|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
74-351 |
3.32e-46 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 163.59 E-value: 3.32e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 74 AFDEANGNGWLPLHKAAVQLNKNILEITMNASEPSTWERTTHNGETALFLAVSSSLLENAHFLLLKGCNPNAKTSEGNSP 153
Cdd:COG0666 11 LLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 154 LLTAVLKDAYDMATLLISHGADVNLRCANERTALHEAAKLGRLDMVKLMLASGAYPDARSSYGFTPLALAAQGGHTGIMQ 233
Cdd:COG0666 91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 234 LLLQKGADVHSQASDSSSVLLEAVRGGNPEAVSLLLEYGADANIPKSSGHLPIHVAADKGHFLALKVLVPVT-DIAAIKK 312
Cdd:COG0666 171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGaDLNAKDK 250
|
250 260 270
....*....|....*....|....*....|....*....
gi 1654220556 313 SGISPVHCAAAGAHPHCLELLIQAGFDVNFMLDQRIRKH 351
Cdd:COG0666 251 DGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
38-301 |
2.56e-45 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 161.28 E-value: 2.56e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 38 EAARLHSFPSDDYKKIAEAIETGKEDALAGFAKYHPAFDEANGNGWLPLHKAAVQLNKNILEITMNASEPSTWERTTHNG 117
Cdd:COG0666 8 LLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 118 ETALFLAVSSSLLENAHFLLLKGCNPNAKTSEGNSPLLTAVLKDAYDMATLLISHGADVNLRCANERTALHEAAKLGRLD 197
Cdd:COG0666 88 NTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 198 MVKLMLASGAYPDARSSYGFTPLALAAQGGHTGIMQLLLQKGADVHSQASDSSSVLLEAVRGGNPEAVSLLLEYGADANI 277
Cdd:COG0666 168 IVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNA 247
|
250 260
....*....|....*....|....
gi 1654220556 278 PKSSGHLPIHVAADKGHFLALKVL 301
Cdd:COG0666 248 KDKDGLTALLLAAAAGAALIVKLL 271
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
130-442 |
2.11e-36 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 137.01 E-value: 2.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 130 LENAHFLLLKGCNPNAKTSEGNSPLLTAVLKDAYDMATLLISHGADVNLRCANERTALHEAAKLGRLDMVKLMLASGAYP 209
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 210 DARSSYGFTPLALAAQGGHTGIMQLLLQKGADVHSQASDSSSVLLEAVRGGNPEAVSLLLEYGADANIPKSSGHLPIHVA 289
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 290 ADKGHflalkvlvpvTDIAaikksgispvhcaaagahphclELLIQAGFDVNfmldqrirkHYDDQRKSALYFAVSNGDL 369
Cdd:COG0666 161 AANGN----------LEIV----------------------KLLLEAGADVN---------ARDNDGETPLHLAAENGHL 199
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1654220556 370 PSVKLLLSAGALPN---QDPVNCLQIALRMGNYELISLLLRHGANVNYFCRVNPLHFPSALQYTLKDEVMLRMLLN 442
Cdd:COG0666 200 EIVKLLLEAGADVNakdNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLAL 275
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
116-343 |
5.73e-21 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 95.44 E-value: 5.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 116 NGETALFLAVSSSLLENAHFLLLKGCNPNAKTSEGNSPLLTAVLKDAYDMATLLISHGADVNLRCANERTALHEAAKLGR 195
Cdd:PHA02875 1 MDQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 196 LDMVKLMLASGAYP-DARSSYGFTPLALAAQGGHTGIMQLLLQKGADVHSQASDSSSVLLEAVRGGNPEAVSLLLEYGAD 274
Cdd:PHA02875 81 VKAVEELLDLGKFAdDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKAC 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1654220556 275 ANIPKSSGHLPIHVAADKGHFLALKVLVPV-TDIAAIKKSGISPVHCAAA-GAHPHCLELLIQAGFDVNFM 343
Cdd:PHA02875 161 LDIEDCCGCTPLIIAMAKGDIAICKMLLDSgANIDYFGKNGCVAALCYAIeNNKIDIVRLFIKRGADCNIM 231
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
169-417 |
1.24e-19 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 91.27 E-value: 1.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 169 LISHGADVNLRCANERTALHEAAKLGRLDMVKLMLASGAYPDARSSYGFTPLALAAQGGHT-----GIMQLLLQKGADVH 243
Cdd:PHA03100 21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 244 SQASDSSSVLLEAV--RGGNPEAVSLLLEYGADANIPKSSGHLPIHvaadkghfLALKVLVPVTDIaaikksgispvhca 321
Cdd:PHA03100 101 APDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLH--------LYLESNKIDLKI-------------- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 322 aagahphcLELLIQAGFDVNFM--LDQRIRKHYDDQRK-----SALYFAVSNGDLPSVKLLLSAGALPN---QDPVNCLQ 391
Cdd:PHA03100 159 --------LKLLIDKGVDINAKnrVNYLLSYGVPINIKdvygfTPLHYAVYNNNPEFVKYLLDLGANPNlvnKYGDTPLH 230
|
250 260
....*....|....*....|....*.
gi 1654220556 392 IALRMGNYELISLLLRHGANVNYFCR 417
Cdd:PHA03100 231 IAILNNNKEIFKLLLNNGPSIKTIIE 256
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
135-377 |
1.48e-18 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 88.54 E-value: 1.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 135 FLLLKGCNPNAKTSEGNSPLLTAVL-KDAYDMATLLISHGADVNLRCANERTALHE--AAKLGRLDMVKLMLASGAYPDA 211
Cdd:PHA03095 68 LLLEAGADVNAPERCGFTPLHLYLYnATTLDVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 212 RSSYGFTPLA--LAAQGGHTGIMQLLLQKGADVHSQASDSSSVL---LEAVRgGNPEAVSLLLEYGADANIPKSSGHLPI 286
Cdd:PHA03095 148 LDLYGMTPLAvlLKSRNANVELLRLLIDAGADVYAVDDRFRSLLhhhLQSFK-PRARIVRELIRAGCDPAATDMLGNTPL 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 287 HVAADKGHFLALKV---LVPVTDIAAIKKSGISPVHCAAAGAHPHCLELLIQAGFDVNfmldqrirkHYDDQRKSALYFA 363
Cdd:PHA03095 227 HSMATGSSCKRSLVlplLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADIN---------AVSSDGNTPLSLM 297
|
250
....*....|....
gi 1654220556 364 VSNGDLPSVKLLLS 377
Cdd:PHA03095 298 VRNNNGRAVRAALA 311
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
94-292 |
1.56e-17 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 84.72 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 94 NKNILEITMNAS--EPSTWERTThngetALFLAVSS---SLLEnahFLLLKGCNPN--AKTSEGNSPLLT---AVLKDAY 163
Cdd:PHA03100 15 VKNIKYIIMEDDlnDYSYKKPVL-----PLYLAKEArniDVVK---ILLDNGADINssTKNNSTPLHYLSnikYNLTDVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 164 DMATLLISHGADVNLRCANERTALHEAA--KLGRLDMVKLMLASGAYPDARSSYGFTPLALAAQGGH--TGIMQLLLQKG 239
Cdd:PHA03100 87 EIVKLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1654220556 240 ADV--------------HSQASD--SSSVLLEAVRGGNPEAVSLLLEYGADANIPKSSGHLPIHVAADK 292
Cdd:PHA03100 167 VDInaknrvnyllsygvPINIKDvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILN 235
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
136-292 |
1.80e-17 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 84.93 E-value: 1.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 136 LLLKGCNPNAKT-SEGNSPLLTAVLKDAYDMATLLISHGADVNLRCANERTALHEAAKLGRLDMVKLMLASGAYPDARSS 214
Cdd:PHA02878 153 LLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 215 YGFTPLALAAQG-GHTGIMQLLLQKGADVHSQASDSS-SVLLEAVRggNPEAVSLLLEYGADANIPKSSGHLPIHVAADK 292
Cdd:PHA02878 233 CGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYILGlTALHSSIK--SERKLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
154-245 |
2.70e-17 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 77.08 E-value: 2.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 154 LLTAVLKDAYDMATLLISHGADVNLRCANERTALHEAAKLGRLDMVKLMLasgAYPDARS-SYGFTPLALAAQGGHTGIM 232
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL---EHADVNLkDNGRTALHYAARSGHLEIV 77
|
90
....*....|...
gi 1654220556 233 QLLLQKGADVHSQ 245
Cdd:pfam12796 78 KLLLEKGADINVK 90
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
144-337 |
4.79e-17 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 83.47 E-value: 4.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 144 NAKTSEGNSPLLTAVLKDAYDMATLLISHGADVNLRCANERTALHEAAKLGRLDMVKLMLASGA------YPDARSSygf 217
Cdd:PHA02874 29 NISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVdtsilpIPCIEKD--- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 218 tplalaaqgghtgIMQLLLQKGADVHSQASDSSSVLLEAVRGGNPEAVSLLLEYGADANIPKSSGHLPIHVAADKGHFLA 297
Cdd:PHA02874 106 -------------MIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDI 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1654220556 298 LKVLVPVTDIAAIKKSGI-SPVHCAAAGAHPHCLELLIQAG 337
Cdd:PHA02874 173 IKLLLEKGAYANVKDNNGeSPLHNAAEYGDYACIKLLIDHG 213
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
53-277 |
2.67e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 81.19 E-value: 2.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 53 IAEAIETGKEDALAGF--AKYHPAFDEANGngWLPLhKAAVQLnKNILEITMNASEPSTWERTTHNGETALFLAVSSSLL 130
Cdd:PHA02875 6 LCDAILFGELDIARRLldIGINPNFEIYDG--ISPI-KLAMKF-RDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 131 ENAHFLLLKGCNPN-AKTSEGNSPLLTAVLKDAYDMATLLISHGADVNLRCANERTALHEAAKLGRLDMVKLMLASGAYP 209
Cdd:PHA02875 82 KAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1654220556 210 DARSSYGFTPLALAAQGGHTGIMQLLLQKGADVHSQASDSSSVLL-EAVRGGNPEAVSLLLEYGADANI 277
Cdd:PHA02875 162 DIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcYAIENNKIDIVRLFIKRGADCNI 230
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
187-277 |
2.19e-15 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 71.69 E-value: 2.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 187 LHEAAKLGRLDMVKLMLASGAYPDARSSYGFTPLALAAQGGHTGIMQLLLQKgADVHSQaSDSSSVLLEAVRGGNPEAVS 266
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLK-DNGRTALHYAARSGHLEIVK 78
|
90
....*....|.
gi 1654220556 267 LLLEYGADANI 277
Cdd:pfam12796 79 LLLEKGADINV 89
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
182-447 |
5.81e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 76.95 E-value: 5.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 182 NERTALHEAAKLGRLDMVKLMLASGAYPDARSSYGFTPLALAaqgghtgimqlllqkgadvhsqasdsssvlleaVRGGN 261
Cdd:PHA02875 1 MDQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLA---------------------------------MKFRD 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 262 PEAVSLLLEYGADANIPKSSGHLPIHVAADKGHFLALKVLVPVTDIA--AIKKSGISPVHCAAAGAHPHCLELLIQAGFD 339
Cdd:PHA02875 48 SEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAddVFYKDGMTPLHLATILKKLDIMKLLIARGAD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 340 VNFMldqrirkhyDDQRKSALYFAVSNGDLPSVKLLLSAGALPN-QDPVNC--LQIALRMGNYELISLLLRHGANVNYFC 416
Cdd:PHA02875 128 PDIP---------NTDKFSPLHLAVMMGDIKGIELLIDHKACLDiEDCCGCtpLIIAMAKGDIAICKMLLDSGANIDYFG 198
|
250 260 270
....*....|....*....|....*....|...
gi 1654220556 417 RvNPLhfPSALQYTLKDEV--MLRMLLNYGYDT 447
Cdd:PHA02875 199 K-NGC--VAALCYAIENNKidIVRLFIKRGADC 228
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
121-212 |
8.24e-15 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 69.76 E-value: 8.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 121 LFLAVSSSLLENAHFLLLKGCNPNAKTSEGNSPLLTAVLKDAYDMATLLISHgADVNLRCaNERTALHEAAKLGRLDMVK 200
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|..
gi 1654220556 201 LMLASGAYPDAR 212
Cdd:pfam12796 79 LLLEKGADINVK 90
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
124-277 |
9.30e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 76.24 E-value: 9.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 124 AVSSSLLENAHFLLLKGCNPNAKTSEGNSPLLTAVLK--DAYDMATLLISHGADVNLRCANERTALHEAAKLGR--LDMV 199
Cdd:PHA03100 80 YNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKIL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 200 KLMLASGAYPDARSS----------------YGFTPLALAAQGGHTGIMQLLLQKGADVHSQASDSSSVLLEAVRGGNPE 263
Cdd:PHA03100 160 KLLIDKGVDINAKNRvnyllsygvpinikdvYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKE 239
|
170
....*....|....
gi 1654220556 264 AVSLLLEYGADANI 277
Cdd:PHA03100 240 IFKLLLNNGPSIKT 253
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
168-407 |
4.62e-14 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 74.29 E-value: 4.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 168 LLISHGADVNLRCANERTALHEAAKLG---RLDMVKLMLASGAYPDARSSYGFTPLALAAQGGHT-GIMQLLLQKGADVH 243
Cdd:PHA03095 32 RLLAAGADVNFRGEYGKTPLHLYLHYSsekVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGADVN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 244 SQaSDSSSVLLEAVRGG---NPEAVSLLLEYGADANIPKSSGHLPIHV-----------------------AADKGHFLA 297
Cdd:PHA03095 112 AK-DKVGRTPLHVYLSGfniNPKVIRLLLRKGADVNALDLYGMTPLAVllksrnanvellrllidagadvyAVDDRFRSL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 298 L---------------KVLVPVTDIAAIKKSGISPVHCAAagAHPHCLELLIQ----AGFDVNfmldqrIRKHYDdqrKS 358
Cdd:PHA03095 191 LhhhlqsfkprarivrELIRAGCDPAATDMLGNTPLHSMA--TGSSCKRSLVLplliAGISIN------ARNRYG---QT 259
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1654220556 359 ALYFAVSNGDLPSVKLLLSAGALPN---QDPVNCLQIALRMGNYELISLLLR 407
Cdd:PHA03095 260 PLHYAAVFNNPRACRRLIALGADINavsSDGNTPLSLMVRNNNGRAVRAALA 311
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
133-444 |
2.41e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 72.79 E-value: 2.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 133 AHFLLLKGCNPNAKTSEGNSPLLTAVLKDAYDMATLLISHGADVNLRCANERTALHEAAKLGRLDMVK------------ 200
Cdd:PHA02876 161 AEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKaiidnrsninkn 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 201 -----------------LMLASGAYPDARSSYGFTPLALAAQGGH-TGIMQLLLQKGADVHSQASDSSSVL-LEAVRGGN 261
Cdd:PHA02876 241 dlsllkairnedletslLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLyLMAKNGYD 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 262 PEAVSLLLEYGADANIPKSSGHLPIHVAA--DKGHFLALKVLVPVTDIAAIKKSGISPVHCAAAGAHPHCLELLIQAGFD 339
Cdd:PHA02876 321 TENIRTLIMLGADVNAADRLYITPLHQAStlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGAD 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 340 VNfMLDQRIrkhyddqrKSALYFAVSnGDLP--SVKLLLSAGA---LPNQDPVNCLQIALRMG-NYELISLLLRHGANVN 413
Cdd:PHA02876 401 IE-ALSQKI--------GTALHFALC-GTNPymSVKTLIDRGAnvnSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVN 470
|
330 340 350
....*....|....*....|....*....|.
gi 1654220556 414 YFCRVNPLHFPSALQYtlkdEVMLRMLLNYG 444
Cdd:PHA02876 471 AINIQNQYPLLIALEY----HGIVNILLHYG 497
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
253-341 |
3.98e-13 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 65.14 E-value: 3.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 253 LLEAVRGGNPEAVSLLLEYGADANIPKSSGHLPIHVAADKGHFLALKVLVPVTDIaAIKKSGISPVHCAAAGAHPHCLEL 332
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV-NLKDNGRTALHYAARSGHLEIVKL 79
|
....*....
gi 1654220556 333 LIQAGFDVN 341
Cdd:pfam12796 80 LLEKGADIN 88
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
231-444 |
5.10e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 71.15 E-value: 5.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 231 IMQLLLQKGADVHSQASDSSSVLLEAVRGGNPEAVSLLLEYGADANIPKSSGHLPIHVAADKGHFLALKVLVpvtdIAAI 310
Cdd:PHA02874 17 IEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI----DNGV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 311 KKSgISPVHCaaagAHPHCLELLIQAGFDVNfmldqrIRkhyDDQRKSALYFAVSNGDLPSVKLLLSAGALPNQDPVNC- 389
Cdd:PHA02874 93 DTS-ILPIPC----IEKDMIKTILDCGIDVN------IK---DAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGc 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1654220556 390 --LQIALRMGNYELISLLLRHGA--NVNYFCRVNPLHFpsALQYtlKDEVMLRMLLNYG 444
Cdd:PHA02874 159 ypIHIAIKHNFFDIIKLLLEKGAyaNVKDNNGESPLHN--AAEY--GDYACIKLLIDHG 213
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
119-321 |
1.59e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 69.61 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 119 TALFLAVSSSLLENAHFLLLKGCNPNAKTSEGNSPLLTAVLKDAYDMATLLISHGADVN---LRCANErtalheaaklgr 195
Cdd:PHA02874 37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSilpIPCIEK------------ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 196 lDMVKLMLASGAYPDARSSYGFTPLALAAQGGHTGIMQLLLQKGADVHSQASDSSSVLLEAVRGGNPEAVSLLLEYGADA 275
Cdd:PHA02874 105 -DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYA 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1654220556 276 NIPKSSGHLPIHVAADKGHFLALKVLVPVTDIAAIK-KSGISPVHCA 321
Cdd:PHA02874 184 NVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKcKNGFTPLHNA 230
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
118-289 |
2.37e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 68.84 E-value: 2.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 118 ETALFLAVSSSLLENAHFLLLKGCNPNAKTSEGNSPLLTAVLKDAYDMATLLISHGADVNLRCANERTALHEAAKLGRLD 197
Cdd:PHA02874 125 KTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYA 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 198 MVKLMLASGAYPDARSSYGFTPLalaaqggHTGIMQ-----LLLQKGADVHSQASDSSSVLLEAVrggNP----EAVSLL 268
Cdd:PHA02874 205 CIKLLIDHGNHIMNKCKNGFTPL-------HNAIIHnrsaiELLINNASINDQDIDGSTPLHHAI---NPpcdiDIIDIL 274
|
170 180
....*....|....*....|.
gi 1654220556 269 LEYGADANIPKSSGHLPIHVA 289
Cdd:PHA02874 275 LYHKADISIKDNKGENPIDTA 295
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
116-290 |
3.94e-12 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 68.51 E-value: 3.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 116 NGETALFLAVSSSLLEN-AHFLLLKGCNPNAKTSEGNSPL---LTAVLKDaYDMATLLISHGADVNLRCANERTALHEAA 191
Cdd:PHA03095 82 CGFTPLHLYLYNATTLDvIKLLIKAGADVNAKDKVGRTPLhvyLSGFNIN-PKVIRLLLRKGADVNALDLYGMTPLAVLL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 192 KLGR--LDMVKLMLASGAYPDARSSYGFTPLALAAQGGHT--GIMQLLLQKGADVHSQASDSSSVLLEAVRGGNPEA--V 265
Cdd:PHA03095 161 KSRNanVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRslV 240
|
170 180
....*....|....*....|....*
gi 1654220556 266 SLLLEYGADANIPKSSGHLPIHVAA 290
Cdd:PHA03095 241 LPLLIAGISINARNRYGQTPLHYAA 265
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
117-289 |
5.78e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 68.17 E-value: 5.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 117 GETALFLAVSSSL-LENAHFLLLKGCNPNAKTSEGNSPLLTAVLKDAY-DMATLLISHGADVNLRCANERTALHEAAKLG 194
Cdd:PHA02876 307 GETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDRNkDIVITLLELGANVNARDYCDKTPIHYAAVRN 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 195 RLDMVKLMLASGAYPDARSSYGFTPLALAAQGGHTGI-MQLLLQKGADVHSQASDSSSVLLEAVRGG-NPEAVSLLLEYG 272
Cdd:PHA02876 387 NVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNG 466
|
170
....*....|....*..
gi 1654220556 273 ADANIPKSSGHLPIHVA 289
Cdd:PHA02876 467 ADVNAINIQNQYPLLIA 483
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
85-242 |
1.24e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 66.61 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 85 PLHKAAVQL-----NKNILEITMNASepSTWERTTHNGETALFLAVSSSL--LENAHFLLLKGCNPNAKTSEGNSpLLTA 157
Cdd:PHA03100 71 PLHYLSNIKynltdVKEIVKLLLEYG--ANVNAPDNNGITPLLYAISKKSnsYSIVEYLLDNGANVNIKNSDGEN-LLHL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 158 VLK-------------------DAYDMATLLISHGADVNLRCANERTALHEAAKLGRLDMVKLMLASGAYPDARSSYGFT 218
Cdd:PHA03100 148 YLEsnkidlkilkllidkgvdiNAKNRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDT 227
|
170 180
....*....|....*....|....
gi 1654220556 219 PLALAAQGGHTGIMQLLLQKGADV 242
Cdd:PHA03100 228 PLHIAILNNNKEIFKLLLNNGPSI 251
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
118-302 |
3.21e-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: 3.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 118 ETALFLAVSSSLLENAHFLLL-KGCNPNAKTSEGNSPLLTAVLKDAYDMATLLISHGAD-VNLRCANE----RTALHEAA 191
Cdd:cd22192 18 ESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMTSDlyqgETALHIAV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 192 KLGRLDMVKLMLASGA--------------YPDARSSYGFTPLALAAQGGHTGIMQLLLQKGADVHSQASDSSSVL---- 253
Cdd:cd22192 98 VNQNLNLVRELIARGAdvvspratgtffrpGPKNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLhilv 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1654220556 254 LEAVRGGNPEAVSLLLEYGADAN------IPKSSGHLPIHVAADKGHFLALKVLV 302
Cdd:cd22192 178 LQPNKTFACQMYDLILSYDKEDDlqpldlVPNNQGLTPFKLAAKEGNIVMFQHLV 232
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
319-413 |
1.01e-10 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 58.20 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 319 HCAAAGAHPHCLELLIQAGFDVNFMldqrirkhyDDQRKSALYFAVSNGDLPSVKLLLSAGALPNQDP-VNCLQIALRMG 397
Cdd:pfam12796 2 HLAAKNGNLELVKLLLENGADANLQ---------DKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNgRTALHYAARSG 72
|
90
....*....|....*.
gi 1654220556 398 NYELISLLLRHGANVN 413
Cdd:pfam12796 73 HLEIVKLLLEKGADIN 88
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
158-446 |
1.10e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 64.31 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 158 VLKDAYDMATLLISHGADVNLRCANERTALHEAAKLGRLDMVKLMLASGAYPDARSSYGFTPLALAAQGGHTGIMQLLLq 237
Cdd:PHA02876 153 IQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII- 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 238 kgaDVHSQASDSSSVLLEAVRGGNPEA----------------------------------VSLLLEYGADANIPKSSGH 283
Cdd:PHA02876 232 ---DNRSNINKNDLSLLKAIRNEDLETslllydagfsvnsiddckntplhhasqapslsrlVPKLLERGADVNAKNIKGE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 284 LPIHVAADKGHFLA-LKVLVPV-TDIAAIKKSGISPVHCAAA-GAHPHCLELLIQAGFDVNfmldqrIRKHYDdqrKSAL 360
Cdd:PHA02876 309 TPLYLMAKNGYDTEnIRTLIMLgADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVN------ARDYCD---KTPI 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 361 YFAVSNGDLPSVKLLLSAGA---LPNQDPVNCLQIALRMGN-YELISLLLRHGANVNYFCR--VNPLHFpsALQYTLKDE 434
Cdd:PHA02876 380 HYAAVRNNVVIINTLLDYGAdieALSQKIGTALHFALCGTNpYMSVKTLIDRGANVNSKNKdlSTPLHY--ACKKNCKLD 457
|
330
....*....|..
gi 1654220556 435 VmLRMLLNYGYD 446
Cdd:PHA02876 458 V-IEMLLDNGAD 468
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
136-289 |
1.55e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 63.44 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 136 LLLKGCNPNAKTSEGNSPLLTAVLKDAYDMATLLISHGADVNLRCANERTALHEAAKLGRLDMVKLMLASGAYPDARSSY 215
Cdd:PHA02874 110 ILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNN 189
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1654220556 216 GFTPLALAAQGGHTGIMQLLLQKGADVHSQASDSSSVLLEAVRgGNPEAVSLLLEyGADANIPKSSGHLPIHVA 289
Cdd:PHA02874 190 GESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII-HNRSAIELLIN-NASINDQDIDGSTPLHHA 261
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
196-448 |
5.37e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 62.00 E-value: 5.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 196 LDMVKLMLASGAYPDARSSYGFTPLALAAQGGHTGIMQLLLQKGADVHSQASDSSSVLLEAVRGGNPEAVSLLLEYGADA 275
Cdd:PHA02876 158 LLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNI 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 276 NIPKSSGHLPIHVAADKGHFLALKVLVPVTDIAAIKKsgiSPVHCAA-AGAHPHCLELLIQAGFDVNfmlDQRIRKhydd 354
Cdd:PHA02876 238 NKNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKN---TPLHHASqAPSLSRLVPKLLERGADVN---AKNIKG---- 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 355 qrKSALYFAVSNG-DLPSVKLLLSAGALPNQ------DPVNclQIALRMGNYELISLLLRHGANVNY--FCRVNPLHFpS 425
Cdd:PHA02876 308 --ETPLYLMAKNGyDTENIRTLIMLGADVNAadrlyiTPLH--QASTLDRNKDIVITLLELGANVNArdYCDKTPIHY-A 382
|
250 260
....*....|....*....|...
gi 1654220556 426 ALQYTLkdeVMLRMLLNYGYDTE 448
Cdd:PHA02876 383 AVRNNV---VIINTLLDYGADIE 402
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
153-446 |
1.21e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 60.66 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 153 PLLTAVLKDAYDMATLLISHGADVNLRCANERTALHEAAKLGRLDMVKLMLASgaYPDARSSYGFTPLALAAQGGHTGIM 232
Cdd:PHA02878 40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRS--INKCSVFYTLVAIKDAFNNRNVEIF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 233 QLLLqkgADVHSQASDSSSVLLEAVRGGN---PEAVSLLLEYGADANI-PKSSGHLPIHVAADKghflalkvlvPVTDIA 308
Cdd:PHA02878 118 KIIL---TNRYKNIQTIDLVYIDKKSKDDiieAEITKLLLSYGADINMkDRHKGNTALHYATEN----------KDQRLT 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 309 aikksgispvhcaaagahphclELLIQAGFDVNFMldqrirkhyDDQRKSALYFAVSNGDLPSVKLLLSAGAlpNQDPVN 388
Cdd:PHA02878 185 ----------------------ELLLSYGANVNIP---------DKTNNSPLHHAVKHYNKPIVHILLENGA--STDARD 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1654220556 389 C-----LQIAL-RMGNYELISLLLRHGANVNYFCRVNPLhfpSALQYTLKDEVMLRMLLNYGYD 446
Cdd:PHA02878 232 KcgntpLHISVgYCKDYDILKLLLEHGVDVNAKSYILGL---TALHSSIKSERKLKLLLEYGAD 292
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
126-274 |
7.60e-09 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 58.34 E-value: 7.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 126 SSSLLENahfLLLKGCNPNAKTSEGNSPLLTAVLKDAYDMATLLISHGADVNLRCANERTALHEAAKLGRLDMVKLM--L 203
Cdd:PLN03192 537 NAALLEE---LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILyhF 613
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1654220556 204 ASGAYPDArssyGFTPLALAAQGGHTGIMQLLLQKGADVHSQASDSSSVLLEAVRGGNPEAVSLLLEYGAD 274
Cdd:PLN03192 614 ASISDPHA----AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGAD 680
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
117-258 |
9.76e-09 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 57.96 E-value: 9.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 117 GETALFLAVSSSLLENAHFLLLKGCNPNAKTSEGNSPLLTAVLKDAYDMATLLISHGADVNLRCANErtALHEAAKLGRL 196
Cdd:PLN03192 558 GRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAGD--LLCTAAKRNDL 635
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1654220556 197 DMVKLMLASGAYPDARSSYGFTPLALAAQGGHTGIMQLLLQKGADVHSQASD---SSSVLLEAVR 258
Cdd:PLN03192 636 TAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDddfSPTELRELLQ 700
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
183-236 |
1.05e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 51.51 E-value: 1.05e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1654220556 183 ERTALHEAAKLGRLDMVKLMLASGAYPDARSSYGFTPLALAAQGGHTGIMQLLL 236
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
360-446 |
1.45e-08 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 52.04 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 360 LYFAVSNGDLPSVKLLLSAGA---LPNQDPVNCLQIALRMGNYELISLLLRHGANVNYFCRVNPLHFpsALQYTLKDevM 436
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGAdanLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRTALHY--AARSGHLE--I 76
|
90
....*....|
gi 1654220556 437 LRMLLNYGYD 446
Cdd:pfam12796 77 VKLLLEKGAD 86
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
166-244 |
3.30e-08 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 56.45 E-value: 3.30e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1654220556 166 ATLLISHGADVNLRCANERTALHEAAKLGRLDMVKLMLASGAYPDARSSYGFTPLALAAQGGHTGIMQLLLQKGADVHS 244
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFE 176
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
140-243 |
4.66e-08 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 55.61 E-value: 4.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 140 GCNPNAKTSEGNSPLLTAV-----LKDAYDMATLLISHGADVNLRCANERTALH---EAAKLGRLDMVKLMLASGAYPDA 211
Cdd:PHA02798 61 GANVNGLDNEYSTPLCTILsnikdYKHMLDIVKILIENGADINKKNSDGETPLYcllSNGYINNLEILLFMIENGADTTL 140
|
90 100 110
....*....|....*....|....*....|....*
gi 1654220556 212 RSSYGFTPLALAAQGGHT---GIMQLLLQKGADVH 243
Cdd:PHA02798 141 LDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDIN 175
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
230-446 |
1.01e-07 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 54.65 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 230 GIMQLLLQKGADVHSQASDSSSVLLEAVRGGNP---EAVSLLLEYGADANIPKSSGHLPIHVaadkghFLALKVLVPVtd 306
Cdd:PHA03095 28 EEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEkvkDIVRLLLEAGADVNAPERCGFTPLHL------YLYNATTLDV-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 307 iaaikksgispvhcaaagahphcLELLIQAGFDVNFMldqrirkhyDDQRKSAL--YFAVSNGDLPSVKLLLSAGALPN- 383
Cdd:PHA03095 100 -----------------------IKLLIKAGADVNAK---------DKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNa 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1654220556 384 --QDPVNCLQIALRMGN--YELISLLLRHGANVNY--FCRVNPLHfpSALQYTLKDEVMLRMLLNYGYD 446
Cdd:PHA03095 148 ldLYGMTPLAVLLKSRNanVELLRLLIDAGADVYAvdDRFRSLLH--HHLQSFKPRARIVRELIRAGCD 214
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
199-281 |
2.61e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 53.36 E-value: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 199 VKLMLASGAYPDARSSYGFTPLALAAQGGHTGIMQLLLQKGADVHSQASDSSSVLLEAVRGGNPEAVSLLLEYG-----A 273
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSqchfeL 177
|
....*...
gi 1654220556 274 DANIPKSS 281
Cdd:PTZ00322 178 GANAKPDS 185
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
116-285 |
2.79e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 53.04 E-value: 2.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 116 NGETALFLAVSSSLLENAHFLLLKGCNPNAKTSEGNSPLLTAVLKDAYDMATLLISHGADVNLRCANERTALHEAAKLGR 195
Cdd:PHA02874 156 NGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 196 lDMVKLMLASGAYPDARSSyGFTPLALAAQ-GGHTGIMQLLLQKGADVHSQASDSSSVLLEAVRGGNPEAVslLLEYGAD 274
Cdd:PHA02874 236 -SAIELLINNASINDQDID-GSTPLHHAINpPCDIDIIDILLYHKADISIKDNKGENPIDTAFKYINKDPV--IKDIIAN 311
|
170
....*....|.
gi 1654220556 275 ANIPKSSGHLP 285
Cdd:PHA02874 312 AVLIKEADKLK 322
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
190-340 |
3.64e-07 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 52.95 E-value: 3.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 190 AAKLGRLDMVKLMLASGAYPDARSSYGFTPLALAAQGGHTGIMQLLLQKGADVHSQASDSSSVLLEAVRGGNPEAVSLLL 269
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY 611
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1654220556 270 EYGADANiPKSSGHLpIHVAADKGHFLALKVLVPV-TDIAAIKKSGISPVHCAAAGAHPHCLELLIQAGFDV 340
Cdd:PLN03192 612 HFASISD-PHAAGDL-LCTAAKRNDLTAMKELLKQgLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
56-146 |
7.92e-07 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 47.03 E-value: 7.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 56 AIETGKEDALAGFAKYHPAFDEANGNGWLPLHKAAVQLNKNILEITMNASEPstweRTTHNGETALFLAVSSSLLENAHF 135
Cdd:pfam12796 4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV----NLKDNGRTALHYAARSGHLEIVKL 79
|
90
....*....|.
gi 1654220556 136 LLLKGCNPNAK 146
Cdd:pfam12796 80 LLEKGADINVK 90
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
85-223 |
8.66e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 51.42 E-value: 8.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 85 PLHKAAVQLNKNILEItmnasepstwertthngetalflavsssLLENahflllkGCNPNAKTSEGNSPLLTAV--LKDa 162
Cdd:PHA02878 204 PLHHAVKHYNKPIVHI----------------------------LLEN-------GASTDARDKCGNTPLHISVgyCKD- 247
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1654220556 163 YDMATLLISHGADVNLRCA-NERTALHEAAKlgRLDMVKLMLASGAYPDARSSYGFTPLALA 223
Cdd:PHA02878 248 YDILKLLLEHGVDVNAKSYiLGLTALHSSIK--SERKLKLLLEYGADINSLNSYKLTPLSSA 307
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
150-203 |
1.35e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 45.34 E-value: 1.35e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1654220556 150 GNSPLLTAVLKDAYDMATLLISHGADVNLRCANERTALHEAAKLGRLDMVKLML 203
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
340-446 |
1.98e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 50.43 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 340 VNFMLDQRIRKH-YDDQRKSALYF-----AVSNGDLPSVKLLLSAGALPN-QDPVNC--LQIAL--RMGNYELISLLLRH 408
Cdd:PHA03100 51 VKILLDNGADINsSTKNNSTPLHYlsnikYNLTDVKEIVKLLLEYGANVNaPDNNGItpLLYAIskKSNSYSIVEYLLDN 130
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1654220556 409 GANVN--YFCRVNPLHFpsALQYTLKDEVMLRMLLNYGYD 446
Cdd:PHA03100 131 GANVNikNSDGENLLHL--YLESNKIDLKILKLLIDKGVD 168
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
116-177 |
5.31e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 48.89 E-value: 5.31e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1654220556 116 NGETALFLAVSSSLLENAHFLLLKGCNPNAKTSEGNSPLLTAVLKDAYDMATLLISHGADVN 177
Cdd:PHA03100 191 YGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
169-223 |
1.28e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 42.72 E-value: 1.28e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1654220556 169 LISHG-ADVNLRCANERTALHEAAKLGRLDMVKLMLASGAYPDARSSYGFTPLALA 223
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
136-318 |
1.36e-05 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 47.74 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 136 LLLKGCNPNAKTSEGNSPLLTAVLKDAYDMATLLISHGADVNLRCANERTALHEAAKLGR--LDMVKLMLASGA-YPDAR 212
Cdd:PHA02946 58 LLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAkINNSV 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 213 SSYGFTPLaLAAQGGHTGIMQLLLQKGADVHSQASDSSSVLLEAVRGGNPEA--VSLLLEYGADANIPKSSGHLPIHVAA 290
Cdd:PHA02946 138 DEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNPKAstISWMMKLGISPSKPDHDGNTPLHIVC 216
|
170 180 190
....*....|....*....|....*....|
gi 1654220556 291 DK--GHFLALKVLVPVTDIAAIKKSGISPV 318
Cdd:PHA02946 217 SKtvKNVDIINLLLPSTDVNKQNKFGDSPL 246
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
229-383 |
1.49e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 47.57 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 229 TGIMQLLLQKGADVHSQASDS-SSVLLEAVRGGNPEAVSLLLEYGADANIPKSSGHLPIHVAADKGHFLALKVLVPV-TD 306
Cdd:PHA02878 147 AEITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENgAS 226
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1654220556 307 IAAIKKSGISPVHCAAAGAHPH-CLELLIQAGFDVNfmLDQRIRKHyddqrkSALYFAVSNGDlpSVKLLLSAGALPN 383
Cdd:PHA02878 227 TDARDKCGNTPLHISVGYCKDYdILKLLLEHGVDVN--AKSYILGL------TALHSSIKSER--KLKLLLEYGADIN 294
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
218-269 |
1.64e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 42.26 E-value: 1.64e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1654220556 218 TPLALAAQGGHTGIMQLLLQKGADVHSQASDSSSVLLEAVRGGNPEAVSLLL 269
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
117-253 |
2.01e-05 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 47.38 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 117 GETALFLAVSSS-LLENAHFLLLKGCNPnaktSEGNSpLLTAVLKDAYD-----MATLLISHGADVNLRCANER------ 184
Cdd:TIGR00870 52 GRSALFVAAIENeNLELTELLLNLSCRG----AVGDT-LLHAISLEYVDaveaiLLHLLAAFRKSGPLELANDQytseft 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 185 ---TALHEAAKLGRLDMVKLMLASGAYPDARS--------------SYGFTPLALAAQGGHTGIMQLLLQKGADVHSQAS 247
Cdd:TIGR00870 127 pgiTALHLAAHRQNYEIVKLLLERGASVPARAcgdffvksqgvdsfYHGESPLNAAACLGSPSIVALLSEDPADILTADS 206
|
....*.
gi 1654220556 248 DSSSVL 253
Cdd:TIGR00870 207 LGNTLL 212
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
86-238 |
2.24e-05 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).
Pssm-ID: 411975 [Multi-domain] Cd Length: 600 Bit Score: 47.18 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 86 LHKAAVQLNKNILEITMN--------------ASEPSTWErtTHNGETALFLAVS-------SSLLENAHFLLLKGCNPN 144
Cdd:cd21882 30 LHKAALNLNDGVNEAIMLlleaapdsgnpkelVNAPCTDE--FYQGQTALHIAIEnrnlnlvRLLVENGADVSARATGRF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 145 AKTSEGNS------PLLTAVLKDAYDMATLLISHGADVNLRCANE---RTALH----------EAAKLGrLDMVKLMLAS 205
Cdd:cd21882 108 FRKSPGNLfyfgelPLSLAACTNQEEIVRLLLENGAQPAALEAQDslgNTVLHalvlqadntpENSAFV-CQMYNLLLSY 186
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1654220556 206 GAYPDARSSY-------GFTPLALAAQGGHTGIMQLLLQK 238
Cdd:cd21882 187 GAHLDPTQQLeeipnhqGLTPLKLAAVEGKIVMFQHILQR 226
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
122-277 |
3.78e-05 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 46.37 E-value: 3.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 122 FLAVSSSLLENAHFLLLKGCNPNaKTSEGNSPLLTAVLKD--AYDMATLLISHGADVNLRCANERTAL-----HEAAKLG 194
Cdd:PHA02798 9 YITFSDNVKLSTVKLLIKSCNPN-EIVNEYSIFQKYLQRDspSTDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 195 RLDMVKLMLASGAYPDARSSYGFTPLALAAQGGHTG---IMQLLLQKGADVHSQASDSSSVLLEAVRGGNP---EAVSLL 268
Cdd:PHA02798 88 MLDIVKILIENGADINKKNSDGETPLYCLLSNGYINnleILLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLL 167
|
....*....
gi 1654220556 269 LEYGADANI 277
Cdd:PHA02798 168 LEKGVDINT 176
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
222-293 |
6.03e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 45.66 E-value: 6.03e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1654220556 222 LAAQGGHTGImQLLLQKGADVHSQASDSSSVLLEAVRGGNPEAVSLLLEYGADANIPKSSGHLPIHVAADKG 293
Cdd:PTZ00322 89 LAASGDAVGA-RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENG 159
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
111-238 |
1.05e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 45.00 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 111 ERTTHnGETALFLAVSSSLLENAHFLLlkGCNP----NAKTSE---GNSPLLTAVLKDAYDMATLLISHGADVnlrcANE 183
Cdd:cd22192 46 QRGAL-GETALHVAALYDNLEAAVVLM--EAAPelvnEPMTSDlyqGETALHIAVVNQNLNLVRELIARGADV----VSP 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 184 RTA------------------LHEAAKLGRLDMVKLMLASGAYPDARSSYG----------------------------- 216
Cdd:cd22192 119 RATgtffrpgpknliyygehpLSFAACVGNEEIVRLLIEHGADIRAQDSLGntvlhilvlqpnktfacqmydlilsydke 198
|
170 180 190
....*....|....*....|....*....|....*.
gi 1654220556 217 --------------FTPLALAAQGGHTGIMQLLLQK 238
Cdd:cd22192 199 ddlqpldlvpnnqgLTPFKLAAKEGNIVMFQHLVQK 234
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
148-293 |
1.31e-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: 44.87 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 148 SEGNSPLLTAVLKD---AYDMATLLISHGAD-------VNLRCANE----RTALHEAAKLGRLDMVKLMLASGAYPDARS 213
Cdd:cd21882 24 ATGKTCLHKAALNLndgVNEAIMLLLEAAPDsgnpkelVNAPCTDEfyqgQTALHIAIENRNLNLVRLLVENGADVSARA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 214 S-------------YGFTPLALAAQGGHTGIMQLLLQKGADVHS-QASDS--SSVL--LEAVRGGNPEAVS-------LL 268
Cdd:cd21882 104 TgrffrkspgnlfyFGELPLSLAACTNQEEIVRLLLENGAQPAAlEAQDSlgNTVLhaLVLQADNTPENSAfvcqmynLL 183
|
170 180 190
....*....|....*....|....*....|..
gi 1654220556 269 LEYGADAN-------IPKSSGHLPIHVAADKG 293
Cdd:cd21882 184 LSYGAHLDptqqleeIPNHQGLTPLKLAAVEG 215
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
285-334 |
1.45e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 39.57 E-value: 1.45e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1654220556 285 PIHVAADKGHFLALKVLVPVT-DIAAIKKSGISPVHCAAAGAHPHCLELLI 334
Cdd:pfam13637 4 ALHAAAASGHLELLRLLLEKGaDINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
316-376 |
1.70e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 39.57 E-value: 1.70e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1654220556 316 SPVHCAAAGAHPHCLELLIQAGFDVNfmldqrirkHYDDQRKSALYFAVSNGDLPSVKLLL 376
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADIN---------AVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
119-170 |
3.13e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 38.79 E-value: 3.13e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1654220556 119 TALFLAVSSSLLENAHFLLLKGCNPNAKTSEGNSPLLTAVLKDAYDMATLLI 170
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
184-253 |
3.75e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411978 [Multi-domain] Cd Length: 680 Bit Score: 43.21 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 184 RTALHEAAKLGRLDMVKLMLASGAYPDARSS--------------YGFTPLALAAQGGHTGIMQLLLQKGAD-VHSQASD 248
Cdd:cd22194 142 QTALNIAIERRQGDIVKLLIAKGADVNAHAKgvffnpkykhegfyFGETPLALAACTNQPEIVQLLMEKESTdITSQDSR 221
|
....*
gi 1654220556 249 SSSVL 253
Cdd:cd22194 222 GNTVL 226
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
250-302 |
6.42e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 38.02 E-value: 6.42e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1654220556 250 SSVLLEAVRGGNPEAVSLLLEYGADANIPKSSGHLPIHVAADKGHFLALKVLV 302
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
142-274 |
7.02e-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: 42.38 E-value: 7.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 142 NPNAKTSEGNSPLLTAVLK-DAYDMATLLISHGADVnlrcANERTALHeAAKLGRLDMVKLMLA--------SGAYPDAR 212
Cdd:TIGR00870 44 NINCPDRLGRSALFVAAIEnENLELTELLLNLSCRG----AVGDTLLH-AISLEYVDAVEAILLhllaafrkSGPLELAN 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 213 SSY------GFTPLALAAQGGHTGIMQLLLQKGADVH----------SQASDS---SSVLLEAVRG-GNPEAVSLLLEYG 272
Cdd:TIGR00870 119 DQYtseftpGITALHLAAHRQNYEIVKLLLERGASVParacgdffvkSQGVDSfyhGESPLNAAAClGSPSIVALLSEDP 198
|
..
gi 1654220556 273 AD 274
Cdd:TIGR00870 199 AD 200
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
141-190 |
8.04e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 37.71 E-value: 8.04e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1654220556 141 CNPNAKTSEGNSPLLTAVLKDAYDMATLLISHGADVNLRCANERTALHEA 190
Cdd:pfam13857 7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
215-243 |
8.50e-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: 36.80 E-value: 8.50e-04
10 20
....*....|....*....|....*....
gi 1654220556 215 YGFTPLALAAQGGHTGIMQLLLQKGADVH 243
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
215-245 |
8.69e-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: 36.88 E-value: 8.69e-04
10 20 30
....*....|....*....|....*....|..
gi 1654220556 215 YGFTPLALAA-QGGHTGIMQLLLQKGADVHSQ 245
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNAR 32
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
358-406 |
9.42e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 37.25 E-value: 9.42e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1654220556 358 SALYFAVSNGDLPSVKLLLSAGALPNQDPVN---CLQIALRMGNYELISLLL 406
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNgetALHFAASNGNVEVLKLLL 54
|
|
| PHA02884 |
PHA02884 |
ankyrin repeat protein; Provisional |
187-289 |
1.15e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165212 [Multi-domain] Cd Length: 300 Bit Score: 41.12 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 187 LHEAAKLGRLDMVKLMLASGAYPDARSSYGF----TPLALAAQGGHTGIMQLLLQKGADVHSQASDSS-SVLLEAVRGGN 261
Cdd:PHA02884 37 LYSSIKFHYTDIIDAILKLGADPEAPFPLSEnsktNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLHGC 116
|
90 100
....*....|....*....|....*...
gi 1654220556 262 PEAVSLLLEYGADANIPKSSGHLPIHVA 289
Cdd:PHA02884 117 LKCLEILLSYGADINIQTNDMVTPIELA 144
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
182-212 |
2.62e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 35.73 E-value: 2.62e-03
10 20 30
....*....|....*....|....*....|..
gi 1654220556 182 NERTALHEAA-KLGRLDMVKLMLASGAYPDAR 212
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNAR 32
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
86-224 |
7.08e-03 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 39.29 E-value: 7.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 86 LHKAAVQLnKNILEITMNasepstWERTTHNGETALFLAVSSSLLEnahflllkgcnpnakTSEGNSPLLTAVLKDAYDM 165
Cdd:TIGR00870 86 LHAISLEY-VDAVEAILL------HLLAAFRKSGPLELANDQYTSE---------------FTPGITALHLAAHRQNYEI 143
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1654220556 166 ATLLISHGADVNLRC-ANE-------------RTALHEAAKLGRLDMVKLMLASGAYPDARSSYGFTPLALAA 224
Cdd:TIGR00870 144 VKLLLERGASVPARAcGDFfvksqgvdsfyhgESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLV 216
|
|
| TRPV2 |
cd22197 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ... |
176-293 |
7.19e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411981 [Multi-domain] Cd Length: 640 Bit Score: 39.07 E-value: 7.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 176 VNLRCANE----RTALHEAAKLGRLDMVKLMLASGAYPDARSS-------------YGFTPLALAAQGGHTGIMQLLLQK 238
Cdd:cd22197 83 VNAQCTDEyyrgHSALHIAIEKRSLQCVKLLVENGADVHARACgrffqkkqgtcfyFGELPLSLAACTKQWDVVNYLLEN 162
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1654220556 239 GADVHS-QASDS--SSVL--LEAVRGGNPEAVSL-------LLEYGADAN-------IPKSSGHLPIHVAADKG 293
Cdd:cd22197 163 PHQPASlQAQDSlgNTVLhaLVMIADNSPENSALvikmydgLLQAGARLCptvqleeISNHEGLTPLKLAAKEG 236
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
234-289 |
7.24e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 35.01 E-value: 7.24e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1654220556 234 LLLQKGADVHSQASDSSSVLLEAVRGGNPEAVSLLLEYGADANIPKSSGHLPIHVA 289
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
314-341 |
7.40e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 34.10 E-value: 7.40e-03
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
98-203 |
7.95e-03 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 39.11 E-value: 7.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220556 98 LEITMNASEPSTWERTTH---NGETALFLAV------SSSLLENAHFLLLKGCNPNAKTSEGNSPLLTAVLKDAYDMATL 168
Cdd:PTZ00322 54 LEATENKDATPDHNLTTEeviDPVVAHMLTVelcqlaASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRV 133
|
90 100 110
....*....|....*....|....*....|....*
gi 1654220556 169 LISHGADVNLRCANERTALHEAAKLGRLDMVKLML 203
Cdd:PTZ00322 134 LLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
388-414 |
8.92e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 34.10 E-value: 8.92e-03
|
| |
