGMFPLHLAALSGFSDCCRKLLSSGFDIDTHDDFGRT 434
Cdd:COG0666 243 ADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
180-469 |
2.45e-42 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 156.65 E-value: 2.45e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 180 VEMVSLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVTHGAEVMCKDKKSYTPLHAAASSGMISVIKYLLDLGVDM 259
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 260 NESNAYGNTPLHVACYNGQDVVVNELIDCGANVNQVNERGFTPLHFAAASTHGALcLELLVCNGADVNIKSKDGKTPLHM 339
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI-VKLLLEAGADVNAQDNDGNTPLHL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 340 TAIHGRFSRSQIIIQNGAEIDCEDKNGNTPLHIAARYGHELLINTLITSRADTSKRGIHGMFPLHLAALSGFSDCCRKLL 419
Cdd:COG0666 160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1785376409 420 SSGFDIDTHDDFGRTCLHAAAAGGNLECLNLLLSTGADFNKKDKFGRTPL 469
Cdd:COG0666 240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
49-337 |
1.19e-40 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 157.11 E-value: 1.19e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 49 DEVRALIFKKEDVNFQDNEKRTPLHAaaYLG-----DAEIIELLILSGARVNAKDSKWLTPLHRAV-ASCSEDAVQVLLK 122
Cdd:PHA03095 28 EEVRRLLAAGADVNFRGEYGKTPLHL--YLHyssekVKDIVRLLLEAGADVNAPERCGFTPLHLYLyNATTLDVIKLLIK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 123 HSADVNARDKNWQTPLHIAAANKAVkcaealvpllsnvnvsdragrtalhhaafsgHVEMVSLLLSRGANINAFDKKDRR 202
Cdd:PHA03095 106 AGADVNAKDKVGRTPLHVYLSGFNI-------------------------------NPKVIRLLLRKGADVNALDLYGMT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 203 AIHwaAYMGH----IEVVKLLVTHGAEVMCKDKKSYTPLHAAASSGMIS--VIKYLLDLGVDMNESNAYGNTPLHVACYN 276
Cdd:PHA03095 155 PLA--VLLKSrnanVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATG 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1785376409 277 G--QDVVVNELIDCGANVNQVNERGFTPLHFAAASTHGALCLELLVCnGADVNIKSKDGKTPL 337
Cdd:PHA03095 233 SscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIAL-GADINAVSSDGNTPL 294
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
213-498 |
4.07e-39 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 147.41 E-value: 4.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 213 IEVVKLLVTHGAEVMCKDKKSYTPLHAAASSGMISVIKYLLDLGVDMNESNAYGNTPLHVACYNGQDVVVNELIDCGANV 292
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 293 NQVNERGFTPLHFAAASTHGALcLELLVCNGADVNIKSKDGKTPLHMTAIHGRFSRSQIIIQNGAEIDCEDKNGNTPLHI 372
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEI-VKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 373 AARYGHELLINTLITSRADTSKRGIHGMFPLHLAALSGFSDCCRKLLSSGFDIDTHDDFGRTCLHAAAAGGNLECLNLLL 452
Cdd:COG0666 160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1785376409 453 STGADFNKKDKFGRTPLHYAAANCNYQCLFALVGSGASVNDLDERG 498
Cdd:COG0666 240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
693-1023 |
1.96e-38 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 145.48 E-value: 1.96e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 693 LRLLIGNADVQAAVDIHDGNGQTPLMLSVLNGHTECVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVEALLQHNANF 772
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 773 LLRDCRGRTPIHLAAACGHIGVLSALLQTAISVDVVpaiaDNHGYTPLHWACYNGHDACVELLLEQevfqkmegnsfspl 852
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNAR----DKDGETPLHLAAYNGNLEIVKLLLEA-------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 853 hcavindneGAAemlidtlgtsiVNSVDSKGRTPLHAAAFTDHIECLQLLLSHNAQVNAVDSTGKTPLMMAAENGQTSAV 932
Cdd:COG0666 143 ---------GAD-----------VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 933 EVLVsSAKADLTLQDKNKNTALHLACSKGHETSALLILEQITDrnlINATNSALQTPLHVAARNGLTVVVQELLGKGASV 1012
Cdd:COG0666 203 KLLL-EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD---LNAKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278
|
330
....*....|.
gi 1785376409 1013 LAVDENGYTPA 1023
Cdd:COG0666 279 AAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
249-530 |
7.05e-38 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 143.94 E-value: 7.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 249 IKYLLDLGVDMNESNAYGNTPLHVACYNGQDVVVNELIDCGANVNQVNERGFTPLHFAAASTHGALCLELLVCNGADVNI 328
Cdd:COG0666 3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 329 KSKDGKTPLHMTAIHGRFSRSQIIIQNGAEIDCEDKNGNTPLHIAARYGHELLINTLITSRADTSKRGIHGMFPLHLAAL 408
Cdd:COG0666 83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 409 SGFSDCCRKLLSSGFDIDTHDDFGRTCLHAAAAGGNLECLNLLLSTGADFNKKDKFGRTPLHYAAANCNYQCLFALVGSG 488
Cdd:COG0666 163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1785376409 489 ASVNDLDERGCSPLHYAATSDTDGKCLEYLLRNDANPGIRDK 530
Cdd:COG0666 243 ADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLD 284
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
50-328 |
1.77e-37 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 146.35 E-value: 1.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 50 EVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLH-----RAVASCSEDAVQVLLKHS 124
Cdd:PHA03100 17 NIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 125 ADVNARDKNWQTPLHIAAANKavkcaealvpllsnvnvsdragrtalhhaafSGHVEMVSLLLSRGANINAFDKKDRRAI 204
Cdd:PHA03100 97 ANVNAPDNNGITPLLYAISKK-------------------------------SNSYSIVEYLLDNGANVNIKNSDGENLL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 205 HWAAYMGHI--EVVKLLVTHGAEVMCKDKksytplhaaassgmisvIKYLLDLGVDMNESNAYGNTPLHVACYNGQDVVV 282
Cdd:PHA03100 146 HLYLESNKIdlKILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFV 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1785376409 283 NELIDCGANVNQVNERGFTPLHFAAASTHGALcLELLVCNGADVNI 328
Cdd:PHA03100 209 KYLLDLGANPNLVNKYGDTPLHIAILNNNKEI-FKLLLNNGPSIKT 253
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
290-552 |
1.82e-37 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 142.79 E-value: 1.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 290 ANVNQVNERGFTPLHFAAASTHGALCLELLVCNGADVNIKSKDGKTPLHMTAIHGRFSRSQIIIQNGAEIDCEDKNGNTP 369
Cdd:COG0666 11 LLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 370 LHIAARYGHELLINTLITSRADTSKRGIHGMFPLHLAALSGFSDCCRKLLSSGFDIDTHDDFGRTCLHAAAAGGNLECLN 449
Cdd:COG0666 91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 450 LLLSTGADFNKKDKFGRTPLHYAAANCNYQCLFALVGSGASVNDLDERGCSPLHYAATSDtDGKCLEYLLRNDANPGIRD 529
Cdd:COG0666 171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENG-NLEIVKLLLEAGADLNAKD 249
|
250 260
....*....|....*....|...
gi 1785376409 530 KHGYNAVHYAAAYGHRLCLELIA 552
Cdd:COG0666 250 KDGLTALLLAAAAGAALIVKLLL 272
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
49-376 |
7.74e-35 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 142.89 E-value: 7.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 49 DEVR---ALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQVLLKHSA 125
Cdd:PHA02876 156 DELLiaeMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRS 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 126 DVNARDKNwqtpLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHV-EMVSLLLSRGANINAFDKKDRRAI 204
Cdd:PHA02876 236 NINKNDLS----LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 205 HWAAYMGH-IEVVKLLVTHGAEVMCKDKKSYTPLHAAAS-SGMISVIKYLLDLGVDMNESNAYGNTPLHVACYNGQDVVV 282
Cdd:PHA02876 312 YLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVII 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 283 NELIDCGANVNQVNERGFTPLHFAAASTHGALCLELLVCNGADVNIKSKDGKTPLHMTAIHG-RFSRSQIIIQNGAEIDC 361
Cdd:PHA02876 392 NTLLDYGADIEALSQKIGTALHFALCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNA 471
|
330
....*....|....*
gi 1785376409 362 EDKNGNTPLHIAARY 376
Cdd:PHA02876 472 INIQNQYPLLIALEY 486
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
43-391 |
8.41e-35 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 138.94 E-value: 8.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 43 IFNGDPDEVRALIFKKED-VNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQVLL 121
Cdd:PHA02874 9 IYSGDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 122 KHSADVNARDknwqtplhiaaankavkcaealVPLLSNvnvsdragrtalhhaafsghvEMVSLLLSRGANINAFDKKDR 201
Cdd:PHA02874 89 DNGVDTSILP----------------------IPCIEK---------------------DMIKTILDCGIDVNIKDAELK 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 202 RAIHWAAYMGHIEVVKLLVTHGAEVMCKDKKSYTPLHAAASSGMISVIKYLLDLGVDMNESNAYGNTPLHVACYNGQDVV 281
Cdd:PHA02874 126 TFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYAC 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 282 VNELIDCGANVNQVNERGFTPLHfaAASTHGALCLELLVcNGADVNIKSKDGKTPLHMtAIHGRFSRS--QIIIQNGAEI 359
Cdd:PHA02874 206 IKLLIDHGNHIMNKCKNGFTPLH--NAIIHNRSAIELLI-NNASINDQDIDGSTPLHH-AINPPCDIDiiDILLYHKADI 281
|
330 340 350
....*....|....*....|....*....|....*...
gi 1785376409 360 DCEDKNGNTPLHIAARYGH------ELLINTLITSRAD 391
Cdd:PHA02874 282 SIKDNKGENPIDTAFKYINkdpvikDIIANAVLIKEAD 319
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
732-1041 |
1.24e-34 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 134.31 E-value: 1.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 732 LLNKGANVDAKDKWGRTALHRGAVTGHEECVEALLQHNANFLLRDCRGRTPIHLAAACGHIGVLSALLQTAISVDvvpaI 811
Cdd:COG0666 7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN----A 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 812 ADNHGYTPLHWACYNGHDACVELLLEQevfqkmegnsfsplhcavindneGAaemlidtlgtsIVNSVDSKGRTPLHAAA 891
Cdd:COG0666 83 KDDGGNTLLHAAARNGDLEIVKLLLEA-----------------------GA-----------DVNARDKDGETPLHLAA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 892 FTDHIECLQLLLSHNAQVNAVDSTGKTPLMMAAENGQTSAVEVLVSsAKADLTLQDKNKNTALHLACSKGHETSALLILE 971
Cdd:COG0666 129 YNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLE-AGADVNARDNDGETPLHLAAENGHLEIVKLLLE 207
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 972 QITDrnlINATNSALQTPLHVAARNGLTVVVQELLGKGASVLAVDENGYTPALACAPNKDVADCLALILA 1041
Cdd:COG0666 208 AGAD---VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLA 274
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
113-393 |
2.71e-33 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 135.15 E-value: 2.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 113 SEDAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLL---SNVNVSDRAGRTALH-HAAFSGHVEMVSLLLS 188
Cdd:PHA03095 26 TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIVRLLLeagADVNAPERCGFTPLHlYLYNATTLDVIKLLIK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 189 RGANINAFDKKDRRAIHwaAYMG----HIEVVKLLVTHGAEVMCKDKKSYTPLHAAASSGMISV--IKYLLDLGVDMNES 262
Cdd:PHA03095 106 AGADVNAKDKVGRTPLH--VYLSgfniNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVYAV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 263 NAYGNTPLHVACYNGQD--VVVNELIDCGANVNQVNERGFTPLHFAAA-STHGALCLELLVCNGADVNIKSKDGKTPLHM 339
Cdd:PHA03095 184 DDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHSMATgSSCKRSLVLPLLIAGISINARNRYGQTPLHY 263
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1785376409 340 TAIHGR---FSRsqiIIQNGAEIDCEDKNGNTPLHIAARYGHELLINTLITSRADTS 393
Cdd:PHA03095 264 AAVFNNpraCRR---LIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAE 317
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
810-1065 |
2.74e-33 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 130.46 E-value: 2.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 810 AIADNHGYTPLHWACYNGHDACVELLLEQEVFQKMEGNSFSPLHCAVINDNEGAAEMLIDTLGTSIvNSVDSKGRTPLHA 889
Cdd:COG0666 15 LLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI-NAKDDGGNTLLHA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 890 AAFTDHIECLQLLLSHNAQVNAVDSTGKTPLMMAAENGQTSAVEVLVSsAKADLTLQDKNKNTALHLACSKGHETSALLI 969
Cdd:COG0666 94 AARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLE-AGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 970 LEQITDrnlINATNSALQTPLHVAARNGLTVVVQELLGKGASVLAVDENGYTPALACAPNKDVADCLALILATMMPVSSS 1049
Cdd:COG0666 173 LEAGAD---VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKD 249
|
250
....*....|....*.
gi 1785376409 1050 SSLPSMTLNAINHYNN 1065
Cdd:COG0666 250 KDGLTALLLAAAAGAA 265
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
567-837 |
2.36e-32 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 127.76 E-value: 2.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 567 DMLNDAETRAPISPLHLAAYHGHHQALEVLVQSLLDLDVRNSTGRTPLDLAAFKGHVECVDVLINQGASILVKDYVvKRT 646
Cdd:COG0666 44 LLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKD-GET 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 647 PIHSAeiqmvdsrnsvnknntelcnsaqkkvrakdmpsAINGHSECLRLLIGNAdvqAAVDIHDGNGQTPLMLSVLNGHT 726
Cdd:COG0666 123 PLHLA---------------------------------AYNGNLEIVKLLLEAG---ADVNAQDNDGNTPLHLAAANGNL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 727 ECVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVEALLQHNANFLLRDCRGRTPIHLAAACGHIGVLSALLQTAISVD 806
Cdd:COG0666 167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246
|
250 260 270
....*....|....*....|....*....|.
gi 1785376409 807 vvpaIADNHGYTPLHWACYNGHDACVELLLE 837
Cdd:COG0666 247 ----AKDKDGLTALLLAAAAGAALIVKLLLL 273
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
246-532 |
4.41e-31 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 128.60 E-value: 4.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 246 ISVIKYLLDLGVDMNESNAYGNTPLHV--ACYNGQDV-VVNELIDCGANVNQVNERGFTPLHFAAASTHGALCLELLVCN 322
Cdd:PHA03095 27 VEEVRRLLAAGADVNFRGEYGKTPLHLylHYSSEKVKdIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDVIKLLIKA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 323 GADVNIKSKDGKTPLHmtaihgrfsrsqiiiqngaeIDCEDKNGNTPlhiaaryghelLINTLITSRADTSKRGIHGMFP 402
Cdd:PHA03095 107 GADVNAKDKVGRTPLH--------------------VYLSGFNINPK-----------VIRLLLRKGADVNALDLYGMTP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 403 LHlaALSGFSDCC----RKLLSSGFDIDTHDDFGRTCLH--AAAAGGNLECLNLLLSTGADFNKKDKFGRTPLHYAAA-- 474
Cdd:PHA03095 156 LA--VLLKSRNANvellRLLIDAGADVYAVDDRFRSLLHhhLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATgs 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1785376409 475 NCNYQCLFALVGSGASVNDLDERGCSPLHYAATSDTDGKClEYLLRNDANPGIRDKHG 532
Cdd:PHA03095 234 SCKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRAC-RRLIALGADINAVSSDG 290
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
213-496 |
1.57e-29 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 122.85 E-value: 1.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 213 IEVVKLLVTHGAEVMCKDKKSYTPLHAAASSGMISVIKYLLDLGVDMNESNAYGNTPLH---VACYNGQDVV--VNELID 287
Cdd:PHA03100 15 VKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsNIKYNLTDVKeiVKLLLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 288 CGANVNQVNERGFTPLHFAAASTHGALCL-ELLVCNGADVNIKSKDGKTPLHMTA--IHGRFSRSQIIIQNGAEIDCEDK 364
Cdd:PHA03100 95 YGANVNAPDNNGITPLLYAISKKSNSYSIvEYLLDNGANVNIKNSDGENLLHLYLesNKIDLKILKLLIDKGVDINAKNR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 365 ngntplhiaaryghellINTLItsradtskrgihgmfplhlaalsgfsdccrkllSSGFDIDTHDDFGRTCLHAAAAGGN 444
Cdd:PHA03100 175 -----------------VNYLL---------------------------------SYGVPINIKDVYGFTPLHYAVYNNN 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1785376409 445 LECLNLLLSTGADFNKKDKFGRTPLHYAAANCNYQCLFALVGSGASVNDLDE 496
Cdd:PHA03100 205 PEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
685-838 |
2.36e-29 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 119.29 E-value: 2.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 685 AINGHSECLRLLIgnaDVQAAVDIHDGNGQTPLMLSVLNGHTECVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVEA 764
Cdd:COG0666 95 ARNGDLEIVKLLL---EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKL 171
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1785376409 765 LLQHNANFLLRDCRGRTPIHLAAACGHIGVLSALLQTAISVDvvpaIADNHGYTPLHWACYNGHDACVELLLEQ 838
Cdd:COG0666 172 LLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVN----AKDNDGKTALDLAAENGNLEIVKLLLEA 241
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
243-573 |
1.30e-28 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 120.45 E-value: 1.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 243 SGMISVIKYLL-DLGVDMNESNAYGNTPLHVACYNGQDVVVNELIDCGANVNQVNERGFTPLhFAAASTHGALCLELLVC 321
Cdd:PHA02874 11 SGDIEAIEKIIkNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPL-LTAIKIGAHDIIKLLID 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 322 NGADVNIkskdgktpLHMTAIHGRFSRSqiIIQNGAEIDCEDKNGNTPLHIAARYGHELLINTLITSRADTSKRGIHGMF 401
Cdd:PHA02874 90 NGVDTSI--------LPIPCIEKDMIKT--ILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 402 PLHLAALSGFSDCCRKLLSSGFDIDTHDDFGRTCLHAAAAGGNLECLNLLLSTGADFNKKDKFGRTPLHYAAanCNYQCL 481
Cdd:PHA02874 160 PIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI--IHNRSA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 482 FALVGSGASVNDLDERGCSPLHYAATSDTDGKCLEYLLRNDANPGIRDKHGYNAVHYAAAYGHRLCL--ELIARETPLDV 559
Cdd:PHA02874 238 IELLINNASINDQDIDGSTPLHHAINPPCDIDIIDILLYHKADISIKDNKGENPIDTAFKYINKDPVikDIIANAVLIKE 317
|
330
....*....|....
gi 1785376409 560 LMETSGTDMLNDAE 573
Cdd:PHA02874 318 ADKLKDSDFLEHIE 331
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
379-652 |
4.98e-28 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 115.44 E-value: 4.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 379 ELLINTLITSRADTSKRGIHGMFPLHLAALSGFSDCCRKLLSSGFDIDTHDDFGRTCLHAAAAGGNLECLNLLLSTGADF 458
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 459 NKKDKFGRTPLHYAAANCNYQCLFALVGSGASVNDLDERGCSPLHYAATSDtDGKCLEYLLRNDANPGIRDKHGYNAVHY 538
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNG-NLEIVKLLLEAGADVNAQDNDGNTPLHL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 539 AAAYGHRLCLE-LIARetpldvlmetsGTDMlnDAETRAPISPLHLAAYHGHHQALEVLVQSLLDLDVRNSTGRTPLDLA 617
Cdd:COG0666 160 AAANGNLEIVKlLLEA-----------GADV--NARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLA 226
|
250 260 270
....*....|....*....|....*....|....*
gi 1785376409 618 AFKGHVECVDVLINQGASILVKDYVVKRTPIHSAE 652
Cdd:COG0666 227 AENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAA 261
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
281-632 |
7.59e-27 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 115.51 E-value: 7.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 281 VVNELIDCGANVNQVNERGFTPLHFAAASTHGAL--CLELLVCNGADVNIKSKDGKTPLHMTAIHGrfSRSQII---IQN 355
Cdd:PHA03095 29 EVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdIVRLLLEAGADVNAPERCGFTPLHLYLYNA--TTLDVIkllIKA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 356 GAEIDCEDKNGNTPLHIAAR--YGHELLINTLITSRADTSKRGIHGMFPLHlaALSGFSDCcrkllssgfdidthddfgr 433
Cdd:PHA03095 107 GADVNAKDKVGRTPLHVYLSgfNINPKVIRLLLRKGADVNALDLYGMTPLA--VLLKSRNA------------------- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 434 tclhaaaaggNLECLNLLLSTGADFNKKDKFGRTPLHYAAANC--NYQCLFALVGSGASVNDLDERGCSPLHYAATSdtd 511
Cdd:PHA03095 166 ----------NVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFkpRARIVRELIRAGCDPAATDMLGNTPLHSMATG--- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 512 GKCLEYLLRNdanpgirdkhgynavhyaaayghrlcleLIARetpldvlmetsGTDMlnDAETRAPISPLHLAAYHGHHQ 591
Cdd:PHA03095 233 SSCKRSLVLP----------------------------LLIA-----------GISI--NARNRYGQTPLHYAAVFNNPR 271
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1785376409 592 ALEVLVQSLLDLDVRNSTGRTPLDLAAFKGHVECVDVLINQ 632
Cdd:PHA03095 272 ACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAK 312
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
418-783 |
8.21e-26 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 108.89 E-value: 8.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 418 LLSSGFDIDTHDDFGRTCLHAAAAGGNLECLNLLLSTGADFNKKDKFGRTPLHYAAANCNYQCLFALVGSGASVNDLDER 497
Cdd:COG0666 7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 498 GCSPLHYAATSDtDGKCLEYLLRNDANPGIRDKHGYnavhyaaayghrlcleliaretpldvlmetsgtdmlndaetrap 577
Cdd:COG0666 87 GNTLLHAAARNG-DLEIVKLLLEAGADVNARDKDGE-------------------------------------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 578 iSPLHLAAYHGHHQALEVLVQSLLDLDVRNSTGRTPLDLAAFKGHVECVDVLINQGASILVKDYVvKRTPIHSAeiqmvd 657
Cdd:COG0666 122 -TPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDND-GETPLHLA------ 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 658 srnsvnknntelcnsaqkkvrakdmpsAINGHSECLRLLIGNAdvqAAVDIHDGNGQTPLMLSVLNGHTECVYSLLNKGA 737
Cdd:COG0666 194 ---------------------------AENGHLEIVKLLLEAG---ADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1785376409 738 NVDAKDKWGRTALHRGAVTGHEECVEALLQHNANFLLRDCRGRTPI 783
Cdd:COG0666 244 DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
102-373 |
7.21e-25 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 109.58 E-value: 7.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 102 LTPLHRAVASCSEDAVQVLLKHSADVNARDKNWQTPLHIA--AANKavkcaEALVPLLSNVNVSD-----RAGRTALHHA 174
Cdd:PHA02878 38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIIckEPNK-----LGMKEMIRSINKCSvfytlVAIKDAFNNR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 175 afsgHVEMV-SLLLSRGANINAFDKKDRRAIHWAAYMgHIEVVKLLVTHGAEVMCKDK-KSYTPLHAAASSGMISVIKYL 252
Cdd:PHA02878 113 ----NVEIFkIILTNRYKNIQTIDLVYIDKKSKDDII-EAEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 253 LDLGVDMNESNAYGNTPLHVACYNGQDVVVNELIDCGANVNQVNERGFTPLHFAAASTHGALCLELLVCNGADVNIKSK- 331
Cdd:PHA02878 188 LSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDYDILKLLLEHGVDVNAKSYi 267
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1785376409 332 DGKTPLHMtAIHGRfSRSQIIIQNGAEIDCEDKNGNTPLHIA 373
Cdd:PHA02878 268 LGLTALHS-SIKSE-RKLKLLLEYGADINSLNSYKLTPLSSA 307
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
57-344 |
3.65e-22 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 101.50 E-value: 3.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 57 KKEDVNFQDNEKRT---------PLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQVLLK----- 122
Cdd:PHA02878 17 LKYIEYIDHTENYStsaslipfiPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRsinkc 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 123 -------------HSADVNA-------RDKNWQTP--LHIAAANKAVKCAEALVPLL----SNVNVSDR-AGRTALHHAA 175
Cdd:PHA02878 97 svfytlvaikdafNNRNVEIfkiiltnRYKNIQTIdlVYIDKKSKDDIIEAEITKLLlsygADINMKDRhKGNTALHYAT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 176 FSGHVEMVSLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVTHGAEVMCKDKKSYTPLHAAASSGM-ISVIKYLLD 254
Cdd:PHA02878 177 ENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKdYDILKLLLE 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 255 LGVDMN-ESNAYGNTPLHVACYNGQdvVVNELIDCGANVNQVNERGFTPLHFAAASTHGALCLELLVCNGADVNIKSKDG 333
Cdd:PHA02878 257 HGVDVNaKSYILGLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPLSSAVKQYLCINIGRILISNICLLKRIKPDI 334
|
330
....*....|....*
gi 1785376409 334 KTPL----HMTAIHG 344
Cdd:PHA02878 335 KNSEgfidNMDCITS 349
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
834-1039 |
6.11e-22 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 97.33 E-value: 6.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 834 LLLEQEVFQKMEGNSFSPLHCAVINDNEGAAEMLIDTLGTSIVNSVDSKGRTPLHAAAFTDHIECLQLLLSHNAQVNAVD 913
Cdd:COG0666 5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 914 STGKTPLMMAAENGQTSAVEVLVSsAKADLTLQDKNKNTALHLACSKGHETSALLILEQITDrnlINATNSALQTPLHVA 993
Cdd:COG0666 85 DGGNTLLHAAARNGDLEIVKLLLE-AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGAD---VNAQDNDGNTPLHLA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1785376409 994 ARNGLTVVVQELLGKGASVLAVDENGYTPALACAPNKDVADCLALI 1039
Cdd:COG0666 161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLL 206
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
105-197 |
4.86e-20 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 85.55 E-value: 4.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 105 LHRAVASCSEDAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLsNVNVSDRaGRTALHHAAFSGHVEMVS 184
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKDN-GRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1785376409 185 LLLSRGANINAFD 197
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
138-230 |
4.86e-20 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 85.55 E-value: 4.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 138 LHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHVEMVSLLLSRgANINAFDkKDRRAIHWAAYMGHIEVVK 217
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1785376409 218 LLVTHGAEVMCKD 230
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
204-296 |
9.60e-20 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 84.78 E-value: 9.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 204 IHWAAYMGHIEVVKLLVTHGAEVMCKDKKSYTPLHAAASSGMISVIKYLLDlGVDMNESNaYGNTPLHVACYNGQDVVVN 283
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1785376409 284 ELIDCGANVNQVN 296
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
171-260 |
1.40e-19 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 84.40 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 171 LHHAAFSGHVEMVSLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVTHgAEVMCKDKKsYTPLHAAASSGMISVIK 250
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG-RTALHYAARSGHLEIVK 78
|
90
....*....|
gi 1785376409 251 YLLDLGVDMN 260
Cdd:pfam12796 79 LLLEKGADIN 88
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
403-495 |
2.07e-19 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 84.01 E-value: 2.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 403 LHLAALSGFSDCCRKLLSSGFDIDTHDDFGRTCLHAAAAGGNLECLNLLLSTgADFNKKDKfGRTPLHYAAANCNYQCLF 482
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1785376409 483 ALVGSGASVNDLD 495
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
219-636 |
2.59e-19 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 93.59 E-value: 2.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 219 LVTHGAEvMCKDKK-SYTPLHAAASSGMISVIKYLLDLGVDMNESNAYG-NTPLHVACY--NGQDVVVNELIDCGANVNq 294
Cdd:PHA02876 27 LHKHGAN-QCENESiPFTAIHQALQLRQIDIVEEIIQQNPELIYITDHKcHSTLHTICIipNVMDIVISLTLDCDIILD- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 295 vnergftpLHFAAASTH----GALCLELL--VCNGADVNIkSKDGKTPLHMTAIHGRFSRSQIII-----QNGAEIDCED 363
Cdd:PHA02876 105 --------IKYASIILNkhklDEACIHILkeAISGNDIHY-DKINESIEYMKLIKERIQQDELLIaemllEGGADVNAKD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 364 KNGNTPLHIAARYGHELLINTLITSRADTSKRGIHGMFPLHLAALSGFSDCCRK-------------------------- 417
Cdd:PHA02876 176 IYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAiidnrsninkndlsllkairnedlet 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 418 ---LLSSGFDIDTHDDFGRTCLHAAAAGGNLECL-NLLLSTGADFNKKDKFGRTPLHYAAAN-CNYQCLFALVGSGASVN 492
Cdd:PHA02876 256 sllLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLYLMAKNgYDTENIRTLIMLGADVN 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 493 DLDERGCSPLHYAATSDTDGKCLEYLLRNDANPGIRDKHGYNAVHYAAAYGHRLCLE-LIARETPLDVLMETSGTdmlnd 571
Cdd:PHA02876 336 AADRLYITPLHQASTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINtLLDYGADIEALSQKIGT----- 410
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1785376409 572 aetrapisPLHLAAYHGH-HQALEVLVQSLLDLDVRNSTGRTPLDLAAFKG-HVECVDVLINQGASI 636
Cdd:PHA02876 411 --------ALHFALCGTNpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADV 469
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
694-1023 |
5.97e-19 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 91.24 E-value: 5.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 694 RLLIGNADVQaavdiHDGN-GQTPLMLSVLNGH---TECVYSLLNKGANVDAKDKWGRTALH---RGAVTghEECVEALL 766
Cdd:PHA03095 32 RLLAAGADVN-----FRGEyGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHlylYNATT--LDVIKLLI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 767 QHNANFLLRDCRGRTPIH--LAAACGHIGVLSALLQTAISVDVVpaiaDNHGYTPLHwACYNGHDACVELLleqevfqkm 844
Cdd:PHA03095 105 KAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNAL----DLYGMTPLA-VLLKSRNANVELL--------- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 845 egnsfsplhcavindnegaaEMLIDTlGTSIVNsVDSKGRTPLH--AAAFTDHIECLQLLLSHNAQVNAVDSTGKTPLMM 922
Cdd:PHA03095 171 --------------------RLLIDA-GADVYA-VDDRFRSLLHhhLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 923 AAengqtsavevLVSSAKADLTLQdknkntalhlacskghetsalLILEQITdrnlINATNSALQTPLHVAARNGLTVVV 1002
Cdd:PHA03095 229 MA----------TGSSCKRSLVLP---------------------LLIAGIS----INARNRYGQTPLHYAAVFNNPRAC 273
|
330 340
....*....|....*....|.
gi 1785376409 1003 QELLGKGASVLAVDENGYTPA 1023
Cdd:PHA03095 274 RRLIALGADINAVSSDGNTPL 294
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
39-131 |
5.98e-19 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 82.47 E-value: 5.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 39 LVQAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLiLSGARVNAKDSKWlTPLHRAVASCSEDAVQ 118
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL-LEHADVNLKDNGR-TALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1785376409 119 VLLKHSADVNARD 131
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
69-295 |
8.13e-18 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 87.35 E-value: 8.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 69 RTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQVLLKHSADVNARDKNWQTPLHIAAANKAVK 148
Cdd:PHA02875 3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 149 CAEALvpLLSNVNVSD---RAGRTALHHAAFSGHVEMVSLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVTHGAE 225
Cdd:PHA02875 83 AVEEL--LDLGKFADDvfyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKAC 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1785376409 226 VMCKDKKSYTPLHAAASSGMISVIKYLLDLGVDMNESNAYGN-TPLHVACYNGQDVVVNELIDCGANVNQV 295
Cdd:PHA02875 161 LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADCNIM 231
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
594-925 |
9.18e-18 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 88.58 E-value: 9.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 594 EVLVQSLLDLDVRNSTGRTPLDLAAFKGHVECVDVLINQGAS---ILVKDYVVKRTPIHSAEIQ----MVDSRNSVNKNN 666
Cdd:PHA02876 162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADvniIALDDLSVLECAVDSKNIDtikaIIDNRSNINKND 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 667 TELCNSaqkkVRAKDMPSA---------INGHSECLRLLIGNAD------------VQAAVDIHDGN--GQTPLMLSVLN 723
Cdd:PHA02876 242 LSLLKA----IRNEDLETSlllydagfsVNSIDDCKNTPLHHASqapslsrlvpklLERGADVNAKNikGETPLYLMAKN 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 724 GH-TECVYSLLNKGANVDAKDKWGRTALHRGAVTG-HEECVEALLQHNANFLLRDCRGRTPIHLAAACGHIGVLSALLQT 801
Cdd:PHA02876 318 GYdTENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDY 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 802 AISVDvvpAIADNHGyTPLHWACYNGhdacvellleqevfqkmegNSFSplhcavindnegAAEMLIDTLGTsiVNSVDS 881
Cdd:PHA02876 398 GADIE---ALSQKIG-TALHFALCGT-------------------NPYM------------SVKTLIDRGAN--VNSKNK 440
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1785376409 882 KGRTPLHAAAFTD-HIECLQLLLSHNAQVNAVDSTGKTPLMMAAE 925
Cdd:PHA02876 441 DLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIALE 485
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
416-808 |
1.07e-17 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 87.39 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 416 RKLLSSGFDIDTHDDFGRTCLHAAAAGGN---LECLNLLLSTGADFNKKDKFGRTPLH-YAAANCNYQCLFALVGSGASV 491
Cdd:PHA03095 31 RRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 492 NDLDERGCSPLH-YAATSDTDGKCLEYLLRNDANPGIRDKHGYnavhyaaayghrlcleliareTPLDVLMETSGTDmln 570
Cdd:PHA03095 111 NAKDKVGRTPLHvYLSGFNINPKVIRLLLRKGADVNALDLYGM---------------------TPLAVLLKSRNAN--- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 571 daetrapisplhlaayhghhqalevlvqslldldvrnstgrtpldlaafkghVECVDVLINQGASILVKDyVVKRTPIHS 650
Cdd:PHA03095 167 ----------------------------------------------------VELLRLLIDAGADVYAVD-DRFRSLLHH 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 651 aEIQMVDSRNSVNKNNTEL-CNSAQKKVRAKDMPSAINGHSECLRLLIGNadvqaavdihdgngqtplmlsvlnghtecv 729
Cdd:PHA03095 194 -HLQSFKPRARIVRELIRAgCDPAATDMLGNTPLHSMATGSSCKRSLVLP------------------------------ 242
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1785376409 730 ysLLNKGANVDAKDKWGRTALHRGAVTGHEECVEALLQHNANFLLRDCRGRTPIHLAAACGHIGVLSALLQTAISVDVV 808
Cdd:PHA03095 243 --LLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETV 319
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
717-807 |
1.19e-17 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 79.00 E-value: 1.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 717 LMLSVLNGHTECVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVEALLQHNAnfLLRDCRGRTPIHLAAACGHIGVLS 796
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78
|
90
....*....|.
gi 1785376409 797 ALLQTAISVDV 807
Cdd:pfam12796 79 LLLEKGADINV 89
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
370-462 |
2.41e-17 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 78.23 E-value: 2.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 370 LHIAARYGHELLINTLITSRADTSKRGIHGMFPLHLAALSGFSDCCRKLLSSgFDIDtHDDFGRTCLHAAAAGGNLECLN 449
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVN-LKDNGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1785376409 450 LLLSTGADFNKKD 462
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
193-472 |
5.75e-17 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 85.32 E-value: 5.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 193 INAFDKKDRRA----------IHWAAYMGHIEVVKLLVTHGAEVMCKDKKSYTPLHAAASSGMISVIKYLLDLGVDMNES 262
Cdd:PHA02878 20 IEYIDHTENYStsaslipfipLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 263 NAYgnTPLHVACYNgQDVVVNE--LIDCGANVNQVNERGFTPLHFAAASThgALCLELLVCNGADVNIKSKD-GKTPLHM 339
Cdd:PHA02878 100 YTL--VAIKDAFNN-RNVEIFKiiLTNRYKNIQTIDLVYIDKKSKDDIIE--AEITKLLLSYGADINMKDRHkGNTALHY 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 340 TAIHGRFSRSQIIIQNGAEIDCEDKNGNTPLHIAARYGHELLINTLITSRADTSKRGIHGMFPLHLAALSGFS-DCCRKL 418
Cdd:PHA02878 175 ATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDyDILKLL 254
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1785376409 419 LSSGFDIDTHDDF-GRTCLHAAAAggNLECLNLLLSTGADFNKKDKFGRTPLHYA 472
Cdd:PHA02878 255 LEHGVDVNAKSYIlGLTALHSSIK--SERKLKLLLEYGADINSLNSYKLTPLSSA 307
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
39-220 |
9.56e-17 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 84.24 E-value: 9.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 39 LVQAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQ 118
Cdd:PHA02874 128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIK 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 119 VLLKHSADVNARDKNWQTPLHIAAA-NKAVkcaealVPLLSN---VNVSDRAGRTALHHA-AFSGHVEMVSLLLSRGANI 193
Cdd:PHA02874 208 LLIDHGNHIMNKCKNGFTPLHNAIIhNRSA------IELLINnasINDQDIDGSTPLHHAiNPPCDIDIIDILLYHKADI 281
|
170 180
....*....|....*....|....*...
gi 1785376409 194 NAFDKKDRRAIHWA-AYMGHIEVVKLLV 220
Cdd:PHA02874 282 SIKDNKGENPIDTAfKYINKDPVIKDII 309
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
685-776 |
1.06e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 76.31 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 685 AINGHSECLRLLIGNadvQAAVDIHDGNGQTPLMLSVLNGHTECVYSLLNKgANVDAKDKwGRTALHRGAVTGHEECVEA 764
Cdd:pfam12796 5 AKNGNLELVKLLLEN---GADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKL 79
|
90
....*....|..
gi 1785376409 765 LLQHNANFLLRD 776
Cdd:pfam12796 80 LLEKGADINVKD 91
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
416-651 |
1.15e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 83.95 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 416 RKLLSSGFDIDTHDDFGRTCLHAAAAGGNLECLNLLLSTGADFNKKDKFGRTPLHYAA-----ANCNYQCLFALVGSGAS 490
Cdd:PHA03100 19 KYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGAN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 491 VNDLDERGCSPLHYAATSD-TDGKCLEYLLRNDANPGIRDKHGYNAVHYAaayghrlcLELIARETPLDVLMETSGTDMl 569
Cdd:PHA03100 99 VNAPDNNGITPLLYAISKKsNSYSIVEYLLDNGANVNIKNSDGENLLHLY--------LESNKIDLKILKLLIDKGVDI- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 570 nDAETRapisplhlaayhghhqaLEVLVQSLLDLDVRNSTGRTPLDLAAFKGHVECVDVLINQGASILVKDYVVKrTPIH 649
Cdd:PHA03100 170 -NAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGD-TPLH 230
|
..
gi 1785376409 650 SA 651
Cdd:PHA03100 231 IA 232
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
750-840 |
1.58e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 75.92 E-value: 1.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 750 LHRGAVTGHEECVEALLQHNANFLLRDCRGRTPIHLAAACGHIGVLSALLQTAISVDvvpaiaDNHGYTPLHWACYNGHD 829
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL------KDNGRTALHYAARSGHL 74
|
90
....*....|.
gi 1785376409 830 ACVELLLEQEV 840
Cdd:pfam12796 75 EIVKLLLEKGA 85
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
887-980 |
3.65e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 74.77 E-value: 3.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 887 LHAAAFTDHIECLQLLLSHNAQVNAVDSTGKTPLMMAAENGQTSAVEVLVSSAKADLTLqdkNKNTALHLACSKGHETSA 966
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD---NGRTALHYAARSGHLEIV 77
|
90
....*....|....
gi 1785376409 967 LLILEQITDRNLIN 980
Cdd:pfam12796 78 KLLLEKGADINVKD 91
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
60-225 |
4.17e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 81.96 E-value: 4.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 60 DVNFQDneKRTPLHAAAYLGDAEIIELLILSGARVN-AKDSKWLTPLHRAVASCSEDAVQVLLKHSADVNARDKNWQTPL 138
Cdd:PHA02875 62 DVKYPD--IESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 139 HIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHVEMVSLLLSRGANINAFDKK-DRRAIHWAAYMGHIEVVK 217
Cdd:PHA02875 140 HLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNgCVAALCYAIENNKIDIVR 219
|
....*...
gi 1785376409 218 LLVTHGAE 225
Cdd:PHA02875 220 LFIKRGAD 227
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
82-345 |
5.87e-16 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 82.19 E-value: 5.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 82 EIIELLILSGARVNAKDSKWLTPLHRAVASCSE-----DAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPL 156
Cdd:PHA02798 52 DIVKLFINLGANVNGLDNEYSTPLCTILSNIKDykhmlDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLFM 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 157 LSN---VNVSDRAGRTALHHAAFSGH---VEMVSLLLSRGANINAFDkkdrraiHWAAYmghievvkllvthgAEVMCKD 230
Cdd:PHA02798 132 IENgadTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINTHN-------NKEKY--------------DTLHCYF 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 231 KKSYTPLHAaassgmiSVIKYLLDLGVDMNESNAYGNTP----LHVACYNGQDVVVN--ELIDCGANVNQVNERGFTPLH 304
Cdd:PHA02798 191 KYNIDRIDA-------DILKLFVDNGFIINKENKSHKKKfmeyLNSLLYDNKRFKKNilDFIFSYIDINQVDELGFNPLY 263
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1785376409 305 FAAASTHGALClELLVCNGADVNIKSKDGKTPLhMTAIHGR 345
Cdd:PHA02798 264 YSVSHNNRKIF-EYLLQLGGDINIITELGNTCL-FTAFENE 302
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
706-915 |
1.20e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 80.48 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 706 VDIHDGNGQTPLMLSVLNGHT-----ECVYSLLNKGANVDAKDKWGRTALHRGAVT--GHEECVEALLQHNANFLLRDCR 778
Cdd:PHA03100 61 INSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSD 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 779 GRTPIHLAAACGHI--GVLSALLQTAISVDV-----------VPA-IADNHGYTPLHWACYNGHDACVELLLEqevfqkm 844
Cdd:PHA03100 141 GENLLHLYLESNKIdlKILKLLIDKGVDINAknrvnyllsygVPInIKDVYGFTPLHYAVYNNNPEFVKYLLD------- 213
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1785376409 845 egnsfsplhcavindnegaaemlidtLGTSIvNSVDSKGRTPLHAAAFTDHIECLQLLLSHNAQVNAVDST 915
Cdd:PHA03100 214 --------------------------LGANP-NLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
57-228 |
1.83e-15 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 81.45 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 57 KKEDVNFQDNEKRTPLHAAAYL------GDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQVLLKHSADVNAR 130
Cdd:PLN03192 508 NVGDLLGDNGGEHDDPNMASNLltvastGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIR 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 131 DKNWQTPLHIAAANKAVKCAEALVPLLSnvnVSD-RAGRTALHHAAFSGHVEMVSLLLSRGANINAFDKKDRRAIHWAAY 209
Cdd:PLN03192 588 DANGNTALWNAISAKHHKIFRILYHFAS---ISDpHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMA 664
|
170
....*....|....*....
gi 1785376409 210 MGHIEVVKLLVTHGAEVMC 228
Cdd:PLN03192 665 EDHVDMVRLLIMNGADVDK 683
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
51-222 |
1.99e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 80.31 E-value: 1.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 51 VRALIFKKEDVNFQDNEK-RTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQVLLKHSADVNA 129
Cdd:PHA02878 150 TKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 130 RDKNWQTPLHIAAAnkAVKCAEALVPLL---SNVNV-SDRAGRTALHHAAFSGHVemVSLLLSRGANINAFDKKDRRAIH 205
Cdd:PHA02878 230 RDKCGNTPLHISVG--YCKDYDILKLLLehgVDVNAkSYILGLTALHSSIKSERK--LKLLLEYGADINSLNSYKLTPLS 305
|
170
....*....|....*....
gi 1785376409 206 WAA--YMGhIEVVKLLVTH 222
Cdd:PHA02878 306 SAVkqYLC-INIGRILISN 323
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
260-529 |
2.94e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 79.92 E-value: 2.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 260 NESNAYGNTPLHVACYNGQDVVVNELIDCGANVNQVNERGFTPLHFAAASTHGALCLELLvcngadvNIKSKDgKTPLHM 339
Cdd:PHA02878 31 TSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMI-------RSINKC-SVFYTL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 340 TAIHGRFSRSQIIIQNGAEIDCEDKNGNTPLHIAARYGHELLINTLITSR-----ADTSKRGIH-GMFPLHLAALSGFSD 413
Cdd:PHA02878 103 VAIKDAFNNRNVEIFKIILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLllsygADINMKDRHkGNTALHYATENKDQR 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 414 CCRKLLSSGFDIDTHDDFGRTCLHAAAAGGNLECLNLLLSTGADFNKKDKFGRTPLHYAAANC-NYQCLFALVGSGASVN 492
Cdd:PHA02878 183 LTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCkDYDILKLLLEHGVDVN 262
|
250 260 270
....*....|....*....|....*....|....*...
gi 1785376409 493 DLDE-RGCSPLHYAATSDtdgKCLEYLLRNDANPGIRD 529
Cdd:PHA02878 263 AKSYiLGLTALHSSIKSE---RKLKLLLEYGADINSLN 297
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
36-247 |
3.58e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 80.49 E-value: 3.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 36 TPPLVQAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLG-DAEIIELLILSGARVNAKDSKWLTPLHRAVASCSE 114
Cdd:PHA02876 309 TPLYLMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNV 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 115 DAVQVLLKHSADVNARDKNWQTPLHIA-AANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSG-HVEMVSLLLSRGAN 192
Cdd:PHA02876 389 VIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGAD 468
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1785376409 193 INAFDKKDRRAIHWAayMGHIEVVKLLVTHGAEVmcKDKKSytpLHAAASSGMIS 247
Cdd:PHA02876 469 VNAINIQNQYPLLIA--LEYHGIVNILLHYGAEL--RDSRV---LHKSLNDNMFS 516
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
820-913 |
4.68e-15 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 71.69 E-value: 4.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 820 LHWACYNGHDACVELLLEQEV-FQKMEGNSFSPLHCAVINDNEGAAEMLIDTLGTSIVNsvdsKGRTPLHAAAFTDHIEC 898
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGAdANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD----NGRTALHYAARSGHLEI 76
|
90
....*....|....*
gi 1785376409 899 LQLLLSHNAQVNAVD 913
Cdd:pfam12796 77 VKLLLEKGADINVKD 91
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
240-459 |
4.80e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 78.88 E-value: 4.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 240 AASSGMISVIKYLLDLGVDMNESNAYGNTPLHVACYNGQDVVVNELIDCGA--NVNQVNERgfTPLHFAAASTHGALCLE 317
Cdd:PHA02875 9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAipDVKYPDIE--SELHDAVEEGDVKAVEE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 318 LLVCNGADVNIKSKDGKTPLHMTAIHGRFSRSQIIIQNGAEIDCEDKNGNTPLHIAARYGHELLINTLITSRADTSKRGI 397
Cdd:PHA02875 87 LLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDC 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1785376409 398 HGMFPLHLAALSGFSDCCRKLLSSGFDIDThddFGR----TCLHAAAAGGNLECLNLLLSTGADFN 459
Cdd:PHA02875 167 CGCTPLIIAMAKGDIAICKMLLDSGANIDY---FGKngcvAALCYAIENNKIDIVRLFIKRGADCN 229
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
763-1017 |
5.75e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 79.72 E-value: 5.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 763 EALLQHNANFLLRDCRGRTPIHLAAACGHIGVLSALLQTAISVDVVPAiadnHGYTPLHWACYNGHDACVELLLEQEvfQ 842
Cdd:PHA02876 162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIAL----DDLSVLECAVDSKNIDTIKAIIDNR--S 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 843 KMEGNSFSPLHcAVINDNEGAAEMLIDTlGTSiVNSVDSKGRTPLHAAAFTDHIECL-QLLLSHNAQVNAVDSTGKTPLM 921
Cdd:PHA02876 236 NINKNDLSLLK-AIRNEDLETSLLLYDA-GFS-VNSIDDCKNTPLHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLY 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 922 MAAENG-QTSAVEVLVSSAkADLTLQDKNKNTALHLACSKGHETSALLILEQITDRnlINATNSALQTPLHVAARNGLTV 1000
Cdd:PHA02876 313 LMAKNGyDTENIRTLIMLG-ADVNAADRLYITPLHQASTLDRNKDIVITLLELGAN--VNARDYCDKTPIHYAAVRNNVV 389
|
250
....*....|....*..
gi 1785376409 1001 VVQELLGKGASVLAVDE 1017
Cdd:PHA02876 390 IINTLLDYGADIEALSQ 406
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
213-459 |
1.59e-14 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 77.57 E-value: 1.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 213 IEVVKLLVTHGAEVMCKDKKSYTPLHAAASS-----GMISVIKYLLDLGVDMNESNAYGNTPLHVACYNG---QDVVVNE 284
Cdd:PHA02798 51 TDIVKLFINLGANVNGLDNEYSTPLCTILSNikdykHMLDIVKILIENGADINKKNSDGETPLYCLLSNGyinNLEILLF 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 285 LIDCGANVNQVNERGFTPLHFAAASTHGAL--CLELLVCNGADVNIKS-KDGKTPLHmTAIHGRFSR-----SQIIIQNG 356
Cdd:PHA02798 131 MIENGADTTLLDKDGFTMLQVYLQSNHHIDieIIKLLLEKGVDINTHNnKEKYDTLH-CYFKYNIDRidadiLKLFVDNG 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 357 AEIDCEDKNGNTPLhiaARYGHELLINT---------LITSRADTSKRGIHGMFPLHLAALSGFSDCCRKLLSSGFDIDT 427
Cdd:PHA02798 210 FIINKENKSHKKKF---MEYLNSLLYDNkrfkknildFIFSYIDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINI 286
|
250 260 270
....*....|....*....|....*....|..
gi 1785376409 428 HDDFGRTCLHAAAAGGNLECLNLLLSTGADFN 459
Cdd:PHA02798 287 ITELGNTCLFTAFENESKFIFNSILNKKPNKN 318
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
418-800 |
2.96e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 77.41 E-value: 2.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 418 LLSSGFDIDTHDDFGRTCLHAAAAGGNLECLNLLLSTGADFNKKDKFGRTPLHYAAANCNYQCLFALVGSGASVNDLDer 497
Cdd:PHA02876 164 LLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKND-- 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 498 gCSPLHYAATSDTDGKCLEYllrnDANPGIR--DKHGYNAVHYA--AAYGHRLCLELIARetpldvlmetsGTDMlnDAE 573
Cdd:PHA02876 242 -LSLLKAIRNEDLETSLLLY----DAGFSVNsiDDCKNTPLHHAsqAPSLSRLVPKLLER-----------GADV--NAK 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 574 TRAPISPLHLAAYHGHH-QALEVLVQSLLDLDVRNSTGRTPLDLAA-FKGHVECVDVLINQGASILVKDYvVKRTPIHSA 651
Cdd:PHA02876 304 NIKGETPLYLMAKNGYDtENIRTLIMLGADVNAADRLYITPLHQAStLDRNKDIVITLLELGANVNARDY-CDKTPIHYA 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 652 EIqmvdsRNSVNKNNTELCNSAQKKVRAKDMPSAINgHSEClrllignadvqaavdihdgnGQTPLMlsvlnghteCVYS 731
Cdd:PHA02876 383 AV-----RNNVVIINTLLDYGADIEALSQKIGTALH-FALC--------------------GTNPYM---------SVKT 427
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 732 LLNKGANVDAKDKWGRTALHRGAVTGHE-ECVEALLQHNANFLLRDCRGRTPihLAAACGHIGVLSALLQ 800
Cdd:PHA02876 428 LIDRGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAINIQNQYP--LLIALEYHGIVNILLH 495
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
732-1024 |
3.28e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 77.41 E-value: 3.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 732 LLNKGANVDAKDKWGRTALHRGAVTGHEECVEALLQHNANFLLRDCRGRTPIHLAAACGHIGVLSALLQTAISVD----- 806
Cdd:PHA02876 164 LLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINkndls 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 807 VVPAIA--------------------DNHGYTPLHWACYNGH-DACVELLLEQEV---FQKMEGNSfsPLHCAVINDNEG 862
Cdd:PHA02876 244 LLKAIRnedletslllydagfsvnsiDDCKNTPLHHASQAPSlSRLVPKLLERGAdvnAKNIKGET--PLYLMAKNGYDT 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 863 AAEMLIDTLGTSiVNSVDSKGRTPLHAAAFTD-HIECLQLLLSHNAQVNAVDSTGKTPLMMAAENGQTSAVEVLVSSAkA 941
Cdd:PHA02876 322 ENIRTLIMLGAD-VNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYG-A 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 942 DLTLQDKNKNTALHLACskgHETSALLILEQITDRNL-INATNSALQTPLHVAARNGLTV-VVQELLGKGASVLAVDENG 1019
Cdd:PHA02876 400 DIEALSQKIGTALHFAL---CGTNPYMSVKTLIDRGAnVNSKNKDLSTPLHYACKKNCKLdVIEMLLDNGADVNAINIQN 476
|
....*
gi 1785376409 1020 YTPAL 1024
Cdd:PHA02876 477 QYPLL 481
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
44-195 |
4.72e-14 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 75.83 E-value: 4.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 44 FNGDPDEVRALIFKKEDVNFQDNEKRTPLHaaAYLG----DAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDA--V 117
Cdd:PHA03095 128 FNINPKVIRLLLRKGADVNALDLYGMTPLA--VLLKsrnaNVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRAriV 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 118 QVLLKHSADVNARDKNWQTPLHIAAANKAVKcAEALVPLLSN---VNVSDRAGRTALHHAAFSGHVEMVSLLLSRGANIN 194
Cdd:PHA03095 206 RELIRAGCDPAATDMLGNTPLHSMATGSSCK-RSLVLPLLIAgisINARNRYGQTPLHYAAVFNNPRACRRLIALGADIN 284
|
.
gi 1785376409 195 A 195
Cdd:PHA03095 285 A 285
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
337-429 |
7.90e-14 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 68.22 E-value: 7.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 337 LHMTAIHGRFSRSQIIIQNGAEIDCEDKNGNTPLHIAARYGH----ELLINTLITSRADtskrgiHGMFPLHLAALSGFS 412
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHleivKLLLEHADVNLKD------NGRTALHYAARSGHL 74
|
90
....*....|....*..
gi 1785376409 413 DCCRKLLSSGFDIDTHD 429
Cdd:pfam12796 75 EIVKLLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
920-1016 |
1.34e-13 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 67.45 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 920 LMMAAENGQTSAVEVLVSSaKADLTLQDKNKNTALHLACSKGHETSALLILEQItDRNLINATNsalqTPLHVAARNGLT 999
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLEN-GADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKDNGR----TALHYAARSGHL 74
|
90
....*....|....*..
gi 1785376409 1000 VVVQELLGKGASVLAVD 1016
Cdd:pfam12796 75 EIVKLLLEKGADINVKD 91
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
101-308 |
1.50e-13 |
|
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: 75.05 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 101 WLTPLHRAVASCSEDAVQVLLK-HSADVNARDKNWQTPLHIAAANKAVKCAEAL---VPLLSNVNV-SD-RAGRTALHHA 174
Cdd:cd22192 17 SESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLmeaAPELVNEPMtSDlYQGETALHIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 175 AFSGHVEMVSLLLSRGANIN-------AFDKKDRRAIHW-------AAYMGHIEVVKLLVTHGAEVMCKDkksytplhaa 240
Cdd:cd22192 97 VVNQNLNLVRELIARGADVVspratgtFFRPGPKNLIYYgehplsfAACVGNEEIVRLLIEHGADIRAQD---------- 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1785376409 241 assgmisvikylldlgvdmnesnAYGNTPLHVACYNGQDVVVNELIDC----GANVNQV------NERGFTPLHFAAA 308
Cdd:cd22192 167 -----------------------SLGNTVLHILVLQPNKTFACQMYDLilsyDKEDDLQpldlvpNNQGLTPFKLAAK 221
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
270-363 |
4.52e-13 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 65.91 E-value: 4.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 270 LHVACYNGQDVVVNELIDCGANVNQVNERGFTPLHFAAASTHGALCLELLvcNGADVNIKSkDGKTPLHMTAIHGRFSRS 349
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL--EHADVNLKD-NGRTALHYAARSGHLEIV 77
|
90
....*....|....
gi 1785376409 350 QIIIQNGAEIDCED 363
Cdd:pfam12796 78 KLLLEKGADINVKD 91
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
281-527 |
5.72e-13 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 72.56 E-value: 5.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 281 VVNELIDCGANVNQVNERGFTPLHFAAAS----THGALCLELLVCNGADVNIKSKDGKTPLHMTAIHGRFSRSQII---I 353
Cdd:PHA02798 53 IVKLFINLGANVNGLDNEYSTPLCTILSNikdyKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILlfmI 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 354 QNGAEIDCEDKNGNTPLHIAARYGHELLINTLitsradtskrgihgmfplhlaalsgfsdccRKLLSSGFDIDTHDD-FG 432
Cdd:PHA02798 133 ENGADTTLLDKDGFTMLQVYLQSNHHIDIEII------------------------------KLLLEKGVDINTHNNkEK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 433 RTCLHAAAAgGNLECLN-----LLLSTGADFNKKDKFGRT-------PLHYAAANCNYQcLFALVGSGASVNDLDERGCS 500
Cdd:PHA02798 183 YDTLHCYFK-YNIDRIDadilkLFVDNGFIINKENKSHKKkfmeylnSLLYDNKRFKKN-ILDFIFSYIDINQVDELGFN 260
|
250 260
....*....|....*....|....*..
gi 1785376409 501 PLHYAATSDTDgKCLEYLLRNDANPGI 527
Cdd:PHA02798 261 PLYYSVSHNNR-KIFEYLLQLGGDINI 286
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
832-1018 |
7.97e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 72.01 E-value: 7.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 832 VELLLEQ--EVFQKMEGNSfSPLH-----CAVINDNEGAAEMLIDtLGTSIvNSVDSKGRTPLHAAAFT--DHIECLQLL 902
Cdd:PHA03100 51 VKILLDNgaDINSSTKNNS-TPLHylsniKYNLTDVKEIVKLLLE-YGANV-NAPDNNGITPLLYAISKksNSYSIVEYL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 903 LSHNAQVNAVDSTGKTPLMMAAENGQ--TSAVEVLVSS-----AK----------ADLTLQDKNKNTALHLACSKGHETS 965
Cdd:PHA03100 128 LDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKgvdinAKnrvnyllsygVPINIKDVYGFTPLHYAVYNNNPEF 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1785376409 966 ALLILEQITDRNLINATNSalqTPLHVAARNGLTVVVQELLGKGASVLAVDEN 1018
Cdd:PHA03100 208 VKYLLDLGANPNLVNKYGD---TPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
614-743 |
1.37e-12 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 64.37 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 614 LDLAAFKGHVECVDVLINQGASILVKDyVVKRTPIHSAeiqmvdsrnsvnknntelcnsaqkkvrakdmpsAINGHSECL 693
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQD-KNGRTALHLA---------------------------------AKNGHLEIV 46
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1785376409 694 RLLIGNADVQAavdihDGNGQTPLMLSVLNGHTECVYSLLNKGANVDAKD 743
Cdd:pfam12796 47 KLLLEHADVNL-----KDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
167-220 |
2.84e-12 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 62.29 E-value: 2.84e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1785376409 167 GRTALHHAAFSGHVEMVSLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLV 220
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
306-460 |
7.49e-12 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 69.90 E-value: 7.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 306 AAASTHGALCLELLVCNGADVNIKSKDGKTPLHMTAIHGRFSRSQIIIQNGAEIDCEDKNGNTPLHIAARYGHELLINTL 385
Cdd:PLN03192 531 TVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1785376409 386 ITSrADTSKRGIHGMFpLHLAALSGFSDCCRKLLSSGFDIDTHDDFGRTCLHAAAAGGNLECLNLLLSTGADFNK 460
Cdd:PLN03192 611 YHF-ASISDPHAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDK 683
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
450-837 |
7.64e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 69.71 E-value: 7.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 450 LLLSTGADFNKKDKFGRTPLHYAAANCNYQCLFALVGSGASVNDLDERGCSPLHYAATSDtDGKCLEYLLRNDANPGIRD 529
Cdd:PHA02876 163 MLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSK-NIDTIKAIIDNRSNINKND 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 530 KHGYNAVhyaaayghrlcleliaRETPLD--VLMETSG--TDMLNDAETrapiSPLHLAAyhgHHQALEVLVQSLL---- 601
Cdd:PHA02876 242 LSLLKAI----------------RNEDLEtsLLLYDAGfsVNSIDDCKN----TPLHHAS---QAPSLSRLVPKLLerga 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 602 DLDVRNSTGRTPLDLAAFKGH-VECVDVLINQGASILVKDYVVKrTPIHSAeiqmvdsrnsvnknntelcnsaqkkvrak 680
Cdd:PHA02876 299 DVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYI-TPLHQA----------------------------- 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 681 dmpsainghseclrllignadvqaavdihdgngqtplmlSVLNGHTECVYSLLNKGANVDAKDKWGRTALHRGAVTGHEE 760
Cdd:PHA02876 349 ---------------------------------------STLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVV 389
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1785376409 761 CVEALLQHNANFLLRDCRGRTPIHLaAACGHIGVLSalLQTAISVDVVPAIADNHGYTPLHWACYNG-HDACVELLLE 837
Cdd:PHA02876 390 IINTLLDYGADIEALSQKIGTALHF-ALCGTNPYMS--VKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLD 464
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
432-485 |
1.07e-11 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 60.75 E-value: 1.07e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1785376409 432 GRTCLHAAAAGGNLECLNLLLSTGADFNKKDKFGRTPLHYAAANCNYQCLFALV 485
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
301-470 |
1.09e-11 |
|
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: 68.89 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 301 TPLhFAAASTHGALCLE-LLVCNGADVNIKSKDGKTPLHMTAIHGRFSRSQIIIQNGAE-----IDCEDKNGNTPLHIAA 374
Cdd:cd22192 19 SPL-LLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElvnepMTSDLYQGETALHIAV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 375 RYGHELLINTLITSRADTSKRGIHGMFplhlaalsgFSDCCRKLLSsgfdidthddFGRTCLHAAAAGGNLECLNLLLST 454
Cdd:cd22192 98 VNQNLNLVRELIARGADVVSPRATGTF---------FRPGPKNLIY----------YGEHPLSFAACVGNEEIVRLLIEH 158
|
170
....*....|....*.
gi 1785376409 455 GADFNKKDKFGRTPLH 470
Cdd:cd22192 159 GADIRAQDSLGNTVLH 174
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
581-823 |
1.99e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 67.68 E-value: 1.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 581 LHLAAYHGHHQALEVLVQS---LLDLDVRNSTgrTPLDLAAFKGHVECVDVLINQGASIlvkDYVVKRTP--------IH 649
Cdd:PHA02874 5 LRMCIYSGDIEAIEKIIKNkgnCINISVDETT--TPLIDAIRSGDAKIVELFIKHGADI---NHINTKIPhplltaikIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 650 SAEIQMVDSRNSVNKN-------NTELCNSAQK---KVRAKDMPSAI-------NGHSECLRLLIgnaDVQAAVDIHDGN 712
Cdd:PHA02874 80 AHDIIKLLIDNGVDTSilpipciEKDMIKTILDcgiDVNIKDAELKTflhyaikKGDLESIKMLF---EYGADVNIEDDN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 713 GQTPLMLSVLNGHTECVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVEALLQHNANFLLRDCRGRTPIHLAAAcgHI 792
Cdd:PHA02874 157 GCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HN 234
|
250 260 270
....*....|....*....|....*....|.
gi 1785376409 793 GVLSALLQTAISVDVvpaiADNHGYTPLHWA 823
Cdd:PHA02874 235 RSAIELLINNASIND----QDIDGSTPLHHA 261
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
537-640 |
2.32e-11 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 60.90 E-value: 2.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 537 HYAAAYGHRLCLELIAREtpldvlmetsGTDMlnDAETRAPISPLHLAAYHGHHQALEVLVQSLlDLDVRNStGRTPLDL 616
Cdd:pfam12796 2 HLAAKNGNLELVKLLLEN----------GADA--NLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKDN-GRTALHY 67
|
90 100
....*....|....*....|....
gi 1785376409 617 AAFKGHVECVDVLINQGASILVKD 640
Cdd:pfam12796 68 AARSGHLEIVKLLLEKGADINVKD 91
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
281-527 |
2.61e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 66.94 E-value: 2.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 281 VVNELIDCGANVNQVNERGFTPLHFAAaSTHGALCLELLVCNGADVNIKSKDGKTPLHMTAIHGRFSRSQIIIQNGAEI- 359
Cdd:PHA02875 17 IARRLLDIGINPNFEIYDGISPIKLAM-KFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAd 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 360 DCEDKNGNTPLHiaaryghellintlitsradtskrgihgmfplhLAALSGFSDCCRKLLSSGFDIDTHDDFGRTCLHAA 439
Cdd:PHA02875 96 DVFYKDGMTPLH---------------------------------LATILKKLDIMKLLIARGADPDIPNTDKFSPLHLA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 440 AAGGNLECLNLLLSTGADFNKKDKFGRTPLHYAAANCNYQCLFALVGSGASVNDLDERGCSPLHYAATSDTDGKCLEYLL 519
Cdd:PHA02875 143 VMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFI 222
|
....*...
gi 1785376409 520 RNDANPGI 527
Cdd:PHA02875 223 KRGADCNI 230
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
825-1029 |
2.91e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 67.00 E-value: 2.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 825 YNGHDACVELLLEQEVFQKMEGNSFS------PLHCAVINDNEGAAEMLIDTlGTSIvNSVDSKGRTPLH-----AAAFT 893
Cdd:PHA03100 6 VLTKSRIIKVKNIKYIIMEDDLNDYSykkpvlPLYLAKEARNIDVVKILLDN-GADI-NSSTKNNSTPLHylsniKYNLT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 894 DHIECLQLLLSHNAQVNAVDSTGKTPLMMAAEN--GQTSAVEVLVSSAkADLTLQDKNKNTALHLACSKGHETSAL--LI 969
Cdd:PHA03100 84 DVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNG-ANVNIKNSDGENLLHLYLESNKIDLKIlkLL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1785376409 970 LEQITDRNLINATNSALQ-------------TPLHVAARNGLTVVVQELLGKGASVLAVDENGYTPA-LACAPN 1029
Cdd:PHA03100 163 IDKGVDINAKNRVNYLLSygvpinikdvygfTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLhIAILNN 236
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
756-1036 |
3.98e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 66.53 E-value: 3.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 756 TGHEECVEALLQHNANFL-LRDCRGRTPIHLAAACGHIGVLSALLQTAISVDVVPAIADNhgytPLHWACYNGHDACVEL 834
Cdd:PHA02874 11 SGDIEAIEKIIKNKGNCInISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPH----PLLTAIKIGAHDIIKL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 835 LLEQEVfqkmeGNSFSPLHCavINDnegaaEMLIDTLGTSI-VNSVDSKGRTPLHAAAFTDHIECLQLLLSHNAQVNAVD 913
Cdd:PHA02874 87 LIDNGV-----DTSILPIPC--IEK-----DMIKTILDCGIdVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIED 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 914 STGKTPLMMAAENGQTSAVEVLVSSAkADLTLQDKNKNTALHLACSKGHETSALLILEQITdrNLINATNSALqTPLHVA 993
Cdd:PHA02874 155 DNGCYPIHIAIKHNFFDIIKLLLEKG-AYANVKDNNGESPLHNAAEYGDYACIKLLIDHGN--HIMNKCKNGF-TPLHNA 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1785376409 994 ARNGLTVVvqELLGKGASVLAVDENGYTP---ALACAPNKDVADCL 1036
Cdd:PHA02874 231 IIHNRSAI--ELLINNASINDQDIDGSTPlhhAINPPCDIDIIDIL 274
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
227-372 |
7.87e-11 |
|
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: 66.19 E-value: 7.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 227 MCKDKK-SYTPLHAAASSGMISVIKYLLDL-GVDMNESNAYGNTPLHVACYNGQDVVVNELIDCGANVnqVNE------- 297
Cdd:cd22192 10 LLQQKRiSESPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPEL--VNEpmtsdly 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 298 RGFTPLHFAAASTHGALcLELLVCNGADVN---------IKSKD-----GKTPLHMTAIHGRFSRSQIIIQNGAEIDCED 363
Cdd:cd22192 88 QGETALHIAVVNQNLNL-VRELIARGADVVspratgtffRPGPKnliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQD 166
|
....*....
gi 1785376409 364 KNGNTPLHI 372
Cdd:cd22192 167 SLGNTVLHI 175
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
502-607 |
1.65e-10 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 58.59 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 502 LHYAATSDtDGKCLEYLLRNDANPGIRDKHGYNAVHYAAAYGHRLCLELiaretpldvLMETSGTDMLNDAETrapisPL 581
Cdd:pfam12796 1 LHLAAKNG-NLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKL---------LLEHADVNLKDNGRT-----AL 65
|
90 100
....*....|....*....|....*.
gi 1785376409 582 HLAAYHGHHQALEVLVQSLLDLDVRN 607
Cdd:pfam12796 66 HYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
689-898 |
2.13e-10 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 64.89 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 689 HSECLRLLIGNADVQAAVDIHDGNGQTPLMLSVLNGHTECVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVEALLQH 768
Cdd:PLN03192 501 HKELHDLNVGDLLGDNGGEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKH 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 769 NANFLLRDCRGRTPIHLAAACGH-------------------------------IGVLSALLQTAISVDVvpaiADNHGY 817
Cdd:PLN03192 581 ACNVHIRDANGNTALWNAISAKHhkifrilyhfasisdphaagdllctaakrndLTAMKELLKQGLNVDS----EDHQGA 656
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 818 TPLHWACYNGHDACVELLLEQ--EVFQKMEGNSFSPLHC-AVINDNE-GAAEMLIDTLGTSIVNSVDSKGRTPLHAAAFT 893
Cdd:PLN03192 657 TALQVAMAEDHVDMVRLLIMNgaDVDKANTDDDFSPTELrELLQKRElGHSITIVDSVPADEPDLGRDGGSRPGRLQGTS 736
|
....*
gi 1785376409 894 DHIEC 898
Cdd:PLN03192 737 SDNQC 741
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
782-1012 |
2.58e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 64.13 E-value: 2.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 782 PIHLAAACGHIGVLSALLQTAISVDVvpaiADNHGYTPLHWACYNGHDACVELLLeQEVFQKMEGNSFSPLHCAVINDNE 861
Cdd:PHA02878 40 PLHQAVEARNLDVVKSLLTRGHNVNQ----PDHRDLTPLHIICKEPNKLGMKEMI-RSINKCSVFYTLVAIKDAFNNRNV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 862 GAAEMLIDTLGTSIVNSVDSKGRTplhaAAFTDHIEC--LQLLLSHNAQVNAVD-STGKTPLMMAAENGQTSAVEVLVSS 938
Cdd:PHA02878 115 EIFKIILTNRYKNIQTIDLVYIDK----KSKDDIIEAeiTKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSY 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1785376409 939 AkADLTLQDKNKNTALHLACSKGHETSALLILEQITDrnlINATNSALQTPLHVAARNGLTV-VVQELLGKGASV 1012
Cdd:PHA02878 191 G-ANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS---TDARDKCGNTPLHISVGYCKDYdILKLLLEHGVDV 261
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
469-551 |
2.95e-10 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 57.82 E-value: 2.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 469 LHYAAANCNYQCLFALVGSGASVNDLDERGCSPLHYAATSDTDgKCLEYLLRNdANPGIRDkHGYNAVHYAAAYGHRLCL 548
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHL-EIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77
|
...
gi 1785376409 549 ELI 551
Cdd:pfam12796 78 KLL 80
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
730-1029 |
2.98e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 64.31 E-value: 2.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 730 YSLLNKGANVDAKDKWGRTALHRGAVTGHEECVEALLQHNANFL-LRDCRGRTPIHlaAACGHIGVLSALLQTAISVDVV 808
Cdd:PHA02876 25 YDLHKHGANQCENESIPFTAIHQALQLRQIDIVEEIIQQNPELIyITDHKCHSTLH--TICIIPNVMDIVISLTLDCDII 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 809 PAIAdnhgYTPLHWACYNGHDACVELLleqevfqkMEGNSFSPLHCAVIN---------------DNEGAAEMLIDtlGT 873
Cdd:PHA02876 103 LDIK----YASIILNKHKLDEACIHIL--------KEAISGNDIHYDKINesieymklikeriqqDELLIAEMLLE--GG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 874 SIVNSVDSKGRTPLHAAAFTDHIECLQLLLSHNAQVNAVDSTGKTPLMMAAENGQTSAVEVLVSSA----KADLTLQDKN 949
Cdd:PHA02876 169 ADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRsninKNDLSLLKAI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 950 KNTALhlacskghETSALLILEQITdrnlINATNSALQTPLHVAARN-GLTVVVQELLGKGASVLAVDENGYTPALACAP 1028
Cdd:PHA02876 249 RNEDL--------ETSLLLYDAGFS----VNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKGETPLYLMAK 316
|
.
gi 1785376409 1029 N 1029
Cdd:PHA02876 317 N 317
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
584-771 |
3.90e-10 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 64.12 E-value: 3.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 584 AAYHGHHQALEVLVQSLLDLDVRNSTGRTPLDLAAFKGHVECVDVLINQGASILVKDYvvkrtpihsaeiqmvdsrnsvn 663
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDA---------------------- 589
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 664 KNNTELCNSAqkkvrakdmpsaINGHSECLRLLIGNA---DVQAAVDIhdgngqtpLMLSVLNGHTECVYSLLNKGANVD 740
Cdd:PLN03192 590 NGNTALWNAI------------SAKHHKIFRILYHFAsisDPHAAGDL--------LCTAAKRNDLTAMKELLKQGLNVD 649
|
170 180 190
....*....|....*....|....*....|.
gi 1785376409 741 AKDKWGRTALHRGAVTGHEECVEALLQHNAN 771
Cdd:PLN03192 650 SEDHQGATALQVAMAEDHVDMVRLLIMNGAD 680
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
579-630 |
5.01e-10 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 56.13 E-value: 5.01e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1785376409 579 SPLHLAAYHGHHQALEVLVQSLLDLDVRNSTGRTPLDLAAFKGHVECVDVLI 630
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
234-278 |
5.01e-10 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 56.13 E-value: 5.01e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1785376409 234 YTPLHAAASSGMISVIKYLLDLGVDMNESNAYGNTPLHVACYNGQ 278
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGN 46
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
101-154 |
9.75e-10 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 55.36 E-value: 9.75e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1785376409 101 WLTPLHRAVASCSEDAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALV 154
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
201-253 |
1.09e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 54.97 E-value: 1.09e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1785376409 201 RRAIHWAAYMGHIEVVKLLVTHGAEVMCKDKKSYTPLHAAASSGMISVIKYLL 253
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
747-938 |
1.19e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 61.93 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 747 RTALHRGAVTGHEECVEALLQ--HNANFLLRDcrGRTPIHLAAACGHIGVLSALLqtaiSVDVVPAIADNHGYTPLHWAC 824
Cdd:PHA02875 3 QVALCDAILFGELDIARRLLDigINPNFEIYD--GISPIKLAMKFRDSEAIKLLM----KHGAIPDVKYPDIESELHDAV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 825 YNGHDACVELLLE-----QEVFQKmEGNSfsPLHCAVINDNEGAAEMLIDTLGTSIVNSVDSKgrTPLHAAAFTDHIECL 899
Cdd:PHA02875 77 EEGDVKAVEELLDlgkfaDDVFYK-DGMT--PLHLATILKKLDIMKLLIARGADPDIPNTDKF--SPLHLAVMMGDIKGI 151
|
170 180 190
....*....|....*....|....*....|....*....
gi 1785376409 900 QLLLSHNAQVNAVDSTGKTPLMMAAENGQTSAVEVLVSS 938
Cdd:PHA02875 152 ELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDS 190
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
567-808 |
1.84e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 61.22 E-value: 1.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 567 DMLNDAETRAPISPLHLAAYHGHHQALEVLVQSLLDLDVRNSTGRTPLDLAAFKGHV-----ECVDVLINQGASILVKDy 641
Cdd:PHA03100 25 DDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPD- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 642 vvkrtpihsaeiqmvdsrnsvNKNNTELCNSAQKKVrakdmpsainGHSECLRLLIGNAdvqAAVDIHDGNGQTPLMLSV 721
Cdd:PHA03100 104 ---------------------NNGITPLLYAISKKS----------NSYSIVEYLLDNG---ANVNIKNSDGENLLHLYL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 722 LNGHTEC------------------VYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVEALLQHNANFLLRDCRGRTPI 783
Cdd:PHA03100 150 ESNKIDLkilkllidkgvdinaknrVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPL 229
|
250 260
....*....|....*....|....*
gi 1785376409 784 HLAAACGHIGVLSALLQTAISVDVV 808
Cdd:PHA03100 230 HIAILNNNKEIFKLLLNNGPSIKTI 254
|
|
| PHA02716 |
PHA02716 |
CPXV016; CPX019; EVM010; Provisional |
281-470 |
3.44e-09 |
|
CPXV016; CPX019; EVM010; Provisional
Pssm-ID: 165089 [Multi-domain] Cd Length: 764 Bit Score: 61.08 E-value: 3.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 281 VVNELIDCG-ANVNQV-NERGFTPLHFAAASTHGAL-CLELLVCNGADVNIKSKDGKTPLHMTAIHGRFSRSQI--IIQN 355
Cdd:PHA02716 157 LIKYMVDVGiVNLNYVcKKTGYGILHAYLGNMYVDIdILEWLCNNGVNVNLQNNHLITPLHTYLITGNVCASVIkkIIEL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 356 GAEIDCEDKNGNTPLH---IAARYGHELLINTLITSRADTSKRGIHGMFPLHLAALSGFS-DCCRKLLSSGFDIDTHDDF 431
Cdd:PHA02716 237 GGDMDMKCVNGMSPIMtyiINIDNINPEITNIYIESLDGNKVKNIPMILHSYITLARNIDiSVVYSFLQPGVKLHYKDSA 316
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1785376409 432 GRTCLHAAAAGGNL--ECLNLLLSTGADFNKKDKFGRTPLH 470
Cdd:PHA02716 317 GRTCLHQYILRHNIstDIIKLLHEYGNDLNEPDNIGNTVLH 357
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
883-936 |
4.15e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 53.43 E-value: 4.15e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1785376409 883 GRTPLHAAAFTDHIECLQLLLSHNAQVNAVDSTGKTPLMMAAENGQTSAVEVLV 936
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02989 |
PHA02989 |
ankyrin repeat protein; Provisional |
82-344 |
5.09e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222954 [Multi-domain] Cd Length: 494 Bit Score: 60.14 E-value: 5.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 82 EIIELLILSGARVNAKdSKWLTPL-----HRAVASCS-EDAVQVLLKHSADVNARDKNWQTPlhiaaankavkcaeaLVP 155
Cdd:PHA02989 51 KIVKLLIDNGADVNYK-GYIETPLcavlrNREITSNKiKKIVKLLLKFGADINLKTFNGVSP---------------IVC 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 156 LLSNVNVSDragrtalhhaafsghVEMVSLLLSRGANINafDKKDRRA-----IHWAAYMGHIEVVKLLVTHGAEVMckD 230
Cdd:PHA02989 115 FIYNSNINN---------------CDMLRFLLSKGINVN--DVKNSRGynllhMYLESFSVKKDVIKILLSFGVNLF--E 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 231 KKSY---TPLHAAASSGM----ISVIKYLLDLGVDMNESNAYGNTPL------HVACYNGQDVVVNeLIDCGANVNQVNE 297
Cdd:PHA02989 176 KTSLyglTPMNIYLRNDIdvisIKVIKYLIKKGVNIETNNNGSESVLesfldnNKILSKKEFKVLN-FILKYIKINKKDK 254
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1785376409 298 RGFTPLHFAAASTHGALCLELLVCnGADVNIKSKDGKTPLHMTAIHG 344
Cdd:PHA02989 255 KGFNPLLISAKVDNYEAFNYLLKL-GDDIYNVSKDGDTVLTYAIKHG 300
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
136-187 |
7.04e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 52.66 E-value: 7.04e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1785376409 136 TPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHVEMVSLLL 187
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
402-452 |
7.46e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 52.66 E-value: 7.46e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1785376409 402 PLHLAALSGFSDCCRKLLSSGFDIDTHDDFGRTCLHAAAAGGNLECLNLLL 452
Cdd:pfam13637 4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
99-277 |
7.97e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 57.14 E-value: 7.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 99 SKWLTPLHRAVASCSEDAVQvllKHSADVNARDKNWQTPLHIAAANKAV--KCAEALVPLLSNVNVSDRA-GRTALHH-A 174
Cdd:PHA02859 19 YRYCNPLFYYVEKDDIEGVK---KWIKFVNDCNDLYETPIFSCLEKDKVnvEILKFLIENGADVNFKTRDnNLSALHHyL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 175 AFSGHV--EMVSLLLSRGANINAFDKKDRRAIHwaAYMGH----IEVVKLLVTHGAEVMCKDKK------SYTPLHAAAS 242
Cdd:PHA02859 96 SFNKNVepEILKILIDSGSSITEEDEDGKNLLH--MYMCNfnvrINVIKLLIDSGVSFLNKDFDnnnilySYILFHSDKK 173
|
170 180 190
....*....|....*....|....*....|....*
gi 1785376409 243 sgmisVIKYLLDLGVDMNESNAYGNTPLHVACYNG 277
Cdd:PHA02859 174 -----IFDFLTSLGIDINETNKSGYNCYDLIKFRN 203
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
786-1041 |
1.11e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 58.85 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 786 AAACGHIGVLSALLQTAISvdvvPAIADNHGYTPLHWACYNGHDACVELLLEQEVFQKMEGNSF-SPLHCAVINDNEGAA 864
Cdd:PHA02875 9 AILFGELDIARRLLDIGIN----PNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIeSELHDAVEEGDVKAV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 865 EMLIDtLGTSIVNSVDSKGRTPLHAAAFTDHIECLQLLLSHNAQVNAVDSTGKTPLMMAAENGQTSAVEVLVSsakadlt 944
Cdd:PHA02875 85 EELLD-LGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLID------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 945 lqdknkntalHLACskghetsallileqitdrnlINATNSALQTPLHVAARNGLTVVVQELLGKGASVLAVDENGYTPAL 1024
Cdd:PHA02875 157 ----------HKAC--------------------LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAAL 206
|
250
....*....|....*..
gi 1785376409 1025 ACAPNKDVADCLALILA 1041
Cdd:PHA02875 207 CYAIENNKIDIVRLFIK 223
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
76-303 |
1.17e-08 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 58.91 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 76 AYLG----DAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQVLLKHSADVNARDKNWQTPLH-IAAANKAVkca 150
Cdd:PHA02946 43 AYCGikglDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYyLSGTDDEV--- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 151 ealvpllsnvnvsdragrtalhhaafsghVEMVSLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVTHGAEVMCKD 230
Cdd:PHA02946 120 -----------------------------IERINLLVQYGAKINNSVDEEGCGPLLACTDPSERVFKKIMSIGFEARIVD 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1785376409 231 K--KSYTPLHAAASSGMISVIKYLLDLGVDMNESNAYGNTPLHVACYNG-QDVVVNELIDCGANVNQVNERGFTPL 303
Cdd:PHA02946 171 KfgKNHIHRHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCSKTvKNVDIINLLLPSTDVNKQNKFGDSPL 246
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
405-662 |
1.47e-08 |
|
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: 58.74 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 405 LAALSGFSDCCRKLLSSgfDIDTHDDFGRTCLHAAA---AGGNLECLNLLLSTGADFNKKDKF-----------GRTPLH 470
Cdd:cd21882 1 LEELLGLLECLRWYLTD--SAYQRGATGKTCLHKAAlnlNDGVNEAIMLLLEAAPDSGNPKELvnapctdefyqGQTALH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 471 YAAANCNYQCLFALVGSGASVN-----DLDER--------GCSPLHYAATSDTDgKCLEYLLRNDANP---GIRDKHGYN 534
Cdd:cd21882 79 IAIENRNLNLVRLLVENGADVSaratgRFFRKspgnlfyfGELPLSLAACTNQE-EIVRLLLENGAQPaalEAQDSLGNT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 535 AVHyaaayghrlCLELIARETPLDVLMETSGTDMLndaetrapispLHLAAYHGHHQALEvlvqslldlDVRNSTGRTPL 614
Cdd:cd21882 158 VLH---------ALVLQADNTPENSAFVCQMYNLL-----------LSYGAHLDPTQQLE---------EIPNHQGLTPL 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1785376409 615 DLAAFKGHVECVDVLINQGASILVKDYVVKRT-----PIHSA--EIQMVDS--RNSV 662
Cdd:cd21882 209 KLAAVEGKIVMFQHILQREFSGPYQPLSRKFTewtygPVTSSlyDLSEIDSweKNSV 265
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
590-821 |
1.47e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 58.74 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 590 HQALEV----LVQSLLDLDVR-NSTGR---TPLDLAAFKGHVECVDVLInqgaSILVKD-----YVVKRTPIHSAEIQMV 656
Cdd:PHA02878 42 HQAVEArnldVVKSLLTRGHNvNQPDHrdlTPLHIICKEPNKLGMKEMI----RSINKCsvfytLVAIKDAFNNRNVEIF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 657 DS--RNSVNKNNTelcnSAQKKVRAKDMPSAINghSECLRLLIG-NADVQAaVDIHDGNgqTPLMLSVLNGHTECVYSLL 733
Cdd:PHA02878 118 KIilTNRYKNIQT----IDLVYIDKKSKDDIIE--AEITKLLLSyGADINM-KDRHKGN--TALHYATENKDQRLTELLL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 734 NKGANVDAKDKWGRTALHRGAVTGHEECVEALLQHNANFLLRDCRGRTPIHLAAA-CGHIGVLSALLQTAISVDVVPAIA 812
Cdd:PHA02878 189 SYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGyCKDYDILKLLLEHGVDVNAKSYIL 268
|
....*....
gi 1785376409 813 dnhGYTPLH 821
Cdd:PHA02878 269 ---GLTALH 274
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
336-651 |
1.51e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 58.35 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 336 PLHMtAIHGR-FSRSQIIIQNGAEIDCEDKNGNTPLHIAARYGHELLINTLITSRADTS----KRGIHGMFplHLAALSG 410
Cdd:PHA02878 40 PLHQ-AVEARnLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSvfytLVAIKDAF--NNRNVEI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 411 FsdccRKLLSSGFDIDTHDDFGRTCLHAAAAGGNLECLNLLLSTGADFNKKDK-FGRTPLHYAAANCNYQCLFALVGSGA 489
Cdd:PHA02878 117 F----KIILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 490 SVNDLDERGCSPLHYAaTSDTDGKCLEYLLRNDANpgirdkhgynavhyaaayghrlcleliaretpldvlmetsgtdml 569
Cdd:PHA02878 193 NVNIPDKTNNSPLHHA-VKHYNKPIVHILLENGAS--------------------------------------------- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 570 ndaetrapisplhlaayhghhqalevlvqslldLDVRNSTGRTPLDLAAfkGHVECVDV---LINQGASILVKDYVVKRT 646
Cdd:PHA02878 227 ---------------------------------TDARDKCGNTPLHISV--GYCKDYDIlklLLEHGVDVNAKSYILGLT 271
|
....*
gi 1785376409 647 PIHSA 651
Cdd:PHA02878 272 ALHSS 276
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
180-302 |
2.19e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 55.60 E-value: 2.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 180 VEMVSLLLSRGANINAFDKKDRRAI--HWAAYMGHI--EVVKLLVTHGAEVMCKDKKSYTPLHAAAS--SGMISVIKYLL 253
Cdd:PHA02859 66 VEILKFLIENGADVNFKTRDNNLSAlhHYLSFNKNVepEILKILIDSGSSITEEDEDGKNLLHMYMCnfNVRINVIKLLI 145
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1785376409 254 DLGVDMNESNAYGNTPLHV-ACYNGQDVVVNELIDCGANVNQVNERGFTP 302
Cdd:PHA02859 146 DSGVSFLNKDFDNNNILYSyILFHSDKKIFDFLTSLGIDINETNKSGYNC 195
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
49-133 |
2.31e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 57.75 E-value: 2.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 49 DEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQVLLKHSADVN 128
Cdd:PHA03100 173 NRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
|
....*
gi 1785376409 129 ARDKN 133
Cdd:PHA03100 253 TIIET 257
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
746-799 |
3.03e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 51.12 E-value: 3.03e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1785376409 746 GRTALHRGAVTGHEECVEALLQHNANFLLRDCRGRTPIHLAAACGHIGVLSALL 799
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
69-121 |
4.27e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 50.35 E-value: 4.27e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1785376409 69 RTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQVLL 121
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
712-912 |
4.48e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 56.92 E-value: 4.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 712 NGQTPLMLSVLNGHTECVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVEALLQHNA---NFLLRDcrGRTPIHLAAA 788
Cdd:PHA02875 34 DGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKfadDVFYKD--GMTPLHLATI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 789 CGHIGVLSALLQTAISVDvvpaIADNHGYTPLHWACYNGHDACVELLLEQEVFQKME-GNSFSPLHCAVINDNEGAAEML 867
Cdd:PHA02875 112 LKKLDIMKLLIARGADPD----IPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEdCCGCTPLIIAMAKGDIAICKML 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1785376409 868 IDTlGTSIvNSVDSKGRTPLHAAAFTDH-IECLQLLLSHNAQVNAV 912
Cdd:PHA02875 188 LDS-GANI-DYFGKNGCVAALCYAIENNkIDIVRLFIKRGADCNIM 231
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
417-537 |
4.76e-08 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 56.99 E-value: 4.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 417 KLLSSGFDIDTHDDFGRTCLHAAAAGGNLECLNLLLSTGADFNKKDKFGRTPLHYAAANCN--YQCLFALVGSGASVND- 493
Cdd:PHA02946 57 ELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKINNs 136
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1785376409 494 LDERGCSPLhyAATSDTDGKCLEYLLRNDANPGIRDKHGYNAVH 537
Cdd:PHA02946 137 VDEEGCGPL--LACTDPSERVFKKIMSIGFEARIVDKFGKNHIH 178
|
|
| PHA02716 |
PHA02716 |
CPXV016; CPX019; EVM010; Provisional |
60-303 |
5.39e-08 |
|
CPXV016; CPX019; EVM010; Provisional
Pssm-ID: 165089 [Multi-domain] Cd Length: 764 Bit Score: 57.23 E-value: 5.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 60 DVNFQDNEKRTP-LHAaaYLG----DAEIIELLILSGARVNAKDSKWLTPLHRAV--ASCSEDAVQVLLKHSADVNARDK 132
Cdd:PHA02716 168 NLNYVCKKTGYGiLHA--YLGnmyvDIDILEWLCNNGVNVNLQNNHLITPLHTYLitGNVCASVIKKIIELGGDMDMKCV 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 133 NWQTPLHIAAANkavkcAEALVPLLSNVNVSDRAGRTALHHAafsghvEMVSLLLSRGANINafdkkdrraihwaaymgh 212
Cdd:PHA02716 246 NGMSPIMTYIIN-----IDNINPEITNIYIESLDGNKVKNIP------MILHSYITLARNID------------------ 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 213 IEVVKLLVTHGAEVMCKDKKSYTPLHAAASSGMIS--VIKYLLDLGVDMNESNAYGNTPLH--------VACYNGQ---D 279
Cdd:PHA02716 297 ISVVYSFLQPGVKLHYKDSAGRTCLHQYILRHNIStdIIKLLHEYGNDLNEPDNIGNTVLHtylsmlsvVNILDPEtdnD 376
|
250 260
....*....|....*....|....*..
gi 1785376409 280 V---VVNELIDCGANVNQVNERGFTPL 303
Cdd:PHA02716 377 IrldVIQCLISLGADITAVNCLGYTPL 403
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
772-1008 |
5.95e-08 |
|
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: 56.94 E-value: 5.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 772 FLLRDCRGR-TPIHLAAACGHIGVLSALLQTAiSVDVVPAIAdnHGYTPLHWACYNGHDACVELLLEQE---VFQKMEGN 847
Cdd:cd22192 9 HLLQQKRISeSPLLLAAKENDVQAIKKLLKCP-SCDLFQRGA--LGETALHVAALYDNLEAAVVLMEAApelVNEPMTSD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 848 SF---SPLHCAVINDNEGAAEMLI----DTL-----GTSIVNSVDSK---GRTPLHAAAFTDHIECLQLLLSHNAQVNAV 912
Cdd:cd22192 86 LYqgeTALHIAVVNQNLNLVRELIargaDVVspratGTFFRPGPKNLiyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 913 DSTGKTPL-MMAAENGQTSAVEVLvssakaDLTL-QDKNKNtalhlacskghetsaLLILEQItdrnlinaTNSALQTPL 990
Cdd:cd22192 166 DSLGNTVLhILVLQPNKTFACQMY------DLILsYDKEDD---------------LQPLDLV--------PNNQGLTPF 216
|
250
....*....|....*...
gi 1785376409 991 HVAARNGLTVVVQELLGK 1008
Cdd:cd22192 217 KLAAKEGNIVMFQHLVQK 234
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
869-942 |
5.99e-08 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 56.83 E-value: 5.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 869 DTLGTSIV-------NSVDSKGRTPLHAAAFTDHIECLQLLLSHNAQVNAVDSTGKTPLMMAAENGQTSAVEVLVSSAKA 941
Cdd:PTZ00322 94 DAVGARILltggadpNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQC 173
|
.
gi 1785376409 942 D 942
Cdd:PTZ00322 174 H 174
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
210-401 |
6.40e-08 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 56.80 E-value: 6.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 210 MGHIEVVKLLVTHGAEVmcKDKKSYTPLHAAASSGMISVIKYLLDLGVDMNESNAYGNTPLHVACYNGQDVVVNELIDCG 289
Cdd:PLN03192 504 LHDLNVGDLLGDNGGEH--DDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 290 ANVNQVNERGFTPLHFAAASTHGALCLELLVCNGADVNIKSKDgktPLHMTAIHGRFSRSQIIIQNGAEIDCEDKNGNTP 369
Cdd:PLN03192 582 CNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAGD---LLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATA 658
|
170 180 190
....*....|....*....|....*....|..
gi 1785376409 370 LHIAARYGHELLINTLITSRADTSKRGIHGMF 401
Cdd:PLN03192 659 LQVAMAEDHVDMVRLLIMNGADVDKANTDDDF 690
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
713-823 |
6.65e-08 |
|
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: 56.56 E-value: 6.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 713 GQTPLMLSVLNGHTECVYSLLNKGANV--------------DAKDKWGRTALHRGAVTGHEECVEALLQHNANFLLRDCR 778
Cdd:cd22192 89 GETALHIAVVNQNLNLVRELIARGADVvspratgtffrpgpKNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1785376409 779 GRTPIHLAA-------ACGHIGVLSAL--LQTAISVDVVPaiaDNHGYTPLHWA 823
Cdd:cd22192 169 GNTVLHILVlqpnktfACQMYDLILSYdkEDDLQPLDLVP---NNQGLTPFKLA 219
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
38-194 |
6.80e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 56.15 E-value: 6.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 38 PLVQAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLIlsgarvnakdskwltplhravascsedav 117
Cdd:PHA02875 105 PLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLI----------------------------- 155
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1785376409 118 qvllKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVN-VSDRAGRTALHHAAFSGHVEMVSLLLSRGANIN 194
Cdd:PHA02875 156 ----DHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDyFGKNGCVAALCYAIENNKIDIVRLFIKRGADCN 229
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
420-636 |
9.30e-08 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 56.41 E-value: 9.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 420 SSGFDIDTHDDFGrtcLHAAAAGGNLECLNLLLSTGADFNKKDKFGRTPLHYAAANCNYQCLFALVGSGASVNdldergc 499
Cdd:PLN03192 516 NGGEHDDPNMASN---LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVH------- 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 500 splhyaatsdtdgkcleyllrndanpgIRDKHGYNAVHYAAAYGHrlcleliarETPLDVLMETSGtdmLNDAETRAPIs 579
Cdd:PLN03192 586 ---------------------------IRDANGNTALWNAISAKH---------HKIFRILYHFAS---ISDPHAAGDL- 625
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1785376409 580 pLHLAAYHGHHQALEVLVQSLLDLDVRNSTGRTPLDLAAFKGHVECVDVLINQGASI 636
Cdd:PLN03192 626 -LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
174-332 |
9.62e-08 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 56.41 E-value: 9.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 174 AAFSGHVEMVSLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVTHGAEVMCKDKKSYTPLHAAASSGMISVIKYLL 253
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 254 DLGvdmNESNAY-GNTPLHVACYNGQDVVVNELIDCGANVNQVNERGFTPLHFAAASTHGALcLELLVCNGADVNIKSKD 332
Cdd:PLN03192 612 HFA---SISDPHaAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDM-VRLLIMNGADVDKANTD 687
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
880-1008 |
1.11e-07 |
|
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: 55.92 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 880 DSKGRTPLHAAAFTDHIECLQLLLSHNAQVNAVDST--------------GKTPLMMAAENGQTSAVEVLVSSAKADLTL 945
Cdd:cd22194 138 AYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEIVQLLMEKESTDITS 217
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1785376409 946 QDKNKNTALHLAC-----SKGHETSALLILEQI----TDRNLINATNSALQTPLHVAARNGLTVVVQELLGK 1008
Cdd:cd22194 218 QDSRGNTVLHALVtvaedSKTQNDFVKRMYDMIllksENKNLETIRNNEGLTPLQLAAKMGKAEILKYILSR 289
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
216-288 |
1.13e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 56.06 E-value: 1.13e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1785376409 216 VKLLVTHGAEVMCKDKKSYTPLHAAASSGMISVIKYLLDLGVDMNESNAYGNTPLHVACYNGQDVVVNELIDC 288
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
161-339 |
1.19e-07 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 55.45 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 161 NVSDRAGRTALHHAAFSGHVEMVSLLLSRGANINAFDKKDRRAIHWAAYMGH--IEVVKLLVTHGAEVMCK-DKKSYTPL 237
Cdd:PHA02946 66 NETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKINNSvDEEGCGPL 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 238 HAAASSGMiSVIKYLLDLGVDMNESNAYGNTPLH--VACYNGQDVVVNELIDCGANVNQVNERGFTPLHFAAASTHGALC 315
Cdd:PHA02946 146 LACTDPSE-RVFKKIMSIGFEARIVDKFGKNHIHrhLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCSKTVKNVD 224
|
170 180
....*....|....*....|....
gi 1785376409 316 LELLVCNGADVNIKSKDGKTPLHM 339
Cdd:PHA02946 225 IINLLLPSTDVNKQNKFGDSPLTL 248
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
404-498 |
1.34e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 55.67 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 404 HLAAlSGFSDCCRKLLSSGFDIDTHDDFGRTCLHAAAAGGNLECLNLLLSTGADFNKKDKFGRTPLHYAAANCNYQCLFA 483
Cdd:PTZ00322 88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166
|
90
....*....|....*
gi 1785376409 484 LVGSGASVNDLDERG 498
Cdd:PTZ00322 167 LSRHSQCHFELGANA 181
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
171-253 |
1.47e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 55.67 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 171 LHHAAFSGHVEMVSLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVTHGAEVMCKDKKSYTPLHAAASSGMISVIK 250
Cdd:PTZ00322 86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165
|
...
gi 1785376409 251 YLL 253
Cdd:PTZ00322 166 LLS 168
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
38-182 |
1.56e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 54.97 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 38 PLVQAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAV-------- 109
Cdd:PHA02874 160 PIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIihnrsaie 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 110 ------------------------ASCSEDAVQVLLKHSADVNARDKNWQTPLHIAAanKAVKCAEALVPLLSNVNVSDR 165
Cdd:PHA02874 240 llinnasindqdidgstplhhainPPCDIDIIDILLYHKADISIKDNKGENPIDTAF--KYINKDPVIKDIIANAVLIKE 317
|
170
....*....|....*..
gi 1785376409 166 AGRtaLHHAAFSGHVEM 182
Cdd:PHA02874 318 ADK--LKDSDFLEHIEI 332
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
260-371 |
1.63e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 53.28 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 260 NESNAYGNTPLHvACYNGQDVVVNE---LIDCGANVN-QVNERGFTPLHFAAASTHGAL--CLELLVCNGADVNIKSKDG 333
Cdd:PHA02859 45 NDCNDLYETPIF-SCLEKDKVNVEIlkfLIENGADVNfKTRDNNLSALHHYLSFNKNVEpeILKILIDSGSSITEEDEDG 123
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1785376409 334 KTPLH--MTAIHGRFSRSQIIIQNGAEIDCEDKNGNTPLH 371
Cdd:PHA02859 124 KNLLHmyMCNFNVRINVIKLLIDSGVSFLNKDFDNNNILY 163
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
918-1012 |
2.08e-07 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 55.02 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 918 TPLMMAAENGQTSAVEVLVSSAKADLTLQDKNKNTALHLACSKGHETSALLILEQitDRNLIN-ATNSAL---QTPLHVA 993
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEA--APELVNePMTSDLyqgETALHIA 96
|
90
....*....|....*....
gi 1785376409 994 ARNGLTVVVQELLGKGASV 1012
Cdd:cd22192 97 VVNQNLNLVRELIARGADV 115
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
880-1022 |
2.56e-07 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 54.87 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 880 DSKGRTPLHAAAFTDHIECLQLLLSHNAQVNAVDSTGKTPLMMAAENGQTSAVEVLVSSAKAdltlqdKNKNTALHLACS 959
Cdd:PLN03192 555 DSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASI------SDPHAAGDLLCT 628
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1785376409 960 KGHETSaLLILEQITDRNL-INATNSALQTPLHVAARNGLTVVVQELLGKGASVLAVD-ENGYTP 1022
Cdd:PLN03192 629 AAKRND-LTAMKELLKQGLnVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANtDDDFSP 692
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
55-307 |
2.80e-07 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 54.70 E-value: 2.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 55 IFKKEDVNFQDNEKrtplhaaAYLGDAEIIELLILSGARVNAK-------DSKWLTPLHRAVA-SCSEDAVQVLLKHSAD 126
Cdd:TIGR00870 6 IVPAEESPLSDEEK-------AFLPAAERGDLASVYRDLEEPKklnincpDRLGRSALFVAAIeNENLELTELLLNLSCR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 127 VNARDknwqTPLHIAAANKAVKCAEALVPLLSN---------VNVSDR----AGRTALHHAAFSGHVEMVSLLLSRGANI 193
Cdd:TIGR00870 79 GAVGD----TLLHAISLEYVDAVEAILLHLLAAfrksgplelANDQYTseftPGITALHLAAHRQNYEIVKLLLERGASV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 194 NA------FDKKDRRA--------IHWAAYMGHIEVVKLLVTHGAEVMCKDKKSYTPLHAAAssgmisvikylldlgvdM 259
Cdd:TIGR00870 155 PAracgdfFVKSQGVDsfyhgespLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLV-----------------M 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1785376409 260 NESNAYGNTPLHVACYNG--------QDVVVNELIdcganvnqVNERGFTPLHFAA 307
Cdd:TIGR00870 218 ENEFKAEYEELSCQMYNFalslldklRDSKELEVI--------LNHQGLTPLKLAA 265
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
515-771 |
3.02e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 54.23 E-value: 3.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 515 LEYLLRNDANPGIRDKHGYNAVHYAAAYGHRLCLELiaretpldvLMETSGTDMLNDAETRapiSPLHLAAYHGHHQALE 594
Cdd:PHA02875 18 ARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKL---------LMKHGAIPDVKYPDIE---SELHDAVEEGDVKAVE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 595 VLVQS--LLDlDVRNSTGRTPLDLAAFKGHVECVDVLINQGASILVKDyVVKRTPIHSAeiqmvdsrnsvnknntelcns 672
Cdd:PHA02875 86 ELLDLgkFAD-DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPN-TDKFSPLHLA--------------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 673 aqkkVRAKDmpsaINGhsecLRLLIgnaDVQAAVDIHDGNGQTPLMLSVLNGHTECVYSLLNKGANVDAKDKWGRTALHR 752
Cdd:PHA02875 143 ----VMMGD----IKG----IELLI---DHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALC 207
|
250 260
....*....|....*....|
gi 1785376409 753 GAVTGHE-ECVEALLQHNAN 771
Cdd:PHA02875 208 YAIENNKiDIVRLFIKRGAD 227
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
433-786 |
3.12e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 54.20 E-value: 3.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 433 RTCLHAaaagGNLECLNLLLSTGADF-NKKDKFGRTPLHYAAANCNYQCLFALVGSGASVNDLDERGCSPLhYAATSDTD 511
Cdd:PHA02874 6 RMCIYS----GDIEAIEKIIKNKGNCiNISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPL-LTAIKIGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 512 GKCLEYLLRNDANPGIrdkhgynavhyaaayghrLCLELIARETPLDVLmeTSGTDM-LNDAETRapiSPLHLAAYHGHH 590
Cdd:PHA02874 81 HDIIKLLIDNGVDTSI------------------LPIPCIEKDMIKTIL--DCGIDVnIKDAELK---TFLHYAIKKGDL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 591 QALEVLVQSLLDLDVRNSTGRTPLDLAAFKGHVECVDVLINQGASILVKDYVVKrTPIHSAeiqmvdsrnsvnknntelc 670
Cdd:PHA02874 138 ESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGE-SPLHNA------------------- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 671 nsaqkkvrakdmpsAINGHSECLRLLIGNADvqaAVDIHDGNGQTPLMLSVLngHTECVYSLLNKGANVDAKDKWGRTAL 750
Cdd:PHA02874 198 --------------AEYGDYACIKLLIDHGN---HIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPL 258
|
330 340 350
....*....|....*....|....*....|....*..
gi 1785376409 751 HRG-AVTGHEECVEALLQHNANFLLRDCRGRTPIHLA 786
Cdd:PHA02874 259 HHAiNPPCDIDIIDILLYHKADISIKDNKGENPIDTA 295
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
111-188 |
3.17e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 54.52 E-value: 3.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 111 SCSEDAV--QVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHVEMVSLLLS 188
Cdd:PTZ00322 90 AASGDAVgaRILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
406-645 |
3.62e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 53.84 E-value: 3.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 406 AALSGFSDCCRKLLSSGFDIDTHDDFGRTCLHAAAAGGNLECLNLLLSTGADFNKKDKFGRTPLHYAAANCNYQCLFALV 485
Cdd:PHA02875 9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 486 GSGASVND-LDERGCSPLHYAATSdtdgKCLEYLlrndanpgirdkhgynavhyaaayghRLcleLIARETPLDVlmetS 564
Cdd:PHA02875 89 DLGKFADDvFYKDGMTPLHLATIL----KKLDIM--------------------------KL---LIARGADPDI----P 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 565 GTDMLndaetrapiSPLHLAAYHGHHQALEVLVQSLLDLDVRNSTGRTPLDLAAFKGHVECVDVLINQGASIlvkDYVVK 644
Cdd:PHA02875 132 NTDKF---------SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANI---DYFGK 199
|
.
gi 1785376409 645 R 645
Cdd:PHA02875 200 N 200
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
308-377 |
4.27e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 54.13 E-value: 4.27e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 308 ASTHGALCLELLVCNGADVNIKSKDGKTPLHMTAIHGRFSRSQIIIQNGAEIDCEDKNGNTPLHIAARYG 377
Cdd:PTZ00322 90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENG 159
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
852-1022 |
4.82e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 53.43 E-value: 4.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 852 LHCAVINDNEGAAEMLIDTlgTSIVNSVDSKGRTPLHAAAFTDHIECLQLLLSHNAQVNAVDSTGKTPLMMAAENGQTSA 931
Cdd:PHA02874 128 LHYAIKKGDLESIKMLFEY--GADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYAC 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 932 VEVLVSSAkADLTLQDKNKNTALHLACSkgHETSALLILeqITDRNlINATNSALQTPLHVAARNGLTV-VVQELLGKGA 1010
Cdd:PHA02874 206 IKLLIDHG-NHIMNKCKNGFTPLHNAII--HNRSAIELL--INNAS-INDQDIDGSTPLHHAINPPCDIdIIDILLYHKA 279
|
170
....*....|..
gi 1785376409 1011 SVLAVDENGYTP 1022
Cdd:PHA02874 280 DISIKDNKGENP 291
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
335-386 |
5.14e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 47.65 E-value: 5.14e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1785376409 335 TPLHMTAIHGRFSRSQIIIQNGAEIDCEDKNGNTPLHIAARYGHELLINTLI 386
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
404-520 |
5.56e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 53.75 E-value: 5.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 404 HLAALSGFSDccrKLLSSGFDIDTHDDFGRTCLHAA-------AAGGNLECLNLLLSTGADFNKKDKFGRTPLHYAAANC 476
Cdd:PTZ00322 50 HLEALEATEN---KDATPDHNLTTEEVIDPVVAHMLtvelcqlAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANG 126
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1785376409 477 NYQCLFALVGSGASVNDLDERGCSPLHYAATSDTdGKCLEYLLR 520
Cdd:PTZ00322 127 HVQVVRVLLEFGADPTLLDKDGKTPLELAEENGF-REVVQLLSR 169
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
47-170 |
6.60e-07 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 53.10 E-value: 6.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 47 DPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGD--AEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQVLLKHS 124
Cdd:PHA03095 201 RARIVRELIRAGCDPAATDMLGNTPLHSMATGSSckRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALG 280
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1785376409 125 ADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTA 170
Cdd:PHA03095 281 ADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAATLNTA 326
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
869-1040 |
7.22e-07 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 53.72 E-value: 7.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 869 DTLGTSIVNSVDSKGRTPLHAAAFTDHIECLQLLLSHNAQVNAVDSTGKTPLMMAAENGQTSAVEVLVSSAkADLTLQDK 948
Cdd:PLN03192 511 DLLGDNGGEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA-CNVHIRDA 589
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 949 NKNTALHLACSKGHETsALLILEQITDRNLINATNSALQTplhvAARNGLTVVVQELLGKGASVLAVDENGYTpALACAP 1028
Cdd:PLN03192 590 NGNTALWNAISAKHHK-IFRILYHFASISDPHAAGDLLCT----AAKRNDLTAMKELLKQGLNVDSEDHQGAT-ALQVAM 663
|
170
....*....|..
gi 1785376409 1029 NKDVADCLALIL 1040
Cdd:PLN03192 664 AEDHVDMVRLLI 675
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
715-766 |
8.40e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 46.88 E-value: 8.40e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1785376409 715 TPLMLSVLNGHTECVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVEALL 766
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
465-519 |
8.65e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 46.88 E-value: 8.65e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1785376409 465 GRTPLHYAAANCNYQCLFALVGSGASVNDLDERGCSPLHYAATSDtDGKCLEYLL 519
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNG-NVEVLKLLL 54
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
726-923 |
1.05e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 52.57 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 726 TECVYSLLNKGANVDAKDK-WGRTALHRGAVTGHEECVEALLQHNANFLLRDCRGRTPIHLAAACGHIGVLSALLQTAIS 804
Cdd:PHA02878 147 AEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 805 VDvvpaIADNHGYTPLHWAcynghdacVELLLEQEVFQkmegnsfsplhcavindnegaaeMLIDTlGTSIVNSVDSKGR 884
Cdd:PHA02878 227 TD----ARDKCGNTPLHIS--------VGYCKDYDILK-----------------------LLLEH-GVDVNAKSYILGL 270
|
170 180 190
....*....|....*....|....*....|....*....
gi 1785376409 885 TPLHAAAFTDHIecLQLLLSHNAQVNAVDSTGKTPLMMA 923
Cdd:PHA02878 271 TALHSSIKSERK--LKLLLEYGADINSLNSYKLTPLSSA 307
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
434-537 |
1.08e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 50.59 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 434 TCLHAAAAggNLECLNLLLSTGADFNKKDK-FGRTPLHYAAA---NCNYQCLFALVGSGASVNDLDERGCSPLH-YAATS 508
Cdd:PHA02859 57 SCLEKDKV--NVEILKFLIENGADVNFKTRdNNLSALHHYLSfnkNVEPEILKILIDSGSSITEEDEDGKNLLHmYMCNF 134
|
90 100
....*....|....*....|....*....
gi 1785376409 509 DTDGKCLEYLLRNDANPGIRDKHGYNAVH 537
Cdd:PHA02859 135 NVRINVIKLLIDSGVSFLNKDFDNNNILY 163
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
707-838 |
1.23e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 52.30 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 707 DIHDGNGQTPLMLSVLNGHTECVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVEALLQHNANFLLRDCRGRTPIHLA 786
Cdd:PHA02875 96 DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIA 175
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1785376409 787 AACGHIGVLSALLQTAISVDVVpaiADNHGYTPLHWACYNGHDACVELLLEQ 838
Cdd:PHA02875 176 MAKGDIAICKMLLDSGANIDYF---GKNGCVAALCYAIENNKIDIVRLFIKR 224
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
406-544 |
1.33e-06 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 52.56 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 406 AALSGFSDCCRKLLSSGFDIDTHDDFGRTCLHAAAAGGNLECLNLLLSTGADFNKKDKFGRTPLhYAAANCNYQCLFALV 485
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTAL-WNAISAKHHKIFRIL 610
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1785376409 486 GSGASVNDLDERGcsPLHYAATSDTDGKCLEYLLRNDANPGIRDKHGYNAVHYAAAYGH 544
Cdd:PLN03192 611 YHFASISDPHAAG--DLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDH 667
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
779-836 |
1.51e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 46.11 E-value: 1.51e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1785376409 779 GRTPIHLAAACGHIGVLSALLQTAISVDVVpaiaDNHGYTPLHWACYNGHDACVELLL 836
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAV----DGNGETALHFAASNGNVEVLKLLL 54
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
786-936 |
1.61e-06 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 52.56 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 786 AAACGHIGVLSALLQTAISVDvvpaIADNHGYTPLHWACYNGHDACVELLLEQEV---FQKMEGNS-------------F 849
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPD----IGDSKGRTPLHIAASKGYEDCVLVLLKHACnvhIRDANGNTalwnaisakhhkiF 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 850 SPL-HCAVINDNEGAAEMLIdtlgtsivnsvdskgrtplhAAAFTDHIECLQLLLSHNAQVNAVDSTGKTPLMMAAENGQ 928
Cdd:PLN03192 608 RILyHFASISDPHAAGDLLC--------------------TAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDH 667
|
....*...
gi 1785376409 929 TSAVEVLV 936
Cdd:PLN03192 668 VDMVRLLI 675
|
|
| PHA02989 |
PHA02989 |
ankyrin repeat protein; Provisional |
213-452 |
2.08e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222954 [Multi-domain] Cd Length: 494 Bit Score: 51.67 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 213 IEVVKLLVTHGAEVmckDKKSY--TPLHAA------ASSGMISVIKYLLDLGVDMNESNAYGNTPLHVACYNGQDVVVNE 284
Cdd:PHA02989 50 IKIVKLLIDNGADV---NYKGYieTPLCAVlrnreiTSNKIKKIVKLLLKFGADINLKTFNGVSPIVCFIYNSNINNCDM 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 285 L---IDCGANVNQV-NERGFTPLH--FAAASTHGALCLELLvcnGADVNIKSKD---GKTPLHmtaIHGRFSRSQI---- 351
Cdd:PHA02989 127 LrflLSKGINVNDVkNSRGYNLLHmyLESFSVKKDVIKILL---SFGVNLFEKTslyGLTPMN---IYLRNDIDVIsikv 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 352 ---IIQNGAEIDCEDKNGNTPLHIAAR-----YGHELLINTLITSRADTSKRGIHGMFPLHLAALSGFSDCCRKLLSSGF 423
Cdd:PHA02989 201 ikyLIKKGVNIETNNNGSESVLESFLDnnkilSKKEFKVLNFILKYIKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGD 280
|
250 260
....*....|....*....|....*....
gi 1785376409 424 DIDTHDDFGRTCLHAAAAGGNLECLNLLL 452
Cdd:PHA02989 281 DIYNVSKDGDTVLTYAIKHGNIDMLNRIL 309
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
241-347 |
2.77e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 51.44 E-value: 2.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 241 ASSGMISVIKYLLDLGVDMNESNAYGNTPLHVACYNGQDVVVNELIDCGANVNQVNERGFTPLHFAAASTHGALCLELLV 320
Cdd:PTZ00322 90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
|
90 100 110
....*....|....*....|....*....|....*..
gi 1785376409 321 CNGADVNI------KSKDGKTPLH----MTAIHGRFS 347
Cdd:PTZ00322 170 HSQCHFELganakpDSFTGKPPSLedspISSHHPDFS 206
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
10-124 |
2.84e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 51.44 E-value: 2.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 10 EEGEDDAPHftsKLPQRKILTPP--GIVTPPLVQAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELL 87
Cdd:PTZ00322 58 ENKDATPDH---NLTTEEVIDPVvaHMLTVELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVL 134
|
90 100 110
....*....|....*....|....*....|....*..
gi 1785376409 88 ILSGARVNAKDSKWLTPLHRAVASCSEDAVQVLLKHS 124
Cdd:PTZ00322 135 LEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHS 171
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
36-88 |
4.91e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 44.57 E-value: 4.91e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1785376409 36 TPPLVQAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLI 88
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
266-320 |
4.91e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 44.57 E-value: 4.91e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1785376409 266 GNTPLHVACYNGQDVVVNELIDCGANVNQVNERGFTPLHFAAASTHGAlCLELLV 320
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVE-VLKLLL 54
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
167-198 |
5.74e-06 |
|
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: 43.82 E-value: 5.74e-06
10 20 30
....*....|....*....|....*....|...
gi 1785376409 167 GRTALHHAAFS-GHVEMVSLLLSRGANINAFDK 198
Cdd:pfam00023 2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
|
|
| PHA02989 |
PHA02989 |
ankyrin repeat protein; Provisional |
246-505 |
5.78e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222954 [Multi-domain] Cd Length: 494 Bit Score: 50.12 E-value: 5.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 246 ISVIKYLLDLGVDMNESnaYGNTPLHVACYNGQDV---VVNELIDCGANVNQvneRGF--TPL-----HFAAASTHGALC 315
Cdd:PHA02989 16 KNALEFLLRTGFDVNEE--YRGNSILLLYLKRKDVkikIVKLLIDNGADVNY---KGYieTPLcavlrNREITSNKIKKI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 316 LELLVCNGADVNIKSKDGKTPLhMTAIHG---------RFsrsqiIIQNGAEI-DCEDKNGNTPLHIaarYGHELLINT- 384
Cdd:PHA02989 91 VKLLLKFGADINLKTFNGVSPI-VCFIYNsninncdmlRF-----LLSKGINVnDVKNSRGYNLLHM---YLESFSVKKd 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 385 ----LITSRADT-SKRGIHGMFPLHLAALSGFS----DCCRKLLSSGFDIDTHDDFGRTCL------HAAAAGGNLECLN 449
Cdd:PHA02989 162 vikiLLSFGVNLfEKTSLYGLTPMNIYLRNDIDvisiKVIKYLIKKGVNIETNNNGSESVLesfldnNKILSKKEFKVLN 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1785376409 450 LLLSTgADFNKKDKFGRTPLHYAAANCNYQCLFALVGSGASVNDLDERGCSPLHYA 505
Cdd:PHA02989 242 FILKY-IKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYA 296
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
218-273 |
5.81e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 44.64 E-value: 5.81e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1785376409 218 LLVTHGAEVMCKDKKSYTPLHAAASSGMISVIKYLLDLGVDMNESNAYGNTPLHVA 273
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
924-1019 |
6.17e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 50.28 E-value: 6.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 924 AENGQTSAVEVLVSSAkADLTLQDKNKNTALHLACSKGHETSALLILEQITDRNLINATNsalQTPLHVAARNGLTVVVQ 1003
Cdd:PTZ00322 90 AASGDAVGARILLTGG-ADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDG---KTPLELAEENGFREVVQ 165
|
90
....*....|....*.
gi 1785376409 1004 ELLGKGASVLAVDENG 1019
Cdd:PTZ00322 166 LLSRHSQCHFELGANA 181
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
338-491 |
6.82e-06 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 50.25 E-value: 6.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 338 HMTAIHGrFSRSQIIIQNGAEIDceDKNGNTPLHIAARYGHELLINTLITSRADTSKRGIHGMFPLHLAALSGFSDCCRK 417
Cdd:PLN03192 500 HHKELHD-LNVGDLLGDNGGEHD--DPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLV 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 418 LLSSGFDIDTHDDFGRTCL------------------------HA-------AAAGGNLECLNLLLSTGADFNKKDKFGR 466
Cdd:PLN03192 577 LLKHACNVHIRDANGNTALwnaisakhhkifrilyhfasisdpHAagdllctAAKRNDLTAMKELLKQGLNVDSEDHQGA 656
|
170 180
....*....|....*....|....*
gi 1785376409 467 TPLHYAAANCNYQCLFALVGSGASV 491
Cdd:PLN03192 657 TALQVAMAEDHVDMVRLLIMNGADV 681
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
70-207 |
8.87e-06 |
|
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: 49.63 E-value: 8.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 70 TPLHAAAYLGDAEIIELLILSGARVNA---------KDSKWLT-----PLHRAVASCSEDAVQVLLKHSADVNARDKNWQ 135
Cdd:cd22192 91 TALHIAVVNQNLNLVRELIARGADVVSpratgtffrPGPKNLIyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGN 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 136 TPLHIAA--ANKAVKCAE-----ALVPLLSNVNVS---DRAGRTALHHAAFSGHVEMVSLLLSRganinafdkkdRRAIH 205
Cdd:cd22192 171 TVLHILVlqPNKTFACQMydlilSYDKEDDLQPLDlvpNNQGLTPFKLAAKEGNIVMFQHLVQK-----------RRHIQ 239
|
..
gi 1785376409 206 WA 207
Cdd:cd22192 240 WT 241
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
816-868 |
9.58e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 43.80 E-value: 9.58e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1785376409 816 GYTPLHWACYNGHDACVELLLEQEV-FQKMEGNSFSPLHCAVINDNEGAAEMLI 868
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGAdINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
167-195 |
9.73e-06 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 43.35 E-value: 9.73e-06
10 20
....*....|....*....|....*....
gi 1785376409 167 GRTALHHAAFSGHVEMVSLLLSRGANINA 195
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
79-153 |
9.79e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 49.90 E-value: 9.79e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1785376409 79 GDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEAL 153
Cdd:PTZ00322 93 GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
282-469 |
1.19e-05 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 49.28 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 282 VNELIDCGANVNQVNERGFTPLHFAAASTHGALcLELLVCNGADVNIKSKDGKTPLHMTAIHGR--FSRSQIIIQNGAEI 359
Cdd:PHA02946 55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRI-VAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKI 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 360 DCE-DKNGNTPLhIAARYGHELLINTLITSRADT------SKRGIHgmfpLHLAALSGFSDCCRKLLSSGFDIDTHDDFG 432
Cdd:PHA02946 134 NNSvDEEGCGPL-LACTDPSERVFKKIMSIGFEArivdkfGKNHIH----RHLMSDNPKASTISWMMKLGISPSKPDHDG 208
|
170 180 190
....*....|....*....|....*....|....*....
gi 1785376409 433 RTCLHAAAAG--GNLECLNLLLSTgADFNKKDKFGRTPL 469
Cdd:PHA02946 209 NTPLHIVCSKtvKNVDIINLLLPS-TDVNKQNKFGDSPL 246
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
424-472 |
1.24e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 43.49 E-value: 1.24e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1785376409 424 DIDTHDDFGRTCLHAAAAGGNLECLNLLLSTGADFNKKDKFGRTPLHYA 472
Cdd:pfam13857 8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
120-174 |
1.30e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 43.49 E-value: 1.30e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1785376409 120 LLKH-SADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHA 174
Cdd:pfam13857 1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
135-309 |
1.75e-05 |
|
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: 48.72 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 135 QTPLHIAAANKAVKCAEALVPLLSNVNVSDRA--------------GRTALHHAAFSGHVEMVSLLLSRGANINA----- 195
Cdd:cd21882 27 KTCLHKAALNLNDGVNEAIMLLLEAAPDSGNPkelvnapctdefyqGQTALHIAIENRNLNLVRLLVENGADVSAratgr 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 196 -FDKKDRRAIHW-------AAYMGHIEVVKLLVTHGAE---VMCKDKKSYTPLHAAAssgmisvikylldlgvdMNESNA 264
Cdd:cd21882 107 fFRKSPGNLFYFgelplslAACTNQEEIVRLLLENGAQpaaLEAQDSLGNTVLHALV-----------------LQADNT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1785376409 265 YGNTPLHVACYNGqdvvvneLIDCGANVNQV-------NERGFTPLHFAAAS 309
Cdd:cd21882 170 PENSAFVCQMYNL-------LLSYGAHLDPTqqleeipNHQGLTPLKLAAVE 214
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
850-903 |
1.76e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 43.03 E-value: 1.76e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1785376409 850 SPLHCAVINDNEGAAEMLIDTlgTSIVNSVDSKGRTPLHAAAFTDHIECLQLLL 903
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEK--GADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
285-339 |
1.96e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 43.10 E-value: 1.96e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1785376409 285 LIDCG-ANVNQVNERGFTPLHFAAasTHGAL-CLELLVCNGADVNIKSKDGKTPLHM 339
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAA--KYGALeIVRVLLAYGVDLNLKDEEGLTALDL 55
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
695-768 |
2.46e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 48.36 E-value: 2.46e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1785376409 695 LLIGNADVqaavDIHDGNGQTPLMLSVLNGHTECVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVEALLQH 768
Cdd:PTZ00322 101 LLTGGADP----NCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
350-420 |
2.84e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 48.36 E-value: 2.84e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1785376409 350 QIIIQNGAEIDCEDKNGNTPLHIAARYGHELLINTLITSRADTSKRGIHGMFPLHLAALSGFSDCCRKLLS 420
Cdd:PTZ00322 99 RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
754-836 |
3.02e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 47.97 E-value: 3.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 754 AVTGHEECVEALLQHNANFLLRDCRGRTPIHLAAACGHIGVLSALLQTAISvdvvPAIADNHGYTPLHWACYNGHDACVE 833
Cdd:PTZ00322 90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGAD----PTLLDKDGKTPLELAEENGFREVVQ 165
|
...
gi 1785376409 834 LLL 836
Cdd:PTZ00322 166 LLS 168
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
732-926 |
3.76e-05 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 47.52 E-value: 3.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 732 LLNKGANVDAKDKWGRTA----LHRGAVTgHEECVEALLQHNANFLLRDCRGRTPIHLAAACGH---IGVLSALLQTAIS 804
Cdd:PHA02798 95 LIENGADINKKNSDGETPlyclLSNGYIN-NLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVD 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 805 VDVvpaIADNHGYTPLHwaCY-----NGHDA-CVELLLEQEVFQKMEGNS----FSPLHCAVINDNEGAAEMLIDTLGTS 874
Cdd:PHA02798 174 INT---HNNKEKYDTLH--CYfkyniDRIDAdILKLFVDNGFIINKENKShkkkFMEYLNSLLYDNKRFKKNILDFIFSY 248
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1785376409 875 I-VNSVDSKGRTPLHAAAFTDHIECLQLLLSHNAQVNAVDSTGKTPLMMAAEN 926
Cdd:PHA02798 249 IdINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFEN 301
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
261-377 |
3.78e-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: 47.83 E-value: 3.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 261 ESNAYGNTPLHVACYNGQDVVVNELIDCGANVN----------QVNERGF----TPLHFAAASTHGALcLELLVCNGADv 326
Cdd:cd22194 136 EEAYEGQTALNIAIERRQGDIVKLLIAKGADVNahakgvffnpKYKHEGFyfgeTPLALAACTNQPEI-VQLLMEKEST- 213
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1785376409 327 NIKSKD--GKTPLHMTAIHGRFSRSQI--IIQNGAEI--DCEDKN--------GNTPLHIAARYG 377
Cdd:cd22194 214 DITSQDsrGNTVLHALVTVAEDSKTQNdfVKRMYDMIllKSENKNletirnneGLTPLQLAAKMG 278
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
167-195 |
4.59e-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.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 41.47 E-value: 4.59e-05
10 20
....*....|....*....|....*....
gi 1785376409 167 GRTALHHAAFSGHVEMVSLLLSRGANINA 195
Cdd:pfam13606 2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
252-306 |
4.71e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 41.95 E-value: 4.71e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1785376409 252 LLDLG-VDMNESNAYGNTPLHVACYNGQDVVVNELIDCGANVNQVNERGFTPLHFA 306
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
418-621 |
5.04e-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: 47.38 E-value: 5.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 418 LLSSGFDIDThddfGRTCLHAAAAG--GNLE-CLNLLL----STGADFNKKDK------FGRTPLHYAAANCNYQCLFAL 484
Cdd:TIGR00870 72 LLNLSCRGAV----GDTLLHAISLEyvDAVEaILLHLLaafrKSGPLELANDQytseftPGITALHLAAHRQNYEIVKLL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 485 VGSGASVN--------------DLDERGCSPLH-YAATSDTDgkCLEYLLRNDANPGIRDKHGyNAVhyaaayghrlcLE 549
Cdd:TIGR00870 148 LERGASVParacgdffvksqgvDSFYHGESPLNaAACLGSPS--IVALLSEDPADILTADSLG-NTL-----------LH 213
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1785376409 550 LIARETPLDVLMETSGTDMLNDAetrapispLHLAAYHGHHQALEVlvqslldldVRNSTGRTPLDLAAFKG 621
Cdd:TIGR00870 214 LLVMENEFKAEYEELSCQMYNFA--------LSLLDKLRDSKELEV---------ILNHQGLTPLKLAAKEG 268
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
713-857 |
5.30e-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: 47.38 E-value: 5.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 713 GQTPLMLSVLNGHTECVYSLLNKGANVDAKDK--------------WGRTALHRGAVTGHEECVEALLQHNANFLLRDCR 778
Cdd:TIGR00870 128 GITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADSL 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 779 GRTPIHLAA------------ACG-HIGVLSALLQTAISVDvVPAIADNHGYTPLHWACYNGHDACVELLLEQEVFQ-KM 844
Cdd:TIGR00870 208 GNTLLHLLVmenefkaeyeelSCQmYNFALSLLDKLRDSKE-LEVILNHQGLTPLKLAAKEGRIVLFRLKLAIKYKQkKF 286
|
170
....*....|...
gi 1785376409 845 EGNSFSPLHCAVI 857
Cdd:TIGR00870 287 VAWPNGQQLLSLY 299
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
402-599 |
6.44e-05 |
|
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: 46.93 E-value: 6.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 402 PLHLAALSGFSDCCRKLL-SSGFDIDTHDDFGRTCLHAAAAGGNLECLNLLLS----------TGADFNkkdkfGRTPLH 470
Cdd:cd22192 20 PLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEaapelvnepmTSDLYQ-----GETALH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 471 YAAANCNYQCLFALVGSGASVN--------------DLDERGCSPLHYAATSDTDgKCLEYLLRNDANPGIRDKHGYNAV 536
Cdd:cd22192 95 IAVVNQNLNLVRELIARGADVVspratgtffrpgpkNLIYYGEHPLSFAACVGNE-EIVRLLIEHGADIRAQDSLGNTVL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 537 HYaaayghrlcLELIARETP----LDVLM--ETSGTDM-LNDAETRAPISPLHLAAYHGHHQALEVLVQS 599
Cdd:cd22192 174 HI---------LVLQPNKTFacqmYDLILsyDKEDDLQpLDLVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
265-293 |
8.34e-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: 40.65 E-value: 8.34e-05
10 20
....*....|....*....|....*....
gi 1785376409 265 YGNTPLHVACYNGQDVVVNELIDCGANVN 293
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
882-913 |
1.01e-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: 40.35 E-value: 1.01e-04
10 20 30
....*....|....*....|....*....|...
gi 1785376409 882 KGRTPLHAAA-FTDHIECLQLLLSHNAQVNAVD 913
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
500-649 |
1.05e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 46.16 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 500 SPLHYAAtSDTDGKCLEYLLR-NDANPGIRDKHGYNAVHYAAAYGHRLCLELIARETPLDVLMETsgTDMLNDAETrapi 578
Cdd:cd22192 19 SPLLLAA-KENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPM--TSDLYQGET---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 579 sPLHLAAYHGHhqalEVLVQSLLD--LDVRNST----------------GRTPLDLAAFKGHVECVDVLINQGASILVKD 640
Cdd:cd22192 92 -ALHIAVVNQN----LNLVRELIArgADVVSPRatgtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQD 166
|
....*....
gi 1785376409 641 YvVKRTPIH 649
Cdd:cd22192 167 S-LGNTVLH 174
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
301-347 |
1.13e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 40.72 E-value: 1.13e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1785376409 301 TPLHFAAASTHGAlCLELLVCNGADVNIKSKDGKTPLHMTAIHGRFS 347
Cdd:pfam13637 3 TALHAAAASGHLE-LLRLLLEKGADINAVDGNGETALHFAASNGNVE 48
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
292-372 |
1.17e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 44.42 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 292 VNQVNERGFTPLHFAAASTHGAL-CLELLVCNGADVNIKSKD-GKTPLH-MTAIHGRFSRS--QIIIQNGAEIDCEDKNG 366
Cdd:PHA02859 44 VNDCNDLYETPIFSCLEKDKVNVeILKFLIENGADVNFKTRDnNLSALHhYLSFNKNVEPEilKILIDSGSSITEEDEDG 123
|
....*.
gi 1785376409 367 NTPLHI 372
Cdd:PHA02859 124 KNLLHM 129
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
265-297 |
1.28e-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: 39.97 E-value: 1.28e-04
10 20 30
....*....|....*....|....*....|....
gi 1785376409 265 YGNTPLHVACY-NGQDVVVNELIDCGANVNQVNE 297
Cdd:pfam00023 1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
703-751 |
1.85e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 40.41 E-value: 1.85e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1785376409 703 QAAVDIHDGNGQTPLMLSVLNGHTECVYSLLNKGANVDAKDKWGRTALH 751
Cdd:pfam13857 6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
186-240 |
2.06e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 40.02 E-value: 2.06e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1785376409 186 LLSRG-ANINAFDKKDRRAIHWAAYMGHIEVVKLLVTHGAEVMCKDKKSYTPLHAA 240
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
432-460 |
2.90e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 39.11 E-value: 2.90e-04
10 20
....*....|....*....|....*....
gi 1785376409 432 GRTCLHAAAAGGNLECLNLLLSTGADFNK 460
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
882-911 |
3.14e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 39.11 E-value: 3.14e-04
10 20 30
....*....|....*....|....*....|
gi 1785376409 882 KGRTPLHAAAFTDHIECLQLLLSHNAQVNA 911
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
249-405 |
3.40e-04 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 44.66 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 249 IKYLLDLGVDMNESNAYGNTPLHVACYNGQDVVVNELIDCGANVNQVNERGFTPLHFAAAS------------THGAL-- 314
Cdd:PHA02946 55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTddevierinllvQYGAKin 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 315 -------CLELLVCN-------------GADVNIKSKDGKTPLHMTAIHGRFSRSQI--IIQNGAEIDCEDKNGNTPLHI 372
Cdd:PHA02946 135 nsvdeegCGPLLACTdpservfkkimsiGFEARIVDKFGKNHIHRHLMSDNPKASTIswMMKLGISPSKPDHDGNTPLHI 214
|
170 180 190
....*....|....*....|....*....|....
gi 1785376409 373 A-ARYGHELLINTLITSRADTSKRGIHGMFPLHL 405
Cdd:PHA02946 215 VcSKTVKNVDIINLLLPSTDVNKQNKFGDSPLTL 248
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
432-463 |
3.55e-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: 3.55e-04
10 20 30
....*....|....*....|....*....|...
gi 1785376409 432 GRTCLHAAAA-GGNLECLNLLLSTGADFNKKDK 463
Cdd:pfam00023 2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
872-923 |
3.79e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 39.64 E-value: 3.79e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1785376409 872 GTSIVNSVDSKGRTPLHAAAFTDHIECLQLLLSHNAQVNAVDSTGKTPLMMA 923
Cdd:pfam13857 5 GPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
59-108 |
3.86e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 39.25 E-value: 3.86e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1785376409 59 EDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRA 108
Cdd:pfam13857 7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
918-963 |
3.90e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 39.18 E-value: 3.90e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1785376409 918 TPLMMAAENGQTSAVEVLVSSaKADLTLQDKNKNTALHLACSKGHE 963
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEK-GADINAVDGNGETALHFAASNGNV 47
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
712-744 |
3.99e-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: 3.99e-04
10 20 30
....*....|....*....|....*....|....
gi 1785376409 712 NGQTPLMLSVL-NGHTECVYSLLNKGANVDAKDK 744
Cdd:pfam00023 1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
977-1022 |
4.43e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 39.25 E-value: 4.43e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1785376409 977 NLINATNSALQTPLHVAARNGLTVVVQELLGKGASVLAVDENGYTP 1022
Cdd:pfam13857 7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTA 52
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
318-373 |
4.52e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 39.25 E-value: 4.52e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1785376409 318 LLVCNGADVNIKSKDGKTPLHMTAIHGRFSRSQIIIQNGAEIDCEDKNGNTPLHIA 373
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
92-141 |
4.84e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 39.25 E-value: 4.84e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1785376409 92 ARVNAKDSKWLTPLHRAVASCSEDAVQVLLKHSADVNARDKNWQTPLHIA 141
Cdd:pfam13857 7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
718-803 |
4.94e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 44.12 E-value: 4.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 718 MLSV------LNGHTECVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVEALLQHNANFLLRDCRGRTPIHLAAACGH 791
Cdd:PTZ00322 81 MLTVelcqlaASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGF 160
|
90
....*....|..
gi 1785376409 792 IGVLSALLQTAI 803
Cdd:PTZ00322 161 REVVQLLSRHSQ 172
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
298-331 |
5.15e-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: 38.42 E-value: 5.15e-04
10 20 30
....*....|....*....|....*....|....
gi 1785376409 298 RGFTPLHFAAASTHGALCLELLVCNGADVNIKSK 331
Cdd:pfam00023 1 DGNTPLHLAAGRRGNLEIVKLLLSKGADVNARDK 34
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
412-601 |
6.62e-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: 43.98 E-value: 6.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 412 SDCCRKLLSSGFdidTHDDF-GRTCLHAAAAGGNLECLNLLLSTGAD---------FNKKDK-----FGRTPLHYAAanC 476
Cdd:cd22194 123 NGILDRFINAEY---TEEAYeGQTALNIAIERRQGDIVKLLIAKGADvnahakgvfFNPKYKhegfyFGETPLALAA--C 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 477 NYQ---CLFALVGSGASVNDLDERGCSPLHYAATSDTDGK--------CLEYLLRNDAN---PGIRDKHGYNAVHYAAAY 542
Cdd:cd22194 198 TNQpeiVQLLMEKESTDITSQDSRGNTVLHALVTVAEDSKtqndfvkrMYDMILLKSENknlETIRNNEGLTPLQLAAKM 277
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1785376409 543 GHRLCLELI-ARETPLDVLMETSG--TDM-----------LNDAETRAPISPLHLAAY---HGHHQ---ALEVLvQSLL 601
Cdd:cd22194 278 GKAEILKYIlSREIKEKPNRSLSRkfTDWaygpvssslydLTNVDTTTDNSVLEIIVYntnIDNRHemlTLEPL-HTLL 355
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
234-261 |
7.30e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 37.95 E-value: 7.30e-04
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
755-1011 |
7.72e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).
Pssm-ID: 411975 [Multi-domain] Cd Length: 600 Bit Score: 43.33 E-value: 7.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 755 VTGHEECVEALLqhNANFLLRDCRGRTPIHLAAACGHIGVLSA---LLQTAISVDVVPAIADN-------HGYTPLHWAC 824
Cdd:cd21882 4 LLGLLECLRWYL--TDSAYQRGATGKTCLHKAALNLNDGVNEAimlLLEAAPDSGNPKELVNApctdefyQGQTALHIAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 825 YNGHDACVELLLEQ--EVFQKMEGNSFSPLHCAVIndnegaaemlidtlgtsivnsvdSKGRTPLHAAAFTDHIECLQLL 902
Cdd:cd21882 82 ENRNLNLVRLLVENgaDVSARATGRFFRKSPGNLF-----------------------YFGELPLSLAACTNQEEIVRLL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 903 LSHNAQVNAV---DSTGKTPLMMaaengqtsavevlvssakadLTLQDKNKNTALHLAC-------SKGHETSALLILEQ 972
Cdd:cd21882 139 LENGAQPAALeaqDSLGNTVLHA--------------------LVLQADNTPENSAFVCqmynlllSYGAHLDPTQQLEE 198
|
250 260 270
....*....|....*....|....*....|....*....
gi 1785376409 973 ITDRNLInatnsalqTPLHVAARNGLTVVVQELLGKGAS 1011
Cdd:cd21882 199 IPNHQGL--------TPLKLAAVEGKIVMFQHILQREFS 229
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
732-786 |
9.01e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 38.48 E-value: 9.01e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1785376409 732 LLNKGANVDAKDKWGRTALHRGAVTGHEECVEALLQHNANFLLRDCRGRTPIHLA 786
Cdd:pfam13857 2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02884 |
PHA02884 |
ankyrin repeat protein; Provisional |
82-222 |
9.16e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165212 [Multi-domain] Cd Length: 300 Bit Score: 42.66 E-value: 9.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 82 EIIELLILSGARVNAK----DSKWLTPLHRAVASCSEDAVQVLLKHSADVNARDKNWQ-TPLHIAAANKAVKCAEALVPL 156
Cdd:PHA02884 47 DIIDAILKLGADPEAPfplsENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLHGCLKCLEILLSY 126
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1785376409 157 LSNVNVSDRAGRTALHHAAFSGHVEMVSLLlsRGANINAFDKKDRRaihwaaYMGHIEVVKLLVTH 222
Cdd:PHA02884 127 GADINIQTNDMVTPIELALMICNNFLAFMI--CDNEISNFYKHPKK------ILINFDILKILVSH 184
|
|
| PHA02795 |
PHA02795 |
ankyrin-like protein; Provisional |
154-195 |
9.18e-04 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165157 [Multi-domain] Cd Length: 437 Bit Score: 43.06 E-value: 9.18e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1785376409 154 VPLLSNVNVSDRAGRTALHHAAFSGHVEMVSLLLSRGANINA 195
Cdd:PHA02795 208 IPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNA 249
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
489-539 |
9.94e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 38.10 E-value: 9.94e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1785376409 489 ASVNDLDERGCSPLHYAAtSDTDGKCLEYLLRNDANPGIRDKHGYNAVHYA 539
Cdd:pfam13857 7 IDLNRLDGEGYTPLHVAA-KYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
450-505 |
1.02e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 38.10 E-value: 1.02e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1785376409 450 LLLSTGADFNKKDKFGRTPLHYAAANCNYQCLFALVGSGASVNDLDERGCSPLHYA 505
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
816-1006 |
1.08e-03 |
|
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: 43.15 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 816 GYTPLHWACYNGHDACVELLLEQEVFQKMEGNSFsplhcavindnegaaeMLIDTLGTSIvnsvdSKGRTPLHAAAFTDH 895
Cdd:TIGR00870 82 GDTLLHAISLEYVDAVEAILLHLLAAFRKSGPLE----------------LANDQYTSEF-----TPGITALHLAAHRQN 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 896 IECLQLLLSHNAQVNA------------VDST--GKTPLMMAAENGQTSAVEvLVSSAKADLTLQDKNKNTALHL----- 956
Cdd:TIGR00870 141 YEIVKLLLERGASVPAracgdffvksqgVDSFyhGESPLNAAACLGSPSIVA-LLSEDPADILTADSLGNTLLHLlvmen 219
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1785376409 957 -------ACSKGHETSALLILEQITD-RNLINATNSALQTPLHVAARNGLTVVVQELL 1006
Cdd:TIGR00870 220 efkaeyeELSCQMYNFALSLLDKLRDsKELEVILNHQGLTPLKLAAKEGRIVLFRLKL 277
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
815-837 |
1.23e-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: 37.18 E-value: 1.23e-03
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
265-293 |
1.24e-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: 37.24 E-value: 1.24e-03
10 20
....*....|....*....|....*....
gi 1785376409 265 YGNTPLHVACYNGQDVVVNELIDCGANVN 293
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
|
|
| PHA02884 |
PHA02884 |
ankyrin repeat protein; Provisional |
248-340 |
1.30e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165212 [Multi-domain] Cd Length: 300 Bit Score: 42.28 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 248 VIKYLLDLGVDMN----ESNAYGNTPLHVACYNGQDVVVNELIDCGANVNQ-VNERGFTPLHFAAasTHGAL-CLELLVC 321
Cdd:PHA02884 48 IIDAILKLGADPEapfpLSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRyAEEAKITPLYISV--LHGCLkCLEILLS 125
|
90
....*....|....*....
gi 1785376409 322 NGADVNIKSKDGKTPLHMT 340
Cdd:PHA02884 126 YGADINIQTNDMVTPIELA 144
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
371-453 |
1.37e-03 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 42.58 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 371 HIAARyGHELLINTLITSRADTSKRGIHGMFPLHLAALSGFSDCCRKLLSSGFDIDTHDDFGRTCLHAAAAGGNLECLNL 450
Cdd:PTZ00322 88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166
|
...
gi 1785376409 451 LLS 453
Cdd:PTZ00322 167 LSR 169
|
|
| TRPV1 |
cd22196 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ... |
276-410 |
1.42e-03 |
|
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: 42.87 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 276 NGQDVVVNELIDCGANVNQVNE-----------RGFTPLHFAAASTHGALcLELLVCNGADVN----------IKSKD-- 332
Cdd:cd22196 60 NGQNDTISLLLDIAEKTGNLKEfvnaaytdsyyKGQTALHIAIERRNMHL-VELLVQNGADVHarasgeffkkKKGGPgf 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 333 --GKTPLHMTAIHGRFSRSQIIIQN---GAEIDCEDKNGNTPLH---------------IAARYGHELL----INTLITS 388
Cdd:cd22196 139 yfGELPLSLAACTNQLDIVKFLLENphsPADISARDSMGNTVLHalvevadntpentkfVTKMYNEILIlgakIRPLLKL 218
|
170 180
....*....|....*....|..
gi 1785376409 389 RADTSKRgihGMFPLHLAALSG 410
Cdd:cd22196 219 EEITNKK---GLTPLKLAAKTG 237
|
|
| TRPV1 |
cd22196 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ... |
882-1008 |
1.63e-03 |
|
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: 42.49 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 882 KGRTPLHAAAFTDHIECLQLLLSHNAQVNAVDST--------------GKTPLMMAAENGQTSAVEVLVSS--AKADLTL 945
Cdd:cd22196 93 KGQTALHIAIERRNMHLVELLVQNGADVHARASGeffkkkkggpgfyfGELPLSLAACTNQLDIVKFLLENphSPADISA 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 946 QDKNKNTALHLACS---------------------KGHETSALLILEQITDRNLInatnsalqTPLHVAARNGLTVVVQE 1004
Cdd:cd22196 173 RDSMGNTVLHALVEvadntpentkfvtkmyneiliLGAKIRPLLKLEEITNKKGL--------TPLKLAAKTGKIGIFAY 244
|
....
gi 1785376409 1005 LLGK 1008
Cdd:cd22196 245 ILGR 248
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
567-617 |
2.08e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 37.33 E-value: 2.08e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1785376409 567 DMLNDAETRAPISPLHLAAYHGHHQALEVLVQSLLDLDVRNSTGRTPLDLA 617
Cdd:pfam13857 6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
69-98 |
2.37e-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: 36.50 E-value: 2.37e-03
10 20 30
....*....|....*....|....*....|.
gi 1785376409 69 RTPLHAAAY-LGDAEIIELLILSGARVNAKD 98
Cdd:pfam00023 3 NTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
36-128 |
2.62e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 41.52 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 36 TPPLVQAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVN-AKDSKWLTPLHRAVASCSE 114
Cdd:PHA02875 136 FSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDyFGKNGCVAALCYAIENNKI 215
|
90
....*....|....
gi 1785376409 115 DAVQVLLKHSADVN 128
Cdd:PHA02875 216 DIVRLFIKRGADCN 229
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
352-502 |
2.75e-03 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 41.58 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 352 IIQNGAEIDCEDKNGNTPLHIAARYGHELLINTLITSRADTSKRGIHGMFPLHLaaLSGFSD------------------ 413
Cdd:PHA02946 58 LLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYY--LSGTDDevierinllvqygakinn 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 414 -----------CC--------RKLLSSGFDIDTHDDFGRTCLHAAAAGGN--LECLNLLLSTGADFNKKDKFGRTPLHYA 472
Cdd:PHA02946 136 svdeegcgpllACtdpservfKKIMSIGFEARIVDKFGKNHIHRHLMSDNpkASTISWMMKLGISPSKPDHDGNTPLHIV 215
|
170 180 190
....*....|....*....|....*....|.
gi 1785376409 473 AANCNYQC-LFALVGSGASVNDLDERGCSPL 502
Cdd:PHA02946 216 CSKTVKNVdIINLLLPSTDVNKQNKFGDSPL 246
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
785-990 |
2.85e-03 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 41.58 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 785 LAAACGHIGVLSALLQTAISVDVVPAIADNHGYTPLHWACYNGHDACVELLLEQEVF-QKMEGNSFSPLHCAVINDNEGA 863
Cdd:PHA02946 41 LHAYCGIKGLDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADpNACDKQHKTPLYYLSGTDDEVI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 864 AEM-LIDTLGTSIVNSVDSKGRTPLHAAafTDHIE-CLQLLLSHNAQVNAVDSTGKTPL--MMAAENGQTSAVEVLVSSA 939
Cdd:PHA02946 121 ERInLLVQYGAKINNSVDEEGCGPLLAC--TDPSErVFKKIMSIGFEARIVDKFGKNHIhrHLMSDNPKASTISWMMKLG 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1785376409 940 KADlTLQDKNKNTALHLACSKghETSALLILEQITDRNLINATNSALQTPL 990
Cdd:PHA02946 199 ISP-SKPDHDGNTPLHIVCSK--TVKNVDIINLLLPSTDVNKQNKFGDSPL 246
|
|
| PHA02791 |
PHA02791 |
ankyrin-like protein; Provisional |
812-981 |
2.87e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165154 [Multi-domain] Cd Length: 284 Bit Score: 41.18 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 812 ADNHGYTPLHWACYNGHDACVELLLEQEVFQKMEGNSFsPLH-CAVINDNEGAAEMLIDTLGTSivnSVDSKGRTPLHAA 890
Cdd:PHA02791 26 ADVHGHSALYYAIADNNVRLVCTLLNAGALKNLLENEF-PLHqAATLEDTKIVKILLFSGMDDS---QFDDKGNTALYYA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 891 AFTDHIECLQLLLSHNAQVNAVDSTG-KTPLMMAAENGQTSAVEVLVSSAKADLTLQDknKNTALHLACSKGHETSALLI 969
Cdd:PHA02791 102 VDSGNMQTVKLFVKKNWRLMFYGKTGwKTSFYHAVMLNDVSIVSYFLSEIPSTFDLAI--LLSCIHITIKNGHVDMMILL 179
|
170
....*....|..
gi 1785376409 970 LEQITDRNLINA 981
Cdd:PHA02791 180 LDYMTSTNTNNS 191
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
497-530 |
3.15e-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: 36.11 E-value: 3.15e-03
10 20 30
....*....|....*....|....*....|....
gi 1785376409 497 RGCSPLHYAATSDTDGKCLEYLLRNDANPGIRDK 530
Cdd:pfam00023 1 DGNTPLHLAAGRRGNLEIVKLLLSKGADVNARDK 34
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
610-640 |
3.21e-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: 36.11 E-value: 3.21e-03
10 20 30
....*....|....*....|....*....|..
gi 1785376409 610 GRTPLDLAAFK-GHVECVDVLINQGASILVKD 640
Cdd:pfam00023 2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
902-957 |
3.47e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 36.94 E-value: 3.47e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1785376409 902 LLSH-NAQVNAVDSTGKTPLMMAAENGQTSAVEVLVsSAKADLTLQDKNKNTALHLA 957
Cdd:pfam13857 1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLL-AYGVDLNLKDEEGLTALDLA 56
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
610-636 |
3.49e-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: 3.49e-03
|
| PHA02792 |
PHA02792 |
ankyrin-like protein; Provisional |
248-335 |
3.51e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165155 [Multi-domain] Cd Length: 631 Bit Score: 41.47 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 248 VIKYLLDLGVDM--NESNAYGNTPLHVACYNGQDVVVNELIDCGA---NVNQVNERGFTPLHFAAAStHGALCLELLVCN 322
Cdd:PHA02792 354 VVEYILKNGNVVveDDDNIINIMPLFPTLSIHESDVLSILKLCKPyidDINKIDKHGRSILYYCIES-HSVSLVEWLIDN 432
|
90
....*....|...
gi 1785376409 323 GADVNIKSKDGKT 335
Cdd:PHA02792 433 GADINITTKYGST 445
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
103-132 |
4.11e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 35.73 E-value: 4.11e-03
10 20 30
....*....|....*....|....*....|.
gi 1785376409 103 TPLHRAVASC-SEDAVQVLLKHSADVNARDK 132
Cdd:pfam00023 4 TPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
|
|
| PHA02736 |
PHA02736 |
Viral ankyrin protein; Provisional |
432-479 |
4.21e-03 |
|
Viral ankyrin protein; Provisional
Pssm-ID: 165103 [Multi-domain] Cd Length: 154 Bit Score: 39.09 E-value: 4.21e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1785376409 432 GRTCLHAAAAGGNL---ECLNLLLSTGADFNKKD-KFGRTPLHYAAANCNYQ 479
Cdd:PHA02736 55 GKQCVHIVSNPDKAdpqEKLKLLMEWGADINGKErVFGNTPLHIAVYTQNYE 106
|
|
| TRPV1 |
cd22196 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ... |
58-276 |
4.33e-03 |
|
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: 40.94 E-value: 4.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 58 KEDVN--FQDNEKR--TPLHAAAYLGDAEIIELLILSGARVNA------------KDSKWLTPLHRAVASCSE--DAVQV 119
Cdd:cd22196 80 KEFVNaaYTDSYYKgqTALHIAIERRNMHLVELLVQNGADVHArasgeffkkkkgGPGFYFGELPLSLAACTNqlDIVKF 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 120 LLKHS---ADVNARDKNWQTPLHiaaankavkcaeALVPLLSNvnvsdragrtALHHAAFSghVEMVSLLLSRGANINAF 196
Cdd:cd22196 160 LLENPhspADISARDSMGNTVLH------------ALVEVADN----------TPENTKFV--TKMYNEILILGAKIRPL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 197 DKkdrraihwaaymghIEVVkllvthgaevmcKDKKSYTPLHAAASSGMISVIKYLLDLGVDMNESN---------AYGn 267
Cdd:cd22196 216 LK--------------LEEI------------TNKKGLTPLKLAAKTGKIGIFAYILGREIKEPECRhlsrkftewAYG- 268
|
....*....
gi 1785376409 268 tPLHVACYN 276
Cdd:cd22196 269 -PVHSSLYD 276
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
38-106 |
4.33e-03 |
|
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: 41.15 E-value: 4.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 38 PLVQAIFNGDPDEVRALIFKKEDVN--------FQDNEKRT------PLHAAAYLGDAEIIELLILSGARVNAKDSKWLT 103
Cdd:cd22192 92 ALHIAVVNQNLNLVRELIARGADVVspratgtfFRPGPKNLiyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNT 171
|
...
gi 1785376409 104 PLH 106
Cdd:cd22192 172 VLH 174
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
82-276 |
4.35e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411978 [Multi-domain] Cd Length: 680 Bit Score: 41.28 E-value: 4.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 82 EIIELLI-----------LSGARVNAKDSKWLTPLHRAVASCSEDAVQVLLKHSADVNARDKN------WQ--------T 136
Cdd:cd22194 111 EIVRILLafaeengildrFINAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkYKhegfyfgeT 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 137 PLHIAAANKAVKCAEALVPLLS-NVNVSDRAGRTALH-----------HAAFSGHVEMVSLLLSRGANINAF-DKKDRRA 203
Cdd:cd22194 191 PLALAACTNQPEIVQLLMEKEStDITSQDSRGNTVLHalvtvaedsktQNDFVKRMYDMILLKSENKNLETIrNNEGLTP 270
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1785376409 204 IHWAAYMGHIEVVKLLVthGAEVMCKDKKSYTPLHAAASSGMISviKYLLDL-GVDMNESNAYgntpLHVACYN 276
Cdd:cd22194 271 LQLAAKMGKAEILKYIL--SREIKEKPNRSLSRKFTDWAYGPVS--SSLYDLtNVDTTTDNSV----LEIIVYN 336
|
|
| PHA02736 |
PHA02736 |
Viral ankyrin protein; Provisional |
164-274 |
4.42e-03 |
|
Viral ankyrin protein; Provisional
Pssm-ID: 165103 [Multi-domain] Cd Length: 154 Bit Score: 39.09 E-value: 4.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 164 DRAGRTALHHAAFSGHVemVSLLLSRGANINA-------FDKKDRRAIHWAAYMGHI---EVVKLLVTHGAEVMCKDKK- 232
Cdd:PHA02736 14 DIEGENILHYLCRNGGV--TDLLAFKNAISDEnrylvleYNRHGKQCVHIVSNPDKAdpqEKLKLLMEWGADINGKERVf 91
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1785376409 233 SYTPLHAAASSGMISVIKYLLDL-GVDMNESNAYGNTPLHVAC 274
Cdd:PHA02736 92 GNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVAC 134
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
712-741 |
5.37e-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: 5.37e-03
10 20 30
....*....|....*....|....*....|
gi 1785376409 712 NGQTPLMLSVLNGHTECVYSLLNKGANVDA 741
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
266-374 |
5.86e-03 |
|
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: 40.83 E-value: 5.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 266 GNTPLHVACYNGQDVVvNELI-------DCGANVNQVNE-------RGFTPLHFAAaSTHGALCLELLVCNGADVNIKSK 331
Cdd:TIGR00870 82 GDTLLHAISLEYVDAV-EAILlhllaafRKSGPLELANDqytseftPGITALHLAA-HRQNYEIVKLLLERGASVPARAC 159
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1785376409 332 DG---KTPLHMTAIHGR--------FSRSQII---IQNGAEIDCEDKNGNTPLHIAA 374
Cdd:TIGR00870 160 GDffvKSQGVDSFYHGEsplnaaacLGSPSIVallSEDPADILTADSLGNTLLHLLV 216
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
264-372 |
5.99e-03 |
|
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: 40.63 E-value: 5.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 264 AYGNTPLHVACYNGQDVVvNELI--------DCGANVNQVNE-------RGFTPLHFAAAStHGALCLELLVCNGADVNI 328
Cdd:cd21882 24 ATGKTCLHKAALNLNDGV-NEAImllleaapDSGNPKELVNApctdefyQGQTALHIAIEN-RNLNLVRLLVENGADVSA 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 329 KSKD-------------GKTPLHMTAIHGRFSRSQIIIQNGAEI---DCEDKNGNTPLHI 372
Cdd:cd21882 102 RATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPaalEAQDSLGNTVLHA 161
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
815-840 |
6.18e-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: 35.31 E-value: 6.18e-03
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
203-226 |
6.87e-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: 35.26 E-value: 6.87e-03
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
876-980 |
6.96e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 40.20 E-value: 6.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 876 VNSVDSKGRTPL-----HAAAFTDHIECLQLLLSHNAQVNAVDSTGKTPLMMAAENGQTSAVEVLVSSAK--ADLTLQDK 948
Cdd:PHA02798 64 VNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLFMIEngADTTLLDK 143
|
90 100 110
....*....|....*....|....*....|....*
gi 1785376409 949 NKNTALHLACSKGHETSALLI---LEQITDRNLIN 980
Cdd:PHA02798 144 DGFTMLQVYLQSNHHIDIEIIkllLEKGVDINTHN 178
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
876-1012 |
7.37e-03 |
|
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: 40.45 E-value: 7.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 876 VNSVDSKGRTPL-HAAAFTDHIECLQLLLSHNAQVnavdSTGKTPLMMAAENGQtSAVEVLvssakadltlqdknkntAL 954
Cdd:TIGR00870 45 INCPDRLGRSALfVAAIENENLELTELLLNLSCRG----AVGDTLLHAISLEYV-DAVEAI-----------------LL 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1785376409 955 HLACSKGHETSALLILEQITDrnlinaTNSALQTPLHVAARNGLTVVVQELLGKGASV 1012
Cdd:TIGR00870 103 HLLAAFRKSGPLELANDQYTS------EFTPGITALHLAAHRQNYEIVKLLLERGASV 154
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
465-493 |
7.44e-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: 35.26 E-value: 7.44e-03
10 20
....*....|....*....|....*....
gi 1785376409 465 GRTPLHYAAANCNYQCLFALVGSGASVND 493
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
203-231 |
7.56e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 35.34 E-value: 7.56e-03
10 20 30
....*....|....*....|....*....|
gi 1785376409 203 AIHWAAYM-GHIEVVKLLVTHGAEVMCKDK 231
Cdd:pfam00023 5 PLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
|
|
| TRPV1-4 |
cd22193 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ... |
691-804 |
7.69e-03 |
|
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: 40.16 E-value: 7.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 691 ECLRLLIGN-ADVQAAV-----DIHDGN-----GQTPLMLSVLNGHTECVYSLL---NKGANVDAKDKWGRTALHrGAVT 756
Cdd:cd22193 90 DIVALLVENgADVHAHAkgrffQPKYQGegfyfGELPLSLAACTNQPDIVQYLLeneHQPADIEAQDSRGNTVLH-ALVT 168
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1785376409 757 GHEECVE--ALLQHNANFLLRDC---------------RGRTPIHLAAACGHIGVLSALLQTAIS 804
Cdd:cd22193 169 VADNTKEntKFVTRMYDMILIRGaklcptveleeirnnDGLTPLQLAAKMGKIEILKYILQREIK 233
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
38-207 |
8.01e-03 |
|
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: 40.25 E-value: 8.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 38 PLVQAifngDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWL-------------TP 104
Cdd:cd21882 47 LLLEA----APDSGNPKELVNAPCTDEFYQGQTALHIAIENRNLNLVRLLVENGADVSARATGRFfrkspgnlfyfgeLP 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 105 LHRAVASCSEDAVQVLLKHSAD---VNARDKNWQTPLH--IAAANKAVKCA--------------EALVPLLSNVNVSDR 165
Cdd:cd21882 123 LSLAACTNQEEIVRLLLENGAQpaaLEAQDSLGNTVLHalVLQADNTPENSafvcqmynlllsygAHLDPTQQLEEIPNH 202
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1785376409 166 AGRTALHHAAFSGHVEMVSLLLSRGANiNAFDKKDRRAIHWA 207
Cdd:cd21882 203 QGLTPLKLAAVEGKIVMFQHILQREFS-GPYQPLSRKFTEWT 243
|
|
| PHA02791 |
PHA02791 |
ankyrin-like protein; Provisional |
124-302 |
8.20e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165154 [Multi-domain] Cd Length: 284 Bit Score: 39.64 E-value: 8.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 124 SADVNARDKNWQTPLHIAAANKAVKC------AEALVPLLSNvnvsdragRTALHHAAFSGHVEMVSLLLSRGANINAFD 197
Cdd:PHA02791 20 SKDAFKADVHGHSALYYAIADNNVRLvctllnAGALKNLLEN--------EFPLHQAATLEDTKIVKILLFSGMDDSQFD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 198 KKDRRAIHWAAYMGHIEVVKLLVTHGAEVMCKDKKSY-TPLHAAASSGMISVIKYLL-------DLGVDMnesnaygnTP 269
Cdd:PHA02791 92 DKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTGWkTSFYHAVMLNDVSIVSYFLseipstfDLAILL--------SC 163
|
170 180 190
....*....|....*....|....*....|...
gi 1785376409 270 LHVACYNGQDVVVNELIDCGANVNQVNERGFTP 302
Cdd:PHA02791 164 IHITIKNGHVDMMILLLDYMTSTNTNNSLLFIP 196
|
|
| TRPV1 |
cd22196 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ... |
199-309 |
8.42e-03 |
|
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: 40.17 E-value: 8.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 199 KDRRAIHWAAYMGHIEVVKLLVTHGAEVMC-------KDKKSYT-------PLHAAASSGMISVIKYLLD---LGVDMNE 261
Cdd:cd22196 93 KGQTALHIAIERRNMHLVELLVQNGADVHArasgeffKKKKGGPgfyfgelPLSLAACTNQLDIVKFLLEnphSPADISA 172
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1785376409 262 SNAYGNTPLHVACYNGQDVVVN---------ELIDCGANVNQV-------NERGFTPLHFAAAS 309
Cdd:cd22196 173 RDSMGNTVLHALVEVADNTPENtkfvtkmynEILILGAKIRPLlkleeitNKKGLTPLKLAAKT 236
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
951-1006 |
8.42e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 35.71 E-value: 8.42e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1785376409 951 NTALHLACSKGHETSALLILEQITDrnlINATNSALQTPLHVAARNGLTVVVQELL 1006
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGAD---INAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
365-391 |
8.88e-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: 34.87 E-value: 8.88e-03
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
357-477 |
9.02e-03 |
|
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: 39.86 E-value: 9.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 357 AEIDCEDKNGNTPLHIAARYGHELLINTLITSRADTSKR------------GIH-GMFPLHLAALSGFSDCCRKLLSSGF 423
Cdd:cd21882 64 APCTDEFYQGQTALHIAIENRNLNLVRLLVENGADVSARatgrffrkspgnLFYfGELPLSLAACTNQEEIVRLLLENGA 143
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1785376409 424 DI---DTHDDFGRTCLHA-------AAAGGNLEC--LNLLLSTGADFNKKDKF-------GRTPLHYAAANCN 477
Cdd:cd21882 144 QPaalEAQDSLGNTVLHAlvlqadnTPENSAFVCqmYNLLLSYGAHLDPTQQLeeipnhqGLTPLKLAAVEGK 216
|
|
| TRPV1-4 |
cd22193 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ... |
298-410 |
9.60e-03 |
|
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: 39.78 E-value: 9.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409 298 RGFTPLHFAAASTHGAlCLELLVCNGADVNIKSKD--------------GKTPLHMTAIHGRFSRSQIIIQNG---AEID 360
Cdd:cd22193 75 EGQTALHIAIERRQGD-IVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLSLAACTNQPDIVQYLLENEhqpADIE 153
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1785376409 361 CEDKNGNTPLHIAARYGHELLINT-LITSRAD-----------TSK----RGIHGMFPLHLAALSG 410
Cdd:cd22193 154 AQDSRGNTVLHALVTVADNTKENTkFVTRMYDmilirgaklcpTVEleeiRNNDGLTPLQLAAKMG 219
|
|
|