|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
29-318 |
4.96e-50 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 178.61 E-value: 4.96e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 29 AEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSV 108
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 109 NVSDRGGRTALHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAA 188
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 189 ASNGQISVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHFAAASTHGALcLELLV 268
Cdd:COG0666 161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI-VKLLL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1907069410 269 NNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPL 318
Cdd:COG0666 240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
1-251 |
2.40e-47 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 170.91 E-value: 2.40e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 1 MLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDK 80
Cdd:COG0666 39 LLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDK 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 81 NWQTPLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGH 160
Cdd:COG0666 119 DGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGH 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 161 LDVVALLINHGAEVTCKDKKGYTPLHAAASNGQISVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANV 240
Cdd:COG0666 199 LEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278
|
250
....*....|.
gi 1907069410 241 NQPNNSGFTPL 251
Cdd:COG0666 279 AAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
2-282 |
2.47e-47 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 170.91 E-value: 2.47e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 2 LIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKN 81
Cdd:COG0666 7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 82 WQTPLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHL 161
Cdd:COG0666 87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 162 DVVALLINHGAEVTCKDKKGYTPLHAAASNGQISVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVN 241
Cdd:COG0666 167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1907069410 242 QPNNSGFTPLHFAAASTHGALCLELLVNNGADVNIQSKDGK 282
Cdd:COG0666 247 AKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
61-334 |
8.84e-40 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 154.03 E-value: 8.84e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 61 SEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSS---VNVSDRGGRTALHHAALNGH-MEMVNLLLA 136
Cdd:PHA03095 26 TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIVRLLLEAgadVNAPERCGFTPLHLYLYNATtLDVIKLLIK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 137 KGANINAFDKKDRRALHwaAYMG----HLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQISV--VKHLLNLGVEIDEI 210
Cdd:PHA03095 106 AGADVNAKDKVGRTPLH--VYLSgfniNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVYAV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 211 NVYGNTALHIACYNGQD--AVVNELIDYGANVNQPNNSGFTPLHFAAA-STHGALCLELLVNNGADVNIQSKDGKSPLHM 287
Cdd:PHA03095 184 DDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHSMATgSSCKRSLVLPLLIAGISINARNRYGQTPLHY 263
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1907069410 288 TAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARHGHELLINTLI 334
Cdd:PHA03095 264 AAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
129-450 |
2.97e-37 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 142.02 E-value: 2.97e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 129 EMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQISVVKHLLNLGVEID 208
Cdd:COG0666 2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 209 EINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHFAAASTHGALcLELLVNNGADVNIQskdgksplhmt 288
Cdd:COG0666 82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI-VKLLLEAGADVNAQ----------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 289 avhgrftrsqtliqnggeidcvDKDGNTPLHVAARHGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLLS 368
Cdd:COG0666 150 ----------------------DNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 369 SGFEIDTPDTFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIKALVTTGANVNETDDWGRT 448
Cdd:COG0666 208 AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
|
..
gi 1907069410 449 AL 450
Cdd:COG0666 288 LL 289
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
1-285 |
4.30e-37 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 145.94 E-value: 4.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 1 MLIHKTEDVNALDSEKRTPLHVaaFLG-----DAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAV-QVLIKHSAD 74
Cdd:PHA03095 32 RLLAAGADVNFRGEYGKTPLHL--YLHyssekVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDViKLLIKAGAD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 75 VNARDKNWQTPLHVAAANKAVkcaeviipllssvnvsdrggrtalhhaalngHMEMVNLLLAKGANINAFDKKDRRALHw 154
Cdd:PHA03095 110 VNAKDKVGRTPLHVYLSGFNI-------------------------------NPKVIRLLLRKGADVNALDLYGMTPLA- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 155 aAYMGH----LDVVALLINHGAEVTCKDKKGYTPLHAAASNGQIS--VVKHLLNLGVEIDEINVYGNTALHIACYNG--Q 226
Cdd:PHA03095 158 -VLLKSrnanVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATGSscK 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907069410 227 DAVVNELIDYGANVNQPNNSGFTPLHFAAASTHGALCLELLvNNGADVNIQSKDGKSPL 285
Cdd:PHA03095 237 RSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLI-ALGADINAVSSDGNTPL 294
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
30-276 |
4.31e-37 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 145.19 E-value: 4.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 30 EIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAV-----KCAEVIIPL 104
Cdd:PHA03100 16 KNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 105 LSSVNVSDRGGRTALHHAALN--GHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGH--LDVVALLINHGAEVTCKDKk 180
Cdd:PHA03100 96 GANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKNR- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 181 gytplhaaasngqisvVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHFAAASTHG 260
Cdd:PHA03100 175 ----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNK 238
|
250
....*....|....*.
gi 1907069410 261 ALcLELLVNNGADVNI 276
Cdd:PHA03100 239 EI-FKLLLNNGPSIKT 253
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
461-735 |
3.64e-36 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 138.55 E-value: 3.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 461 NKMILGNAHDNSEELERAREVKEKDAALCLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNTGFEESDGG 540
Cdd:COG0666 8 LLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 541 AlkSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQGASIFVKDNvTKRTPLHASVING 620
Cdd:COG0666 88 N--TLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN-DGNTPLHLAAANG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 621 HTLCLRLLLE-TADnpevVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIVGCTALHRGIMTGHEECVQMLLE 699
Cdd:COG0666 165 NLEIVKLLLEaGAD----VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
|
250 260 270
....*....|....*....|....*....|....*.
gi 1907069410 700 QEASILCKDSRGRTPLHYAAARGHATWLNELLQIAL 735
Cdd:COG0666 241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALL 276
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
3-241 |
1.16e-34 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 137.87 E-value: 1.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 3 IHKTEDVN-ALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLH-----RAVASRSEEAVQVLIKHSADVN 76
Cdd:PHA03100 21 IIMEDDLNdYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGANVN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 77 ARDKNWQTPLHVAAANKavKCAEVIIPLLSS----VNVSDRGGRTALHHAALNGH--MEMVNLLLAKGANINAfdkKDRr 150
Cdd:PHA03100 101 APDNNGITPLLYAISKK--SNSYSIVEYLLDnganVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINA---KNR- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 151 alhwaaymghldvVALLINHGAEVTCKDKKGYTPLHAAASNGQISVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVV 230
Cdd:PHA03100 175 -------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIF 241
|
250
....*....|.
gi 1907069410 231 NELIDYGANVN 241
Cdd:PHA03100 242 KLLLNNGPSIK 252
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
1-339 |
4.92e-34 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 139.81 E-value: 4.92e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 1 MLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDK 80
Cdd:PHA02876 163 MLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 81 NwqtpLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHM-EMVNLLLAKGANINAFDKKDRRALHWAAYMG 159
Cdd:PHA02876 243 S----LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAKNG 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 160 H-LDVVALLINHGAEVTCKDKKGYTPLHAAAS-NGQISVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYG 237
Cdd:PHA02876 319 YdTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYG 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 238 ANVNQPNNSGFTPLHFAAASTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHG-RFTRSQTLIQNGGEIDCVDKDGNT 316
Cdd:PHA02876 399 ADIEALSQKIGTALHFALCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQY 478
|
330 340
....*....|....*....|...
gi 1907069410 317 PLHVAArhGHELLINTLITSGAD 339
Cdd:PHA02876 479 PLLIAL--EYHGIVNILLHYGAE 499
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
593-917 |
1.07e-32 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 128.53 E-value: 1.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 593 ALVNQGASIFVKDNVTKRTPLHASVINGHTLCLRLLLETADNpevVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVD 672
Cdd:COG0666 5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLA---LALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 673 AVDIVGCTALHRGIMTGHEECVQMLLEQEASILCKDSRGRTPLHYAAARGHATWLNELLQialSEEDCCLKDNQGYTPLH 752
Cdd:COG0666 82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLE---AGADVNAQDNDGNTPLH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 753 WACYNGNENCIEVLLEqkcfrkfignpftplHCAIINGhescaslllgaidpsivscRDDKGRTTLHAAAFGDHAECLQL 832
Cdd:COG0666 159 LAAANGNLEIVKLLLE---------------AGADVNA-------------------RDNDGETPLHLAAENGHLEIVKL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 833 LLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNsAQADLTVKDKDLNTPLHLAISKGHEKCALLILDKIQDESLINA 912
Cdd:COG0666 205 LLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE-AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
|
....*
gi 1907069410 913 KNSAL 917
Cdd:COG0666 284 DLLTL 288
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
228-509 |
1.49e-32 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 128.15 E-value: 1.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 228 AVVNELIDYGANVNQPNNSGFTPLHFAAASTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEI 307
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 308 DCVDKDGNTPLHVAARHGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSGFEIDTPDTFGRTCLHAA 387
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 388 AAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIKALVTTGANVNETDDWGRTALHYAAASDMDRNKMILGN 467
Cdd:COG0666 161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1907069410 468 AHDNSEELERAREVKEKDAALCLEFLLQNDANPSIRDKEGYN 509
Cdd:COG0666 241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
31-360 |
2.09e-32 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 134.81 E-value: 2.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 31 IIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVNV 110
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINK 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 111 SDrggrTALHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLD-VVALLINHGAEVTCKDKKGYTPLHAAA 189
Cdd:PHA02876 240 ND----LSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMA 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 190 SNG-QISVVKHLLNLGVEIDEINVYGNTALHIACY--NGQDAVVNeLIDYGANVNQPNNSGFTPLHFAAAStHGALCLEL 266
Cdd:PHA02876 316 KNGyDTENIRTLIMLGADVNAADRLYITPLHQASTldRNKDIVIT-LLELGANVNARDYCDKTPIHYAAVR-NNVVIINT 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 267 LVNNGADVNIQSKDGKSPLHMtAVHGR--FTRSQTLIQNGGEIDCVDKDGNTPLHVAARHGHEL-LINTLITSGADTAKC 343
Cdd:PHA02876 394 LLDYGADIEALSQKIGTALHF-ALCGTnpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKLdVIEMLLDNGADVNAI 472
|
330
....*....|....*..
gi 1907069410 344 GIHSMFPLhLAALNAHS 360
Cdd:PHA02876 473 NIQNQYPL-LIALEYHG 488
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
541-770 |
8.21e-32 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 126.22 E-value: 8.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 541 ALKSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQGASIFVKDNvTKRTPLHASVING 620
Cdd:COG0666 20 LLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD-GGNTLLHAAARNG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 621 HTLCLRLLLETADNpevVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIVGCTALHRGIMTGHEECVQMLLEQ 700
Cdd:COG0666 99 DLEIVKLLLEAGAD---VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 701 EASILCKDSRGRTPLHYAAARGHATWLNELLQialSEEDCCLKDNQGYTPLHWACYNGNENCIEVLLEQK 770
Cdd:COG0666 176 GADVNARDNDGETPLHLAAENGHLEIVKLLLE---AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
27-342 |
1.44e-31 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 128.93 E-value: 1.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 27 GDAEIIELLILS-GARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVA---AANKAVKcaeviI 102
Cdd:PHA02874 12 GDIEAIEKIIKNkGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAikiGAHDIIK-----L 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 103 PLLSSVNVSdrggrtALHHAALNGhmEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGY 182
Cdd:PHA02874 87 LIDNGVDTS------ILPIPCIEK--DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 183 TPLHAAASNGQISVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHfaAASTHGAL 262
Cdd:PHA02874 159 YPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLH--NAIIHNRS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 263 CLELLVNNgADVNIQSKDGKSPLHMtAVHGRFTRS--QTLIQNGGEIDCVDKDGNTPLHVAARHGH------ELLINTLI 334
Cdd:PHA02874 237 AIELLINN-ASINDQDIDGSTPLHH-AINPPCDIDiiDILLYHKADISIKDNKGENPIDTAFKYINkdpvikDIIANAVL 314
|
....*...
gi 1907069410 335 TSGADTAK 342
Cdd:PHA02874 315 IKEADKLK 322
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
300-644 |
1.01e-30 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 122.76 E-value: 1.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 300 LIQNGGEIDCVDKDGNTPLHVAARHGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSGFEIDTPDTF 379
Cdd:COG0666 7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 380 GRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIKALVTTGANVNETDDWGRTALHYAAASdmd 459
Cdd:COG0666 87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN--- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 460 rnkmilgnahdNSEELerarevkekdaalcLEFLLQNDANPSIRDKEGYnsihyaaayghrqclelllertntgfeesdg 539
Cdd:COG0666 164 -----------GNLEI--------------VKLLLEAGADVNARDNDGE------------------------------- 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 540 galkSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQGASIFVKDNVTKRTPLHASVIN 619
Cdd:COG0666 188 ----TPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAG 263
|
330 340
....*....|....*....|....*
gi 1907069410 620 GHTLCLRLLLETADNPEVVDVKDAK 644
Cdd:COG0666 264 AALIVKLLLLALLLLAAALLDLLTL 288
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
625-950 |
1.29e-30 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 122.76 E-value: 1.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 625 LRLLLETADNPEVVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIVGCTALHRGIMTGHEECVQMLLEQEASI 704
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 705 LCKDSRGRTPLHYAAARGHATWLNELLQialSEEDCCLKDNQGYTPLHWACYNGNENCIEVLLEQkcfrkfignpftplh 784
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLE---AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA--------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 785 caiinghescaslllGAiDPSIvscRDDKGRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVD 864
Cdd:COG0666 143 ---------------GA-DVNA---QDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 865 ILVNsAQADLTVKDKDLNTPLHLAISKGHEKCALLILDKIQDeslINAKNSALQTPLHIAARNGLKVVVEELLAKGACVL 944
Cdd:COG0666 204 LLLE-AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD---LNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLA 279
|
....*.
gi 1907069410 945 AVDENA 950
Cdd:COG0666 280 AALLDL 285
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
449-715 |
4.00e-30 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 121.21 E-value: 4.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 449 ALHYAAASDMDRNKMILGNAHDNSEELERAREVKEKDAALCLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLE 528
Cdd:COG0666 29 ALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 529 R-TNTGFEESDGGalkSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQGASIFVKDNv 607
Cdd:COG0666 109 AgADVNARDKDGE---TPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 608 TKRTPLHASVINGHTLCLRLLLET-ADnpevVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIVGCTALHRGI 686
Cdd:COG0666 185 DGETPLHLAAENGHLEIVKLLLEAgAD----VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAA 260
|
250 260
....*....|....*....|....*....
gi 1907069410 687 MTGHEECVQMLLEQEASILCKDSRGRTPL 715
Cdd:COG0666 261 AAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
98-440 |
4.13e-30 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 127.49 E-value: 4.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 98 AEVIIPLLSSVNVSDRGGRTALHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCK 177
Cdd:PHA02876 161 AEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKN 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 178 DkkgyTPLHAAASNGQISVVKHLLNLGVEIDEINVYGNTALHIACYNGQ-DAVVNELIDYGANVNQPNNSGFTPLHFAAA 256
Cdd:PHA02876 241 D----LSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAK 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 257 STHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQ-TLIQNGGEIDCVDKDGNTPLHVAARHGHELLINTLIT 335
Cdd:PHA02876 317 NGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIViTLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLD 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 336 SGADtakcgihsmfplhLAALNAHSDccrkllssgfeidtpdtfgrTCLHAAAAGGN-VECIKLLQSSGADFHKKDKCGR 414
Cdd:PHA02876 397 YGAD-------------IEALSQKIG--------------------TALHFALCGTNpYMSVKTLIDRGANVNSKNKDLS 443
|
330 340
....*....|....*....|....*..
gi 1907069410 415 TPLHYAAA-NCHFHCIKALVTTGANVN 440
Cdd:PHA02876 444 TPLHYACKkNCKLDVIEMLLDNGADVN 470
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
187-450 |
7.21e-29 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 121.29 E-value: 7.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 187 AAASNGQISVVKHLLNLGVEIDEINVYGNTALH--IACYNGQDA-VVNELIDYGANVNQPNNSGFTPLHFAAASTHGALC 263
Cdd:PHA03095 20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHlyLHYSSEKVKdIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 264 LELLVNNGADVNIQSKDGKSPLH--MTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAAR-HGHEL-LINTLITSGAD 339
Cdd:PHA03095 100 IKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKsRNANVeLLRLLIDAGAD 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 340 TAKCGIHSMFPLHLAALNAHSD--CCRKLLSSGFEIDTPDTFGRTCLHAAAAGGNVECIKLLQ--SSGADFHKKDKCGRT 415
Cdd:PHA03095 180 VYAVDDRFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVLPllIAGISINARNRYGQT 259
|
250 260 270
....*....|....*....|....*....|....*....
gi 1907069410 416 PLHYAAA--NCHF--HCIKAlvttGANVNETDDWGRTAL 450
Cdd:PHA03095 260 PLHYAAVfnNPRAcrRLIAL----GADINAVSSDGNTPL 294
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
167-440 |
1.20e-27 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 117.07 E-value: 1.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 167 LINHGAEVTCKDKKGYTPLHAAASNGQISVVKHLLNLGVEIDEINVYGNTALHIAC---YNGQDAV--VNELIDYGANVN 241
Cdd:PHA03100 21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSnikYNLTDVKeiVKLLLEYGANVN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 242 QPNNSGFTPLHFAAASTHGALCL-ELLVNNGADVNIQSKDGKSPLHMtavhgrFTRSqtliqnggeiDCVDKDgntplhv 320
Cdd:PHA03100 101 APDNNGITPLLYAISKKSNSYSIvEYLLDNGANVNIKNSDGENLLHL------YLES----------NKIDLK------- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 321 aarhghelLINTLITSGAD-TAKCGIHSmfplhlaalnahsdccrkLLSSGFEIDTPDTFGRTCLHAAAAGGNVECIKLL 399
Cdd:PHA03100 158 --------ILKLLIDKGVDiNAKNRVNY------------------LLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYL 211
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1907069410 400 QSSGADFHKKDKCGRTPLHYAAANCHFHCIKALVTTGANVN 440
Cdd:PHA03100 212 LDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
50-321 |
3.66e-26 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 113.44 E-value: 3.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 50 LTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVA--AANKavkcaEVIIPLLSSVNVSDRG-GRTALHHAALNG 126
Cdd:PHA02878 38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIIckEPNK-----LGMKEMIRSINKCSVFyTLVAIKDAFNNR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 127 HMEMVNLLLakganINAFDKK---DRRALHWAAYMGHLD--VVALLINHGAEVTCKDK-KGYTPLHAAASNGQISVVKHL 200
Cdd:PHA02878 113 NVEIFKIIL-----TNRYKNIqtiDLVYIDKKSKDDIIEaeITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 201 LNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHFAAASTHGALCLELLVNNGADVNIQSK- 279
Cdd:PHA02878 188 LSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDYDILKLLLEHGVDVNAKSYi 267
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1907069410 280 DGKSPLHMTAVHGRFTRsqTLIQNGGEIDCVDKDGNTPLHVA 321
Cdd:PHA02878 268 LGLTALHSSIKSERKLK--LLLEYGADINSLNSYKLTPLSSA 307
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
330-639 |
5.24e-23 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 103.57 E-value: 5.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 330 INTLITSGADTAKCGIHSMFPLHLAALNAHSDC---CRKLLSSGFEIDTPDTFGRTCLHAAAAGGNVE-CIKLLQSSGAD 405
Cdd:PHA03095 30 VRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAGAD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 406 FHKKDKCGRTPLH-YAA-ANCHFHCIKALVTTGANVNETDDWGRTALHyaaasdmdrnkmILGNAHDNSEELerarevke 483
Cdd:PHA03095 110 VNAKDKVGRTPLHvYLSgFNINPKVIRLLLRKGADVNALDLYGMTPLA------------VLLKSRNANVEL-------- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 484 kdaalcLEFLLQNDANPSIRDKEGYNSIHYAAAYGH--RQCLELLLERTNTGFEESDGGalKSPLHLAAYNGHHQALEV- 560
Cdd:PHA03095 170 ------LRLLIDAGADVYAVDDRFRSLLHHHLQSFKprARIVRELIRAGCDPAATDMLG--NTPLHSMATGSSCKRSLVl 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 561 -LLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQGASIFVKDNvTKRTPLHASVINGHTLCLRLLLETADNPEVVD 639
Cdd:PHA03095 242 pLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSS-DGNTPLSLMVRNNNGRAVRAALAKNPSAETVA 320
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
4-270 |
1.51e-22 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 102.27 E-value: 1.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 4 HKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIK------------- 70
Cdd:PHA02878 25 HTENYSTSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRsinkcsvfytlva 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 71 -----HSADVNA-------RDKNWQTP--LHVAAANKAVKCAEVIIPLL----SSVNVSDR-GGRTALHHAALNGHMEMV 131
Cdd:PHA02878 105 ikdafNNRNVEIfkiiltnRYKNIQTIdlVYIDKKSKDDIIEAEITKLLlsygADINMKDRhKGNTALHYATENKDQRLT 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 132 NLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASN-GQISVVKHLLNLGVEID-E 209
Cdd:PHA02878 185 ELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNaK 264
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907069410 210 INVYGNTALHIACYNGQdaVVNELIDYGANVNQPNNSGFTPLHFAAASTHGALCLELLVNN 270
Cdd:PHA02878 265 SYILGLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPLSSAVKQYLCINIGRILISN 323
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
265-582 |
1.74e-22 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 101.58 E-value: 1.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 265 ELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARHGHELLINTLITSGADTakcg 344
Cdd:PHA02874 19 KIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDT---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 345 ihSMFPLHlaalNAHSDCCRKLLSSGFEIDTPDTFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANC 424
Cdd:PHA02874 95 --SILPIP----CIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHN 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 425 HFHCIKALVTTGANVNETDDWGRTALHYAaasdmdrnkmilgnahdnseelerareVKEKDAAlCLEFLLQNDANPSIRD 504
Cdd:PHA02874 169 FFDIIKLLLEKGAYANVKDNNGESPLHNA---------------------------AEYGDYA-CIKLLIDHGNHIMNKC 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907069410 505 KEGYNSIHYAAAYgHRQCLELLLERTNTGFEESDGgalKSPLHLA-AYNGHHQALEVLLQSLVDLDIRDEKGRTALYLA 582
Cdd:PHA02874 221 KNGFTPLHNAIIH-NRSAIELLINNASINDQDIDG---STPLHHAiNPPCDIDIIDILLYHKADISIKDNKGENPIDTA 295
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
8-211 |
9.94e-22 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 99.27 E-value: 9.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 8 DVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLH 87
Cdd:PHA02874 116 DVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLH 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 88 VAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALngHMEMVNLLLAKGANINAFDKKDRRALHWA-AYMGHLDVVAL 166
Cdd:PHA02874 196 NAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAiNPPCDIDIIDI 273
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1907069410 167 LINHGAEVTCKDKKGYTPLHAAASN-GQISVVKHLLNLGVEIDEIN 211
Cdd:PHA02874 274 LLYHKADISIKDNKGENPIDTAFKYiNKDPVIKDIIANAVLIKEAD 319
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
193-470 |
1.17e-21 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 100.91 E-value: 1.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 193 QISVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHFAAAS----THGALC----- 263
Cdd:PHA02876 157 ELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSknidTIKAIIdnrsn 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 264 ----------------LE---LLVNNGADVNIQSKDGKSPLHMTAVHGRFTR-SQTLIQNGGEIDCVDKDGNTPLHVAAR 323
Cdd:PHA02876 237 inkndlsllkairnedLEtslLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRlVPKLLERGADVNAKNIKGETPLYLMAK 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 324 HGHELL-INTLITSGADTAKCGIHSMFPLHLAA-LNAHSDCCRKLLSSGFEIDTPDTFGRTCLHAAAAGGNVECIKLLQS 401
Cdd:PHA02876 317 NGYDTEnIRTLIMLGADVNAADRLYITPLHQAStLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLD 396
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907069410 402 SGADFHKKDKCGRTPLHYAAANCH-FHCIKALVTTGANVNETDDWGRTALHYAAASD--MDRNKMILGNAHD 470
Cdd:PHA02876 397 YGADIEALSQKIGTALHFALCGTNpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNckLDVIEMLLDNGAD 468
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
626-941 |
7.82e-21 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 97.02 E-value: 7.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 626 RLLLETADnpevVDVKDAKGQTPLMLAVAYGH---IDAVSLLLEKEANVDAVDIVGCTALHRGIMTGHEE-CVQMLLEQE 701
Cdd:PHA03095 32 RLLAAGAD----VNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 702 ASILCKDSRGRTPLH-YAA-ARGHATWLNELLQIALseeDCCLKDNQGYTPLHwaCYNGNENC----IEVLLEQKCF--- 772
Cdd:PHA03095 108 ADVNAKDKVGRTPLHvYLSgFNINPKVIRLLLRKGA---DVNALDLYGMTPLA--VLLKSRNAnvelLRLLIDAGADvya 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 773 RKFIGNpfTPLH--CAIINGHESCASLLLGA-IDPsivSCRDDKGRTTLHAAAFGDHAECLQL--LLRHDAQVNAVDNSG 847
Cdd:PHA03095 183 VDDRFR--SLLHhhLQSFKPRARIVRELIRAgCDP---AATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 848 KTALMMAAENGQAGAVDILVNsAQADLTVKDKDLNTPLHLAISKGHEKCALLILDKIQDESLINAKNSALQTPLHIAARN 927
Cdd:PHA03095 258 QTPLHYAAVFNNPRACRRLIA-LGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAATLNTASVAGGDIPSD 336
|
330
....*....|....
gi 1907069410 928 GLKVVVEELLAKGA 941
Cdd:PHA03095 337 ATRLCVAKVVLRGA 350
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
152-244 |
9.86e-21 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 87.48 E-value: 9.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 152 LHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQISVVKHLLNlGVEIDEINvYGNTALHIACYNGQDAVVN 231
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1907069410 232 ELIDYGANVNQPN 244
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
23-241 |
2.25e-20 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 94.67 E-value: 2.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 23 AAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVII 102
Cdd:PHA02875 9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 103 PLLSSVN-VSDRGGRTALHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKG 181
Cdd:PHA02875 89 DLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCG 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907069410 182 YTPLHAAASNGQISVVKHLLNLGVEIDEINVYGN-TALHIACYNGQDAVVNELIDYGANVN 241
Cdd:PHA02875 169 CTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADCN 229
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
1-210 |
2.33e-20 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 95.48 E-value: 2.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 1 MLIHKTEDVNALDSEKRTPLHV--AAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASR--SEEAVQVLIKHSADVN 76
Cdd:PHA03095 102 LLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRnaNVELLRLLIDAGADVY 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 77 ARDKNWQTPLHVAAAN--KAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHMEMVNL--LLAKGANINAFDKKDRRAL 152
Cdd:PHA03095 182 AVDDRFRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPL 261
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907069410 153 HWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQISVVKHLLNLGVEIDEI 210
Cdd:PHA03095 262 HYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETV 319
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
119-211 |
3.43e-20 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 85.94 E-value: 3.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 119 LHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHgAEVTCKDkKGYTPLHAAASNGQISVVK 198
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1907069410 199 HLLNLGVEIDEIN 211
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
191-520 |
3.76e-20 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 94.26 E-value: 3.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 191 NGQISVVKHLLN-----LGVEIDEINvygnTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLhFAAASTHGALCLE 265
Cdd:PHA02874 11 SGDIEAIEKIIKnkgncINISVDETT----TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPL-LTAIKIGAHDIIK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 266 LLVNNGADVNIqskdgkspLHMTAVHGRFTRsqTLIQNGGEIDCVDKDGNTPLHVAARHGHELLINTLITSGADTAKCGI 345
Cdd:PHA02874 86 LLIDNGVDTSI--------LPIPCIEKDMIK--TILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 346 HSMFPLHLAALNAHSDCCRKLLSSGFEIDTPDTFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAanCH 425
Cdd:PHA02874 156 NGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI--IH 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 426 FHCIKALVTTGANVNETDDWGRTALHYAAASDMDRNkmilgnahdnseelerarevkekdaalCLEFLLQNDANPSIRDK 505
Cdd:PHA02874 234 NRSAIELLINNASINDQDIDGSTPLHHAINPPCDID---------------------------IIDILLYHKADISIKDN 286
|
330
....*....|....*
gi 1907069410 506 EGYNSIHYAAAYGHR 520
Cdd:PHA02874 287 KGENPIDTAFKYINK 301
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
364-639 |
4.31e-19 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 90.88 E-value: 4.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 364 RKLLSSGFEIDTPDTFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCH-----FHCIKALVTTGAN 438
Cdd:PHA03100 19 KYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGAN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 439 VNETDDWGRTALHYAAASDMDRNKMIlgnahdnseelerarevkekdaalclEFLLQNDANPSIRDKEGYNSIHYAAAYG 518
Cdd:PHA03100 99 VNAPDNNGITPLLYAISKKSNSYSIV--------------------------EYLLDNGANVNIKNSDGENLLHLYLESN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 519 HR--QCLELLLERTNtgfeesdggalksplHLAAYNghhqALEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVN 596
Cdd:PHA03100 153 KIdlKILKLLIDKGV---------------DINAKN----RVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLD 213
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1907069410 597 QGASIFVKDNVTKrTPLHASVINGHTLCLRLLLETADNPEVVD 639
Cdd:PHA03100 214 LGANPNLVNKYGD-TPLHIAILNNNKEIFKLLLNNGPSIKTII 255
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
86-178 |
6.99e-19 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 82.09 E-value: 6.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 86 LHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHMEMVNLLLAKgANINAFDkKDRRALHWAAYMGHLDVVA 165
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1907069410 166 LLINHGAEVTCKD 178
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
579-675 |
1.94e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 80.93 E-value: 1.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 579 LYLAAFKGHTECVEALVNQGASIFVKDNvTKRTPLHASVINGHTLCLRLLLETADnpevVDVKDaKGQTPLMLAVAYGHI 658
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDK-NGRTALHLAAKNGHLEIVKLLLEHAD----VNLKD-NGRTALHYAARSGHL 74
|
90
....*....|....*..
gi 1907069410 659 DAVSLLLEKEANVDAVD 675
Cdd:pfam12796 75 EIVKLLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
351-443 |
2.12e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 80.93 E-value: 2.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 351 LHLAALNAHSDCCRKLLSSGFEIDTPDTFGRTCLHAAAAGGNVECIKLLqSSGADFHKKDKcGRTPLHYAAANCHFHCIK 430
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL-LEHADVNLKDN-GRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1907069410 431 ALVTTGANVNETD 443
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
185-277 |
2.53e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 80.55 E-value: 2.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 185 LHAAASNGQISVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYgANVNQPNNsGFTPLHFAAASTHGAlCL 264
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLE-IV 77
|
90
....*....|...
gi 1907069410 265 ELLVNNGADVNIQ 277
Cdd:pfam12796 78 KLLLEKGADINVK 90
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
546-639 |
7.97e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 79.39 E-value: 7.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 546 LHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQgasIFVKDNVTKRTPLHASVINGHTLCL 625
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLEIV 77
|
90
....*....|....
gi 1907069410 626 RLLLETADNPEVVD 639
Cdd:pfam12796 78 KLLLEKGADINVKD 91
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
17-173 |
1.81e-17 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 85.81 E-value: 1.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 17 RTPLHVAAFLGDAEIIELLILSGARVN---AKDNMwlTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANK 93
Cdd:PHA02875 69 ESELHDAVEEGDVKAVEELLDLGKFADdvfYKDGM--TPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMG 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 94 AVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHMEMVNLLLAKGANINAFDKK-DRRALHWAAYMGHLDVVALLINHGA 172
Cdd:PHA02875 147 DIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNgCVAALCYAIENNKIDIVRLFIKRGA 226
|
.
gi 1907069410 173 E 173
Cdd:PHA02875 227 D 227
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
546-821 |
2.10e-17 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 85.79 E-value: 2.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 546 LHLAAYNGHHQALEVLLQSLVD-LDIRDEKGRTALYLAAFKGHTECVEALVNQGASIfvkDNVTKRTP---LHASVINGH 621
Cdd:PHA02874 5 LRMCIYSGDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADI---NHINTKIPhplLTAIKIGAH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 622 TLCLRLLLETADN-----PEV--------------VDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIVGCTAL 682
Cdd:PHA02874 82 DIIKLLIDNGVDTsilpiPCIekdmiktildcgidVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 683 HRGIMTGHEECVQMLLEQEASILCKDSRGRTPLHYAAARGHATWLNELLQialSEEDCCLKDNQGYTPLHWACYNgNENC 762
Cdd:PHA02874 162 HIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLID---HGNHIMNKCKNGFTPLHNAIIH-NRSA 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907069410 763 IEVLLEQKCFRKFIGNPFTPLHCAIingHESCA-----SLLLGAIDPSIvscRDDKGRTTLHAA 821
Cdd:PHA02874 238 IELLINNASINDQDIDGSTPLHHAI---NPPCDidiidILLYHKADISI---KDNKGENPIDTA 295
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
157-671 |
2.23e-17 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 87.04 E-value: 2.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 157 YMGHLDVVALLIN-----HGAEvTCKDKK-GYTPLHAAASNGQISVVKHLLNLGVEIDEINVYG-NTALHIACY--NGQD 227
Cdd:PHA02876 12 RGNCIDILSAIDNydlhkHGAN-QCENESiPFTAIHQALQLRQIDIVEEIIQQNPELIYITDHKcHSTLHTICIipNVMD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 228 AVVNELIDYGANVNQPNNSGFTPLHfaaasTHGALCLELLVN--NGADVNIqSKDGKSPLHMTAVHGRFTR-----SQTL 300
Cdd:PHA02876 91 IVISLTLDCDIILDIKYASIILNKH-----KLDEACIHILKEaiSGNDIHY-DKINESIEYMKLIKERIQQdelliAEML 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 301 IQNGGEIDCVDKDGNTPLHVAARHGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRK--------------- 365
Cdd:PHA02876 165 LEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAiidnrsninkndlsl 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 366 --------------LLSSGFEIDTPDTFGRTCLHAAAAGGNVECI--KLLQsSGADFHKKDKCGRTPLHYAAANCH-FHC 428
Cdd:PHA02876 245 lkairnedletsllLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLvpKLLE-RGADVNAKNIKGETPLYLMAKNGYdTEN 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 429 IKALVTTGANVNETDDWGRTALHyaAASDMDRNKMILGNahdnseelerarevkekdaalclefLLQNDANPSIRDKEGY 508
Cdd:PHA02876 324 IRTLIMLGADVNAADRLYITPLH--QASTLDRNKDIVIT-------------------------LLELGANVNARDYCDK 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 509 NSIHYAAAYGHRQCLELLLertntgfeesDGGAlksplhlaaynghhqalevllqslvDLDIRDEKGRTALYLAAFKGHT 588
Cdd:PHA02876 377 TPIHYAAVRNNVVIINTLL----------DYGA-------------------------DIEALSQKIGTALHFALCGTNP 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 589 -ECVEALVNQGASIFVKdNVTKRTPLHASVINGHTL-CLRLLLetaDNPEVVDVKDAKGQTPLMLAVAYGHIdaVSLLLE 666
Cdd:PHA02876 422 yMSVKTLIDRGANVNSK-NKDLSTPLHYACKKNCKLdVIEMLL---DNGADVNAINIQNQYPLLIALEYHGI--VNILLH 495
|
....*
gi 1907069410 667 KEANV 671
Cdd:PHA02876 496 YGAEL 500
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
20-145 |
5.81e-17 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 76.69 E-value: 5.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 20 LHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHsADVNARDKnwqtplhvaaankavkcae 99
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN------------------- 60
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1907069410 100 viipllssvnvsdrgGRTALHHAALNGHMEMVNLLLAKGANINAFD 145
Cdd:pfam12796 61 ---------------GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
208-525 |
6.31e-17 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 84.93 E-value: 6.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 208 DEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHFAAASTHGALCLELL-VNNGADVNIQSKDGKSPLH 286
Cdd:PHA02878 31 TSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIrSINKCSVFYTLVAIKDAFN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 287 MTAVH-------GRFTRSQTLiqNGGEIDCVDKDGNTPLHVaarhghellINTLITSGADTAKCGIHSM-FPLHLAALNA 358
Cdd:PHA02878 111 NRNVEifkiiltNRYKNIQTI--DLVYIDKKSKDDIIEAEI---------TKLLLSYGADINMKDRHKGnTALHYATENK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 359 HSDCCRKLLSSGFEIDTPDTFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANC-HFHCIKALVTTGA 437
Cdd:PHA02878 180 DQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCkDYDILKLLLEHGV 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 438 NVN-ETDDWGRTALHYAAASDmDRNKMILG-----NAHDNSEELERAREVKEKDAALCLEFL-----LQNDANPSIRDKE 506
Cdd:PHA02878 260 DVNaKSYILGLTALHSSIKSE-RKLKLLLEygadiNSLNSYKLTPLSSAVKQYLCINIGRILisnicLLKRIKPDIKNSE 338
|
330
....*....|....*....
gi 1907069410 507 GYnSIHYAAAYGHRQCLEL 525
Cdd:PHA02878 339 GF-IDNMDCITSNKRLNQI 356
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
490-702 |
1.21e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 83.50 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 490 LEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLerTNTGFEESDGGALKSPLHLAAYNGHHQALEVLLQS--LVD 567
Cdd:PHA02875 18 ARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLM--KHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLgkFAD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 568 lDIRDEKGRTALYLAAFKGHTECVEALVNQGASIFVKdNVTKRTPLHASVINGHTLCLRLLLetaDNPEVVDVKDAKGQT 647
Cdd:PHA02875 96 -DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIP-NTDKFSPLHLAVMMGDIKGIELLI---DHKACLDIEDCCGCT 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907069410 648 PLMLAVAYGHIDAVSLLLEKEANVDAVDIVGC-TALHRGIMTGHEECVQMLLEQEA 702
Cdd:PHA02875 171 PLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGA 226
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
818-914 |
1.30e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 75.92 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 818 LHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNSAQADLTVKDKdlnTPLHLAISKGHEKCA 897
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR---TALHYAARSGHLEIV 77
|
90
....*....|....*..
gi 1907069410 898 LLILDKIQDeslINAKN 914
Cdd:pfam12796 78 KLLLEKGAD---INVKD 91
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
49-256 |
2.19e-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: 2.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 49 WLTPLHRAVASRSEEAVQVLIK-HSADVNARDKNWQTPLHVAAANKAVKCAEVII---PLLssVNV---SD-RGGRTALH 120
Cdd:cd22192 17 SESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMeaaPEL--VNEpmtSDlYQGETALH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 121 HAALNGHMEMVNLLLAKGANIN------AFDKKDRRAL-----H---WAAYMGHLDVVALLINHGAEVTCKDKKGYTPLH 186
Cdd:cd22192 95 IAVVNQNLNLVRELIARGADVVspratgTFFRPGPKNLiyygeHplsFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907069410 187 AAASNGQISVVKH----LLNLGVEIDEINVYgntalHIacyngqdavvnelidyganvnqPNNSGFTPLHFAAA 256
Cdd:cd22192 175 ILVLQPNKTFACQmydlILSYDKEDDLQPLD-----LV----------------------PNNQGLTPFKLAAK 221
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
116-348 |
3.27e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 81.96 E-value: 3.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 116 RTALHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQIS 195
Cdd:PHA02875 3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 196 VVKHLLNLGVEIDEInVY--GNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHFAAASTHGALcLELLVNNGAD 273
Cdd:PHA02875 83 AVEELLDLGKFADDV-FYkdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKG-IELLIDHKAC 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907069410 274 VNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARHGHEL-LINTLITSGADtakCGIHSM 348
Cdd:PHA02875 161 LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIdIVRLFIKRGAD---CNIMFM 233
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
53-339 |
5.45e-16 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 81.80 E-value: 5.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 53 LHRAvaSRSEEAVQVLIKHSADVNARDKNWQTPLhvaaankavkCAeviipLLSsvNVSDrggrtalhhaaLNGHMEMVN 132
Cdd:PHA02798 44 LQRD--SPSTDIVKLFINLGANVNGLDNEYSTPL----------CT-----ILS--NIKD-----------YKHMLDIVK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 133 LLLAKGANINAFDKKDRRALHWA---AYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNG---QISVVKHLLNLGVE 206
Cdd:PHA02798 94 ILIENGADINKKNSDGETPLYCLlsnGYINNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNhhiDIEIIKLLLEKGVD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 207 IDEI-NVYGNTALHiaCY-----NGQDA-VVNELIDYGANVNQPNNSgftplhfaAASTHGALCLELLVNNG-------- 271
Cdd:PHA02798 174 INTHnNKEKYDTLH--CYfkyniDRIDAdILKLFVDNGFIINKENKS--------HKKKFMEYLNSLLYDNKrfkknild 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907069410 272 ---ADVNIQSKD--GKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARHGHELLINTLITSGAD 339
Cdd:PHA02798 244 fifSYIDINQVDelGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKPN 316
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
682-771 |
9.68e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 73.23 E-value: 9.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 682 LHRGIMTGHEECVQMLLEQEASILCKDSRGRTPLHYAAARGHAtwlnELLQIALSEEDCCLKDNqGYTPLHWACYNGNEN 761
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHL----EIVKLLLEHADVNLKDN-GRTALHYAARSGHLE 75
|
90
....*....|
gi 1907069410 762 CIEVLLEQKC 771
Cdd:pfam12796 76 IVKLLLEKGA 85
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
366-718 |
9.98e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 81.65 E-value: 9.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 366 LLSSGFEIDTPDTFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIKALVTTGANVNetddw 445
Cdd:PHA02876 164 LLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNIN----- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 446 grtalhyaaasdmdRNKMILGNAHDNsEELERArevkekdaalclefLLQNDANPSIRDKEGYNSihyaaayghrqclel 525
Cdd:PHA02876 239 --------------KNDLSLLKAIRN-EDLETS--------------LLLYDAGFSVNSIDDCKN--------------- 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 526 llertntgfeesdggalkSPLHLAAYNGHHQAL-EVLLQSLVDLDIRDEKGRTALYLAAFKGH-TECVEALVNQGASIFV 603
Cdd:PHA02876 275 ------------------TPLHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNA 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 604 KDNVTKrTPLH-ASVINGHTLCLRLLLETADNpevVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIVGCTAL 682
Cdd:PHA02876 337 ADRLYI-TPLHqASTLDRNKDIVITLLELGAN---VNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTAL 412
|
330 340 350
....*....|....*....|....*....|....*..
gi 1907069410 683 HRGIM-TGHEECVQMLLEQEASILCKDSRGRTPLHYA 718
Cdd:PHA02876 413 HFALCgTNPYMSVKTLIDRGANVNSKNKDLSTPLHYA 449
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
511-605 |
1.17e-15 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 73.23 E-value: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 511 IHYAAAYGHRQCLELLLE-RTNTGFEESDGgalKSPLHLAAYNGHHQALEVLLQSlVDLDIRDEkGRTALYLAAFKGHTE 589
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLEnGADANLQDKNG---RTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLE 75
|
90
....*....|....*.
gi 1907069410 590 CVEALVNQGASIFVKD 605
Cdd:pfam12796 76 IVKLLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
384-457 |
1.36e-15 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 72.84 E-value: 1.36e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907069410 384 LHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIKALVTTgANVNETDDwGRTALHYAAASD 457
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSG 72
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
524-706 |
1.44e-15 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 81.45 E-value: 1.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 524 ELLLERTntgfEESDGGALKSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQGASIFV 603
Cdd:PLN03192 511 DLLGDNG----GEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHI 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 604 KDnVTKRTPLHASVINGHTLCLRLL--LETADNPEVvdvkdakGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIVGCTA 681
Cdd:PLN03192 587 RD-ANGNTALWNAISAKHHKIFRILyhFASISDPHA-------AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATA 658
|
170 180
....*....|....*....|....*
gi 1907069410 682 LHRGIMTGHEECVQMLLEQEASILC 706
Cdd:PLN03192 659 LQVAMAEDHVDMVRLLIMNGADVDK 683
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
751-844 |
1.93e-15 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 72.46 E-value: 1.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 751 LHWACYNGNENCIEVLLEQKC-FRKFIGNPFTPLHCAIINGHESCASLLLGAIDPSIvscrDDKGRTTLHAAAFGDHAEC 829
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGAdANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL----KDNGRTALHYAARSGHLEI 76
|
90
....*....|....*
gi 1907069410 830 LQLLLRHDAQVNAVD 844
Cdd:pfam12796 77 VKLLLEKGADINVKD 91
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
229-440 |
2.14e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 79.65 E-value: 2.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 229 VVNELIDYGANVNQPNNSGFTPLHFAAaSTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEI- 307
Cdd:PHA02875 17 IARRLLDIGINPNFEIYDGISPIKLAM-KFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAd 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 308 DCVDKDGNTPLHVAARHGHELLINTLITSGADTakcgihsmfplhlaalnahsdccrkllssgfeiDTPDTFGRTCLHAA 387
Cdd:PHA02875 96 DVFYKDGMTPLHLATILKKLDIMKLLIARGADP---------------------------------DIPNTDKFSPLHLA 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907069410 388 AAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIKALVTTGANVN 440
Cdd:PHA02875 143 VMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANID 195
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
472-883 |
5.72e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 79.34 E-value: 5.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 472 SEELERAREVKEK---DAALCLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLER-TNTGFEESDGgalkspLH 547
Cdd:PHA02876 140 NESIEYMKLIKERiqqDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYgADVNIIALDD------LS 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 548 LAAYNGHHQALEVLlQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQGASIFVKDnVTKRTPLHASVINGH--TLCL 625
Cdd:PHA02876 214 VLECAVDSKNIDTI-KAIIDNRSNINKNDLSLLKAIRNEDLETSLLLYDAGFSVNSID-DCKNTPLHHASQAPSlsRLVP 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 626 RLLLETADnpevVDVKDAKGQTPLMLAVAYGH-IDAVSLLLEKEANVDAVDIVGCTALHRG-IMTGHEECVQMLLEQEAS 703
Cdd:PHA02876 292 KLLERGAD----VNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQAsTLDRNKDIVITLLELGAN 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 704 ILCKDSRGRTPLHYAAARGHATWLNELLQIALSEEdcCLKDNQGyTPLHWACYNgnencievlleqkcfrkfiGNPFTPL 783
Cdd:PHA02876 368 VNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIE--ALSQKIG-TALHFALCG-------------------TNPYMSV 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 784 HCAIINGHEscaslllgaidpsiVSCRDDKGRTTLHAAAFGD-HAECLQLLLRHDAQVNAVDNSGKTALMMAAenGQAGA 862
Cdd:PHA02876 426 KTLIDRGAN--------------VNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGI 489
|
410 420
....*....|....*....|...
gi 1907069410 863 VDILVNSAQA--DLTVKDKDLNT 883
Cdd:PHA02876 490 VNILLHYGAElrDSRVLHKSLND 512
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
1-145 |
1.05e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 78.00 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 1 MLIHKTEDVNALDSEK-RTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARD 79
Cdd:PHA02878 152 LLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARD 231
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907069410 80 KNWQTPLHVAAAnkAVKCAEVIIPLL---SSVNV-SDRGGRTALHHAAlngHMEMV-NLLLAKGANINAFD 145
Cdd:PHA02878 232 KCGNTPLHISVG--YCKDYDILKLLLehgVDVNAkSYILGLTALHSSI---KSERKlKLLLEYGADINSLN 297
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
542-718 |
1.63e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 76.93 E-value: 1.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 542 LKSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQGASIFVKDNVTKrTPLHASVINGH 621
Cdd:PHA02874 124 LKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGE-SPLHNAAEYGD 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 622 TLCLRLLLETADNpevVDVKDAKGQTPLMLAVAYGHiDAVSLLLeKEANVDAVDIVGCTALHRGIMTG-HEECVQMLLEQ 700
Cdd:PHA02874 203 YACIKLLIDHGNH---IMNKCKNGFTPLHNAIIHNR-SAIELLI-NNASINDQDIDGSTPLHHAINPPcDIDIIDILLYH 277
|
170
....*....|....*...
gi 1907069410 701 EASILCKDSRGRTPLHYA 718
Cdd:PHA02874 278 KADISIKDNKGENPIDTA 295
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
649-723 |
1.98e-14 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 69.76 E-value: 1.98e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907069410 649 LMLAVAYGHIDAVSLLLEKEANVDAVDIVGCTALHRGIMTGHEECVQMLLEQEAsiLCKDSRGRTPLHYAAARGH 723
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGH 73
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
592-947 |
4.02e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 76.64 E-value: 4.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 592 EALVNQGASIFVKDnVTKRTPLHASVINGHTLCLRLLLETADNPEVVDVKDAkgqTPLMLAVAYGHIDAVSLLLEKEANV 671
Cdd:PHA02876 162 EMLLEGGADVNAKD-IYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDL---SVLECAVDSKNIDTIKAIIDNRSNI 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 672 DAVDIvgctALHRGIMTGHEECVQMLLEQEASILCKDSRGRTPLHYAAargHATWLNELLQIALSE-EDCCLKDNQGYTP 750
Cdd:PHA02876 238 NKNDL----SLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHAS---QAPSLSRLVPKLLERgADVNAKNIKGETP 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 751 LHWACYNGNENcievlleqkcfrkfignpftplhcaiinghESCASLLLGAIDpsiVSCRDDKGRTTLHAAAFGD-HAEC 829
Cdd:PHA02876 311 LYLMAKNGYDT------------------------------ENIRTLIMLGAD---VNAADRLYITPLHQASTLDrNKDI 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 830 LQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNSAqADLTVKDKDLNTPLHLAISKGHEKCALLILdkIQDESL 909
Cdd:PHA02876 358 VITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYG-ADIEALSQKIGTALHFALCGTNPYMSVKTL--IDRGAN 434
|
330 340 350
....*....|....*....|....*....|....*....
gi 1907069410 910 INAKNSALQTPLHIAARNGLKV-VVEELLAKGACVLAVD 947
Cdd:PHA02876 435 VNSKNKDLSTPLHYACKKNCKLdVIEMLLDNGADVNAIN 473
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
715-799 |
4.28e-14 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 68.60 E-value: 4.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 715 LHYAAARGHATWLNELLQialSEEDCCLKDNQGYTPLHWACYNGNENCIEVLLEQKCFRKFiGNPFTPLHCAIINGHESC 794
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLE---NGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLK-DNGRTALHYAARSGHLEI 76
|
....*
gi 1907069410 795 ASLLL 799
Cdd:pfam12796 77 VKLLL 81
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
141-420 |
8.78e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 74.92 E-value: 8.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 141 INAFDKKDRRA----------LHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQISVVKHLLNLGVEIDEI 210
Cdd:PHA02878 20 IEYIDHTENYStsaslipfipLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 211 NVYgnTALHIACYNGQDAVVNE-LIDYGANVNQPNNSGFTPLHFAAASThgALCLELLVNNGADVNIQSKD-GKSPLHMT 288
Cdd:PHA02878 100 YTL--VAIKDAFNNRNVEIFKIiLTNRYKNIQTIDLVYIDKKSKDDIIE--AEITKLLLSYGADINMKDRHkGNTALHYA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 289 AVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARHGHELLINTLITSGADT---AKCGihsMFPLHLAALNAHS-DCCR 364
Cdd:PHA02878 176 TENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTdarDKCG---NTPLHISVGYCKDyDILK 252
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907069410 365 KLLSSGFEIDTPDTF-GRTCLHAAAAGGNVecIKLLQSSGADFHKKDKCGRTPLHYA 420
Cdd:PHA02878 253 LLLEHGVDVNAKSYIlGLTALHSSIKSERK--LKLLLEYGADINSLNSYKLTPLSSA 307
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
559-941 |
9.02e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 75.49 E-value: 9.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 559 EVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQGA--SIFVKDNVTKrtpLHASVINGHTLCLRLLLETADNPE 636
Cdd:PHA02876 162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGAdvNIIALDDLSV---LECAVDSKNIDTIKAIIDNRSNIN 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 637 vvdvkdaKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIVGCTALHRGIMTGH-EECVQMLLEQEASILCKDSRGRTPL 715
Cdd:PHA02876 239 -------KNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 716 HYAAARGHATwlNELLQIALSEEDCCLKDNQGYTPLHWA-CYNGNENCIEVLLEqkcfrkfignpftplhcaiinghesc 794
Cdd:PHA02876 312 YLMAKNGYDT--ENIRTLIMLGADVNAADRLYITPLHQAsTLDRNKDIVITLLE-------------------------- 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 795 asllLGAidpsIVSCRDDKGRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMA-AENGQAGAVDILVNSAqAD 873
Cdd:PHA02876 364 ----LGA----NVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRG-AN 434
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907069410 874 LTVKDKDLNTPLHLAISKgheKCALLILDKIQDESL-INAKNSALQTPLHIAArnGLKVVVEELLAKGA 941
Cdd:PHA02876 435 VNSKNKDLSTPLHYACKK---NCKLDVIEMLLDNGAdVNAINIQNQYPLLIAL--EYHGIVNILLHYGA 498
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
30-248 |
1.16e-13 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 74.49 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 30 EIIELLILSGARVNAKDNMWLTPLHRAVASRSE-----EAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPL 104
Cdd:PHA02798 52 DIVKLFINLGANVNGLDNEYSTPLCTILSNIKDykhmlDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLFM 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 105 L---SSVNVSDRGGRTALHHAALNGH---MEMVNLLLAKGANINAFDKKDR-RALHwaAYMGH------LDVVALLINHG 171
Cdd:PHA02798 132 IengADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINTHNNKEKyDTLH--CYFKYnidridADILKLFVDNG 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 172 ---------------------------------------AEVTCKDKKGYTPLHAAASNGQISVVKHLLNLGVEIDEINV 212
Cdd:PHA02798 210 fiinkenkshkkkfmeylnsllydnkrfkknildfifsyIDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITE 289
|
250 260 270
....*....|....*....|....*....|....*.
gi 1907069410 213 YGNTALHIACYNGQDAVVNELIDYGANVNQPNNSGF 248
Cdd:PHA02798 290 LGNTCLFTAFENESKFIFNSILNKKPNKNTISYTYY 325
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
695-948 |
1.18e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 75.10 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 695 QMLLEQEASILCKDSRGRTPLHYAAARGHATWLNELLQIAlseEDCCLKDNQGYTPLHWACYNGNENCIEVLLEQkcfRK 774
Cdd:PHA02876 162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYG---ADVNIIALDDLSVLECAVDSKNIDTIKAIIDN---RS 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 775 FIGNPFTPLHCAIINgHESCASLLLGAIDPSIVSCRDDKGRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMA 854
Cdd:PHA02876 236 NINKNDLSLLKAIRN-EDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLM 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 855 AENGQAGAVDILVNSAQADLTVKDKDLNTPLHLAISKGHEKCALLILdkIQDESLINAKNSALQTPLHIAARNGLKVVVE 934
Cdd:PHA02876 315 AKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVITL--LELGANVNARDYCDKTPIHYAAVRNNVVIIN 392
|
250
....*....|....
gi 1907069410 935 ELLAKGACVLAVDE 948
Cdd:PHA02876 393 TLLDYGADIEALSQ 406
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
318-410 |
1.20e-13 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 67.45 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 318 LHVAARHGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSgFEIDtPDTFGRTCLHAAAAGGNVECIK 397
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVN-LKDNGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1907069410 398 LLQSSGADFHKKD 410
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
851-947 |
3.99e-13 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 65.91 E-value: 3.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 851 LMMAAENGQAGAVDILVNSaQADLTVKDKDLNTPLHLAISKGHEKCALLILDKIQdeslINAKNSAlQTPLHIAARNGLK 930
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLEN-GADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD----VNLKDNG-RTALHYAARSGHL 74
|
90
....*....|....*..
gi 1907069410 931 VVVEELLAKGACVLAVD 947
Cdd:pfam12796 75 EIVKLLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
2-79 |
4.80e-13 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 65.52 E-value: 4.80e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907069410 2 LIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLiLSGARVNAKDNMWlTPLHRAVASRSEEAVQVLIKHSADVNARD 79
Cdd:pfam12796 16 LLENGADANLQDKNGRTALHLAAKNGHLEIVKLL-LEHADVNLKDNGR-TALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
567-799 |
8.19e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 71.62 E-value: 8.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 567 DLDIRDEKGRTALYLAAFKGHTECVEALVNQGASIFVKDNvTKRTPLHASVINGHTLclrllletADNPEVVDvkdakgq 646
Cdd:PHA03100 27 LNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTK-NNSTPLHYLSNIKYNL--------TDVKEIVK------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 647 tplmlavayghidavsLLLEKEANVDAVDIVGCTALHRGIMT--GHEECVQMLLEQEASILCKDSRGRTPLHYAAARGHA 724
Cdd:PHA03100 91 ----------------LLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 725 TwlNELLQIALS---------EEDCCL--------KDNQGYTPLHWACYNGNENCIEVLLEQKCF---RKFIGNpfTPLH 784
Cdd:PHA03100 155 D--LKILKLLIDkgvdinaknRVNYLLsygvpiniKDVYGFTPLHYAVYNNNPEFVKYLLDLGANpnlVNKYGD--TPLH 230
|
250
....*....|....*
gi 1907069410 785 CAIINGHESCASLLL 799
Cdd:PHA03100 231 IAILNNNKEIFKLLL 245
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
18-142 |
1.06e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 71.18 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 18 TPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKC 97
Cdd:PHA02875 104 TPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAI 183
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1907069410 98 AEVIIPLLSSVN-VSDRGGRTALHHAALNGHMEMVNLLLAKGANIN 142
Cdd:PHA02875 184 CKMLLDSGANIDyFGKNGCVAALCYAIENNKIDIVRLFIKRGADCN 229
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
23-176 |
1.11e-12 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 72.21 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 23 AAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVII 102
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY 611
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907069410 103 PLLSSVNVSDRGgrTALHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTC 176
Cdd:PLN03192 612 HFASISDPHAAG--DLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDK 683
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
68-213 |
1.58e-12 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 71.82 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 68 LIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHMEMVNLLLAKGANINAFDKK 147
Cdd:PLN03192 544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAG 623
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907069410 148 DrrALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQISVVKHLLNLGVEIDEINVY 213
Cdd:PLN03192 624 D--LLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTD 687
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
284-585 |
2.34e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 70.29 E-value: 2.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 284 PLHMtAVHGR-FTRSQTLIQNGGEIDCVDKDGNTPLHVAARHGHELLINTLITSgadTAKCGI-HSMFPLHLAALNAHSD 361
Cdd:PHA02878 40 PLHQ-AVEARnLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRS---INKCSVfYTLVAIKDAFNNRNVE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 362 CCRKLLSSGFEIDTPDTFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDK-CGRTPLHYAAANCHFHCIKALVTTGANVN 440
Cdd:PHA02878 116 IFKIILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVN 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 441 ETDDWGRTALHYAAASdmdRNKMIlgnahdnseelerarevkekdaalcLEFLLQNDANPSIRDKEGYNSIHYAAAY-GH 519
Cdd:PHA02878 196 IPDKTNNSPLHHAVKH---YNKPI-------------------------VHILLENGASTDARDKCGNTPLHISVGYcKD 247
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907069410 520 RQCLELLLERTNTGFEESDGGALkSPLHLAAYNghHQALEVLLQSLVDLDIRDEKGRTALYLAAFK 585
Cdd:PHA02878 248 YDILKLLLEHGVDVNAKSYILGL-TALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
718-887 |
2.52e-12 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 71.05 E-value: 2.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 718 AAARGHATWLNELLQIALSEEdccLKDNQGYTPLHWACYNGNENCIEVLLEQKC---FRKFIGNpfTPLHCAIINGHESC 794
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPD---IGDSKGRTPLHIAASKGYEDCVLVLLKHACnvhIRDANGN--TALWNAISAKHHKI 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 795 ASLLL---GAIDPSIvscrddkGRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILV-NSA 870
Cdd:PLN03192 607 FRILYhfaSISDPHA-------AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLImNGA 679
|
170
....*....|....*..
gi 1907069410 871 QADLTVKDKDLnTPLHL 887
Cdd:PLN03192 680 DVDKANTDDDF-SPTEL 695
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
416-653 |
2.53e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 70.29 E-value: 2.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 416 PLHYAAANCHFHCIKALVTTGANVNETDDWGRTALH--------------------------YAAASDM--DRN----KM 463
Cdd:PHA02878 40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHiickepnklgmkemirsinkcsvfytLVAIKDAfnNRNveifKI 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 464 ILGNAHDNSEELErAREVKEKDAALCLE-----FLLQNDANPSIRDKEGYNS-IHYAAAYGHRQCLELLL---------E 528
Cdd:PHA02878 120 ILTNRYKNIQTID-LVYIDKKSKDDIIEaeitkLLLSYGADINMKDRHKGNTaLHYATENKDQRLTELLLsyganvnipD 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 529 RTNtgfeesdggalKSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLA-AFKGHTECVEALVNQGASIFVKDNV 607
Cdd:PHA02878 199 KTN-----------NSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYI 267
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1907069410 608 TKRTPLHASVINGHTlcLRLLLETADNPEVVdvkDAKGQTPLMLAV 653
Cdd:PHA02878 268 LGLTALHSSIKSERK--LKLLLEYGADINSL---NSYKLTPLSSAV 308
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
148-370 |
2.62e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 70.02 E-value: 2.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 148 DRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQISVVKHLLNLGVeIDEINVYG-NTALHIACYNGQ 226
Cdd:PHA02875 2 DQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGA-IPDVKYPDiESELHDAVEEGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 227 DAVVNELIDYGANVNQP-NNSGFTPLHFAAASTHGALcLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGG 305
Cdd:PHA02875 81 VKAVEELLDLGKFADDVfYKDGMTPLHLATILKKLDI-MKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907069410 306 EIDCVDKDGNTPLHVAARHGHELLINTLITSGADTAKCGIHSMFPLHLAAL-NAHSDCCRKLLSSG 370
Cdd:PHA02875 160 CLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIeNNKIDIVRLFIKRG 225
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
489-572 |
3.57e-12 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 63.21 E-value: 3.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 489 CLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNTGFEESDggalKSPLHLAAYNGHHQALEVLLQSLVDL 568
Cdd:pfam12796 12 LVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNG----RTALHYAARSGHLEIVKLLLEKGADI 87
|
....
gi 1907069410 569 DIRD 572
Cdd:pfam12796 88 NVKD 91
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
558-770 |
4.38e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 69.31 E-value: 4.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 558 LEVLLQSLVDLDIRDEKGRTALYLAAFKGHT-----ECVEALVNQGASIFVKDNVTKrTPLHASVIN--GHTLCLRLLLE 630
Cdd:PHA03100 51 VKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGI-TPLLYAISKksNSYSIVEYLLD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 631 TADNpevVDVKDAKGQTPLMLAVAYGHIDA--VSLLLEKEANVDAVDIVgctalhrgimtgheecvQMLLEQEASILCKD 708
Cdd:PHA03100 130 NGAN---VNIKNSDGENLLHLYLESNKIDLkiLKLLIDKGVDINAKNRV-----------------NYLLSYGVPINIKD 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907069410 709 SRGRTPLHYAAARGHATWLNELLQIALSEEDCclkDNQGYTPLHWACYNGNENCIEVLLEQK 770
Cdd:PHA03100 190 VYGFTPLHYAVYNNNPEFVKYLLDLGANPNLV---NKYGDTPLHIAILNNNKEIFKLLLNNG 248
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
115-168 |
8.30e-12 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 60.75 E-value: 8.30e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1907069410 115 GRTALHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLI 168
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
82-334 |
1.12e-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: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 82 WQTPLHVAAANKAVKCaevIIPLL--SSVNVSDRG--GRTALHHAALNGHMEMVNLLLakganinafdkkdrralhwaay 157
Cdd:cd22192 17 SESPLLLAAKENDVQA---IKKLLkcPSCDLFQRGalGETALHVAALYDNLEAAVVLM---------------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 158 mghlDVVALLINHgaEVTCkdkkgytplhaaasngqisvvkhllnlgveideiNVY-GNTALHIACYNGQDAVVNELIDY 236
Cdd:cd22192 72 ----EAAPELVNE--PMTS----------------------------------DLYqGETALHIAVVNQNLNLVRELIAR 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 237 GANVNQPNNSG--FT------------PLHFAAASTHGALcLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLI- 301
Cdd:cd22192 112 GADVVSPRATGtfFRpgpknliyygehPLSFAACVGNEEI-VRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFACQMYd 190
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1907069410 302 --------QNGGEIDCV-DKDGNTPLHVAARHGHELLINTLI 334
Cdd:cd22192 191 lilsydkeDDLQPLDLVpNNQGLTPFKLAAKEGNIVMFQHLV 232
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
149-201 |
1.31e-11 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 60.37 E-value: 1.31e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1907069410 149 RRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQISVVKHLL 201
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
285-377 |
1.54e-11 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 61.29 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 285 LHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARHGHELLINTLITSGAdtAKCGIHSMFPLHLAALNAHSDCCR 364
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1907069410 365 KLLSSGFEIDTPD 377
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
251-339 |
2.23e-11 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 60.90 E-value: 2.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 251 LHFAAASTHgALCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNgGEIDCVDkDGNTPLHVAARHGHELLI 330
Cdd:pfam12796 1 LHLAAKNGN-LELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77
|
....*....
gi 1907069410 331 NTLITSGAD 339
Cdd:pfam12796 78 KLLLEKGAD 86
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
24-255 |
2.39e-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: 2.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 24 AFLGDAEIIELLILSGARVNAK-------DNMWLTPLHRAVA-SRSEEAVQVLIKHSADVNARDknwqTPLHVAAANKAV 95
Cdd:TIGR00870 20 AFLPAAERGDLASVYRDLEEPKklnincpDRLGRSALFVAAIeNENLELTELLLNLSCRGAVGD----TLLHAISLEYVD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 96 KCAEVIIPLLSS---------VNVSDRG----GRTALHHAALNGHMEMVNLLLAKGANINA------FDKKDRRA----- 151
Cdd:TIGR00870 96 AVEAILLHLLAAfrksgplelANDQYTSeftpGITALHLAAHRQNYEIVKLLLERGASVPAracgdfFVKSQGVDsfyhg 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 152 ---LHWAAYMGHLDVVALLINHGAEVTCKDKKGYTplhaaasngqisvVKHLLNLGVEideiNVYGNTALHIACYngqda 228
Cdd:TIGR00870 176 espLNAAACLGSPSIVALLSEDPADILTADSLGNT-------------LLHLLVMENE----FKAEYEELSCQMY----- 233
|
250 260 270
....*....|....*....|....*....|....
gi 1907069410 229 vvNELIDYGANVNQ-------PNNSGFTPLHFAA 255
Cdd:TIGR00870 234 --NFALSLLDKLRDskeleviLNHQGLTPLKLAA 265
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
158-405 |
2.44e-11 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 67.97 E-value: 2.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 158 MGHLDVVALLINHGAEVTckDKKGYTPLHAAASNGQISVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYG 237
Cdd:PLN03192 504 LHDLNVGDLLGDNGGEHD--DPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 238 ANVNQPNNSGFTPLHFAAASTHGALcLELLVNNGADVNIQSkdGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTP 317
Cdd:PLN03192 582 CNVHIRDANGNTALWNAISAKHHKI-FRILYHFASISDPHA--AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATA 658
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 318 LHVAARHGHELLINTLITSGADTAKCGIHSMF-PLHLaalnahsdccRKLLSS---GFEIDTPDTFGRTCLHAAAAGGNV 393
Cdd:PLN03192 659 LQVAMAEDHVDMVRLLIMNGADVDKANTDDDFsPTEL----------RELLQKrelGHSITIVDSVPADEPDLGRDGGSR 728
|
250
....*....|..
gi 1907069410 394 ECikLLQSSGAD 405
Cdd:PLN03192 729 PG--RLQGTSSD 738
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
380-433 |
2.46e-11 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 59.60 E-value: 2.46e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1907069410 380 GRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIKALV 433
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
697-949 |
6.10e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 65.84 E-value: 6.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 697 LLEQEASILCKDSRGRTPLHYAAARGHATWLNELLqialsEEDCCL--KDNQGYTPLH---WACYNGNEN--CIEVLLEQ 769
Cdd:PHA03100 21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILL-----DNGADInsSTKNNSTPLHylsNIKYNLTDVkeIVKLLLEY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 770 -KCFRKFIGNPFTPLHCAIIN--GHESCASLLLG-AIDPSIVSCRddkGRTTLHAAAFGDHA--ECLQLLLRHDAQVNAV 843
Cdd:PHA03100 96 gANVNAPDNNGITPLLYAISKksNSYSIVEYLLDnGANVNIKNSD---GENLLHLYLESNKIdlKILKLLIDKGVDINAK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 844 DNsgktalmmaaengqagaVDILVNSAqADLTVKDKDLNTPLHLAISKGHEKCALLILDKIQDeslINAKNSALQTPLHI 923
Cdd:PHA03100 173 NR-----------------VNYLLSYG-VPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGAN---PNLVNKYGDTPLHI 231
|
250 260
....*....|....*....|....*.
gi 1907069410 924 AARNGLKVVVEELLAKGACVLAVDEN 949
Cdd:PHA03100 232 AILNNNKEIFKLLLNNGPSIKTIIET 257
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
744-943 |
7.63e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 65.67 E-value: 7.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 744 DNQGYTPLHWACYNGNENCIEVLLEQKCFRKfIGNPFTPLHCAIINGHESCASLLLGAIDPSIVSCRDDKGRTTLHAAAF 823
Cdd:PHA02878 67 DHRDLTPLHIICKEPNKLGMKEMIRSINKCS-VFYTLVAIKDAFNNRNVEIFKIILTNRYKNIQTIDLVYIDKKSKDDII 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 824 gdHAECLQLLLRHDAQVNAVD-NSGKTALMMAAENGQAGAVDILVnSAQADLTVKDKDLNTPLHLAISKGHEKcALLILd 902
Cdd:PHA02878 146 --EAEITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLL-SYGANVNIPDKTNNSPLHHAVKHYNKP-IVHIL- 220
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1907069410 903 kIQDESLINAKNSALQTPLHIAARNGLKV-VVEELLAKGACV 943
Cdd:PHA02878 221 -LENGASTDARDKCGNTPLHISVGYCKDYdILKLLLEHGVDV 261
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
577-759 |
8.10e-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: 8.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 577 TALYLAAFKGHTECVEAL-VNQGASIFVKDNVTKrTPLHASVINGHTLCLRLLLETAdnPEVVDVKDA----KGQTPLML 651
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLlKCPSCDLFQRGALGE-TALHVAALYDNLEAAVVLMEAA--PELVNEPMTsdlyQGETALHI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 652 AVAYGHIDAVSLLLEKEANVDAVDIVGcTALHRGI---------------MTGHEECVQMLLEQEASILCKDSRGRTPLH 716
Cdd:cd22192 96 AVVNQNLNLVRELIARGADVVSPRATG-TFFRPGPknliyygehplsfaaCVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1907069410 717 YAAARGHATWLNELLQIALSEE----DCCL---KDNQGYTPLHWACYNGN 759
Cdd:cd22192 175 ILVLQPNKTFACQMYDLILSYDkeddLQPLdlvPNNQGLTPFKLAAKEGN 224
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
125-250 |
8.13e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 62.53 E-value: 8.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 125 NGHMEMVNLLLAKGANINAFDKKDRRAL--HWAAYMGHL--DVVALLINHGAEVTCKDKKGYTPLHAAASNG--QISVVK 198
Cdd:PHA02859 63 KVNVEILKFLIENGADVNFKTRDNNLSAlhHYLSFNKNVepEILKILIDSGSSITEEDEDGKNLLHMYMCNFnvRINVIK 142
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1907069410 199 HLLNLGVEIDEINVYGNTALH-IACYNGQDAVVNELIDYGANVNQPNNSGFTP 250
Cdd:PHA02859 143 LLIDSGVSFLNKDFDNNNILYsYILFHSDKKIFDFLTSLGIDINETNKSGYNC 195
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
531-714 |
2.43e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 63.86 E-value: 2.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 531 NTGFEESDGgalKSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQGAsiFVKDNVTKR 610
Cdd:PHA02875 27 NPNFEIYDG---ISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK--FADDVFYKD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 611 --TPLHASVINGHTLCLRLLLETADNPevvDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIVGCTALHRGIMT 688
Cdd:PHA02875 102 gmTPLHLATILKKLDIMKLLIARGADP---DIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAK 178
|
170 180
....*....|....*....|....*.
gi 1907069410 689 GHEECVQMLLEQEASIlckDSRGRTP 714
Cdd:PHA02875 179 GDIAICKMLLDSGANI---DYFGKNG 201
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
122-251 |
2.98e-10 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 64.12 E-value: 2.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 122 AALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPL---------------- 185
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnaisakhhkifrily 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 186 --------HA-------AASNGQISVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPN-NSGFT 249
Cdd:PLN03192 612 hfasisdpHAagdllctAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANtDDDFS 691
|
..
gi 1907069410 250 PL 251
Cdd:PLN03192 692 PT 693
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
513-732 |
3.64e-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: 3.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 513 YAAAYGHRQCLELLLERTNTGFEESdgGAL-KSPLHLAAYNGHHQALEVLLQS---LVDLDIRDE--KGRTALYLAAFKG 586
Cdd:cd22192 23 LAAKENDVQAIKKLLKCPSCDLFQR--GALgETALHVAALYDNLEAAVVLMEAapeLVNEPMTSDlyQGETALHIAVVNQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 587 HTECVEALVNQGAsifvkDNVTKRTPLHASVINGHTLCLRllletadnpevvdvkdakGQTPLMLAVAYGHIDAVSLLLE 666
Cdd:cd22192 101 NLNLVRELIARGA-----DVVSPRATGTFFRPGPKNLIYY------------------GEHPLSFAACVGNEEIVRLLIE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907069410 667 KEANVDAVDIVGCTALHRGIMTGHEECV-QM---LLEQEASI------LCKDSRGRTPLHYAAARGHATWLNELLQ 732
Cdd:cd22192 158 HGADIRAQDSLGNTVLHILVLQPNKTFAcQMydlILSYDKEDdlqpldLVPNNQGLTPFKLAAKEGNIVMFQHLVQ 233
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
647-948 |
7.76e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 62.29 E-value: 7.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 647 TPLMLAVAYGHIDAVSLLLEKEANVDAVDIVGCTALHRGIMTGHEECVQMLLEQ--EASIL------------------- 705
Cdd:PHA02874 37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNgvDTSILpipciekdmiktildcgid 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 706 --CKDSRGRTPLHYAAARGHATWLNELLQIAlseEDCCLKDNQGYTPLHWACYNGNENCIEVLLEQKCFrkfignpftpl 783
Cdd:PHA02874 117 vnIKDAELKTFLHYAIKKGDLESIKMLFEYG---ADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY----------- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 784 hcaiinghescaslllgaidpsiVSCRDDKGRTTLH-AAAFGDHAeCLQLLLRHDAQVNAVDNSGKTALMMAAENGQAgA 862
Cdd:PHA02874 183 -----------------------ANVKDNNGESPLHnAAEYGDYA-CIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRS-A 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 863 VDILVNSAQadLTVKDKDLNTPLHLAIskgHEKCALLILDK-IQDESLINAKNSALQTPLHIAARNGLKV-VVEELLAKG 940
Cdd:PHA02874 238 IELLINNAS--INDQDIDGSTPLHHAI---NPPCDIDIIDIlLYHKADISIKDNKGENPIDTAFKYINKDpVIKDIIANA 312
|
....*...
gi 1907069410 941 ACVLAVDE 948
Cdd:PHA02874 313 VLIKEADK 320
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
647-698 |
8.14e-10 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 55.36 E-value: 8.14e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1907069410 647 TPLMLAVAYGHIDAVSLLLEKEANVDAVDIVGCTALHRGIMTGHEECVQMLL 698
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
610-722 |
8.30e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 61.93 E-value: 8.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 610 RTPLHASVINGHTLCLRLLLETadNPEVVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIVGCTALHRGIMTG 689
Cdd:PHA02875 69 ESELHDAVEEGDVKAVEELLDL--GKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMG 146
|
90 100 110
....*....|....*....|....*....|...
gi 1907069410 690 HEECVQMLLEQEASILCKDSRGRTPLHYAAARG 722
Cdd:PHA02875 147 DIKGIELLIDHKACLDIEDCCGCTPLIIAMAKG 179
|
|
| PHA02716 |
PHA02716 |
CPXV016; CPX019; EVM010; Provisional |
264-450 |
9.28e-10 |
|
CPXV016; CPX019; EVM010; Provisional
Pssm-ID: 165089 [Multi-domain] Cd Length: 764 Bit Score: 62.62 E-value: 9.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 264 LELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRS--QTLIQNGGEIDCVDKDGNTPLH---VAARHGHELLINTLITSGA 338
Cdd:PHA02716 195 LEWLCNNGVNVNLQNNHLITPLHTYLITGNVCASviKKIIELGGDMDMKCVNGMSPIMtyiINIDNINPEITNIYIESLD 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 339 DTAKCGIHSMFPLHLA-ALNAHSDCCRKLLSSGFEIDTPDTFGRTCLHAAAAGGNV--ECIKLLQSSGADFHKKDKCGRT 415
Cdd:PHA02716 275 GNKVKNIPMILHSYITlARNIDISVVYSFLQPGVKLHYKDSAGRTCLHQYILRHNIstDIIKLLHEYGNDLNEPDNIGNT 354
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1907069410 416 PLH-YAAANCHFH-------------CIKALVTTGANVNETDDWGRTAL 450
Cdd:PHA02716 355 VLHtYLSMLSVVNildpetdndirldVIQCLISLGADITAVNCLGYTPL 403
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
83-257 |
9.32e-10 |
|
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: 9.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 83 QTPLHVAAANKAVKCAEVIIPLLSSVNVSDRG--------------GRTALHHAALNGHMEMVNLLLAKGANINA----- 143
Cdd:cd21882 27 KTCLHKAALNLNDGVNEAIMLLLEAAPDSGNPkelvnapctdefyqGQTALHIAIENRNLNLVRLLVENGADVSAratgr 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 144 FDKKDRR--------ALHWAAYMGHLDVVALLINHGAE---VTCKDKKGYTPLHAAasngqisvvkhllnlgVEIDEiNV 212
Cdd:cd21882 107 FFRKSPGnlfyfgelPLSLAACTNQEEIVRLLLENGAQpaaLEAQDSLGNTVLHAL----------------VLQAD-NT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1907069410 213 YGNTALHIACYNGqdavvneLIDYGANVNQ-------PNNSGFTPLHFAAAS 257
Cdd:cd21882 170 PENSAFVCQMYNL-------LLSYGAHLDPtqqleeiPNHQGLTPLKLAAVE 214
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
119-201 |
2.01e-09 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 61.45 E-value: 2.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 119 LHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQISVVK 198
Cdd:PTZ00322 86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165
|
...
gi 1907069410 199 HLL 201
Cdd:PTZ00322 166 LLS 168
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
315-451 |
2.06e-09 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 61.18 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 315 NTPLHVAARHGHELLINTLITS-GADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSG----FEIDTPDTF-GRTCLHAAA 388
Cdd:cd22192 18 ESPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLMEAApelvNEPMTSDLYqGETALHIAV 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907069410 389 AGGNVECIKLLQSSGAD----------FHKKDKC----GRTPLHYAAANCHFHCIKALVTTGANVNETDDWGRTALH 451
Cdd:cd22192 98 VNQNLNLVRELIARGADvvspratgtfFRPGPKNliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
|
|
| PHA02989 |
PHA02989 |
ankyrin repeat protein; Provisional |
30-331 |
2.08e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222954 [Multi-domain] Cd Length: 494 Bit Score: 60.91 E-value: 2.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 30 EIIELLILSGARVNAKDNMwLTPL-----HRAVAS-RSEEAVQVLIKHSADVNARDKNWQTPlhvaaankavkcaevIIP 103
Cdd:PHA02989 51 KIVKLLIDNGADVNYKGYI-ETPLcavlrNREITSnKIKKIVKLLLKFGADINLKTFNGVSP---------------IVC 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 104 LLSSVNVSDrggrtalhhaalnghMEMVNLLLAKGANINafdkkdrralhwaaymghldvvallinhgaevTCKDKKGYT 183
Cdd:PHA02989 115 FIYNSNINN---------------CDMLRFLLSKGINVN--------------------------------DVKNSRGYN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 184 PLHAAASNGQIS--VVKHLLNLGVEIDEI-NVYGNTALHIACYNGQDAVVNELIDY----GANVNQPNNSGFTPLHfAAA 256
Cdd:PHA02989 148 LLHMYLESFSVKkdVIKILLSFGVNLFEKtSLYGLTPMNIYLRNDIDVISIKVIKYlikkGVNIETNNNGSESVLE-SFL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 257 STHGAL---CLELL--VNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARHGHELLIN 331
Cdd:PHA02989 227 DNNKILskkEFKVLnfILKYIKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLN 306
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
544-595 |
2.74e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 53.82 E-value: 2.74e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1907069410 544 SPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALV 595
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
350-399 |
4.09e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 53.43 E-value: 4.09e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1907069410 350 PLHLAALNAHSDCCRKLLSSGFEIDTPDTFGRTCLHAAAAGGNVECIKLL 399
Cdd:pfam13637 4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
249-418 |
8.58e-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: 8.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 249 TPLhFAAASTHGALCLE-LLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGE-----IDCVDKDGNTPLHVAA 322
Cdd:cd22192 19 SPL-LLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElvnepMTSDLYQGETALHIAV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 323 RHGHELLINTLITSGADTAK---CGihSMFplhlaALNAHSDCcrkllssgfeidtpdTFGRTCLHAAAAGGNVECIKLL 399
Cdd:cd22192 98 VNQNLNLVRELIARGADVVSpraTG--TFF-----RPGPKNLI---------------YYGEHPLSFAACVGNEEIVRLL 155
|
170
....*....|....*....
gi 1907069410 400 QSSGADFHKKDKCGRTPLH 418
Cdd:cd22192 156 IEHGADIRAQDSLGNTVLH 174
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
667-947 |
1.17e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 58.74 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 667 KEANVDAVDIVGCTALHRGIMTGHEECVQMLLEQEASILCKDSRGRTPLHYAAARGHATWLNELLQIALseedcclKDNQ 746
Cdd:PHA02878 26 TENYSTSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSIN-------KCSV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 747 GYT--PLHWACYNGNENCIEVLLeqkcFRKFIGNpftplhcAIINGHESCASLLLGAIDPSIVSC-----------RDDK 813
Cdd:PHA02878 99 FYTlvAIKDAFNNRNVEIFKIIL----TNRYKNI-------QTIDLVYIDKKSKDDIIEAEITKLllsygadinmkDRHK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 814 GRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNSAqADLTVKDKDLNTPLHLAISKGH 893
Cdd:PHA02878 168 GNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENG-ASTDARDKCGNTPLHISVGYCK 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1907069410 894 EKCALLILdkIQDESLINAKNSALQ-TPLHIAARNGLKVVVeeLLAKGACVLAVD 947
Cdd:PHA02878 247 DYDILKLL--LEHGVDVNAKSYILGlTALHSSIKSERKLKL--LLEYGADINSLN 297
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
413-455 |
1.43e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 51.89 E-value: 1.43e-08
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1907069410 413 GRTPLHYAAANCHFHCIKALVTTGANVNETDDWGRTALHYAAA 455
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAAS 43
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
28-287 |
1.52e-08 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 58.14 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 28 DAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKavkcAEVIipllss 107
Cdd:PHA02946 51 DERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTD----DEVI------ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 108 vnvsdrggrtalhhaalnghmEMVNLLLAKGANINafdkkdrralhwaaymghldvvallinhgaevTCKDKKGYTPLHA 187
Cdd:PHA02946 121 ---------------------ERINLLVQYGAKIN--------------------------------NSVDEEGCGPLLA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 188 AASNGQiSVVKHLLNLGVEIDEINVYGNTAL--HIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHFAAASTHGALCLE 265
Cdd:PHA02946 148 CTDPSE-RVFKKIMSIGFEARIVDKFGKNHIhrHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCSKTVKNVDII 226
|
250 260
....*....|....*....|..
gi 1907069410 266 LLVNNGADVNIQSKDGKSPLHM 287
Cdd:PHA02946 227 NLLLPSTDVNKQNKFGDSPLTL 248
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
181-234 |
1.89e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 51.51 E-value: 1.89e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1907069410 181 GYTPLHAAASNGQISVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELI 234
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
749-951 |
2.31e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 57.67 E-value: 2.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 749 TPLHWACYNGNENCIEVLLEQKCFRKFIG-NPFTPLHCAI-INGHESCASLLLGAIDPSI-------------------- 806
Cdd:PHA02874 37 TPLIDAIRSGDAKIVELFIKHGADINHINtKIPHPLLTAIkIGAHDIIKLLIDNGVDTSIlpipciekdmiktildcgid 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 807 VSCRDDKGRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNSAqADLTVKDKDLNTPLH 886
Cdd:PHA02874 117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKG-AYANVKDNNGESPLH 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907069410 887 LAISKGHEKCALLILDkiqDESLINAKNSALQTPLHIAARNGLKVVveELLAKGACVLAVDENAS 951
Cdd:PHA02874 196 NAAEYGDYACIKLLID---HGNHIMNKCKNGFTPLHNAIIHNRSAI--ELLINNASINDQDIDGS 255
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
298-528 |
2.43e-08 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 57.37 E-value: 2.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 298 QTLIQNGGEIDCVDKDGNTPLHVAARHGHELLINTLITSGADTAKCGIHSMFPLH------------------------- 352
Cdd:PHA02946 56 EELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYylsgtddevierinllvqygakinn 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 353 ----------LAALNAHSDCCRKLLSSGFEIDTPDTFGRTCLHAAAAGGN--VECIKLLQSSGADFHKKDKCGRTPLHYA 420
Cdd:PHA02946 136 svdeegcgplLACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNpkASTISWMMKLGISPSKPDHDGNTPLHIV 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 421 AANCHFHC-IKALVTTGANVNETDDWGRTALHYAAASdmdrnkmiLGNAHDNSEELERAREVKEKDAALCLeFLLQNDAN 499
Cdd:PHA02946 216 CSKTVKNVdIINLLLPSTDVNKQNKFGDSPLTLLIKT--------LSPAHLINKLLSTSNVITDQTVNICI-FYDRDDVL 286
|
250 260 270
....*....|....*....|....*....|..
gi 1907069410 500 PSIRDK-EGYNSIHY--AAAYGHRQCLELLLE 528
Cdd:PHA02946 287 EIINDKgKQYDSTDFkmAVEVGSIRCVKYLLD 318
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
52-225 |
2.96e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 55.21 E-value: 2.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 52 PLHRAVASRSEEAVQVLIKHSADVNardKNWQTPLHVAAANKAV--KCAEVIIPLLSSVNVSDRGGRTALHHAAL----N 125
Cdd:PHA02859 24 PLFYYVEKDDIEGVKKWIKFVNDCN---DLYETPIFSCLEKDKVnvEILKFLIENGADVNFKTRDNNLSALHHYLsfnkN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 126 GHMEMVNLLLAKGANINAFDKKDRRALHwaAYMGH----LDVVALLINHGAEVTCKDKKGYTPLHA-AASNGQISVVKHL 200
Cdd:PHA02859 101 VEPEILKILIDSGSSITEEDEDGKNLLH--MYMCNfnvrINVIKLLIDSGVSFLNKDFDNNNILYSyILFHSDKKIFDFL 178
|
170 180
....*....|....*....|....*
gi 1907069410 201 LNLGVEIDEINVYGNTALHIACYNG 225
Cdd:PHA02859 179 TSLGIDINETNKSGYNCYDLIKFRN 203
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
300-450 |
5.35e-08 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 56.80 E-value: 5.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 300 LIQNGGEIDCVDKDGNtpLHVAARHGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSGFEIDTPDTF 379
Cdd:PLN03192 513 LGDNGGEHDDPNMASN--LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDAN 590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 380 GRTCL------------------------HA-------AAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHC 428
Cdd:PLN03192 591 GNTALwnaisakhhkifrilyhfasisdpHAagdllctAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDM 670
|
170 180
....*....|....*....|....*
gi 1907069410 429 IKALVTTGANV---NETDDWGRTAL 450
Cdd:PLN03192 671 VRLLIMNGADVdkaNTDDDFSPTEL 695
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
49-102 |
5.70e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 49.97 E-value: 5.70e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1907069410 49 WLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVII 102
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
566-788 |
7.28e-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: 7.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 566 VDLDIRDEKGRTALYLAAFKG-HTECVEALVNQGASIFVKDNVtkrtpLHASVINGH---TLCLRLLL----ETADNPEV 637
Cdd:TIGR00870 43 LNINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAVGDTL-----LHAISLEYVdavEAILLHLLaafrKSGPLELA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 638 VDVKDA---KGQTPLMLAVAYGHIDAVSLLLEKEANVDAVdiVGCTALHRGIM----------------TGHEECVQMLL 698
Cdd:TIGR00870 118 NDQYTSeftPGITALHLAAHRQNYEIVKLLLERGASVPAR--ACGDFFVKSQGvdsfyhgesplnaaacLGSPSIVALLS 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 699 EQEASILCKDSRGRTPLHYAAARGHATWLNELL-------------QIALSEEDCCLKDNQGYTPLHWACYNGNENCIEV 765
Cdd:TIGR00870 196 EDPADILTADSLGNTLLHLLVMENEFKAEYEELscqmynfalslldKLRDSKELEVILNHQGLTPLKLAAKEGRIVLFRL 275
|
250 260
....*....|....*....|....
gi 1907069410 766 LLEQKCF-RKFIGNPFTPLHCAII 788
Cdd:TIGR00870 276 KLAIKYKqKKFVAWPNGQQLLSLY 299
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
1-139 |
7.93e-08 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 55.80 E-value: 7.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 1 MLIHKTEDVNALDSEKRTPLHVAAFLGD--AEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNAR 78
Cdd:PHA03095 207 ELIRAGCDPAATDMLGNTPLHSMATGSSckRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAV 286
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907069410 79 DKNWQTPLHVAAANKAVKCAEVIIPLLSSVNVSDRggrtALHHAALNGHM-------EMVNLLLAKGA 139
Cdd:PHA03095 287 SSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAA----TLNTASVAGGDipsdatrLCVAKVVLRGA 350
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
256-325 |
8.59e-08 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 56.06 E-value: 8.59e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 256 ASTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARHG 325
Cdd:PTZ00322 90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENG 159
|
|
| PHA02716 |
PHA02716 |
CPXV016; CPX019; EVM010; Provisional |
20-301 |
8.77e-08 |
|
CPXV016; CPX019; EVM010; Provisional
Pssm-ID: 165089 [Multi-domain] Cd Length: 764 Bit Score: 56.07 E-value: 8.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 20 LHvaAFLG----DAEIIELLILSGARVNAKDNMWLTPLHRAV--ASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANK 93
Cdd:PHA02716 181 LH--AYLGnmyvDIDILEWLCNNGVNVNLQNNHLITPLHTYLitGNVCASVIKKIIELGGDMDMKCVNGMSPIMTYIINI 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 94 AVKCAEVI----------------------IPLLSSVNVS---------------DRGGRTALHHAAL--NGHMEMVNLL 134
Cdd:PHA02716 259 DNINPEITniyiesldgnkvknipmilhsyITLARNIDISvvysflqpgvklhykDSAGRTCLHQYILrhNISTDIIKLL 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 135 LAKGANINAFDKKDRRALHwaAYMG----------------HLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQ----- 193
Cdd:PHA02716 339 HEYGNDLNEPDNIGNTVLH--TYLSmlsvvnildpetdndiRLDVIQCLISLGADITAVNCLGYTPLTSYICTAQnymyy 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 194 -----------ISVVKH--LLNLGVEIDE---------------INVYGNTALHIACYNGQDAVVNELIDYGANVNQPnN 245
Cdd:PHA02716 417 diidclisdkvLNMVKHriLQDLLIRVDDtpciihhiiakynipTDLYTDEYEPYDSTKIHDVYHCAIIERYNNAVCE-T 495
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 246 SGFTPLHFAAASTHGAL----CLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLI 301
Cdd:PHA02716 496 SGMTPLHVSIISHTNANivmdSFVYLLSIQYNINIPTKNGVTPLMLTMRNNRLSGHQWYI 555
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
386-601 |
8.77e-08 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 56.41 E-value: 8.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 386 AAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIKALVTTGANVNETDDWGRTALHYAAASDMDRNKMIL 465
Cdd:PLN03192 531 TVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 466 gnahdnseelerarevkekdaalclefllqndanpsirdkegynsIHYAAAyghrqclelllertntgfeeSDGGALKSP 545
Cdd:PLN03192 611 ---------------------------------------------YHFASI--------------------SDPHAAGDL 625
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907069410 546 LHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQGASI 601
Cdd:PLN03192 626 LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
84-135 |
1.30e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 48.81 E-value: 1.30e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1907069410 84 TPLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHMEMVNLLL 135
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
610-867 |
1.70e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 54.61 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 610 RTPLHASVINGHTLCLRLLLETADNP--EVVDvkdakGQTPLMLAVAYGHIDAVSLLLEKEA--NVDAVDIVgcTALHRG 685
Cdd:PHA02875 3 QVALCDAILFGELDIARRLLDIGINPnfEIYD-----GISPIKLAMKFRDSEAIKLLMKHGAipDVKYPDIE--SELHDA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 686 IMTGHEECVQMLLEQEA---SILCKDsrGRTPLHYAAARGHATWLNELLQialSEEDCCLKDNQGYTPLHWACYNGNENC 762
Cdd:PHA02875 76 VEEGDVKAVEELLDLGKfadDVFYKD--GMTPLHLATILKKLDIMKLLIA---RGADPDIPNTDKFSPLHLAVMMGDIKG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 763 IEVLLEQK-CFRKFIGNPFTPLHCAIINGH-ESCASLLLGAIDPSIVSCRDDKgrTTLHAAAFGDHAECLQLLLRHDAQV 840
Cdd:PHA02875 151 IELLIDHKaCLDIEDCCGCTPLIIAMAKGDiAICKMLLDSGANIDYFGKNGCV--AALCYAIENNKIDIVRLFIKRGADC 228
|
250 260 270
....*....|....*....|....*....|...
gi 1907069410 841 N---AVDNSGKTALMMAAE---NGQAGAVDILV 867
Cdd:PHA02875 229 NimfMIEGEECTILDMICNmctNLESEAIDALI 261
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
680-723 |
2.10e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 48.42 E-value: 2.10e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1907069410 680 TALHRGIMTGHEECVQMLLEQEASILCKDSRGRTPLHYAAARGH 723
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGN 46
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
451-676 |
2.13e-07 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 54.87 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 451 HYAAASDMDRNKMILGNA--HDNSEELERAREVKEKDAALCLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQClellle 528
Cdd:PLN03192 500 HHKELHDLNVGDLLGDNGgeHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDC------ 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 529 rtntgfeesdggalksplhlaaynghhqaLEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALvNQGASIfvKDNVT 608
Cdd:PLN03192 574 -----------------------------VLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL-YHFASI--SDPHA 621
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907069410 609 KRTPLHASVINGHTLCLRLLLETADNpevVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDI 676
Cdd:PLN03192 622 AGDLLCTAAKRNDLTAMKELLKQGLN---VDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANT 686
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
184-343 |
2.93e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 52.13 E-value: 2.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 184 PLHAAASNGQISVVKHLLNLgveIDEINVYGNTALHiACYNGQDAVVNE---LIDYGANVN-QPNNSGFTPLHFAAASTH 259
Cdd:PHA02859 24 PLFYYVEKDDIEGVKKWIKF---VNDCNDLYETPIF-SCLEKDKVNVEIlkfLIENGADVNfKTRDNNLSALHHYLSFNK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 260 GAL--CLELLVNNGADVNIQSKDGKSPLH--MTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHV-AARHGHELLINTLI 334
Cdd:PHA02859 100 NVEpeILKILIDSGSSITEEDEDGKNLLHmyMCNFNVRINVIKLLIDSGVSFLNKDFDNNNILYSyILFHSDKKIFDFLT 179
|
....*....
gi 1907069410 335 TSGADTAKC 343
Cdd:PHA02859 180 SLGIDINET 188
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
167-221 |
3.61e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 47.73 E-value: 3.61e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907069410 167 LINHG-AEVTCKDKKGYTPLHAAASNGQISVVKHLLNLGVEIDEINVYGNTALHIA 221
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
18-155 |
4.35e-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: 4.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 18 TPLHVAAFLGDAEIIELLILSGARVNA-----------KDNMWL---TPLHRAVASRSEEAVQVLIKHSADVNARDKNWQ 83
Cdd:cd22192 91 TALHIAVVNQNLNLVRELIARGADVVSpratgtffrpgPKNLIYygeHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGN 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 84 TPLH--VAAANKAVKCaEVIIPLLSSV---------NVSDRGGRTALHHAALNGHMEMVNLLLAKganinafdkkdRRAL 152
Cdd:cd22192 171 TVLHilVLQPNKTFAC-QMYDLILSYDkeddlqpldLVPNNQGLTPFKLAAKEGNIVMFQHLVQK-----------RRHI 238
|
...
gi 1907069410 153 HWA 155
Cdd:cd22192 239 QWT 241
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
17-69 |
5.03e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 47.27 E-value: 5.03e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1907069410 17 RTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLI 69
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
214-268 |
5.03e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 47.27 E-value: 5.03e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1907069410 214 GNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHFAAASTHGAlCLELLV 268
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVE-VLKLLL 54
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
352-457 |
5.18e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 53.75 E-value: 5.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 352 HLAALNAHSDccrKLLSSGFEIDTPDTFGRTCLHAA-------AAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANC 424
Cdd:PTZ00322 50 HLEALEATEN---KDATPDHNLTTEEVIDPVVAHMLtvelcqlAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANG 126
|
90 100 110
....*....|....*....|....*....|...
gi 1907069410 425 HFHCIKALVTTGANVNETDDWGRTALHYAAASD 457
Cdd:PTZ00322 127 HVQVVRVLLEFGADPTLLDKDGKTPLELAEENG 159
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
544-770 |
6.37e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 52.96 E-value: 6.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 544 SPLHLAAYNGHHQALEVLLQSLVDLDIRDE--KGRTALY---LAAFKghtecvEALVNQGASIFVKDNVTKRTPLHASVI 618
Cdd:PHA02878 72 TPLHIICKEPNKLGMKEMIRSINKCSVFYTlvAIKDAFNnrnVEIFK------IILTNRYKNIQTIDLVYIDKKSKDDII 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 619 NghTLCLRLLLETADNPEVVDvkDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIVGCTALHRGIMTGHEECVQMLL 698
Cdd:PHA02878 146 E--AEITKLLLSYGADINMKD--RHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILL 221
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907069410 699 EQEASILCKDSRGRTPLHYAAARGHATwlnELLQIALsEEDCCLKDNQ---GYTPLHWACYngNENCIEVLLEQK 770
Cdd:PHA02878 222 ENGASTDARDKCGNTPLHISVGYCKDY---DILKLLL-EHGVDVNAKSyilGLTALHSSIK--SERKLKLLLEYG 290
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
164-236 |
6.80e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 53.36 E-value: 6.80e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907069410 164 VALLINHGAEVTCKDKKGYTPLHAAASNGQISVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDY 236
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
44-173 |
7.41e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 52.98 E-value: 7.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 44 AKDNMWLTPLHRAVasrSEEAVQVLIKHSADVNArdknwqtpLHVAAANKAVKcAEVIIPLLSSVNVSDRGGRTALHHAA 123
Cdd:PTZ00322 56 ATENKDATPDHNLT---TEEVIDPVVAHMLTVEL--------CQLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIAC 123
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1907069410 124 LNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAE 173
Cdd:PTZ00322 124 ANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQC 173
|
|
| 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 1907069410 283 SPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARHGHELLINTLI 334
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
30-146 |
1.04e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 50.59 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 30 EIIELLILSGARVNAK---DNmwLTPLHRAVA---SRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAevIIP 103
Cdd:PHA02859 67 EILKFLIENGADVNFKtrdNN--LSALHHYLSfnkNVEPEILKILIDSGSSITEEDEDGKNLLHMYMCNFNVRIN--VIK 142
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1907069410 104 LLSSVNVS----DRGGRTALH-HAALNGHMEMVNLLLAKGANINAFDK 146
Cdd:PHA02859 143 LLIDSGVSflnkDFDNNNILYsYILFHSDKKIFDFLTSLGIDINETNK 190
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
797-947 |
1.48e-06 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 52.18 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 797 LLLGAIDPSIvscRDDKGRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNSAQADLTV 876
Cdd:PLN03192 544 LLKAKLDPDI---GDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPH 620
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907069410 877 KDKDLntpLHLAISKGHekcaLLILDKIQDESL-INAKNSALQTPLHIAARNGLKVVVEELLAKGACVLAVD 947
Cdd:PLN03192 621 AAGDL---LCTAAKRND----LTAMKELLKQGLnVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
366-470 |
1.71e-06 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 52.18 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 366 LLSSGFEIDTPDTFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPL-------HYAAANCHFHC---------- 428
Cdd:PLN03192 544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnaisakHHKIFRILYHFasisdphaag 623
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907069410 429 --------------IKALVTTGANVNETDDWGRTALHYAAASD-MDRNKMILGNAHD 470
Cdd:PLN03192 624 dllctaakrndltaMKELLKQGLNVDSEDHQGATALQVAMAEDhVDMVRLLIMNGAD 680
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
814-867 |
2.37e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 45.34 E-value: 2.37e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1907069410 814 GRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILV 867
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
711-767 |
2.44e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 45.34 E-value: 2.44e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907069410 711 GRTPLHYAAARGHatwlNELLQIAL-SEEDCCLKDNQGYTPLHWACYNGNENCIEVLL 767
Cdd:pfam13637 1 ELTALHAAAASGH----LELLRLLLeKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
797-873 |
3.31e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 51.05 E-value: 3.31e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907069410 797 LLLGAIDPSivsCRDDKGRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNSAQAD 873
Cdd:PTZ00322 101 LLTGGADPN---CRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCH 174
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
747-799 |
4.14e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 44.57 E-value: 4.14e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1907069410 747 GYTPLHWACYNGNENCIEVLLEQKC-FRKFIGNPFTPLHCAIINGHESCASLLL 799
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGAdINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
695-939 |
4.87e-06 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 50.40 E-value: 4.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 695 QMLLEQEasiLCKDSRGR-TPLHYAAARGHATWLNELLQiaLSEEDCCLKDNQGYTPLHWACYNGNENCIEVLLEqkCFR 773
Cdd:cd22192 3 QMLDELH---LLQQKRISeSPLLLAAKENDVQAIKKLLK--CPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 774 KFIGNPFT--------PLHCAIINGHESCASLLL--GAidpSIVSCRDD-----KGRTTLhaAAFGDHAeclqlllrhda 838
Cdd:cd22192 76 ELVNEPMTsdlyqgetALHIAVVNQNLNLVRELIarGA---DVVSPRATgtffrPGPKNL--IYYGEHP----------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 839 qvnavdnsgktaLMMAAENGQAGAVDILVNSAqADLTVKDKDLNTPLHLAISKGHEKCA------LLILDKIQDE-SLIN 911
Cdd:cd22192 140 ------------LSFAACVGNEEIVRLLIEHG-ADIRAQDSLGNTVLHILVLQPNKTFAcqmydlILSYDKEDDLqPLDL 206
|
250 260
....*....|....*....|....*...
gi 1907069410 912 AKNSALQTPLHIAARNGLKVVVEELLAK 939
Cdd:cd22192 207 VPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
2-270 |
5.20e-06 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 50.05 E-value: 5.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 2 LIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSE--EAVQVLIKHSADV-NAR 78
Cdd:PHA02946 58 LLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEviERINLLVQYGAKInNSV 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 79 DKNWQTPLhVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAAL--NGHMEMVNLLLAKGANINAFDKKDRRALH--W 154
Cdd:PHA02946 138 DEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMsdNPKASTISWMMKLGISPSKPDHDGNTPLHivC 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 155 AAYMGHLDVVALLINhGAEVTCKDKKGYTPLHAAASNGQISvvkHLLNLGVEIDeiNVYGNTALHIACYNGQDAVVNELI 234
Cdd:PHA02946 217 SKTVKNVDIINLLLP-STDVNKQNKFGDSPLTLLIKTLSPA---HLINKLLSTS--NVITDQTVNICIFYDRDDVLEIIN 290
|
250 260 270
....*....|....*....|....*....|....*..
gi 1907069410 235 DYGANVNQPNnsgftplhFAAASTHGAL-CLELLVNN 270
Cdd:PHA02946 291 DKGKQYDSTD--------FKMAVEVGSIrCVKYLLDN 319
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
115-143 |
5.24e-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: 5.24e-06
10 20
....*....|....*....|....*....
gi 1907069410 115 GRTALHHAALNGHMEMVNLLLAKGANINA 143
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
518-757 |
6.62e-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: 6.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 518 GHRQCLELLLertnTGFEESDGGALKSPLHLAAYNGHHQALE---VLLQS---------LVDLDIRDE--KGRTALYLAA 583
Cdd:cd21882 6 GLLECLRWYL----TDSAYQRGATGKTCLHKAALNLNDGVNEaimLLLEAapdsgnpkeLVNAPCTDEfyQGQTALHIAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 584 FKGHTECVEALVNQGASIFVKDNVT--KRTPlhasvingHTLCLRllletadnpevvdvkdakGQTPLMLAVAYGHIDAV 661
Cdd:cd21882 82 ENRNLNLVRLLVENGADVSARATGRffRKSP--------GNLFYF------------------GELPLSLAACTNQEEIV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 662 SLLLE---KEANVDAVDIVGCTALHRGIMTGHEE------CVQM---LLEQEASI-------LCKDSRGRTPLHYAAARG 722
Cdd:cd21882 136 RLLLEngaQPAALEAQDSLGNTVLHALVLQADNTpensafVCQMynlLLSYGAHLdptqqleEIPNHQGLTPLKLAAVEG 215
|
250 260 270
....*....|....*....|....*....|....*...
gi 1907069410 723 HATWLNELLQIALSEEDCCL--KDNQ-GYTPLHWACYN 757
Cdd:cd21882 216 KIVMFQHILQREFSGPYQPLsrKFTEwTYGPVTSSLYD 253
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
133-188 |
7.26e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 44.26 E-value: 7.26e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907069410 133 LLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAA 188
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| TRPV1 |
cd22196 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ... |
115-257 |
8.27e-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: 8.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 115 GRTALHHAALN---GHMEMVNLLL---AKGANINAF------DK--KDRRALHWAAYMGHLDVVALLINHGAEVTC---- 176
Cdd:cd22196 47 GKTCLLKAMLNlhnGQNDTISLLLdiaEKTGNLKEFvnaaytDSyyKGQTALHIAIERRNMHLVELLVQNGADVHArasg 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 177 ------KDKKGY----TPLHAAASNGQISVVKHLLN---LGVEIDEINVYGNTALH----IAcYNGQD------AVVNEL 233
Cdd:cd22196 127 effkkkKGGPGFyfgeLPLSLAACTNQLDIVKFLLEnphSPADISARDSMGNTVLHalveVA-DNTPEntkfvtKMYNEI 205
|
170 180 190
....*....|....*....|....*....|.
gi 1907069410 234 IDYGANVNQ-------PNNSGFTPLHFAAAS 257
Cdd:cd22196 206 LILGAKIRPllkleeiTNKKGLTPLKLAAKT 236
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
781-834 |
8.91e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 43.80 E-value: 8.91e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1907069410 781 TPLHCAIINGHESCASLLLGAidPSIVSCRDDKGRTTLHAAAFGDHAECLQLLL 834
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEK--GADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
619-698 |
1.16e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 49.13 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 619 NGHTLCLRLLLETADNPevvDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIVGCTALHRGIMTGHEECVQMLL 698
Cdd:PTZ00322 92 SGDAVGARILLTGGADP---NCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
197-497 |
1.18e-05 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 48.90 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 197 VKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHFAAASTHGAL-CLELLVNNGADVN 275
Cdd:PHA02946 55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIeRINLLVQYGAKIN 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 276 IQ-SKDGKSPLhMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHvaarhghellintlitsgadtakcgihsmfpLHLA 354
Cdd:PHA02946 135 NSvDEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFGKNHIH-------------------------------RHLM 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 355 ALNAHSDCCRKLLSSGFEIDTPDTFGRTCLHAAAAG--GNVECIKLLQSSgADFHKKDKCGRTPLHYAAANCH-FHCIKA 431
Cdd:PHA02946 183 SDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCSKtvKNVDIINLLLPS-TDVNKQNKFGDSPLTLLIKTLSpAHLINK 261
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907069410 432 LVTTGANVneTDDWGRTALHYaaasdmDRNKMI-----LGNAHDnSEELERAREVkekDAALCLEFLLQND 497
Cdd:PHA02946 262 LLSTSNVI--TDQTVNICIFY------DRDDVLeiindKGKQYD-STDFKMAVEV---GSIRCVKYLLDND 320
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
855-950 |
1.53e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 48.74 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 855 AENGQAGAVDILVNSAqADLTVKDKDLNTPLHLAISKGHEKCALLILDKIQDESLINAKNsalQTPLHIAARNGLKVVVE 934
Cdd:PTZ00322 90 AASGDAVGARILLTGG-ADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDG---KTPLELAEENGFREVVQ 165
|
90
....*....|....*.
gi 1907069410 935 ELLAKGACVLAVDENA 950
Cdd:PTZ00322 166 LLSRHSQCHFELGANA 181
|
|
| PHA02791 |
PHA02791 |
ankyrin-like protein; Provisional |
725-920 |
1.68e-05 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165154 [Multi-domain] Cd Length: 284 Bit Score: 47.73 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 725 TWLNELLQIALSEEDCCLKDNQGYTPLHWACYNGNENCIEVLLEQKCFRKFIGNPFtPLH-CAIINGHESCASLLLGAID 803
Cdd:PHA02791 8 TWKSKQLKSFLSSKDAFKADVHGHSALYYAIADNNVRLVCTLLNAGALKNLLENEF-PLHqAATLEDTKIVKILLFSGMD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 804 PSIVscrDDKGRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSG-KTALMMAAENGQAGAVDILVNSAQA--DLTVkdkd 880
Cdd:PHA02791 87 DSQF---DDKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTGwKTSFYHAVMLNDVSIVSYFLSEIPStfDLAI---- 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1907069410 881 LNTPLHLAISKGHEKCALLILDKIQDeslINAKNSALQTP 920
Cdd:PHA02791 160 LLSCIHITIKNGHVDMMILLLDYMTS---TNTNNSLLFIP 196
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
115-146 |
1.77e-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: 42.28 E-value: 1.77e-05
10 20 30
....*....|....*....|....*....|...
gi 1907069410 115 GRTALHHAAL-NGHMEMVNLLLAKGANINAFDK 146
Cdd:pfam00023 2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
646-869 |
2.15e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 48.06 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 646 QTPLMLAVAYGHIDAVSLLLEKEANVDAVDIVGCTALHRGIMTGHEECVQMLLEQEASILCKDSRGRTPLHYAAARGHAT 725
Cdd:PHA02875 3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 726 WLNELLQIALSEEDCCLKDnqGYTPLHWACYNGNENCIEVLLEQKCfrkfignpftplhcaiinghescaslllgaiDPS 805
Cdd:PHA02875 83 AVEELLDLGKFADDVFYKD--GMTPLHLATILKKLDIMKLLIARGA-------------------------------DPD 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907069410 806 IVSCrdDKgRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNS 869
Cdd:PHA02875 130 IPNT--DK-FSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDS 190
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
186-289 |
2.17e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 48.36 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 186 HAAASnGQISVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHFAAASTHGALcLE 265
Cdd:PTZ00322 88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREV-VQ 165
|
90 100 110
....*....|....*....|....*....|....*..
gi 1907069410 266 LLV-------NNGADVNIQSKDGK------SPLHMTA 289
Cdd:PTZ00322 166 LLSrhsqchfELGANAKPDSFTGKppsledSPISSHH 202
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
849-943 |
3.15e-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: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 849 TALMMAAENGQAGAVDILVNSAQADLTVKDKDLNTPLHLAISKGHEKCALLILDkiQDESLIN-AKNSAL---QTPLHIA 924
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNePMTSDLyqgETALHIA 96
|
90
....*....|....*....
gi 1907069410 925 ARNGLKVVVEELLAKGACV 943
Cdd:cd22192 97 VVNQNLNLVRELIARGADV 115
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
1-72 |
3.21e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 47.97 E-value: 3.21e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907069410 1 MLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHS 72
Cdd:PTZ00322 100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHS 171
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
115-143 |
3.22e-05 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 41.47 E-value: 3.22e-05
10 20
....*....|....*....|....*....
gi 1907069410 115 GRTALHHAALNGHMEMVNLLLAKGANINA 143
Cdd:pfam13606 2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
307-451 |
3.35e-05 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 47.77 E-value: 3.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 307 IDCVDKDGNTPLHVAARHG-HELLINTLITSGA-----DTAkcgihsmfpLHLAALNAH---SDCCRKLLSSGFEIDTPD 377
Cdd:TIGR00870 45 INCPDRLGRSALFVAAIENeNLELTELLLNLSCrgavgDTL---------LHAISLEYVdavEAILLHLLAAFRKSGPLE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 378 ----------TFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKC--------------GRTPLHYAAANCHFHCIKALV 433
Cdd:TIGR00870 116 landqytsefTPGITALHLAAHRQNYEIVKLLLERGASVPARACGdffvksqgvdsfyhGESPLNAAACLGSPSIVALLS 195
|
170
....*....|....*...
gi 1907069410 434 TTGANVNETDDWGRTALH 451
Cdd:TIGR00870 196 EDPADILTADSLGNTLLH 213
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
211-254 |
3.56e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 42.33 E-value: 3.56e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1907069410 211 NVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHFA 254
Cdd:pfam13857 13 DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
68-122 |
3.64e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 42.33 E-value: 3.64e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907069410 68 LIKH-SADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHA 122
Cdd:pfam13857 1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
21-92 |
3.71e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 47.59 E-value: 3.71e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907069410 21 HVAAFlGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAAN 92
Cdd:PTZ00322 88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEEN 158
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
819-912 |
3.84e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 47.59 E-value: 3.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 819 HAAAFGDhAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNSAqADLTVKDKDLNTPLHLAISKGHEKCAL 898
Cdd:PTZ00322 88 QLAASGD-AVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFG-ADPTLLDKDGKTPLELAEENGFREVVQ 165
|
90
....*....|....
gi 1907069410 899 LILDKIQDESLINA 912
Cdd:PTZ00322 166 LLSRHSQCHFELGA 179
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
4-56 |
3.97e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 41.95 E-value: 3.97e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1907069410 4 HKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRA 56
Cdd:pfam13857 4 HGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
233-287 |
4.01e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 41.95 E-value: 4.01e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907069410 233 LIDYG-ANVNQPNNSGFTPLHFAAasTHGAL-CLELLVNNGADVNIQSKDGKSPLHM 287
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAA--KYGALeIVRVLLAYGVDLNLKDEEGLTALDL 55
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
398-453 |
4.05e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 41.95 E-value: 4.05e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907069410 398 LLQSSGADFHKKDKCGRTPLHYAAANCHFHCIKALVTTGANVNETDDWGRTALHYA 453
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
626-758 |
4.23e-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: 47.45 E-value: 4.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 626 RLLLETADNPEVVDV--------KDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVD--------------IVGCTALH 683
Cdd:cd22194 114 RILLAFAEENGILDRfinaeyteEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAkgvffnpkykhegfYFGETPLA 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 684 RGIMTGHEECVQMLLEQEAS-ILCKDSRGRTPLHYAA-----ARGHATWLNELL-QIALSEEDCCL---KDNQGYTPLHW 753
Cdd:cd22194 194 LAACTNQPEIVQLLMEKESTdITSQDSRGNTVLHALVtvaedSKTQNDFVKRMYdMILLKSENKNLetiRNNEGLTPLQL 273
|
....*
gi 1907069410 754 ACYNG 758
Cdd:cd22194 274 AAKMG 278
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
575-629 |
4.33e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 41.88 E-value: 4.33e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1907069410 575 GRTALYLAAFKGHTECVEALVNQGASIFVKDNvTKRTPLHASVINGHTLCLRLLL 629
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDG-NGETALHFAASNGNVEVLKLLL 54
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
649-734 |
4.35e-05 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 47.56 E-value: 4.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 649 LMLAVAYGHIDAVSLLLEKEANVDAVDIVGCTALHRGIMTGHEECVQMLLEQEASILCKDSRGRTPLHYAAARGHATWLN 728
Cdd:PLN03192 529 LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR 608
|
....*.
gi 1907069410 729 ELLQIA 734
Cdd:PLN03192 609 ILYHFA 614
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
610-665 |
4.60e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 41.88 E-value: 4.60e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907069410 610 RTPLHASVINGHTLCLRLLLEtadNPEVVDVKDAKGQTPLMLAVAYGHIDAVSLLL 665
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLE---KGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
832-888 |
4.88e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 41.95 E-value: 4.88e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907069410 832 LLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNsAQADLTVKDKDLNTPLHLA 888
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLA-YGVDLNLKDEEGLTALDLA 56
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
213-241 |
5.00e-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: 5.00e-05
10 20
....*....|....*....|....*....
gi 1907069410 213 YGNTALHIACYNGQDAVVNELIDYGANVN 241
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
|
|
| PHA02884 |
PHA02884 |
ankyrin repeat protein; Provisional |
211-288 |
5.03e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165212 [Multi-domain] Cd Length: 300 Bit Score: 46.51 E-value: 5.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 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 |
5.65e-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: 5.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 188 AASNGqisVVKHLLNlgVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVN--------QP--NNSGF----TPLHF 253
Cdd:cd22194 120 AEENG---ILDRFIN--AEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNahakgvffNPkyKHEGFyfgeTPLAL 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 254 AAASTHGALcLELLVNNGADvNIQSKD--GKSPLHMTAVHGRFTRSQT-----------LIQNGGEIDCV-DKDGNTPLH 319
Cdd:cd22194 195 AACTNQPEI-VQLLMEKEST-DITSQDsrGNTVLHALVTVAEDSKTQNdfvkrmydmilLKSENKNLETIrNNEGLTPLQ 272
|
....*.
gi 1907069410 320 VAARHG 325
Cdd:cd22194 273 LAAKMG 278
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
694-767 |
5.93e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 46.82 E-value: 5.93e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907069410 694 VQMLLEQEASILCKDSRGRTPLHYAAARGHATWLNELLQIAlseEDCCLKDNQGYTPLHWACYNGNENCIEVLL 767
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFG---ADPTLLDKDGKTPLELAEENGFREVVQLLS 168
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
285-379 |
6.03e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 46.82 E-value: 6.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 285 LHMTAVH-------GRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARHGHELLINTLITSGADTAKCGIHSMFPLHLAALN 357
Cdd:PTZ00322 79 AHMLTVElcqlaasGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEEN 158
|
90 100
....*....|....*....|....*...
gi 1907069410 358 AHSDCCRKLLS---SGFEIDT---PDTF 379
Cdd:PTZ00322 159 GFREVVQLLSRhsqCHFELGAnakPDSF 186
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
115-255 |
7.75e-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: 7.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 115 GRTALHHAALNGHMEMVNLLLAKGANINA------FDKKDRralHWAAYMGHldvvallinhgaevtckdkkgyTPLHAA 188
Cdd:cd22194 141 GQTALNIAIERRQGDIVKLLIAKGADVNAhakgvfFNPKYK---HEGFYFGE----------------------TPLALA 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 189 ASNGQISVVKHLL-NLGVEIDEINVYGNTALH---IACYN--GQDAVVNELIDY------GANVNQ-PNNSGFTPLHFAA 255
Cdd:cd22194 196 ACTNQPEIVQLLMeKESTDITSQDSRGNTVLHalvTVAEDskTQNDFVKRMYDMillkseNKNLETiRNNEGLTPLQLAA 275
|
|
| TRPV1-4 |
cd22193 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ... |
115-257 |
8.36e-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: 8.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 115 GRTALHHAALNGHMEMVNLLLAKGANINA------FDKKDRRA--------LHWAAYMGHLDVVALLINHG---AEVTCK 177
Cdd:cd22193 76 GQTALHIAIERRQGDIVALLVENGADVHAhakgrfFQPKYQGEgfyfgelpLSLAACTNQPDIVQYLLENEhqpADIEAQ 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 178 DKKGYTPLHAAasngqisvvkhllnlgVEIDEiNVYGNTALHIACYNGqdavvneLIDYGANVNQP-------NNSGFTP 250
Cdd:cd22193 156 DSRGNTVLHAL----------------VTVAD-NTKENTKFVTRMYDM-------ILIRGAKLCPTveleeirNNDGLTP 211
|
....*..
gi 1907069410 251 LHFAAAS 257
Cdd:cd22193 212 LQLAAKM 218
|
|
| TRPV2 |
cd22197 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ... |
380-533 |
1.02e-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: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 380 GRTCLHAAAAGGNVECIKLLQSSGADFH----------KKDKC---GRTPLHYAAANCHFHCIKALVTTG---ANVNETD 443
Cdd:cd22197 94 GHSALHIAIEKRSLQCVKLLVENGADVHaracgrffqkKQGTCfyfGELPLSLAACTKQWDVVNYLLENPhqpASLQAQD 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 444 DWGRTALHYAAasdmdrnkMILGNAHDNSEELERA-REVKEKDAALCLEFLLQndanpSIRDKEGYNSIHYAAAYGHRQC 522
Cdd:cd22197 174 SLGNTVLHALV--------MIADNSPENSALVIKMyDGLLQAGARLCPTVQLE-----EISNHEGLTPLKLAAKEGKIEI 240
|
170
....*....|.
gi 1907069410 523 LELLLERTNTG 533
Cdd:cd22197 241 FRHILQREFSG 251
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
107-155 |
1.15e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 40.79 E-value: 1.15e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1907069410 107 SVNVSDRGGRTALHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWA 155
Cdd:pfam13857 8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
213-245 |
1.20e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 39.97 E-value: 1.20e-04
10 20 30
....*....|....*....|....*....|....
gi 1907069410 213 YGNTALHIACY-NGQDAVVNELIDYGANVNQPNN 245
Cdd:pfam00023 1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
686-892 |
1.52e-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: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 686 IMTGHEECVQMLLEQeaSILCKDSRGRTPLHYAAARGHATWLNE---LLQIA--------LSEEDCCLKDNQGYTPLHWA 754
Cdd:cd21882 3 ELLGLLECLRWYLTD--SAYQRGATGKTCLHKAALNLNDGVNEAimlLLEAApdsgnpkeLVNAPCTDEFYQGQTALHIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 755 CYNGNENCIEVLLEQKC----------FRKFIGNPF----TPLHCAIINGHESCASLLL-GAIDPSIVSCRDDKGRTTLH 819
Cdd:cd21882 81 IENRNLNLVRLLVENGAdvsaratgrfFRKSPGNLFyfgeLPLSLAACTNQEEIVRLLLeNGAQPAALEAQDSLGNTVLH 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907069410 820 AaafgdhaeclqLLLRHDaqvNAVDNSgKTALMMAAENGQAGAVdiLVNSAQADLTVKDKDLnTPLHLAISKG 892
Cdd:cd21882 161 A-----------LVLQAD---NTPENS-AFVCQMYNLLLSYGAH--LDPTQQLEEIPNHQGL-TPLKLAAVEG 215
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
489-527 |
2.47e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 39.57 E-value: 2.47e-04
10 20 30
....*....|....*....|....*....|....*....
gi 1907069410 489 CLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLL 527
Cdd:pfam13637 16 LLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
413-441 |
2.96e-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: 2.96e-04
10 20
....*....|....*....|....*....
gi 1907069410 413 GRTPLHYAAANCHFHCIKALVTTGANVNE 441
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
581-665 |
3.00e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 44.50 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 581 LAAfKGHTECVEALVNQGASIFVKDnVTKRTPLHASVINGHTLCLRLLLETADNPEVVDvKDakGQTPLMLAVAYGHIDA 660
Cdd:PTZ00322 89 LAA-SGDAVGARILLTGGADPNCRD-YDGRTPLHIACANGHVQVVRVLLEFGADPTLLD-KD--GKTPLELAEENGFREV 163
|
....*
gi 1907069410 661 VSLLL 665
Cdd:PTZ00322 164 VQLLS 168
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
30-202 |
3.01e-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: 44.75 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 30 EIIELLI-----------LSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKN-WQTPLHvaaankavkc 97
Cdd:cd22194 111 EIVRILLafaeengildrFINAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGvFFNPKY---------- 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 98 aeviipllssvnvSDRG---GRTALHHAALNGHMEMVNLLLAKGANINAF-DKKDRRALHwAAYM------GHLDVV--- 164
Cdd:cd22194 181 -------------KHEGfyfGETPLALAACTNQPEIVQLLMEKESTDITSqDSRGNTVLH-ALVTvaedskTQNDFVkrm 246
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1907069410 165 --ALLINHGAEV--TCKDKKGYTPLHAAASNGQISVVKHLLN 202
Cdd:cd22194 247 ydMILLKSENKNleTIRNNEGLTPLQLAAKMGKAEILKYILS 288
|
|
| 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 1907069410 247 GFTPLHFAAASTHGALCLELLVNNGADVNIQSK 279
Cdd:pfam00023 2 GNTPLHLAAGRRGNLEIVKLLLSKGADVNARDK 34
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
176-322 |
3.12e-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: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 176 CKDKKGYTPL-HAAASNGQISVVKHLLNLGVEIDEinvyGNTALHIACYNGQDAVvNELI----------DYGANVNQPN 244
Cdd:TIGR00870 47 CPDRLGRSALfVAAIENENLELTELLLNLSCRGAV----GDTLLHAISLEYVDAV-EAILlhllaafrksGPLELANDQY 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 245 NSGF----TPLHFAAaSTHGALCLELLVNNGADVNIQSKDG---KSPLHMTAVHGRFTRS-----------QTLIQNGGE 306
Cdd:TIGR00870 122 TSEFtpgiTALHLAA-HRQNYEIVKLLLERGASVPARACGDffvKSQGVDSFYHGESPLNaaaclgspsivALLSEDPAD 200
|
170
....*....|....*.
gi 1907069410 307 IDCVDKDGNTPLHVAA 322
Cdd:TIGR00870 201 ILTADSLGNTLLHLLV 216
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
813-928 |
3.45e-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: 3.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 813 KGRTTLHAAAFGDHAECLQLLLRHDAQVNA---------VDNS-----GKTALMMAAENGQAGAVDILVNSAQADLTVKD 878
Cdd:cd22194 140 EGQTALNIAIERRQGDIVKLLIAKGADVNAhakgvffnpKYKHegfyfGETPLALAACTNQPEIVQLLMEKESTDITSQD 219
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907069410 879 KDLNTPLHLAI-----SKGHEKCALLILDKI----QDESLINAKNSALQTPLHIAARNG 928
Cdd:cd22194 220 SRGNTVLHALVtvaedSKTQNDFVKRMYDMIllksENKNLETIRNNEGLTPLQLAAKMG 278
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
413-444 |
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: 38.42 E-value: 3.91e-04
10 20 30
....*....|....*....|....*....|...
gi 1907069410 413 GRTPLHYAAANC-HFHCIKALVTTGANVNETDD 444
Cdd:pfam00023 2 GNTPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
644-675 |
3.99e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 38.42 E-value: 3.99e-04
10 20 30
....*....|....*....|....*....|...
gi 1907069410 644 KGQTPLMLAVA-YGHIDAVSLLLEKEANVDAVD 675
Cdd:pfam00023 1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
319-413 |
4.12e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 44.12 E-value: 4.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 319 HVAARhGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSGFEIDTPDTFGRTCLHAAAAGGNVECIKL 398
Cdd:PTZ00322 88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166
|
90
....*....|....*
gi 1907069410 399 LQSSGADFHKKDKCG 413
Cdd:PTZ00322 167 LSRHSQCHFELGANA 181
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
180-209 |
4.74e-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: 4.74e-04
10 20 30
....*....|....*....|....*....|
gi 1907069410 180 KGYTPLHAAASNGQISVVKHLLNLGVEIDE 209
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| TRPV2 |
cd22197 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ... |
115-255 |
5.32e-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: 5.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 115 GRTALHHAALNGHMEMVNLLLAKGANINA------FDKKDRRALhwaaYMGHLdvvallinhgaevtckdkkgytPLHAA 188
Cdd:cd22197 94 GHSALHIAIEKRSLQCVKLLVENGADVHAracgrfFQKKQGTCF----YFGEL----------------------PLSLA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 189 ASNGQISVVKHLLNLGVE---IDEINVYGNTALHIACYNGQDAVVN---------ELIDYGANVNQ-------PNNSGFT 249
Cdd:cd22197 148 ACTKQWDVVNYLLENPHQpasLQAQDSLGNTVLHALVMIADNSPENsalvikmydGLLQAGARLCPtvqleeiSNHEGLT 227
|
....*.
gi 1907069410 250 PLHFAA 255
Cdd:cd22197 228 PLKLAA 233
|
|
| PHA02791 |
PHA02791 |
ankyrin-like protein; Provisional |
119-250 |
5.52e-04 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165154 [Multi-domain] Cd Length: 284 Bit Score: 43.11 E-value: 5.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 119 LHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGY-TPLHAAASNGQISVV 197
Cdd:PHA02791 65 LHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTGWkTSFYHAVMLNDVSIV 144
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1907069410 198 KHLLNLGVEIDEINVYgNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTP 250
Cdd:PHA02791 145 SYFLSEIPSTFDLAIL-LSCIHITIKNGHVDMMILLLDYMTSTNTNNSLLFIP 196
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
801-854 |
5.71e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 38.87 E-value: 5.71e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1907069410 801 AIDPSIVSCRDDKGRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMA 854
Cdd:pfam13857 3 EHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02743 |
PHA02743 |
Viral ankyrin protein; Provisional |
128-247 |
6.01e-04 |
|
Viral ankyrin protein; Provisional
Pssm-ID: 222925 [Multi-domain] Cd Length: 166 Bit Score: 41.73 E-value: 6.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 128 MEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVV---ALLINHGAEVTCKDKK-GYTPLHAAASNGQISVVKHLL-N 202
Cdd:PHA02743 37 MEVAPFISGDGHLLHRYDHHGRQCTHMVAWYDRANAVmkiELLVNMGADINARELGtGNTLLHIAASTKNYELAEWLCrQ 116
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1907069410 203 LGVEIDEINVYGNTALHIAcYNGQDAVVNE-LIDYGANVNQPNNSG 247
Cdd:PHA02743 117 LGVNLGAINYQHETAYHIA-YKMRDRRMMEiLRANGAVCDDPLSIG 161
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
393-686 |
7.21e-04 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 43.28 E-value: 7.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 393 VECIKLLQSSGADFHKKDKCGRTPL-----HYAAANCHFHCIKALVTTGANVNETDDWGRTALHyaaasdmdrnkMILGN 467
Cdd:PHA02798 51 TDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLY-----------CLLSN 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 468 AHDNSEELerarevkekdaalcLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELllertntgfeesdggalksplh 547
Cdd:PHA02798 120 GYINNLEI--------------LLFMIENGADTTLLDKDGFTMLQVYLQSNHHIDIEI---------------------- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 548 laaynghhqaLEVLLQSLVDLD-IRDEKGRTALYlAAFKGHTECVEA-----LVNQGASIFVKDNVTKRTPLhasvingH 621
Cdd:PHA02798 164 ----------IKLLLEKGVDINtHNNKEKYDTLH-CYFKYNIDRIDAdilklFVDNGFIINKENKSHKKKFM-------E 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907069410 622 TLCLRLLLETADNPEVVDV---------KDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIVGCTALHRGI 686
Cdd:PHA02798 226 YLNSLLYDNKRFKKNILDFifsyidinqVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAF 299
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
15-201 |
7.38e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).
Pssm-ID: 411975 [Multi-domain] Cd Length: 600 Bit Score: 43.33 E-value: 7.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 15 EKRTPLHVAAFLGDAEIIELLILSGARVNAKDN-------------MWLTPLHRAVASRSEEAVQVLIKHSAD---VNAR 78
Cdd:cd21882 72 QGQTALHIAIENRNLNLVRLLVENGADVSARATgrffrkspgnlfyFGELPLSLAACTNQEEIVRLLLENGAQpaaLEAQ 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 79 DKNWQTPLH--VAAANKAVKCAEVIIpllssvnvsdrggrtalhhaalnghmEMVNLLLAKGANINafdkkdrralhwaa 156
Cdd:cd21882 152 DSLGNTVLHalVLQADNTPENSAFVC--------------------------QMYNLLLSYGAHLD-------------- 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907069410 157 ymgHLDVVALLINHgaevtckdkKGYTPLHAAASNGQISVVKHLL 201
Cdd:cd21882 192 ---PTQQLEEIPNH---------QGLTPLKLAAVEGKIVMFQHIL 224
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
213-241 |
7.38e-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: 7.38e-04
10 20
....*....|....*....|....*....
gi 1907069410 213 YGNTALHIACYNGQDAVVNELIDYGANVN 241
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
692-858 |
7.45e-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: 7.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 692 ECVQMLLEQEASILC-KDSRGRTPLHYAAarghatwLNELLQIA--LSEEDCCLKDN-------QGYTPLHWACYNGNEN 761
Cdd:cd22192 31 QAIKKLLKCPSCDLFqRGALGETALHVAA-------LYDNLEAAvvLMEAAPELVNEpmtsdlyQGETALHIAVVNQNLN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 762 CIEVLLEQ-----------KCFRKFIGNPFT----PLHCAIINGHESCASLLL--GAidpSIVScRDDKGRTTLHAAAFG 824
Cdd:cd22192 104 LVRELIARgadvvspratgTFFRPGPKNLIYygehPLSFAACVGNEEIVRLLIehGA---DIRA-QDSLGNTVLHILVLQ 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1907069410 825 DHA----ECLQLLLRHDAQVNAV------DNSGKTALMMAAENG 858
Cdd:cd22192 180 PNKtfacQMYDLILSYDKEDDLQpldlvpNNQGLTPFKLAAKEG 223
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
351-451 |
7.64e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).
Pssm-ID: 411975 [Multi-domain] Cd Length: 600 Bit Score: 43.33 E-value: 7.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 351 LHLAALNAHS---DCCRKLLSSGFEIDTPDTF-----------GRTCLHAAAAGGNVECIKLLQSSGADFH--------K 408
Cdd:cd21882 30 LHKAALNLNDgvnEAIMLLLEAAPDSGNPKELvnapctdefyqGQTALHIAIENRNLNLVRLLVENGADVSaratgrffR 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1907069410 409 KDKC-----GRTPLHYAAANCHFHCIKALVTTG---ANVNETDDWGRTALH 451
Cdd:cd21882 110 KSPGnlfyfGELPLSLAACTNQEEIVRLLLENGaqpAALEAQDSLGNTVLH 160
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
249-301 |
7.66e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 38.41 E-value: 7.66e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1907069410 249 TPLHFAAASTHGAlCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLI 301
Cdd:pfam13637 3 TALHAAAASGHLE-LLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
882-928 |
7.89e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 38.41 E-value: 7.89e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1907069410 882 NTPLHLAISKGHEKCALLILDKIQDeslINAKNSALQTPLHIAARNG 928
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGAD---INAVDGNGETALHFAASNG 45
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
164-320 |
7.91e-04 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 43.12 E-value: 7.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 164 VALLINHGAEVTCKDKKGYTPLHAAASNGQISVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAV--VNELIDYGANVN 241
Cdd:PHA02946 55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIerINLLVQYGAKIN 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 242 QP-NNSGFTPLhfAAASTHGALCLELLVNNGADVNIQSKDGKSPL--HMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPL 318
Cdd:PHA02946 135 NSvDEEGCGPL--LACTDPSERVFKKIMSIGFEARIVDKFGKNHIhrHLMSDNPKASTISWMMKLGISPSKPDHDGNTPL 212
|
..
gi 1907069410 319 HV 320
Cdd:PHA02946 213 HI 214
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
618-740 |
8.51e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 43.35 E-value: 8.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 618 INGHTLCLRLLLETADNP-------EVVDVKDAKgqtplMLAVAYGHIDA------VSLLLEKEANVDAVDIVGCTALHR 684
Cdd:PTZ00322 47 IDTHLEALEATENKDATPdhnltteEVIDPVVAH-----MLTVELCQLAAsgdavgARILLTGGADPNCRDYDGRTPLHI 121
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907069410 685 GIMTGHEECVQMLLEQEASILCKDSRGRTPLHYAAARGhatwLNELLQIALSEEDC 740
Cdd:PTZ00322 122 ACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENG----FREVVQLLSRHSQC 173
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
702-754 |
8.71e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 38.10 E-value: 8.71e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1907069410 702 ASILCKDSRGRTPLHYAAARGHATWLNELLqiaLSEEDCCLKDNQGYTPLHWA 754
Cdd:pfam13857 7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLL---AYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02791 |
PHA02791 |
ankyrin-like protein; Provisional |
492-666 |
1.03e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165154 [Multi-domain] Cd Length: 284 Bit Score: 42.34 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 492 FLLQNDANPSirDKEGYNSIHYAAAYGHRQCLELLLertntgfeesDGGALKS------PLHLAAYNGHHQALEVLLQSL 565
Cdd:PHA02791 17 FLSSKDAFKA--DVHGHSALYYAIADNNVRLVCTLL----------NAGALKNllenefPLHQAATLEDTKIVKILLFSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 566 VDLDIRDEKGRTALYLAAFKGHTECVEALVNQGASIFVKDNVTKRTPL-HASVINGHTLCLRLLLETadnPEVVDVkdAK 644
Cdd:PHA02791 85 MDDSQFDDKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTGWKTSFyHAVMLNDVSIVSYFLSEI---PSTFDL--AI 159
|
170 180
....*....|....*....|..
gi 1907069410 645 GQTPLMLAVAYGHIDAVSLLLE 666
Cdd:PHA02791 160 LLSCIHITIKNGHVDMMILLLD 181
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
663-718 |
1.07e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 38.10 E-value: 1.07e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907069410 663 LLLEKEANVDAVDIVGCTALHRGIMTGHEECVQMLLEQEASILCKDSRGRTPLHYA 718
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
40-89 |
1.10e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 38.10 E-value: 1.10e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1907069410 40 ARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVA 89
Cdd:pfam13857 7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
507-562 |
1.19e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 37.64 E-value: 1.19e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907069410 507 GYNSIHYAAAYGHRQCLELLLERTNTGFEESDGGAlkSPLHLAAYNGHHQALEVLL 562
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGE--TALHFAASNGNVEVLKLLL 54
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
372-420 |
1.32e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 37.71 E-value: 1.32e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1907069410 372 EIDTPDTFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYA 420
Cdd:pfam13857 8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
313-339 |
1.47e-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: 1.47e-03
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
180-209 |
1.47e-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: 1.47e-03
10 20 30
....*....|....*....|....*....|
gi 1907069410 180 KGYTPLHAAASNGQISVVKHLLNLGVEIDE 209
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
164-293 |
1.85e-03 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 42.19 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 164 VALLINHGAEVTCKDKKGYTPLHAAASNGQIS-VVKHLLNlgVEIDEINVYGntalhiacyngqDAV-VNELIDYGANVN 241
Cdd:PTZ00322 44 IARIDTHLEALEATENKDATPDHNLTTEEVIDpVVAHMLT--VELCQLAASG------------DAVgARILLTGGADPN 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1907069410 242 QPNNSGFTPLHFAAASTHGALcLELLVNNGADVNIQSKDGKSPLHMTAVHGR 293
Cdd:PTZ00322 110 CRDYDGRTPLHIACANGHVQV-VRVLLEFGADPTLLDKDGKTPLELAEENGF 160
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
17-47 |
1.90e-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: 1.90e-03
10 20 30
....*....|....*....|....*....|..
gi 1907069410 17 RTPLHVAA-FLGDAEIIELLILSGARVNAKDN 47
Cdd:pfam00023 3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
746-768 |
2.01e-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: 2.01e-03
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
644-673 |
2.05e-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: 2.05e-03
10 20 30
....*....|....*....|....*....|
gi 1907069410 644 KGQTPLMLAVAYGHIDAVSLLLEKEANVDA 673
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| PHA02795 |
PHA02795 |
ankyrin-like protein; Provisional |
99-176 |
2.18e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165157 [Multi-domain] Cd Length: 437 Bit Score: 41.52 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 99 EVIIPLLSSVNVSDRGGRTALHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMG--------HLDVVALLINH 170
Cdd:PHA02795 205 KLCIPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRGsviarretHLKILEILLRE 284
|
....*.
gi 1907069410 171 GAEVTC 176
Cdd:PHA02795 285 PLSIDC 290
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
635-683 |
2.27e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 36.94 E-value: 2.27e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1907069410 635 PEVVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIVGCTALH 683
Cdd:pfam13857 6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
574-606 |
2.32e-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: 2.32e-03
10 20 30
....*....|....*....|....*....|....
gi 1907069410 574 KGRTALYLAAFK-GHTECVEALVNQGASIFVKDN 606
Cdd:pfam00023 1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
695-938 |
2.33e-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: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 695 QMLLEQEAS-ILCKDSRGRTPLHYAAARGHatwlNELLQIALSEEDCclKDNQGYTPLHWACYNGNENCIEVLLEQKCFR 773
Cdd:TIGR00870 35 RDLEEPKKLnINCPDRLGRSALFVAAIENE----NLELTELLLNLSC--RGAVGDTLLHAISLEYVDAVEAILLHLLAAF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 774 KFIGNPF--------------TPLHCAIINGHESCASLLL--GAIDPSIVSCRDDK----------GRTTLHAAAFGDHA 827
Cdd:TIGR00870 109 RKSGPLElandqytseftpgiTALHLAAHRQNYEIVKLLLerGASVPARACGDFFVksqgvdsfyhGESPLNAAACLGSP 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 828 ECLQLLLRHDAQVNAVDNSGKTALMMAAEngqagavdilvnsaQADLTVKDKDLNTPLHLAiskghekcALLILDKIQD- 906
Cdd:TIGR00870 189 SIVALLSEDPADILTADSLGNTLLHLLVM--------------ENEFKAEYEELSCQMYNF--------ALSLLDKLRDs 246
|
250 260 270
....*....|....*....|....*....|..
gi 1907069410 907 ESLINAKNSALQTPLHIAARNGLKVVVEELLA 938
Cdd:TIGR00870 247 KELEVILNHQGLTPLKLAAKEGRIVLFRLKLA 278
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
18-96 |
2.35e-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: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 18 TPLHVAAFLGDAEIIELLILSGARVNAKDN--MWLT------------PLHRAVASRSEEAVQVLIKHSADVNARDKNWQ 83
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLLERGASVPARACgdFFVKsqgvdsfyhgesPLNAAACLGSPSIVALLSEDPADILTADSLGN 209
|
90
....*....|...
gi 1907069410 84 TPLHVAAANKAVK 96
Cdd:TIGR00870 210 TLLHLLVMENEFK 222
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
412-441 |
2.38e-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: 2.38e-03
10 20 30
....*....|....*....|....*....|
gi 1907069410 412 CGRTPLHYAAANCHFHCIKALVTTGANVNE 441
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
151-179 |
2.66e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 36.11 E-value: 2.66e-03
10 20 30
....*....|....*....|....*....|
gi 1907069410 151 ALHWAAYM-GHLDVVALLINHGAEVTCKDK 179
Cdd:pfam00023 5 PLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
380-408 |
2.78e-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: 2.78e-03
10 20
....*....|....*....|....*....
gi 1907069410 380 GRTCLHAAAAGGNVECIKLLQSSGADFHK 408
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| TRPV1-4 |
cd22193 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ... |
338-529 |
3.06e-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: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 338 ADTAK-CGIHSMFPLHlaalNAHSDCCRKLLSSGFEIDTPDTF-----------GRTCLHAAAAGGNVECIKLLQSSGAD 405
Cdd:cd22193 26 SSTGKtCLMKALLNLN----PGTNDTIRILLDIAEKTDNLKRFinaeytdeyyeGQTALHIAIERRQGDIVALLVENGAD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 406 ---------FHKKDK-----CGRTPLHYAAANCHFHCIKALVT---TGANVNETDDWGRTALHYAAasdmdrnkMILGNA 468
Cdd:cd22193 102 vhahakgrfFQPKYQgegfyFGELPLSLAACTNQPDIVQYLLEnehQPADIEAQDSRGNTVLHALV--------TVADNT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907069410 469 HDNSEELERA-REVKEKDAALCLEFLLQndanpSIRDKEGYNSIHYAAAYGHRQCLELLLER 529
Cdd:cd22193 174 KENTKFVTRMyDMILIRGAKLCPTVELE-----EIRNNDGLTPLQLAAKMGKIEILKYILQR 230
|
|
| TRPV1-4 |
cd22193 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ... |
604-716 |
3.16e-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: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 604 KDNVTKRTPLHASVIN---GHTLCLRLLLETAD---------NPEVVDVKdAKGQTPLMLAVAYGHIDAVSLLLEKEANV 671
Cdd:cd22193 24 TESSTGKTCLMKALLNlnpGTNDTIRILLDIAEktdnlkrfiNAEYTDEY-YEGQTALHIAIERRQGDIVALLVENGADV 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907069410 672 DAVD--------------IVGCTALHRGIMTGHEECVQMLLE---QEASILCKDSRGRTPLH 716
Cdd:cd22193 103 HAHAkgrffqpkyqgegfYFGELPLSLAACTNQPDIVQYLLEnehQPADIEAQDSRGNTVLH 164
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
644-673 |
3.42e-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: 3.42e-03
10 20 30
....*....|....*....|....*....|
gi 1907069410 644 KGQTPLMLAVAYGHIDAVSLLLEKEANVDA 673
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
827-943 |
3.49e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 40.74 E-value: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 827 AECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNSAQADLTVKDKDLNTPLHLA-ISKGHEKCALLILDKIQ 905
Cdd:PHA02875 48 SEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLAtILKKLDIMKLLIARGAD 127
|
90 100 110
....*....|....*....|....*....|....*...
gi 1907069410 906 DEslinAKNSALQTPLHIAARNGLKVVVEELLAKGACV 943
Cdd:PHA02875 128 PD----IPNTDKFSPLHLAVMMGDIKGIELLIDHKACL 161
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
360-529 |
3.96e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411978 [Multi-domain] Cd Length: 680 Bit Score: 40.90 E-value: 3.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 360 SDCCRKLLSSGFEidTPDTFGRTCLHAAAAGGNVECIKLLQSSGAD---------FHKKDK-----CGRTPLHYAAANCH 425
Cdd:cd22194 123 NGILDRFINAEYT--EEAYEGQTALNIAIERRQGDIVKLLIAKGADvnahakgvfFNPKYKhegfyFGETPLALAACTNQ 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 426 FHCIKALVTTGA-NVNETDDWGRTALH--YAAASDMDRNKMILGNAHDnseELERAREVKEkdaalcLEfllqndanpSI 502
Cdd:cd22194 201 PEIVQLLMEKEStDITSQDSRGNTVLHalVTVAEDSKTQNDFVKRMYD---MILLKSENKN------LE---------TI 262
|
170 180
....*....|....*....|....*..
gi 1907069410 503 RDKEGYNSIHYAAAYGHRQCLELLLER 529
Cdd:cd22194 263 RNNEGLTPLQLAAKMGKAEILKYILSR 289
|
|
| PHA02884 |
PHA02884 |
ankyrin repeat protein; Provisional |
30-170 |
4.15e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165212 [Multi-domain] Cd Length: 300 Bit Score: 40.35 E-value: 4.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 30 EIIELLILSGARVNAK----DNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQ-TPLHVAAANKAVKCAEVIIPL 104
Cdd:PHA02884 47 DIIDAILKLGADPEAPfplsENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLHGCLKCLEILLSY 126
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907069410 105 LSSVNVSDRGGRTALHHAAL--NGHMEMVnlllAKGANINAFDKKDRRalhwaaYMGHLDVVALLINH 170
Cdd:PHA02884 127 GADINIQTNDMVTPIELALMicNNFLAFM----ICDNEISNFYKHPKK------ILINFDILKILVSH 184
|
|
| PHA02791 |
PHA02791 |
ankyrin-like protein; Provisional |
15-212 |
4.62e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165154 [Multi-domain] Cd Length: 284 Bit Score: 40.03 E-value: 4.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 15 EKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKhsadvnardKNWQTPLHvaaanka 94
Cdd:PHA02791 60 ENEFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGNMQTVKLFVK---------KNWRLMFY------- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 95 vkcaeviipllssvnvSDRGGRTALHHAALNGHMEMVNLLLAKGAniNAFDKKDRRA-LHWAAYMGHLDVVALLINHGAE 173
Cdd:PHA02791 124 ----------------GKTGWKTSFYHAVMLNDVSIVSYFLSEIP--STFDLAILLScIHITIKNGHVDMMILLLDYMTS 185
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1907069410 174 VTCKDKKGYTP-LHAAASNGQISVVKHLLNLGVEIDEINV 212
Cdd:PHA02791 186 TNTNNSLLFIPdIKLAIDNKDLEMLQALFKYDINIYSVNL 225
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
151-176 |
4.77e-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: 35.26 E-value: 4.77e-03
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
266-321 |
5.83e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 35.79 E-value: 5.83e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907069410 266 LLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVA 321
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
543-594 |
6.05e-03 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 40.27 E-value: 6.05e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1907069410 543 KSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEAL 594
Cdd:PTZ00322 116 RTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
574-603 |
6.16e-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: 6.16e-03
10 20 30
....*....|....*....|....*....|
gi 1907069410 574 KGRTALYLAAFKGHTECVEALVNQGASIFV 603
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
866-924 |
7.04e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 35.79 E-value: 7.04e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907069410 866 LVNSAQADLTVKDKDLNTPLHLAISKGHEKCALLILDKIQDeslINAKNSALQTPLHIA 924
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVD---LNLKDEEGLTALDLA 56
|
|
| PHA02791 |
PHA02791 |
ankyrin-like protein; Provisional |
311-399 |
7.31e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165154 [Multi-domain] Cd Length: 284 Bit Score: 39.64 E-value: 7.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 311 DKDGNTPLHVAARHGHELLINTLITSGAdtAKCGIHSMFPLHLAALNAHSDCCRKLLSSGFEIDTPDTFGRTCLHAAAAG 390
Cdd:PHA02791 27 DVHGHSALYYAIADNNVRLVCTLLNAGA--LKNLLENEFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDS 104
|
....*....
gi 1907069410 391 GNVECIKLL 399
Cdd:PHA02791 105 GNMQTVKLF 113
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
813-845 |
7.41e-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: 7.41e-03
10 20 30
....*....|....*....|....*....|....
gi 1907069410 813 KGRTTLHAAA-FGDHAECLQLLLRHDAQVNAVDN 845
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
380-411 |
8.67e-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: 8.67e-03
10 20 30
....*....|....*....|....*....|...
gi 1907069410 380 GRTCLHAAAA-GGNVECIKLLQSSGADFHKKDK 411
Cdd:pfam00023 2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
|
|
| TRPV1-4 |
cd22193 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ... |
214-325 |
8.82e-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: 8.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069410 214 GNTALHIACYNGQDAVVNELIDYGANVN--------QPNNS------GFTPLHFAAASTHGALCLELLVNNGADVNIQSK 279
Cdd:cd22193 76 GQTALHIAIERRQGDIVALLVENGADVHahakgrffQPKYQgegfyfGELPLSLAACTNQPDIVQYLLENEHQPADIEAQ 155
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907069410 280 D--GKSPLHMTAVHGRFTRSQT---------LIQNGGEI-------DCVDKDGNTPLHVAARHG 325
Cdd:cd22193 156 DsrGNTVLHALVTVADNTKENTkfvtrmydmILIRGAKLcptveleEIRNNDGLTPLQLAAKMG 219
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
382-451 |
8.91e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 38.65 E-value: 8.91e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907069410 382 TCLHAAAAggNVECIKLLQSSGADF-HKKDKCGRTPLHYAAA---NCHFHCIKALVTTGANVNETDDWGRTALH 451
Cdd:PHA02859 57 SCLEKDKV--NVEILKFLIENGADVnFKTRDNNLSALHHYLSfnkNVEPEILKILIDSGSSITEEDEDGKNLLH 128
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
51-80 |
9.02e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 34.96 E-value: 9.02e-03
10 20 30
....*....|....*....|....*....|.
gi 1907069410 51 TPLHRAVASR-SEEAVQVLIKHSADVNARDK 80
Cdd:pfam00023 4 TPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
|
|
| |
