|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
29-318 |
6.74e-51 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 181.31 E-value: 6.74e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 29 AEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSV 108
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 109 NVSDRGGRTALHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAA 188
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 189 ASNGQISVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHFAAASTHGALcLELLV 268
Cdd:COG0666 161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI-VKLLL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 755492548 269 NNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPL 318
Cdd:COG0666 240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
1-251 |
3.74e-48 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 173.60 E-value: 3.74e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 1 MLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDK 80
Cdd:COG0666 39 LLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDK 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 81 NWQTPLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGH 160
Cdd:COG0666 119 DGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGH 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 161 LDVVALLINHGAEVTCKDKKGYTPLHAAASNGQISVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANV 240
Cdd:COG0666 199 LEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278
|
250
....*....|.
gi 755492548 241 NQPNNSGFTPL 251
Cdd:COG0666 279 AAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
2-282 |
3.96e-48 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 173.60 E-value: 3.96e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 2 LIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKN 81
Cdd:COG0666 7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 82 WQTPLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHL 161
Cdd:COG0666 87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 162 DVVALLINHGAEVTCKDKKGYTPLHAAASNGQISVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVN 241
Cdd:COG0666 167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 755492548 242 QPNNSGFTPLHFAAASTHGALCLELLVNNGADVNIQSKDGK 282
Cdd:COG0666 247 AKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
61-334 |
1.21e-39 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 154.03 E-value: 1.21e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 61 SEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSS---VNVSDRGGRTALHHAALNGH-MEMVNLLLA 136
Cdd:PHA03095 26 TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIVRLLLEAgadVNAPERCGFTPLHLYLYNATtLDVIKLLIK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 137 KGANINAFDKKDRRALHwaAYMG----HLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQISV--VKHLLNLGVEIDEI 210
Cdd:PHA03095 106 AGADVNAKDKVGRTPLH--VYLSgfniNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVYAV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 211 NVYGNTALHIACYNGQD--AVVNELIDYGANVNQPNNSGFTPLHFAAA-STHGALCLELLVNNGADVNIQSKDGKSPLHM 287
Cdd:PHA03095 184 DDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHSMATgSSCKRSLVLPLLIAGISINARNRYGQTPLHY 263
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 755492548 288 TAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARHGHELLINTLI 334
Cdd:PHA03095 264 AAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
1-285 |
5.80e-37 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 145.94 E-value: 5.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 1 MLIHKTEDVNALDSEKRTPLHVaaFLG-----DAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAV-QVLIKHSAD 74
Cdd:PHA03095 32 RLLAAGADVNFRGEYGKTPLHL--YLHyssekVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDViKLLIKAGAD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 75 VNARDKNWQTPLHVAAANKAVkcaeviipllssvnvsdrggrtalhhaalngHMEMVNLLLAKGANINAFDKKDRRALHw 154
Cdd:PHA03095 110 VNAKDKVGRTPLHVYLSGFNI-------------------------------NPKVIRLLLRKGADVNALDLYGMTPLA- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 155 aAYMGH----LDVVALLINHGAEVTCKDKKGYTPLHAAASNGQIS--VVKHLLNLGVEIDEINVYGNTALHIACYNG--Q 226
Cdd:PHA03095 158 -VLLKSrnanVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATGSscK 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 755492548 227 DAVVNELIDYGANVNQPNNSGFTPLHFAAASTHGALCLELLvNNGADVNIQSKDGKSPL 285
Cdd:PHA03095 237 RSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLI-ALGADINAVSSDGNTPL 294
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
479-753 |
6.50e-37 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 140.86 E-value: 6.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 479 NKMILGNAHDNSEELERAREVKEKDAALCLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNTGFEESDGG 558
Cdd:COG0666 8 LLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 559 AlkSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQGASIFVKDNvTKRTPLHASVING 638
Cdd:COG0666 88 N--TLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN-DGNTPLHLAAANG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 639 HTLCLRLLLE-TADnpevVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIVGCTALHRGIMTGHEECVQMLLE 717
Cdd:COG0666 165 NLEIVKLLLEaGAD----VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
|
250 260 270
....*....|....*....|....*....|....*.
gi 755492548 718 QEASILCKDSRGRTPLHYAAARGHATWLNELLQIAL 753
Cdd:COG0666 241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALL 276
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
30-276 |
1.43e-36 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 143.65 E-value: 1.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 30 EIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAV-----KCAEVIIPL 104
Cdd:PHA03100 16 KNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 105 LSSVNVSDRGGRTALHHAALN--GHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGH--LDVVALLINHGAEVTCKDKk 180
Cdd:PHA03100 96 GANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKNR- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 181 gytplhaaasngqisvVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHFAAASTHG 260
Cdd:PHA03100 175 ----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNK 238
|
250
....*....|....*.
gi 755492548 261 ALcLELLVNNGADVNI 276
Cdd:PHA03100 239 EI-FKLLLNNGPSIKT 253
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
508-788 |
2.34e-36 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 139.32 E-value: 2.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 508 LEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNTGFEESDGGALKSPLHLAAYNGHHQALEVLLQSLVDLD 587
Cdd:COG0666 2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 588 IRDEKGRTALYLAAFKGHTECVEALVNQGASIFVKDNvTKRTPLHASVINGHTLCLRLLLET-ADnpevVDVKDAKGQTP 666
Cdd:COG0666 82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDK-DGETPLHLAAYNGNLEIVKLLLEAgAD----VNAQDNDGNTP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 667 LMLAVAYGHIDAVSLLLEKEANVDAVDIVGCTALHRGIMTGHEECVQMLLEQEASILCKDSRGRTPLHYAAARGHATWLN 746
Cdd:COG0666 157 LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVK 236
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 755492548 747 ELLQIALSEEDcclKDNQGYTPLHWACYNGNENCIEVLLEQK 788
Cdd:COG0666 237 LLLEAGADLNA---KDKDGLTALLLAAAAGAALIVKLLLLAL 275
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
129-498 |
1.26e-35 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 137.39 E-value: 1.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 129 EMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQISVVKHLLNLGVEID 208
Cdd:COG0666 2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 209 EINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHFAAASTHGALcLELLVNNGADVNIQskdgksplhmt 288
Cdd:COG0666 82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI-VKLLLEAGADVNAQ----------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 289 avhgrftrsqtliqnggeidcvDKDGNTPLHVAARHGHELLINTLITSGADtakcgihsmfplhlaalnahsdccrklls 368
Cdd:COG0666 150 ----------------------DNDGNTPLHLAAANGNLEIVKLLLEAGAD----------------------------- 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 369 sgqkysivslfsnehvlsagfeIDTPDTFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIK 448
Cdd:COG0666 179 ----------------------VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVK 236
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 755492548 449 ALVTTGANVNETDDWGRTALHYAAASDMDRNKMILGNAHDNSEELERARE 498
Cdd:COG0666 237 LLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLL 286
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
3-241 |
4.10e-34 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 136.33 E-value: 4.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 3 IHKTEDVN-ALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLH-----RAVASRSEEAVQVLIKHSADVN 76
Cdd:PHA03100 21 IIMEDDLNdYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGANVN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 77 ARDKNWQTPLHVAAANKavKCAEVIIPLLSS----VNVSDRGGRTALHHAALNGH--MEMVNLLLAKGANINAfdkKDRr 150
Cdd:PHA03100 101 APDNNGITPLLYAISKK--SNSYSIVEYLLDnganVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINA---KNR- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 151 alhwaaymghldvVALLINHGAEVTCKDKKGYTPLHAAASNGQISVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVV 230
Cdd:PHA03100 175 -------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIF 241
|
250
....*....|.
gi 755492548 231 NELIDYGANVN 241
Cdd:PHA03100 242 KLLLNNGPSIK 252
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
1-339 |
9.13e-34 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 139.43 E-value: 9.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 1 MLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDK 80
Cdd:PHA02876 163 MLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 81 NwqtpLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHM-EMVNLLLAKGANINAFDKKDRRALHWAAYMG 159
Cdd:PHA02876 243 S----LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAKNG 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 160 H-LDVVALLINHGAEVTCKDKKGYTPLHAAAS-NGQISVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYG 237
Cdd:PHA02876 319 YdTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYG 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 238 ANVNQPNNSGFTPLHFAAASTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHG-RFTRSQTLIQNGGEIDCVDKDGNT 316
Cdd:PHA02876 399 ADIEALSQKIGTALHFALCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQY 478
|
330 340
....*....|....*....|...
gi 755492548 317 PLHVAArhGHELLINTLITSGAD 339
Cdd:PHA02876 479 PLLIAL--EYHGIVNILLHYGAE 499
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
31-360 |
3.89e-32 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 134.42 E-value: 3.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 31 IIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVNV 110
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINK 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 111 SDrggrTALHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLD-VVALLINHGAEVTCKDKKGYTPLHAAA 189
Cdd:PHA02876 240 ND----LSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMA 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 190 SNG-QISVVKHLLNLGVEIDEINVYGNTALHIACY--NGQDAVVNeLIDYGANVNQPNNSGFTPLHFAAAStHGALCLEL 266
Cdd:PHA02876 316 KNGyDTENIRTLIMLGADVNAADRLYITPLHQASTldRNKDIVIT-LLELGANVNARDYCDKTPIHYAAVR-NNVVIINT 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 267 LVNNGADVNIQSKDGKSPLHMtAVHGR--FTRSQTLIQNGGEIDCVDKDGNTPLHVAARHGHEL-LINTLITSGADTAKC 343
Cdd:PHA02876 394 LLDYGADIEALSQKIGTALHF-ALCGTnpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKLdVIEMLLDNGADVNAI 472
|
330
....*....|....*..
gi 755492548 344 GIHSMFPLhLAALNAHS 360
Cdd:PHA02876 473 NIQNQYPL-LIALEYHG 488
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
643-972 |
9.09e-32 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 126.22 E-value: 9.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 643 LRLLLETADNPEVVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIVGCTALHRGIMTGHEECVQMLLEQEASI 722
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 723 LCKDSRGRTPLHYAAARGHATWLNELLQialSEEDCCLKDNQGYTPLHWACYNGNENCIEVLLEQkcfrkfignpftplh 802
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLE---AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA--------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 803 caiinghescaslllGAiDPSIvscRDDKGRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVD 882
Cdd:COG0666 143 ---------------GA-DVNA---QDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 883 ILVNsAQADLTVKDKDLNTPLHLAISKGHEKCALLILDKIQDeslINAKNSALQTPLHIAARNGLKVVVEELLAKGACVL 962
Cdd:COG0666 204 LLLE-AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD---LNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLA 279
|
330
....*....|
gi 755492548 963 AVDENGHTPA 972
Cdd:COG0666 280 AALLDLLTLL 289
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
27-342 |
3.48e-31 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 127.77 E-value: 3.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 27 GDAEIIELLILS-GARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVA---AANKAVKcaeviI 102
Cdd:PHA02874 12 GDIEAIEKIIKNkGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAikiGAHDIIK-----L 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 103 PLLSSVNVSdrggrtALHHAALNGhmEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGY 182
Cdd:PHA02874 87 LIDNGVDTS------ILPIPCIEK--DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 183 TPLHAAASNGQISVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHfaAASTHGAL 262
Cdd:PHA02874 159 YPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLH--NAIIHNRS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 263 CLELLVNNgADVNIQSKDGKSPLHMtAVHGRFTRS--QTLIQNGGEIDCVDKDGNTPLHVAARHGH------ELLINTLI 334
Cdd:PHA02874 237 AIELLINN-ASINDQDIDGSTPLHH-AINPPCDIDiiDILLYHKADISIKDNKGENPIDTAFKYINkdpvikDIIANAVL 314
|
....*...
gi 755492548 335 TSGADTAK 342
Cdd:PHA02874 315 IKEADKLK 322
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
264-597 |
5.20e-31 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 123.91 E-value: 5.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 264 LELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARHGHELLINTLITSGADTAKC 343
Cdd:COG0666 4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 344 GIHSMFPLHLAALNAHSDCCRKLLSsgqkysivslfsnehvlsAGFEIDTPDTFGRTCLHAAAAGGNVECIKLLQSSGAD 423
Cdd:COG0666 84 DDGGNTLLHAAARNGDLEIVKLLLE------------------AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGAD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 424 FHKKDKCGRTPLHYAAANCHFHCIKALVTTGANVNETDDWGRTALHYAAASdmdrnkmilgnahdNSEELerarevkekd 503
Cdd:COG0666 146 VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAEN--------------GHLEI---------- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 504 aalcLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNTGFEESDGGalKSPLHLAAYNGHHQALEVLLQSL 583
Cdd:COG0666 202 ----VKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDG--LTALLLAAAAGAALIVKLLLLAL 275
|
330
....*....|....
gi 755492548 584 VDLDIRDEKGRTAL 597
Cdd:COG0666 276 LLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
467-733 |
8.21e-31 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 123.14 E-value: 8.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 467 ALHYAAASDMDRNKMILGNAHDNSEELERAREVKEKDAALCLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLE 546
Cdd:COG0666 29 ALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 547 R-TNTGFEESDGGalkSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQGASIFVKDNv 625
Cdd:COG0666 109 AgADVNARDKDGE---TPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 626 TKRTPLHASVINGHTLCLRLLLET-ADnpevVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIVGCTALHRGI 704
Cdd:COG0666 185 DGETPLHLAAENGHLEIVKLLLEAgAD----VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAA 260
|
250 260
....*....|....*....|....*....
gi 755492548 705 MTGHEECVQMLLEQEASILCKDSRGRTPL 733
Cdd:COG0666 261 AAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
677-990 |
2.97e-30 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 121.60 E-value: 2.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 677 DAVSLLLEKEANVDAVDIVGCTALHRGIMTGHEECVQMLLEQEASILCKDSRGRTPLHYAAARGHATWLNELLQIALSEE 756
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 757 DccLKDNQGYTPLHWACYNGNENCIEVLLEQKcfrkfignpftplhcAIINGhescaslllgaidpsivscRDDKGRTTL 836
Cdd:COG0666 81 N--AKDDGGNTLLHAAARNGDLEIVKLLLEAG---------------ADVNA-------------------RDKDGETPL 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 837 HAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNsAQADLTVKDKDLNTPLHLAISKGHEKCAL 916
Cdd:COG0666 125 HLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLE-AGADVNARDNDGETPLHLAAENGHLEIVK 203
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755492548 917 LILDKIQDeslINAKNSALQTPLHIAARNGLKVVVEELLAKGACVLAVDENGHTPALACAPNKDVADCLALILA 990
Cdd:COG0666 204 LLLEAGAD---VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLA 274
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
228-527 |
8.87e-30 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 120.44 E-value: 8.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 228 AVVNELIDYGANVNQPNNSGFTPLHFAAASTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEI 307
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 308 DCVDKDGNTPLHVAARHGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLLSsgqkysivslfsnehvlsA 387
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLE------------------A 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 388 GFEIDTPDTFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIKALVTTGANVNETDDWGRTA 467
Cdd:COG0666 143 GADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTA 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 468 LHYAAASDMDRNKMILGNAHDNSEELERAREVKEKDAALCLEFLLQNDANPSIRDKEGYN 527
Cdd:COG0666 223 LDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
385-662 |
2.19e-28 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 116.21 E-value: 2.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 385 LSAGFEIDTPDTFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIKALVTTGANVNETDDWG 464
Cdd:COG0666 74 LAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDG 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 465 RTALHYAAASdmdrnkmilgnahdNSEELerarevkekdaalcLEFLLQNDANPSIRDKEGYnsihyaaayghrqclell 544
Cdd:COG0666 154 NTPLHLAAAN--------------GNLEI--------------VKLLLEAGADVNARDNDGE------------------ 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 545 lertntgfeesdggalkSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQGASIFVKDN 624
Cdd:COG0666 188 -----------------TPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250
|
250 260 270
....*....|....*....|....*....|....*...
gi 755492548 625 VTKRTPLHASVINGHTLCLRLLLETADNPEVVDVKDAK 662
Cdd:COG0666 251 DGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
98-458 |
3.75e-28 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 121.71 E-value: 3.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 98 AEVIIPLLSSVNVSDRGGRTALHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCK 177
Cdd:PHA02876 161 AEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKN 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 178 DkkgyTPLHAAASNGQISVVKHLLNLGVEIDEINVYGNTALHIACYNGQ-DAVVNELIDYGANVNQPNNSGFTPLHFAAA 256
Cdd:PHA02876 241 D----LSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAK 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 257 STHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQ-TLIQNGGEIDCVDKDGNTPLHVAARHGHELLINTLIT 335
Cdd:PHA02876 317 NGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIViTLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLD 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 336 SGADtakcgihsmfplhLAALNahsdccrkllssgQKYSivslfsnehvlsagfeidtpdtfgrTCLHAAAAGGN-VECI 414
Cdd:PHA02876 397 YGAD-------------IEALS-------------QKIG-------------------------TALHFALCGTNpYMSV 425
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 755492548 415 KLLQSSGADFHKKDKCGRTPLHYAAA-NCHFHCIKALVTTGANVN 458
Cdd:PHA02876 426 KTLIDRGANVNSKNKDLSTPLHYACKkNCKLDVIEMLLDNGADVN 470
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
50-321 |
6.95e-26 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 112.67 E-value: 6.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 50 LTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVA--AANKavkcaEVIIPLLSSVNVSDRG-GRTALHHAALNG 126
Cdd:PHA02878 38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIIckEPNK-----LGMKEMIRSINKCSVFyTLVAIKDAFNNR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 127 HMEMVNLLLakganINAFDKK---DRRALHWAAYMGHLD--VVALLINHGAEVTCKDK-KGYTPLHAAASNGQISVVKHL 200
Cdd:PHA02878 113 NVEIFKIIL-----TNRYKNIqtiDLVYIDKKSKDDIIEaeITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 201 LNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHFAAASTHGALCLELLVNNGADVNIQSK- 279
Cdd:PHA02878 188 LSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDYDILKLLLEHGVDVNAKSYi 267
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 755492548 280 DGKSPLHMTAVHGRFTRsqTLIQNGGEIDCVDKDGNTPLHVA 321
Cdd:PHA02878 268 LGLTALHSSIKSERKLK--LLLEYGADINSLNSYKLTPLSSA 307
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
187-468 |
1.54e-25 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 111.66 E-value: 1.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 187 AAASNGQISVVKHLLNLGVEIDEINVYGNTALH--IACYNGQDA-VVNELIDYGANVNQPNNSGFTPLHFAAASTHGALC 263
Cdd:PHA03095 20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHlyLHYSSEKVKdIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 264 LELLVNNGADVNIQSKDGKSPLH--MTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAAR-HGHEL-LINTLITSGAD 339
Cdd:PHA03095 100 IKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKsRNANVeLLRLLIDAGAD 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 340 TAKCGIHSMFPLHLAALNAHSDccrkllssgqkYSIVslfsnEHVLSAGFEIDTPDTFGRTCLHAAAAGGNVECIKLLQ- 418
Cdd:PHA03095 180 VYAVDDRFRSLLHHHLQSFKPR-----------ARIV-----RELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVLPl 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 755492548 419 -SSGADFHKKDKCGRTPLHYAAA--NCHF--HCIKAlvttGANVNETDDWGRTAL 468
Cdd:PHA03095 244 lIAGISINARNRYGQTPLHYAAVfnNPRAcrRLIAL----GADINAVSSDGNTPL 294
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
4-270 |
2.85e-22 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 101.50 E-value: 2.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 4 HKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIK------------- 70
Cdd:PHA02878 25 HTENYSTSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRsinkcsvfytlva 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 71 -----HSADVNA-------RDKNWQTP--LHVAAANKAVKCAEVIIPLL----SSVNVSDR-GGRTALHHAALNGHMEMV 131
Cdd:PHA02878 105 ikdafNNRNVEIfkiiltnRYKNIQTIdlVYIDKKSKDDIIEAEITKLLlsygADINMKDRhKGNTALHYATENKDQRLT 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 132 NLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASN-GQISVVKHLLNLGVEID-E 209
Cdd:PHA02878 185 ELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNaK 264
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755492548 210 INVYGNTALHIACYNGQdaVVNELIDYGANVNQPNNSGFTPLHFAAASTHGALCLELLVNN 270
Cdd:PHA02878 265 SYILGLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPLSSAVKQYLCINIGRILISN 323
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
330-657 |
1.13e-21 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 99.71 E-value: 1.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 330 INTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRkllssgqkysIVSLfsnehVLSAGFEIDTPDTFGRTCLHAAAAGG 409
Cdd:PHA03095 30 VRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKD----------IVRL-----LLEAGADVNAPERCGFTPLHLYLYNA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 410 NVE-CIKLLQSSGADFHKKDKCGRTPLH-YAA-ANCHFHCIKALVTTGANVNETDDWGRTALHyaaasdmdrnkmILGNA 486
Cdd:PHA03095 95 TTLdVIKLLIKAGADVNAKDKVGRTPLHvYLSgFNINPKVIRLLLRKGADVNALDLYGMTPLA------------VLLKS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 487 HDNSEELerarevkekdaalcLEFLLQNDANPSIRDKEGYNSIHYAAAYGH--RQCLELLLERTNTGFEESDGGalKSPL 564
Cdd:PHA03095 163 RNANVEL--------------LRLLIDAGADVYAVDDRFRSLLHHHLQSFKprARIVRELIRAGCDPAATDMLG--NTPL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 565 HLAAYNGHHQALEV--LLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQGASIFVKDNvTKRTPLHASVINGHTLC 642
Cdd:PHA03095 227 HSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSS-DGNTPLSLMVRNNNGRA 305
|
330
....*....|....*
gi 755492548 643 LRLLLETADNPEVVD 657
Cdd:PHA03095 306 VRAALAKNPSAETVA 320
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
167-523 |
1.22e-21 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 98.97 E-value: 1.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 167 LINHGAEVTCKDKKGYTPLHAAASNGQISVVKHLLNLGVEIDEINVYGNTALHIAC---YNGQDAV--VNELIDYGANVN 241
Cdd:PHA03100 21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSnikYNLTDVKeiVKLLLEYGANVN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 242 QPNNSGFTPLHFAAASTHGALCL-ELLVNNGADVNIQSKDGKSPLHMtavhgrFTRSqtliqnggeiDCVDKDgntplhv 320
Cdd:PHA03100 101 APDNNGITPLLYAISKKSNSYSIvEYLLDNGANVNIKNSDGENLLHL------YLES----------NKIDLK------- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 321 aarhghelLINTLITSGADtakcgihsmfplhlaaLNAhsdCCRkllssgqkysivslfsnehvlsagfeidtpdtfgrt 400
Cdd:PHA03100 158 --------ILKLLIDKGVD----------------INA---KNR------------------------------------ 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 401 clhaaaaggnvecIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIKALVTTGANVNETDDWGRTALHYAAASdmdRNK 480
Cdd:PHA03100 175 -------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILN---NNK 238
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 755492548 481 MILgnahdnSEELERAREVKEKDAALclefLLQNDANPSIRDK 523
Cdd:PHA03100 239 EIF------KLLLNNGPSIKTIIETL----LYFKDKDLNTITK 271
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
8-211 |
1.61e-21 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 98.88 E-value: 1.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 8 DVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLH 87
Cdd:PHA02874 116 DVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLH 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 88 VAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALngHMEMVNLLLAKGANINAFDKKDRRALHWA-AYMGHLDVVAL 166
Cdd:PHA02874 196 NAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAiNPPCDIDIIDI 273
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 755492548 167 LINHGAEVTCKDKKGYTPLHAAASN-GQISVVKHLLNLGVEIDEIN 211
Cdd:PHA02874 274 LLYHKADISIKDNKGENPIDTAFKYiNKDPVIKDIIANAVLIKEAD 319
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
298-600 |
5.66e-21 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 96.96 E-value: 5.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 298 QTLIQNGGE-IDCVDKDGNTPLHVAARHGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSGQKYSIV 376
Cdd:PHA02874 18 EKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSIL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 377 SL--FSNEHV---LSAGFEIDTPDTFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIKALV 451
Cdd:PHA02874 98 PIpcIEKDMIktiLDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 452 TTGANVNETDDWGRTALHYAaasdmdrnkmilgnahdnseelerareVKEKDAAlCLEFLLQNDANPSIRDKEGYNSIHY 531
Cdd:PHA02874 178 EKGAYANVKDNNGESPLHNA---------------------------AEYGDYA-CIKLLIDHGNHIMNKCKNGFTPLHN 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 532 AAAYgHRQCLELLLERTNTGFEESDGgalKSPLHLA-AYNGHHQALEVLLQSLVDLDIRDEKGRTALYLA 600
Cdd:PHA02874 230 AIIH-NRSAIELLINNASINDQDIDG---STPLHHAiNPPCDIDIIDILLYHKADISIKDNKGENPIDTA 295
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
152-244 |
8.74e-21 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 87.86 E-value: 8.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 152 LHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQISVVKHLLNlGVEIDEINvYGNTALHIACYNGQDAVVN 231
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 755492548 232 ELIDYGANVNQPN 244
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
644-959 |
9.46e-21 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 96.63 E-value: 9.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 644 RLLLETADnpevVDVKDAKGQTPLMLAVAYGH---IDAVSLLLEKEANVDAVDIVGCTALHRGIMTGHEE-CVQMLLEQE 719
Cdd:PHA03095 32 RLLAAGAD----VNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 720 ASILCKDSRGRTPLH-YAA-ARGHATWLNELLQIALseeDCCLKDNQGYTPLHwaCYNGNENC----IEVLLEQKCF--- 790
Cdd:PHA03095 108 ADVNAKDKVGRTPLHvYLSgFNINPKVIRLLLRKGA---DVNALDLYGMTPLA--VLLKSRNAnvelLRLLIDAGADvya 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 791 RKFIGNpfTPLH--CAIINGHESCASLLLGA-IDPsivSCRDDKGRTTLHAAAFGDHAECLQL--LLRHDAQVNAVDNSG 865
Cdd:PHA03095 183 VDDRFR--SLLHhhLQSFKPRARIVRELIRAgCDP---AATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 866 KTALMMAAENGQAGAVDILVNsAQADLTVKDKDLNTPLHLAISKGHEKCALLILDKIQDESLINAKNSALQTPLHIAARN 945
Cdd:PHA03095 258 QTPLHYAAVFNNPRACRRLIA-LGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAATLNTASVAGGDIPSD 336
|
330
....*....|....
gi 755492548 946 GLKVVVEELLAKGA 959
Cdd:PHA03095 337 ATRLCVAKVVLRGA 350
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
1-210 |
2.80e-20 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 95.48 E-value: 2.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 1 MLIHKTEDVNALDSEKRTPLHV--AAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASR--SEEAVQVLIKHSADVN 76
Cdd:PHA03095 102 LLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRnaNVELLRLLIDAGADVY 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 77 ARDKNWQTPLHVAAAN--KAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHMEMVNL--LLAKGANINAFDKKDRRAL 152
Cdd:PHA03095 182 AVDDRFRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPL 261
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 755492548 153 HWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQISVVKHLLNLGVEIDEI 210
Cdd:PHA03095 262 HYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETV 319
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
119-211 |
3.13e-20 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 86.32 E-value: 3.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 119 LHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHgAEVTCKDkKGYTPLHAAASNGQISVVK 198
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 755492548 199 HLLNLGVEIDEIN 211
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
23-241 |
3.94e-20 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 94.29 E-value: 3.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 23 AAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVII 102
Cdd:PHA02875 9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 103 PLLSSVN-VSDRGGRTALHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKG 181
Cdd:PHA02875 89 DLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCG 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755492548 182 YTPLHAAASNGQISVVKHLLNLGVEIDEINVYGN-TALHIACYNGQDAVVNELIDYGANVN 241
Cdd:PHA02875 169 CTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADCN 229
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
372-657 |
1.40e-19 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 92.81 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 372 KYSIVSLFSNEHVLSAGFEIDTPDTFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCH-----FHC 446
Cdd:PHA03100 9 KSRIIKVKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 447 IKALVTTGANVNETDDWGRTALHYAAASDMDRNKMIlgnahdnseelerarevkekdaalclEFLLQNDANPSIRDKEGY 526
Cdd:PHA03100 89 VKLLLEYGANVNAPDNNGITPLLYAISKKSNSYSIV--------------------------EYLLDNGANVNIKNSDGE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 527 NSIHYAAAYGHR--QCLELLLERTNtgfeesdggalksplHLAAYNghhqALEVLLQSLVDLDIRDEKGRTALYLAAFKG 604
Cdd:PHA03100 143 NLLHLYLESNKIdlKILKLLIDKGV---------------DINAKN----RVNYLLSYGVPINIKDVYGFTPLHYAVYNN 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 755492548 605 HTECVEALVNQGASIFVKDNVTKrTPLHASVINGHTLCLRLLLETADNPEVVD 657
Cdd:PHA03100 204 NPEFVKYLLDLGANPNLVNKYGD-TPLHIAILNNNKEIFKLLLNNGPSIKTII 255
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
157-689 |
2.73e-19 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 93.59 E-value: 2.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 157 YMGHLDVVALLIN-----HGAEvTCKDKK-GYTPLHAAASNGQISVVKHLLNLGVEIDEINVYG-NTALHIACY--NGQD 227
Cdd:PHA02876 12 RGNCIDILSAIDNydlhkHGAN-QCENESiPFTAIHQALQLRQIDIVEEIIQQNPELIYITDHKcHSTLHTICIipNVMD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 228 AVVNELIDYGANVNQPNNSGFTPLHfaaasTHGALCLELLVN--NGADVNIqSKDGKSPLHMTAVHGRFTR-----SQTL 300
Cdd:PHA02876 91 IVISLTLDCDIILDIKYASIILNKH-----KLDEACIHILKEaiSGNDIHY-DKINESIEYMKLIKERIQQdelliAEML 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 301 IQNGGEIDCVDKDGNTPLHVAARHGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLLS-----SGQKYSI 375
Cdd:PHA02876 165 LEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDnrsniNKNDLSL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 376 VSLFSNEH------VLSAGFEIDTPDTFGRTCLHAAAAGGNVECI--KLLQsSGADFHKKDKCGRTPLHYAAANCH-FHC 446
Cdd:PHA02876 245 LKAIRNEDletsllLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLvpKLLE-RGADVNAKNIKGETPLYLMAKNGYdTEN 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 447 IKALVTTGANVNETDDWGRTALHyaAASDMDRNKMILGNahdnseelerarevkekdaalclefLLQNDANPSIRDKEGY 526
Cdd:PHA02876 324 IRTLIMLGADVNAADRLYITPLH--QASTLDRNKDIVIT-------------------------LLELGANVNARDYCDK 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 527 NSIHYAAAYGHRQCLELLLertntgfeesDGGAlksplhlaaynghhqalevllqslvDLDIRDEKGRTALYLAAFKGHT 606
Cdd:PHA02876 377 TPIHYAAVRNNVVIINTLL----------DYGA-------------------------DIEALSQKIGTALHFALCGTNP 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 607 -ECVEALVNQGASIFVKdNVTKRTPLHASVINGHTL-CLRLLLetaDNPEVVDVKDAKGQTPLMLAVAYGHIdaVSLLLE 684
Cdd:PHA02876 422 yMSVKTLIDRGANVNSK-NKDLSTPLHYACKKNCKLdVIEMLL---DNGADVNAINIQNQYPLLIALEYHGI--VNILLH 495
|
....*
gi 755492548 685 KEANV 689
Cdd:PHA02876 496 YGAEL 500
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
86-178 |
6.32e-19 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 82.47 E-value: 6.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 86 LHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHMEMVNLLLAKgANINAFDkKDRRALHWAAYMGHLDVVA 165
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 755492548 166 LLINHGAEVTCKD 178
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
597-693 |
1.79e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 81.32 E-value: 1.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 597 LYLAAFKGHTECVEALVNQGASIFVKDNvTKRTPLHASVINGHTLCLRLLLETADnpevVDVKDaKGQTPLMLAVAYGHI 676
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDK-NGRTALHLAAKNGHLEIVKLLLEHAD----VNLKD-NGRTALHYAARSGHL 74
|
90
....*....|....*..
gi 755492548 677 DAVSLLLEKEANVDAVD 693
Cdd:pfam12796 75 EIVKLLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
185-277 |
2.22e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 80.93 E-value: 2.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 185 LHAAASNGQISVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYgANVNQPNNsGFTPLHFAAASTHGAlCL 264
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLE-IV 77
|
90
....*....|...
gi 755492548 265 ELLVNNGADVNIQ 277
Cdd:pfam12796 78 KLLLEKGADINVK 90
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
564-657 |
7.13e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 79.39 E-value: 7.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 564 LHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQgasIFVKDNVTKRTPLHASVINGHTLCL 643
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLEIV 77
|
90
....*....|....
gi 755492548 644 RLLLETADNPEVVD 657
Cdd:pfam12796 78 KLLLEKGADINVKD 91
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
17-173 |
2.90e-17 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 85.43 E-value: 2.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 17 RTPLHVAAFLGDAEIIELLILSGARVN---AKDNMwlTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANK 93
Cdd:PHA02875 69 ESELHDAVEEGDVKAVEELLDLGKFADdvfYKDGM--TPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMG 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 94 AVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHMEMVNLLLAKGANINAFDKK-DRRALHWAAYMGHLDVVALLINHGA 172
Cdd:PHA02875 147 DIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNgCVAALCYAIENNKIDIVRLFIKRGA 226
|
.
gi 755492548 173 E 173
Cdd:PHA02875 227 D 227
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
564-839 |
3.98e-17 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 85.40 E-value: 3.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 564 LHLAAYNGHHQALEVLLQSLVD-LDIRDEKGRTALYLAAFKGHTECVEALVNQGASIfvkDNVTKRTP---LHASVINGH 639
Cdd:PHA02874 5 LRMCIYSGDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADI---NHINTKIPhplLTAIKIGAH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 640 TLCLRLLLETADN-----PEV--------------VDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIVGCTAL 700
Cdd:PHA02874 82 DIIKLLIDNGVDTsilpiPCIekdmiktildcgidVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 701 HRGIMTGHEECVQMLLEQEASILCKDSRGRTPLHYAAARGHATWLNELLQialSEEDCCLKDNQGYTPLHWACYNgNENC 780
Cdd:PHA02874 162 HIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLID---HGNHIMNKCKNGFTPLHNAIIH-NRSA 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755492548 781 IEVLLEQKCFRKFIGNPFTPLHCAIingHESCA-----SLLLGAIDPSIvscRDDKGRTTLHAA 839
Cdd:PHA02874 238 IELLINNASINDQDIDGSTPLHHAI---NPPCDidiidILLYHKADISI---KDNKGENPIDTA 295
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
20-145 |
5.14e-17 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 77.08 E-value: 5.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 20 LHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHsADVNARDKnwqtplhvaaankavkcae 99
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN------------------- 60
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 755492548 100 viipllssvnvsdrgGRTALHHAALNGHMEMVNLLLAKGANINAFD 145
Cdd:pfam12796 61 ---------------GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
836-932 |
1.20e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 75.92 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 836 LHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNSAQADLTVKDKdlnTPLHLAISKGHEKCA 915
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR---TALHYAARSGHLEIV 77
|
90
....*....|....*..
gi 755492548 916 LLILDKIQDeslINAKN 932
Cdd:pfam12796 78 KLLLEKGAD---INVKD 91
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
191-538 |
1.27e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 83.86 E-value: 1.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 191 NGQISVVKHLLN-----LGVEIDEINvygnTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLhFAAASTHGALCLE 265
Cdd:PHA02874 11 SGDIEAIEKIIKnkgncINISVDETT----TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPL-LTAIKIGAHDIIK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 266 LLVNNGADVNIqskdgkspLHMTAVHGRFTRsqTLIQNGGEIDCVDKDGNTPLHVAARHGHELLINTLITSGADTAKCGI 345
Cdd:PHA02874 86 LLIDNGVDTSI--------LPIPCIEKDMIK--TILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 346 HSMFPLHLAalnahsdccrkllSSGQKYSIVSLfsnehVLSAGFEIDTPDTFGRTCLHAAAAGGNVECIKLLQSSGADFH 425
Cdd:PHA02874 156 NGCYPIHIA-------------IKHNFFDIIKL-----LLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIM 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 426 KKDKCGRTPLHYAAanCHFHCIKALVTTGANVNETDDWGRTALHYAAASDMDRNkmilgnahdnseelerarevkekdaa 505
Cdd:PHA02874 218 NKCKNGFTPLHNAI--IHNRSAIELLINNASINDQDIDGSTPLHHAINPPCDID-------------------------- 269
|
330 340 350
....*....|....*....|....*....|...
gi 755492548 506 lCLEFLLQNDANPSIRDKEGYNSIHYAAAYGHR 538
Cdd:PHA02874 270 -IIDILLYHKADISIKDNKGENPIDTAFKYINK 301
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
508-720 |
2.07e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 82.73 E-value: 2.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 508 LEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLerTNTGFEESDGGALKSPLHLAAYNGHHQALEVLLQS--LVD 585
Cdd:PHA02875 18 ARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLM--KHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLgkFAD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 586 lDIRDEKGRTALYLAAFKGHTECVEALVNQGASIFVKdNVTKRTPLHASVINGHTLCLRLLLetaDNPEVVDVKDAKGQT 665
Cdd:PHA02875 96 -DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIP-NTDKFSPLHLAVMMGDIKGIELLI---DHKACLDIEDCCGCT 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 755492548 666 PLMLAVAYGHIDAVSLLLEKEANVDAVDIVGC-TALHRGIMTGHEECVQMLLEQEA 720
Cdd:PHA02875 171 PLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGA 226
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
49-256 |
2.47e-16 |
|
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: 83.91 E-value: 2.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 49 WLTPLHRAVASRSEEAVQVLIK-HSADVNARDKNWQTPLHVAAANKAVKCAEVII---PLLssVNV---SD-RGGRTALH 120
Cdd:cd22192 17 SESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMeaaPEL--VNEpmtSDlYQGETALH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 121 HAALNGHMEMVNLLLAKGANIN------AFDKKDRRAL-----H---WAAYMGHLDVVALLINHGAEVTCKDKKGYTPLH 186
Cdd:cd22192 95 IAVVNQNLNLVRELIARGADVVspratgTFFRPGPKNLiyygeHplsFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755492548 187 AAASNGQISVVKH----LLNLGVEIDEINVYgntalHIacyngqdavvnelidyganvnqPNNSGFTPLHFAAA 256
Cdd:cd22192 175 ILVLQPNKTFACQmydlILSYDKEDDLQPLD-----LV----------------------PNNQGLTPFKLAAK 221
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
116-348 |
5.37e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 81.58 E-value: 5.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 116 RTALHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQIS 195
Cdd:PHA02875 3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 196 VVKHLLNLGVEIDEInVY--GNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHFAAASTHGALcLELLVNNGAD 273
Cdd:PHA02875 83 AVEELLDLGKFADDV-FYkdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKG-IELLIDHKAC 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755492548 274 VNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARHGHEL-LINTLITSGADtakCGIHSM 348
Cdd:PHA02875 161 LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIdIVRLFIKRGAD---CNIMFM 233
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
700-789 |
9.01e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 73.61 E-value: 9.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 700 LHRGIMTGHEECVQMLLEQEASILCKDSRGRTPLHYAAARGHAtwlnELLQIALSEEDCCLKDNqGYTPLHWACYNGNEN 779
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHL----EIVKLLLEHADVNLKDN-GRTALHYAARSGHLE 75
|
90
....*....|
gi 755492548 780 CIEVLLEQKC 789
Cdd:pfam12796 76 IVKLLLEKGA 85
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
529-623 |
1.07e-15 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 73.23 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 529 IHYAAAYGHRQCLELLLE-RTNTGFEESDGgalKSPLHLAAYNGHHQALEVLLQSlVDLDIRDEkGRTALYLAAFKGHTE 607
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLEnGADANLQDKNG---RTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLE 75
|
90
....*....|....*.
gi 755492548 608 CVEALVNQGASIFVKD 623
Cdd:pfam12796 76 IVKLLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
402-475 |
1.23e-15 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 73.23 E-value: 1.23e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755492548 402 LHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIKALVTTgANVNETDDwGRTALHYAAASD 475
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSG 72
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
53-339 |
1.35e-15 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 81.03 E-value: 1.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 53 LHRAvaSRSEEAVQVLIKHSADVNARDKNWQTPLhvaaankavkCAeviipLLSsvNVSDrggrtalhhaaLNGHMEMVN 132
Cdd:PHA02798 44 LQRD--SPSTDIVKLFINLGANVNGLDNEYSTPL----------CT-----ILS--NIKD-----------YKHMLDIVK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 133 LLLAKGANINAFDKKDRRALHWA---AYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNG---QISVVKHLLNLGVE 206
Cdd:PHA02798 94 ILIENGADINKKNSDGETPLYCLlsnGYINNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNhhiDIEIIKLLLEKGVD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 207 IDEI-NVYGNTALHiaCY-----NGQDA-VVNELIDYGANVNQPNNSgftplhfaAASTHGALCLELLVNNG-------- 271
Cdd:PHA02798 174 INTHnNKEKYDTLH--CYfkyniDRIDAdILKLFVDNGFIINKENKS--------HKKKFMEYLNSLLYDNKrfkknild 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755492548 272 ---ADVNIQSKD--GKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARHGHELLINTLITSGAD 339
Cdd:PHA02798 244 fifSYIDINQVDelGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKPN 316
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
382-736 |
1.63e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 81.26 E-value: 1.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 382 EHVLSAGFEIDTPDTFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIKALVTTGANVNetd 461
Cdd:PHA02876 162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNIN--- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 462 dwgrtalhyaaasdmdRNKMILGNAHDNsEELERArevkekdaalclefLLQNDANPSIRDKEGYNSihyaaayghrqcl 541
Cdd:PHA02876 239 ----------------KNDLSLLKAIRN-EDLETS--------------LLLYDAGFSVNSIDDCKN------------- 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 542 elllertntgfeesdggalkSPLHLAAYNGHHQAL-EVLLQSLVDLDIRDEKGRTALYLAAFKGH-TECVEALVNQGASI 619
Cdd:PHA02876 275 --------------------TPLHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADV 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 620 FVKDNVTKrTPLH-ASVINGHTLCLRLLLETADNpevVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIVGCT 698
Cdd:PHA02876 335 NAADRLYI-TPLHqASTLDRNKDIVITLLELGAN---VNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGT 410
|
330 340 350
....*....|....*....|....*....|....*....
gi 755492548 699 ALHRGIM-TGHEECVQMLLEQEASILCKDSRGRTPLHYA 736
Cdd:PHA02876 411 ALHFALCgTNPYMSVKTLIDRGANVNSKNKDLSTPLHYA 449
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
542-724 |
1.74e-15 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 81.45 E-value: 1.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 542 ELLLERTntgfEESDGGALKSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQGASIFV 621
Cdd:PLN03192 511 DLLGDNG----GEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHI 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 622 KDnVTKRTPLHASVINGHTLCLRLL--LETADNPEVvdvkdakGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIVGCTA 699
Cdd:PLN03192 587 RD-ANGNTALWNAISAKHHKIFRILyhFASISDPHA-------AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATA 658
|
170 180
....*....|....*....|....*
gi 755492548 700 LHRGIMTGHEECVQMLLEQEASILC 724
Cdd:PLN03192 659 LQVAMAEDHVDMVRLLIMNGADVDK 683
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
769-862 |
1.85e-15 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 72.46 E-value: 1.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 769 LHWACYNGNENCIEVLLEQKC-FRKFIGNPFTPLHCAIINGHESCASLLLGAIDPSIvscrDDKGRTTLHAAAFGDHAEC 847
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGAdANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL----KDNGRTALHYAARSGHLEI 76
|
90
....*....|....*
gi 755492548 848 LQLLLRHDAQVNAVD 862
Cdd:pfam12796 77 VKLLLEKGADINVKD 91
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
490-901 |
9.72e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 78.95 E-value: 9.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 490 SEELERAREVKEK---DAALCLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLER-TNTGFEESDGgalkspLH 565
Cdd:PHA02876 140 NESIEYMKLIKERiqqDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYgADVNIIALDD------LS 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 566 LAAYNGHHQALEVLlQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQGASIFVKDnVTKRTPLHASVINGH--TLCL 643
Cdd:PHA02876 214 VLECAVDSKNIDTI-KAIIDNRSNINKNDLSLLKAIRNEDLETSLLLYDAGFSVNSID-DCKNTPLHHASQAPSlsRLVP 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 644 RLLLETADnpevVDVKDAKGQTPLMLAVAYGH-IDAVSLLLEKEANVDAVDIVGCTALHRG-IMTGHEECVQMLLEQEAS 721
Cdd:PHA02876 292 KLLERGAD----VNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQAsTLDRNKDIVITLLELGAN 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 722 ILCKDSRGRTPLHYAAARGHATWLNELLQIALSEEdcCLKDNQGyTPLHWACYNgnencievlleqkcfrkfiGNPFTPL 801
Cdd:PHA02876 368 VNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIE--ALSQKIG-TALHFALCG-------------------TNPYMSV 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 802 HCAIINGHEscaslllgaidpsiVSCRDDKGRTTLHAAAFGD-HAECLQLLLRHDAQVNAVDNSGKTALMMAAenGQAGA 880
Cdd:PHA02876 426 KTLIDRGAN--------------VNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGI 489
|
410 420
....*....|....*....|...
gi 755492548 881 VDILVNSAQA--DLTVKDKDLNT 901
Cdd:PHA02876 490 VNILLHYGAElrDSRVLHKSLND 512
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
676-991 |
1.32e-14 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 77.76 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 676 IDAVSLLLEKEANVDAVDIVGCTALHRGIMTGHEEC---VQMLLEQEASILCKDSRGRTPLHYaaarghatwlnellqia 752
Cdd:PHA03095 27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLHL----------------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 753 lseedcclkdnqgytplhWACYNGNENCIEVLLEQKC-FRKFIGNPFTPLH--CAIINGHESCASLLLGA-IDpsiVSCR 828
Cdd:PHA03095 90 ------------------YLYNATTLDVIKLLIKAGAdVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKgAD---VNAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 829 DDKGRTTLHA--AAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAEN--GQAGAVDILVnSAQADLTVKDKDLNTPLH 904
Cdd:PHA03095 149 DLYGMTPLAVllKSRNANVELLRLLIDAGADVYAVDDRFRSLLHHHLQSfkPRARIVRELI-RAGCDPAATDMLGNTPLH 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 905 LAISKGHEKcALLILDKIQDESLINAKNSALQTPLHIAARNGLKVVVEELLAKGACVLAVDENGHTPALACAPNKDVaDC 984
Cdd:PHA03095 228 SMATGSSCK-RSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNG-RA 305
|
....*..
gi 755492548 985 LALILAT 991
Cdd:PHA03095 306 VRAALAK 312
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
1-145 |
1.56e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 77.61 E-value: 1.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 1 MLIHKTEDVNALDSEK-RTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARD 79
Cdd:PHA02878 152 LLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARD 231
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755492548 80 KNWQTPLHVAAAnkAVKCAEVIIPLL---SSVNV-SDRGGRTALHHAAlngHMEMV-NLLLAKGANINAFD 145
Cdd:PHA02878 232 KCGNTPLHISVG--YCKDYDILKLLLehgVDVNAkSYILGLTALHSSI---KSERKlKLLLEYGADINSLN 297
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
351-461 |
1.61e-14 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 69.76 E-value: 1.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 351 LHLAALNAHSDCCRKLLSSGqkysivslfsnehvlsagFEIDTPDTFGRTCLHAAAAGGNVECIKLLqSSGADFHKKDKc 430
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENG------------------ADANLQDKNGRTALHLAAKNGHLEIVKLL-LEHADVNLKDN- 60
|
90 100 110
....*....|....*....|....*....|.
gi 755492548 431 GRTPLHYAAANCHFHCIKALVTTGANVNETD 461
Cdd:pfam12796 61 GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
610-973 |
1.73e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 78.18 E-value: 1.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 610 EALVNQGASIFVKDnVTKRTPLHASVINGHTLCLRLLLETADNPEVVDVKDAkgqTPLMLAVAYGHIDAVSLLLEKEANV 689
Cdd:PHA02876 162 EMLLEGGADVNAKD-IYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDL---SVLECAVDSKNIDTIKAIIDNRSNI 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 690 DAVDIvgctALHRGIMTGHEECVQMLLEQEASILCKDSRGRTPLHYAAargHATWLNELLQIALSE-EDCCLKDNQGYTP 768
Cdd:PHA02876 238 NKNDL----SLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHAS---QAPSLSRLVPKLLERgADVNAKNIKGETP 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 769 LHWACYNGNENcievlleqkcfrkfignpftplhcaiinghESCASLLLGAIDpsiVSCRDDKGRTTLHAAAFGD-HAEC 847
Cdd:PHA02876 311 LYLMAKNGYDT------------------------------ENIRTLIMLGAD---VNAADRLYITPLHQASTLDrNKDI 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 848 LQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNSAqADLTVKDKDLNTPLHLAISKGHEKCALLILdkIQDESL 927
Cdd:PHA02876 358 VITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYG-ADIEALSQKIGTALHFALCGTNPYMSVKTL--IDRGAN 434
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 755492548 928 INAKNSALQTPLHIAARNGLKV-VVEELLAKGACVLAVDENGHTPAL 973
Cdd:PHA02876 435 VNSKNKDLSTPLHYACKKNCKLdVIEMLLDNGADVNAINIQNQYPLL 481
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
667-741 |
1.84e-14 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 69.76 E-value: 1.84e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755492548 667 LMLAVAYGHIDAVSLLLEKEANVDAVDIVGCTALHRGIMTGHEECVQMLLEQEAsiLCKDSRGRTPLHYAAARGH 741
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGH 73
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
560-736 |
2.57e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 76.54 E-value: 2.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 560 LKSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQGASIFVKDNVTKrTPLHASVINGH 639
Cdd:PHA02874 124 LKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGE-SPLHNAAEYGD 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 640 TLCLRLLLETADNpevVDVKDAKGQTPLMLAVAYGHiDAVSLLLeKEANVDAVDIVGCTALHRGIMTG-HEECVQMLLEQ 718
Cdd:PHA02874 203 YACIKLLIDHGNH---IMNKCKNGFTPLHNAIIHNR-SAIELLI-NNASINDQDIDGSTPLHHAINPPcDIDIIDILLYH 277
|
170
....*....|....*...
gi 755492548 719 EASILCKDSRGRTPLHYA 736
Cdd:PHA02874 278 KADISIKDNKGENPIDTA 295
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
733-817 |
3.98e-14 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 68.99 E-value: 3.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 733 LHYAAARGHATWLNELLQialSEEDCCLKDNQGYTPLHWACYNGNENCIEVLLEQKCFRKFiGNPFTPLHCAIINGHESC 812
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLE---NGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLK-DNGRTALHYAARSGHLEI 76
|
....*
gi 755492548 813 ASLLL 817
Cdd:pfam12796 77 VKLLL 81
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
148-383 |
7.09e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 75.03 E-value: 7.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 148 DRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQISVVKHLLNLGVeIDEINVYG-NTALHIACYNGQ 226
Cdd:PHA02875 2 DQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGA-IPDVKYPDiESELHDAVEEGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 227 DAVVNELIDYGANVNQP-NNSGFTPLHFAAASTHGALcLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGG 305
Cdd:PHA02875 81 VKAVEELLDLGKFADDVfYKDGMTPLHLATILKKLDI-MKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755492548 306 EIDCVDKDGNTPLHVAARHGHELLINTLITSGADTAKCGIHSMFPLHLAAL-NAHSDCCRKLLSSGQKYSIVSLFSNEH 383
Cdd:PHA02875 160 CLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIeNNKIDIVRLFIKRGADCNIMFMIEGEE 238
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
577-959 |
1.39e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 75.10 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 577 EVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQGA--SIFVKDNVTKrtpLHASVINGHTLCLRLLLETADNPE 654
Cdd:PHA02876 162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGAdvNIIALDDLSV---LECAVDSKNIDTIKAIIDNRSNIN 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 655 vvdvkdaKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIVGCTALHRGIMTGH-EECVQMLLEQEASILCKDSRGRTPL 733
Cdd:PHA02876 239 -------KNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 734 HYAAARGHATwlNELLQIALSEEDCCLKDNQGYTPLHWA-CYNGNENCIEVLLEqkcfrkfignpftplhcaiinghesc 812
Cdd:PHA02876 312 YLMAKNGYDT--ENIRTLIMLGADVNAADRLYITPLHQAsTLDRNKDIVITLLE-------------------------- 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 813 asllLGAidpsIVSCRDDKGRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMA-AENGQAGAVDILVNSAqAD 891
Cdd:PHA02876 364 ----LGA----NVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRG-AN 434
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755492548 892 LTVKDKDLNTPLHLAISKgheKCALLILDKIQDESL-INAKNSALQTPLHIAArnGLKVVVEELLAKGA 959
Cdd:PHA02876 435 VNSKNKDLSTPLHYACKK---NCKLDVIEMLLDNGAdVNAINIQNQYPLLIAL--EYHGIVNILLHYGA 498
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
30-248 |
2.28e-13 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 73.72 E-value: 2.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 30 EIIELLILSGARVNAKDNMWLTPLHRAVASRSE-----EAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPL 104
Cdd:PHA02798 52 DIVKLFINLGANVNGLDNEYSTPLCTILSNIKDykhmlDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLFM 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 105 L---SSVNVSDRGGRTALHHAALNGH---MEMVNLLLAKGANINAFDKKDR-RALHwaAYMGH------LDVVALLINHG 171
Cdd:PHA02798 132 IengADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINTHNNKEKyDTLH--CYFKYnidridADILKLFVDNG 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 172 ---------------------------------------AEVTCKDKKGYTPLHAAASNGQISVVKHLLNLGVEIDEINV 212
Cdd:PHA02798 210 fiinkenkshkkkfmeylnsllydnkrfkknildfifsyIDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITE 289
|
250 260 270
....*....|....*....|....*....|....*.
gi 755492548 213 YGNTALHIACYNGQDAVVNELIDYGANVNQPNNSGF 248
Cdd:PHA02798 290 LGNTCLFTAFENESKFIFNSILNKKPNKNTISYTYY 325
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
208-543 |
2.73e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 73.38 E-value: 2.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 208 DEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHFAAASTHGALCLELL-VNNGADVNIQSKDGKSPLH 286
Cdd:PHA02878 31 TSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIrSINKCSVFYTLVAIKDAFN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 287 MTAVH-------GRFTRSQTLiqNGGEIDCVDKDGNTPLHVaarhghellINTLITSGADTAKCGIHSM-FPLHLAALNA 358
Cdd:PHA02878 111 NRNVEifkiiltNRYKNIQTI--DLVYIDKKSKDDIIEAEI---------TKLLLSYGADINMKDRHKGnTALHYATENK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 359 HSDCCRKLLSSGQkysivslfsnehvlsagfEIDTPDTFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYA 438
Cdd:PHA02878 180 DQRLTELLLSYGA------------------NVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 439 AANC-HFHCIKALVTTGANVN-ETDDWGRTALHYAAASDmDRNKMILG-----NAHDNSEELERAREVKEKDAALCLEFL 511
Cdd:PHA02878 242 VGYCkDYDILKLLLEHGVDVNaKSYILGLTALHSSIKSE-RKLKLLLEygadiNSLNSYKLTPLSSAVKQYLCINIGRIL 320
|
330 340 350
....*....|....*....|....*....|....*..
gi 755492548 512 -----LQNDANPSIRDKEGYnSIHYAAAYGHRQCLEL 543
Cdd:PHA02878 321 isnicLLKRIKPDIKNSEGF-IDNMDCITSNKRLNQI 356
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
869-965 |
3.64e-13 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 65.91 E-value: 3.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 869 LMMAAENGQAGAVDILVNSaQADLTVKDKDLNTPLHLAISKGHEKCALLILDKIQdeslINAKNSAlQTPLHIAARNGLK 948
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLEN-GADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD----VNLKDNG-RTALHYAARSGHL 74
|
90
....*....|....*..
gi 755492548 949 VVVEELLAKGACVLAVD 965
Cdd:pfam12796 75 EIVKLLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
2-79 |
4.68e-13 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 65.91 E-value: 4.68e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755492548 2 LIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLiLSGARVNAKDNMWlTPLHRAVASRSEEAVQVLIKHSADVNARD 79
Cdd:pfam12796 16 LLENGADANLQDKNGRTALHLAAKNGHLEIVKLL-LEHADVNLKDNGR-TALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
229-458 |
5.97e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 71.95 E-value: 5.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 229 VVNELIDYGANVNQPNNSGFTPLHFAAaSTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEI- 307
Cdd:PHA02875 17 IARRLLDIGINPNFEIYDGISPIKLAM-KFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAd 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 308 DCVDKDGNTPLHVAARHGHELLINTLITSGADTakcgihsmfplhlaalnahsdccrkllssgqkysivslfsnehvlsa 387
Cdd:PHA02875 96 DVFYKDGMTPLHLATILKKLDIMKLLIARGADP----------------------------------------------- 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755492548 388 gfeiDTPDTFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIKALVTTGANVN 458
Cdd:PHA02875 129 ----DIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANID 195
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
23-176 |
1.31e-12 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 72.21 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 23 AAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVII 102
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY 611
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755492548 103 PLLSSVNVSDRGgrTALHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTC 176
Cdd:PLN03192 612 HFASISDPHAAG--DLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDK 683
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
18-142 |
1.62e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 70.79 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 18 TPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKC 97
Cdd:PHA02875 104 TPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAI 183
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 755492548 98 AEVIIPLLSSVN-VSDRGGRTALHHAALNGHMEMVNLLLAKGANIN 142
Cdd:PHA02875 184 CKMLLDSGANIDyFGKNGCVAALCYAIENNKIDIVRLFIKRGADCN 229
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
585-817 |
1.85e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 70.46 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 585 DLDIRDEKGRTALYLAAFKGHTECVEALVNQGASIFVKDNvTKRTPLHASVINGHTLclrllletADNPEVVDvkdakgq 664
Cdd:PHA03100 27 LNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTK-NNSTPLHYLSNIKYNL--------TDVKEIVK------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 665 tplmlavayghidavsLLLEKEANVDAVDIVGCTALHRGIMT--GHEECVQMLLEQEASILCKDSRGRTPLHYAAARGHA 742
Cdd:PHA03100 91 ----------------LLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 743 TwlNELLQIALS---------EEDCCL--------KDNQGYTPLHWACYNGNENCIEVLLEQKCF---RKFIGNpfTPLH 802
Cdd:PHA03100 155 D--LKILKLLIDkgvdinaknRVNYLLsygvpiniKDVYGFTPLHYAVYNNNPEFVKYLLDLGANpnlVNKYGD--TPLH 230
|
250
....*....|....*
gi 755492548 803 CAIINGHESCASLLL 817
Cdd:PHA03100 231 IAILNNNKEIFKLLL 245
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
68-213 |
1.86e-12 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 71.44 E-value: 1.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 68 LIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHMEMVNLLLAKGANINAFDKK 147
Cdd:PLN03192 544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAG 623
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755492548 148 DrrALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQISVVKHLLNLGVEIDEINVY 213
Cdd:PLN03192 624 D--LLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTD 687
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
141-438 |
1.99e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 70.68 E-value: 1.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 141 INAFDKKDRRA----------LHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQISVVKHLLNLGVEIDEI 210
Cdd:PHA02878 20 IEYIDHTENYStsaslipfipLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 211 NVYgnTALHIACYNGQDAVVNE-LIDYGANVNQPNNSGFTPLHFAAASThgALCLELLVNNGADVNIQSKD-GKSPLHMT 288
Cdd:PHA02878 100 YTL--VAIKDAFNNRNVEIFKIiLTNRYKNIQTIDLVYIDKKSKDDIIE--AEITKLLLSYGADINMKDRHkGNTALHYA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 289 AVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARHGHELLINTLITSGADTAKCGIHSMFPLHLAAlnahsdccrkllS 368
Cdd:PHA02878 176 TENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISV------------G 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755492548 369 SGQKYSIVSLfsnehVLSAGFEIDTPDTF-GRTCLHAAAAGGNVecIKLLQSSGADFHKKDKCGRTPLHYA 438
Cdd:PHA02878 244 YCKDYDILKL-----LLEHGVDVNAKSYIlGLTALHSSIKSERK--LKLLLEYGADINSLNSYKLTPLSSA 307
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
736-905 |
2.87e-12 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 71.05 E-value: 2.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 736 AAARGHATWLNELLQIALSEEdccLKDNQGYTPLHWACYNGNENCIEVLLEQKC---FRKFIGNpfTPLHCAIINGHESC 812
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPD---IGDSKGRTPLHIAASKGYEDCVLVLLKHACnvhIRDANGN--TALWNAISAKHHKI 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 813 ASLLL---GAIDPSIvscrddkGRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILV-NSA 888
Cdd:PLN03192 607 FRILYhfaSISDPHA-------AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLImNGA 679
|
170
....*....|....*..
gi 755492548 889 QADLTVKDKDLnTPLHL 905
Cdd:PLN03192 680 DVDKANTDDDF-SPTEL 695
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
507-590 |
3.52e-12 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 63.21 E-value: 3.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 507 CLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNTGFEESDggalKSPLHLAAYNGHHQALEVLLQSLVDL 586
Cdd:pfam12796 12 LVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNG----RTALHYAARSGHLEIVKLLLEKGADI 87
|
....
gi 755492548 587 DIRD 590
Cdd:pfam12796 88 NVKD 91
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
434-671 |
4.10e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 69.91 E-value: 4.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 434 PLHYAAANCHFHCIKALVTTGANVNETDDWGRTALH--------------------------YAAASDMDRN------KM 481
Cdd:PHA02878 40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHiickepnklgmkemirsinkcsvfytLVAIKDAFNNrnveifKI 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 482 ILGNAHDNSEELErAREVKEKDAALCLE-----FLLQNDANPSIRDKEGYNS-IHYAAAYGHRQCLELLL---------E 546
Cdd:PHA02878 120 ILTNRYKNIQTID-LVYIDKKSKDDIIEaeitkLLLSYGADINMKDRHKGNTaLHYATENKDQRLTELLLsyganvnipD 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 547 RTNtgfeesdggalKSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLA-AFKGHTECVEALVNQGASIFVKDNV 625
Cdd:PHA02878 199 KTN-----------NSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYI 267
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 755492548 626 TKRTPLHASVINGHTlcLRLLLETADNPEVVdvkDAKGQTPLMLAV 671
Cdd:PHA02878 268 LGLTALHSSIKSERK--LKLLLEYGADINSL---NSYKLTPLSSAV 308
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
318-428 |
7.91e-12 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 62.44 E-value: 7.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 318 LHVAARHGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSGQKYSivslfsnehvlsagfeidtpDTF 397
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--------------------KDN 60
|
90 100 110
....*....|....*....|....*....|.
gi 755492548 398 GRTCLHAAAAGGNVECIKLLQSSGADFHKKD 428
Cdd:pfam12796 61 GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
115-168 |
8.24e-12 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 61.14 E-value: 8.24e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 755492548 115 GRTALHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLI 168
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
576-788 |
9.78e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 68.15 E-value: 9.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 576 LEVLLQSLVDLDIRDEKGRTALYLAAFKGHT-----ECVEALVNQGASIFVKDNVTKrTPLHASVIN--GHTLCLRLLLE 648
Cdd:PHA03100 51 VKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGI-TPLLYAISKksNSYSIVEYLLD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 649 TADNpevVDVKDAKGQTPLMLAVAYGHIDA--VSLLLEKEANVDAVDIVgctalhrgimtgheecvQMLLEQEASILCKD 726
Cdd:PHA03100 130 NGAN---VNIKNSDGENLLHLYLESNKIDLkiLKLLIDKGVDINAKNRV-----------------NYLLSYGVPINIKD 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755492548 727 SRGRTPLHYAAARGHATWLNELLQIALSEEDCclkDNQGYTPLHWACYNGNENCIEVLLEQK 788
Cdd:PHA03100 190 VYGFTPLHYAVYNNNPEFVKYLLDLGANPNLV---NKYGDTPLHIAILNNNKEIFKLLLNNG 248
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
82-334 |
1.25e-11 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 68.50 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 82 WQTPLHVAAANKAVKCaevIIPLL--SSVNVSDRG--GRTALHHAALNGHMEMVNLLLakganinafdkkdrralhwaay 157
Cdd:cd22192 17 SESPLLLAAKENDVQA---IKKLLkcPSCDLFQRGalGETALHVAALYDNLEAAVVLM---------------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 158 mghlDVVALLINHgaEVTCkdkkgytplhaaasngqisvvkhllnlgveideiNVY-GNTALHIACYNGQDAVVNELIDY 236
Cdd:cd22192 72 ----EAAPELVNE--PMTS----------------------------------DLYqGETALHIAVVNQNLNLVRELIAR 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 237 GANVNQPNNSG--FT------------PLHFAAASTHGALcLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLI- 301
Cdd:cd22192 112 GADVVSPRATGtfFRpgpknliyygehPLSFAACVGNEEI-VRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFACQMYd 190
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 755492548 302 --------QNGGEIDCV-DKDGNTPLHVAARHGHELLINTLI 334
Cdd:cd22192 191 lilsydkeDDLQPLDLVpNNQGLTPFKLAAKEGNIVMFQHLV 232
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
284-603 |
1.28e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 68.37 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 284 PLHMtAVHGR-FTRSQTLIQNGGEIDCVDKDGNTPLHVAARHGHELLINTLITSgadTAKCGIHSmfplhlaALNAHSDC 362
Cdd:PHA02878 40 PLHQ-AVEARnLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRS---INKCSVFY-------TLVAIKDA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 363 CRKLLSSGQKYSIVSLFSNEHVLSAgFEIDTPDTFGRTclhaaaaggNVECIKLLQSSGADFHKKDK-CGRTPLHYAAAN 441
Cdd:PHA02878 109 FNNRNVEIFKIILTNRYKNIQTIDL-VYIDKKSKDDII---------EAEITKLLLSYGADINMKDRhKGNTALHYATEN 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 442 CHFHCIKALVTTGANVNETDDWGRTALHYAAASdmdRNKMIlgnahdnseelerarevkekdaalcLEFLLQNDANPSIR 521
Cdd:PHA02878 179 KDQRLTELLLSYGANVNIPDKTNNSPLHHAVKH---YNKPI-------------------------VHILLENGASTDAR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 522 DKEGYNSIHYAAAY-GHRQCLELLLERTNTGFEESDGGALkSPLHLAAYNghHQALEVLLQSLVDLDIRDEKGRTALYLA 600
Cdd:PHA02878 231 DKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYILGL-TALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSA 307
|
...
gi 755492548 601 AFK 603
Cdd:PHA02878 308 VKQ 310
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
149-201 |
1.34e-11 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 60.37 E-value: 1.34e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 755492548 149 RRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQISVVKHLL 201
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
251-339 |
2.10e-11 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 60.90 E-value: 2.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 251 LHFAAASTHgALCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNgGEIDCVDkDGNTPLHVAARHGHELLI 330
Cdd:pfam12796 1 LHLAAKNGN-LELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77
|
....*....
gi 755492548 331 NTLITSGAD 339
Cdd:pfam12796 78 KLLLEKGAD 86
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
398-451 |
2.49e-11 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 59.60 E-value: 2.49e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 755492548 398 GRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIKALV 451
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
24-255 |
2.67e-11 |
|
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: 67.80 E-value: 2.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 24 AFLGDAEIIELLILSGARVNAK-------DNMWLTPLHRAVA-SRSEEAVQVLIKHSADVNARDknwqTPLHVAAANKAV 95
Cdd:TIGR00870 20 AFLPAAERGDLASVYRDLEEPKklnincpDRLGRSALFVAAIeNENLELTELLLNLSCRGAVGD----TLLHAISLEYVD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 96 KCAEVIIPLLSS---------VNVSDRG----GRTALHHAALNGHMEMVNLLLAKGANINA------FDKKDRRA----- 151
Cdd:TIGR00870 96 AVEAILLHLLAAfrksgplelANDQYTSeftpGITALHLAAHRQNYEIVKLLLERGASVPAracgdfFVKSQGVDsfyhg 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 152 ---LHWAAYMGHLDVVALLINHGAEVTCKDKKGYTplhaaasngqisvVKHLLNLGVEideiNVYGNTALHIACYngqda 228
Cdd:TIGR00870 176 espLNAAACLGSPSIVALLSEDPADILTADSLGNT-------------LLHLLVMENE----FKAEYEELSCQMY----- 233
|
250 260 270
....*....|....*....|....*....|....
gi 755492548 229 vvNELIDYGANVNQ-------PNNSGFTPLHFAA 255
Cdd:TIGR00870 234 --NFALSLLDKLRDskeleviLNHQGLTPLKLAA 265
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
767-985 |
2.76e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 66.91 E-value: 2.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 767 TPLHWACYNGNENCIEVLLEQKCFRKFIG-NPFTPLHCAI-INGHESCASLLLGAIDPSI-------------------- 824
Cdd:PHA02874 37 TPLIDAIRSGDAKIVELFIKHGADINHINtKIPHPLLTAIkIGAHDIIKLLIDNGVDTSIlpipciekdmiktildcgid 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 825 VSCRDDKGRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNSAqADLTVKDKDLNTPLH 904
Cdd:PHA02874 117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKG-AYANVKDNNGESPLH 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 905 LAISKGHEKCALLILDkiqDESLINAKNSALQTPLHIAARNGLKVVveELLAKGACVLAVDENGHTP---ALACAPNKDV 981
Cdd:PHA02874 196 NAAEYGDYACIKLLID---HGNHIMNKCKNGFTPLHNAIIHNRSAI--ELLINNASINDQDIDGSTPlhhAINPPCDIDI 270
|
....
gi 755492548 982 ADCL 985
Cdd:PHA02874 271 IDIL 274
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
158-349 |
4.29e-11 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 67.20 E-value: 4.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 158 MGHLDVVALLINHGAEVTckDKKGYTPLHAAASNGQISVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYG 237
Cdd:PLN03192 504 LHDLNVGDLLGDNGGEHD--DPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 238 ANVNQPNNSGFTPLHFAAASTHGALcLELLVNNGADVNIQSkdGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTP 317
Cdd:PLN03192 582 CNVHIRDANGNTALWNAISAKHHKI-FRILYHFASISDPHA--AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATA 658
|
170 180 190
....*....|....*....|....*....|..
gi 755492548 318 LHVAARHGHELLINTLITSGADTAKCGIHSMF 349
Cdd:PLN03192 659 LQVAMAEDHVDMVRLLIMNGADVDKANTDDDF 690
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
595-777 |
9.02e-11 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 65.80 E-value: 9.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 595 TALYLAAFKGHTECVEAL-VNQGASIFVKDNVTKrTPLHASVINGHTLCLRLLLETAdnPEVVDVKDA----KGQTPLML 669
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLlKCPSCDLFQRGALGE-TALHVAALYDNLEAAVVLMEAA--PELVNEPMTsdlyQGETALHI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 670 AVAYGHIDAVSLLLEKEANVDAVDIVGcTALHRGI---------------MTGHEECVQMLLEQEASILCKDSRGRTPLH 734
Cdd:cd22192 96 AVVNQNLNLVRELIARGADVVSPRATG-TFFRPGPknliyygehplsfaaCVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 755492548 735 YAAARGHATWLNELLQIALSEE----DCCL---KDNQGYTPLHWACYNGN 777
Cdd:cd22192 175 ILVLQPNKTFACQMYDLILSYDkeddLQPLdlvPNNQGLTPFKLAAKEGN 224
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
762-961 |
1.07e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 65.29 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 762 DNQGYTPLHWACYNGNENCIEVLLEQKCFRKfIGNPFTPLHCAIINGHESCASLLLGAIDPSIVSCRDDKGRTTLHAAAF 841
Cdd:PHA02878 67 DHRDLTPLHIICKEPNKLGMKEMIRSINKCS-VFYTLVAIKDAFNNRNVEIFKIILTNRYKNIQTIDLVYIDKKSKDDII 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 842 gdHAECLQLLLRHDAQVNAVD-NSGKTALMMAAENGQAGAVDILVnSAQADLTVKDKDLNTPLHLAISKGHEKcALLILd 920
Cdd:PHA02878 146 --EAEITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLL-SYGANVNIPDKTNNSPLHHAVKHYNKP-IVHIL- 220
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 755492548 921 kIQDESLINAKNSALQTPLHIAARNGLKV-VVEELLAKGACV 961
Cdd:PHA02878 221 -LENGASTDARDKCGNTPLHISVGYCKDYdILKLLLEHGVDV 261
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
715-967 |
1.55e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 64.69 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 715 LLEQEASILCKDSRGRTPLHYAAARGHATWLNELLqialsEEDCCL--KDNQGYTPLH---WACYNGNEN--CIEVLLEQ 787
Cdd:PHA03100 21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILL-----DNGADInsSTKNNSTPLHylsNIKYNLTDVkeIVKLLLEY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 788 -KCFRKFIGNPFTPLHCAIIN--GHESCASLLLG-AIDPSIVSCRddkGRTTLHAAAFGDHA--ECLQLLLRHDAQVNAV 861
Cdd:PHA03100 96 gANVNAPDNNGITPLLYAISKksNSYSIVEYLLDnGANVNIKNSD---GENLLHLYLESNKIdlKILKLLIDKGVDINAK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 862 DNsgktalmmaaengqagaVDILVNSAqADLTVKDKDLNTPLHLAISKGHEKCALLILDKIQDeslINAKNSALQTPLHI 941
Cdd:PHA03100 173 NR-----------------VNYLLSYG-VPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGAN---PNLVNKYGDTPLHI 231
|
250 260
....*....|....*....|....*.
gi 755492548 942 AARNGLKVVVEELLAKGACVLAVDEN 967
Cdd:PHA03100 232 AILNNNKEIFKLLLNNGPSIKTIIET 257
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
125-250 |
1.78e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 61.76 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 125 NGHMEMVNLLLAKGANINAFDKKDRRAL--HWAAYMGHL--DVVALLINHGAEVTCKDKKGYTPLHAAASNG--QISVVK 198
Cdd:PHA02859 63 KVNVEILKFLIENGADVNFKTRDNNLSAlhHYLSFNKNVepEILKILIDSGSSITEEDEDGKNLLHMYMCNFnvRINVIK 142
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 755492548 199 HLLNLGVEIDEINVYGNTALH-IACYNGQDAVVNELIDYGANVNQPNNSGFTP 250
Cdd:PHA02859 143 LLIDSGVSFLNKDFDNNNILYsYILFHSDKKIFDFLTSLGIDINETNKSGYNC 195
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
122-251 |
3.52e-10 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 64.12 E-value: 3.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 122 AALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPL---------------- 185
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnaisakhhkifrily 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 186 --------HA-------AASNGQISVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPN-NSGFT 249
Cdd:PLN03192 612 hfasisdpHAagdllctAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANtDDDFS 691
|
..
gi 755492548 250 PL 251
Cdd:PLN03192 692 PT 693
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
285-375 |
3.54e-10 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 57.43 E-value: 3.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 285 LHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARHGHELLINTLITSGAdtAKCGIHSMFPLHLAALNAHSDCCR 364
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78
|
90
....*....|.
gi 755492548 365 KLLSSGQKYSI 375
Cdd:pfam12796 79 LLLEKGADINV 89
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
549-732 |
3.79e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 63.09 E-value: 3.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 549 NTGFEESDGgalKSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQGAsiFVKDNVTKR 628
Cdd:PHA02875 27 NPNFEIYDG---ISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK--FADDVFYKD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 629 --TPLHASVINGHTLCLRLLLETADNPevvDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIVGCTALHRGIMT 706
Cdd:PHA02875 102 gmTPLHLATILKKLDIMKLLIARGADP---DIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAK 178
|
170 180
....*....|....*....|....*.
gi 755492548 707 GHEECVQMLLEQEASIlckDSRGRTP 732
Cdd:PHA02875 179 GDIAICKMLLDSGANI---DYFGKNG 201
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
531-750 |
4.05e-10 |
|
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: 63.88 E-value: 4.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 531 YAAAYGHRQCLELLLERTNTGFEESdgGAL-KSPLHLAAYNGHHQALEVLLQS---LVDLDIRDE--KGRTALYLAAFKG 604
Cdd:cd22192 23 LAAKENDVQAIKKLLKCPSCDLFQR--GALgETALHVAALYDNLEAAVVLMEAapeLVNEPMTSDlyQGETALHIAVVNQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 605 HTECVEALVNQGAsifvkDNVTKRTPLHASVINGHTLCLRllletadnpevvdvkdakGQTPLMLAVAYGHIDAVSLLLE 684
Cdd:cd22192 101 NLNLVRELIARGA-----DVVSPRATGTFFRPGPKNLIYY------------------GEHPLSFAACVGNEEIVRLLIE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755492548 685 KEANVDAVDIVGCTALHRGIMTGHEECV-QM---LLEQEASI------LCKDSRGRTPLHYAAARGHATWLNELLQ 750
Cdd:cd22192 158 HGADIRAQDSLGNTVLHILVLQPNKTFAcQMydlILSYDKEDdlqpldLVPNNQGLTPFKLAAKEGNIVMFQHLVQ 233
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
665-716 |
8.41e-10 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 55.36 E-value: 8.41e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 755492548 665 TPLMLAVAYGHIDAVSLLLEKEANVDAVDIVGCTALHRGIMTGHEECVQMLL 716
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
83-257 |
1.04e-09 |
|
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: 62.59 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 83 QTPLHVAAANKAVKCAEVIIPLLSSVNVSDRG--------------GRTALHHAALNGHMEMVNLLLAKGANINA----- 143
Cdd:cd21882 27 KTCLHKAALNLNDGVNEAIMLLLEAAPDSGNPkelvnapctdefyqGQTALHIAIENRNLNLVRLLVENGADVSAratgr 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 144 FDKKDRR--------ALHWAAYMGHLDVVALLINHGAE---VTCKDKKGYTPLHAAasngqisvvkhllnlgVEIDEiNV 212
Cdd:cd21882 107 FFRKSPGnlfyfgelPLSLAACTNQEEIVRLLLENGAQpaaLEAQDSLGNTVLHAL----------------VLQAD-NT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 755492548 213 YGNTALHIACYNGqdavvneLIDYGANVNQ-------PNNSGFTPLHFAAAS 257
Cdd:cd21882 170 PENSAFVCQMYNL-------LLSYGAHLDPtqqleeiPNHQGLTPLKLAAVE 214
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
628-740 |
1.16e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 61.55 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 628 RTPLHASVINGHTLCLRLLLETadNPEVVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIVGCTALHRGIMTG 707
Cdd:PHA02875 69 ESELHDAVEEGDVKAVEELLDL--GKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMG 146
|
90 100 110
....*....|....*....|....*....|...
gi 755492548 708 HEECVQMLLEQEASILCKDSRGRTPLHYAAARG 740
Cdd:PHA02875 147 DIKGIELLIDHKACLDIEDCCGCTPLIIAMAKG 179
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
685-971 |
2.16e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 61.05 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 685 KEANVDAVDIVGCTALHRGIMTGHEECVQMLLEQEASILCKDSRGRTPLHYAAARGHATWLNELLQIALseedcclKDNQ 764
Cdd:PHA02878 26 TENYSTSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSIN-------KCSV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 765 GYT--PLHWACYNGNENCIEVLLeqkcFRKFIGNpftplhcAIINGHESCASLLLGAIDPSIVSC-----------RDDK 831
Cdd:PHA02878 99 FYTlvAIKDAFNNRNVEIFKIIL----TNRYKNI-------QTIDLVYIDKKSKDDIIEAEITKLllsygadinmkDRHK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 832 GRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNSAqADLTVKDKDLNTPLHLAISKGH 911
Cdd:PHA02878 168 GNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENG-ASTDARDKCGNTPLHISVGYCK 246
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755492548 912 EKCALLILdkIQDESLINAKNSALQ-TPLHIAARNGLKVVVeeLLAKGACVLAVDENGHTP 971
Cdd:PHA02878 247 DYDILKLL--LEHGVDVNAKSYILGlTALHSSIKSERKLKL--LLEYGADINSLNSYKLTP 303
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
119-201 |
2.23e-09 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 61.45 E-value: 2.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 119 LHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQISVVK 198
Cdd:PTZ00322 86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165
|
...
gi 755492548 199 HLL 201
Cdd:PTZ00322 166 LLS 168
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
562-613 |
2.80e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 53.82 E-value: 2.80e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 755492548 562 SPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALV 613
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02989 |
PHA02989 |
ankyrin repeat protein; Provisional |
30-331 |
5.33e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222954 [Multi-domain] Cd Length: 494 Bit Score: 59.75 E-value: 5.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 30 EIIELLILSGARVNAKDNMwLTPL-----HRAVAS-RSEEAVQVLIKHSADVNARDKNWQTPlhvaaankavkcaevIIP 103
Cdd:PHA02989 51 KIVKLLIDNGADVNYKGYI-ETPLcavlrNREITSnKIKKIVKLLLKFGADINLKTFNGVSP---------------IVC 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 104 LLSSVNVSDrggrtalhhaalnghMEMVNLLLAKGANINafdkkdrralhwaaymghldvvallinhgaevTCKDKKGYT 183
Cdd:PHA02989 115 FIYNSNINN---------------CDMLRFLLSKGINVN--------------------------------DVKNSRGYN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 184 PLHAAASNGQIS--VVKHLLNLGVEIDEI-NVYGNTALHIACYNGQDAVVNELIDY----GANVNQPNNSGFTPLHfAAA 256
Cdd:PHA02989 148 LLHMYLESFSVKkdVIKILLSFGVNLFEKtSLYGLTPMNIYLRNDIDVISIKVIKYlikkGVNIETNNNGSESVLE-SFL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 257 STHGAL---CLELL--VNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARHGHELLIN 331
Cdd:PHA02989 227 DNNKILskkEFKVLnfILKYIKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLN 306
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
315-469 |
9.45e-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: 59.26 E-value: 9.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 315 NTPLHVAARHGHELLINTLITS-GADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSgqkysiVSLFSNEHVLSAGFEidt 393
Cdd:cd22192 18 ESPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLMEA------APELVNEPMTSDLYQ--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 394 pdtfGRTCLHAAAAGGNVECIKLLQSSGAD----------FHKKDKC----GRTPLHYAAANCHFHCIKALVTTGANVNE 459
Cdd:cd22192 89 ----GETALHIAVVNQNLNLVRELIARGADvvspratgtfFRPGPKNliyyGEHPLSFAACVGNEEIVRLLIEHGADIRA 164
|
170
....*....|
gi 755492548 460 TDDWGRTALH 469
Cdd:cd22192 165 QDSLGNTVLH 174
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
431-473 |
1.49e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 51.89 E-value: 1.49e-08
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 755492548 431 GRTPLHYAAANCHFHCIKALVTTGANVNETDDWGRTALHYAAA 473
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAAS 43
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
249-436 |
1.75e-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: 58.49 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 249 TPLhFAAASTHGALCLE-LLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGE-----IDCVDKDGNTPLHVAA 322
Cdd:cd22192 19 SPL-LLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElvnepMTSDLYQGETALHIAV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 323 RHGHELLINTLITSGADTAK---CGihSMFPLHLAALnahsdccrkllssgqkysivsLFSNEHVLSagfeidtpdtFgr 399
Cdd:cd22192 98 VNQNLNLVRELIARGADVVSpraTG--TFFRPGPKNL---------------------IYYGEHPLS----------F-- 142
|
170 180 190
....*....|....*....|....*....|....*..
gi 755492548 400 tclhaAAAGGNVECIKLLQSSGADFHKKDKCGRTPLH 436
Cdd:cd22192 143 -----AACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
181-234 |
1.93e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 51.51 E-value: 1.93e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 755492548 181 GYTPLHAAASNGQISVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELI 234
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
28-287 |
2.56e-08 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 57.76 E-value: 2.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 28 DAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKavkcAEVIipllss 107
Cdd:PHA02946 51 DERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTD----DEVI------ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 108 vnvsdrggrtalhhaalnghmEMVNLLLAKGANINafdkkdrralhwaaymghldvvallinhgaevTCKDKKGYTPLHA 187
Cdd:PHA02946 121 ---------------------ERINLLVQYGAKIN--------------------------------NSVDEEGCGPLLA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 188 AASNGQiSVVKHLLNLGVEIDEINVYGNTAL--HIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHFAAASTHGALCLE 265
Cdd:PHA02946 148 CTDPSE-RVFKKIMSIGFEARIVDKFGKNHIhrHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCSKTVKNVDII 226
|
250 260
....*....|....*....|..
gi 755492548 266 LLVNNGADVNIQSKDGKSPLHM 287
Cdd:PHA02946 227 NLLLPSTDVNKQNKFGDSPLTL 248
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
49-102 |
6.01e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 49.97 E-value: 6.01e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 755492548 49 WLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVII 102
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
298-546 |
6.14e-08 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 56.22 E-value: 6.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 298 QTLIQNGGEIDCVDKDGNTPLHVAARHGHELLINTLITSGADTAKCGIHSMFPLHL-------------------AALNA 358
Cdd:PHA02946 56 EELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYlsgtddevierinllvqygAKINN 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 359 HSD--CCRKLLSSGQKYSIVSlfsnEHVLSAGFEIDTPDTFGRTCLHAAAAGGN--VECIKLLQSSGADFHKKDKCGRTP 434
Cdd:PHA02946 136 SVDeeGCGPLLACTDPSERVF----KKIMSIGFEARIVDKFGKNHIHRHLMSDNpkASTISWMMKLGISPSKPDHDGNTP 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 435 LHYAAANCHFHC-IKALVTTGANVNETDDWGRTALHYAAASdmdrnkmiLGNAHDNSEELERAREVKEKDAALCLeFLLQ 513
Cdd:PHA02946 212 LHIVCSKTVKNVdIINLLLPSTDVNKQNKFGDSPLTLLIKT--------LSPAHLINKLLSTSNVITDQTVNICI-FYDR 282
|
250 260 270
....*....|....*....|....*....|....*.
gi 755492548 514 NDANPSIRDK-EGYNSIHY--AAAYGHRQCLELLLE 546
Cdd:PHA02946 283 DDVLEIINDKgKQYDSTDFkmAVEVGSIRCVKYLLD 318
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
52-225 |
7.20e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 54.05 E-value: 7.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 52 PLHRAVASRSEEAVQVLIKHSADVNardKNWQTPLHVAAANKAV--KCAEVIIPLLSSVNVSDRGGRTALHHAAL----N 125
Cdd:PHA02859 24 PLFYYVEKDDIEGVKKWIKFVNDCN---DLYETPIFSCLEKDKVnvEILKFLIENGADVNFKTRDNNLSALHHYLsfnkN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 126 GHMEMVNLLLAKGANINAFDKKDRRALHwaAYMGH----LDVVALLINHGAEVTCKDKKGYTPLHA-AASNGQISVVKHL 200
Cdd:PHA02859 101 VEPEILKILIDSGSSITEEDEDGKNLLH--MYMCNfnvrINVIKLLIDSGVSFLNKDFDNNNILYSyILFHSDKKIFDFL 178
|
170 180
....*....|....*....|....*
gi 755492548 201 LNLGVEIDEINVYGNTALHIACYNG 225
Cdd:PHA02859 179 TSLGIDINETNKSGYNCYDLIKFRN 203
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
584-806 |
8.07e-08 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 56.63 E-value: 8.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 584 VDLDIRDEKGRTALYLAAFKG-HTECVEALVNQGASIFVKDNVtkrtpLHASVINGH---TLCLRLLL----ETADNPEV 655
Cdd:TIGR00870 43 LNINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAVGDTL-----LHAISLEYVdavEAILLHLLaafrKSGPLELA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 656 VDVKDA---KGQTPLMLAVAYGHIDAVSLLLEKEANVDAVdiVGCTALHRGIM----------------TGHEECVQMLL 716
Cdd:TIGR00870 118 NDQYTSeftPGITALHLAAHRQNYEIVKLLLERGASVPAR--ACGDFFVKSQGvdsfyhgesplnaaacLGSPSIVALLS 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 717 EQEASILCKDSRGRTPLHYAAARGHATWLNELL-------------QIALSEEDCCLKDNQGYTPLHWACYNGNENCIEV 783
Cdd:TIGR00870 196 EDPADILTADSLGNTLLHLLVMENEFKAEYEELscqmynfalslldKLRDSKELEVILNHQGLTPLKLAAKEGRIVLFRL 275
|
250 260
....*....|....*....|....
gi 755492548 784 LLEQKCF-RKFIGNPFTPLHCAII 806
Cdd:TIGR00870 276 KLAIKYKqKKFVAWPNGQQLLSLY 299
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
1-139 |
9.01e-08 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 55.80 E-value: 9.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 1 MLIHKTEDVNALDSEKRTPLHVAAFLGD--AEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNAR 78
Cdd:PHA03095 207 ELIRAGCDPAATDMLGNTPLHSMATGSSckRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAV 286
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755492548 79 DKNWQTPLHVAAANKAVKCAEVIIPLLSSVNVSDRggrtALHHAALNGHM-------EMVNLLLAKGA 139
Cdd:PHA03095 287 SSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAA----TLNTASVAGGDipsdatrLCVAKVVLRGA 350
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
256-325 |
9.44e-08 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 56.06 E-value: 9.44e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 256 ASTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARHG 325
Cdd:PTZ00322 90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENG 159
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
404-619 |
1.07e-07 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 56.03 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 404 AAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIKALVTTGANVNETDDWGRTALHYAAASDMDRNKMIL 483
Cdd:PLN03192 531 TVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 484 gnahdnseelerarevkekdaalclefllqndanpsirdkegynsIHYAAAyghrqclelllertntgfeeSDGGALKSP 563
Cdd:PLN03192 611 ---------------------------------------------YHFASI--------------------SDPHAAGDL 625
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 755492548 564 LHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQGASI 619
Cdd:PLN03192 626 LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
799-971 |
1.21e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 55.35 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 799 TPLHCAIINGH-ESCASLLLGAIDpsiVSCRDDKGRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQ 877
Cdd:PHA02874 126 TFLHYAIKKGDlESIKMLFEYGAD---VNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGD 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 878 AGAVDILVNSAqADLTVKDKDLNTPLHLAISKGHEKCALLIldkiqDESLINAKNSALQTPLHIAARNGLKV-VVEELLA 956
Cdd:PHA02874 203 YACIKLLIDHG-NHIMNKCKNGFTPLHNAIIHNRSAIELLI-----NNASINDQDIDGSTPLHHAINPPCDIdIIDILLY 276
|
170
....*....|....*
gi 755492548 957 KGACVLAVDENGHTP 971
Cdd:PHA02874 277 HKADISIKDNKGENP 291
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
84-135 |
1.29e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 49.20 E-value: 1.29e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 755492548 84 TPLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHMEMVNLLL 135
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
300-468 |
1.32e-07 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 55.64 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 300 LIQNGGEIDCVDKDGNtpLHVAARHGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSGQKYSIVSLF 379
Cdd:PLN03192 513 LGDNGGEHDDPNMASN--LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDAN 590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 380 SNE---HVLSAG----FEI-------DTPDTFGrTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFH 445
Cdd:PLN03192 591 GNTalwNAISAKhhkiFRIlyhfasiSDPHAAG-DLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVD 669
|
170 180
....*....|....*....|....*.
gi 755492548 446 CIKALVTTGANV---NETDDWGRTAL 468
Cdd:PLN03192 670 MVRLLIMNGADVdkaNTDDDFSPTEL 695
|
|
| PHA02716 |
PHA02716 |
CPXV016; CPX019; EVM010; Provisional |
24-301 |
1.89e-07 |
|
CPXV016; CPX019; EVM010; Provisional
Pssm-ID: 165089 [Multi-domain] Cd Length: 764 Bit Score: 55.30 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 24 AFLG----DAEIIELLILSGARVNAKDNMWLTPLHRAV--ASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKC 97
Cdd:PHA02716 183 AYLGnmyvDIDILEWLCNNGVNVNLQNNHLITPLHTYLitGNVCASVIKKIIELGGDMDMKCVNGMSPIMTYIINIDNIN 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 98 AEVI----------------------IPLLSSVNVS---------------DRGGRTALHHAAL--NGHMEMVNLLLAKG 138
Cdd:PHA02716 263 PEITniyiesldgnkvknipmilhsyITLARNIDISvvysflqpgvklhykDSAGRTCLHQYILrhNISTDIIKLLHEYG 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 139 ANINAFDKKDRRALHwaAYMG----------------HLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQ--------- 193
Cdd:PHA02716 343 NDLNEPDNIGNTVLH--TYLSmlsvvnildpetdndiRLDVIQCLISLGADITAVNCLGYTPLTSYICTAQnymyydiid 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 194 -------ISVVKH--LLNLGVEIDE---------------INVYGNTALHIACYNGQDAVVNELIDYGANVNQPnNSGFT 249
Cdd:PHA02716 421 clisdkvLNMVKHriLQDLLIRVDDtpciihhiiakynipTDLYTDEYEPYDSTKIHDVYHCAIIERYNNAVCE-TSGMT 499
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 755492548 250 PLHFAAASTHGAL----CLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLI 301
Cdd:PHA02716 500 PLHVSIISHTNANivmdSFVYLLSIQYNINIPTKNGVTPLMLTMRNNRLSGHQWYI 555
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
698-741 |
2.19e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 48.42 E-value: 2.19e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 755492548 698 TALHRGIMTGHEECVQMLLEQEASILCKDSRGRTPLHYAAARGH 741
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGN 46
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
469-694 |
2.54e-07 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 54.87 E-value: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 469 HYAAASDMDRNKMILGNA--HDNSEELERAREVKEKDAALCLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQClellle 546
Cdd:PLN03192 500 HHKELHDLNVGDLLGDNGgeHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDC------ 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 547 rtntgfeesdggalksplhlaaynghhqaLEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALvNQGASIfvKDNVT 626
Cdd:PLN03192 574 -----------------------------VLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL-YHFASI--SDPHA 621
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755492548 627 KRTPLHASVINGHTLCLRLLLETADNpevVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDI 694
Cdd:PLN03192 622 AGDLLCTAAKRNDLTAMKELLKQGLN---VDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANT 686
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
628-885 |
2.85e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 54.23 E-value: 2.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 628 RTPLHASVINGHTLCLRLLLETADNP--EVVDvkdakGQTPLMLAVAYGHIDAVSLLLEKEA--NVDAVDIVgcTALHRG 703
Cdd:PHA02875 3 QVALCDAILFGELDIARRLLDIGINPnfEIYD-----GISPIKLAMKFRDSEAIKLLMKHGAipDVKYPDIE--SELHDA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 704 IMTGHEECVQMLLEQEA---SILCKDsrGRTPLHYAAARGHATWLNELLQialSEEDCCLKDNQGYTPLHWACYNGNENC 780
Cdd:PHA02875 76 VEEGDVKAVEELLDLGKfadDVFYKD--GMTPLHLATILKKLDIMKLLIA---RGADPDIPNTDKFSPLHLAVMMGDIKG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 781 IEVLLEQK-CFRKFIGNPFTPLHCAIINGH-ESCASLLLGAIDPSIVSCRDDKgrTTLHAAAFGDHAECLQLLLRHDAQV 858
Cdd:PHA02875 151 IELLIDHKaCLDIEDCCGCTPLIIAMAKGDiAICKMLLDSGANIDYFGKNGCV--AALCYAIENNKIDIVRLFIKRGADC 228
|
250 260 270
....*....|....*....|....*....|...
gi 755492548 859 N---AVDNSGKTALMMAAE---NGQAGAVDILV 885
Cdd:PHA02875 229 NimfMIEGEECTILDMICNmctNLESEAIDALI 261
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
167-221 |
3.44e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 48.11 E-value: 3.44e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 755492548 167 LINHG-AEVTCKDKKGYTPLHAAASNGQISVVKHLLNLGVEIDEINVYGNTALHIA 221
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
846-978 |
3.92e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 53.90 E-value: 3.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 846 ECLQLLLRHDAQVNAVDNSGKTALMMAAEN--GQAGAVDILVNSAqADLTVKDKDLNTPLHLAISKGHEK---CALLILD 920
Cdd:PHA03100 87 EIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNG-ANVNIKNSDGENLLHLYLESNKIDlkiLKLLIDK 165
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755492548 921 K------------IQDESLINAKNSALQTPLHIAARNGLKVVVEELLAKGACVLAVDENGHTPA-LACAPN 978
Cdd:PHA03100 166 GvdinaknrvnylLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLhIAILNN 236
|
|
| PHA02716 |
PHA02716 |
CPXV016; CPX019; EVM010; Provisional |
264-468 |
4.55e-07 |
|
CPXV016; CPX019; EVM010; Provisional
Pssm-ID: 165089 [Multi-domain] Cd Length: 764 Bit Score: 54.15 E-value: 4.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 264 LELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRS--QTLIQNGGEIDCVDKDGNTPLH---VAARHGHELLINTLITSGA 338
Cdd:PHA02716 195 LEWLCNNGVNVNLQNNHLITPLHTYLITGNVCASviKKIIELGGDMDMKCVNGMSPIMtyiINIDNINPEITNIYIESLD 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 339 DTAKCGIHSMFPLHLAalnahsdccrklLSSGQKYSIVslfsnEHVLSAGFEIDTPDTFGRTCLHAAAAGGNV--ECIKL 416
Cdd:PHA02716 275 GNKVKNIPMILHSYIT------------LARNIDISVV-----YSFLQPGVKLHYKDSAGRTCLHQYILRHNIstDIIKL 337
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755492548 417 LQSSGADFHKKDKCGRTPLH-YAAANCHFH-------------CIKALVTTGANVNETDDWGRTAL 468
Cdd:PHA02716 338 LHEYGNDLNEPDNIGNTVLHtYLSMLSVVNildpetdndirldVIQCLISLGADITAVNCLGYTPL 403
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
18-155 |
4.82e-07 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 53.86 E-value: 4.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 18 TPLHVAAFLGDAEIIELLILSGARVNA-----------KDNMWL---TPLHRAVASRSEEAVQVLIKHSADVNARDKNWQ 83
Cdd:cd22192 91 TALHIAVVNQNLNLVRELIARGADVVSpratgtffrpgPKNLIYygeHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGN 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 84 TPLH--VAAANKAVKCaEVIIPLLSSV---------NVSDRGGRTALHHAALNGHMEMVNLLLAKganinafdkkdRRAL 152
Cdd:cd22192 171 TVLHilVLQPNKTFAC-QMYDLILSYDkeddlqpldLVPNNQGLTPFKLAAKEGNIVMFQHLVQK-----------RRHI 238
|
...
gi 755492548 153 HWA 155
Cdd:cd22192 239 QWT 241
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
214-268 |
5.14e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 47.27 E-value: 5.14e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 755492548 214 GNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHFAAASTHGAlCLELLV 268
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVE-VLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
17-69 |
5.19e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 47.27 E-value: 5.19e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 755492548 17 RTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLI 69
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
184-343 |
6.65e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 51.36 E-value: 6.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 184 PLHAAASNGQISVVKHLLNLgveIDEINVYGNTALHiACYNGQDAVVNE---LIDYGANVN-QPNNSGFTPLHFAAASTH 259
Cdd:PHA02859 24 PLFYYVEKDDIEGVKKWIKF---VNDCNDLYETPIF-SCLEKDKVNVEIlkfLIENGADVNfKTRDNNLSALHHYLSFNK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 260 GAL--CLELLVNNGADVNIQSKDGKSPLH--MTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHV-AARHGHELLINTLI 334
Cdd:PHA02859 100 NVEpeILKILIDSGSSITEEDEDGKNLLHmyMCNFNVRINVIKLLIDSGVSFLNKDFDNNNILYSyILFHSDKKIFDFLT 179
|
....*....
gi 755492548 335 TSGADTAKC 343
Cdd:PHA02859 180 SLGIDINET 188
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
382-488 |
7.31e-07 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 53.33 E-value: 7.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 382 EHVLSAGFEIDTPDTFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPL-------HYAAANCHFHC-------- 446
Cdd:PLN03192 542 EELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnaisakHHKIFRILYHFasisdpha 621
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 755492548 447 ----------------IKALVTTGANVNETDDWGRTALHYAAASD-MDRNKMILGNAHD 488
Cdd:PLN03192 622 agdllctaakrndltaMKELLKQGLNVDSEDHQGATALQVAMAEDhVDMVRLLIMNGAD 680
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
164-236 |
7.53e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 53.36 E-value: 7.53e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755492548 164 VALLINHGAEVTCKDKKGYTPLHAAASNGQISVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDY 236
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
44-173 |
8.27e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 52.98 E-value: 8.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 44 AKDNMWLTPLHRAVasrSEEAVQVLIKHSADVNArdknwqtpLHVAAANKAVKcAEVIIPLLSSVNVSDRGGRTALHHAA 123
Cdd:PTZ00322 56 ATENKDATPDHNLT---TEEVIDPVVAHMLTVEL--------CQLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIAC 123
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 755492548 124 LNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAE 173
Cdd:PTZ00322 124 ANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQC 173
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
562-788 |
9.19e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 52.57 E-value: 9.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 562 SPLHLAAYNGHHQALEVLLQSLVDLDIRDE--KGRTALY---LAAFKghtecvEALVNQGASIFVKDNVTKRTPLHASVI 636
Cdd:PHA02878 72 TPLHIICKEPNKLGMKEMIRSINKCSVFYTlvAIKDAFNnrnVEIFK------IILTNRYKNIQTIDLVYIDKKSKDDII 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 637 NghTLCLRLLLETADNPEVVDvkDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIVGCTALHRGIMTGHEECVQMLL 716
Cdd:PHA02878 146 E--AEITKLLLSYGADINMKD--RHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILL 221
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755492548 717 EQEASILCKDSRGRTPLHYAAARGHATwlnELLQIALsEEDCCLKDNQ---GYTPLHWACYngNENCIEVLLEQK 788
Cdd:PHA02878 222 ENGASTDARDKCGNTPLHISVGYCKDY---DILKLLL-EHGVDVNAKSyilGLTALHSSIK--SERKLKLLLEYG 290
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
283-334 |
1.01e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 46.50 E-value: 1.01e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 755492548 283 SPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARHGHELLINTLI 334
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
845-988 |
1.68e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 51.53 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 845 AECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNSAQADLTVKDKDLNTPLHLA-ISKGHEKCALLILDKIQ 923
Cdd:PHA02875 48 SEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLAtILKKLDIMKLLIARGAD 127
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755492548 924 DEslinAKNSALQTPLHIAARNGLKVVVEELLAKGACVLAVDENGHTPALACAPNKDVADCLALI 988
Cdd:PHA02875 128 PD----IPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLL 188
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
815-965 |
1.73e-06 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 52.18 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 815 LLLGAIDPSIvscRDDKGRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNSAQADLTV 894
Cdd:PLN03192 544 LLKAKLDPDI---GDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPH 620
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755492548 895 KDKDLntpLHLAISKGHekcaLLILDKIQDESL-INAKNSALQTPLHIAARNGLKVVVEELLAKGACVLAVD 965
Cdd:PLN03192 621 AAGDL---LCTAAKRND----LTAMKELLKQGLnVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
30-146 |
2.17e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 49.82 E-value: 2.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 30 EIIELLILSGARVNAK---DNmwLTPLHRAVA---SRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAevIIP 103
Cdd:PHA02859 67 EILKFLIENGADVNFKtrdNN--LSALHHYLSfnkNVEPEILKILIDSGSSITEEDEDGKNLLHMYMCNFNVRIN--VIK 142
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 755492548 104 LLSSVNVS----DRGGRTALH-HAALNGHMEMVNLLLAKGANINAFDK 146
Cdd:PHA02859 143 LLIDSGVSflnkDFDNNNILYsYILFHSDKKIFDFLTSLGIDINETNK 190
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
729-785 |
2.42e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 45.34 E-value: 2.42e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 755492548 729 GRTPLHYAAARGHatwlNELLQIAL-SEEDCCLKDNQGYTPLHWACYNGNENCIEVLL 785
Cdd:pfam13637 1 ELTALHAAAASGH----LELLRLLLeKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
832-885 |
2.47e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 45.34 E-value: 2.47e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 755492548 832 GRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILV 885
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
406-475 |
2.78e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 51.44 E-value: 2.78e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 406 AAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIKALVTTGANVNETDDWGRTALHYAAASD 475
Cdd:PTZ00322 90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENG 159
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
815-891 |
3.65e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 51.05 E-value: 3.65e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755492548 815 LLLGAIDPSivsCRDDKGRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNSAQAD 891
Cdd:PTZ00322 101 LLTGGADPN---CRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCH 174
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
765-817 |
4.24e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 44.96 E-value: 4.24e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 755492548 765 GYTPLHWACYNGNENCIEVLLEQKC-FRKFIGNPFTPLHCAIINGHESCASLLL 817
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGAdINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
713-957 |
5.38e-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: 50.40 E-value: 5.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 713 QMLLEQEasiLCKDSRGR-TPLHYAAARGHATWLNELLQiaLSEEDCCLKDNQGYTPLHWACYNGNENCIEVLLEqkCFR 791
Cdd:cd22192 3 QMLDELH---LLQQKRISeSPLLLAAKENDVQAIKKLLK--CPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 792 KFIGNPFT--------PLHCAIINGHESCASLLL--GAidpSIVSCRDD-----KGRTTLhaAAFGDHAeclqlllrhda 856
Cdd:cd22192 76 ELVNEPMTsdlyqgetALHIAVVNQNLNLVRELIarGA---DVVSPRATgtffrPGPKNL--IYYGEHP----------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 857 qvnavdnsgktaLMMAAENGQAGAVDILVNSAqADLTVKDKDLNTPLHLAISKGHEKCA------LLILDKIQDE-SLIN 929
Cdd:cd22192 140 ------------LSFAACVGNEEIVRLLIEHG-ADIRAQDSLGNTVLHILVLQPNKTFAcqmydlILSYDKEDDLqPLDL 206
|
250 260
....*....|....*....|....*...
gi 755492548 930 AKNSALQTPLHIAARNGLKVVVEELLAK 957
Cdd:cd22192 207 VPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
115-143 |
5.85e-06 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 43.73 E-value: 5.85e-06
10 20
....*....|....*....|....*....
gi 755492548 115 GRTALHHAALNGHMEMVNLLLAKGANINA 143
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
133-188 |
7.00e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 44.26 E-value: 7.00e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 755492548 133 LLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAA 188
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
536-775 |
7.31e-06 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).
Pssm-ID: 411975 [Multi-domain] Cd Length: 600 Bit Score: 49.88 E-value: 7.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 536 GHRQCLELLLertnTGFEESDGGALKSPLHLAAYNGHHQALE---VLLQS---------LVDLDIRDE--KGRTALYLAA 601
Cdd:cd21882 6 GLLECLRWYL----TDSAYQRGATGKTCLHKAALNLNDGVNEaimLLLEAapdsgnpkeLVNAPCTDEfyQGQTALHIAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 602 FKGHTECVEALVNQGASIFVKDNVT--KRTPlhasvingHTLCLRllletadnpevvdvkdakGQTPLMLAVAYGHIDAV 679
Cdd:cd21882 82 ENRNLNLVRLLVENGADVSARATGRffRKSP--------GNLFYF------------------GELPLSLAACTNQEEIV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 680 SLLLE---KEANVDAVDIVGCTALHRGIMTGHEE------CVQM---LLEQEASI-------LCKDSRGRTPLHYAAARG 740
Cdd:cd21882 136 RLLLEngaQPAALEAQDSLGNTVLHALVLQADNTpensafVCQMynlLLSYGAHLdptqqleEIPNHQGLTPLKLAAVEG 215
|
250 260 270
....*....|....*....|....*....|....*...
gi 755492548 741 HATWLNELLQIALSEEDCCL--KDNQ-GYTPLHWACYN 775
Cdd:cd21882 216 KIVMFQHILQREFSGPYQPLsrKFTEwTYGPVTSSLYD 253
|
|
| TRPV1 |
cd22196 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ... |
115-257 |
9.14e-06 |
|
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: 49.80 E-value: 9.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 115 GRTALHHAALN---GHMEMVNLLL---AKGANINAF------DK--KDRRALHWAAYMGHLDVVALLINHGAEVTC---- 176
Cdd:cd22196 47 GKTCLLKAMLNlhnGQNDTISLLLdiaEKTGNLKEFvnaaytDSyyKGQTALHIAIERRNMHLVELLVQNGADVHArasg 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 177 ------KDKKGY----TPLHAAASNGQISVVKHLLN---LGVEIDEINVYGNTALH----IAcYNGQD------AVVNEL 233
Cdd:cd22196 127 effkkkKGGPGFyfgeLPLSLAACTNQLDIVKFLLEnphSPADISARDSMGNTVLHalveVA-DNTPEntkfvtKMYNEI 205
|
170 180 190
....*....|....*....|....*....|.
gi 755492548 234 IDYGANVNQ-------PNNSGFTPLHFAAAS 257
Cdd:cd22196 206 LILGAKIRPllkleeiTNKKGLTPLKLAAKT 236
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
799-852 |
9.20e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 43.80 E-value: 9.20e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 755492548 799 TPLHCAIINGHESCASLLLGAidPSIVSCRDDKGRTTLHAAAFGDHAECLQLLL 852
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEK--GADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
2-270 |
9.23e-06 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 49.28 E-value: 9.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 2 LIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSE--EAVQVLIKHSADV-NAR 78
Cdd:PHA02946 58 LLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEviERINLLVQYGAKInNSV 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 79 DKNWQTPLhVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAAL--NGHMEMVNLLLAKGANINAFDKKDRRALH--W 154
Cdd:PHA02946 138 DEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMsdNPKASTISWMMKLGISPSKPDHDGNTPLHivC 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 155 AAYMGHLDVVALLINhGAEVTCKDKKGYTPLHAAASNGQISvvkHLLNLGVEIDeiNVYGNTALHIACYNGQDAVVNELI 234
Cdd:PHA02946 217 SKTVKNVDIINLLLP-STDVNKQNKFGDSPLTLLIKTLSPA---HLINKLLSTS--NVITDQTVNICIFYDRDDVLEIIN 290
|
250 260 270
....*....|....*....|....*....|....*..
gi 755492548 235 DYGANVNQPNnsgftplhFAAASTHGAL-CLELLVNN 270
Cdd:PHA02946 291 DKGKQYDSTD--------FKMAVEVGSIrCVKYLLDN 319
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
637-716 |
1.28e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 49.13 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 637 NGHTLCLRLLLETADNPevvDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIVGCTALHRGIMTGHEECVQMLL 716
Cdd:PTZ00322 92 SGDAVGARILLTGGADP---NCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
115-146 |
1.74e-05 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 42.66 E-value: 1.74e-05
10 20 30
....*....|....*....|....*....|...
gi 755492548 115 GRTALHHAAL-NGHMEMVNLLLAKGANINAFDK 146
Cdd:pfam00023 2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
873-968 |
1.79e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 48.74 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 873 AENGQAGAVDILVNSAqADLTVKDKDLNTPLHLAISKGHEKCALLILDKIQDESLINAKNsalQTPLHIAARNGLKVVVE 952
Cdd:PTZ00322 90 AASGDAVGARILLTGG-ADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDG---KTPLELAEENGFREVVQ 165
|
90
....*....|....*.
gi 755492548 953 ELLAKGACVLAVDENG 968
Cdd:PTZ00322 166 LLSRHSQCHFELGANA 181
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
186-289 |
2.39e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 48.36 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 186 HAAASnGQISVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHFAAASTHGALcLE 265
Cdd:PTZ00322 88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREV-VQ 165
|
90 100 110
....*....|....*....|....*....|....*..
gi 755492548 266 LLV-------NNGADVNIQSKDGK------SPLHMTA 289
Cdd:PTZ00322 166 LLSrhsqchfELGANAKPDSFTGKppsledSPISSHH 202
|
|
| PHA02791 |
PHA02791 |
ankyrin-like protein; Provisional |
743-938 |
2.74e-05 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165154 [Multi-domain] Cd Length: 284 Bit Score: 47.34 E-value: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 743 TWLNELLQIALSEEDCCLKDNQGYTPLHWACYNGNENCIEVLLEQKCFRKFIGNPFtPLH-CAIINGHESCASLLLGAID 821
Cdd:PHA02791 8 TWKSKQLKSFLSSKDAFKADVHGHSALYYAIADNNVRLVCTLLNAGALKNLLENEF-PLHqAATLEDTKIVKILLFSGMD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 822 PSIVscrDDKGRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSG-KTALMMAAENGQAGAVDILVNSAQA--DLTVkdkd 898
Cdd:PHA02791 87 DSQF---DDKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTGwKTSFYHAVMLNDVSIVSYFLSEIPStfDLAI---- 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 755492548 899 LNTPLHLAISKGHEKCALLILDKIQDeslINAKNSALQTP 938
Cdd:PHA02791 160 LLSCIHITIKNGHVDMMILLLDYMTS---TNTNNSLLFIP 196
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
115-143 |
3.19e-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: 41.86 E-value: 3.19e-05
10 20
....*....|....*....|....*....
gi 755492548 115 GRTALHHAALNGHMEMVNLLLAKGANINA 143
Cdd:pfam13606 2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
664-887 |
3.24e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 47.68 E-value: 3.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 664 QTPLMLAVAYGHIDAVSLLLEKEANVDAVDIVGCTALHRGIMTGHEECVQMLLEQEASILCKDSRGRTPLHYAAARGHAT 743
Cdd:PHA02875 3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 744 WLNELLQIALSEEDCCLKDnqGYTPLHWACYNGNENCIEVLLEQKCfrkfignpftplhcaiinghescaslllgaiDPS 823
Cdd:PHA02875 83 AVEELLDLGKFADDVFYKD--GMTPLHLATILKKLDIMKLLIARGA-------------------------------DPD 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755492548 824 IVSCrdDKgRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNS 887
Cdd:PHA02875 130 IPNT--DK-FSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDS 190
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
68-122 |
3.44e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 42.33 E-value: 3.44e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 755492548 68 LIKH-SADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHA 122
Cdd:pfam13857 1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
867-961 |
3.47e-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: 47.70 E-value: 3.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 867 TALMMAAENGQAGAVDILVNSAQADLTVKDKDLNTPLHLAISKGHEKCALLILDkiQDESLIN-AKNSAL---QTPLHIA 942
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNePMTSDLyqgETALHIA 96
|
90
....*....|....*....
gi 755492548 943 ARNGLKVVVEELLAKGACV 961
Cdd:cd22192 97 VVNQNLNLVRELIARGADV 115
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
211-254 |
3.54e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 42.33 E-value: 3.54e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 755492548 211 NVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHFA 254
Cdd:pfam13857 13 DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
1-72 |
3.57e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 47.97 E-value: 3.57e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755492548 1 MLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHS 72
Cdd:PTZ00322 100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHS 171
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
350-417 |
3.68e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 42.26 E-value: 3.68e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755492548 350 PLHLAALNAHSDCCRKLLSSGqkysivslfsnehvlsagFEIDTPDTFGRTCLHAAAAGGNVECIKLL 417
Cdd:pfam13637 4 ALHAAAASGHLELLRLLLEKG------------------ADINAVDGNGETALHFAASNGNVEVLKLL 53
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
233-287 |
3.90e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 42.33 E-value: 3.90e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 755492548 233 LIDYG-ANVNQPNNSGFTPLHFAAasTHGAL-CLELLVNNGADVNIQSKDGKSPLHM 287
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAA--KYGALeIVRVLLAYGVDLNLKDEEGLTALDL 55
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
416-471 |
3.98e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 42.33 E-value: 3.98e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 755492548 416 LLQSSGADFHKKDKCGRTPLHYAAANCHFHCIKALVTTGANVNETDDWGRTALHYA 471
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
4-56 |
4.02e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 41.95 E-value: 4.02e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 755492548 4 HKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRA 56
Cdd:pfam13857 4 HGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
21-92 |
4.09e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 47.59 E-value: 4.09e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755492548 21 HVAAFlGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAAN 92
Cdd:PTZ00322 88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEEN 158
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
837-930 |
4.20e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 47.59 E-value: 4.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 837 HAAAFGDhAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNSAqADLTVKDKDLNTPLHLAISKGHEKCAL 916
Cdd:PTZ00322 88 QLAASGD-AVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFG-ADPTLLDKDGKTPLELAEENGFREVVQ 165
|
90
....*....|....
gi 755492548 917 LILDKIQDESLINA 930
Cdd:PTZ00322 166 LLSRHSQCHFELGA 179
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
593-647 |
4.30e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 41.88 E-value: 4.30e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 755492548 593 GRTALYLAAFKGHTECVEALVNQGASIFVKDNvTKRTPLHASVINGHTLCLRLLL 647
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDG-NGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
628-683 |
4.70e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 41.88 E-value: 4.70e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 755492548 628 RTPLHASVINGHTLCLRLLLEtadNPEVVDVKDAKGQTPLMLAVAYGHIDAVSLLL 683
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLE---KGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
850-906 |
4.71e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 41.95 E-value: 4.71e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 755492548 850 LLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNsAQADLTVKDKDLNTPLHLA 906
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLA-YGVDLNLKDEEGLTALDLA 56
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
667-752 |
4.97e-05 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 47.56 E-value: 4.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 667 LMLAVAYGHIDAVSLLLEKEANVDAVDIVGCTALHRGIMTGHEECVQMLLEQEASILCKDSRGRTPLHYAAARGHATWLN 746
Cdd:PLN03192 529 LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR 608
|
....*.
gi 755492548 747 ELLQIA 752
Cdd:PLN03192 609 ILYHFA 614
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
644-776 |
5.53e-05 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411978 [Multi-domain] Cd Length: 680 Bit Score: 47.06 E-value: 5.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 644 RLLLETADNPEVVDV--------KDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVD--------------IVGCTALH 701
Cdd:cd22194 114 RILLAFAEENGILDRfinaeyteEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAkgvffnpkykhegfYFGETPLA 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 702 RGIMTGHEECVQMLLEQEAS-ILCKDSRGRTPLHYAA-----ARGHATWLNELL-QIALSEEDCCL---KDNQGYTPLHW 771
Cdd:cd22194 194 LAACTNQPEIVQLLMEKESTdITSQDSRGNTVLHALVtvaedSKTQNDFVKRMYdMILLKSENKNLetiRNNEGLTPLQL 273
|
....*
gi 755492548 772 ACYNG 776
Cdd:cd22194 274 AAKMG 278
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
213-241 |
5.80e-05 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 41.03 E-value: 5.80e-05
10 20
....*....|....*....|....*....
gi 755492548 213 YGNTALHIACYNGQDAVVNELIDYGANVN 241
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
712-785 |
6.54e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 46.82 E-value: 6.54e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755492548 712 VQMLLEQEASILCKDSRGRTPLHYAAARGHATWLNELLQIAlseEDCCLKDNQGYTPLHWACYNGNENCIEVLL 785
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFG---ADPTLLDKDGKTPLELAEENGFREVVQLLS 168
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
285-374 |
6.77e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 46.82 E-value: 6.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 285 LHMTAVH-------GRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARHGHELLINTLITSGADTAKCGIHSMFPLHLAALN 357
Cdd:PTZ00322 79 AHMLTVElcqlaasGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEEN 158
|
90
....*....|....*..
gi 755492548 358 AHSDCCRKLLSSGQKYS 374
Cdd:PTZ00322 159 GFREVVQLLSRHSQCHF 175
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
351-469 |
6.93e-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: 46.80 E-value: 6.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 351 LHLAALNAHS---DCCRKLLSSGQKYSIVSLFSNEHVLSAGFEidtpdtfGRTCLHAAAAGGNVECIKLLQSSGADFH-- 425
Cdd:cd21882 30 LHKAALNLNDgvnEAIMLLLEAAPDSGNPKELVNAPCTDEFYQ-------GQTALHIAIENRNLNLVRLLVENGADVSar 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 755492548 426 ------KKDKC-----GRTPLHYAAANCHFHCIKALVTTG---ANVNETDDWGRTALH 469
Cdd:cd21882 103 atgrffRKSPGnlfyfGELPLSLAACTNQEEIVRLLLENGaqpAALEAQDSLGNTVLH 160
|
|
| PHA02884 |
PHA02884 |
ankyrin repeat protein; Provisional |
211-288 |
7.21e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165212 [Multi-domain] Cd Length: 300 Bit Score: 46.13 E-value: 7.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 211 NVYGNTALHIACYNGQDAVVNeLIDYGANVNQ-PNNSGFTPLHFAAasTHGAL-CLELLVNNGADVNIQSKDGKSPLHMT 288
Cdd:PHA02884 68 NSKTNPLIYAIDCDNDDAAKL-LIRYGADVNRyAEEAKITPLYISV--LHGCLkCLEILLSYGADINIQTNDMVTPIELA 144
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
188-325 |
8.19e-05 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411978 [Multi-domain] Cd Length: 680 Bit Score: 46.68 E-value: 8.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 188 AASNGqisVVKHLLNlgVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVN--------QP--NNSGF----TPLHF 253
Cdd:cd22194 120 AEENG---ILDRFIN--AEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNahakgvffNPkyKHEGFyfgeTPLAL 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 254 AAASTHGALcLELLVNNGADvNIQSKD--GKSPLHMTAVHGRFTRSQT-----------LIQNGGEIDCV-DKDGNTPLH 319
Cdd:cd22194 195 AACTNQPEI-VQLLMEKEST-DITSQDsrGNTVLHALVTVAEDSKTQNdfvkrmydmilLKSENKNLETIrNNEGLTPLQ 272
|
....*.
gi 755492548 320 VAARHG 325
Cdd:cd22194 273 LAAKMG 278
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
314-367 |
8.31e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 41.11 E-value: 8.31e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 755492548 314 GNTPLHVAARHGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLL 367
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| TRPV1-4 |
cd22193 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ... |
115-257 |
9.22e-05 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411977 [Multi-domain] Cd Length: 607 Bit Score: 46.33 E-value: 9.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 115 GRTALHHAALNGHMEMVNLLLAKGANINA------FDKKDRRA--------LHWAAYMGHLDVVALLINHG---AEVTCK 177
Cdd:cd22193 76 GQTALHIAIERRQGDIVALLVENGADVHAhakgrfFQPKYQGEgfyfgelpLSLAACTNQPDIVQYLLENEhqpADIEAQ 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 178 DKKGYTPLHAAasngqisvvkhllnlgVEIDEiNVYGNTALHIACYNGqdavvneLIDYGANVNQP-------NNSGFTP 250
Cdd:cd22193 156 DSRGNTVLHAL----------------VTVAD-NTKENTKFVTRMYDM-------ILIRGAKLCPTveleeirNNDGLTP 211
|
....*..
gi 755492548 251 LHFAAAS 257
Cdd:cd22193 212 LQLAAKM 218
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
115-255 |
1.13e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411978 [Multi-domain] Cd Length: 680 Bit Score: 46.29 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 115 GRTALHHAALNGHMEMVNLLLAKGANINA------FDKKDRralHWAAYMGHldvvallinhgaevtckdkkgyTPLHAA 188
Cdd:cd22194 141 GQTALNIAIERRQGDIVKLLIAKGADVNAhakgvfFNPKYK---HEGFYFGE----------------------TPLALA 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 189 ASNGQISVVKHLL-NLGVEIDEINVYGNTALH---IACYN--GQDAVVNELIDY------GANVNQ-PNNSGFTPLHFAA 255
Cdd:cd22194 196 ACTNQPEIVQLLMeKESTDITSQDSRGNTVLHalvTVAEDskTQNDFVKRMYDMillkseNKNLETiRNNEGLTPLQLAA 275
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
107-155 |
1.14e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 40.79 E-value: 1.14e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 755492548 107 SVNVSDRGGRTALHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWA 155
Cdd:pfam13857 8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
213-245 |
1.19e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 40.35 E-value: 1.19e-04
10 20 30
....*....|....*....|....*....|....
gi 755492548 213 YGNTALHIACY-NGQDAVVNELIDYGANVNQPNN 245
Cdd:pfam00023 1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
|
|
| TRPV2 |
cd22197 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ... |
398-551 |
1.20e-04 |
|
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: 46.00 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 398 GRTCLHAAAAGGNVECIKLLQSSGADFH----------KKDKC---GRTPLHYAAANCHFHCIKALVTTG---ANVNETD 461
Cdd:cd22197 94 GHSALHIAIEKRSLQCVKLLVENGADVHaracgrffqkKQGTCfyfGELPLSLAACTKQWDVVNYLLENPhqpASLQAQD 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 462 DWGRTALHYAAasdmdrnkMILGNAHDNSEELERA-REVKEKDAALCLEFLLQndanpSIRDKEGYNSIHYAAAYGHRQC 540
Cdd:cd22197 174 SLGNTVLHALV--------MIADNSPENSALVIKMyDGLLQAGARLCPTVQLE-----EISNHEGLTPLKLAAKEGKIEI 240
|
170
....*....|.
gi 755492548 541 LELLLERTNTG 551
Cdd:cd22197 241 FRHILQREFSG 251
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
704-910 |
1.67e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).
Pssm-ID: 411975 [Multi-domain] Cd Length: 600 Bit Score: 45.64 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 704 IMTGHEECVQMLLEQeaSILCKDSRGRTPLHYAAARGHATWLNE---LLQIA--------LSEEDCCLKDNQGYTPLHWA 772
Cdd:cd21882 3 ELLGLLECLRWYLTD--SAYQRGATGKTCLHKAALNLNDGVNEAimlLLEAApdsgnpkeLVNAPCTDEFYQGQTALHIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 773 CYNGNENCIEVLLEQKC----------FRKFIGNPF----TPLHCAIINGHESCASLLL-GAIDPSIVSCRDDKGRTTLH 837
Cdd:cd21882 81 IENRNLNLVRLLVENGAdvsaratgrfFRKSPGNLFyfgeLPLSLAACTNQEEIVRLLLeNGAQPAALEAQDSLGNTVLH 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755492548 838 AaafgdhaeclqLLLRHDaqvNAVDNSgKTALMMAAENGQAGAVdiLVNSAQADLTVKDKDLnTPLHLAISKG 910
Cdd:cd21882 161 A-----------LVLQAD---NTPENS-AFVCQMYNLLLSYGAH--LDPTQQLEEIPNHQGL-TPLKLAAVEG 215
|
|
| PHA02716 |
PHA02716 |
CPXV016; CPX019; EVM010; Provisional |
189-318 |
1.90e-04 |
|
CPXV016; CPX019; EVM010; Provisional
Pssm-ID: 165089 [Multi-domain] Cd Length: 764 Bit Score: 45.67 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 189 ASNGQISVVKHLLNLGVEIDEINVYGNTALH--IACYNGQDAVVNELIDYGANVNQPNNSGFTPLHfaaaSTHGALCLEL 266
Cdd:PHA02716 292 ARNIDISVVYSFLQPGVKLHYKDSAGRTCLHqyILRHNISTDIIKLLHEYGNDLNEPDNIGNTVLH----TYLSMLSVVN 367
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 755492548 267 LVNNGADVNIqskdgksplhmtavhgRFTRSQTLIQNGGEIDCVDKDGNTPL 318
Cdd:PHA02716 368 ILDPETDNDI----------------RLDVIQCLISLGADITAVNCLGYTPL 403
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
131-417 |
1.99e-04 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 45.04 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 131 VNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHaaasngqisvvkHLLNLGVEIDEi 210
Cdd:PHA02946 55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLY------------YLSGTDDEVIE- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 211 nvygntalhiacyngqdaVVNELIDYGANVNQP-NNSGFTPLhfAAASTHGALCLELLVNNGADVNIQSKDGKSPLH--M 287
Cdd:PHA02946 122 ------------------RINLLVQYGAKINNSvDEEGCGPL--LACTDPSERVFKKIMSIGFEARIVDKFGKNHIHrhL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 288 TAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLH-VAARHGHELLINTLITSGADTAKCGIHSMFPLHLAALN-AHSDCCRK 365
Cdd:PHA02946 182 MSDNPKASTISWMMKLGISPSKPDHDGNTPLHiVCSKTVKNVDIINLLLPSTDVNKQNKFGDSPLTLLIKTlSPAHLINK 261
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 755492548 366 LLSSG-----QKYSIVSLFSNEHVLsagfEI--DTPDTFGRTCLHAAAAGGNVECIKLL 417
Cdd:PHA02946 262 LLSTSnvitdQTVNICIFYDRDDVL----EIinDKGKQYDSTDFKMAVEVGSIRCVKYL 316
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
307-469 |
2.31e-04 |
|
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: 45.07 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 307 IDCVDKDGNTPLHVAARHG-HELLINTLITSGA-----DTAkcgihsmfpLHLAALNAH---SDCCRKLLSSGQKYSIVS 377
Cdd:TIGR00870 45 INCPDRLGRSALFVAAIENeNLELTELLLNLSCrgavgDTL---------LHAISLEYVdavEAILLHLLAAFRKSGPLE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 378 LfsnehvlsaGFEIDTPD-TFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKC--------------GRTPLHYAAANC 442
Cdd:TIGR00870 116 L---------ANDQYTSEfTPGITALHLAAHRQNYEIVKLLLERGASVPARACGdffvksqgvdsfyhGESPLNAAACLG 186
|
170 180
....*....|....*....|....*..
gi 755492548 443 HFHCIKALVTTGANVNETDDWGRTALH 469
Cdd:TIGR00870 187 SPSIVALLSEDPADILTADSLGNTLLH 213
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
815-978 |
2.32e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 45.05 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 815 LLLGAIDpsiVSCRDDKGRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNSAQadlTV 894
Cdd:PHA02876 164 LLEGGAD---VNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRS---NI 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 895 KDKDLNtpLHLAISKGHEKCALLILDKiqdESLINAKNSALQTPLHIAARN-GLKVVVEELLAKGACVLAVDENGHTPAL 973
Cdd:PHA02876 238 NKNDLS--LLKAIRNEDLETSLLLYDA---GFSVNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKGETPLY 312
|
....*
gi 755492548 974 ACAPN 978
Cdd:PHA02876 313 LMAKN 317
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
507-545 |
2.58e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 39.95 E-value: 2.58e-04
10 20 30
....*....|....*....|....*....|....*....
gi 755492548 507 CLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLL 545
Cdd:pfam13637 16 LLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
197-515 |
2.62e-04 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 44.66 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 197 VKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHFAAASTHGAL-CLELLVNNGADVN 275
Cdd:PHA02946 55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIeRINLLVQYGAKIN 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 276 iqskdgksplhmtavhgrftrsqtliqnggeiDCVDKDGNTPLhVAARHGHELLINTLITSGadtakcgihsmFPLHLAA 355
Cdd:PHA02946 135 --------------------------------NSVDEEGCGPL-LACTDPSERVFKKIMSIG-----------FEARIVD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 356 LNAHSDCCRKLLSSGQKYSIVSLfsnehVLSAGFEIDTPDTFGRTCLHAAAAG--GNVECIKLLQSSgADFHKKDKCGRT 433
Cdd:PHA02946 171 KFGKNHIHRHLMSDNPKASTISW-----MMKLGISPSKPDHDGNTPLHIVCSKtvKNVDIINLLLPS-TDVNKQNKFGDS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 434 PLHYAAANCH-FHCIKALVTTGANVneTDDWGRTALHYaaasdmDRNKMI-----LGNAHDnSEELERAREVkekDAALC 507
Cdd:PHA02946 245 PLTLLIKTLSpAHLINKLLSTSNVI--TDQTVNICIFY------DRDDVLeiindKGKQYD-STDFKMAVEV---GSIRC 312
|
....*...
gi 755492548 508 LEFLLQND 515
Cdd:PHA02946 313 VKYLLDND 320
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
836-989 |
2.96e-04 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 44.86 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 836 LHAAAFGDhAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNSAqADLTVKDKDLNTPLHLAISKGHEKCa 915
Cdd:PLN03192 530 LTVASTGN-AALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA-CNVHIRDANGNTALWNAISAKHHKI- 606
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755492548 916 LLILDKIQDESLINAKNSALQTplhiAARNGLKVVVEELLAKGACVLAVDENGHTpALACAPNKDVADCLALIL 989
Cdd:PLN03192 607 FRILYHFASISDPHAAGDLLCT----AAKRNDLTAMKELLKQGLNVDSEDHQGAT-ALQVAMAEDHVDMVRLLI 675
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
247-279 |
3.09e-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: 3.09e-04
10 20 30
....*....|....*....|....*....|...
gi 755492548 247 GFTPLHFAAASTHGALCLELLVNNGADVNIQSK 279
Cdd:pfam00023 2 GNTPLHLAAGRRGNLEIVKLLLSKGADVNARDK 34
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
431-459 |
3.30e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 38.72 E-value: 3.30e-04
10 20
....*....|....*....|....*....
gi 755492548 431 GRTPLHYAAANCHFHCIKALVTTGANVNE 459
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
599-683 |
3.31e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 44.50 E-value: 3.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 599 LAAfKGHTECVEALVNQGASIFVKDnVTKRTPLHASVINGHTLCLRLLLETADNPEVVDvKDakGQTPLMLAVAYGHIDA 678
Cdd:PTZ00322 89 LAA-SGDAVGARILLTGGADPNCRD-YDGRTPLHIACANGHVQVVRVLLEFGADPTLLD-KD--GKTPLELAEENGFREV 163
|
....*
gi 755492548 679 VSLLL 683
Cdd:PTZ00322 164 VQLLS 168
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
176-322 |
3.44e-04 |
|
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: 44.69 E-value: 3.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 176 CKDKKGYTPL-HAAASNGQISVVKHLLNLGVEIDEinvyGNTALHIACYNGQDAVvNELI----------DYGANVNQPN 244
Cdd:TIGR00870 47 CPDRLGRSALfVAAIENENLELTELLLNLSCRGAV----GDTLLHAISLEYVDAV-EAILlhllaafrksGPLELANDQY 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 245 NSGF----TPLHFAAaSTHGALCLELLVNNGADVNIQSKDG---KSPLHMTAVHGRFTRS-----------QTLIQNGGE 306
Cdd:TIGR00870 122 TSEFtpgiTALHLAA-HRQNYEIVKLLLERGASVPARACGDffvKSQGVDSFYHGESPLNaaaclgspsivALLSEDPAD 200
|
170
....*....|....*.
gi 755492548 307 IDCVDKDGNTPLHVAA 322
Cdd:TIGR00870 201 ILTADSLGNTLLHLLV 216
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
431-462 |
3.91e-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: 3.91e-04
10 20 30
....*....|....*....|....*....|...
gi 755492548 431 GRTPLHYAAANC-HFHCIKALVTTGANVNETDD 462
Cdd:pfam00023 2 GNTPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
662-693 |
3.91e-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: 3.91e-04
10 20 30
....*....|....*....|....*....|...
gi 755492548 662 KGQTPLMLAVA-YGHIDAVSLLLEKEANVDAVD 693
Cdd:pfam00023 1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
30-202 |
4.21e-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: 44.36 E-value: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 30 EIIELLI-----------LSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKN-WQTPLHvaaankavkc 97
Cdd:cd22194 111 EIVRILLafaeengildrFINAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGvFFNPKY---------- 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 98 aeviipllssvnvSDRG---GRTALHHAALNGHMEMVNLLLAKGANINAF-DKKDRRALHwAAYM------GHLDVV--- 164
Cdd:cd22194 181 -------------KHEGfyfGETPLALAACTNQPEIVQLLMEKESTDITSqDSRGNTVLH-ALVTvaedskTQNDFVkrm 246
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 755492548 165 --ALLINHGAEV--TCKDKKGYTPLHAAASNGQISVVKHLLN 202
Cdd:cd22194 247 ydMILLKSENKNleTIRNNEGLTPLQLAAKMGKAEILKYILS 288
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
831-946 |
4.62e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411978 [Multi-domain] Cd Length: 680 Bit Score: 44.36 E-value: 4.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 831 KGRTTLHAAAFGDHAECLQLLLRHDAQVNA---------VDNS-----GKTALMMAAENGQAGAVDILVNSAQADLTVKD 896
Cdd:cd22194 140 EGQTALNIAIERRQGDIVKLLIAKGADVNAhakgvffnpKYKHegfyfGETPLALAACTNQPEIVQLLMEKESTDITSQD 219
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 755492548 897 KDLNTPLHLAI-----SKGHEKCALLILDKI----QDESLINAKNSALQTPLHIAARNG 946
Cdd:cd22194 220 SRGNTVLHALVtvaedSKTQNDFVKRMYDMIllksENKNLETIRNNEGLTPLQLAAKMG 278
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
180-209 |
5.39e-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: 5.39e-04
10 20 30
....*....|....*....|....*....|
gi 755492548 180 KGYTPLHAAASNGQISVVKHLLNLGVEIDE 209
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
819-872 |
5.61e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 38.87 E-value: 5.61e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 755492548 819 AIDPSIVSCRDDKGRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMA 872
Cdd:pfam13857 3 EHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| TRPV2 |
cd22197 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ... |
115-255 |
6.27e-04 |
|
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: 43.69 E-value: 6.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 115 GRTALHHAALNGHMEMVNLLLAKGANINA------FDKKDRRALhwaaYMGHLdvvallinhgaevtckdkkgytPLHAA 188
Cdd:cd22197 94 GHSALHIAIEKRSLQCVKLLVENGADVHAracgrfFQKKQGTCF----YFGEL----------------------PLSLA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 189 ASNGQISVVKHLLNLGVE---IDEINVYGNTALHIACYNGQDAVVN---------ELIDYGANVNQ-------PNNSGFT 249
Cdd:cd22197 148 ACTKQWDVVNYLLENPHQpasLQAQDSLGNTVLHALVMIADNSPENsalvikmydGLLQAGARLCPtvqleeiSNHEGLT 227
|
....*.
gi 755492548 250 PLHFAA 255
Cdd:cd22197 228 PLKLAA 233
|
|
| PHA02743 |
PHA02743 |
Viral ankyrin protein; Provisional |
128-247 |
6.95e-04 |
|
Viral ankyrin protein; Provisional
Pssm-ID: 222925 [Multi-domain] Cd Length: 166 Bit Score: 41.34 E-value: 6.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 128 MEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVV---ALLINHGAEVTCKDKK-GYTPLHAAASNGQISVVKHLL-N 202
Cdd:PHA02743 37 MEVAPFISGDGHLLHRYDHHGRQCTHMVAWYDRANAVmkiELLVNMGADINARELGtGNTLLHIAASTKNYELAEWLCrQ 116
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 755492548 203 LGVEIDEINVYGNTALHIAcYNGQDAVVNE-LIDYGANVNQPNNSG 247
Cdd:PHA02743 117 LGVNLGAINYQHETAYHIA-YKMRDRRMMEiLRANGAVCDDPLSIG 161
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
213-241 |
7.76e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 37.62 E-value: 7.76e-04
10 20
....*....|....*....|....*....
gi 755492548 213 YGNTALHIACYNGQDAVVNELIDYGANVN 241
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
249-301 |
7.91e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 38.41 E-value: 7.91e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 755492548 249 TPLHFAAASTHGAlCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLI 301
Cdd:pfam13637 3 TALHAAAASGHLE-LLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
900-946 |
7.99e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 38.41 E-value: 7.99e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 755492548 900 NTPLHLAISKGHEKCALLILDKIQDeslINAKNSALQTPLHIAARNG 946
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGAD---INAVDGNGETALHFAASNG 45
|
|
| PHA02791 |
PHA02791 |
ankyrin-like protein; Provisional |
119-250 |
8.05e-04 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165154 [Multi-domain] Cd Length: 284 Bit Score: 42.72 E-value: 8.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 119 LHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGY-TPLHAAASNGQISVV 197
Cdd:PHA02791 65 LHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTGWkTSFYHAVMLNDVSIV 144
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 755492548 198 KHLLNLGVEIDEINVYgNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTP 250
Cdd:PHA02791 145 SYFLSEIPSTFDLAIL-LSCIHITIKNGHVDMMILLLDYMTSTNTNNSLLFIP 196
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
15-201 |
8.12e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).
Pssm-ID: 411975 [Multi-domain] Cd Length: 600 Bit Score: 43.33 E-value: 8.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 15 EKRTPLHVAAFLGDAEIIELLILSGARVNAKDN-------------MWLTPLHRAVASRSEEAVQVLIKHSAD---VNAR 78
Cdd:cd21882 72 QGQTALHIAIENRNLNLVRLLVENGADVSARATgrffrkspgnlfyFGELPLSLAACTNQEEIVRLLLENGAQpaaLEAQ 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 79 DKNWQTPLH--VAAANKAVKCAEVIIpllssvnvsdrggrtalhhaalnghmEMVNLLLAKGANINafdkkdrralhwaa 156
Cdd:cd21882 152 DSLGNTVLHalVLQADNTPENSAFVC--------------------------QMYNLLLSYGAHLD-------------- 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 755492548 157 ymgHLDVVALLINHgaevtckdkKGYTPLHAAASNGQISVVKHLL 201
Cdd:cd21882 192 ---PTQQLEEIPNH---------QGLTPLKLAAVEGKIVMFQHIL 224
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
710-876 |
8.20e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 43.46 E-value: 8.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 710 ECVQMLLEQEASILC-KDSRGRTPLHYAAarghatwLNELLQIA--LSEEDCCLKDN-------QGYTPLHWACYNGNEN 779
Cdd:cd22192 31 QAIKKLLKCPSCDLFqRGALGETALHVAA-------LYDNLEAAvvLMEAAPELVNEpmtsdlyQGETALHIAVVNQNLN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 780 CIEVLLEQ-----------KCFRKFIGNPFT----PLHCAIINGHESCASLLL--GAidpSIVScRDDKGRTTLHAAAFG 842
Cdd:cd22192 104 LVRELIARgadvvspratgTFFRPGPKNLIYygehPLSFAACVGNEEIVRLLIehGA---DIRA-QDSLGNTVLHILVLQ 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 755492548 843 DHA----ECLQLLLRHDAQVNAV------DNSGKTALMMAAENG 876
Cdd:cd22192 180 PNKtfacQMYDLILSYDKEDDLQpldlvpNNQGLTPFKLAAKEG 223
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
720-772 |
8.65e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 38.48 E-value: 8.65e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 755492548 720 ASILCKDSRGRTPLHYAAARGHATWLNELLqiaLSEEDCCLKDNQGYTPLHWA 772
Cdd:pfam13857 7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLL---AYGVDLNLKDEEGLTALDLA 56
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
636-758 |
9.36e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 43.35 E-value: 9.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 636 INGHTLCLRLLLETADNP-------EVVDVKDAKgqtplMLAVAYGHIDA------VSLLLEKEANVDAVDIVGCTALHR 702
Cdd:PTZ00322 47 IDTHLEALEATENKDATPdhnltteEVIDPVVAH-----MLTVELCQLAAsgdavgARILLTGGADPNCRDYDGRTPLHI 121
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 755492548 703 GIMTGHEECVQMLLEQEASILCKDSRGRTPLHYAAARGhatwLNELLQIALSEEDC 758
Cdd:PTZ00322 122 ACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENG----FREVVQLLSRHSQC 173
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
681-736 |
1.03e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 38.10 E-value: 1.03e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 755492548 681 LLLEKEANVDAVDIVGCTALHRGIMTGHEECVQMLLEQEASILCKDSRGRTPLHYA 736
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
384-441 |
1.05e-03 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 42.96 E-value: 1.05e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 755492548 384 VLSAGFEIDTPDTFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAAN 441
Cdd:PTZ00322 101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEEN 158
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
411-704 |
1.12e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 42.90 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 411 VECIKLLQSSGADFHKKDKCGRTPL-----HYAAANCHFHCIKALVTTGANVNETDDWGRTALHyaaasdmdrnkMILGN 485
Cdd:PHA02798 51 TDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLY-----------CLLSN 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 486 AHDNSEELerarevkekdaalcLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELllertntgfeesdggalksplh 565
Cdd:PHA02798 120 GYINNLEI--------------LLFMIENGADTTLLDKDGFTMLQVYLQSNHHIDIEI---------------------- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 566 laaynghhqaLEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEA-----LVNQGASIFVKDNVTKRTPLhasvingHT 640
Cdd:PHA02798 164 ----------IKLLLEKGVDINTHNNKEKYDTLHCYFKYNIDRIDAdilklFVDNGFIINKENKSHKKKFM-------EY 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755492548 641 LCLRLLLETADNPEVVDV---------KDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIVGCTALHRGI 704
Cdd:PHA02798 227 LNSLLYDNKRFKKNILDFifsyidinqVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAF 299
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
40-89 |
1.13e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 38.10 E-value: 1.13e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 755492548 40 ARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVA 89
Cdd:pfam13857 7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
525-580 |
1.22e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 38.02 E-value: 1.22e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 755492548 525 GYNSIHYAAAYGHRQCLELLLERTNTGFEESDGGAlkSPLHLAAYNGHHQALEVLL 580
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGE--TALHFAASNGNVEVLKLLL 54
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
390-438 |
1.30e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 37.71 E-value: 1.30e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 755492548 390 EIDTPDTFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYA 438
Cdd:pfam13857 8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
180-209 |
1.51e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 36.85 E-value: 1.51e-03
10 20 30
....*....|....*....|....*....|
gi 755492548 180 KGYTPLHAAASNGQISVVKHLLNLGVEIDE 209
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
313-339 |
1.64e-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: 1.64e-03
10 20
....*....|....*....|....*..
gi 755492548 313 DGNTPLHVAARHGHELLINTLITSGAD 339
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
|
|
| PHA02791 |
PHA02791 |
ankyrin-like protein; Provisional |
510-684 |
1.74e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165154 [Multi-domain] Cd Length: 284 Bit Score: 41.57 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 510 FLLQNDANPSirDKEGYNSIHYAAAYGHRQCLELLLertntgfeesDGGALKS------PLHLAAYNGHHQALEVLLQSL 583
Cdd:PHA02791 17 FLSSKDAFKA--DVHGHSALYYAIADNNVRLVCTLL----------NAGALKNllenefPLHQAATLEDTKIVKILLFSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 584 VDLDIRDEKGRTALYLAAFKGHTECVEALVNQGASIFVKDNVTKRTPL-HASVINGHTLCLRLLLETadnPEVVDVkdAK 662
Cdd:PHA02791 85 MDDSQFDDKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTGWKTSFyHAVMLNDVSIVSYFLSEI---PSTFDL--AI 159
|
170 180
....*....|....*....|..
gi 755492548 663 GQTPLMLAVAYGHIDAVSLLLE 684
Cdd:PHA02791 160 LLSCIHITIKNGHVDMMILLLD 181
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
17-47 |
1.89e-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: 36.88 E-value: 1.89e-03
10 20 30
....*....|....*....|....*....|..
gi 755492548 17 RTPLHVAA-FLGDAEIIELLILSGARVNAKDN 47
Cdd:pfam00023 3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
164-293 |
2.03e-03 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 42.19 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 164 VALLINHGAEVTCKDKKGYTPLHAAASNGQIS-VVKHLLNlgVEIDEINVYGntalhiacyngqDAV-VNELIDYGANVN 241
Cdd:PTZ00322 44 IARIDTHLEALEATENKDATPDHNLTTEEVIDpVVAHMLT--VELCQLAASG------------DAVgARILLTGGADPN 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 755492548 242 QPNNSGFTPLHFAAASTHGALcLELLVNNGADVNIQSKDGKSPLHMTAVHGR 293
Cdd:PTZ00322 110 CRDYDGRTPLHIACANGHVQV-VRVLLEFGADPTLLDKDGKTPLELAEENGF 160
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
662-691 |
2.07e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 36.47 E-value: 2.07e-03
10 20 30
....*....|....*....|....*....|
gi 755492548 662 KGQTPLMLAVAYGHIDAVSLLLEKEANVDA 691
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
764-786 |
2.26e-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: 2.26e-03
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
592-624 |
2.28e-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: 2.28e-03
10 20 30
....*....|....*....|....*....|....
gi 755492548 592 KGRTALYLAAFK-GHTECVEALVNQGASIFVKDN 624
Cdd:pfam00023 1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
653-701 |
2.32e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 37.33 E-value: 2.32e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 755492548 653 PEVVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIVGCTALH 701
Cdd:pfam13857 6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
430-459 |
2.36e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 36.47 E-value: 2.36e-03
10 20 30
....*....|....*....|....*....|
gi 755492548 430 CGRTPLHYAAANCHFHCIKALVTTGANVNE 459
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
151-179 |
2.51e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 36.50 E-value: 2.51e-03
10 20 30
....*....|....*....|....*....|
gi 755492548 151 ALHWAAYM-GHLDVVALLINHGAEVTCKDK 179
Cdd:pfam00023 5 PLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
713-956 |
2.56e-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: 41.99 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 713 QMLLEQEAS-ILCKDSRGRTPLHYAAARGHatwlNELLQIALSEEDCclKDNQGYTPLHWACYNGNENCIEVLLEQKCFR 791
Cdd:TIGR00870 35 RDLEEPKKLnINCPDRLGRSALFVAAIENE----NLELTELLLNLSC--RGAVGDTLLHAISLEYVDAVEAILLHLLAAF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 792 KFIGNPF--------------TPLHCAIINGHESCASLLL--GAIDPSIVSCRDDK----------GRTTLHAAAFGDHA 845
Cdd:TIGR00870 109 RKSGPLElandqytseftpgiTALHLAAHRQNYEIVKLLLerGASVPARACGDFFVksqgvdsfyhGESPLNAAACLGSP 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 846 ECLQLLLRHDAQVNAVDNSGKTALMMAAEngqagavdilvnsaQADLTVKDKDLNTPLHLAiskghekcALLILDKIQD- 924
Cdd:TIGR00870 189 SIVALLSEDPADILTADSLGNTLLHLLVM--------------ENEFKAEYEELSCQMYNF--------ALSLLDKLRDs 246
|
250 260 270
....*....|....*....|....*....|..
gi 755492548 925 ESLINAKNSALQTPLHIAARNGLKVVVEELLA 956
Cdd:TIGR00870 247 KELEVILNHQGLTPLKLAAKEGRIVLFRLKLA 278
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
18-96 |
2.59e-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: 41.99 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 18 TPLHVAAFLGDAEIIELLILSGARVNAKDN--MWLT------------PLHRAVASRSEEAVQVLIKHSADVNARDKNWQ 83
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLLERGASVPARACgdFFVKsqgvdsfyhgesPLNAAACLGSPSIVALLSEDPADILTADSLGN 209
|
90
....*....|...
gi 755492548 84 TPLHVAAANKAVK 96
Cdd:TIGR00870 210 TLLHLLVMENEFK 222
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
833-1044 |
2.81e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 41.52 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 833 RTTLHAAAFGDHAECLQLLLRHDAQVNAV-DNSGKTALMMAAENGQAGAVDILVnSAQADLTVKDKDLNTPLHLAISKGH 911
Cdd:PHA02875 69 ESELHDAVEEGDVKAVEELLDLGKFADDVfYKDGMTPLHLATILKKLDIMKLLI-ARGADPDIPNTDKFSPLHLAVMMGD 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 912 EKCALLILDKiqdESLINAKNSALQTPLHIAARNGLKVVVEELLAKGACVLAVDENGHTPALACAPNKDVADCLALIL-- 989
Cdd:PHA02875 148 IKGIELLIDH---KACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIkr 224
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 990 ---ATMMTFSPSSTMTAVNFVCFRKDNLSRMTHSNLGSRVSLC--SNNVGSEDGYNENDS 1044
Cdd:PHA02875 225 gadCNIMFMIEGEECTILDMICNMCTNLESEAIDALIADIAIRihKKTIRRDEGFKNNMS 284
|
|
| PHA02795 |
PHA02795 |
ankyrin-like protein; Provisional |
99-176 |
2.91e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165157 [Multi-domain] Cd Length: 437 Bit Score: 41.52 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 99 EVIIPLLSSVNVSDRGGRTALHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMG--------HLDVVALLINH 170
Cdd:PHA02795 205 KLCIPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRGsviarretHLKILEILLRE 284
|
....*.
gi 755492548 171 GAEVTC 176
Cdd:PHA02795 285 PLSIDC 290
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
398-426 |
3.07e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 36.03 E-value: 3.07e-03
10 20
....*....|....*....|....*....
gi 755492548 398 GRTCLHAAAAGGNVECIKLLQSSGADFHK 426
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| TRPV1-4 |
cd22193 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ... |
622-734 |
3.48e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411977 [Multi-domain] Cd Length: 607 Bit Score: 41.32 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 622 KDNVTKRTPLHASVIN---GHTLCLRLLLETAD---------NPEVVDVKdAKGQTPLMLAVAYGHIDAVSLLLEKEANV 689
Cdd:cd22193 24 TESSTGKTCLMKALLNlnpGTNDTIRILLDIAEktdnlkrfiNAEYTDEY-YEGQTALHIAIERRQGDIVALLVENGADV 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755492548 690 DAVD--------------IVGCTALHRGIMTGHEECVQMLLE---QEASILCKDSRGRTPLH 734
Cdd:cd22193 103 HAHAkgrffqpkyqgegfYFGELPLSLAACTNQPDIVQYLLEnehQPADIEAQDSRGNTVLH 164
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
662-691 |
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 755492548 662 KGQTPLMLAVAYGHIDAVSLLLEKEANVDA 691
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
151-176 |
5.38e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 35.26 E-value: 5.38e-03
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
266-321 |
5.79e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 36.17 E-value: 5.79e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 755492548 266 LLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVA 321
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
561-612 |
6.65e-03 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 40.27 E-value: 6.65e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 755492548 561 KSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEAL 612
Cdd:PTZ00322 116 RTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
|
|
| PHA02884 |
PHA02884 |
ankyrin repeat protein; Provisional |
30-170 |
6.70e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165212 [Multi-domain] Cd Length: 300 Bit Score: 39.97 E-value: 6.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 30 EIIELLILSGARVNAK----DNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQ-TPLHVAAANKAVKCAEVIIPL 104
Cdd:PHA02884 47 DIIDAILKLGADPEAPfplsENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLHGCLKCLEILLSY 126
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755492548 105 LSSVNVSDRGGRTALHHAALNGHMEMVNLLlaKGANINAFDKKDRRalhwaaYMGHLDVVALLINH 170
Cdd:PHA02884 127 GADINIQTNDMVTPIELALMICNNFLAFMI--CDNEISNFYKHPKK------ILINFDILKILVSH 184
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
884-942 |
6.85e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 35.79 E-value: 6.85e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 755492548 884 LVNSAQADLTVKDKDLNTPLHLAISKGHEKCALLILDKIQDeslINAKNSALQTPLHIA 942
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVD---LNLKDEEGLTALDLA 56
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
592-621 |
6.94e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 35.26 E-value: 6.94e-03
10 20 30
....*....|....*....|....*....|
gi 755492548 592 KGRTALYLAAFKGHTECVEALVNQGASIFV 621
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
831-863 |
7.34e-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: 7.34e-03
10 20 30
....*....|....*....|....*....|....
gi 755492548 831 KGRTTLHAAA-FGDHAECLQLLLRHDAQVNAVDN 863
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
|
|
| PHA02791 |
PHA02791 |
ankyrin-like protein; Provisional |
15-212 |
7.81e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165154 [Multi-domain] Cd Length: 284 Bit Score: 39.64 E-value: 7.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 15 EKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKhsadvnardKNWQTPLHvaaanka 94
Cdd:PHA02791 60 ENEFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGNMQTVKLFVK---------KNWRLMFY------- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 95 vkcaeviipllssvnvSDRGGRTALHHAALNGHMEMVNLLLAKGAniNAFDKKDRRA-LHWAAYMGHLDVVALLINHGAE 173
Cdd:PHA02791 124 ----------------GKTGWKTSFYHAVMLNDVSIVSYFLSEIP--STFDLAILLScIHITIKNGHVDMMILLLDYMTS 185
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 755492548 174 VTCKDKKGYTP-LHAAASNGQISVVKHLLNLGVEIDEINV 212
Cdd:PHA02791 186 TNTNNSLLFIPdIKLAIDNKDLEMLQALFKYDINIYSVNL 225
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| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
398-429 |
8.60e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 34.96 E-value: 8.60e-03
10 20 30
....*....|....*....|....*....|...
gi 755492548 398 GRTCLHAAAA-GGNVECIKLLQSSGADFHKKDK 429
Cdd:pfam00023 2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
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| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
51-80 |
8.94e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 34.96 E-value: 8.94e-03
10 20 30
....*....|....*....|....*....|.
gi 755492548 51 TPLHRAVASR-SEEAVQVLIKHSADVNARDK 80
Cdd:pfam00023 4 TPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
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| TRPV1-4 |
cd22193 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ... |
214-325 |
9.69e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411977 [Multi-domain] Cd Length: 607 Bit Score: 39.78 E-value: 9.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492548 214 GNTALHIACYNGQDAVVNELIDYGANVN--------QPNNS------GFTPLHFAAASTHGALCLELLVNNGADVNIQSK 279
Cdd:cd22193 76 GQTALHIAIERRQGDIVALLVENGADVHahakgrffQPKYQgegfyfGELPLSLAACTNQPDIVQYLLENEHQPADIEAQ 155
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755492548 280 D--GKSPLHMTAVHGRFTRSQT---------LIQNGGEI-------DCVDKDGNTPLHVAARHG 325
Cdd:cd22193 156 DsrGNTVLHALVTVADNTKENTkfvtrmydmILIRGAKLcptveleEIRNNDGLTPLQLAAKMG 219
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