|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
54-343 |
7.27e-51 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 181.31 E-value: 7.27e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 54 AEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNV 133
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 134 NVSDRAGRTALHHAAFSGHGEMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVAHGAEVTCKDKKSYTPLHAA 213
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 214 ASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGANVNQKNEKGFTPLHFAAASTHGALcLELLV 293
Cdd:COG0666 161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI-VKLLL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1953334639 294 GNGADVNMKSKDGKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPL 343
Cdd:COG0666 240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
12-276 |
9.03e-50 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 178.22 E-value: 9.03e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 12 LVQAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQ 91
Cdd:COG0666 25 LLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 92 VLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLLSRGANINAFDK 171
Cdd:COG0666 105 LLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 172 KDRRAIHWAAYMGHIEVVKLLVAHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQ 251
Cdd:COG0666 185 DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGA 264
|
250 260
....*....|....*....|....*
gi 1953334639 252 DVVVNELIDCGANVNQKNEKGFTPL 276
Cdd:COG0666 265 ALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
22-308 |
2.90e-49 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 176.68 E-value: 2.90e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 22 DEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQVLLKHSADVN 101
Cdd:COG0666 2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 102 ARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLLSRGANINAFDKKDRRAIHWAA 181
Cdd:COG0666 82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 182 YMGHIEVVKLLVAHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDC 261
Cdd:COG0666 162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1953334639 262 GANVNQKNEKGFTPLHFAAASTHGALCLELLVGNGADVNMKSKDGKT 308
Cdd:COG0666 242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
22-310 |
9.15e-41 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 157.11 E-value: 9.15e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 22 DEVRALIFKKEDVNFQDNEKRTPLHaaAYLG-----DAEIIELLILSGARVNAKDSKWLTPLHRAV-ASCSEEAVQVLLK 95
Cdd:PHA03095 28 EEVRRLLAAGADVNFRGEYGKTPLH--LYLHyssekVKDIVRLLLEAGADVNAPERCGFTPLHLYLyNATTLDVIKLLIK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 96 HSADVNARDKNWQTPLHIAAANKAVkcaealvpllsnvnvsdragrtalhhaafsgHGEMVKLLLSRGANINAFDKKDRR 175
Cdd:PHA03095 106 AGADVNAKDKVGRTPLHVYLSGFNI-------------------------------NPKVIRLLLRKGADVNALDLYGMT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 176 AIHwaAYMGH----IEVVKLLVAHGAEVTCKDKKSYTPLHAAASSGMIS--VVKYLLDLGVDMNEPNAYGNTPLHVACYN 249
Cdd:PHA03095 155 PLA--VLLKSrnanVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATG 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953334639 250 G--QDVVVNELIDCGANVNQKNEKGFTPLHFAAASTHGALCLELLVGnGADVNMKSKDGKTPL 310
Cdd:PHA03095 233 SscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIAL-GADINAVSSDGNTPL 294
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
23-301 |
1.07e-39 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 152.90 E-value: 1.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 23 EVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLH-----RAVASCSEEAVQVLLKHS 97
Cdd:PHA03100 17 NIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 98 ADVNARDKNWQTPLHIAAANKavkcaealvpllsnvnvsdragrtalhhaafSGHGEMVKLLLSRGANINAFDKKDRRAI 177
Cdd:PHA03100 97 ANVNAPDNNGITPLLYAISKK-------------------------------SNSYSIVEYLLDNGANVNIKNSDGENLL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 178 HWAAYMGHI--EVVKLLVAHGAEVTCKDKksytplhaaassgmisvVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVV 255
Cdd:PHA03100 146 HLYLESNKIdlKILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFV 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1953334639 256 NELIDCGANVNQKNEKGFTPLHFAAASTHGALcLELLVGNGADVNM 301
Cdd:PHA03100 209 KYLLDLGANPNLVNKYGDTPLHIAILNNNKEI-FKLLLNNGPSIKT 253
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
154-475 |
1.85e-37 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 142.79 E-value: 1.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 154 EMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVAHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMN 233
Cdd:COG0666 2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 234 EPNAYGNTPLHVACYNGQDVVVNELIDCGANVNQKNEKGFTPLHFAAASTHGALcLELLVGNGADVNMKskdgktplhmt 313
Cdd:COG0666 82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI-VKLLLEAGADVNAQ----------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 314 alhgrfsrsqtiiqsgavidceDKNGNTPLHIAARYGHELLINTLITSGADTAKRGIHGMFPLHLAALSGFSDCCRKLLS 393
Cdd:COG0666 150 ----------------------DNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 394 SGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGADFNKKDKFGRSPLHYAAANCNYQCLFALVGSGASVNDLDERGCT 473
Cdd:COG0666 208 AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
|
..
gi 1953334639 474 PL 475
Cdd:COG0666 288 LL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
602-926 |
2.37e-37 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 142.40 E-value: 2.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 602 LINQGASILVKDYILKRTPIHAAATNGHSECLRLLIGNAEPQNAVDIQDGNGQTPLMLSVLNGHTDCVYSLLNKGANVDA 681
Cdd:COG0666 3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 682 KDKWGRTALHRGAVTGHEECVDALLQHGAKCLFRDSRGRTPIHLSAACGHIGVLGALLQSAASVDAnpaiADNHGYTALH 761
Cdd:COG0666 83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNA----QDNDGNTPLH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 762 WACYNGHETCVELLLEQevfqktegnafsplhcavindneGAaemlidtlgasIVNATDSKGRTPLHAAAFTDHVECLQL 841
Cdd:COG0666 159 LAAANGNLEIVKLLLEA-----------------------GA-----------DVNARDNDGETPLHLAAENGHLEIVKL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 842 LLSHNAQVNSIDSSGKTPLMMAAENGQTNTVEMLVsSASADLTLQDNSKNTALHLACSKGHETSALLILEKITDRNLINA 921
Cdd:COG0666 205 LLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL-EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
|
....*
gi 1953334639 922 TNAAL 926
Cdd:COG0666 284 DLLTL 288
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
633-963 |
7.33e-37 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 140.86 E-value: 7.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 633 LRLLIGNAEPQNAVDIQDGNGQTPLMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQHGAKC 712
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 713 LFRDSRGRTPIHLSAACGHIGVLGALLQSAASVDAnpaiADNHGYTALHWACYNGHETCVELLLEQevfqktegnafspl 792
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNA----RDKDGETPLHLAAYNGNLEIVKLLLEA-------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 793 hcavindnegaaemlidtlGASiVNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSIDSSGKTPLMMAAENGQTNTV 872
Cdd:COG0666 143 -------------------GAD-VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 873 EMLVsSASADLTLQDNSKNTALHLACSKGHETSALLILEKITDrnlINATNAALQTPLHVAARNGLTMVVQELLGKGASV 952
Cdd:COG0666 203 KLLL-EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD---LNAKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278
|
330
....*....|.
gi 1953334639 953 LAVDENGYTPA 963
Cdd:COG0666 279 AAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
507-754 |
4.86e-36 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 138.55 E-value: 4.86e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 507 NAVHYSAAYGHRLCLQLIASETPLDVLMETSGTDMLNDSDNRATISPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTP 586
Cdd:COG0666 44 LLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETP 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 587 LDLAAFKGHVECVDVLINQGASILVKDyILKRTPIHAAATNGHSECLRLLIGNaepqNA-VDIQDGNGQTPLMLSVLNGH 665
Cdd:COG0666 124 LHLAAYNGNLEIVKLLLEAGADVNAQD-NDGNTPLHLAAANGNLEIVKLLLEA----GAdVNARDNDGETPLHLAAENGH 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 666 TDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQHGAKCLFRDSRGRTPIHLSAACGHIGVLGALLQSAASV 745
Cdd:COG0666 199 LEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278
|
....*....
gi 1953334639 746 DANPAIADN 754
Cdd:COG0666 279 AAALLDLLT 287
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
540-825 |
1.33e-34 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 134.31 E-value: 1.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 540 DMLNDSDNRATISPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPLDLAAFKGHVECVDVLINQGASILVKDYILkRT 619
Cdd:COG0666 11 LLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGG-NT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 620 PIHAAATNGHSECLRLLIGNAEPqnaVDIQDGNGQTPLMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHE 699
Cdd:COG0666 90 LLHAAARNGDLEIVKLLLEAGAD---VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 700 ECVDALLQHGAKCLFRDSRGRTPIHLSAACGHIGVLGALLQSaasvDANPAIADNHGYTALHWACYNGHETCVELLLEQE 779
Cdd:COG0666 167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA----GADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1953334639 780 VFQKTEGNAFSPLHCAVINDNEGAAEMLIDTLGASIVNATDSKGRT 825
Cdd:COG0666 243 ADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
22-364 |
1.74e-34 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 141.74 E-value: 1.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 22 DEVR---ALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQVLLKHSA 98
Cdd:PHA02876 156 DELLiaeMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRS 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 99 DVNARDKNwqtpLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGH-GEMVKLLLSRGANINAFDKKDRRAI 177
Cdd:PHA02876 236 NINKNDLS----LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 178 HWAAYMGH-IEVVKLLVAHGAEVTCKDKKSYTPLHAAAS-SGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVV 255
Cdd:PHA02876 312 YLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVII 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 256 NELIDCGANVNQKNEKGFTPLHFAAASTHGALCLELLVGNGADVNMKSKDGKTPLHMTALHG-RFSRSQTIIQSGAVIDC 334
Cdd:PHA02876 392 NTLLDYGADIEALSQKIGTALHFALCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNA 471
|
330 340 350
....*....|....*....|....*....|
gi 1953334639 335 EDKNGNTPLHIAarYGHELLINTLITSGAD 364
Cdd:PHA02876 472 INIQNQYPLLIA--LEYHGIVNILLHYGAE 499
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
737-981 |
2.87e-34 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 133.54 E-value: 2.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 737 ALLQSAASVDANPAIADNHGYTALHWACYNGHETCVELLLEQEVF-QKTEGNAFSPLHCAVINDNEGAAEMLIDtLGASi 815
Cdd:COG0666 35 LLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADiNAKDDGGNTLLHAAARNGDLEIVKLLLE-AGAD- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 816 VNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSIDSSGKTPLMMAAENGQTNTVEMLVSsASADLTLQDNSKNTALH 895
Cdd:COG0666 113 VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLE-AGADVNARDNDGETPLH 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 896 LACSKGHETSALLILEKITDrnlINATNAALQTPLHVAARNGLTMVVQELLGKGASVLAVDENGYTPALACAPNKDVADC 975
Cdd:COG0666 192 LAAENGHLEIVKLLLEAGAD---VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIV 268
|
....*.
gi 1953334639 976 LALILA 981
Cdd:COG0666 269 KLLLLA 274
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
16-367 |
4.28e-34 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 136.63 E-value: 4.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 16 IFNGDPDEVRALIFKKED-VNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQVLL 94
Cdd:PHA02874 9 IYSGDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 95 KHSADVNARDknwqtplhiaaankavkcaealVPLLSNvnvsdragrtalhhaafsghgEMVKLLLSRGANINAFDKKDR 174
Cdd:PHA02874 89 DNGVDTSILP----------------------IPCIEK---------------------DMIKTILDCGIDVNIKDAELK 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 175 RAIHWAAYMGHIEVVKLLVAHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVV 254
Cdd:PHA02874 126 TFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYAC 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 255 VNELIDCGANVNQKNEKGFTPLHfaAASTHGALCLELLVgNGADVNMKSKDGKTPLHMtALHGRFSRS--QTIIQSGAVI 332
Cdd:PHA02874 206 IKLLIDHGNHIMNKCKNGFTPLH--NAIIHNRSAIELLI-NNASINDQDIDGSTPLHH-AINPPCDIDiiDILLYHKADI 281
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1953334639 333 DCEDKNGNTPLHIAARYGH------ELLINTLITSGADTAK 367
Cdd:PHA02874 282 SIKDNKGENPIDTAFKYINkdpvikDIIANAVLIKEADKLK 322
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
86-359 |
7.54e-33 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 133.61 E-value: 7.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 86 SEEAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLL---SNVNVSDRAGRTALH-HAAFSGHGEMVKLLLS 161
Cdd:PHA03095 26 TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIVRLLLeagADVNAPERCGFTPLHlYLYNATTLDVIKLLIK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 162 RGANINAFDKKDRRAIHwaAYMG----HIEVVKLLVAHGAEVTCKDKKSYTPLHAAASSGMISV--VKYLLDLGVDMNEP 235
Cdd:PHA03095 106 AGADVNAKDKVGRTPLH--VYLSgfniNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVYAV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 236 NAYGNTPLHVACYNGQD--VVVNELIDCGANVNQKNEKGFTPLHFAAA-STHGALCLELLVGNGADVNMKSKDGKTPLHM 312
Cdd:PHA03095 184 DDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHSMATgSSCKRSLVLPLLIAGISINARNRYGQTPLHY 263
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1953334639 313 TALHGR---FSRsqtIIQSGAVIDCEDKNGNTPLHIAARYGHELLINTLI 359
Cdd:PHA03095 264 AAVFNNpraCRR---LIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
225-503 |
1.15e-32 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 128.53 E-value: 1.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 225 LLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGANVNQKNEKGFTPLHFAAASTHGALCLELLVGNGADVNMKSK 304
Cdd:COG0666 6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 305 DGKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGHELLINTLITSGADTAKRGIHGMFPLHLAALSGF 384
Cdd:COG0666 86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 385 SDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGADFNKKDKFGRSPLHYAAANCNYQCLFALVGSGASV 464
Cdd:COG0666 166 LEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADL 245
|
250 260 270
....*....|....*....|....*....|....*....
gi 1953334639 465 NDLDERGCTPLHYAATSDTDGKCLEYLLRNDANPGIRDK 503
Cdd:COG0666 246 NAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLD 284
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
186-454 |
2.93e-32 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 131.69 E-value: 2.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 186 IEVVKLLVAHGAEVTCKDKKSYTPLHAAASSGM---ISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDV-VVNELIDC 261
Cdd:PHA03095 27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 262 GANVNQKNEKGFTPLH--FAAASTHgALCLELLVGNGADVNMKSKDGKTPLHMtalhgrFSRS--------QTIIQSGAV 331
Cdd:PHA03095 107 GADVNAKDKVGRTPLHvyLSGFNIN-PKVIRLLLRKGADVNALDLYGMTPLAV------LLKSrnanvellRLLIDAGAD 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 332 IDCEDKNGNTPLHIAARYGH--ELLINTLITSGADTAKRGIHGMFPLHLAALsgFSDCCR----KLLSSGFDIDTPDDFG 405
Cdd:PHA03095 180 VYAVDDRFRSLLHHHLQSFKprARIVRELIRAGCDPAATDMLGNTPLHSMAT--GSSCKRslvlPLLIAGISINARNRYG 257
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1953334639 406 RTCLHAAAAGGNLECLNLLLNTGADFNKKDKFGRSPLHYAAANCNYQCL 454
Cdd:PHA03095 258 QTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAV 306
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
737-981 |
4.26e-32 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 126.99 E-value: 4.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 737 ALLQSAASVDANPAIADNHGYTALHWACYNGHETCVELLLEQEVFQKTEGNAFSPLHCAVINDNEGAAEMLIDTLGASIv 816
Cdd:COG0666 2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 817 NATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSIDSSGKTPLMMAAENGQTNTVEMLVSsASADLTLQDNSKNTALHL 896
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLE-AGADVNAQDNDGNTPLHL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 897 ACSKGHETSALLILEKITDrnlINATNAALQTPLHVAARNGLTMVVQELLGKGASVLAVDENGYTPALACAPNKDVADCL 976
Cdd:COG0666 160 AAANGNLEIVKLLLEAGAD---VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVK 236
|
....*
gi 1953334639 977 ALILA 981
Cdd:COG0666 237 LLLEA 241
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
7-177 |
1.35e-31 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 125.45 E-value: 1.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 7 RDQPSLVQAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCS 86
Cdd:COG0666 119 DGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGH 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 87 EEAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLLSRGANI 166
Cdd:COG0666 199 LEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278
|
170
....*....|.
gi 1953334639 167 NAFDKKDRRAI 177
Cdd:COG0666 279 AAALLDLLTLL 289
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
219-475 |
1.45e-31 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 129.76 E-value: 1.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 219 ISVVKYLLDLGVDMNEPNAYGNTPLHV--ACYNGQDV-VVNELIDCGANVNQKNEKGFTPLHFAAASTHGALCLELLVGN 295
Cdd:PHA03095 27 VEEVRRLLAAGADVNFRGEYGKTPLHLylHYSSEKVKdIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDVIKLLIKA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 296 GADVNMKSKDGKTPLH--MTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGH---ELLiNTLITSGADTAKRGI 370
Cdd:PHA03095 107 GADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanvELL-RLLIDAGADVYAVDD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 371 HGMFPLHLAALS--GFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLL--NTGADFNKKDKFGRSPLHYAA 446
Cdd:PHA03095 186 RFRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVLPllIAGISINARNRYGQTPLHYAA 265
|
250 260 270
....*....|....*....|....*....|
gi 1953334639 447 ANCNyQCLFA-LVGSGASVNDLDERGCTPL 475
Cdd:PHA03095 266 VFNN-PRACRrLIALGADINAVSSDGNTPL 294
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
263-525 |
1.16e-30 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 122.76 E-value: 1.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 263 ANVNQKNEKGFTPLHFAAASTHGALCLELLVGNGADVNMKSKDGKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTP 342
Cdd:COG0666 11 LLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 343 LHIAARYGHELLINTLITSGADTAKRGIHGMFPLHLAALSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLN 422
Cdd:COG0666 91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 423 LLLNTGADFNKKDKFGRSPLHYAAANCNYQCLFALVGSGASVNDLDERGCTPLHYAATSDtDGKCLEYLLRNDANPGIRD 502
Cdd:COG0666 171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENG-NLEIVKLLLEAGADLNAKD 249
|
250 260
....*....|....*....|...
gi 1953334639 503 KQGYNAVHYSAAYGHRLCLQLIA 525
Cdd:COG0666 250 KDGLTALLLAAAAGAALIVKLLL 272
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
289-587 |
1.15e-29 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 120.06 E-value: 1.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 289 LELLVGNGADVNMKSKDGKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGHELLINTLITSGADTAKR 368
Cdd:COG0666 4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 369 GIHGMFPLHLAALSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGADFNKKDKFGRSPLHYAAAN 448
Cdd:COG0666 84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 449 CNYQCLFALVGSGASVNDLDERGCTPLHYAATSDtDGKCLEYLLRNDANPGIRDKQGYNAVHYSAAYGHRLCLQLIASET 528
Cdd:COG0666 164 GNLEIVKLLLEAGADVNARDNDGETPLHLAAENG-HLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1953334639 529 PldvlmetsgtdmLNDSDNRATISPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPL 587
Cdd:COG0666 243 A------------DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
352-690 |
6.14e-29 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 117.75 E-value: 6.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 352 ELLINTLITSGADTAKRGIHGMFPLHLAALSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGADF 431
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 432 NKKDKFGRSPLHYAAANCNYQCLFALVGSGASVNDLDERGCTPLHYAATSDtDGKCLEYLLRNDANPGIRDKQGYnavhy 511
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNG-NLEIVKLLLEAGADVNAQDNDGN----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 512 saayghrlclqliasetpldvlmetsgtdmlndsdnratiSPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPLDLAA 591
Cdd:COG0666 155 ----------------------------------------TPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 592 FKGHVECVDVLINQGASILVKDYiLKRTPIHAAATNGHSECLRLLIGNAEpqnAVDIQDGNGQTPLMLSVLNGHTDCVYS 671
Cdd:COG0666 195 ENGHLEIVKLLLEAGADVNAKDN-DGKTALDLAAENGNLEIVKLLLEAGA---DLNAKDKDGLTALLLAAAAGAALIVKL 270
|
330
....*....|....*....
gi 1953334639 672 LLNKGANVDAKDKWGRTAL 690
Cdd:COG0666 271 LLLALLLLAAALLDLLTLL 289
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
75-353 |
8.09e-26 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 112.67 E-value: 8.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 75 LTPLHRAVASCSEEAVQVLLKHSADVNARDKNWQTPLHIA--AANKavkcaEALVPLLSNVNVSD-----RAGRTALHHA 147
Cdd:PHA02878 38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIIckEPNK-----LGMKEMIRSINKCSvfytlVAIKDAFNNR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 148 AFsghgEMVK-LLLSRGANINAFDKKDRRAIHWAAYMgHIEVVKLLVAHGAEVTCKDK-KSYTPLHAAASSGMISVVKYL 225
Cdd:PHA02878 113 NV----EIFKiILTNRYKNIQTIDLVYIDKKSKDDII-EAEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 226 LDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGANVNQKNEKGFTPLHFAAASTHGALCLELLVGNGADVNMKSK- 304
Cdd:PHA02878 188 LSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDYDILKLLLEHGVDVNAKSYi 267
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1953334639 305 DGKTPLHMtALHGRfSRSQTIIQSGAVIDCEDKNGNTPLHIAA--RYGHEL 353
Cdd:PHA02878 268 LGLTALHS-SIKSE-RKLKLLLEYGADINSLNSYKLTPLSSAVkqYLCINI 316
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
186-400 |
4.21e-25 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 109.37 E-value: 4.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 186 IEVVKLLVAHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLH---VACYNGQDVV--VNELID 260
Cdd:PHA03100 15 VKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsNIKYNLTDVKeiVKLLLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 261 CGANVNQKNEKGFTPLHFAAASTHGALCL-ELLVGNGADVNMKSKDGKTPLHMtAL---HGRFSRSQTIIQSGA------ 330
Cdd:PHA03100 95 YGANVNAPDNNGITPLLYAISKKSNSYSIvEYLLDNGANVNIKNSDGENLLHL-YLesnKIDLKILKLLIDKGVdinakn 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 331 ----------VIDCEDKNGNTPLHIAARYGHELLINTLITSGADTAKRGIHGMFPLHLAALSGFSDCCRKLLSSGFDIDT 400
Cdd:PHA03100 174 rvnyllsygvPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
10-270 |
2.03e-24 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 107.44 E-value: 2.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 10 PSLVQAIFN-GDPDEVRALIFKKE-DVNFQDNEKRTPLHAAAY--LGDAEIIELLILSGARVNAKDSKWLTPLHRAVASC 85
Cdd:PHA03100 73 HYLSNIKYNlTDVKEIVKLLLEYGaNVNAPDNNGITPLLYAISkkSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESN 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 86 SEEAvqvllkhsadvnardknwqtplhiaaankavkcaealvpllsnvnvsdragrtalhhaafsghgEMVKLLLSRGAN 165
Cdd:PHA03100 153 KIDL----------------------------------------------------------------KILKLLIDKGVD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 166 INAfdkKDRraihwaaymghievVKLLVAHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHV 245
Cdd:PHA03100 169 INA---KNR--------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHI 231
|
250 260
....*....|....*....|....*
gi 1953334639 246 ACYNGQDVVVNELIDCGANVNQKNE 270
Cdd:PHA03100 232 AILNNNKEIFKLLLNNGPSIKTIIE 256
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
241-543 |
1.92e-23 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 104.66 E-value: 1.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 241 TPLHVACYNGQDVVVNELIDCGANVNQKNEKGFTPLhFAAASTHGALCLELLVGNGADVNMkskdgktpLHMTALHGRFS 320
Cdd:PHA02874 37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPL-LTAIKIGAHDIIKLLIDNGVDTSI--------LPIPCIEKDMI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 321 RsqTIIQSGAVIDCEDKNGNTPLHIAARYGHELLINTLITSGADTAKRGIHGMFPLHLAALSGFSDCCRKLLSSGFDIDT 400
Cdd:PHA02874 108 K--TILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 401 PDDFGRTCLHAAAAGGNLECLNLLLNTGADFNKKDKFGRSPLHYAAanCNYQCLFALVGSGASVNDLDERGCTPLHYAAT 480
Cdd:PHA02874 186 KDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI--IHNRSAIELLINNASINDQDIDGSTPLHHAIN 263
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953334639 481 SDTDGKCLEYLLRNDANPGIRDKQGYNAVHYSAAYGHRLCL--QLIASETPLDVLMETSGTDMLN 543
Cdd:PHA02874 264 PPCDIDIIDILLYHKADISIKDNKGENPIDTAFKYINKDPVikDIIANAVLIKEADKLKDSDFLE 328
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
554-863 |
2.23e-22 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 101.58 E-value: 2.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 554 LHLAAYHGHHQALEVLVQS---LLDLDVRNSSgrTPLDLAAFKGHVECVDVLINQGASIlvkDYILKRTP--IHAAATNG 628
Cdd:PHA02874 5 LRMCIYSGDIEAIEKIIKNkgnCINISVDETT--TPLIDAIRSGDAKIVELFIKHGADI---NHINTKIPhpLLTAIKIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 629 HSECLRLLIGNAEPQNAVDIQDGNGQTplmlsvlnghtdcVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQH 708
Cdd:PHA02874 80 AHDIIKLLIDNGVDTSILPIPCIEKDM-------------IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 709 GAKCLFRDSRGRTPIHLSAACGHIGVLGALLQSAASVDANpaiaDNHGYTALHWACYNGHETCVELLLEQ--EVFQKTEg 786
Cdd:PHA02874 147 GADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVK----DNNGESPLHNAAEYGDYACIKLLIDHgnHIMNKCK- 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953334639 787 NAFSPLHCAVINdNEGAAEMLIDTlgASIvNATDSKGRTPLH-AAAFTDHVECLQLLLSHNAQVNSIDSSGKTPLMMA 863
Cdd:PHA02874 222 NGFTPLHNAIIH-NRSAIELLINN--ASI-NDQDIDGSTPLHhAINPPCDIDIIDILLYHKADISIKDNKGENPIDTA 295
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
30-317 |
4.93e-21 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 97.64 E-value: 4.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 30 KKEDVNFQDNEKRT---------PLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQVLLK----- 95
Cdd:PHA02878 17 LKYIEYIDHTENYStsaslipfiPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRsinkc 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 96 -------------HSADVNA-------RDKNWQTP--LHIAAANKAVKCAEALVPLL----SNVNVSDR-AGRTALHHAA 148
Cdd:PHA02878 97 svfytlvaikdafNNRNVEIfkiiltnRYKNIQTIdlVYIDKKSKDDIIEAEITKLLlsygADINMKDRhKGNTALHYAT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 149 FSGHGEMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVAHGAEVTCKDKKSYTPLHAAASSGM-ISVVKYLLD 227
Cdd:PHA02878 177 ENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKdYDILKLLLE 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 228 LGVDMN-EPNAYGNTPLHVACYNGQdvVVNELIDCGANVNQKNEKGFTPLHFAAASTHGALCLELLVGNGADVNMKSKDG 306
Cdd:PHA02878 257 HGVDVNaKSYILGLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPLSSAVKQYLCINIGRILISNICLLKRIKPDI 334
|
330
....*....|....*
gi 1953334639 307 KTPL----HMTALHG 317
Cdd:PHA02878 335 KNSEgfidNMDCITS 349
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
144-236 |
8.44e-21 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 87.86 E-value: 8.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 144 LHHAAFSGHGEMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVAHgAEVTCKDKKsYTPLHAAASSGMISVVK 223
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG-RTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1953334639 224 YLLDLGVDMNEPN 236
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
177-269 |
1.27e-20 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 87.48 E-value: 1.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 177 IHWAAYMGHIEVVKLLVAHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLgVDMNEPNaYGNTPLHVACYNGQDVVVN 256
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1953334639 257 ELIDCGANVNQKN 269
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
111-203 |
1.32e-20 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 87.09 E-value: 1.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 111 LHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLLSRgANINAFDkKDRRAIHWAAYMGHIEVVK 190
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1953334639 191 LLVAHGAEVTCKD 203
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
702-982 |
2.51e-20 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 95.48 E-value: 2.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 702 VDALLQHGAKCLFRDSRGRTPIHLSAACGH---IGVLGALLQSAASVDAnpaiADNHGYTALH-WACYNGHETCVELLLE 777
Cdd:PHA03095 30 VRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNA----PERCGFTPLHlYLYNATTLDVIKLLIK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 778 QEV-FQKTEGNAFSPLH--CAVINDNEGAAEMLIDtLGASiVNATDSKGRTPLHAA-AFTD-HVECLQLLLSHNAQVNSI 852
Cdd:PHA03095 106 AGAdVNAKDKVGRTPLHvyLSGFNINPKVIRLLLR-KGAD-VNALDLYGMTPLAVLlKSRNaNVELLRLLIDAGADVYAV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 853 DSSGKTPLMMAAENGQTNT--VEMLVSsASADLTLQDNSKNTALHLACSKGHETSALLI--LEKITDrnlINATNAALQT 928
Cdd:PHA03095 184 DDRFRSLLHHHLQSFKPRAriVRELIR-AGCDPAATDMLGNTPLHSMATGSSCKRSLVLplLIAGIS---INARNRYGQT 259
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1953334639 929 PLHVAARNGLTMVVQELLGKGASVLAVDENGYTPALACAPNKDVaDCLALILAT 982
Cdd:PHA03095 260 PLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNG-RAVRAALAK 312
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
192-679 |
1.20e-19 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 94.74 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 192 LVAHGAEvTCKDKK-SYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYG-NTPLHVACY--NGQDVVVNELIDCGANVNQ 267
Cdd:PHA02876 27 LHKHGAN-QCENESiPFTAIHQALQLRQIDIVEEIIQQNPELIYITDHKcHSTLHTICIipNVMDIVISLTLDCDIILDI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 268 KNEKGFTPLHfaaasTHGALCLELLVG--NGADVNMkSKDGKTPLHMTALHGRFSR-----SQTIIQSGAVIDCEDKNGN 340
Cdd:PHA02876 106 KYASIILNKH-----KLDEACIHILKEaiSGNDIHY-DKINESIEYMKLIKERIQQdelliAEMLLEGGADVNAKDIYCI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 341 TPLHIAARYGHELLINTLITSGADTAKRGIHGMFPLHLAALSGFSDCCRK-----------------------------L 391
Cdd:PHA02876 180 TPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAiidnrsninkndlsllkairnedletsllL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 392 LSSGFDIDTPDDFGRTCLH-AAAAGGNLECLNLLLNTGADFNKKDKFGRSPLHYAAAN-CNYQCLFALVGSGASVNDLDE 469
Cdd:PHA02876 260 YDAGFSVNSIDDCKNTPLHhASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNgYDTENIRTLIMLGADVNAADR 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 470 RGCTPLHYAATSDTDGKCLEYLLRNDANPGIRDKQGYNAVHYSAAYGhrlclQLIASETPLDVlmetsGTDMLNDSDNRA 549
Cdd:PHA02876 340 LYITPLHQASTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRN-----NVVIINTLLDY-----GADIEALSQKIG 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 550 TIspLHLAAYhghhqalevlvqslldldvrnssGRTPLdlaafkghvECVDVLINQGASILVKDYILKrTPIH-AAATNG 628
Cdd:PHA02876 410 TA--LHFALC-----------------------GTNPY---------MSVKTLIDRGANVNSKNKDLS-TPLHyACKKNC 454
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1953334639 629 HSECLRLLIGNAEPQNAVDIQDgngQTPLMLSVlnGHTDCVYSLLNKGANV 679
Cdd:PHA02876 455 KLDVIEMLLDNGADVNAINIQN---QYPLLIAL--EYHGIVNILLHYGAEL 500
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
12-104 |
4.83e-19 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 82.86 E-value: 4.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 12 LVQAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLiLSGARVNAKDSKWlTPLHRAVASCSEEAVQ 91
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL-LEHADVNLKDNGR-TALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1953334639 92 VLLKHSADVNARD 104
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
587-683 |
2.81e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 80.55 E-value: 2.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 587 LDLAAFKGHVECVDVLINQGASILVKDyILKRTPIHAAATNGHSECLRLLIGNAEPQNavdiqDGNGQTPLMLSVLNGHT 666
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQD-KNGRTALHLAAKNGHLEIVKLLLEHADVNL-----KDNGRTALHYAARSGHL 74
|
90
....*....|....*..
gi 1953334639 667 DCVYSLLNKGANVDAKD 683
Cdd:pfam12796 75 EIVKLLLEKGADINVKD 91
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
8-266 |
3.09e-18 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 88.51 E-value: 3.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 8 DQPSLVQAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSE 87
Cdd:PHA02875 2 DQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 88 EAVQVLL---KHSADVNARDKNwqTPLHIAAANKAVkcaealvpllsnvnvsdragrtalhhaafsghgEMVKLLLSRGA 164
Cdd:PHA02875 82 KAVEELLdlgKFADDVFYKDGM--TPLHLATILKKL---------------------------------DIMKLLIARGA 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 165 NINAFDKKDRRAIHWAAYMGHIEVVKLLVAHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDmnePNAYGNTP-L 243
Cdd:PHA02875 127 DPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGAN---IDYFGKNGcV 203
|
250 260
....*....|....*....|....*.
gi 1953334639 244 HVACY---NGQDVVVNELIDCGANVN 266
Cdd:PHA02875 204 AALCYaieNNKIDIVRLFIKRGADCN 229
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
621-716 |
4.49e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 80.16 E-value: 4.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 621 IHAAATNGHSECLRLLIgnaEPQNAVDIQDGNGQTPLMLSVLNGHTDCVYSLLNKgANVDAKDKwGRTALHRGAVTGHEE 700
Cdd:pfam12796 1 LHLAAKNGNLELVKLLL---ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLE 75
|
90
....*....|....*.
gi 1953334639 701 CVDALLQHGAKCLFRD 716
Cdd:pfam12796 76 IVKLLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
210-302 |
4.99e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 79.77 E-value: 4.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 210 LHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCgANVNQKNEkGFTPLHFAAASTHGAlCL 289
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLE-IV 77
|
90
....*....|...
gi 1953334639 290 ELLVGNGADVNMK 302
Cdd:pfam12796 78 KLLLEKGADINVK 90
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
45-170 |
1.22e-17 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 79.00 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 45 LHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQVLLKHsADVNARDKnwqtplhiaaankavkcae 124
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN------------------- 60
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1953334639 125 alvpllsnvnvsdraGRTALHHAAFSGHGEMVKLLLSRGANINAFD 170
Cdd:pfam12796 61 ---------------GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
575-855 |
1.48e-17 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 87.00 E-value: 1.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 575 DLDVRNSSGRTPLDLAAFKGHVECVDV---LINQGASILVKDyILKRTPIHAAATNGHSE-CLRLLIGNaepqNA-VDIQ 649
Cdd:PHA03095 39 DVNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPE-RCGFTPLHLYLYNATTLdVIKLLIKA----GAdVNAK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 650 DGNGQTPL--MLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALH----RGAVTghEECVDALLQHGAKCLFRDSRGRTPI 723
Cdd:PHA03095 114 DKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAvllkSRNAN--VELLRLLIDAGADVYAVDDRFRSLL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 724 HLSAACGHI--GVLGALLQSAASvdanPAIADNHGYTALHWACYngHETCVELLLEQEVFQKTEGNA-----FSPLHCAV 796
Cdd:PHA03095 192 HHHLQSFKPraRIVRELIRAGCD----PAATDMLGNTPLHSMAT--GSSCKRSLVLPLLIAGISINArnrygQTPLHYAA 265
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1953334639 797 INDNEGAAEMLIdTLGASIvNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSIDSS 855
Cdd:PHA03095 266 VFNNPRACRRLI-ALGADI-NAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAAT 322
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
12-195 |
2.10e-17 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 86.17 E-value: 2.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 12 LVQAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQ 91
Cdd:PHA02874 128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIK 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 92 VLLKHSADVNARDKNWQTPLHIAAA-NKAVkcaealVPLLSN---VNVSDRAGRTALHHA-AFSGHGEMVKLLLSRGANI 166
Cdd:PHA02874 208 LLIDHGNHIMNKCKNGFTPLHNAIIhNRSA------IELLINnasINDQDIDGSTPLHHAiNPPCDIDIIDILLYHKADI 281
|
170 180 190
....*....|....*....|....*....|
gi 1953334639 167 NAFDKKDRRAIHWA-AYMGHIEVVKLLVAH 195
Cdd:PHA02874 282 SIKDNKGENPIDTAfKYINKDPVIKDIIAN 311
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
428-777 |
7.21e-17 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 85.50 E-value: 7.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 428 GADFNKKDKFGRSPLHYAAANCNYQCLFALVGSGASVNDLDERGCTPLHYAATSDtDGKCLEYLLRNDANPGIRDKQGYN 507
Cdd:PHA02876 168 GADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSK-NIDTIKAIIDNRSNINKNDLSLLK 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 508 AVHYSAAyghrlclqliasETPLdvLMETSGTDMLNDSDNRATisPLHLAAyhgHHQALEVLVQSLL----DLDVRNSSG 583
Cdd:PHA02876 247 AIRNEDL------------ETSL--LLYDAGFSVNSIDDCKNT--PLHHAS---QAPSLSRLVPKLLergaDVNAKNIKG 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 584 RTPLDLAAFKGH-VECVDVLINQGASILVKDYiLKRTPIHAAATnghseclrllignaepqnavdiqdgngqtplmlsvL 662
Cdd:PHA02876 308 ETPLYLMAKNGYdTENIRTLIMLGADVNAADR-LYITPLHQAST-----------------------------------L 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 663 NGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQHGAKCLFRDSRGRTPIHLsAACGH--IGVLGALLQ 740
Cdd:PHA02876 352 DRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHF-ALCGTnpYMSVKTLID 430
|
330 340 350
....*....|....*....|....*....|....*...
gi 1953334639 741 SAASVDANpaiaDNHGYTALHWACYNGHE-TCVELLLE 777
Cdd:PHA02876 431 RGANVNSK----NKDLSTPLHYACKKNCKlDVIEMLLD 464
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
827-920 |
1.01e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 76.31 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 827 LHAAAFTDHVECLQLLLSHNAQVNSIDSSGKTPLMMAAENGQTNTVEMLVSSASADLtlqDNSKNTALHLACSKGHETSA 906
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL---KDNGRTALHYAARSGHLEIV 77
|
90
....*....|....
gi 1953334639 907 LLILEKITDRNLIN 920
Cdd:pfam12796 78 KLLLEKGADINVKD 91
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
389-747 |
1.22e-16 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 83.92 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 389 RKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECL---NLLLNTGADFNKKDKFGRSPLH-YAAANCNYQCLFALVGSGASV 464
Cdd:PHA03095 31 RRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKdivRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 465 NDLDERGCTPLH-YAATSDTDGKCLEYLLRNDANPGIRDKqgynavhysaaYGHrlclqliaseTPLDVLMetsgtdmln 543
Cdd:PHA03095 111 NAKDKVGRTPLHvYLSGFNINPKVIRLLLRKGADVNALDL-----------YGM----------TPLAVLL--------- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 544 dSDNRATISPLHLaayhghhqalevLVQSLLDLDVRNSSGRTPLD--LAAFKGHVECVDVLINQGASILVKDyILKRTPI 621
Cdd:PHA03095 161 -KSRNANVELLRL------------LIDAGADVYAVDDRFRSLLHhhLQSFKPRARIVRELIRAGCDPAATD-MLGNTPL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 622 HAAATngHSECLRLLIGNaepqnavdiqdgngqtplmlsvlnghtdcvysLLNKGANVDAKDKWGRTALHRGAVTGHEEC 701
Cdd:PHA03095 227 HSMAT--GSSCKRSLVLP--------------------------------LLIAGISINARNRYGQTPLHYAAVFNNPRA 272
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1953334639 702 VDALLQHGAKCLFRDSRGRTPIHLSAACGHIGVLGALLQSAASVDA 747
Cdd:PHA03095 273 CRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAET 318
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
657-748 |
3.76e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 74.77 E-value: 3.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 657 LMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQHGAkcLFRDSRGRTPIHLSAACGHIGVLG 736
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78
|
90
....*....|..
gi 1953334639 737 ALLQSAASVDAN 748
Cdd:pfam12796 79 LLLEKGADINVK 90
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
531-710 |
1.28e-15 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 81.84 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 531 DVLMETSGTDmlndsDNRATISPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPLDLAAFKGHVECVDVLINQGASIL 610
Cdd:PLN03192 511 DLLGDNGGEH-----DDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVH 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 611 VKDyILKRTPIHAAATNGHSECLRLLIGNA---EPQNAVDIqdgngqtpLMLSVLNGHTDCVYSLLNKGANVDAKDKWGR 687
Cdd:PLN03192 586 IRD-ANGNTALWNAISAKHHKIFRILYHFAsisDPHAAGDL--------LCTAAKRNDLTAMKELLKQGLNVDSEDHQGA 656
|
170 180
....*....|....*....|...
gi 1953334639 688 TALHRGAVTGHEECVDALLQHGA 710
Cdd:PLN03192 657 TALQVAMAEDHVDMVRLLIMNGA 679
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
18-220 |
2.08e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 80.88 E-value: 2.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 18 NG-DPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLG-DAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQVLLK 95
Cdd:PHA02876 317 NGyDTENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLD 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 96 HSADVNARDKNWQTPLHIA-AANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSG-HGEMVKLLLSRGANINAFDKKD 173
Cdd:PHA02876 397 YGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQN 476
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1953334639 174 RRAIHWAayMGHIEVVKLLVAHGAEVtcKDKKSytpLHAAASSGMIS 220
Cdd:PHA02876 477 QYPLLIA--LEYHGIVNILLHYGAEL--RDSRV---LHKSLNDNMFS 516
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
760-853 |
2.33e-15 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 72.46 E-value: 2.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 760 LHWACYNGHETCVELLLEQEV-FQKTEGNAFSPLHCAVINDNEGAAEMLIDTLGASIVNatdsKGRTPLHAAAFTDHVEC 838
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGAdANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD----NGRTALHYAARSGHLEI 76
|
90
....*....|....*
gi 1953334639 839 LQLLLSHNAQVNSID 853
Cdd:pfam12796 77 VKLLLEKGADINVKD 91
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
24-195 |
2.34e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 79.92 E-value: 2.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 24 VRALIFKKEDVNFQDNEK-RTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQVLLKHSADVNA 102
Cdd:PHA02878 150 TKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 103 RDKNWQTPLHIAAAnkAVKCAEALVPLL---SNVNV-SDRAGRTALHHAAFSghGEMVKLLLSRGANINAFDKKDRRAIH 178
Cdd:PHA02878 230 RDKCGNTPLHISVG--YCKDYDILKLLLehgVDVNAkSYILGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLS 305
|
170
....*....|....*....
gi 1953334639 179 WAA--YMGhIEVVKLLVAH 195
Cdd:PHA02878 306 SAVkqYLC-INIGRILISN 323
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
42-301 |
2.36e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 79.65 E-value: 2.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 42 RTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQVLLKHSADVNARDKNWQTPLHIAAANKAVK 121
Cdd:PHA02875 3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 122 CAEALvpLLSNVNVSD---RAGRTALHHAAFSGHGEMVKLLLSRGANinafdkkdrraihwaaymghievvkllvahgAE 198
Cdd:PHA02875 83 AVEEL--LDLGKFADDvfyKDGMTPLHLATILKKLDIMKLLIARGAD-------------------------------PD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 199 VTCKDKksYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGANVNQKNEKGFTPLHF 278
Cdd:PHA02875 130 IPNTDK--FSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALC 207
|
250 260
....*....|....*....|...
gi 1953334639 279 AAASTHGALCLELLVGNGADVNM 301
Cdd:PHA02875 208 YAIENNKIDIVRLFIKRGADCNI 230
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
55-310 |
3.79e-15 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 79.49 E-value: 3.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 55 EIIELLILSGARVNAKDSKWLTPLHRAVASCSE-----EAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPL 129
Cdd:PHA02798 52 DIVKLFINLGANVNGLDNEYSTPLCTILSNIKDykhmlDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLFM 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 130 LSN---VNVSDRAGRTALHHAAFSGHG---EMVKLLLSRGANINAFDkkdrraiHWAAYmghievvkllvahgAEVTCKD 203
Cdd:PHA02798 132 IENgadTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDINTHN-------NKEKY--------------DTLHCYF 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 204 KKSYTPLHAaassgmiSVVKYLLDLGVDMNEPNAYGNTP----LHVACYNGQDVVVN--ELIDCGANVNQKNEKGFTPLH 277
Cdd:PHA02798 191 KYNIDRIDA-------DILKLFVDNGFIINKENKSHKKKfmeyLNSLLYDNKRFKKNilDFIFSYIDINQVDELGFNPLY 263
|
250 260 270
....*....|....*....|....*....|...
gi 1953334639 278 FAAASTHGALClELLVGNGADVNMKSKDGKTPL 310
Cdd:PHA02798 264 YSVSHNNRKIF-EYLLQLGGDINIITELGNTCL 295
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
30-201 |
5.67e-15 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 79.91 E-value: 5.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 30 KKEDVNFQDNEKRTPLHAAAYL------GDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQVLLKHSADVNAR 103
Cdd:PLN03192 508 NVGDLLGDNGGEHDDPNMASNLltvastGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIR 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 104 DKNWQTPLHIAAANKAVKCAEALVPLLSnvnVSD-RAGRTALHHAAFSGHGEMVKLLLSRGANINAFDKKDRRAIHWAAY 182
Cdd:PLN03192 588 DANGNTALWNAISAKHHKIFRILYHFAS---ISDpHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMA 664
|
170
....*....|....*....
gi 1953334639 183 MGHIEVVKLLVAHGAEVTC 201
Cdd:PLN03192 665 EDHVDMVRLLIMNGADVDK 683
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
209-523 |
5.70e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 78.77 E-value: 5.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 209 PLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYN----GQDVVVNELIDCGA--------------NVN---- 266
Cdd:PHA02878 40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEpnklGMKEMIRSINKCSVfytlvaikdafnnrNVEifki 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 267 -----QKNEKGFTPLHFAAASTHGAL---CLELLVGNGADVNMKSKD-GKTPLHMTALHGRFSRSQTIIQSGAVIDCEDK 337
Cdd:PHA02878 120 iltnrYKNIQTIDLVYIDKKSKDDIIeaeITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDK 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 338 NGNTPLHIAARYGHELLINTLITSGADTAKRGIHGMFPLHLAALSGFS-DCCRKLLSSGFDIDTpddfgrtclhaaaagg 416
Cdd:PHA02878 200 TNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDyDILKLLLEHGVDVNA---------------- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 417 nleclnlllntgadfnKKDKFGRSPLHYAAAncNYQCLFALVGSGASVNDLDERGCTPLHYAATSDTDGKCLEYL----- 491
Cdd:PHA02878 264 ----------------KSYILGLTALHSSIK--SERKLKLLLEYGADINSLNSYKLTPLSSAVKQYLCINIGRILisnic 325
|
330 340 350
....*....|....*....|....*....|..
gi 1953334639 492 LRNDANPGIRDKQGYnAVHYSAAYGHRLCLQL 523
Cdd:PHA02878 326 LLKRIKPDIKNSEGF-IDNMDCITSNKRLNQI 356
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
772-958 |
8.47e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 77.78 E-value: 8.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 772 VELLLEQ--EVFQKTEGNaFSPLH-----CAVINDNEGAAEMLIDtLGASIvNATDSKGRTPLHAAAFT--DHVECLQLL 842
Cdd:PHA03100 51 VKILLDNgaDINSSTKNN-STPLHylsniKYNLTDVKEIVKLLLE-YGANV-NAPDNNGITPLLYAISKksNSYSIVEYL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 843 LSHNAQVNSIDSSGKTPLMMAAENG------------------QTNTVEMLVSSASaDLTLQDNSKNTALHLACSKGHET 904
Cdd:PHA03100 128 LDNGANVNIKNSDGENLLHLYLESNkidlkilkllidkgvdinAKNRVNYLLSYGV-PINIKDVYGFTPLHYAVYNNNPE 206
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1953334639 905 SALLILEKITDRNLINATNaalQTPLHVAARNGLTMVVQELLGKGASVLAVDEN 958
Cdd:PHA03100 207 FVKYLLDLGANPNLVNKYG---DTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
427-684 |
1.94e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 76.63 E-value: 1.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 427 TGADFNKKDKFGRSPLHYAA-----ANCNYQCLFALVGSGASVNDLDERGCTPLHYAATSD-TDGKCLEYLLRNDANPGI 500
Cdd:PHA03100 57 NGADINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKKsNSYSIVEYLLDNGANVNI 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 501 RDKQGYNAVHYSAAYGHRlclqliasETPLDVLMETSGTDMlnDSDNRatisplhlaayhghhqaLEVLVQSLLDLDVRN 580
Cdd:PHA03100 137 KNSDGENLLHLYLESNKI--------DLKILKLLIDKGVDI--NAKNR-----------------VNYLLSYGVPINIKD 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 581 SSGRTPLDLAAFKGHVECVDVLINQGASIlvkdyilkrtpihaaatnghseclrllignaepqNAVDIqdgNGQTPLMLS 660
Cdd:PHA03100 190 VYGFTPLHYAVYNNNPEFVKYLLDLGANP----------------------------------NLVNK---YGDTPLHIA 232
|
250 260
....*....|....*....|....
gi 1953334639 661 VLNGHTDCVYSLLNKGANVDAKDK 684
Cdd:PHA03100 233 ILNNNKEIFKLLLNNGPSIKTIIE 256
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
17-168 |
3.54e-14 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 76.22 E-value: 3.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 17 FNGDPDEVRALIFKKEDVNFQDNEKRTPLHaaAYLG----DAEIIELLILSGARVNAKDSKWLTPLH------RAVASCS 86
Cdd:PHA03095 128 FNINPKVIRLLLRKGADVNALDLYGMTPLA--VLLKsrnaNVELLRLLIDAGADVYAVDDRFRSLLHhhlqsfKPRARIV 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 87 EEavqvLLKHSADVNARDKNWQTPLHIAAANKAVKcAEALVPLLSN---VNVSDRAGRTALHHAAFSGHGEMVKLLLSRG 163
Cdd:PHA03095 206 RE----LIRAGCDPAATDMLGNTPLHSMATGSSCK-RSLVLPLLIAgisINARNRYGQTPLHYAAVFNNPRACRRLIALG 280
|
....*
gi 1953334639 164 ANINA 168
Cdd:PHA03095 281 ADINA 285
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
74-259 |
7.24e-14 |
|
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: 75.82 E-value: 7.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 74 WLTPLHRAVASCSEEAVQVLLK-HSADVNARDKNWQTPLHIAAANKAVKCAEAL---VPLLSNVNV-SD-RAGRTALHHA 147
Cdd:cd22192 17 SESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLmeaAPELVNEPMtSDlYQGETALHIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 148 AFSGHGEMVKLLLSRGANIN-------AFDKKDRRAIHW-------AAYMGHIEVVKLLVAHGAEVTCKDKKSYTPLHAA 213
Cdd:cd22192 97 VVNQNLNLVRELIARGADVVspratgtFFRPGPKNLIYYgehplsfAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHIL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1953334639 214 ASSGMISVVKYLLDLGVDMNE----------PNAYGNTPLHVACYNGQDVVVNELI 259
Cdd:cd22192 177 VLQPNKTFACQMYDLILSYDKeddlqpldlvPNNQGLTPFKLAAKEGNIVMFQHLV 232
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
655-885 |
7.34e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 75.09 E-value: 7.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 655 TPLMLSVLNGHT-----DCVYSLLNKGANVDAKDKWGRTALHRGAVT--GHEECVDALLQHGAKCLFRDSRGRTPIHLSA 727
Cdd:PHA03100 70 TPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 728 ACGHI--GVLGALLQSAASVDAnpaiadnhgytalhwacynghETCVELLLEQEV-FQKTEGNAFSPLHCAVINDNEGAA 804
Cdd:PHA03100 150 ESNKIdlKILKLLIDKGVDINA---------------------KNRVNYLLSYGVpINIKDVYGFTPLHYAVYNNNPEFV 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 805 EMLIDtLGASIvNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSIDSSgktpLMMAAEN--GQTNTVEMLVSSASAD 882
Cdd:PHA03100 209 KYLLD-LGANP-NLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET----LLYFKDKdlNTITKIKMLKKSIMYM 282
|
...
gi 1953334639 883 LTL 885
Cdd:PHA03100 283 FLL 285
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
309-603 |
1.34e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 74.53 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 309 PLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGHELLINTLITS----GADTAKRGIHGMFplHLAALSGF 384
Cdd:PHA02878 40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSinkcSVFYTLVAIKDAF--NNRNVEIF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 385 sdccRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGADFNKKDK-FGRSPLHYAAANCNYQCLFALVGSGAS 463
Cdd:PHA02878 118 ----KIILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGAN 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 464 VNDLDERGCTPLHYaATSDTDGKCLEYLLRNDANPGIRDKQGYNAVHYSAAYghrlclqlIASETPLDVLMEtSGTDmLN 543
Cdd:PHA02878 194 VNIPDKTNNSPLHH-AVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGY--------CKDYDILKLLLE-HGVD-VN 262
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953334639 544 DSDNRATISPLHLAAYhgHHQALEVLVQSLLDLDVRNSSGRTPLDLAAFKGH-VECVDVLI 603
Cdd:PHA02878 263 AKSYILGLTALHSSIK--SERKLKLLLEYGADINSLNSYKLTPLSSAVKQYLcINIGRILI 321
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
18-168 |
2.07e-13 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 73.91 E-value: 2.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 18 NGDPDEVRALIFKKEDVNFQDNEKRTPLH--AAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQV--L 93
Cdd:PHA03095 164 NANVELLRLLIDAGADVYAVDDRFRSLLHhhLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpL 243
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953334639 94 LKHSADVNARDKNWQTPLHIAAA-NKAVKCAEaLVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLLSRGANINA 168
Cdd:PHA03095 244 LIAGISINARNRYGQTPLHYAAVfNNPRACRR-LIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAET 318
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
860-956 |
3.38e-13 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 66.29 E-value: 3.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 860 LMMAAENGQTNTVEMLVSSaSADLTLQDNSKNTALHLACSKGHETSALLILEKItDRNLINATNaalqTPLHVAARNGLT 939
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLEN-GADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKDNGR----TALHYAARSGHL 74
|
90
....*....|....*..
gi 1953334639 940 MVVQELLGKGASVLAVD 956
Cdd:pfam12796 75 EIVKLLLEKGADINVKD 91
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
791-969 |
4.40e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 72.39 E-value: 4.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 791 PLHCAVINDNEGAAEMLIDTlGASIvNATDSKGRTPLH-----AAAFTDHVECLQLLLSHNAQVNSIDSSGKTPLMMAAE 865
Cdd:PHA03100 38 PLYLAKEARNIDVVKILLDN-GADI-NSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAIS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 866 N--GQTNTVEMLVSSAsADLTLQDNSKNTALHLACSKGHETSAL--LILEKITDRNL-------------INATNAALQT 928
Cdd:PHA03100 116 KksNSYSIVEYLLDNG-ANVNIKNSDGENLLHLYLESNKIDLKIlkLLIDKGVDINAknrvnyllsygvpINIKDVYGFT 194
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1953334639 929 PLHVAARNGLTMVVQELLGKGASVLAVDENGYTPA-LACAPN 969
Cdd:PHA03100 195 PLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLhIAILNN 236
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
600-952 |
4.65e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 73.56 E-value: 4.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 600 DVLINQGASILVKDyILKRTPIHAAATNGHSECLRLLIGNAEPQNAVDIqdgNGQTPLMLSVLNGHTDCVYSLLNKGANV 679
Cdd:PHA02876 162 EMLLEGGADVNAKD-IYCITPIHYAAERGNAKMVNLLLSYGADVNIIAL---DDLSVLECAVDSKNIDTIKAIIDNRSNI 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 680 DAKDkwgrTALHRGAVTGHEECVDALLQHGAKCLFRDSRGRTPIHLSAACGHIGVL-GALLQSAASVDANpaiaDNHGYT 758
Cdd:PHA02876 238 NKND----LSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLvPKLLERGADVNAK----NIKGET 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 759 ALHWACYNGHET--CVELLLEQEVFQKTEGNAFSPLHCAVINDNEGAAEMLIDTLGASiVNATDSKGRTPLHAAAFTDHV 836
Cdd:PHA02876 310 PLYLMAKNGYDTenIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVITLLELGAN-VNARDYCDKTPIHYAAVRNNV 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 837 ECLQLLLSHNAQVNSIDSSGKTPLMMAAENGQTNTVEMLVSSASADLTLQDNSKNTALHLACSKGHETSAL-LILEKITD 915
Cdd:PHA02876 389 VIINTLLDYGADIEALSQKIGTALHFALCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKLDVIeMLLDNGAD 468
|
330 340 350
....*....|....*....|....*....|....*..
gi 1953334639 916 RNLINATNaalQTPLHVAArnGLTMVVQELLGKGASV 952
Cdd:PHA02876 469 VNAINIQN---QYPLLIAL--EYHGIVNILLHYGAEL 500
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
703-957 |
7.57e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 72.79 E-value: 7.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 703 DALLQHGAKCLFRDSRGRTPIHLSAACGHIGVLGALLQSAASVDanpaIADNHGYTALHWACYNGHETCVELLLEQEvfQ 782
Cdd:PHA02876 162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVN----IIALDDLSVLECAVDSKNIDTIKAIIDNR--S 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 783 KTEGNAFSPLHcAVINDNEGAAEMLIDTlGASiVNATDSKGRTPLHAAAFTDHVECL-QLLLSHNAQVNSIDSSGKTPLM 861
Cdd:PHA02876 236 NINKNDLSLLK-AIRNEDLETSLLLYDA-GFS-VNSIDDCKNTPLHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLY 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 862 MAAENG-QTNTVEMLVSSAsADLTLQDNSKNTALHLACSKGHETSALLILEKITDRnlINATNAALQTPLHVAARNGLTM 940
Cdd:PHA02876 313 LMAKNGyDTENIRTLIMLG-ADVNAADRLYITPLHQASTLDRNKDIVITLLELGAN--VNARDYCDKTPIHYAAVRNNVV 389
|
250
....*....|....*..
gi 1953334639 941 VVQELLGKGASVLAVDE 957
Cdd:PHA02876 390 IINTLLDYGADIEALSQ 406
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
310-402 |
9.39e-13 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 64.75 E-value: 9.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 310 LHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGHELLINTLITSGAdtAKRGIHGMFPLHLAALSGFSDCCR 389
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1953334639 390 KLLSSGFDIDTPD 402
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
213-397 |
1.26e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 71.18 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 213 AASSGMISVVKYLLDLGVDMN--------------------------EPNAYGN-------TPLHVACYNGQDVVVNELI 259
Cdd:PHA02875 9 AILFGELDIARRLLDIGINPNfeiydgispiklamkfrdseaikllmKHGAIPDvkypdieSELHDAVEEGDVKAVEELL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 260 DCGANVNQK-NEKGFTPLHFAAASTHGALcLELLVGNGADVNMKSKDGKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKN 338
Cdd:PHA02875 89 DLGKFADDVfYKDGMTPLHLATILKKLDI-MKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCC 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 339 GNTPLHIAARYGHELLINTLITSGADTAKRGIHGMFPLHLAALSGFS-DCCRKLLSSGFD 397
Cdd:PHA02875 168 GCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKiDIVRLFIKRGAD 227
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
186-412 |
1.48e-12 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 71.40 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 186 IEVVKLLVAHGAEVTCKDKKSYTPLHAAASS-----GMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGqdvVVNEL-- 258
Cdd:PHA02798 51 TDIVKLFINLGANVNGLDNEYSTPLCTILSNikdykHMLDIVKILIENGADINKKNSDGETPLYCLLSNG---YINNLei 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 259 ----IDCGANVNQKNEKGFTPLHFAAASTHGAL--CLELLVGNGADVNMKSKDGKtplhMTALHGRFSRS---------Q 323
Cdd:PHA02798 128 llfmIENGADTTLLDKDGFTMLQVYLQSNHHIDieIIKLLLEKGVDINTHNNKEK----YDTLHCYFKYNidridadilK 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 324 TIIQSGAVIDCEDKNGNTPLhiaARYGHELLINT---------LITSGADTAKRGIHGMFPLHLAALSGFSDCCRKLLSS 394
Cdd:PHA02798 204 LFVDNGFIINKENKSHKKKF---MEYLNSLLYDNkrfkknildFIFSYIDINQVDELGFNPLYYSVSHNNRKIFEYLLQL 280
|
250
....*....|....*...
gi 1953334639 395 GFDIDTPDDFGRTCLHAA 412
Cdd:PHA02798 281 GGDINIITELGNTCLFTA 298
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
537-723 |
1.92e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 70.76 E-value: 1.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 537 SGTDMlnDSDNRATISPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPLDLAAFKGHVECVDVLINQGASILVKDYIL 616
Cdd:PHA02874 113 CGIDV--NIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNG 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 617 KrTPIHAAATNGHSECLRLLIGNAepqNAVDIQDGNGQTPLMLSVLngHTDCVYSLLNKGANVDAKDKWGRTALHRG-AV 695
Cdd:PHA02874 191 E-SPLHNAAEYGDYACIKLLIDHG---NHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAiNP 264
|
170 180
....*....|....*....|....*...
gi 1953334639 696 TGHEECVDALLQHGAKCLFRDSRGRTPI 723
Cdd:PHA02874 265 PCDIDIIDILLYHKADISIKDNKGENPI 292
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
612-879 |
2.34e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 70.08 E-value: 2.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 612 KDYILKRTPIHAAATNGHseclrllignaepqnAVDIQDGNGQTPLMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALH 691
Cdd:PHA03100 9 KSRIIKVKNIKYIIMEDD---------------LNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 692 RGAVTGHE-----ECVDALLQHGAKCLFRDSRGRTPIHLSAAC--GHIGVLGALLQSAASVDanpaIADNHGYTALHWA- 763
Cdd:PHA03100 74 YLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVN----IKNSDGENLLHLYl 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 764 --CYNGHETcVELLLEqevfqktegnafsplHCAVINdNEGAAEMLIdTLGASIvNATDSKGRTPLHAAAFTDHVECLQL 841
Cdd:PHA03100 150 esNKIDLKI-LKLLID---------------KGVDIN-AKNRVNYLL-SYGVPI-NIKDVYGFTPLHYAVYNNNPEFVKY 210
|
250 260 270
....*....|....*....|....*....|....*...
gi 1953334639 842 LLSHNAQVNSIDSSGKTPLMMAAENGQTNTVEMLVSSA 879
Cdd:PHA03100 211 LLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNG 248
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
376-468 |
3.03e-12 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 63.60 E-value: 3.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 376 LHLAALSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTgADFNKKDKfGRSPLHYAAANCNYQCLF 455
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1953334639 456 ALVGSGASVNDLD 468
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
243-336 |
6.79e-12 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 62.44 E-value: 6.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 243 LHVACYNGQDVVVNELIDCGANVNQKNEKGFTPLHFAAASTHGALCLELLvgNGADVNMKSkDGKTPLHMTALHGRFSRS 322
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL--EHADVNLKD-NGRTALHYAARSGHLEIV 77
|
90
....*....|....
gi 1953334639 323 QTIIQSGAVIDCED 336
Cdd:pfam12796 78 KLLLEKGADINVKD 91
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
542-777 |
8.87e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 68.75 E-value: 8.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 542 LNDSDNRATiSPLHLAAYHGHHQALEVLVQSLLDLDVRNSsgRTPLDLAAFKGHVECVD-VLINQGASILVKDYILKRTP 620
Cdd:PHA02878 63 VNQPDHRDL-TPLHIICKEPNKLGMKEMIRSINKCSVFYT--LVAIKDAFNNRNVEIFKiILTNRYKNIQTIDLVYIDKK 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 621 IHAAATNghSECLRLLIGNAEPQNAVDIQDGNgqTPLMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEE 700
Cdd:PHA02878 140 SKDDIIE--AEITKLLLSYGADINMKDRHKGN--TALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKP 215
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953334639 701 CVDALLQHGAKCLFRDSRGRTPIHLSAA-CGHIGVLGALLQSAASVDANPAIAdnhGYTALHWACYNghETCVELLLE 777
Cdd:PHA02878 216 IVHILLENGASTDARDKCGNTPLHISVGyCKDYDILKLLLEHGVDVNAKSYIL---GLTALHSSIKS--ERKLKLLLE 288
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
140-193 |
9.67e-12 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 60.75 E-value: 9.67e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1953334639 140 GRTALHHAAFSGHGEMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLV 193
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
276-364 |
1.45e-11 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 61.67 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 276 LHFAAASTHgALCLELLVGNGADVNMKSKDGKTPLHMTALHGRFSRSQTIIQSgAVIDCEDkNGNTPLHIAARYGHELLI 355
Cdd:pfam12796 1 LHLAAKNGN-LELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77
|
....*....
gi 1953334639 356 NTLITSGAD 364
Cdd:pfam12796 78 KLLLEKGAD 86
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
174-226 |
4.03e-11 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 59.21 E-value: 4.03e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1953334639 174 RRAIHWAAYMGHIEVVKLLVAHGAEVTCKDKKSYTPLHAAASSGMISVVKYLL 226
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
629-838 |
4.98e-11 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 66.82 E-value: 4.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 629 HSECLRLLIGNAEPQNAVDIQDGNGQTPLMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQH 708
Cdd:PLN03192 501 HKELHDLNVGDLLGDNGGEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKH 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 709 GAKCLFRDSRGRTPIHLSAACGH-------------------------------IGVLGALLQSAASVDANpaiaDNHGY 757
Cdd:PLN03192 581 ACNVHIRDANGNTALWNAISAKHhkifrilyhfasisdphaagdllctaakrndLTAMKELLKQGLNVDSE----DHQGA 656
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 758 TALHWACYNGHETCVELLLEQ--EVFQKTEGNAFSPLHC-AVINDNE-GAAEMLIDTLGASIVNATDSKGRTPLHAAAFT 833
Cdd:PLN03192 657 TALQVAMAEDHVDMVRLLIMNgaDVDKANTDDDFSPTELrELLQKRElGHSITIVDSVPADEPDLGRDGGSRPGRLQGTS 736
|
....*
gi 1953334639 834 DHVEC 838
Cdd:PLN03192 737 SDNQC 741
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
670-969 |
5.98e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 66.63 E-value: 5.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 670 YSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQHGAKCLF-RDSRGRTPIHLsaacghIGVLGALLQSAASVDAN 748
Cdd:PHA02876 25 YDLHKHGANQCENESIPFTAIHQALQLRQIDIVEEIIQQNPELIYiTDHKCHSTLHT------ICIIPNVMDIVISLTLD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 749 PAIADNHGYTALHWACYNGHETCVELLleqevfqkTEGNAFSPLHCAVIN---------------DNEGAAEMLIDtlGA 813
Cdd:PHA02876 99 CDIILDIKYASIILNKHKLDEACIHIL--------KEAISGNDIHYDKINesieymklikeriqqDELLIAEMLLE--GG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 814 SIVNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSIDSSGKTPLMMAAENGQTNTVEMLVSSAS----ADLTLQDNS 889
Cdd:PHA02876 169 ADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSninkNDLSLLKAI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 890 KNTALhlacskghETSALLILEKITdrnlINATNAALQTPLHVAARN-GLTMVVQELLGKGASVLAVDENGYTPALACAP 968
Cdd:PHA02876 249 RNEDL--------ETSLLLYDAGFS----VNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKGETPLYLMAK 316
|
.
gi 1953334639 969 N 969
Cdd:PHA02876 317 N 317
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
391-745 |
9.02e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 65.86 E-value: 9.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 391 LLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGADFNKKDKFGRSPLHYAAANCNYQCLFALV------------ 458
Cdd:PHA02876 164 LLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIdnrsninkndls 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 459 -----------------GSGASVNDLDERGCTPLHYAATSDTDGKCLEYLLRNDANPGIRDKQGynavhysaayghrlcl 521
Cdd:PHA02876 244 llkairnedletslllyDAGFSVNSIDDCKNTPLHHASQAPSLSRLVPKLLERGADVNAKNIKG---------------- 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 522 qliasETPLdVLMETSGTDMLNdsdnratisplhlaayhghhqaLEVLVQSLLDLDVRNSSGRTPLDLAA-FKGHVECVD 600
Cdd:PHA02876 308 -----ETPL-YLMAKNGYDTEN----------------------IRTLIMLGADVNAADRLYITPLHQAStLDRNKDIVI 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 601 VLINQGASILVKDYiLKRTPIHAAATNGHSECLRLLIGNAEPQNAVDIQDGN-------GQTPLMlsvlnghtdCVYSLL 673
Cdd:PHA02876 360 TLLELGANVNARDY-CDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTalhfalcGTNPYM---------SVKTLI 429
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953334639 674 NKGANVDAKDKWGRTALHRGAVTGHE-ECVDALLQHGAKCLFRDSRGRTPihLSAACGHIGVLGALLQSAASV 745
Cdd:PHA02876 430 DRGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAINIQNQYP--LLIALEYHGIVNILLHYGAEL 500
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
552-603 |
1.70e-10 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 57.28 E-value: 1.70e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1953334639 552 SPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPLDLAAFKGHVECVDVLI 603
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02989 |
PHA02989 |
ankyrin repeat protein; Provisional |
55-327 |
1.77e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222954 [Multi-domain] Cd Length: 494 Bit Score: 64.76 E-value: 1.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 55 EIIELLILSGARVNAKdSKWLTPL-----HRAVASCS-EEAVQVLLKHSADVNARDKNWQTPlhiaaankavkcaeaLVP 128
Cdd:PHA02989 51 KIVKLLIDNGADVNYK-GYIETPLcavlrNREITSNKiKKIVKLLLKFGADINLKTFNGVSP---------------IVC 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 129 LLSNVNVSDRagrtalhhaafsghgEMVKLLLSRGANINafDKKDRRA-----IHWAAYMGHIEVVKLLVAHGaeVTCKD 203
Cdd:PHA02989 115 FIYNSNINNC---------------DMLRFLLSKGINVN--DVKNSRGynllhMYLESFSVKKDVIKILLSFG--VNLFE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 204 KKSY---TPLHAAASSGM----ISVVKYLLDLGVDMNEPNAYGNTPL------HVACYNGQDVVVNeLIDCGANVNQKNE 270
Cdd:PHA02989 176 KTSLyglTPMNIYLRNDIdvisIKVIKYLIKKGVNIETNNNGSESVLesfldnNKILSKKEFKVLN-FILKYIKINKKDK 254
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1953334639 271 KGFTPLHFAA-ASTHGALCLELLVGNgaDVNMKSKDGKTPLHMTALHGRFSRSQTIIQ 327
Cdd:PHA02989 255 KGFNPLLISAkVDNYEAFNYLLKLGD--DIYNVSKDGDTVLTYAIKHGNIDMLNRILQ 310
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
540-747 |
1.88e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 64.30 E-value: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 540 DMLNDSDNRATISPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPLDLAAFKGHV-----ECVDVLINQGASILVKDY 614
Cdd:PHA03100 25 DDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 615 IlKRTPIHAAATN--GHSECLRLLIGNAEPQNAVDiqdGNGQTPLMLSVLNGHTDC------------------VYSLLN 674
Cdd:PHA03100 105 N-GITPLLYAISKksNSYSIVEYLLDNGANVNIKN---SDGENLLHLYLESNKIDLkilkllidkgvdinaknrVNYLLS 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953334639 675 KGANVDAKDKWGRTALHRGAVTGHEECVDALLQHGAKCLFRDSRGRTPIHLSAACGHIGVLGALLQSAASVDA 747
Cdd:PHA03100 181 YGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
207-251 |
5.12e-10 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 55.74 E-value: 5.12e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1953334639 207 YTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQ 251
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGN 46
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
442-526 |
5.68e-10 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 57.05 E-value: 5.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 442 LHYAAANCNYQCLFALVGSGASVNDLDERGCTPLHYAATSDTDgKCLEYLLRNdANPGIRDkQGYNAVHYSAAYGHRLCL 521
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHL-EIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77
|
....*
gi 1953334639 522 QLIAS 526
Cdd:pfam12796 78 KLLLE 82
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
254-500 |
7.17e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 62.32 E-value: 7.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 254 VVNELIDCGANVNQKNEKGFTPLHFAAaSTHGALCLELLVGNGADVNMKSKDGKTPLHMTALHGRFSRSQTIIQSGAVI- 332
Cdd:PHA02875 17 IARRLLDIGINPNFEIYDGISPIKLAM-KFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAd 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 333 DCEDKNGNTPLHiaaryghellintlitsgadtakrgihgmfplhLAALSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAA 412
Cdd:PHA02875 96 DVFYKDGMTPLH---------------------------------LATILKKLDIMKLLIARGADPDIPNTDKFSPLHLA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 413 AAGGNLECLNLLLNTGADFNKKDKFGRSPLHYAAANCNYQCLFALVGSGASVNDLDERGCTPLHYAATSDTDGKCLEYLL 492
Cdd:PHA02875 143 VMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFI 222
|
....*...
gi 1953334639 493 RNDANPGI 500
Cdd:PHA02875 223 KRGADCNI 230
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
242-535 |
7.22e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 62.59 E-value: 7.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 242 PLHVACYNGQDVVVNELIDCGANVNQKNEKGFTPLHFAAASTHGALCLELLvgngadvNMKSKDgKTPLHMTALHGRFSR 321
Cdd:PHA02878 40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMI-------RSINKC-SVFYTLVAIKDAFNN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 322 SQTIIQSGAVIDCEDKNGNTPLHIAARYGHELLINTLITsgadtakrgihgmfplhlaalsgfsdccRKLLSSGFDIDTP 401
Cdd:PHA02878 112 RNVEIFKIILTNRYKNIQTIDLVYIDKKSKDDIIEAEIT----------------------------KLLLSYGADINMK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 402 D-DFGRTCLHAAAAGGNLECLNLLLNTGADFNKKDKFGRSPLHYAAANCNYQCLFALVGSGASVNDLDERGCTPLHYAAT 480
Cdd:PHA02878 164 DrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVG 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1953334639 481 SDTDGKCLEYLLRNDANPGIRDK-QGYNAVHYSaayghrlclqlIASETPLDVLME 535
Cdd:PHA02878 244 YCKDYDILKLLLEHGVDVNAKSYiLGLTALHSS-----------IKSERKLKLLLE 288
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
816-976 |
7.52e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 62.29 E-value: 7.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 816 VNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSIDSSGKTPLMMAAENGQTNTVEMLVSSAsADLTLQDNSKNTALH 895
Cdd:PHA02874 117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKG-AYANVKDNNGESPLH 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 896 LACSKGHETSALLILEKITdrNLINATNAALqTPLHVAARNGLTMVvqELLGKGASVLAVDENGYTP---ALACAPNKDV 972
Cdd:PHA02874 196 NAAEYGDYACIKLLIDHGN--HIMNKCKNGF-TPLHNAIIHNRSAI--ELLINNASINDQDIDGSTPlhhAINPPCDIDI 270
|
....
gi 1953334639 973 ADCL 976
Cdd:PHA02874 271 IDIL 274
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
74-127 |
8.86e-10 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 55.36 E-value: 8.86e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1953334639 74 WLTPLHRAVASCSEEAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALV 127
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
475-580 |
9.81e-10 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 56.28 E-value: 9.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 475 LHYAATSDtDGKCLEYLLRNDANPGIRDKQGYNAVHYSAAYGHRLCLQLIASEtpldvlmetsgtDMLNDSDNRATisPL 554
Cdd:pfam12796 1 LHLAAKNG-NLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH------------ADVNLKDNGRT--AL 65
|
90 100
....*....|....*....|....*.
gi 1953334639 555 HLAAYHGHHQALEVLVQSLLDLDVRN 580
Cdd:pfam12796 66 HYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
147-305 |
1.19e-09 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 62.58 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 147 AAFSGHGEMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVAHGAEVTCKDKKSYTPLHAAASSGMISVVKYLL 226
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY 611
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953334639 227 DLGvDMNEPNAYGNTpLHVACYNGQDVVVNELIDCGANVNQKNEKGFTPLHFAAASTHGALcLELLVGNGADVNMKSKD 305
Cdd:PLN03192 612 HFA-SISDPHAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDM-VRLLIMNGADVDKANTD 687
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
49-276 |
1.31e-09 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 61.61 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 49 AYLG----DAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQVLLKHSADVNARDKNWQTPLHIAAAnkavkcae 124
Cdd:PHA02946 43 AYCGikglDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSG-------- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 125 alvpllSNVNVSDRagrtalhhaafsghgemVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVAHGAEVTCKDK 204
Cdd:PHA02946 115 ------TDDEVIER-----------------INLLVQYGAKINNSVDEEGCGPLLACTDPSERVFKKIMSIGFEARIVDK 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953334639 205 --KSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNG-QDVVVNELIDCGANVNQKNEKGFTPL 276
Cdd:PHA02946 172 fgKNHIHRHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCSKTvKNVDIINLLLPSTDVNKQNKFGDSPL 246
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
583-778 |
1.77e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 61.16 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 583 GRTPLDLAAFKGHVECVDVLINQGASILVKdYILKRTPIHAAATNGHSECLRLLIGNAEPQNAVDIQDGNgqTPLMLSVL 662
Cdd:PHA02875 35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVK-YPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGM--TPLHLATI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 663 NGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQHGAKCLFRDSRGRTPIHLSAACGHIGVLGALLQSA 742
Cdd:PHA02875 112 LKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSG 191
|
170 180 190
....*....|....*....|....*....|....*.
gi 1953334639 743 ASVDanpAIADNHGYTALHWACYNGHETCVELLLEQ 778
Cdd:PHA02875 192 ANID---YFGKNGCVAALCYAIENNKIDIVRLFIKR 224
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
585-725 |
2.06e-09 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 61.57 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 585 TPLDLAAFKGHVECVDVLINQGASILVKDYILKRTPIHAAATNGHSECLRLLIGNA-----EPQNAVDIQdgnGQTPLML 659
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAApelvnEPMTSDLYQ---GETALHI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 660 SVLNGHTDCVYSLLNKGANV--------------DAKDKWGRTALHRGAVTGHEECVDALLQHGAKCLFRDSRGRTPIHL 725
Cdd:cd22192 96 AVVNQNLNLVRELIARGADVvspratgtffrpgpKNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
690-962 |
2.12e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 61.05 E-value: 2.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 690 LHRGAVTGHEECVDALLQHGAKCLFRDSRGRTPIHLsaACGHIGVLGA--LLQSAasvdanpaIADNHGYT--ALHWACY 765
Cdd:PHA02878 41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHI--ICKEPNKLGMkeMIRSI--------NKCSVFYTlvAIKDAFN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 766 NGHETCVELLLeqevFQKTEGNAFSPLHCAVINDNEGAAEMLIDTL----GASIVNATDSKGRTPLHAAAFTDHVECLQL 841
Cdd:PHA02878 111 NRNVEIFKIIL----TNRYKNIQTIDLVYIDKKSKDDIIEAEITKLllsyGADINMKDRHKGNTALHYATENKDQRLTEL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 842 LLSHNAQVNSIDSSGKTPLMMAAENGQTNTVEMLVSSAsADLTLQDNSKNTALHLACSKGHETSAL-LILEKITDrnlIN 920
Cdd:PHA02878 187 LLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENG-ASTDARDKCGNTPLHISVGYCKDYDILkLLLEHGVD---VN 262
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1953334639 921 ATNAALQ-TPLHVAARNglTMVVQELLGKGASVLAVDENGYTP 962
Cdd:PHA02878 263 AKSYILGlTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTP 303
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
72-250 |
3.09e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 58.29 E-value: 3.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 72 SKWLTPLHRAVASCSEEAVQvllKHSADVNARDKNWQTPLHIAAANKAV--KCAEALVPLLSNVNVSDRA-GRTALHHAA 148
Cdd:PHA02859 19 YRYCNPLFYYVEKDDIEGVK---KWIKFVNDCNDLYETPIFSCLEKDKVnvEILKFLIENGADVNFKTRDnNLSALHHYL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 149 FSGHG---EMVKLLLSRGANINAFDKKDRRAIHwaAYMGH----IEVVKLLVAHGAEVTCKDKK------SYTPLHAAAS 215
Cdd:PHA02859 96 SFNKNvepEILKILIDSGSSITEEDEDGKNLLH--MYMCNfnvrINVIKLLIDSGVSFLNKDFDnnnilySYILFHSDKK 173
|
170 180 190
....*....|....*....|....*....|....*
gi 1953334639 216 sgmisVVKYLLDLGVDMNEPNAYGNTPLHVACYNG 250
Cdd:PHA02859 174 -----IFDFLTSLGIDINETNKSGYNCYDLIKFRN 203
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
183-374 |
3.81e-09 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 61.04 E-value: 3.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 183 MGHIEVVKLLVAHGAEVTckDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCG 262
Cdd:PLN03192 504 LHDLNVGDLLGDNGGEHD--DPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 263 ANVNQKNEKGFTPLHFAAASTHGALcLELLVGNGADVNMKSkdGKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTP 342
Cdd:PLN03192 582 CNVHIRDANGNTALWNAISAKHHKI-FRILYHFASISDPHA--AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATA 658
|
170 180 190
....*....|....*....|....*....|..
gi 1953334639 343 LHIAARYGHELLINTLITSGADTAKRGIHGMF 374
Cdd:PLN03192 659 LQVAMAEDHVDMVRLLIMNGADVDKANTDDDF 690
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
144-226 |
3.98e-09 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 60.68 E-value: 3.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 144 LHHAAFSGHGEMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVAHGAEVTCKDKKSYTPLHAAASSGMISVVK 223
Cdd:PTZ00322 86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165
|
...
gi 1953334639 224 YLL 226
Cdd:PTZ00322 166 LLS 168
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
208-345 |
5.21e-09 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 60.03 E-value: 5.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 208 TPLHAAASSGMISVVKYLLDL-GVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGAN-VNQKNE----KGFTPLHFAAA 281
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMTsdlyQGETALHIAVV 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953334639 282 STHGALcLELLVGNGADVN---------MKSKD-----GKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHI 345
Cdd:cd22192 99 NQNLNL-VRELIARGADVVspratgtffRPGPKnliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
779-890 |
5.23e-09 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 60.30 E-value: 5.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 779 EVFQKTEGNAFSPLHCAVIND--NEGAAEMLI----------DTLGASIV-------NATDSKGRTPLHAAAFTDHVECL 839
Cdd:PTZ00322 52 EALEATENKDATPDHNLTTEEviDPVVAHMLTvelcqlaasgDAVGARILltggadpNCRDYDGRTPLHIACANGHVQVV 131
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1953334639 840 QLLLSHNAQVNSIDSSGKTPLMMAAENGQTNTVEMLVSSASADLTLQDNSK 890
Cdd:PTZ00322 132 RVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGANAK 182
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
823-876 |
7.86e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 52.66 E-value: 7.86e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1953334639 823 GRTPLHAAAFTDHVECLQLLLSHNAQVNSIDSSGKTPLMMAAENGQTNTVEMLV 876
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
109-160 |
8.34e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 52.66 E-value: 8.34e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1953334639 109 TPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLL 160
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
687-932 |
9.23e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 58.85 E-value: 9.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 687 RTALHRGAVTGHEECVDALLQHGAKCLFRDSRGRTPIHLSAACGHIGVLGALLQSAASVDAN-PAIAdnhgyTALHWACY 765
Cdd:PHA02875 3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKyPDIE-----SELHDAVE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 766 NGHETCVELLLE-----QEVFQKtEGNafSPLHCAVINDNEGAAEMLIDTLGASIVNATDSKgrTPLHAAAFTDHVECLQ 840
Cdd:PHA02875 78 EGDVKAVEELLDlgkfaDDVFYK-DGM--TPLHLATILKKLDIMKLLIARGADPDIPNTDKF--SPLHLAVMMGDIKGIE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 841 LLLSHNAQVNSIDSSGKTPLMMAAENGQTNTVEMLVSSASADLTLQDNSKNTALHLACSKGHETSALLILEKITDRNLIN 920
Cdd:PHA02875 153 LLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGADCNIMF 232
|
250
....*....|..
gi 1953334639 921 ATNAALQTPLHV 932
Cdd:PHA02875 233 MIEGEECTILDM 244
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
22-106 |
1.06e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 58.52 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 22 DEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQVLLKHSADVN 101
Cdd:PHA03100 173 NRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
|
....*
gi 1953334639 102 ARDKN 106
Cdd:PHA03100 253 TIIET 257
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
42-94 |
2.42e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 51.12 E-value: 2.42e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1953334639 42 RTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQVLL 94
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
254-500 |
2.44e-08 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 57.92 E-value: 2.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 254 VVNELIDCGANVNQKNEKGFTPLHFAAAS----THGALCLELLVGNGADVNMKSKDGKTPLHmTALHGRFSRSQTI---- 325
Cdd:PHA02798 53 IVKLFINLGANVNGLDNEYSTPLCTILSNikdyKHMLDIVKILIENGADINKKNSDGETPLY-CLLSNGYINNLEIllfm 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 326 IQSGAVIDCEDKNGNTPLHIAARYGHELLINTLitsgadtakrgihgmfplhlaalsgfsdccRKLLSSGFDIDTPDD-F 404
Cdd:PHA02798 132 IENGADTTLLDKDGFTMLQVYLQSNHHIDIEII------------------------------KLLLEKGVDINTHNNkE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 405 GRTCLHAAAAGGNLECLNLLLN----TGADFNKKDKFGRS-------PLHYAAANCNYQcLFALVGSGASVNDLDERGCT 473
Cdd:PHA02798 182 KYDTLHCYFKYNIDRIDADILKlfvdNGFIINKENKSHKKkfmeylnSLLYDNKRFKKN-ILDFIFSYIDINQVDELGFN 260
|
250 260
....*....|....*....|....*..
gi 1953334639 474 PLHYAATSDTDgKCLEYLLRNDANPGI 500
Cdd:PHA02798 261 PLYYSVSHNNR-KIFEYLLQLGGDINI 286
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
583-637 |
2.47e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 51.12 E-value: 2.47e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1953334639 583 GRTPLDLAAFKGHVECVDVLINQGASILVKDYiLKRTPIHAAATNGHSECLRLLI 637
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDG-NGETALHFAASNGNVEVLKLLL 54
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
820-948 |
2.79e-08 |
|
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: 57.85 E-value: 2.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 820 DSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSIDSS--------------GKTPLMMAAENGQTNTVEMLVSSASADLTL 885
Cdd:cd22194 138 AYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEIVQLLMEKESTDITS 217
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953334639 886 QDNSKNTALHLAC-----SKGHETSAL----LILEKITDRNLINATNAALQTPLHVAARNGLTMVVQELLGK 948
Cdd:cd22194 218 QDSRGNTVLHALVtvaedSKTQNDFVKrmydMILLKSENKNLETIRNNEGLTPLQLAAKMGKAEILKYILSR 289
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
792-962 |
3.48e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 57.28 E-value: 3.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 792 LHCAVINDNEGAAEMLIDtLGASiVNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSIDSSGKTPLMMAAENGQTNT 871
Cdd:PHA02874 128 LHYAIKKGDLESIKMLFE-YGAD-VNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYAC 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 872 VEMLVSSASaDLTLQDNSKNTALHLACSkgHETSALLILekITDRNlINATNAALQTPLHVAARNGLTM-VVQELLGKGA 950
Cdd:PHA02874 206 IKLLIDHGN-HIMNKCKNGFTPLHNAII--HNRSAIELL--INNAS-INDQDIDGSTPLHHAINPPCDIdIIDILLYHKA 279
|
170
....*....|..
gi 1953334639 951 SVLAVDENGYTP 962
Cdd:PHA02874 280 DISIKDNKGENP 291
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
445-693 |
3.67e-08 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 57.57 E-value: 3.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 445 AAANCNYQCLFALVGSGASVNDLDERGCTPLHYAATSDTDgKCLEYLLRNDANPGIRDKQGYNAVHYSAAYGHrlclqli 524
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYE-DCVLVLLKHACNVHIRDANGNTALWNAISAKH------- 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 525 asETPLDVLMETSGTdmlndSDNRATISPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPLDLAAFKGHVECVDVLIN 604
Cdd:PLN03192 604 --HKIFRILYHFASI-----SDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIM 676
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 605 QGASIlvkdyilkrtpIHAAATNGHS-ECLRLLIGNAEPQNAVDIQDGNGQTPLMLSVLNGHTDCvySLLNKGANvdaKD 683
Cdd:PLN03192 677 NGADV-----------DKANTDDDFSpTELRELLQKRELGHSITIVDSVPADEPDLGRDGGSRPG--RLQGTSSD---NQ 740
|
250
....*....|
gi 1953334639 684 KWGRTALHRG 693
Cdd:PLN03192 741 CRPRVSIYKG 750
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
206-364 |
4.09e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 54.83 E-value: 4.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 206 SYT-PLHAAASSGMISVVKYLLDLgvdMNEPNAYGNTPLHvACYNGQDVVVNE---LIDCGANVNQK-NEKGFTPLHFAA 280
Cdd:PHA02859 20 RYCnPLFYYVEKDDIEGVKKWIKF---VNDCNDLYETPIF-SCLEKDKVNVEIlkfLIENGADVNFKtRDNNLSALHHYL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 281 ASTHGAL--CLELLVGNGADVNMKSKDGKTPLH--MTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGHELLI- 355
Cdd:PHA02859 96 SFNKNVEpeILKILIDSGSSITEEDEDGKNLLHmyMCNFNVRINVIKLLIDSGVSFLNKDFDNNNILYSYILFHSDKKIf 175
|
....*....
gi 1953334639 356 NTLITSGAD 364
Cdd:PHA02859 176 DFLTSLGID 184
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
83-161 |
4.47e-08 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 57.22 E-value: 4.47e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953334639 83 ASCSEEAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLLS 161
Cdd:PTZ00322 91 ASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
574-797 |
4.78e-08 |
|
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: 57.40 E-value: 4.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 574 LDLDVRNSSGRTPLDLAAFKG-HVECVDVLINQGASILVKDyilkrTPIHAAATNGH---SECLRLLIGNAE----PQNA 645
Cdd:TIGR00870 43 LNINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAVGD-----TLLHAISLEYVdavEAILLHLLAAFRksgpLELA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 646 VDIQDGN---GQTPLMLSVLNGHTDCVYSLLNKGANVDAKDK--------------WGRTALHRGAVTGHEECVDALLQH 708
Cdd:TIGR00870 118 NDQYTSEftpGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSED 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 709 GAKCLFRDSRGRTPIHLSA------------ACG-HIGVLGALLQSAASVDANpAIADNHGYTALHWACYNGHETCVELL 775
Cdd:TIGR00870 198 PADILTADSLGNTLLHLLVmenefkaeyeelSCQmYNFALSLLDKLRDSKELE-VILNHQGLTPLKLAAKEGRIVLFRLK 276
|
250 260
....*....|....*....|...
gi 1953334639 776 LEQEVFQKT-EGNAFSPLHCAVI 797
Cdd:TIGR00870 277 LAIKYKQKKfVAWPNGQQLLSLY 299
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
279-433 |
6.66e-08 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 56.80 E-value: 6.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 279 AAASTHGALCLELLVGNGADVNMKSKDGKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGHELLINTL 358
Cdd:PLN03192 531 TVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953334639 359 --ITSGADTAKRGIhgmfPLHLAALSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGADFNK 433
Cdd:PLN03192 611 yhFASISDPHAAGD----LLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDK 683
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
817-979 |
7.18e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 56.15 E-value: 7.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 817 NATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSIDSSGKTPLMMAAENGQTNTVEMLVSSAS--ADLTLQDNskNTAL 894
Cdd:PHA02875 29 NFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKfaDDVFYKDG--MTPL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 895 HLAC-SKGHETSALLILEKiTDRNLINATNAalqTPLHVAARNGLTMVVQELLGKGASVLAVDENGYTPALACAPNKDVA 973
Cdd:PHA02875 107 HLATiLKKLDIMKLLIARG-ADPDIPNTDKF---SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIA 182
|
....*.
gi 1953334639 974 DCLALI 979
Cdd:PHA02875 183 ICKMLL 188
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
28-247 |
8.11e-08 |
|
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: 56.63 E-value: 8.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 28 IFKKEDVNFQDNEKrtplhaaAYLGDAEIIELLILSGARVNAK-------DSKWLTPLHRAVA-SCSEEAVQVLLKHSAD 99
Cdd:TIGR00870 6 IVPAEESPLSDEEK-------AFLPAAERGDLASVYRDLEEPKklnincpDRLGRSALFVAAIeNENLELTELLLNLSCR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 100 VNARDknwqTPLHIAAANKAVKCAEALVPLLSN---------VNVSDR----AGRTALHHAAFSGHGEMVKLLLSRGANI 166
Cdd:TIGR00870 79 GAVGD----TLLHAISLEYVDAVEAILLHLLAAfrksgplelANDQYTseftPGITALHLAAHRQNYEIVKLLLERGASV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 167 NA------FDKKDRRA--------IHWAAYMGHIEVVKLLVAHGAEVTCKDKKSYTPLHAAA------------SSGMIS 220
Cdd:TIGR00870 155 PAracgdfFVKSQGVDsfyhgespLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVmenefkaeyeelSCQMYN 234
|
250 260 270
....*....|....*....|....*....|.
gi 1953334639 221 VVKYLLDLGVDMNE----PNAYGNTPLHVAC 247
Cdd:TIGR00870 235 FALSLLDKLRDSKEleviLNHQGLTPLKLAA 265
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
189-261 |
1.10e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 56.06 E-value: 1.10e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953334639 189 VKLLVAHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDC 261
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
|
|
| PHA02716 |
PHA02716 |
CPXV016; CPX019; EVM010; Provisional |
33-261 |
1.10e-07 |
|
CPXV016; CPX019; EVM010; Provisional
Pssm-ID: 165089 [Multi-domain] Cd Length: 764 Bit Score: 56.07 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 33 DVNFQDNEKRTP-LHAaaYLG----DAEIIELLILSGARVNAKDSKWLTPLHRAV--ASCSEEAVQVLLKHSADVNARDK 105
Cdd:PHA02716 168 NLNYVCKKTGYGiLHA--YLGnmyvDIDILEWLCNNGVNVNLQNNHLITPLHTYLitGNVCASVIKKIIELGGDMDMKCV 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 106 NWQTPL--HIAAA-----------------NKAVKCAEAL---VPLLSNVNVS---------------DRAGRTALHHAA 148
Cdd:PHA02716 246 NGMSPImtYIINIdninpeitniyiesldgNKVKNIPMILhsyITLARNIDISvvysflqpgvklhykDSAGRTCLHQYI 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 149 FSGH--GEMVKLLLSRGANINAFDKKDRRAIHwaAYMGHIEVVKLLvahgaevtckDKKSYTPLHaaassgmISVVKYLL 226
Cdd:PHA02716 326 LRHNisTDIIKLLHEYGNDLNEPDNIGNTVLH--TYLSMLSVVNIL----------DPETDNDIR-------LDVIQCLI 386
|
250 260 270
....*....|....*....|....*....|....*
gi 1953334639 227 DLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDC 261
Cdd:PHA02716 387 SLGADITAVNCLGYTPLTSYICTAQNYMYYDIIDC 421
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
730-981 |
1.52e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 55.00 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 730 GHIGVLGALLQSAAsvdaNPAIADNHGYTALHWACYNGHETCVELLLEQEVFQKTEG-NAFSPLHCAVINDNEGAAEMLI 808
Cdd:PHA02875 13 GELDIARRLLDIGI----NPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYpDIESELHDAVEEGDVKAVEELL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 809 DtLGASIVNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSIDSSGKTPLMMAAENGQTNTVEMLVSsasadltlqdn 888
Cdd:PHA02875 89 D-LGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLID----------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 889 skntalHLACskghetsallilekitdrnlINATNAALQTPLHVAARNGLTMVVQELLGKGASVLAVDENGYTPALACAP 968
Cdd:PHA02875 157 ------HKAC--------------------LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAI 210
|
250
....*....|...
gi 1953334639 969 NKDVADCLALILA 981
Cdd:PHA02875 211 ENNKIDIVRLFIK 223
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
686-739 |
2.01e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 48.42 E-value: 2.01e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1953334639 686 GRTALHRGAVTGHEECVDALLQHGAKCLFRDSRGRTPIHLSAACGHIGVLGALL 739
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
652-875 |
2.15e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 54.61 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 652 NGQTPLMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQHGA---KCLFRDsrGRTPIHLSAA 728
Cdd:PHA02875 34 DGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKfadDVFYKD--GMTPLHLATI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 729 CGHIGVLGALLQSAasvdANPAIADNHGYTALHWACYNGHETCVELLLEQEVFQKTE-GNAFSPLHCAVINDNEGAAEML 807
Cdd:PHA02875 112 LKKLDIMKLLIARG----ADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEdCCGCTPLIIAMAKGDIAICKML 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953334639 808 IDTlGASIVNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNsidssgktpLMMAAENGQTNTVEML 875
Cdd:PHA02875 188 LDS-GANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGADCN---------IMFMIEGEECTILDMI 245
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
20-143 |
2.24e-07 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 54.65 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 20 DPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGD--AEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQVLLKHS 97
Cdd:PHA03095 201 RARIVRELIRAGCDPAATDMLGNTPLHSMATGSSckRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALG 280
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1953334639 98 ADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTA 143
Cdd:PHA03095 281 ADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAATLNTA 326
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
438-492 |
2.57e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 48.42 E-value: 2.57e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1953334639 438 GRSPLHYAAANCNYQCLFALVGSGASVNDLDERGCTPLHYAATSDtDGKCLEYLL 492
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNG-NVEVLKLLL 54
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
802-962 |
3.03e-07 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 54.49 E-value: 3.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 802 GAAEMLIDTLGASI-VNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSIDSSGKTPLMMAAENGQTNTVEMLVSSAS 880
Cdd:PLN03192 536 GNAALLEELLKAKLdPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFAS 615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 881 AdltlqdNSKNTALHLACSKGHETSaLLILEKITDRNL-INATNAALQTPLHVAARNGLTMVVQELLGKGASVLAVD-EN 958
Cdd:PLN03192 616 I------SDPHAAGDLLCTAAKRND-LTAMKELLKQGLnVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANtDD 688
|
....
gi 1953334639 959 GYTP 962
Cdd:PLN03192 689 DFSP 692
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
858-952 |
5.27e-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: 53.86 E-value: 5.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 858 TPLMMAAENGQTNTVEMLVSSASADLTLQDNSKNTALHLACSKGHETSALLILEkiTDRNLIN-ATNAAL---QTPLHVA 933
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNePMTSDLyqgETALHIA 96
|
90
....*....|....*....
gi 1953334639 934 ARNGLTMVVQELLGKGASV 952
Cdd:cd22192 97 VVNQNLNLVRELIARGADV 115
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
803-962 |
5.94e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 53.04 E-value: 5.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 803 AAEMLIDTLGaSIVNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSIDSSGKTPLMMAAENGQTNTVEMLVssasad 882
Cdd:PHA02874 16 AIEKIIKNKG-NCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 883 ltlqDNSKNTA-LHLACSKGHETSAllILEKITDrnlINATNAALQTPLHVAARNGLTMVVQELLGKGASVLAVDENGYT 961
Cdd:PHA02874 89 ----DNGVDTSiLPIPCIEKDMIKT--ILDCGID---VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCY 159
|
.
gi 1953334639 962 P 962
Cdd:PHA02874 160 P 160
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
790-843 |
8.02e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 46.88 E-value: 8.02e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1953334639 790 SPLHCAVINDNEGAAEMLIDTlGASIvNATDSKGRTPLHAAAFTDHVECLQLLL 843
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEK-GADI-NAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
281-350 |
1.20e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 52.59 E-value: 1.20e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 281 ASTHGALCLELLVGNGADVNMKSKDGKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYG 350
Cdd:PTZ00322 90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENG 159
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
274-479 |
1.45e-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: 52.32 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 274 TPLhFAAASTHGALCLE-LLVGNGADVNMKSKDGKTPLHMTALHGRFSRSQTIIQSGA-----VIDCEDKNGNTPLHIAA 347
Cdd:cd22192 19 SPL-LLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPelvnePMTSDLYQGETALHIAV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 348 RYGHELLINTLITSGADTAKRGIHGMFplhlaalsgFSDCCRKLLSsgfdidtpddFGRTCLHAAAAGGNLECLNLLLNT 427
Cdd:cd22192 98 VNQNLNLVRELIARGADVVSPRATGTF---------FRPGPKNLIY----------YGEHPLSFAACVGNEEIVRLLIEH 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953334639 428 GADFNKKDKFGRSPLHYAA--ANCNYQC-----LFALVGSGASVNdLD----ERGCTPLHYAA 479
Cdd:cd22192 159 GADIRAQDSLGNTVLHILVlqPNKTFACqmydlILSYDKEDDLQP-LDlvpnNQGLTPFKLAA 220
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
655-706 |
1.61e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 46.11 E-value: 1.61e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1953334639 655 TPLMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDALL 706
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
755-948 |
1.89e-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: 51.94 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 755 HGYTALHWACYNGHETCVELLLEQE---VFQKTEGNAF---SPLHCAVINDNEGAAEMLIDTlGASIVN--ATDS---KG 823
Cdd:cd22192 50 LGETALHVAALYDNLEAAVVLMEAApelVNEPMTSDLYqgeTALHIAVVNQNLNLVRELIAR-GADVVSprATGTffrPG 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 824 RT--------PLHAAAFTDHVECLQLLLSHNAQVNSIDSSGKTPLMMaaengqtntvemlvssasadLTLQDNSKntalh 895
Cdd:cd22192 129 PKnliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI--------------------LVLQPNKT----- 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1953334639 896 LACskgHETSALLILEK-ITDRNLINATNAALQTPLHVAARNGLTMVVQELLGK 948
Cdd:cd22192 184 FAC---QMYDLILSYDKeDDLQPLDLVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
192-246 |
1.90e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 45.80 E-value: 1.90e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1953334639 192 LVAHG-AEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVA 246
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
618-673 |
1.94e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 45.73 E-value: 1.94e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1953334639 618 RTPIHAAATNGHSECLRLLIGNAEPqnaVDIQDGNGQTPLMLSVLNGHTDCVYSLL 673
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGAD---INAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
767-951 |
2.05e-06 |
|
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: 51.80 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 767 GHETCVELLLEQEVFQKTEGNAfSPLHCAVINDNEG---AAEMLIDTLGAS-----IVNA--TDS--KGRTPLHAAAFTD 834
Cdd:cd21882 6 GLLECLRWYLTDSAYQRGATGK-TCLHKAALNLNDGvneAIMLLLEAAPDSgnpkeLVNApcTDEfyQGQTALHIAIENR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 835 HVECLQLLLSHNAQVNSIDSS-------------GKTPLMMAAENGQTNTVEMLVSSAS--ADLTLQDNSKNTALH---L 896
Cdd:cd21882 85 NLNLVRLLVENGADVSARATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAqpAALEAQDSLGNTVLHalvL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953334639 897 ACSKGHETSA--------LLILEKITD--RNLINATNAALQTPLHVAARNGLTMVVQELLGKGAS 951
Cdd:cd21882 165 QADNTPENSAfvcqmynlLLSYGAHLDptQQLEEIPNHQGLTPLKLAAVEGKIVMFQHILQREFS 229
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
258-312 |
2.34e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 45.80 E-value: 2.34e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1953334639 258 LIDCG-ANVNQKNEKGFTPLHFAAasTHGAL-CLELLVGNGADVNMKSKDGKTPLHM 312
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAA--KYGALeIVRVLLAYGVDLNLKDEEGLTALDL 55
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
12-97 |
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 1953334639 12 LVQAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQ 91
Cdd:PTZ00322 86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165
|
....*.
gi 1953334639 92 VLLKHS 97
Cdd:PTZ00322 166 LLSRHS 171
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
190-374 |
3.65e-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: 50.78 E-value: 3.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 190 KLLVAHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDM-NEP---NAY-GNTPLHVACYNGQDVVVNELIDCGAN 264
Cdd:cd22192 35 KLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELvNEPmtsDLYqGETALHIAVVNQNLNLVRELIARGAD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 265 VN---------QKNEK-----GFTPLHFAAASTHGALcLELLVGNGADVNMKSKDGKTPLHMTALhgrfsrsqtiiQSGA 330
Cdd:cd22192 115 VVspratgtffRPGPKnliyyGEHPLSFAACVGNEEI-VRLLIEHGADIRAQDSLGNTVLHILVL-----------QPNK 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953334639 331 VIDCE--------DKNGN-------------TPLHIAARYGHELLINTLITSgadtaKRGIHGMF 374
Cdd:cd22192 183 TFACQmydlilsyDKEDDlqpldlvpnnqglTPFKLAAKEGNIVMFQHLVQK-----RRHIQWTY 242
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
694-776 |
3.96e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 51.05 E-value: 3.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 694 AVTGHEECVDALLQHGAKCLFRDSRGRTPIHLSAACGHIGVLGALLQsaasVDANPAIADNHGYTALHWACYNGHETCVE 773
Cdd:PTZ00322 90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLE----FGADPTLLDKDGKTPLELAEENGFREVVQ 165
|
...
gi 1953334639 774 LLL 776
Cdd:PTZ00322 166 LLS 168
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
140-171 |
5.17e-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: 44.20 E-value: 5.17e-06
10 20 30
....*....|....*....|....*....|...
gi 1953334639 140 GRTALHHAAFS-GHGEMVKLLLSRGANINAFDK 171
Cdd:pfam00023 2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
375-416 |
5.38e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 44.57 E-value: 5.38e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1953334639 375 PLHLAALSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGG 416
Cdd:pfam13637 4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNG 45
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
52-126 |
6.45e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 50.28 E-value: 6.45e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953334639 52 GDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEAL 126
Cdd:PTZ00322 93 GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
214-320 |
7.27e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 49.90 E-value: 7.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 214 ASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGANVNQKNEKGFTPLHFAAASTHGALcLELLV 293
Cdd:PTZ00322 90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREV-VQLLS 168
|
90 100 110
....*....|....*....|....*....|....*...
gi 1953334639 294 GN-------GADVNMKSKDGKTPLH----MTALHGRFS 320
Cdd:PTZ00322 169 RHsqchfelGANAKPDSFTGKPPSLedspISSHHPDFS 206
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
108-259 |
7.60e-06 |
|
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: 49.88 E-value: 7.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 108 QTPLHIAAANKAVKCAEALVPLLSNVNVSDRA--------------GRTALHHAAFSGHGEMVKLLLSRGANINA----- 168
Cdd:cd21882 27 KTCLHKAALNLNDGVNEAIMLLLEAAPDSGNPkelvnapctdefyqGQTALHIAIENRNLNLVRLLVENGADVSAratgr 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 169 -FDKKDRRAIHW-------AAYMGHIEVVKLLVAHGAE---VTCKDKKSYTPLHA---------AASSGMISVVKYLLDL 228
Cdd:cd21882 107 fFRKSPGNLFYFgelplslAACTNQEEIVRLLLENGAQpaaLEAQDSLGNTVLHAlvlqadntpENSAFVCQMYNLLLSY 186
|
170 180 190
....*....|....*....|....*....|....*...
gi 1953334639 229 G------VDMNE-PNAYGNTPLHVACYNGQDVVVNELI 259
Cdd:cd21882 187 GahldptQQLEEiPNHQGLTPLKLAAVEGKIVMFQHIL 224
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
308-359 |
8.05e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 44.19 E-value: 8.05e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1953334639 308 TPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGHELLINTLI 359
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
239-293 |
8.13e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 44.19 E-value: 8.13e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1953334639 239 GNTPLHVACYNGQDVVVNELIDCGANVNQKNEKGFTPLHFAAASTHGAlCLELLV 293
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVE-VLKLLL 54
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
439-657 |
1.05e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 49.22 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 439 RSPLHYAAANCNYQCLFALVGSGASVND-LDERGCTPLHYAaTSDTDGKCLEYLLRNDANPGIrdkqgynavhysaaygh 517
Cdd:PHA02875 69 ESELHDAVEEGDVKAVEELLDLGKFADDvFYKDGMTPLHLA-TILKKLDIMKLLIARGADPDI----------------- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 518 rlclqliasetpldvlmetSGTDmlndsdnraTISPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPLDLAAFKGHVE 597
Cdd:PHA02875 131 -------------------PNTD---------KFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIA 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953334639 598 CVDVLINQGASIlvkDYILKRTPIHA---AATNGHSECLRLLIGNAEPQNAVDIQDGNGQTPL 657
Cdd:PHA02875 183 ICKMLLDSGANI---DYFGKNGCVAAlcyAIENNKIDIVRLFIKRGADCNIMFMIEGEECTIL 242
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
93-147 |
1.06e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 43.87 E-value: 1.06e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1953334639 93 LLKH-SADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHA 147
Cdd:pfam13857 1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
695-869 |
1.26e-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: 49.11 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 695 VTGHEECVDALLQHGAKClfRDSRGRTPIHLSAACGHIGVLGA---LLQSAASVDANPAIADN-------HGYTALHWAC 764
Cdd:cd21882 4 LLGLLECLRWYLTDSAYQ--RGATGKTCLHKAALNLNDGVNEAimlLLEAAPDSGNPKELVNApctdefyQGQTALHIAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 765 YNGHETCVELLLEQ----------EVFQKTEGNAF----SPLHCAVINDNEGAAEMLIDTlGASI--VNATDSKGRTPLH 828
Cdd:cd21882 82 ENRNLNLVRLLVENgadvsaratgRFFRKSPGNLFyfgeLPLSLAACTNQEEIVRLLLEN-GAQPaaLEAQDSLGNTVLH 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1953334639 829 A-----------AAFTDHVecLQLLLSHNAQVNSIDS-------SGKTPLMMAAENGQT 869
Cdd:cd21882 161 AlvlqadntpenSAFVCQM--YNLLLSYGAHLDPTQQleeipnhQGLTPLKLAAVEGKI 217
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
140-168 |
1.83e-05 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 42.19 E-value: 1.83e-05
10 20
....*....|....*....|....*....
gi 1953334639 140 GRTALHHAAFSGHGEMVKLLLSRGANINA 168
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
719-776 |
1.84e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 43.03 E-value: 1.84e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1953334639 719 GRTPIHLSAACGHIGVLGALLQSAASVDAnpaiADNHGYTALHWACYNGHETCVELLL 776
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINA----VDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
724-864 |
1.87e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 48.74 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 724 HLSAACGHIGVLgALLQSAAsvdaNPAIADNHGYTALHWACYNGHETCVELLLEqevfqktegnafsplhcavindnega 803
Cdd:PTZ00322 88 QLAASGDAVGAR-ILLTGGA----DPNCRDYDGRTPLHIACANGHVQVVRVLLE-------------------------- 136
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953334639 804 aemlidtLGASiVNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSIDSSGK-------------TPLMMAA 864
Cdd:PTZ00322 137 -------FGAD-PTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGANAKpdsftgkppsledSPISSHH 202
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
12-61 |
1.97e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 43.03 E-value: 1.97e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1953334639 12 LVQAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLI 61
Cdd:pfam13637 5 LHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
325-404 |
1.97e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 48.74 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 325 IIQSGAVIDCEDKNGNTPLHIAARYGHELLINTLITSGADTAKRGIHGMFPLHLAALSGFSDCCRKLLS---SGFDIDT- 400
Cdd:PTZ00322 101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRhsqCHFELGAn 180
|
....*.
gi 1953334639 401 --PDDF 404
Cdd:PTZ00322 181 akPDSF 186
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
43-180 |
2.16e-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: 48.47 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 43 TPLHAAAYLGDAEIIELLILSGARVNA---------KDSKWLT-----PLHRAVASCSEEAVQVLLKHSADVNARDKNWQ 108
Cdd:cd22192 91 TALHIAVVNQNLNLVRELIARGADVVSpratgtffrPGPKNLIyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGN 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 109 TPLHIAA--ANKAVKCAE-----ALVPLLSNVNVS---DRAGRTALHHAAFSGHGEMVKLLLSRganinafdkkdRRAIH 178
Cdd:cd22192 171 TVLHILVlqPNKTFACQMydlilSYDKEDDLQPLDlvpNNQGLTPFKLAAKEGNIVMFQHLVQK-----------RRHIQ 239
|
..
gi 1953334639 179 WA 180
Cdd:cd22192 240 WT 241
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
473-675 |
2.22e-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: 48.47 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 473 TPLHYAAtSDTDGKCLEYLLR-NDANPGIRDKQGYNAVHYSAAYGHRLCLQLIASETPLDVLMETSgtdmlndSDNRATI 551
Cdd:cd22192 19 SPLLLAA-KENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMT-------SDLYQGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 552 SPLHLAAYHGHhqalEVLVQSLLD--LDVRNSS----------------GRTPLDLAAFKGHVECVDVLINQGASILVKD 613
Cdd:cd22192 91 TALHIAVVNQN----LNLVRELIArgADVVSPRatgtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953334639 614 YiLKRTPIHAAAT--NGHSECLRL-LIGNAEP---QNAVD-IQDGNGQTPLMLSVLNGHTDCVYSLLNK 675
Cdd:cd22192 167 S-LGNTVLHILVLqpNKTFACQMYdLILSYDKeddLQPLDlVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
|
|
| PHA02716 |
PHA02716 |
CPXV016; CPX019; EVM010; Provisional |
254-475 |
2.26e-05 |
|
CPXV016; CPX019; EVM010; Provisional
Pssm-ID: 165089 [Multi-domain] Cd Length: 764 Bit Score: 48.37 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 254 VVNELIDCG-ANVNQK-NEKGFTPLHFAAASTHGAL-CLELLVGNGADVNMKSKDGKTPLHMTALHGRFSRS--QTIIQS 328
Cdd:PHA02716 157 LIKYMVDVGiVNLNYVcKKTGYGILHAYLGNMYVDIdILEWLCNNGVNVNLQNNHLITPLHTYLITGNVCASviKKIIEL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 329 GAVIDCEDKNGNTPLH---IAARYGHELLINTLITSGADTAKRGIHGMFPLHLAALSGFS-DCCRKLLSSGFDIDTPDDF 404
Cdd:PHA02716 237 GGDMDMKCVNGMSPIMtyiINIDNINPEITNIYIESLDGNKVKNIPMILHSYITLARNIDiSVVYSFLQPGVKLHYKDSA 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 405 GRTCLHAAAAGGNLECL--NLLLNTGADFNKKDKFGRSPLHYAAA--------------NCNYQCLFALVGSGASVNDLD 468
Cdd:PHA02716 317 GRTCLHQYILRHNISTDiiKLLHEYGNDLNEPDNIGNTVLHTYLSmlsvvnildpetdnDIRLDVIQCLISLGADITAVN 396
|
....*..
gi 1953334639 469 ERGCTPL 475
Cdd:PHA02716 397 CLGYTPL 403
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
405-458 |
2.30e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 42.65 E-value: 2.30e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1953334639 405 GRTCLHAAAAGGNLECLNLLLNTGADFNKKDKFGRSPLHYAAANCNYQCLFALV 458
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
646-866 |
2.45e-05 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 48.29 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 646 VDIQDGNGQTPL--MLSVL---NGHTDCVYSLLNKGANVDAKDKWGRTA----LHRGAVTgHEECVDALLQHGAKCLFRD 716
Cdd:PHA02798 64 VNGLDNEYSTPLctILSNIkdyKHMLDIVKILIENGADINKKNSDGETPlyclLSNGYIN-NLEILLFMIENGADTTLLD 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 717 SRGRTPIHLSAACGH---IGVLGALLQSAasVDANpAIADNHGYTALHwaCYNGHE------TCVELLLEQ----EVFQK 783
Cdd:PHA02798 143 KDGFTMLQVYLQSNHhidIEIIKLLLEKG--VDIN-THNNKEKYDTLH--CYFKYNidridaDILKLFVDNgfiiNKENK 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 784 TEGNAFSPLHCAVINDNEGAAEMLIDTLGASI-VNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSIDSSGKTPLMM 862
Cdd:PHA02798 218 SHKKKFMEYLNSLLYDNKRFKKNILDFIFSYIdINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFT 297
|
....
gi 1953334639 863 AAEN 866
Cdd:PHA02798 298 AFEN 301
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
625-708 |
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 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 625 ATNGHSECLRLLI-GNAEPqnavDIQDGNGQTPLMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVD 703
Cdd:PTZ00322 90 AASGDAVGARILLtGGADP----NCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165
|
....*
gi 1953334639 704 ALLQH 708
Cdd:PTZ00322 166 LLSRH 170
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
643-691 |
2.59e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 42.72 E-value: 2.59e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1953334639 643 QNAVDIQDGNGQTPLMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALH 691
Cdd:pfam13857 6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
864-959 |
3.46e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 47.97 E-value: 3.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 864 AENGQTNTVEMLVSSAsADLTLQDNSKNTALHLACSKGHETSALLILEKITDRNLINATNaalQTPLHVAARNGLTMVVQ 943
Cdd:PTZ00322 90 AASGDAVGARILLTGG-ADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDG---KTPLELAEENGFREVVQ 165
|
90
....*....|....*.
gi 1953334639 944 ELLGKGASVLAVDENG 959
Cdd:PTZ00322 166 LLSRHSQCHFELGANA 181
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
339-392 |
3.58e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 42.26 E-value: 3.58e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1953334639 339 GNTPLHIAARYGHELLINTLITSGADTAKRGIHGMFPLHLAALSGFSDCCRKLL 392
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
207-442 |
3.66e-05 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 47.36 E-value: 3.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 207 YTPLHAAASSGMISVVKYLLDlgvdMNEPNayGNTP-LHVAC-YNGQDV-VVNELIDCGANVNQKNEKGFTPLHFAAAST 283
Cdd:PHA02946 10 YLSLYAKYNSKNLDVFRNMLQ----AIEPS--GNYHiLHAYCgIKGLDErFVEELLHRGYSPNETDDDGNYPLHIASKIN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 284 HGALcLELLVGNGADVNMKSKDGKTPLHMtaLHGR----FSRSQTIIQSGAVIDCE-DKNGNTPLhIAARYGHELLINTL 358
Cdd:PHA02946 84 NNRI-VAMLLTHGADPNACDKQHKTPLYY--LSGTddevIERINLLVQYGAKINNSvDEEGCGPL-LACTDPSERVFKKI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 359 ITSGADT------AKRGIHgmfpLHLAALSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLN-LLLNTGADF 431
Cdd:PHA02946 160 MSIGFEArivdkfGKNHIH----RHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCSKTVKNVDIiNLLLPSTDV 235
|
250
....*....|.
gi 1953334639 432 NKKDKFGRSPL 442
Cdd:PHA02946 236 NKQNKFGDSPL 246
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
225-279 |
3.77e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 42.33 E-value: 3.77e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1953334639 225 LLDLG-VDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGANVNQKNEKGFTPLHFA 279
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
140-168 |
4.18e-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: 4.18e-05
10 20
....*....|....*....|....*....
gi 1953334639 140 GRTALHHAAFSGHGEMVKLLLSRGANINA 168
Cdd:pfam13606 2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
550-660 |
4.87e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 47.20 E-value: 4.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 550 TISPLHLAAyHGHHQALEVLVQSLLDLDVRNSSGRTPLDLAAFKGHVECVDVLINQGA--SILVKDyilKRTPIHAAATN 627
Cdd:PTZ00322 83 TVELCQLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGAdpTLLDKD---GKTPLELAEEN 158
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1953334639 628 GHSECLRLLIG----------NAEPQNAVDIQDGNGQTPLMLS 660
Cdd:PTZ00322 159 GFREVVQLLSRhsqchfelgaNAKPDSFTGKPPSLEDSPISSH 201
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
112-198 |
5.31e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 47.20 E-value: 5.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 112 HIAAANKAVKcAEALVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKL 191
Cdd:PTZ00322 88 QLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166
|
....*..
gi 1953334639 192 LVAHGAE 198
Cdd:PTZ00322 167 LSRHSQC 173
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
274-320 |
6.09e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 41.49 E-value: 6.09e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1953334639 274 TPLHFAAASTHGAlCLELLVGNGADVNMKSKDGKTPLHMTALHGRFS 320
Cdd:pfam13637 3 TALHAAAASGHLE-LLRLLLEKGADINAVDGNGETALHFAASNGNVE 48
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
234-350 |
6.21e-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: 47.06 E-value: 6.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 234 EPNAYGNTPLHVACYNGQDVVVNELIDCGANVNQK----------NEKGF----TPLHFAAASTHGALcLELLVGNGAD- 298
Cdd:cd22194 136 EEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHakgvffnpkyKHEGFyfgeTPLALAACTNQPEI-VQLLMEKESTd 214
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953334639 299 VNMKSKDGKTPLHMTALHGRFSRSQT--IIQSGAVI--DCEDKN--------GNTPLHIAARYG 350
Cdd:cd22194 215 ITSQDSRGNTVLHALVTVAEDSKTQNdfVKRMYDMIllKSENKNletirnneGLTPLQLAAKMG 278
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
238-266 |
6.30e-05 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 41.03 E-value: 6.30e-05
10 20
....*....|....*....|....*....
gi 1953334639 238 YGNTPLHVACYNGQDVVVNELIDCGANVN 266
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
809-980 |
6.83e-05 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 47.17 E-value: 6.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 809 DTLGASIVNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSIDSSGKTPLMMAAENGQTNTVEMLVSSAsADLTLQDN 888
Cdd:PLN03192 511 DLLGDNGGEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA-CNVHIRDA 589
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 889 SKNTALHLACSKGHETsallILEKITDRNLINATNAALQTPLHVAARNGLTMvVQELLGKGASVLAVDENGYTpALACAP 968
Cdd:PLN03192 590 NGNTALWNAISAKHHK----IFRILYHFASISDPHAAGDLLCTAAKRNDLTA-MKELLKQGLNVDSEDHQGAT-ALQVAM 663
|
170
....*....|..
gi 1953334639 969 NKDVADCLALIL 980
Cdd:PLN03192 664 AEDHVDMVRLLI 675
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
390-510 |
6.87e-05 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 46.59 E-value: 6.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 390 KLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGADFNKKDKFGRSPLHYAAANCN--YQCLFALVGSGASVND- 466
Cdd:PHA02946 57 ELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKINNs 136
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1953334639 467 LDERGCTPLhyAATSDTDGKCLEYLLRNDANPGIRDKQGYNAVH 510
Cdd:PHA02946 137 VDEEGCGPL--LACTDPSERVFKKIMSIGFEARIVDKFGKNHIH 178
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
238-270 |
7.25e-05 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 40.74 E-value: 7.25e-05
10 20 30
....*....|....*....|....*....|....
gi 1953334639 238 YGNTPLHVACY-NGQDVVVNELIDCGANVNQKNE 270
Cdd:pfam00023 1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
378-597 |
9.23e-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: 46.41 E-value: 9.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 378 LAALSGFSDCCRKLLSSgfDIDTPDDFGRTCLHAAA---AGGNLECLNLLLNTGADFNKKDKF-----------GRSPLH 443
Cdd:cd21882 1 LEELLGLLECLRWYLTD--SAYQRGATGKTCLHKAAlnlNDGVNEAIMLLLEAAPDSGNPKELvnapctdefyqGQTALH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 444 YAAANCNYQCLFALVGSGASVND------LDERGCT-------PLHYAATSDTDgKCLEYLLRNDANP---GIRDKQGYN 507
Cdd:cd21882 79 IAIENRNLNLVRLLVENGADVSAratgrfFRKSPGNlfyfgelPLSLAACTNQE-EIVRLLLENGAQPaalEAQDSLGNT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 508 AVHysaayghrlCLQLIASETPLDVLMETSGTDMLndsdnratispLHLAAYHGHHQALEvlvqslldlDVRNSSGRTPL 587
Cdd:cd21882 158 VLH---------ALVLQADNTPENSAFVCQMYNLL-----------LSYGAHLDPTQQLE---------EIPNHQGLTPL 208
|
250
....*....|
gi 1953334639 588 DLAAFKGHVE 597
Cdd:cd21882 209 KLAAVEGKIV 218
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
159-213 |
1.31e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 40.79 E-value: 1.31e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1953334639 159 LLSRG-ANINAFDKKDRRAIHWAAYMGHIEVVKLLVAHGAEVTCKDKKSYTPLHAA 213
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
655-878 |
1.33e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 45.77 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 655 TPLMLSVLNGHTDCVYSLL-NKGANVDAKDKWGRTALHRGAVTGHEECVDALLQhGAKCLFRDS------RGRTPIHLSA 727
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLME-AAPELVNEPmtsdlyQGETALHIAV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 728 ACGHIGVLGALLQSAASVdANPAIAdnhGYtalhwacynghetcvellleqeVFQKTEGNAF----SPLHCAVINDNEGA 803
Cdd:cd22192 98 VNQNLNLVRELIARGADV-VSPRAT---GT----------------------FFRPGPKNLIyygeHPLSFAACVGNEEI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 804 AEMLIDTlGASIVnATDSKGRTPLHAAAF----TDHVECLQLLLSHNAQVNSI------DSSGKTPLMMAAENGQTNTVE 873
Cdd:cd22192 152 VRLLIEH-GADIR-AQDSLGNTVLHILVLqpnkTFACQMYDLILSYDKEDDLQpldlvpNNQGLTPFKLAAKEGNIVMFQ 229
|
....*
gi 1953334639 874 MLVSS 878
Cdd:cd22192 230 HLVQK 234
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
377-493 |
1.42e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 46.04 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 377 HLAALSGFSDccrKLLSSGFDIDTPDDFGRTCLHAA-------AAGGNLECLNLLLNTGADFNKKDKFGRSPLHYAAANC 449
Cdd:PTZ00322 50 HLEALEATEN---KDATPDHNLTTEEVIDPVVAHMLtvelcqlAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANG 126
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1953334639 450 NYQCLFALVGSGASVNDLDERGCTPLHYAATSDTdGKCLEYLLR 493
Cdd:PTZ00322 127 HVQVVRVLLEFGADPTLLDKDGKTPLELAEENGF-REVVQLLSR 169
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
812-863 |
2.15e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 40.02 E-value: 2.15e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1953334639 812 GASIVNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSIDSSGKTPLMMA 863
Cdd:pfam13857 5 GPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
822-853 |
2.29e-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: 39.19 E-value: 2.29e-04
10 20 30
....*....|....*....|....*....|...
gi 1953334639 822 KGRTPLHAAA-FTDHVECLQLLLSHNAQVNSID 853
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
540-590 |
2.61e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 40.02 E-value: 2.61e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1953334639 540 DMLNDSDNRATISPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPLDLA 590
Cdd:pfam13857 6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
140-280 |
2.74e-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: 45.13 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 140 GRTALHHAAFSGHGEMVKLLLSRGANINA------FDKKDRraiHWAAYMGHievvkllvahgaevtckdkksyTPLHAA 213
Cdd:cd22194 141 GQTALNIAIERRQGDIVKLLIAKGADVNAhakgvfFNPKYK---HEGFYFGE----------------------TPLALA 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 214 ASSGMISVVKYLLDlgvdmNEPNAY------GNTPLH----VA-CYNGQDVVVNELIDC------GANVNQ-KNEKGFTP 275
Cdd:cd22194 196 ACTNQPEIVQLLME-----KESTDItsqdsrGNTVLHalvtVAeDSKTQNDFVKRMYDMillkseNKNLETiRNNEGLTP 270
|
....*
gi 1953334639 276 LHFAA 280
Cdd:cd22194 271 LQLAA 275
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
32-81 |
3.28e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 39.64 E-value: 3.28e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1953334639 32 EDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRA 81
Cdd:pfam13857 7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
652-684 |
3.67e-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: 3.67e-04
10 20 30
....*....|....*....|....*....|....
gi 1953334639 652 NGQTPLMLSVL-NGHTDCVYSLLNKGANVDAKDK 684
Cdd:pfam00023 1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
207-234 |
3.72e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 38.72 E-value: 3.72e-04
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
65-114 |
4.19e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 39.25 E-value: 4.19e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1953334639 65 ARVNAKDSKWLTPLHRAVASCSEEAVQVLLKHSADVNARDKNWQTPLHIA 114
Cdd:pfam13857 7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02989 |
PHA02989 |
ankyrin repeat protein; Provisional |
219-478 |
4.53e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222954 [Multi-domain] Cd Length: 494 Bit Score: 43.96 E-value: 4.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 219 ISVVKYLLDLGVDMNEpnAYGNTPLHVACYNGQDV---VVNELIDCGANVNQKnekGF--TPL-----HFAAASTHGALC 288
Cdd:PHA02989 16 KNALEFLLRTGFDVNE--EYRGNSILLLYLKRKDVkikIVKLLIDNGADVNYK---GYieTPLcavlrNREITSNKIKKI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 289 LELLVGNGADVNMKSKDGKTPLhMTALHG---------RFsrsqtIIQSGA-VIDCEDKNGNTPLHIaarYGHELLINT- 357
Cdd:PHA02989 91 VKLLLKFGADINLKTFNGVSPI-VCFIYNsninncdmlRF-----LLSKGInVNDVKNSRGYNLLHM---YLESFSVKKd 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 358 ----LITSGADT-AKRGIHGMFPLHLAALSGFS----DCCRKLLSSGFDIDTPDDFGRTCLHAAAagGNLECLNLLLNTG 428
Cdd:PHA02989 162 vikiLLSFGVNLfEKTSLYGLTPMNIYLRNDIDvisiKVIKYLIKKGVNIETNNNGSESVLESFL--DNNKILSKKEFKV 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1953334639 429 ADF-------NKKDKFGRSPLHYAAANCNYQCLFALVGSGASVNDLDERGCTPLHYA 478
Cdd:PHA02989 240 LNFilkyikiNKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYA 296
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
470-503 |
4.88e-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: 4.88e-04
10 20 30
....*....|....*....|....*....|....
gi 1953334639 470 RGCTPLHYAATSDTDGKCLEYLLRNDANPGIRDK 503
Cdd:pfam00023 1 DGNTPLHLAAGRRGNLEIVKLLLSKGADVNARDK 34
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
377-471 |
4.96e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 44.12 E-value: 4.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 377 HLAAlSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGADFNKKDKFGRSPLHYAAANCNYQCLFA 456
Cdd:PTZ00322 88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166
|
90
....*....|....*
gi 1953334639 457 LVGSGASVNDLDERG 471
Cdd:PTZ00322 167 LSRHSQCHFELGANA 181
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
639-748 |
5.49e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 44.12 E-value: 5.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 639 NAEPQNAVDiqdgngQTPL-MLSV------LNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQHGAK 711
Cdd:PTZ00322 67 NLTTEEVID------PVVAhMLTVelcqlaASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGAD 140
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1953334639 712 CLFRDSRGRTPIHLSAACGHIGVLGALL---QSAASVDAN 748
Cdd:PTZ00322 141 PTLLDKDGKTPLELAEENGFREVVQLLSrhsQCHFELGAN 180
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
822-850 |
5.52e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 38.34 E-value: 5.52e-04
10 20
....*....|....*....|....*....
gi 1953334639 822 KGRTPLHAAAFTDHVECLQLLLSHNAQVN 850
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
805-920 |
5.80e-04 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 43.67 E-value: 5.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 805 EMLIDtLGASiVNATDSKGRTPL-----HAAAFTDHVECLQLLLSHNAQVNSIDSSGKTPLMMAAENGQTNTVEMLVS-- 877
Cdd:PHA02798 55 KLFIN-LGAN-VNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLFmi 132
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1953334639 878 SASADLTLQDNSKNTALHLACSKGHETSALLI---LEKITDRNLIN 920
Cdd:PHA02798 133 ENGADTTLLDKDGFTMLQVYLQSNHHIDIEIIkllLEKGVDINTHN 178
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
428-510 |
6.12e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 42.50 E-value: 6.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 428 GADFNKKDK-FGRSPLHYAAA---NCNYQCLFALVGSGASVNDLDERGCTPLH-YAATSDTDGKCLEYLLRNDANPGIRD 502
Cdd:PHA02859 76 GADVNFKTRdNNLSALHHYLSfnkNVEPEILKILIDSGSSITEEDEDGKNLLHmYMCNFNVRINVIKLLIDSGVSFLNKD 155
|
....*...
gi 1953334639 503 KQGYNAVH 510
Cdd:PHA02859 156 FDNNNILY 163
|
|
| PHA02884 |
PHA02884 |
ankyrin repeat protein; Provisional |
221-315 |
6.48e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165212 [Multi-domain] Cd Length: 300 Bit Score: 43.05 E-value: 6.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 221 VVKYLLDLGVDMNEP-----NAYgNTPLHVACYNGQDVVVNELIDCGANVNQ-KNEKGFTPLHFAAasTHGAL-CLELLV 293
Cdd:PHA02884 48 IIDAILKLGADPEAPfplseNSK-TNPLIYAIDCDNDDAAKLLIRYGADVNRyAEEAKITPLYISV--LHGCLkCLEILL 124
|
90 100
....*....|....*....|..
gi 1953334639 294 GNGADVNMKSKDGKTPLHMTAL 315
Cdd:PHA02884 125 SYGADINIQTNDMVTPIELALM 146
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
618-724 |
6.64e-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: 43.59 E-value: 6.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 618 RTPIHAAATNGhseCLRLLIgNAEPQNavdiQDGNGQTPLMLSVLNGHTDCVYSLLNKGANVDAKDK------------- 684
Cdd:cd22194 114 RILLAFAEENG---ILDRFI-NAEYTE----EAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKgvffnpkykhegf 185
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1953334639 685 -WGRTALHRGAVTGHEECVDALLQHGAKCLF-RDSRGRTPIH 724
Cdd:cd22194 186 yFGETPLALAACTNQPEIVQLLMEKESTDITsQDSRGNTVLH 227
|
|
| TRPV1 |
cd22196 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ... |
816-948 |
7.97e-04 |
|
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: 43.26 E-value: 7.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 816 VNA--TDS--KGRTPLHAAAFTDHVECLQLLLSHNAQVNSIDSS--------------GKTPLMMAAENGQTNTVEMLVS 877
Cdd:cd22196 83 VNAayTDSyyKGQTALHIAIERRNMHLVELLVQNGADVHARASGeffkkkkggpgfyfGELPLSLAACTNQLDIVKFLLE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 878 S--ASADLTLQDNSKNTALHLACS---------------------KGHETSALLILEKITDRNLInatnaalqTPLHVAA 934
Cdd:cd22196 163 NphSPADISARDSMGNTVLHALVEvadntpentkfvtkmyneiliLGAKIRPLLKLEEITNKKGL--------TPLKLAA 234
|
170
....*....|....
gi 1953334639 935 RNGLTMVVQELLGK 948
Cdd:cd22196 235 KTGKIGIFAYILGR 248
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
271-304 |
8.79e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 37.65 E-value: 8.79e-04
10 20 30
....*....|....*....|....*....|....
gi 1953334639 271 KGFTPLHFAAASTHGALCLELLVGNGADVNMKSK 304
Cdd:pfam00023 1 DGNTPLHLAAGRRGNLEIVKLLLSKGADVNARDK 34
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
238-266 |
9.77e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 37.62 E-value: 9.77e-04
10 20
....*....|....*....|....*....
gi 1953334639 238 YGNTPLHVACYNGQDVVVNELIDCGANVN 266
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
338-364 |
1.11e-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: 1.11e-03
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
618-724 |
1.20e-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: 42.94 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 618 RTPIHAAATN---GHSECLRLLIgNAEPQNAVDIQDGN---------GQTPLMLSVLNGHTDCVYSLLNKGANVDAK--- 682
Cdd:cd21882 27 KTCLHKAALNlndGVNEAIMLLL-EAAPDSGNPKELVNapctdefyqGQTALHIAIENRNLNLVRLLVENGADVSARatg 105
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1953334639 683 ---DKWGRTALHRG-------AVTGHEECVDALLQHGAK---CLFRDSRGRTPIH 724
Cdd:cd21882 106 rffRKSPGNLFYFGelplslaACTNQEEIVRLLLENGAQpaaLEAQDSLGNTVLH 160
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
755-777 |
1.27e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 37.18 E-value: 1.27e-03
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
429-478 |
1.39e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 37.71 E-value: 1.39e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1953334639 429 ADFNKKDKFGRSPLHYAAANCNYQCLFALVGSGASVNDLDERGCTPLHYA 478
Cdd:pfam13857 7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| TRPV1 |
cd22196 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ... |
172-282 |
1.54e-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: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 172 KDRRAIHWAAYMGHIEVVKLLVAHGAEVTC-------KDKKSYT-------PLHAAASSGMISVVKYLLD---LGVDMNE 234
Cdd:cd22196 93 KGQTALHIAIERRNMHLVELLVQNGADVHArasgeffKKKKGGPgfyfgelPLSLAACTNQLDIVKFLLEnphSPADISA 172
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953334639 235 PNAYGNTPLHVACYNGQDVVVN---------ELIDCGANVNQK-------NEKGFTPLHFAAAS 282
Cdd:cd22196 173 RDSMGNTVLHALVEVADNTPENtkfvtkmynEILILGAKIRPLlkleeitNKKGLTPLKLAAKT 236
|
|
| PHA02884 |
PHA02884 |
ankyrin repeat protein; Provisional |
55-195 |
1.77e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165212 [Multi-domain] Cd Length: 300 Bit Score: 41.51 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 55 EIIELLILSGARVNAK----DSKWLTPLHRAVASCSEEAVQVLLKHSADVNARDKNWQ-TPLHIAAANKAVKCAEALVPL 129
Cdd:PHA02884 47 DIIDAILKLGADPEAPfplsENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLHGCLKCLEILLSY 126
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953334639 130 LSNVNVSDRAGRTALHHAAFSGHGEMVKLLlsRGANINAFDKKDRRaihwaaYMGHIEVVKLLVAH 195
Cdd:PHA02884 127 GADINIQTNDMVTPIELALMICNNFLAFMI--CDNEISNFYKHPKK------ILINFDILKILVSH 184
|
|
| PHA02736 |
PHA02736 |
Viral ankyrin protein; Provisional |
137-247 |
1.85e-03 |
|
Viral ankyrin protein; Provisional
Pssm-ID: 165103 [Multi-domain] Cd Length: 154 Bit Score: 40.24 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 137 DRAGRTALHHaaFSGHGEMVKLLLSRGANINA-------FDKKDRRAIHWAAYMGHI---EVVKLLVAHGAEVTCKDKK- 205
Cdd:PHA02736 14 DIEGENILHY--LCRNGGVTDLLAFKNAISDEnrylvleYNRHGKQCVHIVSNPDKAdpqEKLKLLMEWGADINGKERVf 91
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1953334639 206 SYTPLHAAASSGMISVVKYLLDL-GVDMNEPNAYGNTPLHVAC 247
Cdd:PHA02736 92 GNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVAC 134
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
891-946 |
1.96e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 37.25 E-value: 1.96e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1953334639 891 NTALHLACSKGHETSALLILEKITDrnlINATNAALQTPLHVAARNGLTMVVQELL 946
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGAD---INAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
858-903 |
2.02e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 37.25 E-value: 2.02e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1953334639 858 TPLMMAAENGQTNTVEMLVSSaSADLTLQDNSKNTALHLACSKGHE 903
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEK-GADINAVDGNGETALHFAASNGNV 47
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
790-895 |
2.07e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 40.57 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 790 SPLHCAVIND--NEGAAEMLIDTlGASIVNATDSKGRTPLHA-AAFTDHV--ECLQLLLSHNAQVNSIDSSGKTPLMMAA 864
Cdd:PHA02859 53 TPIFSCLEKDkvNVEILKFLIEN-GADVNFKTRDNNLSALHHyLSFNKNVepEILKILIDSGSSITEEDEDGKNLLHMYM 131
|
90 100 110
....*....|....*....|....*....|...
gi 1953334639 865 ENGQTN--TVEMLVSSASADLTlQDNSKNTALH 895
Cdd:PHA02859 132 CNFNVRinVIKLLIDSGVSFLN-KDFDNNNILY 163
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
42-71 |
2.13e-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: 2.13e-03
10 20 30
....*....|....*....|....*....|.
gi 1953334639 42 RTPLHAAAY-LGDAEIIELLILSGARVNAKD 71
Cdd:pfam00023 3 NTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
917-962 |
2.62e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 36.94 E-value: 2.62e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1953334639 917 NLINATNAALQTPLHVAARNGLTMVVQELLGKGASVLAVDENGYTP 962
Cdd:pfam13857 7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTA 52
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
583-609 |
2.68e-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: 36.41 E-value: 2.68e-03
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
583-613 |
2.84e-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: 2.84e-03
10 20 30
....*....|....*....|....*....|..
gi 1953334639 583 GRTPLDLAAFK-GHVECVDVLINQGASILVKD 613
Cdd:pfam00023 2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
344-416 |
2.97e-03 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 41.42 E-value: 2.97e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953334639 344 HIAARyGHELLINTLITSGADTAKRGIHGMFPLHLAALSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGG 416
Cdd:PTZ00322 88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENG 159
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
132-171 |
3.22e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 36.94 E-value: 3.22e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1953334639 132 NVNVSDRAGRTALHHAAFSGHGEMVKLLLSRGANINAFDK 171
Cdd:pfam13857 8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDE 47
|
|
| TRPV2 |
cd22197 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ... |
815-937 |
3.30e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411981 [Multi-domain] Cd Length: 640 Bit Score: 41.38 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 815 IVNA--TDS--KGRTPLHAAAFTDHVECLQLLLSHNAQVNSIDSS-------------GKTPLMMAAENGQTNTVEMLVS 877
Cdd:cd22197 82 LVNAqcTDEyyRGHSALHIAIEKRSLQCVKLLVENGADVHARACGrffqkkqgtcfyfGELPLSLAACTKQWDVVNYLLE 161
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953334639 878 SAS--ADLTLQDNSKNTALH---LACSKGHETSALL------ILEKITDRN----LINATNAALQTPLHVAARNG 937
Cdd:cd22197 162 NPHqpASLQAQDSLGNTVLHalvMIADNSPENSALVikmydgLLQAGARLCptvqLEEISNHEGLTPLKLAAKEG 236
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
462-511 |
3.32e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 36.56 E-value: 3.32e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1953334639 462 ASVNDLDERGCTPLHYAAtSDTDGKCLEYLLRNDANPGIRDKQGYNAVHY 511
Cdd:pfam13857 7 IDLNRLDGEGYTPLHVAA-KYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
76-105 |
3.59e-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: 3.59e-03
10 20 30
....*....|....*....|....*....|.
gi 1953334639 76 TPLHRAVASC-SEEAVQVLLKHSADVNARDK 105
Cdd:pfam00023 4 TPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
176-204 |
3.66e-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: 3.66e-03
10 20 30
....*....|....*....|....*....|
gi 1953334639 176 AIHWAAYM-GHIEVVKLLVAHGAEVTCKDK 204
Cdd:pfam00023 5 PLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
652-681 |
3.98e-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: 3.98e-03
10 20 30
....*....|....*....|....*....|
gi 1953334639 652 NGQTPLMLSVLNGHTDCVYSLLNKGANVDA 681
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
222-378 |
4.18e-03 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 40.81 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 222 VKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGANVNQKNEKGFTPLHFAAASTHGAL-CLELLVGNGADVN 300
Cdd:PHA02946 55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIeRINLLVQYGAKIN 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 301 MK-SKDGKTPL----------------------------------HMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHI 345
Cdd:PHA02946 135 NSvDEEGCGPLlactdpservfkkimsigfearivdkfgknhihrHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHI 214
|
170 180 190
....*....|....*....|....*....|....
gi 1953334639 346 A-ARYGHELLINTLITSGADTAKRGIHGMFPLHL 378
Cdd:PHA02946 215 VcSKTVKNVDIINLLLPSTDVNKQNKFGDSPLTL 248
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
176-201 |
4.56e-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: 4.56e-03
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
391-571 |
4.71e-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: 4.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 391 LLSSGFDIDTpddfGRTCLHAA-----------------AAGGNLECLNLLLNTGADFNkkdkFGRSPLHYAAANCNYQC 453
Cdd:TIGR00870 72 LLNLSCRGAV----GDTLLHAIsleyvdaveaillhllaAFRKSGPLELANDQYTSEFT----PGITALHLAAHRQNYEI 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 454 LFALVGSGASVN--------------DLDERGCTPLH-YAATSDTDgkCLEYLLRNDANPGIRDKQGYNAVH-------Y 511
Cdd:TIGR00870 144 VKLLLERGASVParacgdffvksqgvDSFYHGESPLNaAACLGSPS--IVALLSEDPADILTADSLGNTLLHllvmeneF 221
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953334639 512 SAAYGH--RLCLQLIasetpLDVLMETSGTDMLNDSDNRATISPLHLAAYHGHHQALEVLVQ 571
Cdd:TIGR00870 222 KAEYEElsCQMYNFA-----LSLLDKLRDSKELEVILNHQGLTPLKLAAKEGRIVLFRLKLA 278
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
928-979 |
4.77e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 36.10 E-value: 4.77e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1953334639 928 TPLHVAARNGLTMVVQELLGKGASVLAVDENGYTPALACAPNKDVADCLALI 979
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| TRPV1-4 |
cd22193 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ... |
140-282 |
4.83e-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: 40.93 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 140 GRTALHHAAFSGHGEMVKLLLSRGANINA------FDKKDRRAihwAAYMGHievvkllvahgaevtckdkksyTPLHAA 213
Cdd:cd22193 76 GQTALHIAIERRQGDIVALLVENGADVHAhakgrfFQPKYQGE---GFYFGE----------------------LPLSLA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 214 ASSGMISVVKYLLD---LGVDMNEPNAYGNTPLHVACYNGQDVVVN---------ELIDCGANVNQ-------KNEKGFT 274
Cdd:cd22193 131 ACTNQPDIVQYLLEnehQPADIEAQDSRGNTVLHALVTVADNTKENtkfvtrmydMILIRGAKLCPtveleeiRNNDGLT 210
|
....*...
gi 1953334639 275 PLHFAAAS 282
Cdd:cd22193 211 PLQLAAKM 218
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
15-79 |
4.99e-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: 40.77 E-value: 4.99e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953334639 15 AIFNGDPDEVRALIFKKEDVN--------FQDNEKRT------PLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLH 79
Cdd:cd22192 96 AVVNQNLNLVRELIARGADVVspratgtfFRPGPKNLiyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
|
|
| PHA02791 |
PHA02791 |
ankyrin-like protein; Provisional |
97-275 |
5.04e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165154 [Multi-domain] Cd Length: 284 Bit Score: 40.03 E-value: 5.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 97 SADVNARDKNWQTPLHIAAANKAVKC------AEALVPLLSNvnvsdragRTALHHAAFSGHGEMVKLLLSRGANINAFD 170
Cdd:PHA02791 20 SKDAFKADVHGHSALYYAIADNNVRLvctllnAGALKNLLEN--------EFPLHQAATLEDTKIVKILLFSGMDDSQFD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 171 KKDRRAIHWAAYMGHIEVVKLLVAHGAEVTCKDKKSY-TPLHAAASSGMISVVKYLL-------DLGVDMnepnaygnTP 242
Cdd:PHA02791 92 DKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTGWkTSFYHAVMLNDVSIVSYFLseipstfDLAILL--------SC 163
|
170 180 190
....*....|....*....|....*....|...
gi 1953334639 243 LHVACYNGQDVVVNELIDCGANVNQKNEKGFTP 275
Cdd:PHA02791 164 IHITIKNGHVDMMILLLDYMTSTNTNNSLLFIP 196
|
|
| PHA02716 |
PHA02716 |
CPXV016; CPX019; EVM010; Provisional |
566-760 |
7.04e-03 |
|
CPXV016; CPX019; EVM010; Provisional
Pssm-ID: 165089 [Multi-domain] Cd Length: 764 Bit Score: 40.28 E-value: 7.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 566 LEVLVQSLLDLDVRNSSGRTPLDLAAFKGHVeCVDVL---INQGASILVKdYILKRTPIHAAATNghseclrllIGNAEP 642
Cdd:PHA02716 195 LEWLCNNGVNVNLQNNHLITPLHTYLITGNV-CASVIkkiIELGGDMDMK-CVNGMSPIMTYIIN---------IDNINP 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 643 Q--NA-VDIQDGNGQT--PLMLSVL-----NGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGH--EECVDALLQHGA 710
Cdd:PHA02716 264 EitNIyIESLDGNKVKniPMILHSYitlarNIDISVVYSFLQPGVKLHYKDSAGRTCLHQYILRHNisTDIIKLLHEYGN 343
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953334639 711 KCLFRDSRGRTPIH--LSAACG------------HIGVLGALLQSAASVDAnpaiADNHGYTAL 760
Cdd:PHA02716 344 DLNEPDNIGNTVLHtyLSMLSVvnildpetdndiRLDVIQCLISLGADITA----VNCLGYTPL 403
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
338-364 |
7.40e-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: 34.93 E-value: 7.40e-03
10 20
....*....|....*....|....*..
gi 1953334639 338 NGNTPLHIAARYGHELLINTLITSGAD 364
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGAD 27
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
766-946 |
7.78e-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: 40.06 E-value: 7.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 766 NGHETCVELLLEQEVFQKTEGNAfspLHCAVINDnEGAAEMLI--------DTLGASIVNATD----SKGRTPLHAAAFT 833
Cdd:TIGR00870 63 NENLELTELLLNLSCRGAVGDTL---LHAISLEY-VDAVEAILlhllaafrKSGPLELANDQYtsefTPGITALHLAAHR 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 834 DHVECLQLLLSHNAQVNS------------IDS--SGKTPLMMAAENGQTNTVEMLvSSASADLTLQDNSKNTALHL--- 896
Cdd:TIGR00870 139 QNYEIVKLLLERGASVPAracgdffvksqgVDSfyHGESPLNAAACLGSPSIVALL-SEDPADILTADSLGNTLLHLlvm 217
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 897 ---------ACSKGHETSALLILEKITD-RNLINATNAALQTPLHVAARNGLTMVVQELL 946
Cdd:TIGR00870 218 enefkaeyeELSCQMYNFALSLLDKLRDsKELEVILNHQGLTPLKLAAKEGRIVLFRLKL 277
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
842-897 |
8.13e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 35.79 E-value: 8.13e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1953334639 842 LLSH-NAQVNSIDSSGKTPLMMAAENGQTNTVEMLVsSASADLTLQDNSKNTALHLA 897
Cdd:pfam13857 1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLL-AYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02989 |
PHA02989 |
ankyrin repeat protein; Provisional |
186-277 |
8.45e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222954 [Multi-domain] Cd Length: 494 Bit Score: 40.11 E-value: 8.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334639 186 IEVVKLLVAHGAEVtckDKKSY--TPLHAA------ASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNE 257
Cdd:PHA02989 50 IKIVKLLIDNGADV---NYKGYieTPLCAVlrnreiTSNKIKKIVKLLLKFGADINLKTFNGVSPIVCFIYNSNINNCDM 126
|
90 100
....*....|....*....|....
gi 1953334639 258 L---IDCGANVNQ-KNEKGFTPLH 277
Cdd:PHA02989 127 LrflLSKGINVNDvKNSRGYNLLH 150
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
338-364 |
8.71e-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: 34.96 E-value: 8.71e-03
10 20
....*....|....*....|....*...
gi 1953334639 338 NGNTPLHIAA-RYGHELLINTLITSGAD 364
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGAD 28
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
473-523 |
8.79e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 35.33 E-value: 8.79e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1953334639 473 TPLHYAATSDtDGKCLEYLLRNDANPGIRDKQGYNAVHYSAAYGHRLCLQL 523
Cdd:pfam13637 3 TALHAAAASG-HLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKL 52
|
|
| |
