|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
25-287 |
2.91e-50 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 179.38 E-value: 2.91e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 25 LNFLFYLEAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLL 104
Cdd:COG0666 28 AALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 105 SRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGN 184
Cdd:COG0666 108 EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 185 TPLHVACYNGQDVVVNELIDCGAIVNQKNEKGFTPLHFAAASTHGALcLELLVGNGADVNMKSKDGKTPLHMTALHGRFS 264
Cdd:COG0666 188 TPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI-VKLLLEAGADLNAKDKDGLTALLLAAAAGAAL 266
|
250 260
....*....|....*....|...
gi 1154884853 265 RSQTIIQSGAVIDCEDKNGNTPL 287
Cdd:COG0666 267 IVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
31-312 |
2.78e-49 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 176.68 E-value: 2.78e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 31 LEAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLLSRGANI 110
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 111 NAFDKKDRRAIHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVA 190
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 191 CYNGQDVVVNELIDCGAIVNQKNEKGFTPLHFAAASTHGALcLELLVGNGADVNMKSKDGKTPLHMTALHGRFSRSQTII 270
Cdd:COG0666 161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEI-VKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1154884853 271 QSGAVIDCEDKNGNTPLHIAARYGHELLINTLITSGADTAKR 312
Cdd:COG0666 240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAA 281
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
484-721 |
7.19e-39 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 146.64 E-value: 7.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 484 DMLSDSDNRATISPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPLDLAAFKGHVECVDVLINQGASILVKDYiLKRT 563
Cdd:COG0666 44 LLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDK-DGET 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 564 PIHAAATNGHSECLRLLIGNaepqNA-VDIQDGNGQTPLMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGH 642
Cdd:COG0666 123 PLHLAAYNGNLEIVKLLLEA----GAdVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGH 198
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1154884853 643 EECVDALLQHGAKCLLRDSRGRTPIHLSAACGHIGVLGALLQSAasmdANPATADNHGYTALHWACYNGHETCVELLLE 721
Cdd:COG0666 199 LEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG----ADLNAKDKDGLTALLLAAAAGAALIVKLLLL 273
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
98-419 |
9.99e-38 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 143.17 E-value: 9.99e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 98 EMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMN 177
Cdd:COG0666 2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 178 EPNAYGNTPLHVACYNGQDVVVNELIDCGAIVNQKNEKGFTPLHFAAASTHGALcLELLVGNGADVNMKskdgktplhmt 257
Cdd:COG0666 82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI-VKLLLEAGADVNAQ----------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 258 alhgrfsrsqtiiqsgavidceDKNGNTPLHIAARYGHELLINTLITSGADTAKRGIHGMFPLHLAALSGFSDCCRKLLS 337
Cdd:COG0666 150 ----------------------DNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 338 SGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGADFNKKDKFGRSPLHYAAANCNYQCLFALVGSGASVNDLDERGCT 417
Cdd:COG0666 208 AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
|
..
gi 1154884853 418 PL 419
Cdd:COG0666 288 LL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
546-870 |
1.44e-37 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 142.79 E-value: 1.44e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 546 LINQGASILVKDYILKRTPIHAAATNGHSECLRLLIGNAEPQNAVDIQDGNGQTPLMLSVLNGHTDCVYSLLNKGANVDA 625
Cdd:COG0666 3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 626 KDKWGRTALHRGAVTGHEECVDALLQHGAKCLLRDSRGRTPIHLSAACGHIGVLGALLQSaasmDANPATADNHGYTALH 705
Cdd:COG0666 83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA----GADVNAQDNDGNTPLH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 706 WACYNGHETCVELLLEQevfqktegnafsplhcavindneGAaemlidtlgasIVNATDSKGRTPLHAAAFTDHVECLQL 785
Cdd:COG0666 159 LAAANGNLEIVKLLLEA-----------------------GA-----------DVNARDNDGETPLHLAAENGHLEIVKL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 786 LLSHNAQVNSVDSTGKTPLMMAAENGQTNTVEMLVsSASAELTLQDNSKNTALHLACSKGHETSALLILEKITDRNLINA 865
Cdd:COG0666 205 LLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL-EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
|
....*
gi 1154884853 866 TNAAL 870
Cdd:COG0666 284 DLLTL 288
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
577-907 |
4.36e-37 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 141.63 E-value: 4.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 577 LRLLIGNAEPQNAVDIQDGNGQTPLMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQHGAKC 656
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 657 LLRDSRGRTPIHLSAACGHIGVLGALLQSaasmDANPATADNHGYTALHWACYNGHETCVELLLEQevfqktegnafspl 736
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEA----GADVNARDKDGETPLHLAAYNGNLEIVKLLLEA-------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 737 hcavindnegaaemlidtlGASiVNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLMMAAENGQTNTV 816
Cdd:COG0666 143 -------------------GAD-VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 817 EMLVsSASAELTLQDNSKNTALHLACSKGHETSALLILEKITDrnlINATNAALQTPLHVAARNGLTMVVQELLGKGASV 896
Cdd:COG0666 203 KLLL-EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD---LNAKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278
|
330
....*....|.
gi 1154884853 897 LAVDENGYTPA 907
Cdd:COG0666 279 AAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
451-698 |
7.89e-37 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 140.86 E-value: 7.89e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 451 NAVHYSAAYGHRLCLQLIASETPLDVLMETSGTDMLSDSDNRATISPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTP 530
Cdd:COG0666 44 LLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETP 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 531 LDLAAFKGHVECVDVLINQGASILVKDyILKRTPIHAAATNGHSECLRLLIGNaepqNA-VDIQDGNGQTPLMLSVLNGH 609
Cdd:COG0666 124 LHLAAYNGNLEIVKLLLEAGADVNAQD-NDGNTPLHLAAANGNLEIVKLLLEA----GAdVNARDNDGETPLHLAAENGH 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 610 TDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQHGAKCLLRDSRGRTPIHLSAACGHIGVLGALLQSAASM 689
Cdd:COG0666 199 LEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278
|
....*....
gi 1154884853 690 DANPATADN 698
Cdd:COG0666 279 AAALLDLLT 287
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
34-245 |
1.46e-35 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 140.57 E-value: 1.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 34 VQVLLKHSADVNARDKNWQTPLHIAAANKAV-----KCAEALVPLLSNVNVSDRAGRTALHHAAF--SGHGEMVKLLLSR 106
Cdd:PHA03100 51 VKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISkkSNSYSIVEYLLDN 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 107 GANINAFDKKDRRAIHWAAYMGHI--EVVKLLVSHGAEVTCKDKksytplhaaassgmisvVKYLLDLGVDMNEPNAYGN 184
Cdd:PHA03100 131 GANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKDVYGF 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154884853 185 TPLHVACYNGQDVVVNELIDCGAIVNQKNEKGFTPLHFAAASTHGALcLELLVGNGADVNM 245
Cdd:PHA03100 194 TPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEI-FKLLLNNGPSIKT 253
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
681-925 |
1.41e-34 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 134.31 E-value: 1.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 681 ALLQSAASMDANPATADNHGYTALHWACYNGHETCVELLLEQEVF-QKTEGNAFSPLHCAVINDNEGAAEMLIDtLGASi 759
Cdd:COG0666 35 LLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADiNAKDDGGNTLLHAAARNGDLEIVKLLLE-AGAD- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 760 VNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLMMAAENGQTNTVEMLVSsASAELTLQDNSKNTALH 839
Cdd:COG0666 113 VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLE-AGADVNARDNDGETPLH 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 840 LACSKGHETSALLILEKITDrnlINATNAALQTPLHVAARNGLTMVVQELLGKGASVLAVDENGYTPALACAPNKDVADC 919
Cdd:COG0666 192 LAAENGHLEIVKLLLEAGAD---VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIV 268
|
....*.
gi 1154884853 920 LALILA 925
Cdd:COG0666 269 KLLLLA 274
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
169-447 |
1.60e-33 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 131.23 E-value: 1.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 169 LLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGAIVNQKNEKGFTPLHFAAASTHGALCLELLVGNGADVNMKSK 248
Cdd:COG0666 6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 249 DGKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGHELLINTLITSGADTAKRGIHGMFPLHLAALSGF 328
Cdd:COG0666 86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 329 SDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGADFNKKDKFGRSPLHYAAANCNYQCLFALVGSGASV 408
Cdd:COG0666 166 LEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADL 245
|
250 260 270
....*....|....*....|....*....|....*....
gi 1154884853 409 NDLDERGCTPLHYAATSDTDGKCLEYLLRNDANPGIRDK 447
Cdd:COG0666 246 NAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLD 284
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
30-254 |
8.49e-33 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 133.23 E-value: 8.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 30 YLEAVQVLLKHSADVNARDKNWQTPLHIAAANKAVkcaEALVPLL----SNVNVSDRAGRTALH-HAA-FSGHGEMVKLL 103
Cdd:PHA03095 62 VKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATT---LDVIKLLikagADVNAKDKVGRTPLHvYLSgFNINPKVIRLL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 104 LSRGANINAFDKKDRRAIHwaAYMGH----IEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMIS--VVKYLLDLGVDMN 177
Cdd:PHA03095 139 LRKGADVNALDLYGMTPLA--VLLKSrnanVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRarIVRELIRAGCDPA 216
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1154884853 178 EPNAYGNTPLHVACYNG--QDVVVNELIDCGAIVNQKNEKGFTPLHFAAASTHGALCLELLVGnGADVNMKSKDGKTPL 254
Cdd:PHA03095 217 ATDMLGNTPLHSMATGSscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIAL-GADINAVSSDGNTPL 294
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
30-303 |
1.48e-32 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 132.46 E-value: 1.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 30 YLEAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLL---SNVNVSDRAGRTALH-HAAFSGHGEMVKLLLS 105
Cdd:PHA03095 26 TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIVRLLLeagADVNAPERCGFTPLHlYLYNATTLDVIKLLIK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 106 RGANINAFDKKDRRAIHwaAYMG----HIEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMISV--VKYLLDLGVDMNEP 179
Cdd:PHA03095 106 AGADVNAKDKVGRTPLH--VYLSgfniNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVYAV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 180 NAYGNTPLHVACYNGQD--VVVNELIDCGAIVNQKNEKGFTPLHFAAA-STHGALCLELLVGNGADVNMKSKDGKTPLHM 256
Cdd:PHA03095 184 DDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHSMATgSSCKRSLVLPLLIAGISINARNRYGQTPLHY 263
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1154884853 257 TALHGR---FSRsqtIIQSGAVIDCEDKNGNTPLHIAARYGHELLINTLI 303
Cdd:PHA03095 264 AAVFNNpraCRR---LIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
681-925 |
3.45e-32 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 127.38 E-value: 3.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 681 ALLQSAASMDANPATADNHGYTALHWACYNGHETCVELLLEQEVFQKTEGNAFSPLHCAVINDNEGAAEMLIDTLGASIv 760
Cdd:COG0666 2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 761 NATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLMMAAENGQTNTVEMLVsSASAELTLQDNSKNTALHL 840
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLL-EAGADVNAQDNDGNTPLHL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 841 ACSKGHETSALLILEKITDrnlINATNAALQTPLHVAARNGLTMVVQELLGKGASVLAVDENGYTPALACAPNKDVADCL 920
Cdd:COG0666 160 AAANGNLEIVKLLLEAGAD---VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVK 236
|
....*
gi 1154884853 921 ALILA 925
Cdd:COG0666 237 LLLEA 241
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
207-469 |
1.54e-31 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 125.45 E-value: 1.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 207 AIVNQKNEKGFTPLHFAAASTHGALCLELLVGNGADVNMKSKDGKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTP 286
Cdd:COG0666 11 LLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 287 LHIAARYGHELLINTLITSGADTAKRGIHGMFPLHLAALSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLN 366
Cdd:COG0666 91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 367 LLLNTGADFNKKDKFGRSPLHYAAANCNYQCLFALVGSGASVNDLDERGCTPLHYAATSDtDGKCLEYLLRNDANPGIRD 446
Cdd:COG0666 171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENG-NLEIVKLLLEAGADLNAKD 249
|
250 260
....*....|....*....|...
gi 1154884853 447 KQGYNAVHYSAAYGHRLCLQLIA 469
Cdd:COG0666 250 KDGLTALLLAAAAGAALIVKLLL 272
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
163-419 |
2.60e-31 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 128.99 E-value: 2.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 163 ISVVKYLLDLGVDMNEPNAYGNTPLHV--ACYNGQDV-VVNELIDCGAIVNQKNEKGFTPLHFAAASTHGALCLELLVGN 239
Cdd:PHA03095 27 VEEVRRLLAAGADVNFRGEYGKTPLHLylHYSSEKVKdIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDVIKLLIKA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 240 GADVNMKSKDGKTPLH--MTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGH---ELLiNTLITSGADTAKRGI 314
Cdd:PHA03095 107 GADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanvELL-RLLIDAGADVYAVDD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 315 HGMFPLHLAALS--GFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLL--NTGADFNKKDKFGRSPLHYAA 390
Cdd:PHA03095 186 RFRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVLPllIAGISINARNRYGQTPLHYAA 265
|
250 260 270
....*....|....*....|....*....|
gi 1154884853 391 ANCNyQCLFA-LVGSGASVNDLDERGCTPL 419
Cdd:PHA03095 266 VFNN-PRACRrLIALGADINAVSSDGNTPL 294
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
130-398 |
8.70e-31 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 127.45 E-value: 8.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 130 IEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGM---ISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDV-VVNELIDC 205
Cdd:PHA03095 27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 206 GAIVNQKNEKGFTPLH--FAAASTHgALCLELLVGNGADVNMKSKDGKTPLHMtalhgrFSRSQTI--------IQSGAV 275
Cdd:PHA03095 107 GADVNAKDKVGRTPLHvyLSGFNIN-PKVIRLLLRKGADVNALDLYGMTPLAV------LLKSRNAnvellrllIDAGAD 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 276 IDCEDKNGNTPLHIAARYGH--ELLINTLITSGADTAKRGIHGMFPLHLAALsgFSDCCR----KLLSSGFDIDTPDDFG 349
Cdd:PHA03095 180 VYAVDDRFRSLLHHHLQSFKprARIVRELIRAGCDPAATDMLGNTPLHSMAT--GSSCKRslvlPLLIAGISINARNRYG 257
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1154884853 350 RTCLHAAAAGGNLECLNLLLNTGADFNKKDKFGRSPLHYAAANCNYQCL 398
Cdd:PHA03095 258 QTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAV 306
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
99-419 |
1.43e-30 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 129.03 E-value: 1.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 99 MVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNE 178
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINK 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 179 P-----NAYGNTPLHVACYngqdvvvneLIDCGAIVNQKNEKGFTPLHFAAASTHGALCLELLVGNGADVNMKSKDGKTP 253
Cdd:PHA02876 240 NdlsllKAIRNEDLETSLL---------LYDAGFSVNSIDDCKNTPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETP 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 254 LHMTALHGRFSRS-QTIIQSGAVIDCEDKNGNTPLHIAA---RYGHELLinTLITSGADTAKRGIHGMFPLHLAALSGFS 329
Cdd:PHA02876 311 LYLMAKNGYDTENiRTLIMLGADVNAADRLYITPLHQAStldRNKDIVI--TLLELGANVNARDYCDKTPIHYAAVRNNV 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 330 DCCRKLLSSGFDIDTPDDFGRTCLHAAAAG-GNLECLNLLLNTGADFNKKDKFGRSPLHYAAA-NCNYQCLFALVGSGAS 407
Cdd:PHA02876 389 VIINTLLDYGADIEALSQKIGTALHFALCGtNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKkNCKLDVIEMLLDNGAD 468
|
330
....*....|..
gi 1154884853 408 VNDLDERGCTPL 419
Cdd:PHA02876 469 VNAINIQNQYPL 480
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
233-531 |
1.54e-30 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 122.37 E-value: 1.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 233 LELLVGNGADVNMKSKDGKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGHELLINTLITSGADTAKR 312
Cdd:COG0666 4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 313 GIHGMFPLHLAALSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGADFNKKDKFGRSPLHYAAAN 392
Cdd:COG0666 84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 393 CNYQCLFALVGSGASVNDLDERGCTPLHYAATSDtDGKCLEYLLRNDANPGIRDKQGYNAVHYSAAYGHRLCLQLIASET 472
Cdd:COG0666 164 GNLEIVKLLLEAGADVNARDNDGETPLHLAAENG-HLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1154884853 473 PLDvlmetsgtdmlsDSDNRATISPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPL 531
Cdd:COG0666 243 ADL------------NAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
296-634 |
5.37e-30 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 120.83 E-value: 5.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 296 ELLINTLITSGADTAKRGIHGMFPLHLAALSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGADF 375
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 376 NKKDKFGRSPLHYAAANCNYQCLFALVGSGASVNDLDERGCTPLHYAATSDtDGKCLEYLLRNDANPGIRDKQGYnavhy 455
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNG-NLEIVKLLLEAGADVNAQDNDGN----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 456 saayghrlclqliasetpldvlmetsgtdmlsdsdnratiSPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPLDLAA 535
Cdd:COG0666 155 ----------------------------------------TPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 536 FKGHVECVDVLINQGASILVKDYiLKRTPIHAAATNGHSECLRLLIGNAEpqnAVDIQDGNGQTPLMLSVLNGHTDCVYS 615
Cdd:COG0666 195 ENGHLEIVKLLLEAGADVNAKDN-DGKTALDLAAENGNLEIVKLLLEAGA---DLNAKDKDGLTALLLAAAAGAALIVKL 270
|
330
....*....|....*....
gi 1154884853 616 LLNKGANVDAKDKWGRTAL 634
Cdd:COG0666 271 LLLALLLLAAALLDLLTLL 289
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
31-214 |
1.65e-29 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 122.47 E-value: 1.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 31 LEAVQVLLKHSADVNARDKNWQTPLHIAAANKavKCAEALVPLL----SNVNVSDRAGRTALHHAAFSGHG--EMVKLLL 104
Cdd:PHA03100 86 KEIVKLLLEYGANVNAPDNNGITPLLYAISKK--SNSYSIVEYLldngANVNIKNSDGENLLHLYLESNKIdlKILKLLI 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 105 SRGANINAfdkKDRraihwaaymghievVKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGN 184
Cdd:PHA03100 164 DKGVDINA---KNR--------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGD 226
|
170 180 190
....*....|....*....|....*....|
gi 1154884853 185 TPLHVACYNGQDVVVNELIDCGAIVNQKNE 214
Cdd:PHA03100 227 TPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
34-311 |
1.75e-27 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 116.60 E-value: 1.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 34 VQVLLKHSADVNARDKNWQTPLHIA---AANKAVK--------CAEALVPLLSNvnvsdragrtalhhaafsghgEMVKL 102
Cdd:PHA02874 51 VELFIKHGADINHINTKIPHPLLTAikiGAHDIIKllidngvdTSILPIPCIEK---------------------DMIKT 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 103 LLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAY 182
Cdd:PHA02874 110 ILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNN 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 183 GNTPLHVACYNGQDVVVNELIDCGAIVNQKNEKGFTPLHfaAASTHGALCLELLVgNGADVNMKSKDGKTPLHMtALHGR 262
Cdd:PHA02874 190 GESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLH--NAIIHNRSAIELLI-NNASINDQDIDGSTPLHH-AINPP 265
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1154884853 263 FSRS--QTIIQSGAVIDCEDKNGNTPLHIAARYGH------ELLINTLITSGADTAK 311
Cdd:PHA02874 266 CDIDiiDILLYHKADISIKDNKGENPIDTAFKYINkdpvikDIIANAVLIKEADKLK 322
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
93-463 |
1.02e-26 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 114.29 E-value: 1.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 93 FSGHGEMV-KLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLD 171
Cdd:PHA02874 10 YSGDIEAIeKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLID 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 172 LGVDmnepnaygNTPLHVACYNGQdvVVNELIDCGAIVNQKNEKGFTPLHFAAASthGAL-CLELLVGNGADVNMKSKDG 250
Cdd:PHA02874 90 NGVD--------TSILPIPCIEKD--MIKTILDCGIDVNIKDAELKTFLHYAIKK--GDLeSIKMLFEYGADVNIEDDNG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 251 KTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGHELLINTLITSGADTAKRGIHGMFPLHLAALsgfsd 330
Cdd:PHA02874 158 CYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII----- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 331 ccrkllssgfdidtpddfgrtclhaaaaggnleclnlllntgadfnkkdkFGRSPLhyaaancnyqclfALVGSGASVND 410
Cdd:PHA02874 233 --------------------------------------------------HNRSAI-------------ELLINNASIND 249
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1154884853 411 LDERGCTPLHYAATSDTDGKCLEYLLRNDANPGIRDKQGYNAVHYSAAYGHRL 463
Cdd:PHA02874 250 QDIDGSTPLHHAINPPCDIDIIDILLYHKADISIKDNKGENPIDTAFKYINKD 302
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
77-323 |
4.11e-26 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 112.75 E-value: 4.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 77 VNVSDRAGRTALHHAAFSGHGEMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVSHGAE-------------- 142
Cdd:PHA02874 28 INISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDtsilpipciekdmi 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 143 ---------VTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGAIVNQKN 213
Cdd:PHA02874 108 ktildcgidVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKD 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 214 EKGFTPLHFAAASTHGAlCLELLVGNGADVNMKSKDGKTPLHMTALHGRfSRSQTIIQSgAVIDCEDKNGNTPLHIAARY 293
Cdd:PHA02874 188 NNGESPLHNAAEYGDYA-CIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLINN-ASINDQDIDGSTPLHHAINP 264
|
250 260 270
....*....|....*....|....*....|.
gi 1154884853 294 GHEL-LINTLITSGADTAKRGIHGMFPLHLA 323
Cdd:PHA02874 265 PCDIdIIDILLYHKADISIKDNKGENPIDTA 295
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
130-344 |
7.90e-25 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 108.60 E-value: 7.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 130 IEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLH---VACYNGQDVV--VNELID 204
Cdd:PHA03100 15 VKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsNIKYNLTDVKeiVKLLLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 205 CGAIVNQKNEKGFTPLHFAAASTHGALCL-ELLVGNGADVNMKSKDGKTPLHMtAL---HGRFSRSQTIIQSGA------ 274
Cdd:PHA03100 95 YGANVNAPDNNGITPLLYAISKKSNSYSIvEYLLDNGANVNIKNSDGENLLHL-YLesnKIDLKILKLLIDKGVdinakn 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 275 ----------VIDCEDKNGNTPLHIAARYGHELLINTLITSGADTAKRGIHGMFPLHLAALSGFSDCCRKLLSSGFDIDT 344
Cdd:PHA03100 174 rvnyllsygvPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
34-308 |
2.02e-24 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 109.77 E-value: 2.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 34 VQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRA-----------------------------G 84
Cdd:PHA02876 194 VNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDLSllkairnedletslllydagfsvnsiddcK 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 85 RTALHHAAFSGH-GEMVKLLLSRGANINAFDKKDRRAIHWAAYMGH-IEVVKLLVSHGAEVTCKDKKSYTPLHAAAS-SG 161
Cdd:PHA02876 274 NTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTlDR 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 162 MISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGAIVNQKNEKGFTPLHFAAASTHGALCLELLVGNGA 241
Cdd:PHA02876 354 NKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMSVKTLIDRGA 433
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1154884853 242 DVNMKSKDGKTPLHMTALHG-RFSRSQTIIQSGAVIDCEDKNGNTPLHIAarYGHELLINTLITSGAD 308
Cdd:PHA02876 434 NVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIA--LEYHGIVNILLHYGAE 499
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
498-807 |
7.99e-23 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 102.73 E-value: 7.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 498 LHLAAYHGHHQALEVLVQS---LLDLDVRNSSgrTPLDLAAFKGHVECVDVLINQGASIlvkDYILKRTP--IHAAATNG 572
Cdd:PHA02874 5 LRMCIYSGDIEAIEKIIKNkgnCINISVDETT--TPLIDAIRSGDAKIVELFIKHGADI---NHINTKIPhpLLTAIKIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 573 HSECLRLLIgnaepQNAVDIQdgngqtplMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQH 652
Cdd:PHA02874 80 AHDIIKLLI-----DNGVDTS--------ILPIPCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 653 GAKCLLRDSRGRTPIHLSAACGHIGVLGALLQSAASMDANpataDNHGYTALHWACYNGHETCVELLLEQ--EVFQKTEg 730
Cdd:PHA02874 147 GADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVK----DNNGESPLHNAAEYGDYACIKLLIDHgnHIMNKCK- 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1154884853 731 NAFSPLHCAVINdNEGAAEMLIDTlgASIvNATDSKGRTPLH-AAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLMMA 807
Cdd:PHA02874 222 NGFTPLHNAIIH-NRSAIELLINN--ASI-NDQDIDGSTPLHhAINPPCDIDIIDILLYHKADISIKDNKGENPIDTA 295
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
31-297 |
1.02e-22 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 103.04 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 31 LEAVQVLLKHSADVNARDKNWQTPLHIA--AANKavkcaEALVPLLSNVNVSD-----RAGRTALHHAAFsghgEMVK-L 102
Cdd:PHA02878 50 LDVVKSLLTRGHNVNQPDHRDLTPLHIIckEPNK-----LGMKEMIRSINKCSvfytlVAIKDAFNNRNV----EIFKiI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 103 LLSRGANINAFDKKDRRAIHWAAYMgHIEVVKLLVSHGAEVTCKDK-KSYTPLHAAASSGMISVVKYLLDLGVDMNEPNA 181
Cdd:PHA02878 121 LTNRYKNIQTIDLVYIDKKSKDDII-EAEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDK 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 182 YGNTPLHVACYNGQDVVVNELIDCGAIVNQKNEKGFTPLHFAAASTHGALCLELLVGNGADVNMKSK-DGKTPLHMtALH 260
Cdd:PHA02878 200 TNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDYDILKLLLEHGVDVNAKSYiLGLTALHS-SIK 278
|
250 260 270
....*....|....*....|....*....|....*....
gi 1154884853 261 GRfSRSQTIIQSGAVIDCEDKNGNTPLHIAA--RYGHEL 297
Cdd:PHA02878 279 SE-RKLKLLLEYGADINSLNSYKLTPLSSAVkqYLCINI 316
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
88-180 |
5.35e-21 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 88.25 E-value: 5.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 88 LHHAAFSGHGEMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVSHgAEVTCKDKKsYTPLHAAASSGMISVVK 167
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG-RTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1154884853 168 YLLDLGVDMNEPN 180
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
55-147 |
7.38e-21 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 87.86 E-value: 7.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 55 LHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLLSRgANINAFDkKDRRAIHWAAYMGHIEVVK 134
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1154884853 135 LLVSHGAEVTCKD 147
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
121-213 |
7.62e-20 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 85.17 E-value: 7.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 121 IHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDlGVDMNEPNaYGNTPLHVACYNGQDVVVN 200
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1154884853 201 ELIDCGAIVNQKN 213
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
597-926 |
2.41e-19 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 92.40 E-value: 2.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 597 GQTPLMLSVLNGHTDC---VYSLLNKGANVDAKDKWGRTALH---RGAVTghEECVDALLQHGAKCLLRDSRGRTPIH-- 668
Cdd:PHA03095 47 GKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLHlylYNATT--LDVIKLLIKAGADVNAKDKVGRTPLHvy 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 669 LSAACGHIGVLGALLQsaasMDANPATADNHGYTalhwacynghetcvellleqevfqktegnafsPLHCAVINdnegaa 748
Cdd:PHA03095 125 LSGFNINPKVIRLLLR----KGADVNALDLYGMT--------------------------------PLAVLLKS------ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 749 emlidtlgasiVNATdskgrtplhaaaftdhVECLQLLLSHNAQVNSVDSTGKTPLMMAAENGQTNT--VEMLVSsASAE 826
Cdd:PHA03095 163 -----------RNAN----------------VELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRAriVRELIR-AGCD 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 827 LTLQDNSKNTALHLACSKGHETSALLI--LEKITDrnlINATNAALQTPLHVAARNGLTMVVQELLGKGASVLAVDENGY 904
Cdd:PHA03095 215 PAATDMLGNTPLHSMATGSSCKRSLVLplLIAGIS---INARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGN 291
|
330 340
....*....|....*....|..
gi 1154884853 905 TPALACAPNKDVaDCLALILAT 926
Cdd:PHA03095 292 TPLSLMVRNNNG-RAVRAALAK 312
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
30-114 |
1.65e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 81.32 E-value: 1.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 30 YLEAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLsNVNVSDRaGRTALHHAAFSGHGEMVKLLLSRGAN 109
Cdd:pfam12796 9 NLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKDN-GRTALHYAARSGHLEIVKLLLEKGAD 86
|
....*
gi 1154884853 110 INAFD 114
Cdd:pfam12796 87 INVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
565-660 |
1.75e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 81.32 E-value: 1.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 565 IHAAATNGHSECLRLLIgnaEPQNAVDIQDGNGQTPLMLSVLNGHTDCVYSLLNKgANVDAKDKwGRTALHRGAVTGHEE 644
Cdd:pfam12796 1 LHLAAKNGNLELVKLLL---ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLE 75
|
90
....*....|....*.
gi 1154884853 645 CVDALLQHGAKCLLRD 660
Cdd:pfam12796 76 IVKLLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
531-627 |
2.30e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 80.93 E-value: 2.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 531 LDLAAFKGHVECVDVLINQGASILVKDyILKRTPIHAAATNGHSECLRLLIGNAEPQNavdiqDGNGQTPLMLSVLNGHT 610
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQD-KNGRTALHLAAKNGHLEIVKLLLEHADVNL-----KDNGRTALHYAARSGHL 74
|
90
....*....|....*..
gi 1154884853 611 DCVYSLLNKGANVDAKD 627
Cdd:pfam12796 75 EIVKLLLEKGADINVKD 91
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
519-799 |
2.95e-18 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 88.93 E-value: 2.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 519 DLDVRNSSGRTPLDLAAFKGHVECVDV---LINQGASILVKDyILKRTPIHAAATNGHSE-CLRLLIGNaepqNA-VDIQ 593
Cdd:PHA03095 39 DVNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPE-RCGFTPLHLYLYNATTLdVIKLLIKA----GAdVNAK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 594 DGNGQTPL--MLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALH----RGAVTghEECVDALLQHGAKCLLRDSRGRTPI 667
Cdd:PHA03095 114 DKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAvllkSRNAN--VELLRLLIDAGADVYAVDDRFRSLL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 668 HLSAACGHI--GVLGALLQSAAsmdaNPATADNHGYTALHWACYngHETCVELLLEQEVFQKTEGNA-----FSPLHCAV 740
Cdd:PHA03095 192 HHHLQSFKPraRIVRELIRAGC----DPAATDMLGNTPLHSMAT--GSSCKRSLVLPLLIAGISINArnrygQTPLHYAA 265
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1154884853 741 INDNEGAAEMLIdTLGASIvNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDST 799
Cdd:PHA03095 266 VFNNPRACRRLI-ALGADI-NAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAAT 322
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
154-246 |
5.90e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 79.77 E-value: 5.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 154 LHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGAIvnQKNEKGFTPLHFAAASTHGAlCL 233
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLE-IV 77
|
90
....*....|...
gi 1154884853 234 ELLVGNGADVNMK 246
Cdd:pfam12796 78 KLLLEKGADINVK 90
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
372-721 |
7.97e-18 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 88.58 E-value: 7.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 372 GADFNKKDKFGRSPLHYAAANCNYQCLFALVGSGASVNDLDERGCTPLHYAATSDtDGKCLEYLLRNDANPGIRDKQGYN 451
Cdd:PHA02876 168 GADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSK-NIDTIKAIIDNRSNINKNDLSLLK 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 452 AVHYSAAyghrlclqliasETPLdvLMETSGTDMLSDSDNRATisPLHLAAyhgHHQALEVLVQSLL----DLDVRNSSG 527
Cdd:PHA02876 247 AIRNEDL------------ETSL--LLYDAGFSVNSIDDCKNT--PLHHAS---QAPSLSRLVPKLLergaDVNAKNIKG 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 528 RTPLDLAAFKGH-VECVDVLINQGASILVKDYiLKRTPIHAAATnghseclrllignaepqnavdiqdgngqtplmlsvL 606
Cdd:PHA02876 308 ETPLYLMAKNGYdTENIRTLIMLGADVNAADR-LYITPLHQAST-----------------------------------L 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 607 NGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQHGAKCLLRDSRGRTPIHLsAACGHIGVLGalLQSA 686
Cdd:PHA02876 352 DRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHF-ALCGTNPYMS--VKTL 428
|
330 340 350
....*....|....*....|....*....|....*.
gi 1154884853 687 ASMDANPATADNHGYTALHWACYNGHE-TCVELLLE 721
Cdd:PHA02876 429 IDRGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLD 464
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
32-261 |
1.08e-17 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 87.24 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 32 EAVQVLLKHSADVNARDKNW-QTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLLSRGANI 110
Cdd:PHA02878 148 EITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAST 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 111 NAFDKKDRRAIHWA-AYMGHIEVVKLLVSHGAEVTCKdkksytplhaaassgmisvvKYLLDLgvdmnepnaygnTPLHV 189
Cdd:PHA02878 228 DARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAK--------------------SYILGL------------TALHS 275
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1154884853 190 ACYNGQdvVVNELIDCGAIVNQKNEKGFTPLHFAAASTHGALCLELLVGNGADVNMKSKDGKTPL----HMTALHG 261
Cdd:PHA02878 276 SIKSER--KLKLLLEYGADINSLNSYKLTPLSSAVKQYLCINIGRILISNICLLKRIKPDIKNSEgfidNMDCITS 349
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
333-701 |
2.34e-17 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 86.23 E-value: 2.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 333 RKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECL---NLLLNTGADFNKKDKFGRSPLH-YAAANCNYQCLFALVGSGASV 408
Cdd:PHA03095 31 RRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKdivRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 409 NDLDERGCTPLH-YAATSDTDGKCLEYLLRNDANPGIRDKqgynavhysaaYGHrlclqliaseTPLDVLMetsgtdmls 487
Cdd:PHA03095 111 NAKDKVGRTPLHvYLSGFNINPKVIRLLLRKGADVNALDL-----------YGM----------TPLAVLL--------- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 488 dSDNRATISPLHLaayhghhqalevLVQSLLDLDVRNSSGRTPLD--LAAFKGHVECVDVLINQGASILVKDyILKRTPI 565
Cdd:PHA03095 161 -KSRNANVELLRL------------LIDAGADVYAVDDRFRSLLHhhLQSFKPRARIVRELIRAGCDPAATD-MLGNTPL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 566 HAAATngHSECLRLLIGNaepqnavdiqdgngqtplmlsvlnghtdcvysLLNKGANVDAKDKWGRTALHRGAVTGHEEC 645
Cdd:PHA03095 227 HSMAT--GSSCKRSLVLP--------------------------------LLIAGISINARNRYGQTPLHYAAVFNNPRA 272
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1154884853 646 VDALLQHGAKCLLRDSRGRTPIHLSAACGHIGVLGALLQ---SAASMDANPATADNHGY 701
Cdd:PHA03095 273 CRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAknpSAETVAATLNTASVAGG 331
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
32-223 |
6.45e-17 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 84.63 E-value: 6.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 32 EAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLLSRGANIN 111
Cdd:PHA02874 105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 112 AFDKKDRRAIHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMiSVVKYLLDlGVDMNEPNAYGNTPLHVAC 191
Cdd:PHA02874 185 VKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLIN-NASINDQDIDGSTPLHHAI 262
|
170 180 190
....*....|....*....|....*....|...
gi 1154884853 192 YNGQDV-VVNELIDCGAIVNQKNEKGFTPLHFA 223
Cdd:PHA02874 263 NPPCDIdIIDILLYHKADISIKDNKGENPIDTA 295
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
32-210 |
1.22e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 83.50 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 32 EAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALvpLLSNVNVSD---RAGRTALHHAAFSGHGEMVKLLLSRGA 108
Cdd:PHA02875 49 EAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEEL--LDLGKFADDvfyKDGMTPLHLATILKKLDIMKLLIARGA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 109 NINAFDKKDRRAIHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDmnePNAYGNTP-L 187
Cdd:PHA02875 127 DPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGAN---IDYFGKNGcV 203
|
170 180
....*....|....*....|....*.
gi 1154884853 188 HVACY---NGQDVVVNELIDCGAIVN 210
Cdd:PHA02875 204 AALCYaieNNKIDIVRLFIKRGADCN 229
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
771-864 |
1.30e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 75.92 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 771 LHAAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLMMAAENGQTNTVEMLVSSASAELtlqDNSKNTALHLACSKGHETSA 850
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL---KDNGRTALHYAARSGHLEIV 77
|
90
....*....|....
gi 1154884853 851 LLILEKITDRNLIN 864
Cdd:pfam12796 78 KLLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
601-692 |
5.62e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 74.00 E-value: 5.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 601 LMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQHGAkcLLRDSRGRTPIHLSAACGHIGVLG 680
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78
|
90
....*....|..
gi 1154884853 681 ALLQSAASMDAN 692
Cdd:pfam12796 79 LLLEKGADINVK 90
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
475-654 |
1.17e-15 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 81.84 E-value: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 475 DVLMETSGTDmlsdsDNRATISPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPLDLAAFKGHVECVDVLINQGASIL 554
Cdd:PLN03192 511 DLLGDNGGEH-----DDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVH 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 555 VKDyILKRTPIHAAATNGHSECLRLLIGNA---EPQNAVDIqdgngqtpLMLSVLNGHTDCVYSLLNKGANVDAKDKWGR 631
Cdd:PLN03192 586 IRD-ANGNTALWNAISAKHHKIFRILYHFAsisDPHAAGDL--------LCTAAKRNDLTAMKELLKQGLNVDSEDHQGA 656
|
170 180
....*....|....*....|...
gi 1154884853 632 TALHRGAVTGHEECVDALLQHGA 654
Cdd:PLN03192 657 TALQVAMAEDHVDMVRLLIMNGA 679
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
6-211 |
1.28e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 80.39 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 6 TMKSEPHCTPQLTLEMQKSLNFLFY------LEAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNV 79
Cdd:PHA02874 106 MIKTILDCGIDVNIKDAELKTFLHYaikkgdLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANV 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 80 SDRAGRTALHHAAFSGHGEMVKLLLSRGANINAFDKKDRRAIHwAAYMGHIEVVKLLVSHgAEVTCKDKKSYTPLHAAAS 159
Cdd:PHA02874 186 KDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLH-NAIIHNRSAIELLINN-ASINDQDIDGSTPLHHAIN 263
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1154884853 160 SGM-ISVVKYLLDLGVDMNEPNAYGNTPLHVAC-YNGQDVVVNELIDCGAIVNQ 211
Cdd:PHA02874 264 PPCdIDIIDILLYHKADISIKDNKGENPIDTAFkYINKDPVIKDIIANAVLIKE 317
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
704-797 |
2.13e-15 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 72.46 E-value: 2.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 704 LHWACYNGHETCVELLLEQEV-FQKTEGNAFSPLHCAVINDNEGAAEMLIDTLGASIVNatdsKGRTPLHAAAFTDHVEC 782
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGAdANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD----NGRTALHYAARSGHLEI 76
|
90
....*....|....*
gi 1154884853 783 LQLLLSHNAQVNSVD 797
Cdd:pfam12796 77 VKLLLEKGADINVKD 91
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
153-467 |
3.81e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 79.15 E-value: 3.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 153 PLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIdcgAIVNQ--------------------- 211
Cdd:PHA02878 40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMI---RSINKcsvfytlvaikdafnnrnvei 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 212 ---------KNEKGFTPLHFAAASTHGAL---CLELLVGNGADVNMKSKD-GKTPLHMTALHGRFSRSQTIIQSGAVIDC 278
Cdd:PHA02878 117 fkiiltnryKNIQTIDLVYIDKKSKDDIIeaeITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNI 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 279 EDKNGNTPLHIAARYGHELLINTLITSGADTAKRGIHGMFPLHLAALSGFS-DCCRKLLSSGFDIDTpddfgrtclhaaa 357
Cdd:PHA02878 197 PDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDyDILKLLLEHGVDVNA------------- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 358 aggnleclnlllntgadfnKKDKFGRSPLHYAAAncNYQCLFALVGSGASVNDLDERGCTPLHYAATSDTDGKCLEYL-- 435
Cdd:PHA02878 264 -------------------KSYILGLTALHSSIK--SERKLKLLLEYGADINSLNSYKLTPLSSAVKQYLCINIGRILis 322
|
330 340 350
....*....|....*....|....*....|....*
gi 1154884853 436 ---LRNDANPGIRDKQGYnAVHYSAAYGHRLCLQL 467
Cdd:PHA02878 323 nicLLKRIKPDIKNSEGF-IDNMDCITSNKRLNQI 356
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
616-908 |
5.48e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 79.34 E-value: 5.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 616 LLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQHGAKCLLRDSRGRTPIHLSAACGHIGVLGALLQSAASMDANPAT 695
Cdd:PHA02876 164 LLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDLS 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 696 -------------------------ADNHGYTALHWACYNGH-ETCVELLLEQEVFQKTEG-NAFSPLHCAVINDNEGAA 748
Cdd:PHA02876 244 llkairnedletslllydagfsvnsIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNiKGETPLYLMAKNGYDTEN 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 749 EMLIDTLGASiVNATDSKGRTPLHAAAFTD-HVECLQLLLSHNAQVNSVDSTGKTPLMMAAENGQTNTVEMLVSSAsAEL 827
Cdd:PHA02876 324 IRTLIMLGAD-VNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYG-ADI 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 828 TLQDNSKNTALHLACskgHETSALLILEKITDRNL-INATNAALQTPLHVAARNGLTM-VVQELLGKGASVLAVDENGYT 905
Cdd:PHA02876 402 EALSQKIGTALHFAL---CGTNPYMSVKTLIDRGAnVNSKNKDLSTPLHYACKKNCKLdVIEMLLDNGADVNAINIQNQY 478
|
...
gi 1154884853 906 PAL 908
Cdd:PHA02876 479 PLL 481
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
716-902 |
5.86e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 78.17 E-value: 5.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 716 VELLLEQ--EVFQKTEGNaFSPLH-----CAVINDNEGAAEMLIDtLGASIvNATDSKGRTPLHAAAFT--DHVECLQLL 786
Cdd:PHA03100 51 VKILLDNgaDINSSTKNN-STPLHylsniKYNLTDVKEIVKLLLE-YGANV-NAPDNNGITPLLYAISKksNSYSIVEYL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 787 LSHNAQVNSVDSTGKTPLMMAAENG------------------QTNTVEMLVSSASaELTLQDNSKNTALHLACSKGHET 848
Cdd:PHA03100 128 LDNGANVNIKNSDGENLLHLYLESNkidlkilkllidkgvdinAKNRVNYLLSYGV-PINIKDVYGFTPLHYAVYNNNPE 206
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1154884853 849 SALLILEKITDRNLINATNaalQTPLHVAARNGLTMVVQELLGKGASVLAVDEN 902
Cdd:PHA03100 207 FVKYLLDLGANPNLVNKYG---DTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
254-591 |
9.29e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 77.70 E-value: 9.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 254 LHMTALHGRFSRSQTIIQS-GAVIDCEDKNGNTPLHIAARYGHELLINTLITSGADTAKRGIHGMFPLHLAALSGFSDCC 332
Cdd:PHA02874 5 LRMCIYSGDIEAIEKIIKNkGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 333 RKLLSSGFDI------DTPDDFGRTCLHaaaaggnleclnlllnTGADFNKKDKFGRSPLHYAAANCNYQCLFALVGSGA 406
Cdd:PHA02874 85 KLLIDNGVDTsilpipCIEKDMIKTILD----------------CGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 407 SVNDLDERGCTPLHYAATSDTdGKCLEYLLRNDANPGIRDKQGYNAVHYSAAYGHRLCLQLIAsetpldvlmeTSGTDML 486
Cdd:PHA02874 149 DVNIEDDNGCYPIHIAIKHNF-FDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLI----------DHGNHIM 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 487 SDSDNRATisPLHLAAYHgHHQALEVLVQSlLDLDVRNSSGRTPLDLA-AFKGHVECVDVLINQGASILVKDYiLKRTPI 565
Cdd:PHA02874 218 NKCKNGFT--PLHNAIIH-NRSAIELLINN-ASINDQDIDGSTPLHHAiNPPCDIDIIDILLYHKADISIKDN-KGENPI 292
|
330 340
....*....|....*....|....*..
gi 1154884853 566 HAAATN-GHSECLRLLIGNAEPQNAVD 591
Cdd:PHA02874 293 DTAFKYiNKDPVIKDIIANAVLIKEAD 319
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
136-662 |
1.05e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 78.57 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 136 LVSHGAEvTCKDKK-SYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYG-NTPLHVACY--NGQDVVVNELIDCGAIVNQ 211
Cdd:PHA02876 27 LHKHGAN-QCENESiPFTAIHQALQLRQIDIVEEIIQQNPELIYITDHKcHSTLHTICIipNVMDIVISLTLDCDIILDI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 212 KNEKGFTPLHfaaasTHGALCLELLVG--NGADVNMkSKDGKTPLHMTALHGRFSRSQTIIQSgavidcedkngntplhi 289
Cdd:PHA02876 106 KYASIILNKH-----KLDEACIHILKEaiSGNDIHY-DKINESIEYMKLIKERIQQDELLIAE----------------- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 290 aaryghellinTLITSGADTAKRGIHGMFPLHLAALSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLL 369
Cdd:PHA02876 163 -----------MLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 370 NTGADFNKKDkfgrSPLHYAAANCNYQCLFALVGSGASVNDLDERGCTPLHYAATSDTDGKCLEYLLRNDANPGIRDKQG 449
Cdd:PHA02876 232 DNRSNINKND----LSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLVPKLLERGADVNAKNIKG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 450 YNAVHYSAAYGHRlclqliaSETPLDVLMEtsGTDMlsDSDNRATISPLHLAAYHGHHQALEVLVQSL-LDLDVRNSSGR 528
Cdd:PHA02876 308 ETPLYLMAKNGYD-------TENIRTLIML--GADV--NAADRLYITPLHQASTLDRNKDIVITLLELgANVNARDYCDK 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 529 TPLDLAAFKGHVECVDVLINQGASILVKDYILKrTPIHAA--ATNGHSECLRLLIGNAEpqnaVDIQDGNGQTPLMLSVL 606
Cdd:PHA02876 377 TPIHYAAVRNNVVIINTLLDYGADIEALSQKIG-TALHFAlcGTNPYMSVKTLIDRGAN----VNSKNKDLSTPLHYACK 451
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1154884853 607 NG-HTDCVYSLLNKGANVDAKDKWGRTALHrgAVTGHEECVDALLQHGAKclLRDSR 662
Cdd:PHA02876 452 KNcKLDVIEMLLDNGADVNAINIQNQYPLL--IALEYHGIVNILLHYGAE--LRDSR 504
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
371-628 |
1.31e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 77.40 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 371 TGADFNKKDKFGRSPLHYAA-----ANCNYQCLFALVGSGASVNDLDERGCTPLHYAATSD-TDGKCLEYLLRNDANPGI 444
Cdd:PHA03100 57 NGADINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKKsNSYSIVEYLLDNGANVNI 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 445 RDKQGYNAVHYSAAYGHRlclqliasETPLDVLMETSGTDMlsDSDNRatisplhlaayhghhqaLEVLVQSLLDLDVRN 524
Cdd:PHA03100 137 KNSDGENLLHLYLESNKI--------DLKILKLLIDKGVDI--NAKNR-----------------VNYLLSYGVPINIKD 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 525 SSGRTPLDLAAFKGHVECVDVLINQGASIlvkdyilkrtpihaaatnghseclrllignaepqNAVDIqdgNGQTPLMLS 604
Cdd:PHA03100 190 VYGFTPLHYAVYNNNPEFVKYLLDLGANP----------------------------------NLVNK---YGDTPLHIA 232
|
250 260
....*....|....*....|....
gi 1154884853 605 VLNGHTDCVYSLLNKGANVDAKDK 628
Cdd:PHA03100 233 ILNNNKEIFKLLLNNGPSIKTIIE 256
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
31-308 |
1.27e-13 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 74.49 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 31 LEAVQVLLKHSADVNARDKNWQTPLhiaaankavkCAealvpLLSNVnvsdRAGRTALhhaafsghgEMVKLLLSRGANI 110
Cdd:PHA02798 51 TDIVKLFINLGANVNGLDNEYSTPL----------CT-----ILSNI----KDYKHML---------DIVKILIENGADI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 111 NAFDKKDRRAIHWA---AYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGM---ISVVKYLLDLGVDMNE-PNAYG 183
Cdd:PHA02798 103 NKKNSDGETPLYCLlsnGYINNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINThNNKEK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 184 NTPLHvaCYNGQDV------VVNELIDCGAIVNQKNEkgftplhfAAASTHGALCLELLVGNGA-------------DVN 244
Cdd:PHA02798 183 YDTLH--CYFKYNIdridadILKLFVDNGFIINKENK--------SHKKKFMEYLNSLLYDNKRfkknildfifsyiDIN 252
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1154884853 245 MKSKDGKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGHELLINTLITSGAD 308
Cdd:PHA02798 253 QVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKPN 316
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
556-823 |
3.19e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 72.78 E-value: 3.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 556 KDYILKRTPIHAAATNGHseclrllignaepqnAVDIQDGNGQTPLMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALH 635
Cdd:PHA03100 9 KSRIIKVKNIKYIIMEDD---------------LNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 636 RGAVTGHE-----ECVDALLQHGAKCLLRDSRGRTPIHLSAAC--GHIGVLGALLQSAAsmDANPATADnhGYTALHWA- 707
Cdd:PHA03100 74 YLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGA--NVNIKNSD--GENLLHLYl 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 708 --CYNGHETcVELLLEqevfqktegnafsplHCAVINdNEGAAEMLIdTLGASIvNATDSKGRTPLHAAAFTDHVECLQL 785
Cdd:PHA03100 150 esNKIDLKI-LKLLID---------------KGVDIN-AKNRVNYLL-SYGVPI-NIKDVYGFTPLHYAVYNNNPEFVKY 210
|
250 260 270
....*....|....*....|....*....|....*...
gi 1154884853 786 LLSHNAQVNSVDSTGKTPLMMAAENGQTNTVEMLVSSA 823
Cdd:PHA03100 211 LLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNG 248
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
804-900 |
5.89e-13 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 65.52 E-value: 5.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 804 LMMAAENGQTNTVEMLVSSaSAELTLQDNSKNTALHLACSKGHETSALLILEKItDRNLINATNaalqTPLHVAARNGLT 883
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLEN-GADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKDNGR----TALHYAARSGHL 74
|
90
....*....|....*..
gi 1154884853 884 MVVQELLGKGASVLAVD 900
Cdd:pfam12796 75 EIVKLLLEKGADINVKD 91
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
157-341 |
6.72e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 71.95 E-value: 6.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 157 AASSGMISVVKYLLDLGVDMN--------------------------EPNAYGN-------TPLHVACYNGQDVVVNELI 203
Cdd:PHA02875 9 AILFGELDIARRLLDIGINPNfeiydgispiklamkfrdseaikllmKHGAIPDvkypdieSELHDAVEEGDVKAVEELL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 204 DCGAIVNQK-NEKGFTPLHFAAASTHGALcLELLVGNGADVNMKSKDGKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKN 282
Cdd:PHA02875 89 DLGKFADDVfYKDGMTPLHLATILKKLDI-MKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCC 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 283 GNTPLHIAARYGHELLINTLITSGADTAKRGIHGMFPLHLAALSGFS-DCCRKLLSSGFD 341
Cdd:PHA02875 168 GCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKiDIVRLFIKRGAD 227
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
254-346 |
7.74e-13 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 65.14 E-value: 7.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 254 LHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGHELLINTLITSGAdtAKRGIHGMFPLHLAALSGFSDCCR 333
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1154884853 334 KLLSSGFDIDTPD 346
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
647-901 |
8.19e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 72.40 E-value: 8.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 647 DALLQHGAKCLLRDSRGRTPIHLSAACGHIGVLGALLQSAAsmDANPATADnhGYTALHWACYNGHETCVELLLEQEvfQ 726
Cdd:PHA02876 162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGA--DVNIIALD--DLSVLECAVDSKNIDTIKAIIDNR--S 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 727 KTEGNAFSPLHcAVINDNEGAAEMLIDTlGASiVNATDSKGRTPLHAAAFTDHVECL-QLLLSHNAQVNSVDSTGKTPLM 805
Cdd:PHA02876 236 NINKNDLSLLK-AIRNEDLETSLLLYDA-GFS-VNSIDDCKNTPLHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLY 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 806 MAAENG-QTNTVEMLVSSAsAELTLQDNSKNTALHLACSKGHETSALLILEKITDRnlINATNAALQTPLHVAARNGLTM 884
Cdd:PHA02876 313 LMAKNGyDTENIRTLIMLG-ADVNAADRLYITPLHQASTLDRNKDIVITLLELGAN--VNARDYCDKTPIHYAAVRNNVV 389
|
250
....*....|....*..
gi 1154884853 885 VVQELLGKGASVLAVDE 901
Cdd:PHA02876 390 IINTLLDYGADIEALSQ 406
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
481-667 |
8.38e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 71.53 E-value: 8.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 481 SGTDMlsDSDNRATISPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPLDLAAFKGHVECVDVLINQGASILVKDYIL 560
Cdd:PHA02874 113 CGIDV--NIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNG 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 561 KrTPIHAAATNGHSECLRLLIGNAepqNAVDIQDGNGQTPLMLSVLngHTDCVYSLLNKGANVDAKDKWGRTALHRG-AV 639
Cdd:PHA02874 191 E-SPLHNAAEYGDYACIKLLIDHG---NHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAiNP 264
|
170 180
....*....|....*....|....*...
gi 1154884853 640 TGHEECVDALLQHGAKCLLRDSRGRTPI 667
Cdd:PHA02874 265 PCDIDIIDILLYHKADISIKDNKGENPI 292
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
53-245 |
1.26e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 70.79 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 53 TPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLLSRGANIN-AFDKKDRRAIHWAAYMGHIE 131
Cdd:PHA02875 37 SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 132 VVKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGAIVNQ 211
Cdd:PHA02875 117 IMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDY 196
|
170 180 190
....*....|....*....|....*....|....
gi 1154884853 212 KNEKGFTPLHFAAASTHGALCLELLVGNGADVNM 245
Cdd:PHA02875 197 FGKNGCVAALCYAIENNKIDIVRLFIKRGADCNI 230
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
31-203 |
1.70e-12 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 71.20 E-value: 1.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 31 LEAVQVLLK-HSADVNARDKNWQTPLHIAAANKAVKCAEAL---VPLLSNVNV-SD-RAGRTALHHAAFSGHGEMVKLLL 104
Cdd:cd22192 30 VQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLmeaAPELVNEPMtSDlYQGETALHIAVVNQNLNLVRELI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 105 SRGANIN-------AFDKKDRRAIHW-------AAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLL 170
Cdd:cd22192 110 ARGADVVspratgtFFRPGPKNLIYYgehplsfAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFACQMY 189
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1154884853 171 DLGVDMNE----------PNAYGNTPLHVACYNGQDVVVNELI 203
Cdd:cd22192 190 DLILSYDKeddlqpldlvPNNQGLTPFKLAAKEGNIVMFQHLV 232
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
320-412 |
2.47e-12 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 63.60 E-value: 2.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 320 LHLAALSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTgADFNKKDKfGRSPLHYAAANCNYQCLF 399
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1154884853 400 ALVGSGASVNDLD 412
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
130-356 |
2.60e-12 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 70.25 E-value: 2.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 130 IEVVKLLVSHGAEVTCKDKKSYTPLHAAASS-----GMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGqdvVVNEL-- 202
Cdd:PHA02798 51 TDIVKLFINLGANVNGLDNEYSTPLCTILSNikdykHMLDIVKILIENGADINKKNSDGETPLYCLLSNG---YINNLei 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 203 ----IDCGAIVNQKNEKGFTPLHFAAASTHGAL--CLELLVGNGADVNMKSKDGKtplhMTALHGRFSRS---------Q 267
Cdd:PHA02798 128 llfmIENGADTTLLDKDGFTMLQVYLQSNHHIDieIIKLLLEKGVDINTHNNKEK----YDTLHCYFKYNidridadilK 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 268 TIIQSGAVIDCEDKNGNTPLhiaARYGHELLINT---------LITSGADTAKRGIHGMFPLHLAALSGFSDCCRKLLSS 338
Cdd:PHA02798 204 LFVDNGFIINKENKSHKKKF---MEYLNSLLYDNkrfkknildFIFSYIDINQVDELGFNPLYYSVSHNNRKIFEYLLQL 280
|
250
....*....|....*...
gi 1154884853 339 GFDIDTPDDFGRTCLHAA 356
Cdd:PHA02798 281 GGDINIITELGNTCLFTA 298
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
84-137 |
9.16e-12 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 60.75 E-value: 9.16e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1154884853 84 GRTALHHAAFSGHGEMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLV 137
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
220-308 |
1.22e-11 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 61.67 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 220 LHFAAASTHgALCLELLVGNGADVNMKSKDGKTPLHMTALHGRFSRSQTIIQSgAVIDCEDkNGNTPLHIAARYGHELLI 299
Cdd:pfam12796 1 LHLAAKNGN-LELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77
|
....*....
gi 1154884853 300 NTLITSGAD 308
Cdd:pfam12796 78 KLLLEKGAD 86
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
541-805 |
1.37e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 67.68 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 541 ECVDVLINQGASILVKDYILKrTPIHAAATNGHSECLRLLIgnaEPQNAVDIQDGNGQTPLMLSVLNGHTDCVYSLLNKG 620
Cdd:PHA02874 105 DMIKTILDCGIDVNIKDAELK-TFLHYAIKKGDLESIKMLF---EYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKG 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 621 ANVDAKDKWGRTALHRGAVTGHEECVDALLQHGAkcllrdsrgrtpiHLSAACghigvlgallqsaasmdanpatadNHG 700
Cdd:PHA02874 181 AYANVKDNNGESPLHNAAEYGDYACIKLLIDHGN-------------HIMNKC------------------------KNG 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 701 YTALHWAC-YNghETCVELLLEQEVFQKTEGNAFSPLHCAVindNEGAAEMLIDTL--GASIVNATDSKGRTPLHAA-AF 776
Cdd:PHA02874 224 FTPLHNAIiHN--RSAIELLINNASINDQDIDGSTPLHHAI---NPPCDIDIIDILlyHKADISIKDNKGENPIDTAfKY 298
|
250 260
....*....|....*....|....*....
gi 1154884853 777 TDHVECLQLLLSHNAQVNSVDSTGKTPLM 805
Cdd:PHA02874 299 INKDPVIKDIIANAVLIKEADKLKDSDFL 327
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
37-182 |
2.04e-11 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 67.97 E-value: 2.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 37 LLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLLSRGANINAFDKK 116
Cdd:PLN03192 544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAG 623
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1154884853 117 DrrAIHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAY 182
Cdd:PLN03192 624 D--LLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTD 687
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
187-280 |
4.01e-11 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 60.13 E-value: 4.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 187 LHVACYNGQDVVVNELIDCGAIVNQKNEKGFTPLHFAAASTHGALCLELLvgNGADVNMKSkDGKTPLHMTALHGRFSRS 266
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL--EHADVNLKD-NGRTALHYAARSGHLEIV 77
|
90
....*....|....
gi 1154884853 267 QTIIQSGAVIDCED 280
Cdd:pfam12796 78 KLLLEKGADINVKD 91
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
573-782 |
4.39e-11 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 67.20 E-value: 4.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 573 HSECLRLLIGNAEPQNAVDIQDGNGQTPLMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQH 652
Cdd:PLN03192 501 HKELHDLNVGDLLGDNGGEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKH 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 653 GAKCLLRDSRGRTPIHLSAACGHIGVLGALLQSAASMDANPA---------------------------TADNHGYTALH 705
Cdd:PLN03192 581 ACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAgdllctaakrndltamkellkqglnvdSEDHQGATALQ 660
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 706 WACYNGHETCVELLLEQ--EVFQKTEGNAFSPLHC-AVINDNE-GAAEMLIDTLGASIVNATDSKGRTPLHAAAFTDHVE 781
Cdd:PLN03192 661 VAMAEDHVDMVRLLIMNgaDVDKANTDDDFSPTELrELLQKRElGHSITIVDSVPADEPDLGRDGGSRPGRLQGTSSDNQ 740
|
.
gi 1154884853 782 C 782
Cdd:PLN03192 741 C 741
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
118-170 |
4.59e-11 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 58.83 E-value: 4.59e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1154884853 118 RRAIHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLL 170
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
496-547 |
1.61e-10 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 57.28 E-value: 1.61e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1154884853 496 SPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPLDLAAFKGHVECVDVLI 547
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
30-178 |
1.80e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 65.08 E-value: 1.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 30 YLEAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHGEM-VKLLLSRGA 108
Cdd:PHA02876 354 NKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGA 433
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154884853 109 NINAFDKKDRRAIHWAAYMG-HIEVVKLLVSHGAEVTCKDKKSYTPLHAAAssGMISVVKYLLDLGVDMNE 178
Cdd:PHA02876 434 NVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGAELRD 502
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
8-254 |
2.77e-10 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 64.09 E-value: 2.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 8 KSEPHCTPQLTLEMQKSLnflfyLEAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSN---VNVSDRAG 84
Cdd:PHA02798 71 YSTPLCTILSNIKDYKHM-----LDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLFMIENgadTTLLDKDG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 85 RTALHHAAFSGHG---EMVKLLLSRGANINAFDkkdrraiHWAAYmghievvkllvshgAEVTCKDKKSYTPLHAaassg 161
Cdd:PHA02798 146 FTMLQVYLQSNHHidiEIIKLLLEKGVDINTHN-------NKEKY--------------DTLHCYFKYNIDRIDA----- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 162 miSVVKYLLDLGVDMNEPNAYGNTP----LHVACYNGQDVVVN--ELIDCGAIVNQKNEKGFTPLHFAAASTHGALClEL 235
Cdd:PHA02798 200 --DILKLFVDNGFIINKENKSHKKKfmeyLNSLLYDNKRFKKNilDFIFSYIDINQVDELGFNPLYYSVSHNNRKIF-EY 276
|
250
....*....|....*....
gi 1154884853 236 LVGNGADVNMKSKDGKTPL 254
Cdd:PHA02798 277 LLQLGGDINIITELGNTCL 295
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
386-470 |
4.73e-10 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 57.05 E-value: 4.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 386 LHYAAANCNYQCLFALVGSGASVNDLDERGCTPLHYAATSDTDgKCLEYLLRNdANPGIRDkQGYNAVHYSAAYGHRLCL 465
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHL-EIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77
|
....*
gi 1154884853 466 QLIAS 470
Cdd:pfam12796 78 KLLLE 82
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
760-920 |
4.73e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 63.06 E-value: 4.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 760 VNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLMMAAENGQTNTVEMLVSSAsAELTLQDNSKNTALH 839
Cdd:PHA02874 117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKG-AYANVKDNNGESPLH 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 840 LACSKGHETSALLILEKITdrNLINATNAALqTPLHVAARNGLTMVvqELLGKGASVLAVDENGYTP---ALACAPNKDV 916
Cdd:PHA02874 196 NAAEYGDYACIKLLIDHGN--HIMNKCKNGF-TPLHNAIIHNRSAI--ELLINNASINDQDIDGSTPlhhAINPPCDIDI 270
|
....
gi 1154884853 917 ADCL 920
Cdd:PHA02874 271 IDIL 274
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
151-195 |
4.85e-10 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 55.74 E-value: 4.85e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1154884853 151 YTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQ 195
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGN 46
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
510-691 |
5.89e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 62.76 E-value: 5.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 510 LEVLVQSLLDLDVRNSSGRTPLDLAAFK--GHVECVDVLINQGASILVKDYILKrTPIHAAATNGH--SECLRLLIgnae 585
Cdd:PHA03100 89 VKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGE-NLLHLYLESNKidLKILKLLI---- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 586 pQNAVDIqdgngqtplmlsvlNGhTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQHGAKCLLRDSRGRT 665
Cdd:PHA03100 164 -DKGVDI--------------NA-KNRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDT 227
|
170 180
....*....|....*....|....*.
gi 1154884853 666 PIHLSAACGHIGVLGALLQSAASMDA 691
Cdd:PHA03100 228 PLHIAILNNNKEIFKLLLNNGPSIKT 253
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
634-906 |
5.91e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 62.98 E-value: 5.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 634 LHRGAVTGHEECVDALLQHGAKCLLRDSRGRTPIHLsaACGHIGVLGA--LLQSAasmdanpaTADNHGYT--ALHWACY 709
Cdd:PHA02878 41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHI--ICKEPNKLGMkeMIRSI--------NKCSVFYTlvAIKDAFN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 710 NGHETCVELLLeqevFQKTEGNAFSPLHCAVINDNEGAAEMLIDTL----GASIVNATDSKGRTPLHAAAFTDHVECLQL 785
Cdd:PHA02878 111 NRNVEIFKIIL----TNRYKNIQTIDLVYIDKKSKDDIIEAEITKLllsyGADINMKDRHKGNTALHYATENKDQRLTEL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 786 LLSHNAQVNSVDSTGKTPLMMAAENGQTNTVEMLVSSAsAELTLQDNSKNTALHLACSKGHETSAL-LILEKITDrnlIN 864
Cdd:PHA02878 187 LLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENG-ASTDARDKCGNTPLHISVGYCKDYDILkLLLEHGVD---VN 262
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1154884853 865 ATNAALQ-TPLHVAARNglTMVVQELLGKGASVLAVDENGYTP 906
Cdd:PHA02878 263 AKSYILGlTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTP 303
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
748-913 |
8.10e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 62.77 E-value: 8.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 748 AEMLIDtlGASIVNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLMMAAENGQTNTVEMLVSSAS--- 824
Cdd:PHA02876 161 AEMLLE--GGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSnin 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 825 -AELTLQDNSKNTALhlacskghETSALLILEKITdrnlINATNAALQTPLHVAARN-GLTMVVQELLGKGASVLAVDEN 902
Cdd:PHA02876 239 kNDLSLLKAIRNEDL--------ETSLLLYDAGFS----VNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIK 306
|
170
....*....|.
gi 1154884853 903 GYTPALACAPN 913
Cdd:PHA02876 307 GETPLYLMAKN 317
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
230-444 |
8.47e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 61.93 E-value: 8.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 230 ALCLELLVGN----------GADVNMKSKDGKTPLHMTAlhgRFSRSQTI---IQSGAVIDCEDKNGNTPLHIAARYGHE 296
Cdd:PHA02875 5 ALCDAILFGEldiarrlldiGINPNFEIYDGISPIKLAM---KFRDSEAIkllMKHGAIPDVKYPDIESELHDAVEEGDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 297 LLINTLITSGA---DTAKRgiHGMFPLHLAALSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGA 373
Cdd:PHA02875 82 KAVEELLDLGKfadDVFYK--DGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154884853 374 DFNKKDKFGRSPLHYAAANCNYQCLFALVGSGASVNDLDERGCTPLHYAATSDTDGKCLEYLLRNDANPGI 444
Cdd:PHA02875 160 CLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGADCNI 230
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
490-721 |
9.27e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 62.20 E-value: 9.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 490 DNRATiSPLHLAAYHGHHQALEVLVQSLLDLDVRNSsgRTPLDLAAFKGHVECVD-VLINQGASILVKDYILKRTPIHAA 568
Cdd:PHA02878 67 DHRDL-TPLHIICKEPNKLGMKEMIRSINKCSVFYT--LVAIKDAFNNRNVEIFKiILTNRYKNIQTIDLVYIDKKSKDD 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 569 ATNghSECLRLLIGNAEPQNAVDIQDGNgqTPLMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDA 648
Cdd:PHA02878 144 IIE--AEITKLLLSYGADINMKDRHKGN--TALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHI 219
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1154884853 649 LLQHGAKCLLRDSRGRTPIHLSAA-CGHIGVLGALLQSAASMDANPATAdnhGYTALHWACYNghETCVELLLE 721
Cdd:PHA02878 220 LLENGASTDARDKCGNTPLHISVGyCKDYDILKLLLEHGVDVNAKSYIL---GLTALHSSIKS--ERKLKLLLE 288
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
31-142 |
1.26e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 61.55 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 31 LEAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLLSRGANI 110
Cdd:PHA02875 115 LDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANI 194
|
90 100 110
....*....|....*....|....*....|...
gi 1154884853 111 NAFDKK-DRRAIHWAAYMGHIEVVKLLVSHGAE 142
Cdd:PHA02875 195 DYFGKNgCVAALCYAIENNKIDIVRLFIKRGAD 227
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
419-524 |
1.36e-09 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 55.89 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 419 LHYAATSDtDGKCLEYLLRNDANPGIRDKQGYNAVHYSAAYGHRLCLQLIASETPLDvlMETSGTdmlsdsdnratiSPL 498
Cdd:pfam12796 1 LHLAAKNG-NLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN--LKDNGR------------TAL 65
|
90 100
....*....|....*....|....*.
gi 1154884853 499 HLAAYHGHHQALEVLVQSLLDLDVRN 524
Cdd:pfam12796 66 HYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
529-669 |
1.52e-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: 61.95 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 529 TPLDLAAFKGHVECVDVLINQGASILVKDYILKRTPIHAAATNGHSECLRLLIGNA-----EPQNAVDIQdgnGQTPLML 603
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAApelvnEPMTSDLYQ---GETALHI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 604 SVLNGHTDCVYSLLNKGANV--------------DAKDKWGRTALHRGAVTGHEECVDALLQHGAKCLLRDSRGRTPIHL 669
Cdd:cd22192 96 AVVNQNLNLVRELIARGADVvspratgtffrpgpKNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
527-722 |
1.80e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 61.16 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 527 GRTPLDLAAFKGHVECVDVLINQGASILVKdYILKRTPIHAAATNGHSECLRLLIGNAEPQNAVDIQDGNgqTPLMLSVL 606
Cdd:PHA02875 35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVK-YPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGM--TPLHLATI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 607 NGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQHGAKCLLRDSRGRTPIHLSAACGHIGVLGALLQSA 686
Cdd:PHA02875 112 LKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSG 191
|
170 180 190
....*....|....*....|....*....|....*.
gi 1154884853 687 ASMDanpATADNHGYTALHWACYNGHETCVELLLEQ 722
Cdd:PHA02875 192 ANID---YFGKNGCVAALCYAIENNKIDIVRLFIKR 224
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
152-289 |
2.66e-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: 61.18 E-value: 2.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 152 TPLHAAASSGMISVVKYLLDL-GVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCG-AIVNQKNE----KGFTPLHFAAA 225
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLMEAApELVNEPMTsdlyQGETALHIAVV 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1154884853 226 STHGALcLELLVGNGADVN---------MKSKD-----GKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHI 289
Cdd:cd22192 99 NQNLNL-VRELIARGADVVspratgtffRPGPKnliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
88-170 |
3.37e-09 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 60.68 E-value: 3.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 88 LHHAAFSGHGEMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVK 167
Cdd:PTZ00322 86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165
|
...
gi 1154884853 168 YLL 170
Cdd:PTZ00322 166 LLS 168
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
401-606 |
3.62e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 60.28 E-value: 3.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 401 LVGSGASVNDLDE-RGCTPLHYAATsDTDGKCLEYLLRNDANPGIRDKqgynavhysaayghrlclqliasetpldvlme 479
Cdd:PHA02878 153 LLSYGADINMKDRhKGNTALHYATE-NKDQRLTELLLSYGANVNIPDK-------------------------------- 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 480 tsgtdmlsdSDNratiSPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPLDLAAfkGHVECVDV---LINQGASILVK 556
Cdd:PHA02878 200 ---------TNN----SPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISV--GYCKDYDIlklLLEHGVDVNAK 264
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1154884853 557 DYILKRTPIHAAAtngHSE-CLRLLIGNAEPQNAVDIQDgngQTPLMLSVL 606
Cdd:PHA02878 265 SYILGLTALHSSI---KSErKLKLLLEYGADINSLNSYK---LTPLSSAVK 309
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
34-220 |
6.07e-09 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 59.68 E-value: 6.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 34 VQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHG--EMVKLLLSRGANIN 111
Cdd:PHA02946 55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEviERINLLVQYGAKIN 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 112 AFDKKDRRAIHWAAYMGHIEVVKLLVSHGAEVTCKDK--KSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHV 189
Cdd:PHA02946 135 NSVDEEGCGPLLACTDPSERVFKKIMSIGFEARIVDKfgKNHIHRHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHI 214
|
170 180 190
....*....|....*....|....*....|..
gi 1154884853 190 ACYNG-QDVVVNELIDCGAIVNQKNEKGFTPL 220
Cdd:PHA02946 215 VCSKTvKNVDIINLLLPSTDVNKQNKFGDSPL 246
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
53-104 |
7.89e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 52.66 E-value: 7.89e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1154884853 53 TPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLL 104
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
767-820 |
8.53e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 52.28 E-value: 8.53e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1154884853 767 GRTPLHAAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLMMAAENGQTNTVEMLV 820
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
91-249 |
1.20e-08 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 59.11 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 91 AAFSGHGEMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLL 170
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY 611
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1154884853 171 DLGvDMNEPNAYGNTpLHVACYNGQDVVVNELIDCGAIVNQKNEKGFTPLHFAAASTHGALcLELLVGNGADVNMKSKD 249
Cdd:PLN03192 612 HFA-SISDPHAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDM-VRLLIMNGADVDKANTD 687
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
30-145 |
1.87e-08 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 58.34 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 30 YLEAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSnvnVSD-RAGRTALHHAAFSGHGEMVKLLLSRGA 108
Cdd:PLN03192 570 YEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFAS---ISDpHAAGDLLCTAAKRNDLTAMKELLKQGL 646
|
90 100 110
....*....|....*....|....*....|....*..
gi 1154884853 109 NINAFDKKDRRAIHWAAYMGHIEVVKLLVSHGAEVTC 145
Cdd:PLN03192 647 NVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDK 683
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
389-637 |
1.97e-08 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 58.34 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 389 AAANCNYQCLFALVGSGASVNDLDERGCTPLHYAATSDTDgKCLEYLLRNDANPGIRDKQGYNAVHYSAAYGHrlclqli 468
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYE-DCVLVLLKHACNVHIRDANGNTALWNAISAKH------- 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 469 asETPLDVLMETSgtdmlSDSDNRATISPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPLDLAAFKGHVECVDVLIN 548
Cdd:PLN03192 604 --HKIFRILYHFA-----SISDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIM 676
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 549 QGASIlvkdyilkrtpIHAAATNGHS-ECLRLLIGNAEPQNAVDIQDGNGQTPLMLSVLNGHTDCvySLLNKGANvdaKD 627
Cdd:PLN03192 677 NGADV-----------DKANTDDDFSpTELRELLQKRELGHSITIVDSVPADEPDLGRDGGSRPG--RLQGTSSD---NQ 740
|
250
....*....|
gi 1154884853 628 KWGRTALHRG 637
Cdd:PLN03192 741 CRPRVSIYKG 750
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
723-834 |
1.98e-08 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 58.37 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 723 EVFQKTEGNAFSPLHCAVIND--NEGAAEMLI----------DTLGASIV-------NATDSKGRTPLHAAAFTDHVECL 783
Cdd:PTZ00322 52 EALEATENKDATPDHNLTTEEviDPVVAHMLTvelcqlaasgDAVGARILltggadpNCRDYDGRTPLHIACANGHVQVV 131
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1154884853 784 QLLLSHNAQVNSVDSTGKTPLMMAAENGQTNTVEMLVSSASAELTLQDNSK 834
Cdd:PTZ00322 132 RVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGANAK 182
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
527-581 |
2.34e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 51.12 E-value: 2.34e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1154884853 527 GRTPLDLAAFKGHVECVDVLINQGASILVKDYiLKRTPIHAAATNGHSECLRLLI 581
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDG-NGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
736-906 |
3.27e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 57.28 E-value: 3.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 736 LHCAVINDNEGAAEMLIDtLGASiVNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLMMAAENGQTNT 815
Cdd:PHA02874 128 LHYAIKKGDLESIKMLFE-YGAD-VNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYAC 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 816 VEMLVSSASaELTLQDNSKNTALHLACSkgHETSALLILekITDRNlINATNAALQTPLHVAARNGLTM-VVQELLGKGA 894
Cdd:PHA02874 206 IKLLIDHGN-HIMNKCKNGFTPLHNAII--HNRSAIELL--INNAS-INDQDIDGSTPLHHAINPPCDIdIIDILLYHKA 279
|
170
....*....|..
gi 1154884853 895 SVLAVDENGYTP 906
Cdd:PHA02874 280 DISIKDNKGENP 291
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
704-876 |
3.28e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 56.92 E-value: 3.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 704 LHWACYNGHETCVELLLE-----QEVFQKtEGNafSPLHCAVINDNEGAAEMLIDTLGASIVNATDSKgrTPLHAAAFTD 778
Cdd:PHA02875 72 LHDAVEEGDVKAVEELLDlgkfaDDVFYK-DGM--TPLHLATILKKLDIMKLLIARGADPDIPNTDKF--SPLHLAVMMG 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 779 HVECLQLLLSHNAQVNSVDSTGKTPLMMAAENGQTNTVEMLVSSASAELTLQDNSKNTALHLACSKGHETSALLILEKIT 858
Cdd:PHA02875 147 DIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGA 226
|
170
....*....|....*...
gi 1154884853 859 DRNLINATNAALQTPLHV 876
Cdd:PHA02875 227 DCNIMFMIEGEECTILDM 244
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
518-741 |
4.27e-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: 4.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 518 LDLDVRNSSGRTPLDLAAFKG-HVECVDVLINQGASILVKDyilkrTPIHAAATNGH---SECLRLLIGNAE----PQNA 589
Cdd:TIGR00870 43 LNINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAVGD-----TLLHAISLEYVdavEAILLHLLAAFRksgpLELA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 590 VDIQDGN---GQTPLMLSVLNGHTDCVYSLLNKGANVDAKDK--------------WGRTALHRGAVTGHEECVDALLQH 652
Cdd:TIGR00870 118 NDQYTSEftpGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSED 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 653 GAKCLLRDSRGRTPIHLSAACGHIGVLGALL-----QSAASMDANPATAD------NH-GYTALHWACYNGHETCVELLL 720
Cdd:TIGR00870 198 PADILTADSLGNTLLHLLVMENEFKAEYEELscqmyNFALSLLDKLRDSKelevilNHqGLTPLKLAAKEGRIVLFRLKL 277
|
250 260
....*....|....*....|..
gi 1154884853 721 EQEVFQKT-EGNAFSPLHCAVI 741
Cdd:TIGR00870 278 AIKYKQKKfVAWPNGQQLLSLY 299
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
26-194 |
4.63e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 54.44 E-value: 4.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 26 NFLFY------LEAVQvllKHSADVNARDKNWQTPLHIAAANKAV--KCAEALVPLLSNVNVSDRA-GRTALHHAAFSGH 96
Cdd:PHA02859 23 NPLFYyvekddIEGVK---KWIKFVNDCNDLYETPIFSCLEKDKVnvEILKFLIENGADVNFKTRDnNLSALHHYLSFNK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 97 G---EMVKLLLSRGANINAFDKKDRRAIHwaAYMGH----IEVVKLLVSHGAEVTCKDKK------SYTPLHAAASsgmi 163
Cdd:PHA02859 100 NvepEILKILIDSGSSITEEDEDGKNLLH--MYMCNfnvrINVIKLLIDSGVSFLNKDFDnnnilySYILFHSDKK---- 173
|
170 180 190
....*....|....*....|....*....|.
gi 1154884853 164 sVVKYLLDLGVDMNEPNAYGNTPLHVACYNG 194
Cdd:PHA02859 174 -IFDFLTSLGIDINETNKSGYNCYDLIKFRN 203
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
133-205 |
4.86e-08 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 56.83 E-value: 4.86e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1154884853 133 VKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDC 205
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
127-318 |
5.19e-08 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 57.19 E-value: 5.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 127 MGHIEVVKLLVSHGAEVTckDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCG 206
Cdd:PLN03192 504 LHDLNVGDLLGDNGGEHD--DPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 207 AIVNQKNEKGFTPLHFAAASTHGALcLELLVGNGADVNMKSkdGKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTP 286
Cdd:PLN03192 582 CNVHIRDANGNTALWNAISAKHHKI-FRILYHFASISDPHA--AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATA 658
|
170 180 190
....*....|....*....|....*....|..
gi 1154884853 287 LHIAARYGHELLINTLITSGADTAKRGIHGMF 318
Cdd:PLN03192 659 LQVAMAEDHVDMVRLLIMNGADVDKANTDDDF 690
|
|
| PHA02989 |
PHA02989 |
ankyrin repeat protein; Provisional |
34-271 |
5.19e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222954 [Multi-domain] Cd Length: 494 Bit Score: 56.67 E-value: 5.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 34 VQVLLKHSADVNARDKNWQTPLhiaaankavkcaealVPLLSNVNVSDRagrtalhhaafsghgEMVKLLLSRGANINaf 113
Cdd:PHA02989 91 VKLLLKFGADINLKTFNGVSPI---------------VCFIYNSNINNC---------------DMLRFLLSKGINVN-- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 114 DKKDRRA-----IHWAAYMGHIEVVKLLVSHGaeVTCKDKKSY---TPLHAAASSGM----ISVVKYLLDLGVDMNEPNA 181
Cdd:PHA02989 139 DVKNSRGynllhMYLESFSVKKDVIKILLSFG--VNLFEKTSLyglTPMNIYLRNDIdvisIKVIKYLIKKGVNIETNNN 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 182 YGNTPL------HVACYNGQDVVVNeLIDCGAIVNQKNEKGFTPLHFAA-ASTHGALCLELLVGNgaDVNMKSKDGKTPL 254
Cdd:PHA02989 217 GSESVLesfldnNKILSKKEFKVLN-FILKYIKINKKDKKGFNPLLISAkVDNYEAFNYLLKLGD--DIYNVSKDGDTVL 293
|
250
....*....|....*..
gi 1154884853 255 HMTALHGRFSRSQTIIQ 271
Cdd:PHA02989 294 TYAIKHGNIDMLNRILQ 310
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
630-683 |
5.54e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 49.97 E-value: 5.54e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1154884853 630 GRTALHRGAVTGHEECVDALLQHGAKCLLRDSRGRTPIHLSAACGHIGVLGALL 683
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
223-377 |
5.90e-08 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 56.80 E-value: 5.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 223 AAASTHGALCLELLVGNGADVNMKSKDGKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGHELLINTL 302
Cdd:PLN03192 531 TVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1154884853 303 --ITSGADTAKRGIhgmfPLHLAALSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGADFNK 377
Cdd:PLN03192 611 yhFASISDPHAAGD----LLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDK 683
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
649-822 |
6.36e-08 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 56.56 E-value: 6.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 649 LLQHGAKCLLRDSRGRTPIHLSAACGHIGVLGALLQSAASMDANPATADNH-GYTALHWACYNGHETCVELLLEQ----- 722
Cdd:cd22192 37 LKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMTSDLYqGETALHIAVVNQNLNLVRELIARgadvv 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 723 ------EVFQKTEGNAF----SPLHCAVINDNEGAAEMLIDTlGASIVnATDSKGRTPLHAAAF----TDHVECLQLLLS 788
Cdd:cd22192 117 spratgTFFRPGPKNLIyygeHPLSFAACVGNEEIVRLLIEH-GADIR-AQDSLGNTVLHILVLqpnkTFACQMYDLILS 194
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1154884853 789 HNAQVNSV------DSTGKTPLMMAAENGQTNTVEMLVSS 822
Cdd:cd22192 195 YDKEDDLQpldlvpNNQGLTPFKLAAKEGNIVMFQHLVQK 234
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
34-105 |
6.90e-08 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 56.45 E-value: 6.90e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1154884853 34 VQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLLS 105
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
764-892 |
9.21e-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: 56.31 E-value: 9.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 764 DSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDST--------------GKTPLMMAAENGQTNTVEMLVSSASAELTL 829
Cdd:cd22194 138 AYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEIVQLLMEKESTDITS 217
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1154884853 830 QDNSKNTALHLAC-----SKGHETSAL----LILEKITDRNLINATNAALQTPLHVAARNGLTMVVQELLGK 892
Cdd:cd22194 218 QDSRGNTVLHALVtvaedSKTQNDFVKrmydMILLKSENKNLETIRNNEGLTPLQLAAKMGKAEILKYILSR 289
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
736-892 |
1.01e-07 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 55.79 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 736 LHCAVINDNEGAAEMLIDTLGASIVNATDS---KGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDST------------- 799
Cdd:cd22192 55 LHVAALYDNLEAAVVLMEAAPELVNEPMTSdlyQGETALHIAVVNQNLNLVRELIARGADVVSPRATgtffrpgpknliy 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 800 -GKTPLMMAAENGQTNTVEMLVsSASAELTLQDNSKNTALHLACSKGHETSA------LLILEK-ITDRNLINATNAALQ 871
Cdd:cd22192 135 yGEHPLSFAACVGNEEIVRLLI-EHGADIRAQDSLGNTVLHILVLQPNKTFAcqmydlILSYDKeDDLQPLDLVPNNQGL 213
|
170 180
....*....|....*....|.
gi 1154884853 872 TPLHVAARNGLTMVVQELLGK 892
Cdd:cd22192 214 TPFKLAAKEGNIVMFQHLVQK 234
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
761-923 |
1.13e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 55.38 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 761 NATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLMMAAENGQTNTVEMLVSSASAELTLQDNSKNTALHL 840
Cdd:PHA02875 29 NFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 841 AC-SKGHETSALLILEKiTDRNLINATNAalqTPLHVAARNGLTMVVQELLGKGASVLAVDENGYTPALACAPNKDVADC 919
Cdd:PHA02875 109 ATiLKKLDIMKLLIARG-ADPDIPNTDKF---SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAIC 184
|
....
gi 1154884853 920 LALI 923
Cdd:PHA02875 185 KMLL 188
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
382-436 |
2.43e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 48.42 E-value: 2.43e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1154884853 382 GRSPLHYAAANCNYQCLFALVGSGASVNDLDERGCTPLHYAATSDtDGKCLEYLL 436
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNG-NVEVLKLLL 54
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
734-925 |
2.78e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 54.23 E-value: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 734 SPLHCAVINDNEGAAEMLIDtLGASIVNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLMMAAENGQT 813
Cdd:PHA02875 70 SELHDAVEEGDVKAVEELLD-LGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 814 NTVEMLVSsasaeltlqdnskntalHLACskghetsallilekitdrnlINATNAALQTPLHVAARNGLTMVVQELLGKG 893
Cdd:PHA02875 149 KGIELLID-----------------HKAC--------------------LDIEDCCGCTPLIIAMAKGDIAICKMLLDSG 191
|
170 180 190
....*....|....*....|....*....|..
gi 1154884853 894 ASVLAVDENGYTPALACAPNKDVADCLALILA 925
Cdd:PHA02875 192 ANIDYFGKNGCVAALCYAIENNKIDIVRLFIK 223
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
746-906 |
2.85e-07 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 54.49 E-value: 2.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 746 GAAEMLIDTLGASI-VNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLMMAAENGQTNTVEMLVSSAS 824
Cdd:PLN03192 536 GNAALLEELLKAKLdPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFAS 615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 825 AeltlqdNSKNTALHLACSKGHETSaLLILEKITDRNL-INATNAALQTPLHVAARNGLTMVVQELLGKGASVLAVD-EN 902
Cdd:PLN03192 616 I------SDPHAAGDLLCTAAKRND-LTAMKELLKQGLnVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANtDD 688
|
....
gi 1154884853 903 GYTP 906
Cdd:PLN03192 689 DFSP 692
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
596-843 |
2.92e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 53.84 E-value: 2.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 596 NGQTPLMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQHGAkcLLRD---SRGRTPIHLSAA 672
Cdd:PHA02875 34 DGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK--FADDvfyKDGMTPLHLATI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 673 CGHIGVLGALLQSAASMDAnPATadnhgytalhwacynghetcvellleqevfqktegNAFSPLHCAVINDNEGAAEMLI 752
Cdd:PHA02875 112 LKKLDIMKLLIARGADPDI-PNT-----------------------------------DKFSPLHLAVMMGDIKGIELLI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 753 DTlgASIVNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLM-MAAENGQTNTVEMLVS--SASAELTL 829
Cdd:PHA02875 156 DH--KACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcYAIENNKIDIVRLFIKrgADCNIMFM 233
|
250
....*....|....
gi 1154884853 830 QDNSKNTALHLACS 843
Cdd:PHA02875 234 IEGEECTILDMICN 247
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
150-308 |
4.57e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 51.74 E-value: 4.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 150 SYT-PLHAAASSGMISVVKYLLDLgvdMNEPNAYGNTPLHvACYNGQDVVVNE---LIDCGAIVNQK-NEKGFTPLHFAA 224
Cdd:PHA02859 20 RYCnPLFYYVEKDDIEGVKKWIKF---VNDCNDLYETPIF-SCLEKDKVNVEIlkfLIENGADVNFKtRDNNLSALHHYL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 225 ASTHGAL--CLELLVGNGADVNMKSKDGKTPLH--MTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGHELLI- 299
Cdd:PHA02859 96 SFNKNVEpeILKILIDSGSSITEEDEDGKNLLHmyMCNFNVRINVIKLLIDSGVSFLNKDFDNNNILYSYILFHSDKKIf 175
|
....*....
gi 1154884853 300 NTLITSGAD 308
Cdd:PHA02859 176 DFLTSLGID 184
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
198-422 |
5.95e-07 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 53.30 E-value: 5.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 198 VVNELIDCGAIVNQKNEKGFTPLHFAAAS----THGALCLELLVGNGADVNMKSKDGKTPLHmTALHGRFSRSQTI---- 269
Cdd:PHA02798 53 IVKLFINLGANVNGLDNEYSTPLCTILSNikdyKHMLDIVKILIENGADINKKNSDGETPLY-CLLSNGYINNLEIllfm 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 270 IQSGAVIDCEDKNGNTPLHIAARYGHEL---LINTLITSGADTAKRG-------IHGMFPLHLAALSgfSDCCRKLLSSG 339
Cdd:PHA02798 132 IENGADTTLLDKDGFTMLQVYLQSNHHIdieIIKLLLEKGVDINTHNnkekydtLHCYFKYNIDRID--ADILKLFVDNG 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 340 FDIDTPDDFGRTCLHAAAAGGNLECLNLLLN------TGADFNKKDKFGRSPLHYAAANCNYQCLFALVGSGASVNDLDE 413
Cdd:PHA02798 210 FIINKENKSHKKKFMEYLNSLLYDNKRFKKNildfifSYIDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITE 289
|
....*....
gi 1154884853 414 RGCTPLHYA 422
Cdd:PHA02798 290 LGNTCLFTA 298
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
747-906 |
6.22e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 53.04 E-value: 6.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 747 AAEMLIDTLGaSIVNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLMMAAENGQTNTVEMLVssasae 826
Cdd:PHA02874 16 AIEKIIKNKG-NCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 827 ltlqDNSKNTA-LHLACSKGHETSAllILEKITDrnlINATNAALQTPLHVAARNGLTMVVQELLGKGASVLAVDENGYT 905
Cdd:PHA02874 89 ----DNGVDTSiLPIPCIEKDMIKT--ILDCGID---VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCY 159
|
.
gi 1154884853 906 P 906
Cdd:PHA02874 160 P 160
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
734-787 |
7.59e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 46.88 E-value: 7.59e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1154884853 734 SPLHCAVINDNEGAAEMLIDTlGASIvNATDSKGRTPLHAAAFTDHVECLQLLL 787
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEK-GADI-NAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
31-191 |
1.16e-06 |
|
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: 52.78 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 31 LEAVQVLLKHSADVNARDknwqTPLHIAAANKAVKCAEALVPLLSN---------VNVSDR----AGRTALHHAAFSGHG 97
Cdd:TIGR00870 66 LELTELLLNLSCRGAVGD----TLLHAISLEYVDAVEAILLHLLAAfrksgplelANDQYTseftPGITALHLAAHRQNY 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 98 EMVKLLLSRGANINA------FDKKDRRA--------IHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAA----- 158
Cdd:TIGR00870 142 EIVKLLLERGASVPAracgdfFVKSQGVDsfyhgespLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVmenef 221
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1154884853 159 -------SSGMISVVKYLLDLGVDMNE----PNAYGNTPLHVAC 191
Cdd:TIGR00870 222 kaeyeelSCQMYNFALSLLDKLRDSKEleviLNHQGLTPLKLAA 265
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
225-294 |
1.22e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 52.59 E-value: 1.22e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 225 ASTHGALCLELLVGNGADVNMKSKDGKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYG 294
Cdd:PTZ00322 90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENG 159
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
218-423 |
1.36e-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: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 218 TPLhFAAASTHGALCLE-LLVGNGADVNMKSKDGKTPLHMTALHGRFSRSQTIIQSGA-----VIDCEDKNGNTPLHIAA 291
Cdd:cd22192 19 SPL-LLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPelvnePMTSDLYQGETALHIAV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 292 RYGHELLINTLITSGADTAKRGIHGMFplhlaalsgFSDCCRKLLSsgfdidtpddFGRTCLHAAAAGGNLECLNLLLNT 371
Cdd:cd22192 98 VNQNLNLVRELIARGADVVSPRATGTF---------FRPGPKNLIY----------YGEHPLSFAACVGNEEIVRLLIEH 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1154884853 372 GADFNKKDKFGRSPLHYAA--ANCNYQC-----LFALVGSGASVNdLD----ERGCTPLHYAA 423
Cdd:cd22192 159 GADIRAQDSLGNTVLHILVlqPNKTFACqmydlILSYDKEDDLQP-LDlvpnNQGLTPFKLAA 220
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
599-650 |
1.55e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 46.11 E-value: 1.55e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1154884853 599 TPLMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDALL 650
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
562-617 |
1.84e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 45.73 E-value: 1.84e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1154884853 562 RTPIHAAATNGHSECLRLLIGNAEPqnaVDIQDGNGQTPLMLSVLNGHTDCVYSLL 617
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGAD---INAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
802-896 |
2.62e-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: 51.17 E-value: 2.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 802 TPLMMAAENGQTNTVEMLVSSASAELTLQDNSKNTALHLACSKGHETSALLILEkiTDRNLIN-ATNAAL---QTPLHVA 877
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNePMTSDLyqgETALHIA 96
|
90
....*....|....*....
gi 1154884853 878 ARNGLTMVVQELLGKGASV 896
Cdd:cd22192 97 VVNQNLNLVRELIARGADV 115
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
136-190 |
2.86e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 45.42 E-value: 2.86e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1154884853 136 LVSHG-AEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVA 190
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
134-318 |
3.84e-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: 3.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 134 KLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDM-NEP---NAY-GNTPLHVACYNGQDVVVNELIDCGAI 208
Cdd:cd22192 35 KLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELvNEPmtsDLYqGETALHIAVVNQNLNLVRELIARGAD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 209 VN---------QKNEK-----GFTPLHFAAASTHGALcLELLVGNGADVNMKSKDGKTPLHMTALhgrfsrsqtiiQSGA 274
Cdd:cd22192 115 VVspratgtffRPGPKnliyyGEHPLSFAACVGNEEI-VRLLIEHGADIRAQDSLGNTVLHILVL-----------QPNK 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1154884853 275 VIDCE--------DKNGN-------------TPLHIAARYGHELLINTLITSgadtaKRGIHGMF 318
Cdd:cd22192 183 TFACQmydlilsyDKEDDlqpldlvpnnqglTPFKLAAKEGNIVMFQHLVQK-----RRHIQWTY 242
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
638-720 |
4.28e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 50.67 E-value: 4.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 638 AVTGHEECVDALLQHGAKCLLRDSRGRTPIHLSAACGHIGVLGALLQsaasMDANPATADNHGYTALHWACYNGHETCVE 717
Cdd:PTZ00322 90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLE----FGADPTLLDKDGKTPLELAEENGFREVVQ 165
|
...
gi 1154884853 718 LLL 720
Cdd:PTZ00322 166 LLS 168
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
84-115 |
4.57e-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: 4.57e-06
10 20 30
....*....|....*....|....*....|...
gi 1154884853 84 GRTALHHAAFS-GHGEMVKLLLSRGANINAFDK 115
Cdd:pfam00023 2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
319-360 |
5.09e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 44.57 E-value: 5.09e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1154884853 319 PLHLAALSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGG 360
Cdd:pfam13637 4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNG 45
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
202-256 |
5.30e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 44.64 E-value: 5.30e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1154884853 202 LIDCGAI-VNQKNEKGFTPLHFAAasTHGAL-CLELLVGNGADVNMKSKDGKTPLHM 256
Cdd:pfam13857 1 LLEHGPIdLNRLDGEGYTPLHVAA--KYGALeIVRVLLAYGVDLNLKDEEGLTALDL 55
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
52-203 |
5.73e-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: 50.26 E-value: 5.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 52 QTPLHIAAANKAVKCAEALVPLLSNVNVSDRA--------------GRTALHHAAFSGHGEMVKLLLSRGANINA----- 112
Cdd:cd21882 27 KTCLHKAALNLNDGVNEAIMLLLEAAPDSGNPkelvnapctdefyqGQTALHIAIENRNLNLVRLLVENGADVSAratgr 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 113 -FDKKDRRAIHW-------AAYMGHIEVVKLLVSHGAE---VTCKDKKSYTPLHA---------AASSGMISVVKYLLDL 172
Cdd:cd21882 107 fFRKSPGNLFYFgelplslAACTNQEEIVRLLLENGAQpaaLEAQDSLGNTVLHAlvlqadntpENSAFVCQMYNLLLSY 186
|
170 180 190
....*....|....*....|....*....|....*...
gi 1154884853 173 G------VDMNE-PNAYGNTPLHVACYNGQDVVVNELI 203
Cdd:cd21882 187 GahldptQQLEEiPNHQGLTPLKLAAVEGKIVMFQHIL 224
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
252-303 |
7.69e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 44.19 E-value: 7.69e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1154884853 252 TPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGHELLINTLI 303
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
37-91 |
9.75e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 43.87 E-value: 9.75e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1154884853 37 LLKH-SADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHA 91
Cdd:pfam13857 1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
383-601 |
9.79e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 49.22 E-value: 9.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 383 RSPLHYAAANCNYQCLFALVGSGASVND-LDERGCTPLHYAaTSDTDGKCLEYLLRNDANPGIrdkqgynavhysaaygh 461
Cdd:PHA02875 69 ESELHDAVEEGDVKAVEELLDLGKFADDvFYKDGMTPLHLA-TILKKLDIMKLLIARGADPDI----------------- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 462 rlclqliasetpldvlmetSGTDmlsdsdnraTISPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPLDLAAFKGHVE 541
Cdd:PHA02875 131 -------------------PNTD---------KFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIA 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1154884853 542 CVDVLINQGASIlvkDYILKRTPIHA---AATNGHSECLRLLIGNAEPQNAVDIQDGNGQTPL 601
Cdd:PHA02875 183 ICKMLLDSGANI---DYFGKNGCVAAlcyAIENNKIDIVRLFIKRGADCNIMFMIEGEECTIL 242
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
639-813 |
1.00e-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: 49.49 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 639 VTGHEECVDALLQHGAKclLRDSRGRTPIHLSAACGHIGVLGA---LLQSAASMDAN------PATADNH-GYTALHWAC 708
Cdd:cd21882 4 LLGLLECLRWYLTDSAY--QRGATGKTCLHKAALNLNDGVNEAimlLLEAAPDSGNPkelvnaPCTDEFYqGQTALHIAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 709 YNGHETCVELLLEQ----------EVFQKTEGNAF----SPLHCAVINDNEGAAEMLIDTlGASI--VNATDSKGRTPLH 772
Cdd:cd21882 82 ENRNLNLVRLLVENgadvsaratgRFFRKSPGNLFyfgeLPLSLAACTNQEEIVRLLLEN-GAQPaaLEAQDSLGNTVLH 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1154884853 773 A-----------AAFTDHVecLQLLLSHNAQVNSVDS-------TGKTPLMMAAENGQT 813
Cdd:cd21882 161 AlvlqadntpenSAFVCQM--YNLLLSYGAHLDPTQQleeipnhQGLTPLKLAAVEGKI 217
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
668-808 |
1.31e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 49.13 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 668 HLSAACGHIGVLgALLQSAAsmdaNPATADNHGYTALHWACYNGHETCVELLLEqevfqktegnafsplhcavindnega 747
Cdd:PTZ00322 88 QLAASGDAVGAR-ILLTGGA----DPNCRDYDGRTPLHIACANGHVQVVRVLLE-------------------------- 136
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1154884853 748 aemlidtLGASiVNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDSTGK-------------TPLMMAA 808
Cdd:PTZ00322 137 -------FGAD-PTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGANAKpdsftgkppsledSPISSHH 202
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
84-112 |
1.72e-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: 1.72e-05
10 20
....*....|....*....|....*....
gi 1154884853 84 GRTALHHAAFSGHGEMVKLLLSRGANINA 112
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
31-71 |
1.88e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 43.03 E-value: 1.88e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1154884853 31 LEAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALV 71
Cdd:pfam13637 14 LELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
269-348 |
1.96e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 48.74 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 269 IIQSGAVIDCEDKNGNTPLHIAARYGHELLINTLITSGADTAKRGIHGMFPLHLAALSGFSDCCRKLLS---SGFDIDT- 344
Cdd:PTZ00322 101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRhsqCHFELGAn 180
|
....*.
gi 1154884853 345 --PDDF 348
Cdd:PTZ00322 181 akPDSF 186
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
417-619 |
2.07e-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: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 417 TPLHYAAtSDTDGKCLEYLLR-NDANPGIRDKQGYNAVHYSAAYGHRLCLQLIASETPLDVLMETSgtdmlsdSDNRATI 495
Cdd:cd22192 19 SPLLLAA-KENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMT-------SDLYQGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 496 SPLHLAAYHGHhqalEVLVQSLLD--LDVRNSS----------------GRTPLDLAAFKGHVECVDVLINQGASILVKD 557
Cdd:cd22192 91 TALHIAVVNQN----LNLVRELIArgADVVSPRatgtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1154884853 558 YiLKRTPIHAAAT--NGHSECLRL-LIGNAEP---QNAVD-IQDGNGQTPLMLSVLNGHTDCVYSLLNK 619
Cdd:cd22192 167 S-LGNTVLHILVLqpNKTFACQMYdLILSYDKeddLQPLDlVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
349-402 |
2.12e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 42.65 E-value: 2.12e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1154884853 349 GRTCLHAAAAGGNLECLNLLLNTGADFNKKDKFGRSPLHYAAANCNYQCLFALV 402
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
587-635 |
2.31e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 42.72 E-value: 2.31e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1154884853 587 QNAVDIQDGNGQTPLMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALH 635
Cdd:pfam13857 6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
56-142 |
2.45e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 48.36 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 56 HIAAANKAVKcAEALVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKL 135
Cdd:PTZ00322 88 QLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166
|
....*..
gi 1154884853 136 LVSHGAE 142
Cdd:PTZ00322 167 LSRHSQC 173
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
158-264 |
2.62e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 47.97 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 158 ASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGAIVNQKNEKGFTPLHFAAASTHGALcLELLV 237
Cdd:PTZ00322 90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREV-VQLLS 168
|
90 100 110
....*....|....*....|....*....|....*...
gi 1154884853 238 GN-------GADVNMKSKDGKTPLH----MTALHGRFS 264
Cdd:PTZ00322 169 RHsqchfelGANAKPDSFTGKPPSLedspISSHHPDFS 206
|
|
| PHA02716 |
PHA02716 |
CPXV016; CPX019; EVM010; Provisional |
233-419 |
3.23e-05 |
|
CPXV016; CPX019; EVM010; Provisional
Pssm-ID: 165089 [Multi-domain] Cd Length: 764 Bit Score: 47.98 E-value: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 233 LELLVGNGADVNMKSKDGKTPLHMTALHGRFSRS--QTIIQSGAVIDCEDKNGNTPLH---IAARYGHELLINTLITSGA 307
Cdd:PHA02716 195 LEWLCNNGVNVNLQNNHLITPLHTYLITGNVCASviKKIIELGGDMDMKCVNGMSPIMtyiINIDNINPEITNIYIESLD 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 308 DTAKRGIHGMFPLHLAALSGFS-DCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECL--NLLLNTGADFNKKDKFGRS 384
Cdd:PHA02716 275 GNKVKNIPMILHSYITLARNIDiSVVYSFLQPGVKLHYKDSAGRTCLHQYILRHNISTDiiKLLHEYGNDLNEPDNIGNT 354
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1154884853 385 PLHYAAA--------------NCNYQCLFALVGSGASVNDLDERGCTPL 419
Cdd:PHA02716 355 VLHTYLSmlsvvnildpetdnDIRLDVIQCLISLGADITAVNCLGYTPL 403
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
283-336 |
3.39e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 42.26 E-value: 3.39e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1154884853 283 GNTPLHIAARYGHELLINTLITSGADTAKRGIHGMFPLHLAALSGFSDCCRKLL 336
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
84-112 |
3.84e-05 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 41.47 E-value: 3.84e-05
10 20
....*....|....*....|....*....
gi 1154884853 84 GRTALHHAAFSGHGEMVKLLLSRGANINA 112
Cdd:pfam13606 2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
663-720 |
4.13e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 41.88 E-value: 4.13e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1154884853 663 GRTPIHLSAACGHIGVLGALLQSAASMDAnpatADNHGYTALHWACYNGHETCVELLL 720
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINA----VDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
34-112 |
4.73e-05 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 46.94 E-value: 4.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 34 VQVLLKHSADVNARDKNWQTPLHIAAA-NKAVKCAEaLVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLLSRGANINA 112
Cdd:PHA03095 240 VLPLLIAGISINARNRYGQTPLHYAAVfNNPRACRR-LIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAET 318
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
494-604 |
4.84e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 47.20 E-value: 4.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 494 TISPLHLAAyHGHHQALEVLVQSLLDLDVRNSSGRTPLDLAAFKGHVECVDVLINQGA--SILVKDyilKRTPIHAAATN 571
Cdd:PTZ00322 83 TVELCQLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGAdpTLLDKD---GKTPLELAEEN 158
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1154884853 572 GHSECLRLLIG----------NAEPQNAVDIQDGNGQTPLMLS 604
Cdd:PTZ00322 159 GFREVVQLLSRhsqchfelgaNAKPDSFTGKPPSLEDSPISSH 201
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
753-924 |
4.91e-05 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 47.56 E-value: 4.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 753 DTLGASIVNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLMMAAENGQTNTVEMLVSSAsAELTLQDN 832
Cdd:PLN03192 511 DLLGDNGGEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA-CNVHIRDA 589
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 833 SKNTALHLACSKGHETsallILEKITDRNLINATNAALQTPLHVAARNGLTMvVQELLGKGASVLAVDENGYTpALACAP 912
Cdd:PLN03192 590 NGNTALWNAISAKHHK----IFRILYHFASISDPHAAGDLLCTAAKRNDLTA-MKELLKQGLNVDSEDHQGAT-ALQVAM 663
|
170
....*....|..
gi 1154884853 913 NKDVADCLALIL 924
Cdd:PLN03192 664 AEDHVDMVRLLI 675
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
183-237 |
5.17e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 41.88 E-value: 5.17e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1154884853 183 GNTPLHVACYNGQDVVVNELIDCGAIVNQKNEKGFTPLHFAAASTHGAlCLELLV 237
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVE-VLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
218-264 |
5.77e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 41.49 E-value: 5.77e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1154884853 218 TPLHFAAASTHGAlCLELLVGNGADVNMKSKDGKTPLHMTALHGRFS 264
Cdd:pfam13637 3 TALHAAAASGHLE-LLRLLLEKGADINAVDGNGETALHFAASNGNVE 48
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
334-454 |
6.55e-05 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 46.59 E-value: 6.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 334 KLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGADFNKKDKFGRSPLHYAAANCN--YQCLFALVGSGASVND- 410
Cdd:PHA02946 57 ELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKINNs 136
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1154884853 411 LDERGCTPLhyAATSDTDGKCLEYLLRNDANPGIRDKQGYNAVH 454
Cdd:PHA02946 137 VDEEGCGPL--LACTDPSERVFKKIMSIGFEARIVDKFGKNHIH 178
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
100-305 |
6.66e-05 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 46.59 E-value: 6.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 100 VKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLH--AAASSGMISVVKYLLDLGVDMN 177
Cdd:PHA02946 55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYylSGTDDEVIERINLLVQYGAKIN 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 178 EP-NAYGNTPLhVACYNGQDVVVNELIDCGAIVNQKNEKGFTPLHFAAASTH-GALCLELLVGNGADVNMKSKDGKTPLH 255
Cdd:PHA02946 135 NSvDEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNpKASTISWMMKLGISPSKPDHDGNTPLH 213
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1154884853 256 MTAlhGRFSRSQTIIQ---SGAVIDCEDKNGNTPLHIAAR-YGHELLINTLITS 305
Cdd:PHA02946 214 IVC--SKTVKNVDIINlllPSTDVNKQNKFGDSPLTLLIKtLSPAHLINKLLST 265
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
322-541 |
8.42e-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: 8.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 322 LAALSGFSDCCRKLLSSgfDIDTPDDFGRTCLHAAA---AGGNLECLNLLLNTGADFNKKDKF-----------GRSPLH 387
Cdd:cd21882 1 LEELLGLLECLRWYLTD--SAYQRGATGKTCLHKAAlnlNDGVNEAIMLLLEAAPDSGNPKELvnapctdefyqGQTALH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 388 YAAANCNYQCLFALVGSGASVND------LDERGCT-------PLHYAATSDTDgKCLEYLLRNDANP---GIRDKQGYN 451
Cdd:cd21882 79 IAIENRNLNLVRLLVENGADVSAratgrfFRKSPGNlfyfgelPLSLAACTNQE-EIVRLLLENGAQPaalEAQDSLGNT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 452 AVHysaayghrlCLQLIASETPLDVLMETSGTDMLsdsdnratispLHLAAYHGHHQALEvlvqslldlDVRNSSGRTPL 531
Cdd:cd21882 158 VLH---------ALVLQADNTPENSAFVCQMYNLL-----------LSYGAHLDPTQQLE---------EIPNHQGLTPL 208
|
250
....*....|
gi 1154884853 532 DLAAFKGHVE 541
Cdd:cd21882 209 KLAAVEGKIV 218
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
590-810 |
1.09e-04 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 45.98 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 590 VDIQDGNGQTPL--MLSVL---NGHTDCVYSLLNKGANVDAKDKWGRTA----LHRGAVTgHEECVDALLQHGAKCLLRD 660
Cdd:PHA02798 64 VNGLDNEYSTPLctILSNIkdyKHMLDIVKILIENGADINKKNSDGETPlyclLSNGYIN-NLEILLFMIENGADTTLLD 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 661 SRGRTPIHLSAACGH---IGVLGALLQSAasMDANpaTADN-HGYTALHwaCYNGHE------TCVELLLEQ----EVFQ 726
Cdd:PHA02798 143 KDGFTMLQVYLQSNHhidIEIIKLLLEKG--VDIN--THNNkEKYDTLH--CYFKYNidridaDILKLFVDNgfiiNKEN 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 727 KTEGNAFSPLHCAVINDNEGAAEMLIDTLGASI-VNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLM 805
Cdd:PHA02798 217 KSHKKKFMEYLNSLLYDNKRFKKNILDFIFSYIdINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLF 296
|
....*
gi 1154884853 806 MAAEN 810
Cdd:PHA02798 297 TAFEN 301
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
583-692 |
1.25e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 46.04 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 583 NAEPQNAVDiqdgngQTPL-MLSV------LNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQHGAK 655
Cdd:PTZ00322 67 NLTTEEVID------PVVAhMLTVelcqlaASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGAD 140
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1154884853 656 CLLRDSRGRTPIHLSAACGHIGVLGALL---QSAASMDAN 692
Cdd:PTZ00322 141 PTLLDKDGKTPLELAEENGFREVVQLLSrhsQCHFELGAN 180
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
766-797 |
1.41e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 39.97 E-value: 1.41e-04
10 20 30
....*....|....*....|....*....|...
gi 1154884853 766 KGRTPLHAAA-FTDHVECLQLLLSHNAQVNSVD 797
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
321-437 |
1.43e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 45.66 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 321 HLAALSGFSDccrKLLSSGFDIDTPDDFGRTCLHAA-------AAGGNLECLNLLLNTGADFNKKDKFGRSPLHYAAANC 393
Cdd:PTZ00322 50 HLEALEATEN---KDATPDHNLTTEEVIDPVVAHMLtvelcqlAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANG 126
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1154884853 394 NYQCLFALVGSGASVNDLDERGCTPLHYAATSDTdGKCLEYLLR 437
Cdd:PTZ00322 127 HVQVVRVLLEFGADPTLLDKDGKTPLELAEENGF-REVVQLLSR 169
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
808-903 |
1.70e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 45.66 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 808 AENGQTNTVEMLVSSAsAELTLQDNSKNTALHLACSKGHETSALLILEKITDRNLINATNaalQTPLHVAARNGLTMVVQ 887
Cdd:PTZ00322 90 AASGDAVGARILLTGG-ADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDG---KTPLELAEENGFREVVQ 165
|
90
....*....|....*.
gi 1154884853 888 ELLGKGASVLAVDENG 903
Cdd:PTZ00322 166 LLSRHSQCHFELGANA 181
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
169-223 |
2.92e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 39.64 E-value: 2.92e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1154884853 169 LLDLG-VDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGAIVNQKNEKGFTPLHFA 223
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
756-807 |
3.16e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 39.64 E-value: 3.16e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1154884853 756 GASIVNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLMMA 807
Cdd:pfam13857 5 GPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
484-534 |
3.19e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 39.64 E-value: 3.19e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1154884853 484 DMLSDSDNRATISPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPLDLA 534
Cdd:pfam13857 6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
596-628 |
3.31e-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: 3.31e-04
10 20 30
....*....|....*....|....*....|....
gi 1154884853 596 NGQTPLMLSVL-NGHTDCVYSLLNKGANVDAKDK 628
Cdd:pfam00023 1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
|
|
| PHA02989 |
PHA02989 |
ankyrin repeat protein; Provisional |
98-229 |
3.48e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222954 [Multi-domain] Cd Length: 494 Bit Score: 44.35 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 98 EMVKLLLSRGANINAFDKKDRRAI------HWAAYMGHIEVVKLLVSHgAEVTCKDKKSYTPLHAAASSGMISVVKYLLD 171
Cdd:PHA02989 199 KVIKYLIKKGVNIETNNNGSESVLesfldnNKILSKKEFKVLNFILKY-IKINKKDKKGFNPLLISAKVDNYEAFNYLLK 277
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1154884853 172 LGVDMNEPNAYGNTPLHVACYNGQDVVVNElidcgaIVNQKNEKGFTPLHFAAASTHG 229
Cdd:PHA02989 278 LGDDIYNVSKDGDTVLTYAIKHGNIDMLNR------ILQLKPGKYLIKKTFEYFSEHG 329
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
151-178 |
3.53e-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: 3.53e-04
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
103-157 |
4.13e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 39.25 E-value: 4.13e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1154884853 103 LLSRG-ANINAFDKKDRRAIHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAA 157
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
414-447 |
4.44e-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: 4.44e-04
10 20 30
....*....|....*....|....*....|....
gi 1154884853 414 RGCTPLHYAATSDTDGKCLEYLLRNDANPGIRDK 447
Cdd:pfam00023 1 DGNTPLHLAAGRRGNLEIVKLLLSKGADVNARDK 34
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
321-415 |
4.65e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 44.12 E-value: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 321 HLAAlSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGADFNKKDKFGRSPLHYAAANCNYQCLFA 400
Cdd:PTZ00322 88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166
|
90
....*....|....*
gi 1154884853 401 LVGSGASVNDLDERG 415
Cdd:PTZ00322 167 LSRHSQCHFELGANA 181
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
178-294 |
4.78e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411978 [Multi-domain] Cd Length: 680 Bit Score: 43.98 E-value: 4.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 178 EPNAYGNTPLHVACYNGQDVVVNELIDCGAIVNQK----------NEKGF----TPLHFAAASTHGALcLELLVGNGAD- 242
Cdd:cd22194 136 EEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHakgvffnpkyKHEGFyfgeTPLALAACTNQPEI-VQLLMEKESTd 214
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1154884853 243 VNMKSKDGKTPLHMTALHGRFSRSQT--IIQSGAVI--DCEDKN--------GNTPLHIAARYG 294
Cdd:cd22194 215 ITSQDSRGNTVLHALVTVAEDSKTQNdfVKRMYDMIllKSENKNletirnneGLTPLQLAAKMG 278
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
766-794 |
5.12e-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: 5.12e-04
10 20
....*....|....*....|....*....
gi 1154884853 766 KGRTPLHAAAFTDHVECLQLLLSHNAQVN 794
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
372-454 |
5.16e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 42.50 E-value: 5.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 372 GADFNKKDK-FGRSPLHYAAA---NCNYQCLFALVGSGASVNDLDERGCTPLH-YAATSDTDGKCLEYLLRNDANPGIRD 446
Cdd:PHA02859 76 GADVNFKTRdNNLSALHHYLSfnkNVEPEILKILIDSGSSITEEDEDGKNLLHmYMCNFNVRINVIKLLIDSGVSFLNKD 155
|
....*...
gi 1154884853 447 KQGYNAVH 454
Cdd:PHA02859 156 FDNNNILY 163
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
182-210 |
6.48e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 37.95 E-value: 6.48e-04
10 20
....*....|....*....|....*....
gi 1154884853 182 YGNTPLHVACYNGQDVVVNELIDCGAIVN 210
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
215-248 |
8.01e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 37.65 E-value: 8.01e-04
10 20 30
....*....|....*....|....*....|....
gi 1154884853 215 KGFTPLHFAAASTHGALCLELLVGNGADVNMKSK 248
Cdd:pfam00023 1 DGNTPLHLAAGRRGNLEIVKLLLSKGADVNARDK 34
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
84-224 |
8.18e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411978 [Multi-domain] Cd Length: 680 Bit Score: 43.21 E-value: 8.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 84 GRTALHHAAFSGHGEMVKLLLSRGANINA------FDKKDRraiHWAAYMGHievvkllvshgaevtckdkksyTPLHAA 157
Cdd:cd22194 141 GQTALNIAIERRQGDIVKLLIAKGADVNAhakgvfFNPKYK---HEGFYFGE----------------------TPLALA 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 158 ASSGMISVVKYLLDlgvdmNEPNAY------GNTPLH----VA-CYNGQDVVVNELID-----CG--AIVNQKNEKGFTP 219
Cdd:cd22194 196 ACTNQPEIVQLLME-----KESTDItsqdsrGNTVLHalvtVAeDSKTQNDFVKRMYDmillkSEnkNLETIRNNEGLTP 270
|
....*
gi 1154884853 220 LHFAA 224
Cdd:cd22194 271 LQLAA 275
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
182-214 |
9.94e-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: 9.94e-04
10 20 30
....*....|....*....|....*....|....
gi 1154884853 182 YGNTPLHVACY-NGQDVVVNELIDCGAIVNQKNE 214
Cdd:pfam00023 1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
562-668 |
1.02e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).
Pssm-ID: 411975 [Multi-domain] Cd Length: 600 Bit Score: 42.94 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 562 RTPIHAAATN---GHSECLRLLIgNAEPQNAVDIQDGN---------GQTPLMLSVLNGHTDCVYSLLNKGANVDAK--- 626
Cdd:cd21882 27 KTCLHKAALNlndGVNEAIMLLL-EAAPDSGNPKELVNapctdefyqGQTALHIAIENRNLNLVRLLVENGADVSARatg 105
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1154884853 627 ---DKWGRTALHRG-------AVTGHEECVDALLQHGAK---CLLRDSRGRTPIH 668
Cdd:cd21882 106 rffRKSPGNLFYFGelplslaACTNQEEIVRLLLENGAQpaaLEAQDSLGNTVLH 160
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
282-308 |
1.04e-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: 1.04e-03
|
| PHA02716 |
PHA02716 |
CPXV016; CPX019; EVM010; Provisional |
98-320 |
1.05e-03 |
|
CPXV016; CPX019; EVM010; Provisional
Pssm-ID: 165089 [Multi-domain] Cd Length: 764 Bit Score: 42.98 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 98 EMVKLLLSRG-ANINAFDKKDRRAIhWAAYMGH----IEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMI--SVVKYLL 170
Cdd:PHA02716 156 DLIKYMVDVGiVNLNYVCKKTGYGI-LHAYLGNmyvdIDILEWLCNNGVNVNLQNNHLITPLHTYLITGNVcaSVIKKII 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 171 DLGVDMNEPNAYGNTPLHVACYNGQDV---VVNELIDCGAIVNQKNEKGFTPLHFAAASTHGALCLELLVGNGADVNMKS 247
Cdd:PHA02716 235 ELGGDMDMKCVNGMSPIMTYIINIDNInpeITNIYIESLDGNKVKNIPMILHSYITLARNIDISVVYSFLQPGVKLHYKD 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 248 KDGKTPLHMTALHGRFSRS--QTIIQSGAVIDCEDKNGNTPLH-------IAARYGHEL-------LINTLITSGADTAK 311
Cdd:PHA02716 315 SAGRTCLHQYILRHNISTDiiKLLHEYGNDLNEPDNIGNTVLHtylsmlsVVNILDPETdndirldVIQCLISLGADITA 394
|
....*....
gi 1154884853 312 RGIHGMFPL 320
Cdd:PHA02716 395 VNCLGYTPL 403
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
699-721 |
1.20e-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: 1.20e-03
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
749-864 |
1.22e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 42.51 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 749 EMLIDtLGASiVNATDSKGRTPL-----HAAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLMMAAENGQTNTVEMLVS-- 821
Cdd:PHA02798 55 KLFIN-LGAN-VNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLFmi 132
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1154884853 822 SASAELTLQDNSKNTALHLACSKGHETSALLI---LEKITDRNLIN 864
Cdd:PHA02798 133 ENGADTTLLDKDGFTMLQVYLQSNHHIDIEIIkllLEKGVDINTHN 178
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
373-422 |
1.25e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 37.71 E-value: 1.25e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1154884853 373 ADFNKKDKFGRSPLHYAAANCNYQCLFALVGSGASVNDLDERGCTPLHYA 422
Cdd:pfam13857 7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02736 |
PHA02736 |
Viral ankyrin protein; Provisional |
81-191 |
1.32e-03 |
|
Viral ankyrin protein; Provisional
Pssm-ID: 165103 [Multi-domain] Cd Length: 154 Bit Score: 40.24 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 81 DRAGRTALHHaaFSGHGEMVKLLLSRGANINA-------FDKKDRRAIHWAAYMGHI---EVVKLLVSHGAEVTCKDKK- 149
Cdd:PHA02736 14 DIEGENILHY--LCRNGGVTDLLAFKNAISDEnrylvleYNRHGKQCVHIVSNPDKAdpqEKLKLLMEWGADINGKERVf 91
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1154884853 150 SYTPLHAAASSGMISVVKYLLDL-GVDMNEPNAYGNTPLHVAC 191
Cdd:PHA02736 92 GNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVAC 134
|
|
| PHA02716 |
PHA02716 |
CPXV016; CPX019; EVM010; Provisional |
81-205 |
1.48e-03 |
|
CPXV016; CPX019; EVM010; Provisional
Pssm-ID: 165089 [Multi-domain] Cd Length: 764 Bit Score: 42.59 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 81 DRAGRTALHHAAFSGH--GEMVKLLLSRGANINAFDKKDRRAIHwaAYMGHIEVVKLLVSHgaevTCKDKKsytplhaaa 158
Cdd:PHA02716 314 DSAGRTCLHQYILRHNisTDIIKLLHEYGNDLNEPDNIGNTVLH--TYLSMLSVVNILDPE----TDNDIR--------- 378
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1154884853 159 ssgmISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDC 205
Cdd:PHA02716 379 ----LDVIQCLISLGADITAVNCLGYTPLTSYICTAQNYMYYDIIDC 421
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
562-668 |
1.55e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411978 [Multi-domain] Cd Length: 680 Bit Score: 42.44 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 562 RTPIHAAATNGhseCLRLLIgNAEPQNavdiQDGNGQTPLMLSVLNGHTDCVYSLLNKGANVDAKDK------------- 628
Cdd:cd22194 114 RILLAFAEENG---ILDRFI-NAEYTE----EAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKgvffnpkykhegf 185
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1154884853 629 -WGRTALHRGAVTGHEECVDALLQHGAKCL-LRDSRGRTPIH 668
Cdd:cd22194 186 yFGETPLALAACTNQPEIVQLLMEKESTDItSQDSRGNTVLH 227
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
120-145 |
1.75e-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: 36.80 E-value: 1.75e-03
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
835-890 |
1.86e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 37.25 E-value: 1.86e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1154884853 835 NTALHLACSKGHETSALLILEKITDrnlINATNAALQTPLHVAARNGLTMVVQELL 890
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGAD---INAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
616-669 |
1.97e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 37.33 E-value: 1.97e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1154884853 616 LLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQHGAKCLLRDSRGRTPIHL 669
Cdd:pfam13857 2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
120-148 |
2.02e-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: 2.02e-03
10 20 30
....*....|....*....|....*....|
gi 1154884853 120 AIHWAAYM-GHIEVVKLLVSHGAEVTCKDK 148
Cdd:pfam00023 5 PLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
861-906 |
2.40e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 36.94 E-value: 2.40e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1154884853 861 NLINATNAALQTPLHVAARNGLTMVVQELLGKGASVLAVDENGYTP 906
Cdd:pfam13857 7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTA 52
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
527-553 |
2.52e-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: 2.52e-03
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
527-557 |
2.53e-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: 2.53e-03
10 20 30
....*....|....*....|....*....|..
gi 1154884853 527 GRTPLDLAAFK-GHVECVDVLINQGASILVKD 557
Cdd:pfam00023 2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
|
|
| TRPV1 |
cd22196 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ... |
116-226 |
2.55e-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: 41.72 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 116 KDRRAIHWAAYMGHIEVVKLLVSHGAEVTC-------KDKKSYT-------PLHAAASSGMISVVKYLLD---LGVDMNE 178
Cdd:cd22196 93 KGQTALHIAIERRNMHLVELLVQNGADVHArasgeffKKKKGGPgfyfgelPLSLAACTNQLDIVKFLLEnphSPADISA 172
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1154884853 179 PNAYGNTPLHVACYNGQDVVVN---------ELIDCGAIVNQK-------NEKGFTPLHFAAAS 226
Cdd:cd22196 173 RDSMGNTVLHALVEVADNTPENtkfvtkmynEILILGAKIRPLlkleeitNKKGLTPLKLAAKT 236
|
|
| PHA02989 |
PHA02989 |
ankyrin repeat protein; Provisional |
163-422 |
2.88e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222954 [Multi-domain] Cd Length: 494 Bit Score: 41.27 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 163 ISVVKYLLDLGVDMNEpnAYGNTPLHVACYNGQDV---VVNELIDCGAIVNQKnekGF--TPL-----HFAAASTHGALC 232
Cdd:PHA02989 16 KNALEFLLRTGFDVNE--EYRGNSILLLYLKRKDVkikIVKLLIDNGADVNYK---GYieTPLcavlrNREITSNKIKKI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 233 LELLVGNGADVNMKSKDGKTPLhMTALHG---------RFsrsqtIIQSGA-VIDCEDKNGNTPLHIaarYGHELLINT- 301
Cdd:PHA02989 91 VKLLLKFGADINLKTFNGVSPI-VCFIYNsninncdmlRF-----LLSKGInVNDVKNSRGYNLLHM---YLESFSVKKd 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 302 ----LITSGADT-AKRGIHGMFPLHLAALSGFS----DCCRKLLSSGFDIDTPDDFGRTCLHAAAagGNLECLNLLLNTG 372
Cdd:PHA02989 162 vikiLLSFGVNLfEKTSLYGLTPMNIYLRNDIDvisiKVIKYLIKKGVNIETNNNGSESVLESFL--DNNKILSKKEFKV 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1154884853 373 ADF-------NKKDKFGRSPLHYAAANCNYQCLFALVGSGASVNDLDERGCTPLHYA 422
Cdd:PHA02989 240 LNFilkyikiNKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYA 296
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
288-360 |
2.88e-03 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 41.42 E-value: 2.88e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1154884853 288 HIAARyGHELLINTLITSGADTAKRGIHGMFPLHLAALSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGG 360
Cdd:PTZ00322 88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENG 159
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
76-115 |
2.93e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 36.94 E-value: 2.93e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1154884853 76 NVNVSDRAGRTALHHAAFSGHGEMVKLLLSRGANINAFDK 115
Cdd:pfam13857 8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDE 47
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
406-455 |
2.93e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 36.94 E-value: 2.93e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1154884853 406 ASVNDLDERGCTPLHYAAtSDTDGKCLEYLLRNDANPGIRDKQGYNAVHY 455
Cdd:pfam13857 7 IDLNRLDGEGYTPLHVAA-KYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
|
|
| TRPV1 |
cd22196 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ... |
760-892 |
3.50e-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: 41.33 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 760 VNA--TDS--KGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDST--------------GKTPLMMAAENGQTNTVEMLVS 821
Cdd:cd22196 83 VNAayTDSyyKGQTALHIAIERRNMHLVELLVQNGADVHARASGeffkkkkggpgfyfGELPLSLAACTNQLDIVKFLLE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 822 S--ASAELTLQDNSKNTALHLACS---------------------KGHETSALLILEKITDRNLInatnaalqTPLHVAA 878
Cdd:cd22196 163 NphSPADISARDSMGNTVLHALVEvadntpentkfvtkmyneiliLGAKIRPLLKLEEITNKKGL--------TPLKLAA 234
|
170
....*....|....
gi 1154884853 879 RNGLTMVVQELLGK 892
Cdd:cd22196 235 KTGKIGIFAYILGR 248
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
596-625 |
3.77e-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: 3.77e-03
10 20 30
....*....|....*....|....*....|
gi 1154884853 596 NGQTPLMLSVLNGHTDCVYSLLNKGANVDA 625
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
335-515 |
4.20e-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: 41.22 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 335 LLSSGFDIDTpddfGRTCLHAA-----------------AAGGNLECLNLLLNTGADFNkkdkFGRSPLHYAAANCNYQC 397
Cdd:TIGR00870 72 LLNLSCRGAV----GDTLLHAIsleyvdaveaillhllaAFRKSGPLELANDQYTSEFT----PGITALHLAAHRQNYEI 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 398 LFALVGSGASVN--------------DLDERGCTPLH-YAATSDTDgkCLEYLLRNDANPGIRDKQGYNAVH-------Y 455
Cdd:TIGR00870 144 VKLLLERGASVParacgdffvksqgvDSFYHGESPLNaAACLGSPS--IVALLSEDPADILTADSLGNTLLHllvmeneF 221
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1154884853 456 SAAYGH--RLCLQLIasetpLDVLMETSGTDMLSDSDNRATISPLHLAAYHGHHQALEVLVQ 515
Cdd:TIGR00870 222 KAEYEElsCQMYNFA-----LSLLDKLRDSKELEVILNHQGLTPLKLAAKEGRIVLFRLKLA 278
|
|
| TRPV2 |
cd22197 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ... |
759-881 |
4.35e-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: 40.99 E-value: 4.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 759 IVNA--TDS--KGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDST-------------GKTPLMMAAENGQTNTVEMLVS 821
Cdd:cd22197 82 LVNAqcTDEyyRGHSALHIAIEKRSLQCVKLLVENGADVHARACGrffqkkqgtcfyfGELPLSLAACTKQWDVVNYLLE 161
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1154884853 822 SAS--AELTLQDNSKNTALH---LACSKGHETSALL------ILEKITDRN----LINATNAALQTPLHVAARNG 881
Cdd:cd22197 162 NPHqpASLQAQDSLGNTVLHalvMIADNSPENSALVikmydgLLQAGARLCptvqLEEISNHEGLTPLKLAAKEG 236
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
872-923 |
4.51e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 36.10 E-value: 4.51e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1154884853 872 TPLHVAARNGLTMVVQELLGKGASVLAVDENGYTPALACAPNKDVADCLALI 923
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
734-839 |
4.86e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 39.42 E-value: 4.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 734 SPLHCAVIND--NEGAAEMLIDTlGASIVNATDSKGRTPLHA-AAFTDHV--ECLQLLLSHNAQVNSVDSTGKTPLMMAA 808
Cdd:PHA02859 53 TPIFSCLEKDkvNVEILKFLIEN-GADVNFKTRDNNLSALHHyLSFNKNVepEILKILIDSGSSITEEDEDGKNLLHMYM 131
|
90 100 110
....*....|....*....|....*....|...
gi 1154884853 809 ENGQTN--TVEMLVSSASAELTlQDNSKNTALH 839
Cdd:PHA02859 132 CNFNVRinVIKLLIDSGVSFLN-KDFDNNNILY 163
|
|
| PHA02791 |
PHA02791 |
ankyrin-like protein; Provisional |
696-865 |
5.46e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165154 [Multi-domain] Cd Length: 284 Bit Score: 40.03 E-value: 5.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 696 ADNHGYTALHWACYNGHETCVELLLEQEVFQKTEGNAFsPLH-CAVINDNEGAAEMLIDTLGASivnATDSKGRTPLHAA 774
Cdd:PHA02791 26 ADVHGHSALYYAIADNNVRLVCTLLNAGALKNLLENEF-PLHqAATLEDTKIVKILLFSGMDDS---QFDDKGNTALYYA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 775 AFTDHVECLQLLLSHNAQVNSVDSTG-KTPLMMAAENGQTNTVEMLVSSASAELTLQdnSKNTALHLACSKGHETSALLI 853
Cdd:PHA02791 102 VDSGNMQTVKLFVKKNWRLMFYGKTGwKTSFYHAVMLNDVSIVSYFLSEIPSTFDLA--ILLSCIHITIKNGHVDMMILL 179
|
170
....*....|..
gi 1154884853 854 LEKITDRNLINA 865
Cdd:PHA02791 180 LDYMTSTNTNNS 191
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
802-847 |
5.72e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 36.10 E-value: 5.72e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1154884853 802 TPLMMAAENGQTNTVEMLVSSaSAELTLQDNSKNTALHLACSKGHE 847
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEK-GADINAVDGNGETALHFAASNGNV 47
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
182-210 |
5.87e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 35.31 E-value: 5.87e-03
10 20
....*....|....*....|....*....
gi 1154884853 182 YGNTPLHVACYNGQDVVVNELIDCGAIVN 210
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
282-308 |
6.81e-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: 6.81e-03
10 20
....*....|....*....|....*..
gi 1154884853 282 NGNTPLHIAARYGHELLINTLITSGAD 308
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGAD 27
|
|
| PHA02884 |
PHA02884 |
ankyrin repeat protein; Provisional |
165-259 |
7.09e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165212 [Multi-domain] Cd Length: 300 Bit Score: 39.58 E-value: 7.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 165 VVKYLLDLGVDMNEP-----NAYgNTPLHVACYNGQDVVVNELIDCGAIVNQ-KNEKGFTPLHFAAasTHGAL-CLELLV 237
Cdd:PHA02884 48 IIDAILKLGADPEAPfplseNSK-TNPLIYAIDCDNDDAAKLLIRYGADVNRyAEEAKITPLYISV--LHGCLkCLEILL 124
|
90 100
....*....|....*....|..
gi 1154884853 238 GNGADVNMKSKDGKTPLHMTAL 259
Cdd:PHA02884 125 SYGADINIQTNDMVTPIELALM 146
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
282-308 |
7.86e-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: 7.86e-03
10 20
....*....|....*....|....*...
gi 1154884853 282 NGNTPLHIAA-RYGHELLINTLITSGAD 308
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGAD 28
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
417-467 |
8.32e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 35.33 E-value: 8.32e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1154884853 417 TPLHYAATSDtDGKCLEYLLRNDANPGIRDKQGYNAVHYSAAYGHRLCLQL 467
Cdd:pfam13637 3 TALHAAAASG-HLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKL 52
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
710-890 |
8.81e-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: 8.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 710 NGHETCVELLLEQEVFQKTEGNAfspLHCAVINDnEGAAEMLI--------DTLGASIVNATD----SKGRTPLHAAAFT 777
Cdd:TIGR00870 63 NENLELTELLLNLSCRGAVGDTL---LHAISLEY-VDAVEAILlhllaafrKSGPLELANDQYtsefTPGITALHLAAHR 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 778 DHVECLQLLLSHNAQVNS------------VDST--GKTPLMMAAENGQTNTVEMLvSSASAELTLQDNSKNTALHL--- 840
Cdd:TIGR00870 139 QNYEIVKLLLERGASVPAracgdffvksqgVDSFyhGESPLNAAACLGSPSIVALL-SEDPADILTADSLGNTLLHLlvm 217
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 841 ---------ACSKGHETSALLILEKITD-RNLINATNAALQTPLHVAARNGLTMVVQELL 890
Cdd:TIGR00870 218 enefkaeyeELSCQMYNFALSLLDKLRDsKELEVILNHQGLTPLKLAAKEGRIVLFRLKL 277
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
463-546 |
8.96e-03 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 39.88 E-value: 8.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 463 LClQLIASETPLDV-LMETSGTDMLS-DSDNRatiSPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPLDLAAFKGHV 540
Cdd:PTZ00322 86 LC-QLAASGDAVGArILLTGGADPNCrDYDGR---TPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFR 161
|
....*.
gi 1154884853 541 ECVDVL 546
Cdd:PTZ00322 162 EVVQLL 167
|
|
| PHA02736 |
PHA02736 |
Viral ankyrin protein; Provisional |
178-307 |
9.34e-03 |
|
Viral ankyrin protein; Provisional
Pssm-ID: 165103 [Multi-domain] Cd Length: 154 Bit Score: 37.93 E-value: 9.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 178 EPNAYGNTPLHVACYNGqDVV-----VNELIDCGA-IVNQKNEKGFTPLHFAAAS--THGALCLELLVGNGADVNMK-SK 248
Cdd:PHA02736 12 EPDIEGENILHYLCRNG-GVTdllafKNAISDENRyLVLEYNRHGKQCVHIVSNPdkADPQEKLKLLMEWGADINGKeRV 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 249 DGKTPLHMTALHGRFSRSQTII-QSGAVIDCEDKNGNTPLHIAARYGHELLINTLITSGA 307
Cdd:PHA02736 91 FGNTPLHIAVYTQNYELATWLCnQPGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGA 150
|
|
| PHA02716 |
PHA02716 |
CPXV016; CPX019; EVM010; Provisional |
510-704 |
9.36e-03 |
|
CPXV016; CPX019; EVM010; Provisional
Pssm-ID: 165089 [Multi-domain] Cd Length: 764 Bit Score: 39.90 E-value: 9.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 510 LEVLVQSLLDLDVRNSSGRTPLDLAAFKGHVeCVDVL---INQGASILVKdYILKRTPIHAAATNghseclrllIGNAEP 586
Cdd:PHA02716 195 LEWLCNNGVNVNLQNNHLITPLHTYLITGNV-CASVIkkiIELGGDMDMK-CVNGMSPIMTYIIN---------IDNINP 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 587 Q--NA-VDIQDGNGQT--PLMLSVL-----NGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGH--EECVDALLQHGA 654
Cdd:PHA02716 264 EitNIyIESLDGNKVKniPMILHSYitlarNIDISVVYSFLQPGVKLHYKDSAGRTCLHQYILRHNisTDIIKLLHEYGN 343
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1154884853 655 KCLLRDSRGRTPIH--LSAACG------------HIGVLGALLQSAASMDAnpatADNHGYTAL 704
Cdd:PHA02716 344 DLNEPDNIGNTVLHtyLSMLSVvnildpetdndiRLDVIQCLISLGADITA----VNCLGYTPL 403
|
|
| PHA02791 |
PHA02791 |
ankyrin-like protein; Provisional |
41-219 |
9.43e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165154 [Multi-domain] Cd Length: 284 Bit Score: 39.25 E-value: 9.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 41 SADVNARDKNWQTPLHIAAANKAVKC------AEALVPLLSNvnvsdragRTALHHAAFSGHGEMVKLLLSRGANINAFD 114
Cdd:PHA02791 20 SKDAFKADVHGHSALYYAIADNNVRLvctllnAGALKNLLEN--------EFPLHQAATLEDTKIVKILLFSGMDDSQFD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884853 115 KKDRRAIHWAAYMGHIEVVKLLVSHGAEVTCKDKKSY-TPLHAAASSGMISVVKYLL-------DLGVDMnepnaygnTP 186
Cdd:PHA02791 92 DKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTGWkTSFYHAVMLNDVSIVSYFLseipstfDLAILL--------SC 163
|
170 180 190
....*....|....*....|....*....|...
gi 1154884853 187 LHVACYNGQDVVVNELIDCGAIVNQKNEKGFTP 219
Cdd:PHA02791 164 IHITIKNGHVDMMILLLDYMTSTNTNNSLLFIP 196
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
699-724 |
9.80e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 34.54 E-value: 9.80e-03
|
|