|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
240-558 |
6.20e-52 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 184.77 E-value: 6.20e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 240 DIVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVARVLLDHGAGINTHSNEFKESALTLACYKGHLDMVRFLLEAGADQ 319
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 320 EHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGANLEEVNDEGYTPLMEA 399
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 400 AREGHEEMVALLLAQGANINAQTEETQetaltlaccggfsevadflikagadielgcsTPLMEASQEGHLELVKYLLASG 479
Cdd:COG0666 161 AANGNLEIVKLLLEAGADVNARDNDGE-------------------------------TPLHLAAENGHLEIVKLLLEAG 209
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 380805869 480 ANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGHLCTVQFLISKGANVNRATANNDHT 558
Cdd:COG0666 210 ADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
306-615 |
2.27e-51 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 183.23 E-value: 2.27e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 306 LDMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGANL 385
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 386 EEVNDEGYTPLMEAAREGHEEMVALLLAQGANINAQTEETQetaltlaccggfsevadflikagadielgcsTPLMEASQ 465
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGE-------------------------------TPLHLAAY 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 466 EGHLELVKYLLASGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGHLCTVQFLISKG 545
Cdd:COG0666 130 NGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAG 209
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 546 ANVNrATANNDHTVVSLACAGGHLAVVELLLAHGADPTHRLKDGSTMLIEAAKGGHTNVVSYLLDYPNNV 615
Cdd:COG0666 210 ADVN-AKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
206-493 |
1.24e-49 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 178.22 E-value: 1.24e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 206 LDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVARVLLDHGAGI 285
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 286 NThSNEFKESALTLACYKGHLDMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTL 365
Cdd:COG0666 81 NA-KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 366 AACGGHVELAALLIERGANLEEVNDEGYTPLMEAAREGHEEMVALLLAQGANINAQTEEtQETALTLACCGGFSEVADFL 445
Cdd:COG0666 160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDND-GKTALDLAAENGNLEIVKLL 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 380805869 446 IKAGADIELGC---STPLMEASQEGHLELVKYLLASGANVHATTATGDTAL 493
Cdd:COG0666 239 LEAGADLNAKDkdgLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
76-357 |
1.35e-48 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 175.14 E-value: 1.35e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 76 IGKLSTADGKAFADPEVLRRLTSSVSCALDEAAAALTRMKAENSHNAGQVDTRSLAEACSDGDVNAVRKLLDEGRSVNEH 155
Cdd:COG0666 4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 156 TEEGESLLCLACSAGYYELAQVLLAMHANVEDRGNKGDiTPLMAASSGGYLDIVKLLLLHDADVNSQSATGNTALTYACA 235
Cdd:COG0666 84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGE-TPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 236 GGFVDIVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVARVLLDHGAGINTHsNEFKESALTLACYKGHLDMVRFLLEA 315
Cdd:COG0666 163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAK-DNDGKTALDLAAENGNLEIVKLLLEA 241
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 380805869 316 GADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPAD 357
Cdd:COG0666 242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
990-1283 |
3.53e-48 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 173.99 E-value: 3.53e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 990 ELVSVLIARDAKIEHRDKKGFTPLILAATAGHVGVVEILLDKGGDIEAQSERTKDTPLSLACSGGRQEVVDLLLARGANK 1069
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1070 EHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSRtgSKLGISPLMLAAMNGHVPAVKLLLDMGSDINAQiETNRNTAL 1149
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNAR--DKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQ-DNDGNTPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1150 TLACFQGRAEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAppVPSSRDTALTIAADKGHYKFC 1229
Cdd:COG0666 158 HLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNA--KDNDGKTALDLAAENGNLEIV 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 380805869 1230 ELLIHRGAHIDVRNKKGNTPLWLASNGGHFDVVQLLVQAGADVDAADNRKITPL 1283
Cdd:COG0666 236 KLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
1027-1301 |
1.09e-46 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 169.75 E-value: 1.09e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1027 ILLDKGGDIEAQSERTKDTPLSLACSGGRQEVVDLLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSRT 1106
Cdd:COG0666 5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1107 gsKLGISPLMLAAMNGHVPAVKLLLDMGSDINAQIEtNRNTALTLACFQGRAEVVSLLLDRKANVEHRAKTGLTPLMEAA 1186
Cdd:COG0666 85 --DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDK-DGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1187 SGGYAEVGRVLLDKGADVNAPPvpSSRDTALTIAADKGHYKFCELLIHRGAHIDVRNKKGNTPLWLASNGGHFDVVQLLV 1266
Cdd:COG0666 162 ANGNLEIVKLLLEAGADVNARD--NDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
|
250 260 270
....*....|....*....|....*....|....*
gi 380805869 1267 QAGADVDAADNRKITPLMSAFRKGHVKVVQYLVKE 1301
Cdd:COG0666 240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLA 274
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
966-1250 |
2.74e-46 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 168.59 E-value: 2.74e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 966 VDIDAHTESNHDTALTLACAGGHEELVSVLIARDAKIEHRDKKGFTPLILAATAGHVGVVEILLDKGGDIEAQSERtKDT 1045
Cdd:COG0666 11 LLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG-GNT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1046 PLSLACSGGRQEVVDLLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSRTgsKLGISPLMLAAMNGHVP 1125
Cdd:COG0666 90 LLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQD--NDGNTPLHLAAANGNLE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1126 AVKLLLDMGSDINAQIEtNRNTALTLACFQGRAEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVN 1205
Cdd:COG0666 168 IVKLLLEAGADVNARDN-DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 380805869 1206 APpvPSSRDTALTIAADKGHYKFCELLIHRGAHIDVRNKKGNTPL 1250
Cdd:COG0666 247 AK--DKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
1057-1300 |
2.30e-43 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 160.12 E-value: 2.30e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1057 EVVDLLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSRtgSKLGISPLMLAAMNGHVPAVKLLLDMGSD 1136
Cdd:COG0666 2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALA--DALGALLLLAAALAGDLLVALLLLAAGAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1137 INAQIEtNRNTALTLACFQGRAEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAPPvpSSRDTA 1216
Cdd:COG0666 80 INAKDD-GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQD--NDGNTP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1217 LTIAADKGHYKFCELLIHRGAHIDVRNKKGNTPLWLASNGGHFDVVQLLVQAGADVDAADNRKITPLMSAFRKGHVKVVQ 1296
Cdd:COG0666 157 LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVK 236
|
....
gi 380805869 1297 YLVK 1300
Cdd:COG0666 237 LLLE 240
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
65-330 |
1.69e-41 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 154.73 E-value: 1.69e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 65 ARLEALLEAAGIGKLSTADGKAFADPEVLRRLTSSVSCALDEAAAALTRMKAENSHNAGQVDTRSLAEACSDGDVNAVRK 144
Cdd:COG0666 26 LAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 145 LLDEGRSVNEHTEEGESLLCLACSAGYYELAQVLLAMHANVEDRGNKGDiTPLMAASSGGYLDIVKLLLLHDADVNSQSA 224
Cdd:COG0666 106 LLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGN-TPLHLAAANGNLEIVKLLLEAGADVNARDN 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 225 TGNTALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVARVLLDHGAGINtHSNEFKESALTLACYKG 304
Cdd:COG0666 185 DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN-AKDKDGLTALLLAAAAG 263
|
250 260
....*....|....*....|....*.
gi 380805869 305 HLDMVRFLLEAGADQEHKTDEMHTAL 330
Cdd:COG0666 264 AALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
1091-1300 |
3.08e-37 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 142.40 E-value: 3.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1091 IIKILLNAGAEINSRTGSKLGISPLMLAAMNGHVPAVKLLLDMGSDINAQIEtNRNTALTLACFQGRAEVVSLLLDRKAN 1170
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADA-LGALLLLAAALAGDLLVALLLLAAGAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1171 VEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAppVPSSRDTALTIAADKGHYKFCELLIHRGAHIDVRNKKGNTPL 1250
Cdd:COG0666 80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNA--RDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 380805869 1251 WLASNGGHFDVVQLLVQAGADVDAADNRKITPLMSAFRKGHVKVVQYLVK 1300
Cdd:COG0666 158 HLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLE 207
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
132-452 |
6.12e-26 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 113.20 E-value: 6.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 132 EACSDGDVNAVRKLLDEGRSVNEHTEEGESLLC--LACSAG-YYELAQVLLAMHANVedrgNKGDI---TPLMA-ASSGG 204
Cdd:PHA03095 20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHlyLHYSSEkVKDIVRLLLEAGADV----NAPERcgfTPLHLyLYNAT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 205 YLDIVKLLLLHDADVNSQSATGNTALtYACAGGF---VDIVKVLLNEGANIEDHNENGHTPL---MEAASAgHVEVARVL 278
Cdd:PHA03095 96 TLDVIKLLIKAGADVNAKDKVGRTPL-HVYLSGFninPKVIRLLLRKGADVNALDLYGMTPLavlLKSRNA-NVELLRLL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 279 LDHGAGI-----------NTHSNEFKESAltlacykghlDMVRFLLEAGADQEHKTDEMHTALMEACMDGHVE--VARLL 345
Cdd:PHA03095 174 IDAGADVyavddrfrsllHHHLQSFKPRA----------RIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 346 LDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGANLEEVNDEGYTPLMEAAREGHEEMVALLLAQGANINA----- 420
Cdd:PHA03095 244 LIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETvaatl 323
|
330 340 350
....*....|....*....|....*....|....*.
gi 380805869 421 ----QTEETQETALTLACcggfseVADFLIKAGADI 452
Cdd:PHA03095 324 ntasVAGGDIPSDATRLC------VAKVVLRGAFSL 353
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
1045-1333 |
7.33e-26 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 112.07 E-value: 7.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1045 TPLSLACSGGRQEVVDLLLARGANKEHRNVSDYTPLSLAASGGYV-----NIIKILLNAGAEINSrtGSKLGISPLMLAA 1119
Cdd:PHA03100 37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNA--PDNNGITPLLYAI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1120 MN--GHVPAVKLLLDMGSDINAqietnrntaltlacfqgraevvsllldrkanvehRAKTGLTPLMEAASGGYA--EVGR 1195
Cdd:PHA03100 115 SKksNSYSIVEYLLDNGANVNI----------------------------------KNSDGENLLHLYLESNKIdlKILK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1196 VLLDKGADVNAppvpssrdtaltiaADKghykfCELLIHRGAHIDVRNKKGNTPLWLASNGGHFDVVQLLVQAGADVDAA 1275
Cdd:PHA03100 161 LLIDKGVDINA--------------KNR-----VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLV 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 380805869 1276 DNRKITPLMSAFRKGHVkvvqYLVKEVNQFPSDIECM---------RYIATITDKELLKKCHQCVET 1333
Cdd:PHA03100 222 NKYGDTPLHIAILNNNK----EIFKLLLNNGPSIKTIietllyfkdKDLNTITKIKMLKKSIMYMFL 284
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
339-517 |
7.11e-25 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 109.37 E-value: 7.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 339 VEVARLLLDSGAQVNMPADSFESPLTLAACGGHV-----ELAALLIERGANLEEVNDEGYTPLMEAARE--GHEEMVALL 411
Cdd:PHA03100 48 IDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 412 LAQGANINAQTEeTQETALTLA--CCGGFSEVADFLIKAGADI----------ELGC---------STPLMEASQEGHLE 470
Cdd:PHA03100 128 LDNGANVNIKNS-DGENLLHLYleSNKIDLKILKLLIDKGVDInaknrvnyllSYGVpinikdvygFTPLHYAVYNNNPE 206
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 380805869 471 LVKYLLASGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEH 517
Cdd:PHA03100 207 FVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
990-1295 |
9.01e-25 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 109.73 E-value: 9.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 990 ELVSVLIARDAKIEHRDKKGFTPL-ILAATAGHVG--VVEILLDKGGDIEAQsERTKDTPL-SLACSGGRQEVVDLLLAR 1065
Cdd:PHA03095 28 EEVRRLLAAGADVNFRGEYGKTPLhLYLHYSSEKVkdIVRLLLEAGADVNAP-ERCGFTPLhLYLYNATTLDVIKLLIKA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1066 GANKEHRNVSDYTPLSLAASGGYVN--IIKILLNAGAEINSRtgSKLGISPLMLAAMNGHVPA--VKLLLDMGSDINAqI 1141
Cdd:PHA03095 107 GADVNAKDKVGRTPLHVYLSGFNINpkVIRLLLRKGADVNAL--DLYGMTPLAVLLKSRNANVelLRLLIDAGADVYA-V 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1142 ETNRNTALTLAC--FQGRAEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRV--LLDKGADVNAppvpssrdtal 1217
Cdd:PHA03095 184 DDRFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINA----------- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1218 tiaadkghykfcellihrgahidvRNKKGNTPLWLAS---NGGHFDvvqLLVQAGADVDAADNRKITPLMSAFRKGHVKV 1294
Cdd:PHA03095 253 ------------------------RNRYGQTPLHYAAvfnNPRACR---RLIALGADINAVSSDGNTPLSLMVRNNNGRA 305
|
.
gi 380805869 1295 V 1295
Cdd:PHA03095 306 V 306
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
197-287 |
1.80e-23 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 95.95 E-value: 1.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 197 LMAASSGGYLDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANieDHNENGHTPLMEAASAGHVEVAR 276
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78
|
90
....*....|.
gi 380805869 277 VLLDHGAGINT 287
Cdd:pfam12796 79 LLLEKGADINV 89
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
118-515 |
6.61e-23 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 105.53 E-value: 6.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 118 NSHNAGQVDTRSLAEACSDGDV--NAVRKLLDEGRSVNEHTEEGESLLclacsagyyelAQVLLAMHANVedrgNKGDI- 194
Cdd:PHA02876 113 NKHKLDEACIHILKEAISGNDIhyDKINESIEYMKLIKERIQQDELLI-----------AEMLLEGGADV----NAKDIy 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 195 --TPLMAASSGGYLDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANIedhNENGHTpLMEAASAGHV 272
Cdd:PHA02876 178 ciTPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNI---NKNDLS-LLKAIRNEDL 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 273 EVARVLLDHGAGINThSNEFKESALTLACYKGHLD-MVRFLLEAGADQEHKTDEMHTALMEACMDGH-VEVARLLLDSGA 350
Cdd:PHA02876 254 ETSLLLYDAGFSVNS-IDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGA 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 351 QVNMPADSFESPLTLAAC-GGHVELAALLIERGANLEEVNDEGYTPLMEAAREGHEEMVALLLAQGANINAQTEETQeTA 429
Cdd:PHA02876 333 DVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIG-TA 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 430 LTLACCGG--FSEVADfLIKAGADIELG---CSTPLMEASQEG-HLELVKYLLASGANVHATTATGDTALTYACenGHTD 503
Cdd:PHA02876 412 LHFALCGTnpYMSVKT-LIDRGANVNSKnkdLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHG 488
|
410
....*....|..
gi 380805869 504 VADVLLQAGADL 515
Cdd:PHA02876 489 IVNILLHYGAEL 500
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
181-420 |
8.87e-23 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 102.82 E-value: 8.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 181 MHANVEDRGNKGDITPLMAASSGGYLDIVKLLLLHDADVNSQSATGNTALTYACAGGFV-----DIVKVLLNEGANIEDH 255
Cdd:PHA03100 23 MEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 256 NENGHTPLMEAASA--GHVEVARVLLDHGAGINTHSNEFKES-ALTLACYKGHLDMVRFLLEAGADQEHKTDemhtalme 332
Cdd:PHA03100 103 DNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLlHLYLESNKIDLKILKLLIDKGVDINAKNR-------- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 333 acmdghVEvarLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGANLEEVNDEGYTPLMEAAREGHEEMVALLL 412
Cdd:PHA03100 175 ------VN---YLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLL 245
|
....*...
gi 380805869 413 AQGANINA 420
Cdd:PHA03100 246 NNGPSIKT 253
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
288-596 |
5.71e-22 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 101.25 E-value: 5.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 288 HSNEFKESAL---TLACYKGHLDMVRFLLEAGADQEHK----TDEMHTALMEACMDGhVEVARLLLDSGAQVNMPADSFE 360
Cdd:PHA03095 6 SVDIIMEAALydyLLNASNVTVEEVRRLLAAGADVNFRgeygKTPLHLYLHYSSEKV-KDIVRLLLEAGADVNAPERCGF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 361 SPLTLAACGGHVE-LAALLIERGANLEEVNDEGYTPLMEAAR--EGHEEMVALLLAQGANINAQTeetqetaltlacCGG 437
Cdd:PHA03095 85 TPLHLYLYNATTLdVIKLLIKAGADVNAKDKVGRTPLHVYLSgfNINPKVIRLLLRKGADVNALD------------LYG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 438 FSEVADFLIKAGADIELgcstplmeasqeghlelVKYLLASGANVHATTATGDTALTYACENGHTDVADV--LLQAGADL 515
Cdd:PHA03095 153 MTPLAVLLKSRNANVEL-----------------LRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRARIVreLIRAGCDP 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 516 EHESEGGRTPLMKAArAGHLCT---VQFLISKGANVNrATANNDHTVVSLACAGGHLAVVELLLAHGADPTHRLKDGSTM 592
Cdd:PHA03095 216 AATDMLGNTPLHSMA-TGSSCKrslVLPLLIAGISIN-ARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTP 293
|
....
gi 380805869 593 LIEA 596
Cdd:PHA03095 294 LSLM 297
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
460-550 |
1.09e-21 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 90.56 E-value: 1.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 460 LMEASQEGHLELVKYLLASGANVHATTATGDTALTYACENGHTDVADVLLQaGADLEHESEgGRTPLMKAARAGHLCTVQ 539
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVK 78
|
90
....*....|.
gi 380805869 540 FLISKGANVNR 550
Cdd:pfam12796 79 LLLEKGADINV 89
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
230-322 |
4.29e-21 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 89.02 E-value: 4.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 230 LTYACAGGFVDIVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVARVLLDHgagINTHSNEFKESALTLACYKGHLDMV 309
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLEIV 77
|
90
....*....|...
gi 380805869 310 RFLLEAGADQEHK 322
Cdd:pfam12796 78 KLLLEKGADINVK 90
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
1005-1241 |
1.13e-20 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 96.66 E-value: 1.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1005 RDKKGFTPLILAATAGHVGVVEILLDKGGDIeAQSERTKDTPLSLACSGGR-----QEVVDLLLARGANKEHRNVSDYTP 1079
Cdd:PHA03100 31 SYKKPVLPLYLAKEARNIDVVKILLDNGADI-NSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1080 LSLAASG--GYVNIIKILLNAGAEINSRTgsKLGISPLMLAAMNGHV--PAVKLLLDMGSDINAqieTNRntaltlacfq 1155
Cdd:PHA03100 110 LLYAISKksNSYSIVEYLLDNGANVNIKN--SDGENLLHLYLESNKIdlKILKLLIDKGVDINA---KNR---------- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1156 graevVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAppVPSSRDTALTIAADKGHYKFCELLIHR 1235
Cdd:PHA03100 175 -----VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNL--VNKYGDTPLHIAILNNNKEIFKLLLNN 247
|
....*.
gi 380805869 1236 GAHIDV 1241
Cdd:PHA03100 248 GPSIKT 253
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
241-611 |
3.06e-20 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 97.06 E-value: 3.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 241 IVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVARVLLDHGAGINTHSNEfKESALTLACYKGHLDMVRFLLeagaDQE 320
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALD-DLSVLECAVDSKNIDTIKAII----DNR 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 321 HKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHV-ELAALLIERGANLEEVNDEGYTPLMEA 399
Cdd:PHA02876 235 SNINKNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLM 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 400 AREGHE-EMVALLLAQGANINAqteetqetaltlaccggfsevADFLIkagadielgcSTPLMEASQ-EGHLELVKYLLA 477
Cdd:PHA02876 315 AKNGYDtENIRTLIMLGADVNA---------------------ADRLY----------ITPLHQASTlDRNKDIVITLLE 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 478 SGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGH-LCTVQFLISKGANVNraTANND 556
Cdd:PHA02876 364 LGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNpYMSVKTLIDRGANVN--SKNKD 441
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 380805869 557 -HTVVSLACAGG-HLAVVELLLAHGADPTH-RLKDGSTMLIEAakgGHTNVVSYLLDY 611
Cdd:PHA02876 442 lSTPLHYACKKNcKLDVIEMLLDNGADVNAiNIQNQYPLLIAL---EYHGIVNILLHY 496
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
142-355 |
3.35e-20 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 95.12 E-value: 3.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 142 VRKLLDEGRSVNEHTEEGESLLCLACSAGYY-----ELAQVLLAMHANVEDRGNKGdITPLMAASSG--GYLDIVKLLLL 214
Cdd:PHA03100 51 VKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNG-ITPLLYAISKksNSYSIVEYLLD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 215 HDADVNSQSATGNTALTYACAGGFVD--IVKVLLNEGAN----------------IEDHNENGHTPLMEAASAGHVEVAR 276
Cdd:PHA03100 130 NGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDinaknrvnyllsygvpINIKDVYGFTPLHYAVYNNNPEFVK 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 277 VLLDHGAGINThSNEFKESALTLACYKGHLDMVRFLLEAGADQEH--------KTDEMHTALMEAcMDGHVEVARLLLDS 348
Cdd:PHA03100 210 YLLDLGANPNL-VNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTiietllyfKDKDLNTITKIK-MLKKSIMYMFLLDP 287
|
....*..
gi 380805869 349 GAQVNMP 355
Cdd:PHA03100 288 GFYKNRK 294
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
330-421 |
3.44e-20 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 86.32 E-value: 3.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 330 LMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGANleEVNDEGYTPLMEAAREGHEEMVA 409
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78
|
90
....*....|..
gi 380805869 410 LLLAQGANINAQ 421
Cdd:pfam12796 79 LLLEKGADINVK 90
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
1115-1206 |
3.44e-20 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 86.32 E-value: 3.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1115 LMLAAMNGHVPAVKLLLDMGSDINAQiETNRNTALTLACFQGRAEVVSLLLDrKANVEHRAKtGLTPLMEAASGGYAEVG 1194
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQ-DKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIV 77
|
90
....*....|..
gi 380805869 1195 RVLLDKGADVNA 1206
Cdd:pfam12796 78 KLLLEKGADINV 89
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
228-526 |
1.03e-19 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 93.87 E-value: 1.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 228 TALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVARVLLDHGagINThsnefkeSALTLACYKGhlD 307
Cdd:PHA02874 37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG--VDT-------SILPIPCIEK--D 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 308 MVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGANLEE 387
Cdd:PHA02874 106 MIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 388 VNDEGYTPLMEAAREGHEEMVALLLAQGANINAQteetqetaltlaCCGGFsevadflikagadielgcsTPLMEASQeg 467
Cdd:PHA02874 186 KDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNK------------CKNGF-------------------TPLHNAII-- 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 380805869 468 HLELVKYLLASGANVHATTATGDTALTYA----CEnghTDVADVLLQAGADLEHESEGGRTPL 526
Cdd:PHA02874 233 HNRSAIELLINNASINDQDIDGSTPLHHAinppCD---IDIIDILLYHKADISIKDNKGENPI 292
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
263-353 |
2.65e-19 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 84.01 E-value: 2.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 263 LMEAASAGHVEVARVLLDHGAGINTHsNEFKESALTLACYKGHLDMVRFLLEaGADQEHKTDEMhTALMEACMDGHVEVA 342
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQ-DKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNGR-TALHYAARSGHLEIV 77
|
90
....*....|.
gi 380805869 343 RLLLDSGAQVN 353
Cdd:pfam12796 78 KLLLEKGADIN 88
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
198-509 |
6.86e-19 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 91.62 E-value: 6.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 198 MAASSGGYLDIVKLLLLHDADVNSQSATGNTALTY--ACAGGFV-DIVKVLLNEGANIEDHNENGHTPLMeaasaghvev 274
Cdd:PHA03095 19 LLNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLylHYSSEKVkDIVRLLLEAGADVNAPERCGFTPLH---------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 275 arvlldhgaginthsnefkesalTLACYKGHLDMVRFLLEAGADQEHKTDEMHTALmEACMDG---HVEVARLLLDSGAQ 351
Cdd:PHA03095 89 -----------------------LYLYNATTLDVIKLLIKAGADVNAKDKVGRTPL-HVYLSGfniNPKVIRLLLRKGAD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 352 VNmpaDSFESPLTLAAC-----GGHVELAALLIERGANLEEVNDEGYTPL---MEAAREgHEEMVALLLAQGANINAqTE 423
Cdd:PHA03095 145 VN---ALDLYGMTPLAVllksrNANVELLRLLIDAGADVYAVDDRFRSLLhhhLQSFKP-RARIVRELIRAGCDPAA-TD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 424 ETQETALTLACCGGF---SEVADFLIkAGADIE----LGcSTPLMEASQEGHLELVKYLLASGANVHATTATGDTALTYA 496
Cdd:PHA03095 220 MLGNTPLHSMATGSSckrSLVLPLLI-AGISINarnrYG-QTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLM 297
|
330
....*....|...
gi 380805869 497 CENGHTDVADVLL 509
Cdd:PHA03095 298 VRNNNGRAVRAAL 310
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
1080-1174 |
1.25e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 82.09 E-value: 1.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1080 LSLAASGGYVNIIKILLNAGAEINSRTgsKLGISPLMLAAMNGHVPAVKLLLDMgsdINAQIETNRNTALTLACFQGRAE 1159
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQD--KNGRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLE 75
|
90
....*....|....*
gi 380805869 1160 VVSLLLDRKANVEHR 1174
Cdd:pfam12796 76 IVKLLLEKGADINVK 90
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
264-577 |
4.33e-18 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 88.93 E-value: 4.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 264 MEAASAGHVEVARVLLDHGAGINtHSNEFKESALTLACYKGH---LDMVRFLLEAGADQEHKTDEMHTAL-MEACMDGHV 339
Cdd:PHA03095 19 LLNASNVTVEEVRRLLAAGADVN-FRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLhLYLYNATTL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 340 EVARLLLDSGAQVNMPADSFESPLTLAACGG--HVELAALLIERGANLEEVNDEGYTPLMeaaregheemvALLLAQGAN 417
Cdd:PHA03095 98 DVIKLLIKAGADVNAKDKVGRTPLHVYLSGFniNPKVIRLLLRKGADVNALDLYGMTPLA-----------VLLKSRNAN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 418 InaqteetqetaltlaccggfsEVADFLIKAGADI---ELGCSTPLmeasqEGHLE-------LVKYLLASGANVHATTA 487
Cdd:PHA03095 167 V---------------------ELLRLLIDAGADVyavDDRFRSLL-----HHHLQsfkprarIVRELIRAGCDPAATDM 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 488 TGDTALTYA---CENGHTDVADvLLQAGADLEHESEGGRTPLMKAARAGHLCTVQFLISKGANVNRATANNDhTVVSLAC 564
Cdd:PHA03095 221 LGNTPLHSMatgSSCKRSLVLP-LLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGN-TPLSLMV 298
|
330
....*....|...
gi 380805869 565 AGGHLAVVELLLA 577
Cdd:PHA03095 299 RNNNGRAVRAALA 311
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
1047-1140 |
6.59e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 79.77 E-value: 6.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1047 LSLACSGGRQEVVDLLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNaGAEINSRTGsklGISPLMLAAMNGHVPA 1126
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN---GRTALHYAARSGHLEI 76
|
90
....*....|....
gi 380805869 1127 VKLLLDMGSDINAQ 1140
Cdd:pfam12796 77 VKLLLEKGADINVK 90
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
396-485 |
8.82e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 79.77 E-value: 8.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 396 LMEAAREGHEEMVALLLAQGANINAQTEETQeTALTLACCGGFSEVADFLI-KAGADIELGCSTPLMEASQEGHLELVKY 474
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGR-TALHLAAKNGHLEIVKLLLeHADVNLKDNGRTALHYAARSGHLEIVKL 79
|
90
....*....|.
gi 380805869 475 LLASGANVHAT 485
Cdd:pfam12796 80 LLEKGADINVK 90
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
363-454 |
1.28e-17 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 79.00 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 363 LTLAACGGHVELAALLIERGANLEEVNDEGYTPLMEAAREGHEEMVALLLAQgANINAQTEetQETALTLACCGGFSEVA 442
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN--GRTALHYAARSGHLEIV 77
|
90
....*....|..
gi 380805869 443 DFLIKAGADIEL 454
Cdd:pfam12796 78 KLLLEKGADINV 89
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
978-1287 |
2.41e-17 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 87.81 E-value: 2.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 978 TALTLACAGGHEELVSVLIARDAKIEHRDKKGFTPLILAATAGHVGVVEILLDKGGDIEAQsertkDTPLSLACSGGRQE 1057
Cdd:PHA02876 180 TPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKN-----DLSLLKAIRNEDLE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1058 VVDLLLARGANKEHRNVSDYTPLSLAASGGYVN-IIKILLNAGAEINSRTGSklGISPLMLAAMNGH-VPAVKLLLDMGS 1135
Cdd:PHA02876 255 TSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIK--GETPLYLMAKNGYdTENIRTLIMLGA 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1136 DINAQiETNRNTALTLACFQGR-AEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAppVPSSRD 1214
Cdd:PHA02876 333 DVNAA-DRLYITPLHQASTLDRnKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEA--LSQKIG 409
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 380805869 1215 TALTIA-ADKGHYKFCELLIHRGAHIDVRNKKGNTPLWLA-SNGGHFDVVQLLVQAGADVDAADNRKITPLMSAF 1287
Cdd:PHA02876 410 TALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYAcKKNCKLDVIEMLLDNGADVNAINIQNQYPLLIAL 484
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
1024-1338 |
4.87e-17 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 85.40 E-value: 4.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1024 VVEILLDKGGDIEAQSERTKdTPLSLACSGGRQEVVDLLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEin 1103
Cdd:PHA02874 17 IEKIIKNKGNCINISVDETT-TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVD-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1104 srtgsklgISPLMLAAMNGHVpaVKLLLDMGSDINAQiETNRNTALTLACFQGRAEVVSLLLDRKANVEHRAKTGLTPLM 1183
Cdd:PHA02874 94 --------TSILPIPCIEKDM--IKTILDCGIDVNIK-DAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1184 EAASGGYAEVGRVLLDKGADVNAPpvPSSRDTALTIAADKGHYKFCELLIHRGAHIDVRNKKGNTPLWLA---------- 1253
Cdd:PHA02874 163 IAIKHNFFDIIKLLLEKGAYANVK--DNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAiihnrsaiel 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1254 -----------SNGG---HF--------DVVQLLVQAGADVDAADNRKITPLMSAFRK-GHVKVVQ------YLVKEVNQ 1304
Cdd:PHA02874 241 linnasindqdIDGStplHHainppcdiDIIDILLYHKADISIKDNKGENPIDTAFKYiNKDPVIKdiianaVLIKEADK 320
|
330 340 350
....*....|....*....|....*....|....
gi 380805869 1305 FPsDIECMRYIATITDKELLKKCHQCVETIVKAK 1338
Cdd:PHA02874 321 LK-DSDFLEHIEIKDNKEFSDFIKECNEEIEDMK 353
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
130-222 |
1.22e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 76.31 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 130 LAEACSDGDVNAVRKLLDEGRSVNEHTEEGESLLCLACSAGYYELAQVLLA-MHANVEDRGNkgdiTPLMAASSGGYLDI 208
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEhADVNLKDNGR----TALHYAARSGHLEI 76
|
90
....*....|....
gi 380805869 209 VKLLLLHDADVNSQ 222
Cdd:pfam12796 77 VKLLLEKGADINVK 90
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
1024-1287 |
2.67e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 84.34 E-value: 2.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1024 VVEILLDKGGDIEAQSERTKdTPLSLACSGGRQEVVDLLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEIN 1103
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCI-TPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNIN 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1104 SRTGSklgispLMLAAMNGHVPAVKLLLDMGSDINAqIETNRNTALTLAC-FQGRAEVVSLLLDRKANVEHRAKTGLTPL 1182
Cdd:PHA02876 239 KNDLS------LLKAIRNEDLETSLLLYDAGFSVNS-IDDCKNTPLHHASqAPSLSRLVPKLLERGADVNAKNIKGETPL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1183 MEAASGGY-AEVGRVLLDKGADVNAppVPSSRDTALTIAADKGHYKFCEL-LIHRGAHIDVRNKKGNTPLWLASNGGHFD 1260
Cdd:PHA02876 312 YLMAKNGYdTENIRTLIMLGADVNA--ADRLYITPLHQASTLDRNKDIVItLLELGANVNARDYCDKTPIHYAAVRNNVV 389
|
250 260
....*....|....*....|....*..
gi 380805869 1261 VVQLLVQAGADVDAADNRKITPLMSAF 1287
Cdd:PHA02876 390 IINTLLDYGADIEALSQKIGTALHFAL 416
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
990-1143 |
3.77e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 82.41 E-value: 3.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 990 ELVSVLIARDAKIEHRDKKGFTPLILAATA--GHVGVVEILLDKGGDIEAQSERTKdTPLSLACSGGRQEV--------- 1058
Cdd:PHA03100 87 EIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGE-NLLHLYLESNKIDLkilkllidk 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1059 ---------VDLLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSRTgsKLGISPLMLAAMNGHVPAVKL 1129
Cdd:PHA03100 166 gvdinaknrVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVN--KYGDTPLHIAILNNNKEIFKL 243
|
170
....*....|....
gi 380805869 1130 LLDMGSDINAQIET 1143
Cdd:PHA03100 244 LLNNGPSIKTIIET 257
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
1182-1276 |
3.93e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 74.77 E-value: 3.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1182 LMEAASGGYAEVGRVLLDKGADVNAppVPSSRDTALTIAADKGHYKFCELLIhrgAHIDVRNK-KGNTPLWLASNGGHFD 1260
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANL--QDKNGRTALHLAAKNGHLEIVKLLL---EHADVNLKdNGRTALHYAARSGHLE 75
|
90
....*....|....*.
gi 380805869 1261 VVQLLVQAGADVDAAD 1276
Cdd:pfam12796 76 IVKLLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
1217-1300 |
4.17e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 74.77 E-value: 4.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1217 LTIAADKGHYKFCELLIHRGAHIDVRNKKGNTPLWLASNGGHFDVVQLLVQaGADVDAADNRKiTPLMSAFRKGHVKVVQ 1296
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNGR-TALHYAARSGHLEIVK 78
|
....
gi 380805869 1297 YLVK 1300
Cdd:pfam12796 79 LLLE 82
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
204-454 |
4.39e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 82.35 E-value: 4.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 204 GYLDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGAnIEDHNENG-HTPLMEAASAGHVEVARVLLDHG 282
Cdd:PHA02875 13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGA-IPDVKYPDiESELHDAVEEGDVKAVEELLDLG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 283 AGINTHSNEFKESALTLACYKGHLDMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESP 362
Cdd:PHA02875 92 KFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 363 LTLAACGGHVELAALLIERGANLEEVNDEGYTPLMEAAREGHE-EMVALLLAQGANINAQTEETQETALTLA-----CCG 436
Cdd:PHA02875 172 LIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKiDIVRLFIKRGADCNIMFMIEGEECTILDmicnmCTN 251
|
250
....*....|....*...
gi 380805869 437 GFSEVADFLIkagADIEL 454
Cdd:PHA02875 252 LESEAIDALI---ADIAI 266
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
406-619 |
4.48e-16 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 82.77 E-value: 4.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 406 EMVALLLAQGANINaQTEETQETALT--LAC-CGGFSEVADFLIKAGADI---ELGCSTPL---MEASQEghLELVKYLL 476
Cdd:PHA03095 28 EEVRRLLAAGADVN-FRGEYGKTPLHlyLHYsSEKVKDIVRLLLEAGADVnapERCGFTPLhlyLYNATT--LDVIKLLI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 477 ASGANVHATTATGDTAL-TYAC-ENGHTDVADVLLQAGADLEHESEGGRTPL---MKAARAgHLCTVQFLISKGANV--- 548
Cdd:PHA03095 105 KAGADVNAKDKVGRTPLhVYLSgFNINPKVIRLLLRKGADVNALDLYGMTPLavlLKSRNA-NVELLRLLIDAGADVyav 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 549 --NRATANNDHTVVSLACAgghlAVVELLLAHGADPTHRLKDGSTMLIEAAKGG---HTNVVSYLL-----DYPNNVLSV 618
Cdd:PHA03095 184 ddRFRSLLHHHLQSFKPRA----RIVRELIRAGCDPAATDMLGNTPLHSMATGSsckRSLVLPLLIagisiNARNRYGQT 259
|
.
gi 380805869 619 P 619
Cdd:PHA03095 260 P 260
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
1149-1243 |
4.82e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 74.77 E-value: 4.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1149 LTLACFQGRAEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKgADVNappVPSSRDTALTIAADKGHYKF 1228
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVN---LKDNGRTALHYAARSGHLEI 76
|
90
....*....|....*
gi 380805869 1229 CELLIHRGAHIDVRN 1243
Cdd:pfam12796 77 VKLLLEKGADINVKD 91
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
229-451 |
4.85e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 82.35 E-value: 4.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 229 ALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVARVLLDHGAGINTHSNEFkESALTLACYKGHLDM 308
Cdd:PHA02875 5 ALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDI-ESELHDAVEEGDVKA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 309 VRFLLEAG--ADQEHKTDEMhTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGANLE 386
Cdd:PHA02875 84 VEELLDLGkfADDVFYKDGM-TPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 380805869 387 EVNDEGYTPLMEAAREGHEEMVALLLAQGANINAQTEETQETALTLACCGGFSEVADFLIKAGAD 451
Cdd:PHA02875 163 IEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGAD 227
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
991-1204 |
7.54e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 82.80 E-value: 7.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 991 LVSVLIARDAKIEHRDKKGFTPLILAATAGH-VGVVEILLDKGGDIEAqSERTKDTPLSLACSGGR-QEVVDLLLARGAN 1068
Cdd:PHA02876 289 LVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNA-ADRLYITPLHQASTLDRnKDIVITLLELGAN 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1069 KEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSRTgSKLGISplMLAAMNGHVP--AVKLLLDMGSDINAQiETNRN 1146
Cdd:PHA02876 368 VNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALS-QKIGTA--LHFALCGTNPymSVKTLIDRGANVNSK-NKDLS 443
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 380805869 1147 TALTLACFQG-RAEVVSLLLDRKANVEHRAKTGLTPLMEAAsgGYAEVGRVLLDKGADV 1204
Cdd:PHA02876 444 TPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGAEL 500
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
978-1170 |
9.84e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 81.19 E-value: 9.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 978 TALTLACAGGHEELVSVLIARDAKIEHRDKKGFTPLILAATAGHVGVVEILLDKGGDIEAQSERTKDTPLSLACSGGRQE 1057
Cdd:PHA02875 37 SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1058 VVDLLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSRTGskLGISPLMLAAMNGHVPAVKLLLDMGSDI 1137
Cdd:PHA02875 117 IMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDC--CGCTPLIIAMAKGDIAICKMLLDSGANI 194
|
170 180 190
....*....|....*....|....*....|....*.
gi 380805869 1138 NAqieTNRNTALTLACF---QGRAEVVSLLLDRKAN 1170
Cdd:PHA02875 195 DY---FGKNGCVAALCYaieNNKIDIVRLFIKRGAD 227
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
1157-1300 |
1.04e-15 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 81.61 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1157 RAEVVSLLLDRKANVEHR---AKTGLTPLMEAASGGYAEVGRVLLDKGADVNAPpvPSSRDTALtiaadkgHYKFC---- 1229
Cdd:PHA03095 26 TVEEVRRLLAAGADVNFRgeyGKTPLHLYLHYSSEKVKDIVRLLLEAGADVNAP--ERCGFTPL-------HLYLYnatt 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1230 ----ELLIHRGAHIDVRNKKGNTPL--WLASNGGHFDVVQLLVQAGADVDAADNRKITPLmSAFRKGH---VKVVQYLVK 1300
Cdd:PHA03095 97 ldviKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPL-AVLLKSRnanVELLRLLID 175
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
138-334 |
1.04e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 81.19 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 138 DVNAVRKLLDEGRSVNEHTEEGESLLCLACSAGYYELAQVLLAMHANVEDRGNKGDITPLMAASSGGYLDIVKLLLLHDA 217
Cdd:PHA02875 47 DSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 218 DVNSQSATGNTALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVARVLLDHGAGINTHSNEFKESAL 297
Cdd:PHA02875 127 DPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAAL 206
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 380805869 298 TLACYKGHLDMVRFLLEAGADQEHKT---DEMHTALMEAC 334
Cdd:PHA02875 207 CYAIENNKIDIVRLFIKRGADCNIMFmieGEECTILDMIC 246
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
370-628 |
1.45e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 80.78 E-value: 1.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 370 GHVELAALLIERGANLEEVN-DEGYTPLMEAAREGHEEMVALLLAQGANINAQTEETQETALTlACCGGFSEVADFLIKA 448
Cdd:PHA02874 12 GDIEAIEKIIKNKGNCINISvDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLT-AIKIGAHDIIKLLIDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 449 GADIELgCSTPLMEAsqeghlELVKYLLASGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPLMK 528
Cdd:PHA02874 91 GVDTSI-LPIPCIEK------DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 529 AARAGHLCTVQFLISKGANVNrATANNDHTVVSLACAGGHLAVVELLLAHGADPTHRLKDGSTMLIEAAKGGHTnVVSYL 608
Cdd:PHA02874 164 AIKHNFFDIIKLLLEKGAYAN-VKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRS-AIELL 241
|
250 260
....*....|....*....|
gi 380805869 609 LdypnNVLSVPTTDVSQLTP 628
Cdd:PHA02874 242 I----NNASINDQDIDGSTP 257
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
184-365 |
1.55e-15 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 82.22 E-value: 1.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 184 NVEDRGNKGDITPLMAASSGGYLDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPL 263
Cdd:PLN03192 516 NGGEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTAL 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 264 MEAASAGHVEVARVLLDHGAGINTHSNefkESALTLACYKGHLDMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVAR 343
Cdd:PLN03192 596 WNAISAKHHKIFRILYHFASISDPHAA---GDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVR 672
|
170 180
....*....|....*....|...
gi 380805869 344 LLLDSGAQVN-MPADSFESPLTL 365
Cdd:PLN03192 673 LLIMNGADVDkANTDDDFSPTEL 695
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
980-1073 |
1.78e-15 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 72.84 E-value: 1.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 980 LTLACAGGHEELVSVLIARDAKIEHRDKKGFTPLILAATAGHVGVVEILLDKgGDIEAQSErtKDTPLSLACSGGRQEVV 1059
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN--GRTALHYAARSGHLEIV 77
|
90
....*....|....
gi 380805869 1060 DLLLARGANKEHRN 1073
Cdd:pfam12796 78 KLLLEKGADINVKD 91
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
329-581 |
9.34e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 78.11 E-value: 9.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 329 ALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGAnLEEVNDEGY-TPLMEAAREGHEEM 407
Cdd:PHA02875 5 ALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGA-IPDVKYPDIeSELHDAVEEGDVKA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 408 VALLLAQGANINaqteetqetaltlaccggfsevaDFLIKAGadielgcSTPLMEASQEGHLELVKYLLASGANVHATTA 487
Cdd:PHA02875 84 VEELLDLGKFAD-----------------------DVFYKDG-------MTPLHLATILKKLDIMKLLIARGADPDIPNT 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 488 TGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGHLCTVQFLISKGANVNRATANNDHTVVSLACAGG 567
Cdd:PHA02875 134 DKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENN 213
|
250
....*....|....
gi 380805869 568 HLAVVELLLAHGAD 581
Cdd:PHA02875 214 KIDIVRLFIKRGAD 227
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
1045-1237 |
1.00e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 78.11 E-value: 1.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1045 TPLSLACSGGRQEVVDLLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSrTGSKLGISPLMLAAMNGHV 1124
Cdd:PHA02875 37 SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADD-VFYKDGMTPLHLATILKKL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1125 PAVKLLLDMGSDINAQiETNRNTALTLACFQGRAEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADV 1204
Cdd:PHA02875 116 DIMKLLIARGADPDIP-NTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANI 194
|
170 180 190
....*....|....*....|....*....|....*..
gi 380805869 1205 N----APPVpssrdTALTIAADKGHYKFCELLIHRGA 1237
Cdd:PHA02875 195 DyfgkNGCV-----AALCYAIENNKIDIVRLFIKRGA 226
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
1050-1271 |
2.79e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 76.57 E-value: 2.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1050 ACSGGRQEVVDLLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSRTGsklGI-SPLMLAAMNGHVPAVK 1128
Cdd:PHA02875 9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYP---DIeSELHDAVEEGDVKAVE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1129 LLLDMGSDINAQIETNRNTALTLACFQGRAEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAPP 1208
Cdd:PHA02875 86 ELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIED 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 380805869 1209 VPSSrdTALTIAADKGHYKFCELLIHRGAHIDVRNKKGN-TPLWLASNGGHFDVVQLLVQAGAD 1271
Cdd:PHA02875 166 CCGC--TPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGAD 227
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
971-1315 |
2.83e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 77.23 E-value: 2.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 971 HTESNHDTALTLACAGGHE-------ELVSVLIARDAKIEHRDKKGFTPL-ILAATAGHVGVVEILLDKGGDIEAQSERT 1042
Cdd:PHA02878 25 HTENYSTSASLIPFIPLHQavearnlDVVKSLLTRGHNVNQPDHRDLTPLhIICKEPNKLGMKEMIRSINKCSVFYTLVA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1043 kdtpLSLACSGGRQEVVDLLLARGANKEHrnVSDYTPLSLAASGGYVN--IIKILLNAGAEINSRTGSKLGiSPLMLAAM 1120
Cdd:PHA02878 105 ----IKDAFNNRNVEIFKIILTNRYKNIQ--TIDLVYIDKKSKDDIIEaeITKLLLSYGADINMKDRHKGN-TALHYATE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1121 NGHVPAVKLLLDMGSDINAQIETNrNTALTLACFQGRAEVVSLLLDRKANVEHRAKTGLTPLMeaASGGYA---EVGRVL 1197
Cdd:PHA02878 178 NKDQRLTELLLSYGANVNIPDKTN-NSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLH--ISVGYCkdyDILKLL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1198 LDKGADVNAppvpssRDTALTIAAdkghykfcellihrgAHIDVRNKkgntplwlasngghfDVVQLLVQAGADVDAADN 1277
Cdd:PHA02878 255 LEHGVDVNA------KSYILGLTA---------------LHSSIKSE---------------RKLKLLLEYGADINSLNS 298
|
330 340 350
....*....|....*....|....*....|....*....
gi 380805869 1278 RKITPLMSAfrkghvkVVQYLVKEV-NQFPSDIECMRYI 1315
Cdd:PHA02878 299 YKLTPLSSA-------VKQYLCINIgRILISNICLLKRI 330
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
967-1209 |
1.00e-13 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 75.45 E-value: 1.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 967 DIDAhTESNHDTAL-TLACAGGHEELVSVLIARDAKIEHRDKKGFTPL--ILAATAGHVGVVEILLDKGGDIEAQSERTK 1043
Cdd:PHA03095 75 DVNA-PERCGFTPLhLYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGM 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1044 dTPLS--------------LACSGG-----------------------RQEVVDLLLARGANKEHRNVSDYTPLSLAASG 1086
Cdd:PHA03095 154 -TPLAvllksrnanvellrLLIDAGadvyavddrfrsllhhhlqsfkpRARIVRELIRAGCDPAATDMLGNTPLHSMATG 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1087 GYVNIIKI--LLNAGAEINSRtgSKLGISPLMLAAMNGHVPAVKLLLDMGSDINAQIETNrNTALTLACFQGRAEVVSLL 1164
Cdd:PHA03095 233 SSCKRSLVlpLLIAGISINAR--NRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDG-NTPLSLMVRNNNGRAVRAA 309
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 380805869 1165 LDRKANVEHRAKTgLTPLMEAASGGYAEVGR-----VLLDKGADVNAPPV 1209
Cdd:PHA03095 310 LAKNPSAETVAAT-LNTASVAGGDIPSDATRlcvakVVLRGAFSLLPEPI 358
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
324-598 |
1.11e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 75.00 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 324 DEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGAnleevnDEGYTPLMEAareg 403
Cdd:PHA02874 33 DETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGV------DTSILPIPCI---- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 404 HEEMVALLLAQGANINAQTEETQeTALTLACCGGFSEVADFLIKAGADIEL----GCsTPLMEASQEGHLELVKYLLASG 479
Cdd:PHA02874 103 EKDMIKTILDCGIDVNIKDAELK-TFLHYAIKKGDLESIKMLFEYGADVNIeddnGC-YPIHIAIKHNFFDIIKLLLEKG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 480 ANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGHlCTVQFLISKgANVNRATANND--- 556
Cdd:PHA02874 181 AYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLINN-ASINDQDIDGStpl 258
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 380805869 557 HTVVSLACAgghLAVVELLLAHGADPTHRLKDGSTMLIEAAK 598
Cdd:PHA02874 259 HHAINPPCD---IDIIDILLYHKADISIKDNKGENPIDTAFK 297
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
1058-1312 |
2.03e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 75.10 E-value: 2.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1058 VVDLLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSRTGSklGISPLMLAAMNGHVPAVKLLLDMGSDI 1137
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALD--DLSVLECAVDSKNIDTIKAIIDNRSNI 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1138 NAQ----IETNRNTALtlacfqgraEVVSLLLDRKANVEHRAKTGLTPLMEAASG-GYAEVGRVLLDKGADVNAPPVPSs 1212
Cdd:PHA02876 238 NKNdlslLKAIRNEDL---------ETSLLLYDAGFSVNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKG- 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1213 rDTALTIAADKGH-YKFCELLIHRGAHIDVRNKKGNTPLWLASNGGHF-DVVQLLVQAGADVDAADNRKITPLMSAFRKG 1290
Cdd:PHA02876 308 -ETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDRNkDIVITLLELGANVNARDYCDKTPIHYAAVRN 386
|
250 260
....*....|....*....|..
gi 380805869 1291 HVKVVQYLVkevnQFPSDIECM 1312
Cdd:PHA02876 387 NVVIINTLL----DYGADIEAL 404
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
526-611 |
2.39e-13 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 67.06 E-value: 2.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 526 LMKAARAGHLCTVQFLISKGANVNrATANNDHTVVSLACAGGHLAVVELLLAHgADPTHRLkDGSTMLIEAAKGGHTNVV 605
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADAN-LQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77
|
....*.
gi 380805869 606 SYLLDY 611
Cdd:pfam12796 78 KLLLEK 83
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
239-531 |
5.68e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 72.99 E-value: 5.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 239 VDIVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVARVLLdhgAGINTHSNEFKESALTLACYKGHLDMVRFLLEAGAD 318
Cdd:PHA02878 50 LDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMI---RSINKCSVFYTLVAIKDAFNNRNVEIFKIILTNRYK 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 319 QEHKTDEMHtaLMEACMDGHVE--VARLLLDSGAQVNM-PADSFESPLTLAACGGHVELAALLIERGANLEEVNDEGYTP 395
Cdd:PHA02878 127 NIQTIDLVY--IDKKSKDDIIEaeITKLLLSYGADINMkDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSP 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 396 LMEAAREGHEEMVALLLAQGANINAQTEetqetaltlacCGgfsevadflikagadielgcSTPL-MEASQEGHLELVKY 474
Cdd:PHA02878 205 LHHAVKHYNKPIVHILLENGASTDARDK-----------CG--------------------NTPLhISVGYCKDYDILKL 253
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 380805869 475 LLASGANVHA-TTATGDTALTYACENghTDVADVLLQAGADLEHESEGGRTPLMKAAR 531
Cdd:PHA02878 254 LLEHGVDVNAkSYILGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAVK 309
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
196-452 |
8.49e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 72.61 E-value: 8.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 196 PLMAASSGGYLDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEgaNIEDHNENGHTPLMEAASAGHVEVA 275
Cdd:PHA02878 40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRS--INKCSVFYTLVAIKDAFNNRNVEIF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 276 RVLLdhgagINTHSNEfKESALTLACYKGHLD-----MVRFLLEAGADQEHKT-DEMHTALMEACMDGHVEVARLLLDSG 349
Cdd:PHA02878 118 KIIL-----TNRYKNI-QTIDLVYIDKKSKDDiieaeITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 350 AQVNMPADSFESPLTLAACGGHVELAALLIERGANLEEVNDEGYTPL-MEAAREGHEEMVALLLAQGANINAQTEETQET 428
Cdd:PHA02878 192 ANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLhISVGYCKDYDILKLLLEHGVDVNAKSYILGLT 271
|
250 260
....*....|....*....|....
gi 380805869 429 ALTLACCGgfSEVADFLIKAGADI 452
Cdd:PHA02878 272 ALHSSIKS--ERKLKLLLEYGADI 293
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
1083-1300 |
8.67e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 71.95 E-value: 8.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1083 AASGGYVNIIKILLNAGaeINSRTGSKLGISPLMLAAMNGHVPAVKLLLDMGSDINAQIETNRnTALTLACFQGRAEVVS 1162
Cdd:PHA02875 9 AILFGELDIARRLLDIG--INPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIE-SELHDAVEEGDVKAVE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1163 LLLDRKANVEHRA-KTGLTPLMEAASGGYAEVGRVLLDKGADvnaPPVPSS-RDTALTIAADKGHYKFCELLIHRGAHID 1240
Cdd:PHA02875 86 ELLDLGKFADDVFyKDGMTPLHLATILKKLDIMKLLIARGAD---PDIPNTdKFSPLHLAVMMGDIKGIELLIDHKACLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 380805869 1241 VRNKKGNTPLWLASNGGHFDVVQLLVQAGADVDAADNRK-ITPLMSAFRKGHVKVVQYLVK 1300
Cdd:PHA02875 163 IEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIK 223
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
128-318 |
1.81e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 71.45 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 128 RSLAEACSDGDVNAVRKLLdegrsVNEHTEEGESLLCLACSAGY-----YELAQVLLAMHANVEDRGNKGDITPLMAASS 202
Cdd:PHA02878 103 VAIKDAFNNRNVEIFKIIL-----TNRYKNIQTIDLVYIDKKSKddiieAEITKLLLSYGADINMKDRHKGNTALHYATE 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 203 GGYLDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPL-MEAASAGHVEVARVLLDH 281
Cdd:PHA02878 178 NKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLhISVGYCKDYDILKLLLEH 257
|
170 180 190
....*....|....*....|....*....|....*..
gi 380805869 282 GAGINTHSNEFKESALTLACYKGhlDMVRFLLEAGAD 318
Cdd:PHA02878 258 GVDVNAKSYILGLTALHSSIKSE--RKLKLLLEYGAD 292
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
341-548 |
1.99e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 71.15 E-value: 1.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 341 VARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGANLEEVNDEGYTPLMEAAREGHEEMVALLLAQGANIna 420
Cdd:PHA02874 17 IEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDT-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 421 qteetqeTALTLACCGgfSEVADFLIKAGADIEL---GCSTPLMEASQEGHLELVKYLLASGANVHATTATGDTALTYAC 497
Cdd:PHA02874 95 -------SILPIPCIE--KDMIKTILDCGIDVNIkdaELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAI 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 380805869 498 ENGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGHLCTVQFLISKGANV 548
Cdd:PHA02874 166 KHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHI 216
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
339-519 |
4.53e-12 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 71.05 E-value: 4.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 339 VEVARLLLDSGAQVNMPADSFeSPLTLAACGGHVELAALLieRGANLEEVND-EGYTPLMEAAREGHEEMVALLLAQGAN 417
Cdd:PLN03192 507 LNVGDLLGDNGGEHDDPNMAS-NLLTVASTGNAALLEELL--KAKLDPDIGDsKGRTPLHIAASKGYEDCVLVLLKHACN 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 418 INAQtEETQETALTLACCGGFSEVADFLIK--------AGADIelgcstpLMEASQEGHLELVKYLLASGANVHATTATG 489
Cdd:PLN03192 584 VHIR-DANGNTALWNAISAKHHKIFRILYHfasisdphAAGDL-------LCTAAKRNDLTAMKELLKQGLNVDSEDHQG 655
|
170 180 190
....*....|....*....|....*....|
gi 380805869 490 DTALTYACENGHTDVADVLLQAGADLEHES 519
Cdd:PLN03192 656 ATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
1144-1300 |
1.16e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 68.48 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1144 NRNTALTLACFQGRAEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGA--DVNAPPVPSSrdtaLTIAA 1221
Cdd:PHA02875 1 MDQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAipDVKYPDIESE----LHDAV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1222 DKGHYKFCELLIHRGAHI-DVRNKKGNTPLWLASNGGHFDVVQLLVQAGADVDAADNRKITPLMSAFRKGHVKVVQYLVK 1300
Cdd:PHA02875 77 EEGDVKAVEELLDLGKFAdDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLID 156
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
378-615 |
1.21e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 68.54 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 378 LIERGANLEEVNDEGY----TPLMEAAREGHEEMVALLLAQGANINaQTEETQETALTLACCGGFS-----EVADFLIKA 448
Cdd:PHA03100 17 NIKYIIMEDDLNDYSYkkpvLPLYLAKEARNIDVVKILLDNGADIN-SSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 449 GADIELG---CSTPLMEASQE--GHLELVKYLLASGANVHATTATGDTALTYACENGHTDvadvllqagadleheseggr 523
Cdd:PHA03100 96 GANVNAPdnnGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKID-------------------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 524 tplmkaaraghLCTVQFLISKGANVNRATanndhtvvslacagghlaVVELLLAHGADPTHRLKDGSTMLIEAAKGGHTN 603
Cdd:PHA03100 156 -----------LKILKLLIDKGVDINAKN------------------RVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPE 206
|
250
....*....|..
gi 380805869 604 VVSYLLDYPNNV 615
Cdd:PHA03100 207 FVKYLLDLGANP 218
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
261-433 |
2.31e-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: 68.12 E-value: 2.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 261 TPLMEAASAGHVEVARVLLdhgagINTHSNEFK-----ESALTLACYKGHLDMVRFLLEAGAD--QEHKTDEMH---TAL 330
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLL-----KCPSCDLFQrgalgETALHVAALYDNLEAAVVLMEAAPElvNEPMTSDLYqgeTAL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 331 MEACMDGHVEVARLLLDSGAQVNMP--ADSF------------ESPLTLAACGGHVELAALLIERGANLEEVNDEGYTPL 396
Cdd:cd22192 94 HIAVVNQNLNLVRELIARGADVVSPraTGTFfrpgpknliyygEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 380805869 397 ----MEAAREGHEEMVALLLAQGANINAQTEETQE-----TALTLA 433
Cdd:cd22192 174 hilvLQPNKTFACQMYDLILSYDKEDDLQPLDLVPnnqglTPFKLA 219
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
457-593 |
2.93e-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: 68.12 E-value: 2.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 457 STPLMEASQEGHLELVKYLLAS-GANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHE---SE--GGRTPLMKAA 530
Cdd:cd22192 18 ESPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEpmtSDlyQGETALHIAV 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 380805869 531 RAGHLCTVQFLISKGANVN--RATAN------------NDHTVVSLACAgGHLAVVELLLAHGADPTHRLKDGSTML 593
Cdd:cd22192 98 VNQNLNLVRELIARGADVVspRATGTffrpgpknliyyGEHPLSFAACV-GNEEIVRLLIEHGADIRAQDSLGNTVL 173
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
130-366 |
2.99e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 67.60 E-value: 2.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 130 LAEACSDGDVNAVRKLLDEGRSVNEHTEEGESLLCLACSAG-----------------YYELAQVLLAMH---------- 182
Cdd:PHA02878 41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPnklgmkemirsinkcsvFYTLVAIKDAFNnrnveifkii 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 183 -ANVEDRGNKGDITPLMAASSGGYLD--IVKLLLLHDADVNSQSA-TGNTALTYACAGGFVDIVKVLLNEGANIEDHNEN 258
Cdd:PHA02878 121 lTNRYKNIQTIDLVYIDKKSKDDIIEaeITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKT 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 259 GHTPLMEAASAGHVEVARVLLDHGAGINtHSNEFKESALTLAC-YKGHLDMVRFLLEAGADQEHKTDEMH-TALMEACMD 336
Cdd:PHA02878 201 NNSPLHHAVKHYNKPIVHILLENGASTD-ARDKCGNTPLHISVgYCKDYDILKLLLEHGVDVNAKSYILGlTALHSSIKS 279
|
250 260 270
....*....|....*....|....*....|
gi 380805869 337 GhvEVARLLLDSGAQVNMPADSFESPLTLA 366
Cdd:PHA02878 280 E--RKLKLLLEYGADINSLNSYKLTPLSSA 307
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
456-509 |
9.68e-11 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 58.44 E-value: 9.68e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 380805869 456 CSTPLMEASQEGHLELVKYLLASGANVHATTATGDTALTYACENGHTDVADVLL 509
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
440-746 |
1.22e-10 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 66.04 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 440 EVADFLIK-AGADIELGCSTPLMEASQEGHLELVKYLLASGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHE 518
Cdd:PLN03192 508 NVGDLLGDnGGEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIR 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 519 SEGGRTPLMKAARAGHLCTVQFLiskganVNRATANNDHT---VVSLACAGGHLAVVELLLAHGADPTHRLKDGSTMLIE 595
Cdd:PLN03192 588 DANGNTALWNAISAKHHKIFRIL------YHFASISDPHAagdLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQV 661
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 596 AAKGGHTNVVSYLLDYPNNVLSVPTTDvsQLTPPSQDQSQVPRVPMHTLAMV--VPPQEPDRTSQEnspallGGQKGTSK 673
Cdd:PLN03192 662 AMAEDHVDMVRLLIMNGADVDKANTDD--DFSPTELRELLQKRELGHSITIVdsVPADEPDLGRDG------GSRPGRLQ 733
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 380805869 674 QKSSSLQVADQDLLPSFHPYQPLECIVEETeGKLNELgqrisaieKAQLKSLELIQGEPLNKDKIEELKKNRE 746
Cdd:PLN03192 734 GTSSDNQCRPRVSIYKGHPLLRNERCCNEA-GKLINL--------PPSLEELKAIAGEKLGFDARKAMVTNEE 797
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
971-1038 |
1.50e-10 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 58.97 E-value: 1.50e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 380805869 971 HTESNHDTALTLACAGGHEELVSVLIARdAKIEHRDkKGFTPLILAATAGHVGVVEILLDKGGDIEAQ 1038
Cdd:pfam12796 25 LQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADINVK 90
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
206-423 |
1.53e-10 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 65.24 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 206 LDIVKLLLLHDADVNSQSATGNTALTYACAGGFV---DIVKVLLNEGANIEDHNENGHTPLMEAASAGH---VEVARVLL 279
Cdd:PHA02798 89 LDIVKILIENGADINKKNSDGETPLYCLLSNGYInnlEILLFMIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 280 DHGAGINTHSNEFKESalTLACY------KGHLDMVRFLLEAG-----ADQEHKTDemhtaLMEACMDghvevarLLLDS 348
Cdd:PHA02798 169 EKGVDINTHNNKEKYD--TLHCYfkynidRIDADILKLFVDNGfiinkENKSHKKK-----FMEYLNS-------LLYDN 234
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 380805869 349 GaqvNMPADSFEspltlaacgghvelaalLIERGANLEEVNDEGYTPLMEAAREGHEEMVALLLAQGANINAQTE 423
Cdd:PHA02798 235 K---RFKKNILD-----------------FIFSYIDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITE 289
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
127-290 |
2.09e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 64.60 E-value: 2.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 127 TRSLAEACSDGDVNAVRKLLDEGRSVNEHTEEGESLLCLACSAGYYELAQVLL-------------------------AM 181
Cdd:PHA02874 36 TTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIdngvdtsilpipciekdmiktildcGI 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 182 HANVEDRGNKgdiTPLMAASSGGYLDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANIEDHNENGHT 261
Cdd:PHA02874 116 DVNIKDAELK---TFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGES 192
|
170 180
....*....|....*....|....*....
gi 380805869 262 PLMEAASAGHVEVARVLLDHGAGINTHSN 290
Cdd:PHA02874 193 PLHNAAEYGDYACIKLLIDHGNHIMNKCK 221
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
137-258 |
5.13e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 63.53 E-value: 5.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 137 GDVNAVRKLLDEGRSVNEHTEEGESLLCLACSAGYYEL--AQVLL--AMHANVEDR--------------GNKGDiTPLM 198
Cdd:PHA03100 119 NSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkiLKLLIdkGVDINAKNRvnyllsygvpinikDVYGF-TPLH 197
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 199 AASSGGYLDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANIEDHNEN 258
Cdd:PHA03100 198 YAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
562-613 |
8.43e-10 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 57.05 E-value: 8.43e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 380805869 562 LACAGGHLAVVELLLAHGADPTHRLKDGSTMLIEAAKGGHTNVVSYLLDYPN 613
Cdd:pfam12796 3 LAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD 54
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
1113-1276 |
1.08e-09 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 62.96 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1113 SPLMLAAMNGHVPAVKLLLDMGSDINAQIETNRnTALTLACFQGRAEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAE 1192
Cdd:PLN03192 527 SNLLTVASTGNAALLEELLKAKLDPDIGDSKGR-TPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHK 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1193 VGRVLLDKGADVNappvPSSRDTALTIAADKGHYKFCELLIHRGAHIDVRNKKGNTPLWLASNGGHFDVVQLLVQAGADV 1272
Cdd:PLN03192 606 IFRILYHFASISD----PHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
|
....
gi 380805869 1273 DAAD 1276
Cdd:PLN03192 682 DKAN 685
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
259-313 |
1.60e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 54.97 E-value: 1.60e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 380805869 259 GHTPLMEAASAGHVEVARVLLDHGAGINtHSNEFKESALTLACYKGHLDMVRFLL 313
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADIN-AVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
1246-1299 |
2.03e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 54.59 E-value: 2.03e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 380805869 1246 GNTPLWLASNGGHFDVVQLLVQAGADVDAADNRKITPLMSAFRKGHVKVVQYLV 1299
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
195-246 |
2.05e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 54.59 E-value: 2.05e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 380805869 195 TPLMAASSGGYLDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLL 246
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
125-266 |
2.53e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 61.13 E-value: 2.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 125 VDTRSLAEACSDGDVnaVRKLLDEGRSVNEHTEEGESLLCLACSAGYYELAQVLLAMHANVEDRGNKGDItPLMAASSGG 204
Cdd:PHA02874 92 VDTSILPIPCIEKDM--IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCY-PIHIAIKHN 168
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 380805869 205 YLDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPLMEA 266
Cdd:PHA02874 169 FFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA 230
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
1250-1304 |
7.14e-09 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 54.35 E-value: 7.14e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 380805869 1250 LWLASNGGHFDVVQLLVQAGADVDAADNRKITPLMSAFRKGHVKVVQYLVKEVNQ 1304
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV 55
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
1082-1184 |
8.11e-09 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 60.30 E-value: 8.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1082 LAASGGYVNIiKILLNAGAEINSRTGSklGISPLMLAAMNGHVPAVKLLLDMGSDINAqIETNRNTALTLACFQGRAEVV 1161
Cdd:PTZ00322 89 LAASGDAVGA-RILLTGGADPNCRDYD--GRTPLHIACANGHVQVVRVLLEFGADPTL-LDKDGKTPLELAEENGFREVV 164
|
90 100 110
....*....|....*....|....*....|
gi 380805869 1162 SLLL-------DRKANVEHRAKTGLTPLME 1184
Cdd:PTZ00322 165 QLLSrhsqchfELGANAKPDSFTGKPPSLE 194
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
489-542 |
8.47e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 52.66 E-value: 8.47e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 380805869 489 GDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGHLCTVQFLI 542
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
1213-1266 |
8.80e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 52.66 E-value: 8.80e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 380805869 1213 RDTALTIAADKGHYKFCELLIHRGAHIDVRNKKGNTPLWLASNGGHFDVVQLLV 1266
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
361-412 |
1.11e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 52.28 E-value: 1.11e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 380805869 361 SPLTLAACGGHVELAALLIERGANLEEVNDEGYTPLMEAAREGHEEMVALLL 412
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02989 |
PHA02989 |
ankyrin repeat protein; Provisional |
205-510 |
1.31e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222954 [Multi-domain] Cd Length: 494 Bit Score: 58.98 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 205 YLDIVKLLLLHDADVNSQSaTGNTALTYACAGGFV--DIVKVLLNEGANIedhNENGH--TPL------MEAASAGHVEV 274
Cdd:PHA02989 15 DKNALEFLLRTGFDVNEEY-RGNSILLLYLKRKDVkiKIVKLLIDNGADV---NYKGYieTPLcavlrnREITSNKIKKI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 275 ARVLLDHGAGINTHSneFKESAlTLAC--YKGH---LDMVRFLLEAGADQEHKTDE-----MHTALmEACMDgHVEVARL 344
Cdd:PHA02989 91 VKLLLKFGADINLKT--FNGVS-PIVCfiYNSNinnCDMLRFLLSKGINVNDVKNSrgynlLHMYL-ESFSV-KKDVIKI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 345 LLDSGAQVNMPADSFE-SPLTL----AACGGHVELAALLIERGANLEEvNDEGYTPLMEAAREGHEEMValllaqganin 419
Cdd:PHA02989 166 LLSFGVNLFEKTSLYGlTPMNIylrnDIDVISIKVIKYLIKKGVNIET-NNNGSESVLESFLDNNKILS----------- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 420 aqteeTQETaltlaccggfsEVADFL---IKAGADIELGCsTPLMEASQEGHLELVKYLLASGANVHATTATGDTALTYA 496
Cdd:PHA02989 234 -----KKEF-----------KVLNFIlkyIKINKKDKKGF-NPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYA 296
|
330
....*....|....
gi 380805869 497 CENGHTDVADVLLQ 510
Cdd:PHA02989 297 IKHGNIDMLNRILQ 310
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
1134-1299 |
1.55e-08 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 59.50 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1134 GSDINAQIETNRNTALTLacfqGRAEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAPPVPSsr 1213
Cdd:PLN03192 518 GEHDDPNMASNLLTVAST----GNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANG-- 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1214 DTALTIAADKGHYKFCELLIHRgAHIDVRNKKGNTpLWLASNGGHFDVVQLLVQAGADVDAADNRKITPLMSAFRKGHVK 1293
Cdd:PLN03192 592 NTALWNAISAKHHKIFRILYHF-ASISDPHAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVD 669
|
....*.
gi 380805869 1294 VVQYLV 1299
Cdd:PLN03192 670 MVRLLI 675
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
558-609 |
2.19e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 51.51 E-value: 2.19e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 380805869 558 TVVSLACAGGHLAVVELLLAHGADPTHRLKDGSTMLIEAAKGGHTNVVSYLL 609
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
1078-1267 |
2.24e-08 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 58.49 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1078 TPLSLAASGGYVNIIKILL-NAGAEINSRtGSkLGISPLMLAAMNGHVPAVKLLLD---------MGSDINAQietnrNT 1147
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLLkCPSCDLFQR-GA-LGETALHVAALYDNLEAAVVLMEaapelvnepMTSDLYQG-----ET 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1148 ALTLACFQGRAEVVSLLLDRKANVE---------HRAKTGLT-----PLMEAASGGYAEVGRVLLDKGADVNAppvpssR 1213
Cdd:cd22192 92 ALHIAVVNQNLNLVRELIARGADVVspratgtffRPGPKNLIyygehPLSFAACVGNEEIVRLLIEHGADIRA------Q 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 380805869 1214 D----TALTIAADKGHYKF-CE---LLIHRGAHID------VRNKKGNTPLWLASNGGHFDVVQLLVQ 1267
Cdd:cd22192 166 DslgnTVLHILVLQPNKTFaCQmydLILSYDKEDDlqpldlVPNNQGLTPFKLAAKEGNIVMFQHLVQ 233
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
326-379 |
2.80e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 51.51 E-value: 2.80e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 380805869 326 MHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLI 379
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
1113-1300 |
2.92e-08 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 58.10 E-value: 2.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1113 SPLMLAAMNGHVPAVKLLLDMGSDINAQIETNRNTALTLACFQGRAEVVSLLLDRKANVEHRAKT-----GLTPLMEAAS 1187
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMTsdlyqGETALHIAVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1188 GGYAEVGRVLLDKGADVNAPPV------PSSR------DTALTIAADKGHYKFCELLIHRGAHIDVRNKKGNTPLwlasn 1255
Cdd:cd22192 99 NQNLNLVRELIARGADVVSPRAtgtffrPGPKnliyygEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL----- 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 380805869 1256 ggHFDVVQ------------LLVQAGADVDAA-----DNRKITPLMSAFRKGHVKVVQYLVK 1300
Cdd:cd22192 174 --HILVLQpnktfacqmydlILSYDKEDDLQPldlvpNNQGLTPFKLAAKEGNIVMFQHLVQ 233
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
262-582 |
4.46e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 57.20 E-value: 4.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 262 PLMEAASAGHVEVARVLLDHGAGINTHSNEFKeSALTLACYKGHLDMVRFLLEAgaDQEHKTDEMHTALMEACMDGHVEV 341
Cdd:PHA02878 40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDL-TPLHIICKEPNKLGMKEMIRS--INKCSVFYTLVAIKDAFNNRNVEI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 342 ARLLLdsgaqvnmpADSFESpltlaacgghvelaalliERGANLEEVNDEGYTPLMEAaregheEMVALLLAQGANINAQ 421
Cdd:PHA02878 117 FKIIL---------TNRYKN------------------IQTIDLVYIDKKSKDDIIEA------EITKLLLSYGADINMK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 422 TEETQetaltlaccggfsevadflikagadielgcSTPLMEASQEGHLELVKYLLASGANVHATTATGDTALTYACENGH 501
Cdd:PHA02878 164 DRHKG------------------------------NTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYN 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 502 TDVADVLLQAGADLEHESEGGRTPL-MKAARAGHLCTVQFLISKGANVNRATANNDHTVVSLACAGGHlaVVELLLAHGA 580
Cdd:PHA02878 214 KPIVHILLENGASTDARDKCGNTPLhISVGYCKDYDILKLLLEHGVDVNAKSYILGLTALHSSIKSER--KLKLLLEYGA 291
|
..
gi 380805869 581 DP 582
Cdd:PHA02878 292 DI 293
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
226-279 |
5.18e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 50.74 E-value: 5.18e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 380805869 226 GNTALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVARVLL 279
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
967-1137 |
9.32e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 56.61 E-value: 9.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 967 DIDAhTESNHDTALTLACA-GGHEELVSVLIARDAKIEHRDKKGFTPLILAATAGHVGVVEILLDKGGDIEAQSERTkDT 1045
Cdd:PHA02876 333 DVNA-ADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKI-GT 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1046 PLSLACSGGRQEV-VDLLLARGANKEHRNVSDYTPLSLAASGG-YVNIIKILLNAGAEINSrtgskLGIS---PLMLAAm 1120
Cdd:PHA02876 411 ALHFALCGTNPYMsVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNA-----INIQnqyPLLIAL- 484
|
170
....*....|....*..
gi 380805869 1121 nGHVPAVKLLLDMGSDI 1137
Cdd:PHA02876 485 -EYHGIVNILLHYGAEL 500
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
114-299 |
1.37e-07 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 56.41 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 114 MKAENS--HNAGQVDTRSLAEAcSDGDVNAVRKLLDEGRSVNEHTEEGESLLCLACSAGYYELAQVLLAMHANVEDRGNK 191
Cdd:PLN03192 512 LLGDNGgeHDDPNMASNLLTVA-STGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDAN 590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 192 GDiTPLMAASSGGYLDIVKlLLLHDADVNSQSATGNTaLTYACAGGFVDIVKVLLNEGANIEDHNENGHTPLMEAASAGH 271
Cdd:PLN03192 591 GN-TALWNAISAKHHKIFR-ILYHFASISDPHAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDH 667
|
170 180
....*....|....*....|....*....
gi 380805869 272 VEVARVLLDHGAGInTHSNEFKE-SALTL 299
Cdd:PLN03192 668 VDMVRLLIMNGADV-DKANTDDDfSPTEL 695
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
295-346 |
1.76e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 49.20 E-value: 1.76e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 380805869 295 SALTLACYKGHLDMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLL 346
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02989 |
PHA02989 |
ankyrin repeat protein; Provisional |
1057-1295 |
1.96e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222954 [Multi-domain] Cd Length: 494 Bit Score: 55.52 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1057 EVVDLLLARGANKEHRNVSDyTPL------SLAASGGYVNIIKILLNAGAEINSRTGSklGISPLMLAAMNGHVPAV--- 1127
Cdd:PHA02989 51 KIVKLLIDNGADVNYKGYIE-TPLcavlrnREITSNKIKKIVKLLLKFGADINLKTFN--GVSPIVCFIYNSNINNCdml 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1128 KLLLDMGSDINAQIETNRNTAL--TLACFQGRAEVVSLLLDRKANV-EHRAKTGLTP----LMEAASGGYAEVGRVLLDK 1200
Cdd:PHA02989 128 RFLLSKGINVNDVKNSRGYNLLhmYLESFSVKKDVIKILLSFGVNLfEKTSLYGLTPmniyLRNDIDVISIKVIKYLIKK 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1201 GADVNAPPVPSSRDTALTIAADKGHYKFC-ELL--IHRGAHIDVRNKKGNTPLWLASNGGHFDVVQLLVQAGADVDAADN 1277
Cdd:PHA02989 208 GVNIETNNNGSESVLESFLDNNKILSKKEfKVLnfILKYIKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSK 287
|
250
....*....|....*...
gi 380805869 1278 RKITPLMSAFRKGHVKVV 1295
Cdd:PHA02989 288 DGDTVLTYAIKHGNIDML 305
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
392-446 |
2.13e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 48.81 E-value: 2.13e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 380805869 392 GYTPLMEAAREGHEEMVALLLAQGANINAQTEEtQETALTLACCGGFSEVADFLI 446
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGN-GETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
976-1029 |
3.27e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 48.42 E-value: 3.27e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 380805869 976 HDTALTLACAGGHEELVSVLIARDAKIEHRDKKGFTPLILAATAGHVGVVEILL 1029
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
1113-1165 |
3.50e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 48.04 E-value: 3.50e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 380805869 1113 SPLMLAAMNGHVPAVKLLLDMGSDINAQIEtNRNTALTLACFQGRAEVVSLLL 1165
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDG-NGETALHFAASNGNVEVLKLLL 54
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
985-1063 |
4.66e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 54.52 E-value: 4.66e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 380805869 985 AGGHEELVSVLIARDAKIEHRDKKGFTPLILAATAGHVGVVEILLDKGGDIEAqSERTKDTPLSLACSGGRQEVVDLLL 1063
Cdd:PTZ00322 91 ASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTL-LDKDGKTPLELAEENGFREVVQLLS 168
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
526-648 |
5.48e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 54.13 E-value: 5.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 526 LMKAARAGHLCTVQFLISKGANVNrATANNDHTVVSLACAGGHLAVVELLLAHGADPTHRLKDGSTMLIEAAKGGHTNVV 605
Cdd:PTZ00322 86 LCQLAASGDAVGARILLTGGADPN-CRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV 164
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 380805869 606 SYLLDY------------PNNVLSVPTT-DVSQLTPPSQDQSQVPRVPMHTLAMVV 648
Cdd:PTZ00322 165 QLLSRHsqchfelganakPDSFTGKPPSlEDSPISSHHPDFSAVPQPMMGSLIVIM 220
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
522-576 |
9.62e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 46.88 E-value: 9.62e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 380805869 522 GRTPLMKAARAGHLCTVQFLISKGANVNRATANNDhTVVSLACAGGHLAVVELLL 576
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGE-TALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
1077-1131 |
1.60e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 46.50 E-value: 1.60e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 380805869 1077 YTPLSLAASGGYVNIIKILLNAGAEINSRTGSklGISPLMLAAMNGHVPAVKLLL 1131
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGADINAVDGN--GETALHFAASNGNVEVLKLLL 54
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
967-1155 |
1.88e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 52.19 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 967 DIDAHTESNHDTALTLACAGGHEELVSVLIARDAKIEHRDKKGFTPLILAATAGHVGVVEILLDKggdieaqsertkdtp 1046
Cdd:PHA02878 159 DINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLEN--------------- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1047 lslacsggrqevvdlllarGANKEHRNVSDYTPLSLAAsgGYV---NIIKILLNAGAEINSRTgSKLGISPLMLAAMNGH 1123
Cdd:PHA02878 224 -------------------GASTDARDKCGNTPLHISV--GYCkdyDILKLLLEHGVDVNAKS-YILGLTALHSSIKSER 281
|
170 180 190
....*....|....*....|....*....|..
gi 380805869 1124 VpaVKLLLDMGSDINAqIETNRNTALTLACFQ 1155
Cdd:PHA02878 282 K--LKLLLEYGADINS-LNSYKLTPLSSAVKQ 310
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
978-1097 |
2.18e-06 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 52.32 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 978 TALTLACAGGHEELVSVLIARDAKIE---------HRDKK-----GFTPLILAATAGHVGVVEILLDKGGDIEAQsERTK 1043
Cdd:cd22192 91 TALHIAVVNQNLNLVRELIARGADVVspratgtffRPGPKnliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQ-DSLG 169
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 380805869 1044 DTPL---------SLACsggrqEVVDLLLARGANK-----EH-RNVSDYTPLSLAASGGYVNIIKILLN 1097
Cdd:cd22192 170 NTVLhilvlqpnkTFAC-----QMYDLILSYDKEDdlqplDLvPNNQGLTPFKLAAKEGNIVMFQHLVQ 233
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
1182-1265 |
2.79e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 51.82 E-value: 2.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1182 LMEAASGGYAEVGRVLLDKGADvnappvPSSRD----TALTIAADKGHYKFCELLIHRGAHIDVRNKKGNTPLWLASNGG 1257
Cdd:PTZ00322 86 LCQLAASGDAVGARILLTGGAD------PNCRDydgrTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENG 159
|
....*...
gi 380805869 1258 HFDVVQLL 1265
Cdd:PTZ00322 160 FREVVQLL 167
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
460-611 |
3.18e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 51.15 E-value: 3.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 460 LMEASQEGHLELVKYLLASGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGHLCTVQ 539
Cdd:PHA02875 6 LCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVE 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 380805869 540 FLISKGANVNRATANNDHTVVSLACAGGHLAVVELLLAHGADPTHRLKDGSTMLIEAAKGGHTNVVSYLLDY 611
Cdd:PHA02875 86 ELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDH 157
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
1165-1300 |
3.18e-06 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 51.56 E-value: 3.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1165 LDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAppVPSSRDTALTIAADKGHYKFCE---LLIHRGAHIDV 1241
Cdd:PHA03095 1 DEEDESVDIIMEAALYDYLLNASNVTVEEVRRLLAAGADVNF--RGEYGKTPLHLYLHYSSEKVKDivrLLLEAGADVNA 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 380805869 1242 RNKKGNTPLWL-ASNGGHFDVVQLLVQAGADVDAADNRKITPL---MSAFRKgHVKVVQYLVK 1300
Cdd:PHA03095 79 PERCGFTPLHLyLYNATTLDVIKLLIKAGADVNAKDKVGRTPLhvyLSGFNI-NPKVIRLLLR 140
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
362-611 |
3.32e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 51.42 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 362 PLTLAACGGHVELAALLIERGANLEEVNDEGYTPL----MEAAREGHEEMVAlllaqgaNINAQTEETQETALTLACCGG 437
Cdd:PHA02878 40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLhiicKEPNKLGMKEMIR-------SINKCSVFYTLVAIKDAFNNR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 438 FSEVADFLI----KAGADIELgcsTPLMEASQEGHLE--LVKYLLASGANVHATTA-TGDTALTYACENGHTDVADVLLQ 510
Cdd:PHA02878 113 NVEIFKIILtnryKNIQTIDL---VYIDKKSKDDIIEaeITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 511 AGADLEHESEGGRTPLMKAARAghlctvqfliskganvnratANNDhtvvslacagghlaVVELLLAHGADPTHRLKDGS 590
Cdd:PHA02878 190 YGANVNIPDKTNNSPLHHAVKH--------------------YNKP--------------IVHILLENGASTDARDKCGN 235
|
250 260
....*....|....*....|.
gi 380805869 591 TMLieaakggHTNvVSYLLDY 611
Cdd:PHA02878 236 TPL-------HIS-VGYCKDY 248
|
|
| PHA02989 |
PHA02989 |
ankyrin repeat protein; Provisional |
138-413 |
3.71e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222954 [Multi-domain] Cd Length: 494 Bit Score: 51.28 E-value: 3.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 138 DVNAVRKLLDEGRSVNEhTEEGESLLCLACSAGYY--ELAQVLLAMHANVEDRGNKGdiTPLMAA------SSGGYLDIV 209
Cdd:PHA02989 15 DKNALEFLLRTGFDVNE-EYRGNSILLLYLKRKDVkiKIVKLLIDNGADVNYKGYIE--TPLCAVlrnreiTSNKIKKIV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 210 KLLLLHDADVNSQSATGNTALT---YACAGGFVDIVKVLLNEGANIED-HNENGHTPL---MEAASAgHVEVARVLLDHG 282
Cdd:PHA02989 92 KLLLKFGADINLKTFNGVSPIVcfiYNSNINNCDMLRFLLSKGINVNDvKNSRGYNLLhmyLESFSV-KKDVIKILLSFG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 283 AGINTHSNEFKESALTLacYKGH------LDMVRFLLEAGADQEhKTDEMHTALMEACMDGH-------VEVARLLLdSG 349
Cdd:PHA02989 171 VNLFEKTSLYGLTPMNI--YLRNdidvisIKVIKYLIKKGVNIE-TNNNGSESVLESFLDNNkilskkeFKVLNFIL-KY 246
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 380805869 350 AQVNMPADSFESPLTLAACGGHVELAALLIERGANLEEVNDEGYTPLMEAAREGHEEMVALLLA 413
Cdd:PHA02989 247 IKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNRILQ 310
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
495-628 |
3.82e-06 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 51.18 E-value: 3.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 495 YACENGHTDVADV--LLQAGADLEHESEGGRTPL-MKAARAGHLCT--VQFLISKGANVNRATANNDHTVVSLACAGGHL 569
Cdd:PHA03095 18 YLLNASNVTVEEVrrLLAAGADVNFRGEYGKTPLhLYLHYSSEKVKdiVRLLLEAGADVNAPERCGFTPLHLYLYNATTL 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 380805869 570 AVVELLLAHGADPTHRLKDGSTMLIEAAKGG--HTNVVSYLLdypNNVLSVPTTDVSQLTP 628
Cdd:PHA03095 98 DVIKLLIKAGADVNAKDKVGRTPLHVYLSGFniNPKVIRLLL---RKGADVNALDLYGMTP 155
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
967-1151 |
3.93e-06 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 51.41 E-value: 3.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 967 DIDAHTESNHDTALTLACAGGHEELVSVliARDAKIEhrDKKGFTPLILAATAGHVGVVEILLDKGGDIEAQsERTKDTP 1046
Cdd:PLN03192 520 HDDPNMASNLLTVASTGNAALLEELLKA--KLDPDIG--DSKGRTPLHIAASKGYEDCVLVLLKHACNVHIR-DANGNTA 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1047 LSLACSGGRQEVVDLLLARGANKEHRNVSDYtpLSLAASGGYVNIIKILLNAGAEINSRtgSKLGISPLMLAAMNGHVPA 1126
Cdd:PLN03192 595 LWNAISAKHHKIFRILYHFASISDPHAAGDL--LCTAAKRNDLTAMKELLKQGLNVDSE--DHQGATALQVAMAEDHVDM 670
|
170 180
....*....|....*....|....*
gi 380805869 1127 VKLLLDMGSDINAQIETNRNTALTL 1151
Cdd:PLN03192 671 VRLLIMNGADVDKANTDDDFSPTEL 695
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
1231-1298 |
4.17e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 51.44 E-value: 4.17e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 380805869 1231 LLIHRGAHIDVRNKKGNTPLWLASNGGHFDVVQLLVQAGADVDAADNRKITPLMSAFRKGHVKVVQYL 1298
Cdd:PTZ00322 100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
233-386 |
5.28e-06 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 50.85 E-value: 5.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 233 ACAGGFVDIVKVLLNEGA--NIEDHNENGHTPLMEAASAG-HVEVARVLLDHGAGINThsnefkESALTLACYKGHLDMV 309
Cdd:TIGR00870 24 AAERGDLASVYRDLEEPKklNINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAV------GDTLLHAISLEYVDAV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 310 ----RFLLEAGADQ-------EHKTDEM---HTALMEACMDGHVEVARLLLDSGAQVNMPA-----------DSF---ES 361
Cdd:TIGR00870 98 eailLHLLAAFRKSgplelanDQYTSEFtpgITALHLAAHRQNYEIVKLLLERGASVPARAcgdffvksqgvDSFyhgES 177
|
170 180
....*....|....*....|....*
gi 380805869 362 PLTLAACGGHVELAALLIERGANLE 386
Cdd:TIGR00870 178 PLNAAACLGSPSIVALLSEDPADIL 202
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
263-367 |
6.06e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 50.67 E-value: 6.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 263 LMEAASAGHVEVARVLLDHGAgiNTHSNEFKESA-LTLACYKGHLDMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEV 341
Cdd:PTZ00322 86 LCQLAASGDAVGARILLTGGA--DPNCRDYDGRTpLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREV 163
|
90 100 110
....*....|....*....|....*....|....*....
gi 380805869 342 ARLLL-----DSGAQVNMPADSF--------ESPLTLAA 367
Cdd:PTZ00322 164 VQLLSrhsqcHFELGANAKPDSFtgkppsleDSPISSHH 202
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
143-381 |
6.59e-06 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 50.85 E-value: 6.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 143 RKLLDEGRSVNEHTEEGESLLCLACSAGYYELAQVLL----AMHANVEDRGNKGDItpLMAASSGGYLDIVKLLLLHDAD 218
Cdd:TIGR00870 1 RGPLDIVPAEESPLSDEEKAFLPAAERGDLASVYRDLeepkKLNINCPDRLGRSAL--FVAAIENENLELTELLLNLSCR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 219 VnsqsATGNTALtYACAGGFVDIVKVLLN-------EGANIEDHNEN-------GHTPLMEAASAGHVEVARVLLDHGAG 284
Cdd:TIGR00870 79 G----AVGDTLL-HAISLEYVDAVEAILLhllaafrKSGPLELANDQytseftpGITALHLAAHRQNYEIVKLLLERGAS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 285 INT--HSNEFKESALT---------LACYK--GHLDMVRFLLEAGADQEhKTDEM-----HTALMEA------------C 334
Cdd:TIGR00870 154 VPAraCGDFFVKSQGVdsfyhgespLNAAAclGSPSIVALLSEDPADIL-TADSLgntllHLLVMENefkaeyeelscqM 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 380805869 335 MDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIER 381
Cdd:TIGR00870 233 YNFALSLLDKLRDSKELEVILNHQGLTPLKLAAKEGRIVLFRLKLAI 279
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
1245-1277 |
6.62e-06 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 44.20 E-value: 6.62e-06
10 20 30
....*....|....*....|....*....|....
gi 380805869 1245 KGNTPLWLAS-NGGHFDVVQLLVQAGADVDAADN 1277
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
315-412 |
7.38e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 50.67 E-value: 7.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 315 AGADQEHKTDE------MHTALMEAC---MDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGANL 385
Cdd:PTZ00322 62 ATPDHNLTTEEvidpvvAHMLTVELCqlaASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADP 141
|
90 100
....*....|....*....|....*..
gi 380805869 386 EEVNDEGYTPLMEAAREGHEEMVALLL 412
Cdd:PTZ00322 142 TLLDKDGKTPLELAEENGFREVVQLLS 168
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
187-233 |
7.42e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 44.64 E-value: 7.42e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 380805869 187 DRGNKGDITPLMAASSGGYLDIVKLLLLHDADVNSQSATGNTALTYA 233
Cdd:pfam13857 10 NRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
209-292 |
7.57e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 50.28 E-value: 7.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 209 VKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVARVLL-----DHGA 283
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSrhsqcHFEL 177
|
....*....
gi 380805869 284 GINTHSNEF 292
Cdd:PTZ00322 178 GANAKPDSF 186
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
1024-1206 |
8.36e-06 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 50.25 E-value: 8.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1024 VVEILLDKGGDieaQSERTKDTPLSLACSGGRQEVVDLLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEIN 1103
Cdd:PLN03192 509 VGDLLGDNGGE---HDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVH 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1104 SRTGSklGISPLMLAAMNGHVPAVKLLLDMGSDINAQIETNrntALTLACFQGRAEVVSLLLDRKANVEHRAKTGLTPLM 1183
Cdd:PLN03192 586 IRDAN--GNTALWNAISAKHHKIFRILYHFASISDPHAAGD---LLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQ 660
|
170 180
....*....|....*....|...
gi 380805869 1184 EAASGGYAEVGRVLLDKGADVNA 1206
Cdd:PLN03192 661 VAMAEDHVDMVRLLIMNGADVDK 683
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
391-423 |
1.24e-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: 43.43 E-value: 1.24e-05
10 20 30
....*....|....*....|....*....|....
gi 380805869 391 EGYTPLMEAA-REGHEEMVALLLAQGANINAQTE 423
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
1045-1096 |
1.28e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 43.80 E-value: 1.28e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 380805869 1045 TPLSLACSGGRQEVVDLLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILL 1096
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
309-378 |
1.56e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 49.51 E-value: 1.56e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 309 VRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALL 378
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
130-285 |
1.86e-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: 49.24 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 130 LAEACSDGDVNAVRKLLdEGRSVNEHTE--EGESLLCLACSAGYYELAQVLLAmhaNVEDRGN--------KGDiTPLMA 199
Cdd:cd22192 21 LLLAAKENDVQAIKKLL-KCPSCDLFQRgaLGETALHVAALYDNLEAAVVLME---AAPELVNepmtsdlyQGE-TALHI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 200 ASSGGYLDIVKLLLLHDADVNSQSATGntalTYacaggFVDIVKVLLNEGanieDHnenghtPLMEAASAGHVEVARVLL 279
Cdd:cd22192 96 AVVNQNLNLVRELIARGADVVSPRATG----TF-----FRPGPKNLIYYG----EH------PLSFAACVGNEEIVRLLI 156
|
....*.
gi 380805869 280 DHGAGI 285
Cdd:cd22192 157 EHGADI 162
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
472-554 |
1.91e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 49.13 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 472 VKYLLASGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGHLCTVQFLISKGANVNRA 551
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFEL 177
|
...
gi 380805869 552 TAN 554
Cdd:PTZ00322 178 GAN 180
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
278-330 |
1.94e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 43.49 E-value: 1.94e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 380805869 278 LLDHGAGINTHSNEFKESALTLACYKGHLDMVRFLLEAGADQEHKTDEMHTAL 330
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
1178-1233 |
2.22e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 43.03 E-value: 2.22e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 380805869 1178 GLTPLMEAASGGYAEVGRVLLDKGADVNAppVPSSRDTALTIAADKGHYKFCELLI 1233
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINA--VDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
1111-1139 |
2.37e-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: 42.24 E-value: 2.37e-05
10 20
....*....|....*....|....*....
gi 380805869 1111 GISPLMLAAMNGHVPAVKLLLDMGSDINA 1139
Cdd:pfam13606 2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
391-420 |
2.46e-05 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 42.19 E-value: 2.46e-05
10 20 30
....*....|....*....|....*....|
gi 380805869 391 EGYTPLMEAAREGHEEMVALLLAQGANINA 420
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
258-286 |
2.58e-05 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 42.19 E-value: 2.58e-05
10 20
....*....|....*....|....*....
gi 380805869 258 NGHTPLMEAASAGHVEVARVLLDHGAGIN 286
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
1111-1267 |
5.48e-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: 47.57 E-value: 5.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1111 GISPLMLAAMN---GHVPAVKLLLDMGSD-------INAQIETNR---NTALTLACFQGRAEVVSLLLDRKANVEHRA-- 1175
Cdd:cd21882 26 GKTCLHKAALNlndGVNEAIMLLLEAAPDsgnpkelVNAPCTDEFyqgQTALHIAIENRNLNLVRLLVENGADVSARAtg 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1176 ----KTGLT-------PLMEAASGGYAEVGRVLLDKGADvnaPPVPSSRDT-------ALTIAADK--GHYKFC----EL 1231
Cdd:cd21882 106 rffrKSPGNlfyfgelPLSLAACTNQEEIVRLLLENGAQ---PAALEAQDSlgntvlhALVLQADNtpENSAFVcqmyNL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 380805869 1232 LIHRGAHID-------VRNKKGNTPLWLASNGGHFDVVQLLVQ 1267
Cdd:cd21882 183 LLSYGAHLDptqqleeIPNHQGLTPLKLAAVEGKIVMFQHILQ 225
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
1119-1208 |
6.47e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 47.59 E-value: 6.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1119 AMNGHVPAVKLLLDMGSDINAQiETNRNTALTLACFQGRAEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLL 1198
Cdd:PTZ00322 90 AASGDAVGARILLTGGADPNCR-DYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
|
90
....*....|....*
gi 380805869 1199 -----DKGADVNAPP 1208
Cdd:PTZ00322 169 rhsqcHFELGANAKP 183
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
1015-1119 |
7.61e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 47.20 E-value: 7.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1015 LAATAGHVGVvEILLDKGGDIEAQsERTKDTPLSLACSGGRQEVVDLLLARGANKEHRNVSDYTPLSLAASGGYVNIIKI 1094
Cdd:PTZ00322 89 LAASGDAVGA-RILLTGGADPNCR-DYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166
|
90 100 110
....*....|....*....|....*....|....*.
gi 380805869 1095 LL---------NAGAEINSRTG--SKLGISPLMLAA 1119
Cdd:PTZ00322 167 LSrhsqchfelGANAKPDSFTGkpPSLEDSPISSHH 202
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
239-499 |
8.01e-05 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 46.75 E-value: 8.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 239 VDIVKVLLNEGANIEDHNENGHTPLMEAASaghvevarvlldhgaginthsnEFKEsaltlacYKGHLDMVRFLLEAGAD 318
Cdd:PHA02798 51 TDIVKLFINLGANVNGLDNEYSTPLCTILS----------------------NIKD-------YKHMLDIVKILIENGAD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 319 QEHKTDEMHTALMEACMDGHV---EVARLLLDSGAQVNM-PADSFESPLTLAACGGHV--ELAALLIERGANLEEVND-E 391
Cdd:PHA02798 102 INKKNSDGETPLYCLLSNGYInnlEILLFMIENGADTTLlDKDGFTMLQVYLQSNHHIdiEIIKLLLEKGVDINTHNNkE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 392 GYTPLMEAAREGHE----EMVALLLAQGANINAQTEETQETALT-----LACCGGF-SEVADFLIKAgADI----ELGCs 457
Cdd:PHA02798 182 KYDTLHCYFKYNIDridaDILKLFVDNGFIINKENKSHKKKFMEylnslLYDNKRFkKNILDFIFSY-IDInqvdELGF- 259
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 380805869 458 TPLMEASQEGHLELVKYLLASGANVHATTATGDTALTYACEN 499
Cdd:PHA02798 260 NPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFEN 301
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
391-420 |
8.56e-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: 40.70 E-value: 8.56e-05
10 20 30
....*....|....*....|....*....|
gi 380805869 391 EGYTPLMEAAREGHEEMVALLLAQGANINA 420
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
127-226 |
9.74e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 46.82 E-value: 9.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 127 TRSLAEACSDGDVNAVRKLLDEGRSVNEHTEEGESLLCLACSAGYYELAQVLLAMHANVE--DRGNKgdiTPLMAASSGG 204
Cdd:PTZ00322 83 TVELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTllDKDGK---TPLELAEENG 159
|
90 100
....*....|....*....|..
gi 380805869 205 YLDIVKLLLLHDADVNSQSATG 226
Cdd:PTZ00322 160 FREVVQLLSRHSQCHFELGANA 181
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
1024-1255 |
1.09e-04 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 46.37 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1024 VVEILLDKGGDIEAQsERTKDTPLSLACSGGRQ-----EVVDLLLARGANKEHRNVSDYTPLSLAASGGYVN---IIKIL 1095
Cdd:PHA02798 53 IVKLFINLGANVNGL-DNEYSTPLCTILSNIKDykhmlDIVKILIENGADINKKNSDGETPLYCLLSNGYINnleILLFM 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1096 LNAGAEINSRtgSKLGISPLMLAAMNGH---VPAVKLLLDMGSDINaqIETNRNTALTLACFQGR------AEVVSLLLD 1166
Cdd:PHA02798 132 IENGADTTLL--DKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDIN--THNNKEKYDTLHCYFKYnidridADILKLFVD 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1167 -----RKANVEHRAKtgLTPLMEAASGGYAEVGRVLLD---KGADVNAPPVPSSrdTALTIAADKGHYKFCELLIHRGAH 1238
Cdd:PHA02798 208 ngfiiNKENKSHKKK--FMEYLNSLLYDNKRFKKNILDfifSYIDINQVDELGF--NPLYYSVSHNNRKIFEYLLQLGGD 283
|
250
....*....|....*..
gi 380805869 1239 IDVRNKKGNTPLWLASN 1255
Cdd:PHA02798 284 INIITELGNTCLFTAFE 300
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
997-1050 |
1.13e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 41.18 E-value: 1.13e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 380805869 997 ARDAKIEHRDKKGFTPLILAATAGHVGVVEILLDKGGDIEAQSERTKdTPLSLA 1050
Cdd:pfam13857 4 HGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGL-TALDLA 56
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
240-412 |
1.16e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411978 [Multi-domain] Cd Length: 680 Bit Score: 46.68 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 240 DIVKVLLNegANIEDHNENGHTPLMEAASAGHVEVARVLLDHGAGIN----------THSNE---FKESALTLACYKGHL 306
Cdd:cd22194 124 GILDRFIN--AEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNahakgvffnpKYKHEgfyFGETPLALAACTNQP 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 307 DMVRFLLEAGADQEHKTDEMHTALMEACmdghVEVARlllDSGAQVNMPADSFESPLTlaACGGHvelaalliergaNLE 386
Cdd:cd22194 202 EIVQLLMEKESTDITSQDSRGNTVLHAL----VTVAE---DSKTQNDFVKRMYDMILL--KSENK------------NLE 260
|
170 180
....*....|....*....|....*..
gi 380805869 387 EV-NDEGYTPLMEAAREGHEEMVALLL 412
Cdd:cd22194 261 TIrNNEGLTPLQLAAKMGKAEILKYIL 287
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
1111-1139 |
1.17e-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: 40.26 E-value: 1.17e-04
10 20
....*....|....*....|....*....
gi 380805869 1111 GISPLMLAAMNGHVPAVKLLLDMGSDINA 1139
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PHA02884 |
PHA02884 |
ankyrin repeat protein; Provisional |
238-335 |
1.70e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165212 [Multi-domain] Cd Length: 300 Bit Score: 45.36 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 238 FVDIVKVLLNEGANIE---DHNENGHT-PLMEAASAGHVEVARVLLDHGAGINTHSNEFKESALTLACYKGHLDMVRFLL 313
Cdd:PHA02884 45 YTDIIDAILKLGADPEapfPLSENSKTnPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKITPLYISVLHGCLKCLEILL 124
|
90 100
....*....|....*....|..
gi 380805869 314 EAGADQEHKTDEMHTALMEACM 335
Cdd:PHA02884 125 SYGADINIQTNDMVTPIELALM 146
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
258-287 |
1.91e-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.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 39.93 E-value: 1.91e-04
10 20 30
....*....|....*....|....*....|
gi 380805869 258 NGHTPLMEAASAGHVEVARVLLDHGAGINT 287
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
378-433 |
2.12e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 40.41 E-value: 2.12e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 380805869 378 LIERG-ANLEEVNDEGYTPLMEAAREGHEEMVALLLAQGANINAQTEETqETALTLA 433
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEG-LTALDLA 56
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
226-254 |
2.15e-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: 39.49 E-value: 2.15e-04
10 20
....*....|....*....|....*....
gi 380805869 226 GNTALTYACAGGFVDIVKVLLNEGANIED 254
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
522-549 |
2.39e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 39.49 E-value: 2.39e-04
10 20
....*....|....*....|....*...
gi 380805869 522 GRTPLMKAARAGHLCTVQFLISKGANVN 549
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
1245-1274 |
2.62e-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: 39.49 E-value: 2.62e-04
10 20 30
....*....|....*....|....*....|
gi 380805869 1245 KGNTPLWLASNGGHFDVVQLLVQAGADVDA 1274
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
211-263 |
2.76e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 40.02 E-value: 2.76e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 380805869 211 LLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPL 263
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
258-286 |
2.76e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. 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: 39.58 E-value: 2.76e-04
10 20 30
....*....|....*....|....*....|
gi 380805869 258 NGHTPLMEAA-SAGHVEVARVLLDHGAGIN 286
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVN 30
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
700-786 |
3.09e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 3.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 700 VEETEGKLNELGQRISAIEKaqlksleliqgeplNKDKIEELKKNREEQVQKKKKILKELQKVERQLqmKTQQQFTKEYL 779
Cdd:PRK03918 233 LEELKEEIEELEKELESLEG--------------SKRKLEEKIRELEERIEELKKEIEELEEKVKEL--KELKEKAEEYI 296
|
....*..
gi 380805869 780 ETKGQKD 786
Cdd:PRK03918 297 KLSEFYE 303
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
161-213 |
3.13e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 39.95 E-value: 3.13e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 380805869 161 SLLCLACSAGYYELAQVLLAMHANVEDRgNKGDITPLMAASSGGYLDIVKLLL 213
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAV-DGNGETALHFAASNGNVEVLKLLL 54
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
399-525 |
3.23e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 45.27 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 399 AAREGHEEMVAlllaqGANINAQTEETQETA----LTLACC----GGFSEVADFLIKAGAD---IELGCSTPLMEASQEG 467
Cdd:PTZ00322 52 EALEATENKDA-----TPDHNLTTEEVIDPVvahmLTVELCqlaaSGDAVGARILLTGGADpncRDYDGRTPLHIACANG 126
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 380805869 468 HLELVKYLLASGANVHATTATGDTALTYACENGHTDVADVLLqaGADLEHESEGGRTP 525
Cdd:PTZ00322 127 HVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS--RHSQCHFELGANAK 182
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
206-320 |
3.29e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 43.65 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 206 LDIVKLLLLHDADVNSQSATGNTAL--TYACAGGFV--DIVKVLLNEGANIEDHNENGHTPL---MEAASAgHVEVARVL 278
Cdd:PHA02859 66 VEILKFLIENGADVNFKTRDNNLSAlhHYLSFNKNVepEILKILIDSGSSITEEDEDGKNLLhmyMCNFNV-RINVIKLL 144
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 380805869 279 LDHGAGINTHSNEFKESALTLACYKGHLDMVRFLLEAGADQE 320
Cdd:PHA02859 145 IDSGVSFLNKDFDNNNILYSYILFHSDKKIFDFLTSLGIDIN 186
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
489-516 |
3.31e-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: 39.11 E-value: 3.31e-04
10 20
....*....|....*....|....*...
gi 380805869 489 GDTALTYACENGHTDVADVLLQAGADLE 516
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
127-220 |
4.18e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 44.60 E-value: 4.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 127 TRSLAEACSDGDVNAVRKLLDEGRSVNEHTEEGESLLCLACSAGYYELAQVLLAMHANVEDRGNKGDITPLMAASSGGYL 206
Cdd:PHA02875 136 FSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKI 215
|
90
....*....|....
gi 380805869 207 DIVKLLLLHDADVN 220
Cdd:PHA02875 216 DIVRLFIKRGADCN 229
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
522-552 |
4.30e-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: 4.30e-04
10 20 30
....*....|....*....|....*....|..
gi 380805869 522 GRTPLMKAA-RAGHLCTVQFLISKGANVNRAT 552
Cdd:pfam00023 2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
257-476 |
4.37e-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: 4.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 257 ENGHTPLMEAasaghvevarvLLDhgagINTHSNEFKESALTLACYKGHLDmvRFLleaGADQEHKTDEMHTALMEACMD 336
Cdd:cd22194 92 DTGKTCLMKA-----------LLN----INENTKEIVRILLAFAEENGILD--RFI---NAEYTEEAYEGQTALNIAIER 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 337 GHVEVARLLLDSGAQVNMPA-----------DSF---ESPLTLAACGGHVELAALLIERGANLEEVNDE-GYTPLmeaar 401
Cdd:cd22194 152 RQGDIVKLLIAKGADVNAHAkgvffnpkykhEGFyfgETPLALAACTNQPEIVQLLMEKESTDITSQDSrGNTVL----- 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 402 egHeemvALLLAqganinAQTEETQETALTlaccggfsEVADFLIKAGADIELGCS------TPLMEASQEGHLELVKYL 475
Cdd:cd22194 227 --H----ALVTV------AEDSKTQNDFVK--------RMYDMILLKSENKNLETIrnneglTPLQLAAKMGKAEILKYI 286
|
.
gi 380805869 476 L 476
Cdd:cd22194 287 L 287
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
522-549 |
4.91e-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.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 38.78 E-value: 4.91e-04
10 20
....*....|....*....|....*...
gi 380805869 522 GRTPLMKAARAGHLCTVQFLISKGANVN 549
Cdd:pfam13606 2 GNTPLHLAARNGRLEIVKLLLENGADIN 29
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
1008-1037 |
5.74e-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: 5.74e-04
10 20 30
....*....|....*....|....*....|
gi 380805869 1008 KGFTPLILAATAGHVGVVEILLDKGGDIEA 1037
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
245-300 |
5.77e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 39.25 E-value: 5.77e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 380805869 245 LLNEG-ANIEDHNENGHTPLMEAASAGHVEVARVLLDHGAGINThSNEFKESALTLA 300
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNL-KDEEGLTALDLA 56
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
1011-1063 |
5.88e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 39.18 E-value: 5.88e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 380805869 1011 TPLILAATAGHVGVVEILLDKGGDIEAQSERtKDTPLSLACSGGRQEVVDLLL 1063
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGN-GETALHFAASNGNVEVLKLLL 54
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
451-496 |
5.95e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 39.25 E-value: 5.95e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 380805869 451 DIELGCSTPLMEASQEGHLELVKYLLASGANVHATTATGDTALTYA 496
Cdd:pfam13857 11 RLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
462-550 |
5.95e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 44.28 E-value: 5.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 462 EASQEGHLELVKYLLASGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGHLCTVQFL 541
Cdd:PHA02876 151 ERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAI 230
|
....*....
gi 380805869 542 ISKGANVNR 550
Cdd:PHA02876 231 IDNRSNINK 239
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
1111-1140 |
6.43e-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: 6.43e-04
10 20 30
....*....|....*....|....*....|.
gi 380805869 1111 GISPLMLAA-MNGHVPAVKLLLDMGSDINAQ 1140
Cdd:pfam00023 2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNAR 32
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
1192-1298 |
6.89e-04 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 44.09 E-value: 6.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1192 EVGRVLLDKGADVNAPPVPSSrdtALTIAAdKGHYKFCELLIHRGAHIDVRNKKGNTPLWLASNGGHFDVVQLLVQAGAD 1271
Cdd:PLN03192 508 NVGDLLGDNGGEHDDPNMASN---LLTVAS-TGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACN 583
|
90 100
....*....|....*....|....*..
gi 380805869 1272 VDAADNRKITPLMSAFRKGHVKVVQYL 1298
Cdd:PLN03192 584 VHIRDANGNTALWNAISAKHHKIFRIL 610
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
1095-1152 |
7.60e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 38.87 E-value: 7.60e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 380805869 1095 LLNAGAeINSRTGSKLGISPLMLAAMNGHVPAVKLLLDMGSDINAQiETNRNTALTLA 1152
Cdd:pfam13857 1 LLEHGP-IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLK-DEEGLTALDLA 56
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
980-1168 |
7.68e-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: 43.92 E-value: 7.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 980 LTLACAGGHEELVSVLIARDAKIEHRDKkgftpLILAATAGHVGVVE----ILLDKGGDI--------EAQSERTKD-TP 1046
Cdd:TIGR00870 57 FVAAIENENLELTELLLNLSCRGAVGDT-----LLHAISLEYVDAVEaillHLLAAFRKSgplelandQYTSEFTPGiTA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1047 LSLACSGGRQEVVDLLLARGAN------------KEHRNVSDYT--PLSLAASGGYVNIIKILLNAGAEInsRTGSKLGI 1112
Cdd:TIGR00870 132 LHLAAHRQNYEIVKLLLERGASvparacgdffvkSQGVDSFYHGesPLNAAACLGSPSIVALLSEDPADI--LTADSLGN 209
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 380805869 1113 SPLMLAAMNGHVPAV---------KLLLDMG--SDINAQIE--TNRN--TALTLACFQGRAEVVSLLLDRK 1168
Cdd:TIGR00870 210 TLLHLLVMENEFKAEyeelscqmyNFALSLLdkLRDSKELEviLNHQglTPLKLAAKEGRIVLFRLKLAIK 280
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
1231-1283 |
7.76e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 38.87 E-value: 7.76e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 380805869 1231 LLIHRGAHIDVRNKKGNTPLWLASNGGHFDVVQLLVQAGADVDAADNRKITPL 1283
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
1145-1198 |
7.82e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 38.79 E-value: 7.82e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 380805869 1145 RNTALTLACFQGRAEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLL 1198
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
968-1097 |
9.55e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411978 [Multi-domain] Cd Length: 680 Bit Score: 43.59 E-value: 9.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 968 IDA-HTESNHD--TALTLACAGGHEELVSVLIARDAKIEHRDKKGF--------------TPLILAATAGHVGVVEILLD 1030
Cdd:cd22194 130 INAeYTEEAYEgqTALNIAIERRQGDIVKLLIAKGADVNAHAKGVFfnpkykhegfyfgeTPLALAACTNQPEIVQLLME 209
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 380805869 1031 KGGDIEAQSERTKDTPL---------SLACSGGRQEVVDLLLARGANKE---HRNVSDYTPLSLAASGGYVNIIKILLN 1097
Cdd:cd22194 210 KESTDITSQDSRGNTVLhalvtvaedSKTQNDFVKRMYDMILLKSENKNletIRNNEGLTPLQLAAKMGKAEILKYILS 288
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
458-484 |
1.07e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 37.57 E-value: 1.07e-03
10 20
....*....|....*....|....*..
gi 380805869 458 TPLMEASQEGHLELVKYLLASGANVHA 484
Cdd:smart00248 4 TPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
327-354 |
1.34e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 37.57 E-value: 1.34e-03
10 20
....*....|....*....|....*...
gi 380805869 327 HTALMEACMDGHVEVARLLLDSGAQVNM 354
Cdd:smart00248 3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
458-486 |
1.41e-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: 37.65 E-value: 1.41e-03
10 20 30
....*....|....*....|....*....|
gi 380805869 458 TPLMEAS-QEGHLELVKYLLASGANVHATT 486
Cdd:pfam00023 4 TPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
304-558 |
1.63e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).
Pssm-ID: 411975 [Multi-domain] Cd Length: 600 Bit Score: 42.94 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 304 GHLDMVRFLLEAGADQEHKTDEmhTALMEACM---DGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIE 380
Cdd:cd21882 6 GLLECLRWYLTDSAYQRGATGK--TCLHKAALnlnDGVNEAIMLLLEAAPDSGNPKELVNAPCTDEFYQGQTALHIAIEN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 381 RGANLeevndegytplmeaaregheemVALLLAQGANINAqteetqetaltlACCGgfsevaDFLIKAGADIELGCSTPL 460
Cdd:cd21882 84 RNLNL----------------------VRLLVENGADVSA------------RATG------RFFRKSPGNLFYFGELPL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 461 MEASQEGHLELVKYLLASGANVHATTAT---GDTAL---------TYACENGHTDVADVLLQAGADLEH-------ESEG 521
Cdd:cd21882 124 SLAACTNQEEIVRLLLENGAQPAALEAQdslGNTVLhalvlqadnTPENSAFVCQMYNLLLSYGAHLDPtqqleeiPNHQ 203
|
250 260 270
....*....|....*....|....*....|....*..
gi 380805869 522 GRTPLMKAARAGHLCTVQFLISKGANVNRATANNDHT 558
Cdd:cd21882 204 GLTPLKLAAVEGKIVMFQHILQREFSGPYQPLSRKFT 240
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
195-222 |
1.70e-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: 37.27 E-value: 1.70e-03
10 20
....*....|....*....|....*....
gi 380805869 195 TPLM-AASSGGYLDIVKLLLLHDADVNSQ 222
Cdd:pfam00023 4 TPLHlAAGRRGNLEIVKLLLSKGADVNAR 32
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
1008-1038 |
2.09e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 36.88 E-value: 2.09e-03
10 20 30
....*....|....*....|....*....|..
gi 380805869 1008 KGFTPLILAAT-AGHVGVVEILLDKGGDIEAQ 1038
Cdd:pfam00023 1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNAR 32
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
489-517 |
2.14e-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: 2.14e-03
10 20
....*....|....*....|....*....
gi 380805869 489 GDTALTYACENGHTDVADVLLQAGADLEH 517
Cdd:pfam13606 2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
1076-1103 |
2.23e-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: 2.23e-03
10 20
....*....|....*....|....*...
gi 380805869 1076 DYTPLSLAASGGYVNIIKILLNAGAEIN 1103
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
|
|
| TRPV1-4 |
cd22193 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ... |
328-544 |
2.43e-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: 42.09 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 328 TALMEACM---DGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAaLLIERganleevndegytplmeaaREGH 404
Cdd:cd22193 31 TCLMKALLnlnPGTNDTIRILLDIAEKTDNLKRFINAEYTDEYYEGQTALH-IAIER-------------------RQGD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 405 eeMVALLLAQGANINAQTeetqetaltlacCGGFsevadFLIKAGADIELGCSTPLMEASQEGHLELVKYLLASG---AN 481
Cdd:cd22193 91 --IVALLVENGADVHAHA------------KGRF-----FQPKYQGEGFYFGELPLSLAACTNQPDIVQYLLENEhqpAD 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 380805869 482 VHATTATGDT---ALTYACENGHTDVA------DVLLQAGADLEHESE-------GGRTPLMKAARAGHLCTVQFLISK 544
Cdd:cd22193 152 IEAQDSRGNTvlhALVTVADNTKENTKfvtrmyDMILIRGAKLCPTVEleeirnnDGLTPLQLAAKMGKIEILKYILQR 230
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
1227-1283 |
2.65e-03 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 41.96 E-value: 2.65e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 380805869 1227 KFCELLIHRGAHIDVRNKKGNTPLWLASNGGHFDVVQLLVQAGADVDAADNRKITPL 1283
Cdd:PHA02946 53 RFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPL 109
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
328-452 |
3.38e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 41.92 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 328 TALMEACMDGHVE-VARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIE---RGANLEEVND--EGYTPLMEAAR 401
Cdd:cd22192 19 SPLLLAAKENDVQaIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEaapELVNEPMTSDlyQGETALHIAVV 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 380805869 402 EGHEEMVALLLAQGAN-INAQTEET------------QETALTLACCGGFSEVADFLIKAGADI 452
Cdd:cd22192 99 NQNLNLVRELIARGADvVSPRATGTffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADI 162
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
163-256 |
3.39e-03 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 41.81 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 163 LCLACSAGYYELAQVLLAMHANVEDRGNKGDiTPLMAASSGGYLDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIV 242
Cdd:PTZ00322 86 LCQLAASGDAVGARILLTGGADPNCRDYDGR-TPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV 164
|
90
....*....|....
gi 380805869 243 KVLLneGANIEDHN 256
Cdd:PTZ00322 165 QLLS--RHSQCHFE 176
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
365-471 |
3.39e-03 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 41.81 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 365 LAACGGHVElAALLIERGANLEEVNDEGYTPLMEAAREGHEEMVALLLAQGANINAqTEETQETALTLACCGGFSEVADF 444
Cdd:PTZ00322 89 LAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTL-LDKDGKTPLELAEENGFREVVQL 166
|
90 100
....*....|....*....|....*....
gi 380805869 445 LIK-AGADIELG-CSTPLMEASQEGHLEL 471
Cdd:PTZ00322 167 LSRhSQCHFELGaNAKPDSFTGKPPSLED 195
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
1163-1220 |
3.40e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 36.94 E-value: 3.40e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 380805869 1163 LLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAPpvPSSRDTALTIA 1220
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLK--DEEGLTALDLA 56
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
701-786 |
3.73e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 3.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 701 EETEGKLNELGQRISAIEKaqlkslELIQGEPLNKdKIEELKKNREEQVQKKKKILKELQKV------ERQLQMKTQQQF 774
Cdd:PRK03918 528 EKLKEKLIKLKGEIKSLKK------ELEKLEELKK-KLAELEKKLDELEEELAELLKELEELgfesveELEERLKELEPF 600
|
90
....*....|..
gi 380805869 775 TKEYLETKGQKD 786
Cdd:PRK03918 601 YNEYLELKDAEK 612
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
1245-1274 |
3.83e-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: 36.08 E-value: 3.83e-03
10 20 30
....*....|....*....|....*....|
gi 380805869 1245 KGNTPLWLASNGGHFDVVQLLVQAGADVDA 1274
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
290-419 |
4.32e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 40.19 E-value: 4.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 290 NEFKESALtLACY---KGHLDMVRFLLEAGADQEHKTDEMHTALMEACM----DGHVEVARLLLDSGAQVNMPADSFESP 362
Cdd:PHA02859 48 NDLYETPI-FSCLekdKVNVEILKFLIENGADVNFKTRDNNLSALHHYLsfnkNVEPEILKILIDSGSSITEEDEDGKNL 126
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 380805869 363 L--TLAACGGHVELAALLIERGANLEEVNDEG----YTPLMeaaREGHEEMVALLLAQGANIN 419
Cdd:PHA02859 127 LhmYMCNFNVRINVIKLLIDSGVSFLNKDFDNnnilYSYIL---FHSDKKIFDFLTSLGIDIN 186
|
|
| PHA02795 |
PHA02795 |
ankyrin-like protein; Provisional |
206-276 |
4.45e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165157 [Multi-domain] Cd Length: 437 Bit Score: 41.13 E-value: 4.45e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 380805869 206 LDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVAR 276
Cdd:PHA02795 201 LEIYKLCIPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRGSVIARR 271
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
1195-1304 |
4.47e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 41.36 E-value: 4.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1195 RVLLDKGADVNAppVPSSRDTAL-TIAADKGHYK----FCELLIHRGAHIDVRNKKGNTPLW-LASNG--GHFDVVQLLV 1266
Cdd:PHA02798 55 KLFINLGANVNG--LDNEYSTPLcTILSNIKDYKhmldIVKILIENGADINKKNSDGETPLYcLLSNGyiNNLEILLFMI 132
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 380805869 1267 QAGADVDAADNRKITPLMSAFRKGH---VKVVQYLVK---EVNQ 1304
Cdd:PHA02798 133 ENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEkgvDINT 176
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
1137-1263 |
4.53e-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: 41.28 E-value: 4.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1137 INAQIeTNRN----TALTLACFQGRAEVVSLLLDRKANVEHRAKT--------------GLTPLMEAASGGYAEVGRVLL 1198
Cdd:cd22194 130 INAEY-TEEAyegqTALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEIVQLLM 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1199 DKGADVNappvpSSRDT-------ALTIAAD--KGHYKFCE------LLIHRGAHID-VRNKKGNTPLWLASNGGHFDVV 1262
Cdd:cd22194 209 EKESTDI-----TSQDSrgntvlhALVTVAEdsKTQNDFVKrmydmiLLKSENKNLEtIRNNEGLTPLQLAAKMGKAEIL 283
|
.
gi 380805869 1263 Q 1263
Cdd:cd22194 284 K 284
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
1061-1118 |
4.99e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 36.56 E-value: 4.99e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 380805869 1061 LLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSRTGSklGISPLMLA 1118
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEE--GLTALDLA 56
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
195-220 |
5.04e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 35.64 E-value: 5.04e-03
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
295-318 |
5.09e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 35.64 E-value: 5.09e-03
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
1044-1267 |
6.10e-03 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 41.22 E-value: 6.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1044 DTPLSLACSGGR-QEVVDLLLarganKEHRNVSDYTPLSLAASGGYVN----IIKILLNAGAE------INSRTGSKL-- 1110
Cdd:TIGR00870 53 RSALFVAAIENEnLELTELLL-----NLSCRGAVGDTLLHAISLEYVDaveaILLHLLAAFRKsgplelANDQYTSEFtp 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1111 GISPLMLAAMNGHVPAVKLLLDMGSDINAQ------IETNRNTAL--------TLACFqGRAEVVSLLLDRKANVEHRAK 1176
Cdd:TIGR00870 128 GITALHLAAHRQNYEIVKLLLERGASVPARacgdffVKSQGVDSFyhgesplnAAACL-GSPSIVALLSEDPADILTADS 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1177 TGLTPL----MEAA-SGGYAEVGRVLLDKGADVNAPPVPSSrdtaltiaadkghykfcELLIhrgahidVRNKKGNTPLW 1251
Cdd:TIGR00870 207 LGNTLLhllvMENEfKAEYEELSCQMYNFALSLLDKLRDSK-----------------ELEV-------ILNHQGLTPLK 262
|
250
....*....|....*.
gi 380805869 1252 LASNGGHFDVVQLLVQ 1267
Cdd:TIGR00870 263 LAAKEGRIVLFRLKLA 278
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
696-767 |
6.32e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 6.32e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 380805869 696 LECIVEETEGKLNELGQRISAIEKaQLKSLELIQGEplnKDKIEELKKNREEQVQKKKKILKELQKVERQLQ 767
Cdd:PRK03918 257 LEEKIRELEERIEELKKEIEELEE-KVKELKELKEK---AEEYIKLSEFYEEYLDELREIEKRLSRLEEEIN 324
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
1008-1124 |
6.40e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 40.77 E-value: 6.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1008 KGFTPLILAATAGHVGVVEILLDKGGDIeaQSERTKDT---------------PLSLACSGGRQEVVDLLLARGANKEHR 1072
Cdd:cd22192 88 QGETALHIAVVNQNLNLVRELIARGADV--VSPRATGTffrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQ 165
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1073 NVSDYTP---LSLAASGGYV-NIIKILLNAGAEINSRTGSKL----GISPLMLAAMNGHV 1124
Cdd:cd22192 166 DSLGNTVlhiLVLQPNKTFAcQMYDLILSYDKEDDLQPLDLVpnnqGLTPFKLAAKEGNI 225
|
|
| PHA02989 |
PHA02989 |
ankyrin repeat protein; Provisional |
1001-1069 |
6.98e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222954 [Multi-domain] Cd Length: 494 Bit Score: 40.49 E-value: 6.98e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 380805869 1001 KIEHRDKKGFTPLILAATAGHVGVVEILLDKGGDIEAQSeRTKDTPLSLACSGGRQEVVDLLLARGANK 1069
Cdd:PHA02989 248 KINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVS-KDGDTVLTYAIKHGNIDMLNRILQLKPGK 315
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
715-785 |
7.38e-03 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 40.10 E-value: 7.38e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 380805869 715 SAIEKAQLKSLELIQGEPLNKDKIEELKKNREEQVQKKKKILKELQKVERQLqmktqQQFTKEYLETKGQK 785
Cdd:COG4026 114 NAIIRAGLKSLQNIPEYNELREELLELKEKIDEIAKEKEKLTKENEELESEL-----EELREEYKKLREEN 179
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
328-354 |
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.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 35.31 E-value: 7.41e-03
10 20
....*....|....*....|....*..
gi 380805869 328 TALMEACMDGHVEVARLLLDSGAQVNM 354
Cdd:pfam13606 4 TPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
1127-1278 |
8.87e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 40.20 E-value: 8.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1127 VKLLLDMGSDINAqIETNRNTAL-----TLACFQGRAEVVSLLLDRKANVEHRAKTGLTPLMEAASGGY---AEVGRVLL 1198
Cdd:PHA02798 54 VKLFINLGANVNG-LDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYinnLEILLFMI 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380805869 1199 DKGADvnappvpssrdtalTIAADKGHYKFCELLIHRGAHIDVrnkkgntplwlasngghfDVVQLLVQAGADVDAADNR 1278
Cdd:PHA02798 133 ENGAD--------------TTLLDKDGFTMLQVYLQSNHHIDI------------------EIIKLLLEKGVDINTHNNK 180
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
226-252 |
9.20e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 34.93 E-value: 9.20e-03
10 20
....*....|....*....|....*..
gi 380805869 226 GNTALTYACAGGFVDIVKVLLNEGANI 252
Cdd:pfam13606 2 GNTPLHLAARNGRLEIVKLLLENGADI 28
|
|
|