|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
379-672 |
1.61e-60 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 209.43 E-value: 1.61e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 379 LDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGHTEVVSALLYAGVKV 458
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 459 DCADADSRTALRAAAWGGHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLDHGAEVNHEDVDGRTALSVA 538
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 539 alcvpASKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVV 618
Cdd:COG0666 161 -----AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIV 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 268607595 619 NTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDENHRDDAGWTPL 672
Cdd:COG0666 236 KLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
450-738 |
1.75e-58 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 203.65 E-value: 1.75e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 450 ALLYAGVKVDCADADSRTALRAAAWGGHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLDHGAEVNHEDV 529
Cdd:COG0666 6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 530 DGRTALSVAAlcvpaSKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAA 609
Cdd:COG0666 86 GGNTLLHAAA-----RNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 610 ASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRLICEALIE 689
Cdd:COG0666 161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 268607595 690 QGARTNEIDNDGRIPFILASQEGHYDCVQILLENKSNIDQRGYDGRNAL 738
Cdd:COG0666 241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
654-923 |
8.68e-58 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 201.72 E-value: 8.68e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 654 LLDRGLDENHRDDAGWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIPFILASQEGHYDCVQILLENKSNIDQRGYD 733
Cdd:COG0666 7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 734 GRNALRVAALEGHRDIVELLFSHGADVNCKDADGRPTLYILALENQLTMAEYFLENGANVEASDAEGRTALHVSCWQGHM 813
Cdd:COG0666 87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 814 EMVQVLIAYHADVNAADNEKRSALQSAAWQGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQEGHIDVVQVLLEHGADPN 893
Cdd:COG0666 167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246
|
250 260 270
....*....|....*....|....*....|
gi 268607595 894 HADQFGRTAMRVAAKNGHSQIIKLLEKYGA 923
Cdd:COG0666 247 AKDKDGLTALLLAAAAGAALIVKLLLLALL 276
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
352-639 |
1.12e-56 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 198.25 E-value: 1.12e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 352 LLDNGASVNQCDSNGRTLLANAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLIGCGANINHTDQD 431
Cdd:COG0666 7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 432 GWTALRSAAWGGHTEVVSALLYAGVKVDCADADSRTALRAAAWGGHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHR 511
Cdd:COG0666 87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 512 EIVEHLLDHGAEVNHEDVDGRTALSVAalcvpASKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEG 591
Cdd:COG0666 167 EIVKLLLEAGADVNARDNDGETPLHLA-----AENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 268607595 592 GADVDHTDNNGRTPLLAAASMGHASVVNTLLFWGAAVDSIDSEGRTVL 639
Cdd:COG0666 242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
682-923 |
2.86e-55 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 194.40 E-value: 2.86e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 682 LICEALIEQGARTNEIDNDGRIPFILASQEGHYDCVQILLENKSNIDQRGYDGRNALRVAALEGHRDIVELLFSHGADVN 761
Cdd:COG0666 2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 762 CKDADGRPTLYILALENQLTMAEYFLENGANVEASDAEGRTALHVSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSAA 841
Cdd:COG0666 82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 842 WQGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQEGHIDVVQVLLEHGADPNHADQFGRTAMRVAAKNGHSQIIKLLEKY 921
Cdd:COG0666 162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
|
..
gi 268607595 922 GA 923
Cdd:COG0666 242 GA 243
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
549-837 |
1.73e-53 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 189.01 E-value: 1.73e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 549 ASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLLFWGAAV 628
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 629 DSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIPFILA 708
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 709 SQEGHYDCVQILLENKSNIDQRGYDGRNALRVAALEGHRDIVELLFSHGADVNCKDADGRPTLYILALENQLTMAEYFLE 788
Cdd:COG0666 161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 268607595 789 NGANVEASDAEGRTALHVSCWQGHMEMVQVLIAYHADVNAADNEKRSAL 837
Cdd:COG0666 241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
316-573 |
4.18e-53 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 188.24 E-value: 4.18e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 316 EVLQLLVKAGAHVNSEDDRTSCIVRQALEREDSIRTLLDNGASVNQCDSNGRTLLANAAYSGSLDVVNLLVSRGADLEIE 395
Cdd:COG0666 37 LLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNAR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 396 DAHGHTPLTLAARQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGHTEVVSALLYAGVKVDCADADSRTALRAAAWG 475
Cdd:COG0666 117 DKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAEN 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 476 GHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLDHGAEVNHEDVDGRTALSVAALcvpasKGHASVVSLL 555
Cdd:COG0666 197 GHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAA-----AGAALIVKLL 271
|
250
....*....|....*...
gi 268607595 556 IDRGAEVDHCDKDGMTPL 573
Cdd:COG0666 272 LLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
528-804 |
1.08e-52 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 186.70 E-value: 1.08e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 528 DVDGRTALSVAALCVPASKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLL 607
Cdd:COG0666 13 AALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 608 AAASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRLICEAL 687
Cdd:COG0666 93 AAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 688 IEQGARTNEIDNDGRIPFILASQEGHYDCVQILLENKSNIDQRGYDGRNALRVAALEGHRDIVELLFSHGADVNCKDADG 767
Cdd:COG0666 173 LEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDG 252
|
250 260 270
....*....|....*....|....*....|....*..
gi 268607595 768 RPTLYILALENQLTMAEYFLENGANVEASDAEGRTAL 804
Cdd:COG0666 253 LTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
625-903 |
2.39e-52 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 185.93 E-value: 2.39e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 625 GAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIP 704
Cdd:COG0666 11 LLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 705 FILASQEGHYDCVQILLENKSNIDQRGYDGRNALRVAALEGHRDIVELLFSHGADVNCKDADGRPTLYILALENQLTMAE 784
Cdd:COG0666 91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 785 YFLENGANVEASDAEGRTALHVSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSAAWQGHVKVVQLLIEHGAVVDHTCN 864
Cdd:COG0666 171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250
|
250 260 270
....*....|....*....|....*....|....*....
gi 268607595 865 QGATALCIAAQEGHIDVVQVLLEHGADPNHADQFGRTAM 903
Cdd:COG0666 251 DGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
582-870 |
1.81e-51 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 183.23 E-value: 1.81e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 582 VDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDE 661
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 662 NHRDDAGWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIPFILASQEGHYDCVQILLENKSNIDQRGYDGRNALRVA 741
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 742 ALEGHRDIVELLFSHGADVNCKDADGRPTLYILALENQLTMAEYFLENGANVEASDAEGRTALHVSCWQGHMEMVQVLIA 821
Cdd:COG0666 161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 268607595 822 YHADVNAADNEKRSALQSAAWQGHVKVVQLLIEHGAVVDHTCNQGATAL 870
Cdd:COG0666 241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
264-535 |
1.16e-48 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 175.14 E-value: 1.16e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 264 QAKNLTPLEAQEFALHLINSNLQLETAELALWMIWNGTPVRDSLSTLIPKEQEVLQLLVKAGAHVNSEDDRTSCIVRQAL 343
Cdd:COG0666 16 LLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 344 E--REDSIRTLLDNGASVNQCDSNGRTLLANAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLIGC 421
Cdd:COG0666 96 RngDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 422 GANINHTDQDGWTALRSAAWGGHTEVVSALLYAGVKVDCADADSRTALRAAAWGGHEDIVLNLLQHGAEVNKADNEGRTA 501
Cdd:COG0666 176 GADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTA 255
|
250 260 270
....*....|....*....|....*....|....
gi 268607595 502 LIAAAYMGHREIVEHLLDHGAEVNHEDVDGRTAL 535
Cdd:COG0666 256 LLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
446-728 |
1.47e-36 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 145.17 E-value: 1.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 446 EVVSALLYAGVKVDCADADSRTALRAAAWGGHE---DIVLNLLQHGAEVNKADNEGRTALIAaaYMGH---REIVEHLLD 519
Cdd:PHA03095 28 EEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEkvkDIVRLLLEAGADVNAPERCGFTPLHL--YLYNattLDVIKLLIK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 520 HGAEVNHEDVDGRTALSVAaLCVPASkgHASVVSLLIDRGAEVDHCDKDGMTPL--LVAAYEGHVDVVDLLLEGGADVDH 597
Cdd:PHA03095 106 AGADVNAKDKVGRTPLHVY-LSGFNI--NPKVIRLLLRKGADVNALDLYGMTPLavLLKSRNANVELLRLLIDAGADVYA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 598 TDNNGRTPL--LAAASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVE--VVRTLLDRGLDENHRDDAGWTPLH 673
Cdd:PHA03095 183 VDDRFRSLLhhHLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLH 262
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 268607595 674 MAAFEGHRLICEALIEQGARTNEIDNDGRIPFILASQEGHYDCVQILLENKSNID 728
Cdd:PHA03095 263 YAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAE 317
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
345-657 |
3.32e-32 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 132.07 E-value: 3.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 345 REDSIRTLLDNGASVNQCDSNGRTLLA---NAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHT-KVVNCLIG 420
Cdd:PHA03095 26 TVEEVRRLLAAGADVNFRGEYGKTPLHlylHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 421 CGANINHTDQDGWTALrsaawggHTevvsallYAGVKvdcadadsRTalraaawggHEDIVLNLLQHGAEVNKADNEGRT 500
Cdd:PHA03095 106 AGADVNAKDKVGRTPL-------HV-------YLSGF--------NI---------NPKVIRLLLRKGADVNALDLYGMT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 501 ALiaAAYMGHR----EIVEHLLDHGAEVNHEDVDGRTALSVAALCVpasKGHASVVSLLIDRGAEVDHCDKDGMTPLLVA 576
Cdd:PHA03095 155 PL--AVLLKSRnanvELLRLLIDAGADVYAVDDRFRSLLHHHLQSF---KPRARIVRELIRAGCDPAATDMLGNTPLHSM 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 577 AYEGHVD--VVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRTL 654
Cdd:PHA03095 230 ATGSSCKrsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAA 309
|
...
gi 268607595 655 LDR 657
Cdd:PHA03095 310 LAK 312
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
379-721 |
1.32e-31 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 132.88 E-value: 1.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 379 LDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGHTEVVSALLYAGVKV 458
Cdd:PHA02876 158 LLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNI 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 459 DCADADSRTALRaaawggHEDIVLNLLQH--GAEVNKADNEGRTAL-IAAAYMGHREIVEHLLDHGAEVNHEDVDGRTAL 535
Cdd:PHA02876 238 NKNDLSLLKAIR------NEDLETSLLLYdaGFSVNSIDDCKNTPLhHASQAPSLSRLVPKLLERGADVNAKNIKGETPL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 536 SVAalcvpASKGHASV-VSLLIDRGAEVDHCDKDGMTPLLVAA-YEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMG 613
Cdd:PHA02876 312 YLM-----AKNGYDTEnIRTLIMLGADVNAADRLYITPLHQAStLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRN 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 614 HASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEV-VRTLLDRGLDENHRDDAGWTPLHMAAFEGHRL-ICEALIEQG 691
Cdd:PHA02876 387 NVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVNSKNKDLSTPLHYACKKNCKLdVIEMLLDNG 466
|
330 340 350
....*....|....*....|....*....|
gi 268607595 692 ARTNEIDNDGRIPFILASqeGHYDCVQILL 721
Cdd:PHA02876 467 ADVNAINIQNQYPLLIAL--EYHGIVNILL 494
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
507-835 |
1.13e-29 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 123.92 E-value: 1.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 507 YMGHREIVEHLLDHGAEVNHEDVDGRTALSVAALcvpaSKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVD 586
Cdd:PHA02874 10 YSGDIEAIEKIIKNKGNCINISVDETTTPLIDAI----RSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 587 LLLEGGADvdhtdnngrTPLLAAASMgHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDENHRDD 666
Cdd:PHA02874 86 LLIDNGVD---------TSILPIPCI-EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 667 AGWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIPFILASQEGHYDCVQILLENKSNIDQRGYDGRNALRVAALEgH 746
Cdd:PHA02874 156 NGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIH-N 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 747 RDIVELLFSHgADVNCKDADG-RPTLYILALENQLTMAEYFLENGANVEASDAEGRTALHVSC-WQGHMEMVQVLIAYHA 824
Cdd:PHA02874 235 RSAIELLINN-ASINDQDIDGsTPLHHAINPPCDIDIIDILLYHKADISIKDNKGENPIDTAFkYINKDPVIKDIIANAV 313
|
330
....*....|.
gi 268607595 825 DVNAADNEKRS 835
Cdd:PHA02874 314 LIKEADKLKDS 324
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
584-923 |
1.21e-27 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 120.55 E-value: 1.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 584 VVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDENH 663
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINK 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 664 RDDAGWTPLHMAAFEGHRLiceaLIEQGARTNEIDNDGRIPFILASQEGHYD-CVQILLENKSNIDQRGYDGRNALRVAA 742
Cdd:PHA02876 240 NDLSLLKAIRNEDLETSLL----LYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMA 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 743 LEGH-RDIVELLFSHGADVNCKDadgrpTLYILALENQLTMAEY------FLENGANVEASDAEGRTALHVSCWQGHMEM 815
Cdd:PHA02876 316 KNGYdTENIRTLIMLGADVNAAD-----RLYITPLHQASTLDRNkdivitLLELGANVNARDYCDKTPIHYAAVRNNVVI 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 816 VQVLIAYHADVNAADNEKRSALQSAAWQGH-VKVVQLLIEHGAVVDHTCNQGATALCIAAQEG-HIDVVQVLLEHGADPN 893
Cdd:PHA02876 391 INTLLDYGADIEALSQKIGTALHFALCGTNpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVN 470
|
330 340 350
....*....|....*....|....*....|
gi 268607595 894 HADQFGRTAMRVAAknGHSQIIKLLEKYGA 923
Cdd:PHA02876 471 AINIQNQYPLLIAL--EYHGIVNILLHYGA 498
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
301-538 |
1.60e-27 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 117.82 E-value: 1.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 301 TPVRDSLSTLIPKEQEVLQLLVKAGAHVNSeddRTSC-------IVRQAlEREDSIRTLLDNGASVNQCDSNGRTLLAna 373
Cdd:PHA03095 49 TPLHLYLHYSSEKVKDIVRLLLEAGADVNA---PERCgftplhlYLYNA-TTLDVIKLLIKAGADVNAKDKVGRTPLH-- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 374 AYSGSL----DVVNLLVSRGADLEIEDAHGHTPLT--LAARQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGHT-- 445
Cdd:PHA03095 123 VYLSGFninpKVIRLLLRKGADVNALDLYGMTPLAvlLKSRNANVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPra 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 446 EVVSALLYAGVKVDCADADSRTALRAAAWGGHED--IVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLDHGAE 523
Cdd:PHA03095 203 RIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGAD 282
|
250
....*....|....*
gi 268607595 524 VNHEDVDGRTALSVA 538
Cdd:PHA03095 283 INAVSSDGNTPLSLM 297
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
378-699 |
3.84e-27 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 116.66 E-value: 3.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 378 SLDVVNLLVSRGADLEIEDAHGHTPLTLAARQGH---TKVVNCLIGCGANINHTDQDGWTALRSAAWGGHTE-VVSALLY 453
Cdd:PHA03095 26 TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 454 AGVKVDCADADSRTALRAAAWGG--HEDIVLNLLQHGAEVNKADNEGRTALiaAAYMGHR----EIVEHLLDHGAEVNHE 527
Cdd:PHA03095 106 AGADVNAKDKVGRTPLHVYLSGFniNPKVIRLLLRKGADVNALDLYGMTPL--AVLLKSRnanvELLRLLIDAGADVYAV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 528 DVDGRTALSVAALCVpasKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVD--VVDLLLEGGADVDHTDNNGRTP 605
Cdd:PHA03095 184 DDRFRSLLHHHLQSF---KPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTP 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 606 LLAAAsmghasvvntllfwgaavdsidsegrtvlsiasAQGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRLICE 685
Cdd:PHA03095 261 LHYAA---------------------------------VFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVR 307
|
330
....*....|....
gi 268607595 686 ALIEQGARTNEIDN 699
Cdd:PHA03095 308 AALAKNPSAETVAA 321
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
683-924 |
5.92e-26 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 112.45 E-value: 5.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 683 ICEALIEQGARTNEIDNDGRIPFILASQEGHydcvqillenksnidqrgydgrNALRVaaleghRDIVELLFSHGADVNC 762
Cdd:PHA03100 50 VVKILLDNGADINSSTKNNSTPLHYLSNIKY----------------------NLTDV------KEIVKLLLEYGANVNA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 763 KDADGRPTLYILALE--NQLTMAEYFLENGANVEASDAEGRTALH--VSCWQGHMEMVQVLIAYHADVNAADNekrsalq 838
Cdd:PHA03100 102 PDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHlyLESNKIDLKILKLLIDKGVDINAKNR------- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 839 saawqghvkvVQLLIEHGAVVDHTCNQGATALCIAAQEGHIDVVQVLLEHGADPNHADQFGRTAMRVAAKNGHSQIIKLL 918
Cdd:PHA03100 175 ----------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLL 244
|
....*.
gi 268607595 919 EKYGAS 924
Cdd:PHA03100 245 LNNGPS 250
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
479-804 |
1.18e-24 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 108.96 E-value: 1.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 479 DIVLNLLQHGAEVNKADNEGRTALiaAAYMGHR-----EIVEHLLDHGAEVNHEDVDGRTALSvaalCVPASKGHASVVS 553
Cdd:PHA03095 28 EEVRRLLAAGADVNFRGEYGKTPL--HLYLHYSsekvkDIVRLLLEAGADVNAPERCGFTPLH----LYLYNATTLDVIK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 554 LLIDRGAEVDHCDKDGMTPLLV--AAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASV--VNTLLFWGAAVD 629
Cdd:PHA03095 102 LLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVY 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 630 SIDSEGRTVLSI--ASAQGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHrliCEALIEQgartneidndgriPFIL 707
Cdd:PHA03095 182 AVDDRFRSLLHHhlQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSS---CKRSLVL-------------PLLI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 708 AsqeghydcvqillenksnidqrgydgrnalrvaaleghrdivellfshGADVNCKDADGRPTLYILALENQLTMAEYFL 787
Cdd:PHA03095 246 A------------------------------------------------GISINARNRYGQTPLHYAAVFNNPRACRRLI 277
|
330
....*....|....*..
gi 268607595 788 ENGANVEASDAEGRTAL 804
Cdd:PHA03095 278 ALGADINAVSSDGNTPL 294
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
446-663 |
2.23e-24 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 107.44 E-value: 2.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 446 EVVSALLYAGVKVDCADADSRTALRAAAWGGHE-----DIVLNLLQHGAEVNKADNEGRTALIAAAY--MGHREIVEHLL 518
Cdd:PHA03100 49 DVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISkkSNSYSIVEYLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 519 DHGAEVNHEDVDGRTALSVAALCVPASKghaSVVSLLIDRGAEVDHCDKdgmtpllvaayeghvdvVDLLLEGGADVDHT 598
Cdd:PHA03100 129 DNGANVNIKNSDGENLLHLYLESNKIDL---KILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIK 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 268607595 599 DNNGRTPLLAAASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDENH 663
Cdd:PHA03100 189 DVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
641-916 |
2.25e-24 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 108.19 E-value: 2.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 641 IASAQGNVEVVRTLLDRGLDENHRDDAGWTPLH--MAAFEGHRL-ICEALIEQGARTNEIDNDGRIPFIL----ASQEgh 713
Cdd:PHA03095 20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHlyLHYSSEKVKdIVRLLLEAGADVNAPERCGFTPLHLylynATTL-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 714 yDCVQILLENKSNIDQRGYDGRNALRV--AALEGHRDIVELLFSHGADVNCKDADGRPTLYILALENQLTMA--EYFLEN 789
Cdd:PHA03095 98 -DVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVEllRLLIDA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 790 GANVEASDAEGRTALHVscwqgHME-------MVQVLIAYHADVNAADNEKRSALQSAAWQGHVK--VVQLLIEHGAVVD 860
Cdd:PHA03095 177 GADVYAVDDRFRSLLHH-----HLQsfkprarIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISIN 251
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 268607595 861 HTCNQGATALCIAAQEGHIDVVQVLLEHGADPNHADQFGRTAMRVAAKNGHSQIIK 916
Cdd:PHA03095 252 ARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVR 307
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
427-618 |
1.61e-23 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 107.65 E-value: 1.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 427 HTDQDGWTALRSAAWGGHTEVVSALLYAGVKVDCADADSRTALRAAAWGGHEDIVLNLLQHGAEVNKADNEGRTALIAAA 506
Cdd:PLN03192 520 HDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAI 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 507 YMGHREIVeHLLDHGAEVNHEDVDGRTalsvaaLCVPASKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVD 586
Cdd:PLN03192 600 SAKHHKIF-RILYHFASISDPHAAGDL------LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVR 672
|
170 180 190
....*....|....*....|....*....|....*...
gi 268607595 587 LLLEGGADVDHTD-NNGRTP-----LLAAASMGHASVV 618
Cdd:PLN03192 673 LLIMNGADVDKANtDDDFSPtelreLLQKRELGHSITI 710
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
313-609 |
5.00e-22 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 100.81 E-value: 5.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 313 KEQEVLQLLVKA-GAHVNSEDDRTSCIVRQALEREDS--IRTLLDNGASVNQCDSNGRTLLANAAYSGSLDVVNLLVSRG 389
Cdd:PHA02874 12 GDIEAIEKIIKNkGNCINISVDETTTPLIDAIRSGDAkiVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 390 ADLEIedahghtpltLAARQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGHTEVVSALLYAGVKVDCADADSRTAL 469
Cdd:PHA02874 92 VDTSI----------LPIPCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 470 RAAAWGGHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLDHGAEVNHEDVDGRTALSVAALcvpaskGHA 549
Cdd:PHA02874 162 HIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII------HNR 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 268607595 550 SVVSLLIDrGAEVDHCDKDGMTPLLVA-AYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAA 609
Cdd:PHA02874 236 SAIELLIN-NASINDQDIDGSTPLHHAiNPPCDIDIIDILLYHKADISIKDNKGENPIDTA 295
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
804-896 |
1.27e-21 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 90.56 E-value: 1.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 804 LHVSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSAAWQGHVKVVQLLIEHGAVVDhtCNQGATALCIAAQEGHIDVVQ 883
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 268607595 884 VLLEHGADPNHAD 896
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
647-865 |
1.47e-21 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 98.97 E-value: 1.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 647 NVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRL-----ICEALIEQGARTNEIDNDGRIP-FILASQE-GHYDCVQI 719
Cdd:PHA03100 47 NIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLtdvkeIVKLLLEYGANVNAPDNNGITPlLYAISKKsNSYSIVEY 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 720 LLENKSNIDQRGYDGRNALRVAALEGHRD--IVELLFSHGADVNCKDAdgrptlyilalenqltmAEYFLENGANVEASD 797
Cdd:PHA03100 127 LLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKD 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 268607595 798 AEGRTALHVSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSAAWQGHVKVVQLLIEHGAVVDHTCNQ 865
Cdd:PHA03100 190 VYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
672-764 |
4.41e-21 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 89.02 E-value: 4.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 672 LHMAAFEGHRLICEALIEQGARTNEIDNDGRIPFILASQEGHYDCVQILLENKsNIDQRGYdGRNALRVAALEGHRDIVE 751
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKDN-GRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 268607595 752 LLFSHGADVNCKD 764
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
539-761 |
1.75e-20 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 95.44 E-value: 1.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 539 ALCVPASKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVV 618
Cdd:PHA02875 5 ALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 619 NTLLFWGA-AVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRLICEALIEQGARTNEI 697
Cdd:PHA02875 85 EELLDLGKfADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 268607595 698 DNDGRIPFILASQEGHYDCVQILLENKSNIDQRGYDGRNALRVAALEGHR-DIVELLFSHGADVN 761
Cdd:PHA02875 165 DCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKiDIVRLFIKRGADCN 229
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
582-766 |
8.64e-20 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 95.71 E-value: 8.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 582 VDVVDLLLEGGADvdHTDNNGRTPLLAAASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDE 661
Cdd:PLN03192 507 LNVGDLLGDNGGE--HDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNV 584
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 662 NHRDDAGWTPLHMAAFEGHRLICEALiEQGARTNEIDNDGRIpFILASQEGHYDCVQILLENKSNIDQRGYDGRNALRVA 741
Cdd:PLN03192 585 HIRDANGNTALWNAISAKHHKIFRIL-YHFASISDPHAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVA 662
|
170 180
....*....|....*....|....*
gi 268607595 742 ALEGHRDIVELLFSHGADVNCKDAD 766
Cdd:PLN03192 663 MAEDHVDMVRLLIMNGADVDKANTD 687
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
712-925 |
4.35e-19 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 91.21 E-value: 4.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 712 GHYDCVQILLENKSNIDQRGYDGRNALRVAALEGHRDIVELLFSHGADVNCKDADGRPTLYILALENQLTMAEYFLEngA 791
Cdd:PHA02875 13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLD--L 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 792 NVEASDA---EGRTALHVSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSAAWQGHVKVVQLLIEHGAVVDHTCNQGAT 868
Cdd:PHA02875 91 GKFADDVfykDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCT 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 268607595 869 ALCIAAQEGHIDVVQVLLEHGADPNHadqFGR----TAMRVAAKNGHSQIIKLLEKYGASS 925
Cdd:PHA02875 171 PLIIAMAKGDIAICKMLLDSGANIDY---FGKngcvAALCYAIENNKIDIVRLFIKRGADC 228
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
573-665 |
6.42e-19 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 82.86 E-value: 6.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 573 LLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLLfwgAAVDS-IDSEGRTVLSIASAQGNVEVV 651
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL---EHADVnLKDNGRTALHYAARSGHLEIV 77
|
90
....*....|....
gi 268607595 652 RTLLDRGLDENHRD 665
Cdd:pfam12796 78 KLLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
439-528 |
7.22e-19 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 82.47 E-value: 7.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 439 AAWGGHTEVVSALLYAGVKVDCADADSRTALRAAAWGGHEDIVLNLLQHgAEVNKADNeGRTALIAAAYMGHREIVEHLL 518
Cdd:pfam12796 4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLL 81
|
90
....*....|
gi 268607595 519 DHGAEVNHED 528
Cdd:pfam12796 82 EKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
639-730 |
8.27e-19 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 82.47 E-value: 8.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 639 LSIASAQGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRLICEALIEQGARtnEIDNDGRIPFILASQEGHYDCVQ 718
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78
|
90
....*....|..
gi 268607595 719 ILLENKSNIDQR 730
Cdd:pfam12796 79 LLLEKGADINVK 90
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
345-567 |
1.00e-18 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 90.49 E-value: 1.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 345 REDSIRTLLDNGASVNQCDSNGRTLL---ANAAYSGS--LDVVNLLVSRGADLEIEDAHGHTPLTLAA--RQGHTKVVNC 417
Cdd:PHA03100 47 NIDVVKILLDNGADINSSTKNNSTPLhylSNIKYNLTdvKEIVKLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEY 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 418 LIGCGANINHTDQDGWTALRSAAWGGH--TEVVSALLYAGVKVDCADAdsrtalraaawgghediVLNLLQHGAEVNKAD 495
Cdd:PHA03100 127 LLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKD 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 268607595 496 NEGRTALIAAAYMGHREIVEHLLDHGAEVNHEDVDGRTALSVAALcvpasKGHASVVSLLIDRGAEVDHCDK 567
Cdd:PHA03100 190 VYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAIL-----NNNKEIFKLLLNNGPSIKTIIE 256
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
403-495 |
1.01e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 82.09 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 403 LTLAARQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGHTEVVSALLyAGVKVDCADaDSRTALRAAAWGGHEDIVL 482
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 268607595 483 NLLQHGAEVNKAD 495
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
545-908 |
1.12e-18 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 90.41 E-value: 1.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 545 SKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLLFW 624
Cdd:PHA02874 11 SGDIEAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 625 GaaVDSidsegrTVLSIASAqgNVEVVRTLLDRGLDENHRDDAGWTPLHMAafeghrlicealieqgartneIDNdgrip 704
Cdd:PHA02874 91 G--VDT------SILPIPCI--EKDMIKTILDCGIDVNIKDAELKTFLHYA---------------------IKK----- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 705 filasqeghydcvqillenksnidqrgydgrnalrvaaleGHRDIVELLFSHGADVNCKDADGRPTLYILALENQLTMAE 784
Cdd:PHA02874 135 ----------------------------------------GDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIK 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 785 YFLENGANVEASDAEGRTALHVSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSAAWQGHvKVVQLLIEHGAVVDHTCN 864
Cdd:PHA02874 175 LLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLINNASINDQDID 253
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 268607595 865 qGATALCIAAQ-EGHIDVVQVLLEHGADPNHADQFGRTAMRVAAK 908
Cdd:PHA02874 254 -GSTPLHHAINpPCDIDIIDILLYHKADISIKDNKGENPIDTAFK 297
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
645-935 |
1.19e-18 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 91.66 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 645 QGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIPFILASQEGHYDCVQILLENK 724
Cdd:PHA02876 155 QDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNR 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 725 SNIDQRGYDGRNALRVAALEGHRdiveLLFSHGADVNCKDA-DGRPTLYILALENQLTMAEYFLENGANVEASDAEGRTA 803
Cdd:PHA02876 235 SNINKNDLSLLKAIRNEDLETSL----LLYDAGFSVNSIDDcKNTPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETP 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 804 LHVSCWQGH-MEMVQVLIAYHADVNAADNEKRSALQSAAWQGHVK-VVQLLIEHGAVVDHTCNQGATALCIAAQEGHIDV 881
Cdd:PHA02876 311 LYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKdIVITLLELGANVNARDYCDKTPIHYAAVRNNVVI 390
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 268607595 882 VQVLLEHGADPNHADQFGRTAMRVA--AKNGHSQIIKLLEKyGA--SSLNGCSPSPVH 935
Cdd:PHA02876 391 INTLLDYGADIEALSQKIGTALHFAlcGTNPYMSVKTLIDR-GAnvNSKNKDLSTPLH 447
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
780-923 |
4.38e-18 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 86.16 E-value: 4.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 780 LTMAEYFLENGANVEASDAEGRTALHVSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSAAWQGHVKVVQLLIEHGAVV 859
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 268607595 860 DHTCNQGATALCIAAQEGHIDVVQVLLEHGADPNHADQFGRTAMRVAAKNGHSQIIKLLEKYGA 923
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGA 144
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
544-632 |
4.54e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 80.16 E-value: 4.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 544 ASKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEgGADVDHTDnNGRTPLLAAASMGHASVVNTLLF 623
Cdd:pfam12796 5 AKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVKLLLE 82
|
....*....
gi 268607595 624 WGAAVDSID 632
Cdd:pfam12796 83 KGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
469-563 |
6.14e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 79.77 E-value: 6.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 469 LRAAAWGGHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLDHgAEVNHEDvDGRTALSVAalcvpASKGH 548
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYA-----ARSGH 73
|
90
....*....|....*
gi 268607595 549 ASVVSLLIDRGAEVD 563
Cdd:pfam12796 74 LEIVKLLLEKGADIN 88
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
370-462 |
1.10e-17 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 79.00 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 370 LANAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLIGCgANINHTDqDGWTALRSAAWGGHTEVVS 449
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 268607595 450 ALLYAGVKVDCAD 462
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
771-862 |
1.19e-17 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 79.00 E-value: 1.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 771 LYILALENQLTMAEYFLENGANVEASDAEGRTALHVSCWQGHMEMVQVLIAyHADVNAADNeKRSALQSAAWQGHVKVVQ 850
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVK 78
|
90
....*....|..
gi 268607595 851 LLIEHGAVVDHT 862
Cdd:pfam12796 79 LLLEKGADINVK 90
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
717-935 |
1.48e-17 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 87.39 E-value: 1.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 717 VQILLENKSNIDQRGYDGRNALRV---AALEGHRDIVELLFSHGADVNCKDADG-RPTLYILALENQLTMAEYFLENGAN 792
Cdd:PHA03095 30 VRRLLAAGADVNFRGEYGKTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGfTPLHLYLYNATTLDVIKLLIKAGAD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 793 VEASDAEGRTALHVsCWQG---HMEMVQVLIAYHADVNAADNEKRSALQ-----SAAwqgHVKVVQLLIEHGAVVDHTCN 864
Cdd:PHA03095 110 VNAKDKVGRTPLHV-YLSGfniNPKVIRLLLRKGADVNALDLYGMTPLAvllksRNA---NVELLRLLIDAGADVYAVDD 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 268607595 865 QGATALCIAAQEGHID--VVQVLLEHGADPNHADQFGRTAMRVAAKNG---HSQIIKLLEKyGAS--SLNGCSPSPVH 935
Cdd:PHA03095 186 RFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATGSsckRSLVLPLLIA-GISinARNRYGQTPLH 262
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
738-830 |
1.67e-17 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 78.62 E-value: 1.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 738 LRVAALEGHRDIVELLFSHGADVNCKDADGRPTLYILALENQLTMAEYFLENgANVEASDaEGRTALHVSCWQGHMEMVQ 817
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 268607595 818 VLIAYHADVNAAD 830
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
837-924 |
1.69e-17 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 78.62 E-value: 1.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 837 LQSAAWQGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQEGHIDVVQVLLEHgADPNHADQfGRTAMRVAAKNGHSQIIK 916
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
|
....*...
gi 268607595 917 LLEKYGAS 924
Cdd:pfam12796 79 LLLEKGAD 86
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
647-908 |
2.41e-17 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 86.47 E-value: 2.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 647 NVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIpfilaSQEGHYDCVQI---LLEN 723
Cdd:PHA02878 49 NLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFYTLVAI-----KDAFNNRNVEIfkiILTN 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 724 KSN---------IDQRGYDGrnalrvaALEGhrDIVELLFSHGADVNCKDADGRPTLYILALENQLT-MAEYFLENGANV 793
Cdd:PHA02878 124 RYKniqtidlvyIDKKSKDD-------IIEA--EITKLLLSYGADINMKDRHKGNTALHYATENKDQrLTELLLSYGANV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 794 EASDAEGRTALHVSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSAAwqGHVK---VVQLLIEHGAVVD-HTCNQGATA 869
Cdd:PHA02878 195 NIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISV--GYCKdydILKLLLEHGVDVNaKSYILGLTA 272
|
250 260 270
....*....|....*....|....*....|....*....
gi 268607595 870 LCIAAQEGhiDVVQVLLEHGADPNHADQFGRTAMRVAAK 908
Cdd:PHA02878 273 LHSSIKSE--RKLKLLLEYGADINSLNSYKLTPLSSAVK 309
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
784-924 |
5.53e-17 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 86.85 E-value: 5.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 784 EYFLENGANVEASDAEGRTALHVSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSAAWQGHVKVVQLLIEHGAVVD-HT 862
Cdd:PLN03192 542 EELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDpHA 621
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 268607595 863 cnqGATALCIAAQEGHIDVVQVLLEHGADPNHADQFGRTAMRVAAKNGHSQIIKLLEKYGAS 924
Cdd:PLN03192 622 ---AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGAD 680
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
522-746 |
1.16e-16 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 85.69 E-value: 1.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 522 AEVNHEDVDGRTALSVAALcvpASKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNN 601
Cdd:PLN03192 514 GDNGGEHDDPNMASNLLTV---ASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDAN 590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 602 GRTPLLAAASMGHASVVNTLLFWGAAVDSidSEGRTVLSIASAQGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHR 681
Cdd:PLN03192 591 GNTALWNAISAKHHKIFRILYHFASISDP--HAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHV 668
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 682 LICEALIEQGARTNEIDND------------------GRIPFILASQEGHYDCVQILLENKSNIDQRGYDGRNALRVAAL 743
Cdd:PLN03192 669 DMVRLLIMNGADVDKANTDddfsptelrellqkrelgHSITIVDSVPADEPDLGRDGGSRPGRLQGTSSDNQCRPRVSIY 748
|
...
gi 268607595 744 EGH 746
Cdd:PLN03192 749 KGH 751
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
365-594 |
1.18e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 83.89 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 365 NGRTLLANAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGH 444
Cdd:PHA02875 1 MDQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 445 TEVVSALLYAGVKV-DCADADSRTALRAAAWGGHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLDHGAE 523
Cdd:PHA02875 81 VKAVEELLDLGKFAdDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKAC 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 268607595 524 VNHEDVDGRTALSVAalcvpASKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGH-VDVVDLLLEGGAD 594
Cdd:PHA02875 161 LDIEDCCGCTPLIIA-----MAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNkIDIVRLFIKRGAD 227
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
466-695 |
6.58e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 81.58 E-value: 6.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 466 RTALRAAAWGGHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLDHGAEVNHEDVDGRTALSVAALcvpas 545
Cdd:PHA02875 3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVE----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 546 KGHASVVSLLIDRGAEVDHC-DKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLLFW 624
Cdd:PHA02875 78 EGDVKAVEELLDLGKFADDVfYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDH 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 268607595 625 GAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRL-ICEALIEQGARTN 695
Cdd:PHA02875 158 KACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIdIVRLFIKRGADCN 229
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
551-831 |
1.14e-15 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 81.42 E-value: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 551 VVSLLIDRGAEVDHCDKDGMTPLL-----VAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLLFW- 624
Cdd:PHA02798 53 IVKLFINLGANVNGLDNEYSTPLCtilsnIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLFMi 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 625 --GAAVDSIDSEGRTVLSIASAQGN---VEVVRTLLDRGLDEN-HRDDAGWTPLH-MAAFEGHRL---ICEALIEQGART 694
Cdd:PHA02798 133 enGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINtHNNKEKYDTLHcYFKYNIDRIdadILKLFVDNGFII 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 695 NEIDNDGRIPFIlasqeghyDCVQILLENKSNIDqrgydgrnalrvaaleghRDIVELLFSHgADVNCKDADGRPTLYIL 774
Cdd:PHA02798 213 NKENKSHKKKFM--------EYLNSLLYDNKRFK------------------KNILDFIFSY-IDINQVDELGFNPLYYS 265
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 268607595 775 ALENQLTMAEYFLENGANVEASDAEGRTALHVSCWQGHMEMVQVLIAYHADVNAADN 831
Cdd:PHA02798 266 VSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKPNKNTISY 322
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
370-645 |
4.46e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 79.54 E-value: 4.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 370 LANAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLAA----RQGHTKVVNCLIGCgaNINHTDQdgwtALRSAAWGGHT 445
Cdd:PHA02878 41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICkepnKLGMKEMIRSINKC--SVFYTLV----AIKDAFNNRNV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 446 EVVSALLYAGVKVDCADADSRTALRAAAWGGHEDIVLNLLQHGAEVNKAD-NEGRTALIAAAYMGHREIVEHLLDHGAEV 524
Cdd:PHA02878 115 EIFKIILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 525 NHEDVDGRTALSVAAlcvpaSKGHASVVSLLIDRGAEVDHCDKDGMTPLLVA-AYEGHVDVVDLLLEGGADVDHTDN-NG 602
Cdd:PHA02878 195 NIPDKTNNSPLHHAV-----KHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYiLG 269
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 268607595 603 RTPLlaAASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQ 645
Cdd:PHA02878 270 LTAL--HSSIKSERKLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
347-429 |
1.80e-14 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 70.14 E-value: 1.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 347 DSIRTLLDNGASVNQCDSNGRTLLANAAYSGSLDVVNLLVSRgADLEIEDaHGHTPLTLAARQGHTKVVNCLIGCGANIN 426
Cdd:pfam12796 11 ELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADIN 88
|
...
gi 268607595 427 HTD 429
Cdd:pfam12796 89 VKD 91
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
636-893 |
2.03e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 76.95 E-value: 2.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 636 RTVLSIASAQGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIPFILASQEGHYD 715
Cdd:PHA02875 3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 716 CVQILLENKSNIDQRGY-DGRNALRVAALEGHRDIVELLFSHGADVNCKDADGRptlyilalenqltmaeyflenganve 794
Cdd:PHA02875 83 AVEELLDLGKFADDVFYkDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKF-------------------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 795 asdaegrTALHVSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSAAWQGHVKVVQLLIEHGAVVDHTCNQG-ATALCIA 873
Cdd:PHA02875 137 -------SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYA 209
|
250 260
....*....|....*....|
gi 268607595 874 AQEGHIDVVQVLLEHGADPN 893
Cdd:PHA02875 210 IENNKIDIVRLFIKRGADCN 229
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
736-915 |
3.56e-14 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 77.60 E-value: 3.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 736 NALRVAALeGHRDIVELLFSHGADVNCKDADGRPTLYILALENQLTMAEYFLENGANVEASDAEGRTALHVSCWQGHMEM 815
Cdd:PLN03192 528 NLLTVAST-GNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKI 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 816 VQVLiaYHADVNAADNEKRSALQSAAWQGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQEGHIDVVQVLLEHGADPNHA 895
Cdd:PLN03192 607 FRIL--YHFASISDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKA 684
|
170 180
....*....|....*....|....*.
gi 268607595 896 ---DQFGRTAMRVAAKN---GHSQII 915
Cdd:PLN03192 685 ntdDDFSPTELRELLQKrelGHSITI 710
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
316-455 |
4.93e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 75.86 E-value: 4.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 316 EVLQLLVKAGAHVNSEDDRTSCIVRQALERE----DSIRTLLDNGASVNQCDSNGRTLLANAAYSGS--LDVVNLLVSRG 389
Cdd:PHA03100 87 EIVKLLLEYGANVNAPDNNGITPLLYAISKKsnsySIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 390 ADLEIE----------------DAHGHTPLTLAARQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGHTEVVSALLY 453
Cdd:PHA03100 167 VDINAKnrvnyllsygvpinikDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLN 246
|
..
gi 268607595 454 AG 455
Cdd:PHA03100 247 NG 248
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
672-936 |
9.19e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 75.00 E-value: 9.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 672 LHMAAFEGHRLICEALIEQgaRTNEID---NDGRIPFILASQEGHYDCVQILLENKSNIDQRGYDGRNALRVAALEGHRD 748
Cdd:PHA02874 5 LRMCIYSGDIEAIEKIIKN--KGNCINisvDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 749 IVELLFSHGADVNckdadgrpTLYILALENQltMAEYFLENGANVEASDAEGRTALHVSCWQGHMEMVQVLIAYHADVNA 828
Cdd:PHA02874 83 IIKLLIDNGVDTS--------ILPIPCIEKD--MIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 829 ADNekrsalqsaawqghvkvvqlliehgavvdhtcnQGATALCIAAQEGHIDVVQVLLEHGADPNHADQFGRTAMRVAAK 908
Cdd:PHA02874 153 EDD---------------------------------NGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAE 199
|
250 260 270
....*....|....*....|....*....|
gi 268607595 909 NGHSQIIKLLEKYGASSLNGCSP--SPVHT 936
Cdd:PHA02874 200 YGDYACIKLLIDHGNHIMNKCKNgfTPLHN 229
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
316-430 |
1.44e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 74.32 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 316 EVLQLLVKAGAHVNSEDdrtscivrqaleredSIRTLLDNGASVNQCDSNGRTLLANAAYSGSLDVVNLLVSRGADLEIE 395
Cdd:PHA03100 157 KILKLLIDKGVDINAKN---------------RVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLV 221
|
90 100 110
....*....|....*....|....*....|....*
gi 268607595 396 DAHGHTPLTLAARQGHTKVVNCLIGCGANINHTDQ 430
Cdd:PHA03100 222 NKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
572-855 |
4.80e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 72.99 E-value: 4.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 572 PLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAA-------------ASMGHASVVNTLLFWGAAVDSIDSEGRTV 638
Cdd:PHA02878 40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIIckepnklgmkemiRSINKCSVFYTLVAIKDAFNNRNVEIFKI 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 639 LSIASAQGN------------------VEVVRTLLDRGLDENHRD-DAGWTPLHMAAFEGHRLICEALIEQGARTNEIDN 699
Cdd:PHA02878 120 ILTNRYKNIqtidlvyidkkskddiieAEITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDK 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 700 DGRIPFILASQEGHYDCVQILLENKSNIDQRGYDGRNALRVAALE-GHRDIVELLFSHGADVNCKDadgrptlYILALen 778
Cdd:PHA02878 200 TNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKS-------YILGL-- 270
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 268607595 779 qltmaeyflenganveasdaegrTALHVSCwqgHMEMV-QVLIAYHADVNAADNEKRSALQSAAWQGH-VKVVQLLIEH 855
Cdd:PHA02878 271 -----------------------TALHSSI---KSERKlKLLLEYGADINSLNSYKLTPLSSAVKQYLcINIGRILISN 323
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
347-561 |
1.06e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 71.56 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 347 DSIRTLLDNGASVNQCDSNGRTLLANAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLIGCGANIN 426
Cdd:PHA02875 16 DIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 427 HT-DQDGWTALRSAAWGGHTEVVSALLYAGVKVDCADADSRTALRAAAWGGHEDIVLNLLQHGAEVNKADNEGRTALIAA 505
Cdd:PHA02875 96 DVfYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 268607595 506 AYMGHREIVEHLLDHGAEVNHEDVDGrtalSVAALCVPASKGHASVVSLLIDRGAE 561
Cdd:PHA02875 176 MAKGDIAICKMLLDSGANIDYFGKNG----CVAALCYAIENNKIDIVRLFIKRGAD 227
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
316-452 |
3.35e-12 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 70.44 E-value: 3.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 316 EVLQLLVKAGAHVNSEDDRTSCIVRQALE----REDSIRTLLDNGASVNQCDSNGRTLLANAAYSGS---LDVVNLLVsR 388
Cdd:PHA03095 168 ELLRLLIDAGADVYAVDDRFRSLLHHHLQsfkpRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSckrSLVLPLLI-A 246
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 268607595 389 GADLEIEDAHGHTPLTLAARQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGHTEVVSALL 452
Cdd:PHA03095 247 GISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
569-622 |
3.52e-12 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 62.29 E-value: 3.52e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 268607595 569 GMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLL 622
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
685-914 |
4.05e-12 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 70.43 E-value: 4.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 685 EALIEQGARTNEIdndgriPFILASQEGHYDCVQILLENKS-NIDQRGYDGRNALRVAALEGHRDIVELLfshgadvnck 763
Cdd:cd22192 7 ELHLLQQKRISES------PLLLAAKENDVQAIKKLLKCPScDLFQRGALGETALHVAALYDNLEAAVVL---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 764 dADGRPTLYILALENQLtmaeYflenganveasdaEGRTALHVSCWQGHMEMVQVLIAYHADVNAAdnekRSA------- 836
Cdd:cd22192 71 -MEAAPELVNEPMTSDL----Y-------------QGETALHIAVVNQNLNLVRELIARGADVVSP----RATgtffrpg 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 837 -----------LQSAAWQGHVKVVQLLIEHGA----------VVDH--TCNQGATALC-----IAAQEGHIDvvQVLLEH 888
Cdd:cd22192 129 pknliyygehpLSFAACVGNEEIVRLLIEHGAdiraqdslgnTVLHilVLQPNKTFACqmydlILSYDKEDD--LQPLDL 206
|
250 260
....*....|....*....|....*.
gi 268607595 889 gaDPNHAdqfGRTAMRVAAKNGHSQI 914
Cdd:cd22192 207 --VPNNQ---GLTPFKLAAKEGNIVM 227
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
868-918 |
1.99e-11 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 59.98 E-value: 1.99e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 268607595 868 TALCIAAQEGHIDVVQVLLEHGADPNHADQFGRTAMRVAAKNGHSQIIKLL 918
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
318-470 |
2.64e-11 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 68.36 E-value: 2.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 318 LQLLVKAG--AHVNSEDDRTSCIVRQALEREDSIRTLLDNGASVNQCDSNGRTLLANAAYSGSLDVVNLLVSRGAdleIE 395
Cdd:PLN03192 541 LEELLKAKldPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFAS---IS 617
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 268607595 396 DAH-GHTPLTLAARQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGHTEVVSALLYAGVKVDCADAD---SRTALR 470
Cdd:PLN03192 618 DPHaAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDddfSPTELR 696
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
527-622 |
5.19e-11 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 67.23 E-value: 5.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 527 EDVDGRTA--LSVAaLCVPASKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRT 604
Cdd:PTZ00322 72 EVIDPVVAhmLTVE-LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKT 150
|
90
....*....|....*...
gi 268607595 605 PLLAAASMGHASVVNTLL 622
Cdd:PTZ00322 151 PLELAEENGFREVVQLLS 168
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
580-808 |
7.28e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 65.78 E-value: 7.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 580 GHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGl 659
Cdd:PHA02875 13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 660 deNHRDDA----GWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIPFILASQEGHYDCVQILLENKSNIDQRGYDGR 735
Cdd:PHA02875 92 --KFADDVfykdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGC 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 268607595 736 NALRVAALEGHRDIVELLFSHGADVNCKDADGRPTLYILALE-NQLTMAEYFLENGAN---VEASDAEGRTALHVSC 808
Cdd:PHA02875 170 TPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIEnNKIDIVRLFIKRGADcniMFMIEGEECTILDMIC 246
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
585-671 |
1.26e-10 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 65.69 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 585 VDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRtLLDRGLDENHR 664
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ-LLSRHSQCHFE 176
|
....*..
gi 268607595 665 DDAGWTP 671
Cdd:PTZ00322 177 LGANAKP 183
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
849-951 |
1.58e-10 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 65.30 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 849 VQLLIEHGAVVDHTCNQGATALCIAAQEGHIDVVQVLLEHGADPNHADQFGRTAMRVAAKNGHSQIIKLLEKYGASSLNG 928
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFEL 177
|
90 100
....*....|....*....|...
gi 268607595 929 CSPSPVHTMEQKPLQSLSSKVQS 951
Cdd:PTZ00322 178 GANAKPDSFTGKPPSLEDSPISS 200
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
635-688 |
4.86e-10 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 56.13 E-value: 4.86e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 268607595 635 GRTVLSIASAQGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRLICEALI 688
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
349-540 |
5.96e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 63.36 E-value: 5.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 349 IRTLLDNGASVNQCDSN-GRTLLANAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLIGCGANINH 427
Cdd:PHA02878 150 TKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 428 TDQDGWTALrsaawggHTEVVSALLYagvkvdcadadsrtalraaawggheDIVLNLLQHGAEVN-KADNEGRTALIAAa 506
Cdd:PHA02878 230 RDKCGNTPL-------HISVGYCKDY-------------------------DILKLLLEHGVDVNaKSYILGLTALHSS- 276
|
170 180 190
....*....|....*....|....*....|....
gi 268607595 507 yMGHREIVEHLLDHGAEVNHEDVDGRTALSVAAL 540
Cdd:PHA02878 277 -IKSERKLKLLLEYGADINSLNSYKLTPLSSAVK 309
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
710-935 |
9.46e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 63.16 E-value: 9.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 710 QEGHYDCVQILLENKSNIDQRGYDGRNALRVAALEGHRDIVELLFSHGADVNCKDADGRPTLYILALENQLTMAEYFLEN 789
Cdd:PHA02876 154 QQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDN 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 790 GANVEASDAEGRTALHvscwqgHMEMVQVLIAYHA--DVNAADNEKRSALQSAAWQGHV-KVVQLLIEHGAVVDHTCNQG 866
Cdd:PHA02876 234 RSNINKNDLSLLKAIR------NEDLETSLLLYDAgfSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKG 307
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 268607595 867 ATALCIAAQEGH-IDVVQVLLEHGADPNHADQFGRTAMRVAAKNGHSQ--IIKLLEkYGA--SSLNGCSPSPVH 935
Cdd:PHA02876 308 ETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKdiVITLLE-LGAnvNARDYCDKTPIH 380
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
834-886 |
9.65e-10 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 55.36 E-value: 9.65e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 268607595 834 RSALQSAAWQGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQEGHIDVVQVLL 886
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
401-582 |
1.19e-09 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 62.72 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 401 TPLTLAARQGHTKVVNCLIGCganiNHTD-----QDGWTALRSAAWGGHTEVVSAL---------------LYAGVkvdc 460
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLLKC----PSCDlfqrgALGETALHVAALYDNLEAAVVLmeaapelvnepmtsdLYQGE---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 461 adadsrTALRAAAWGGHEDIVLNLLQHGAEVNKADNEG------RTALIA--------AAYMGHREIVEHLLDHGAEVNH 526
Cdd:cd22192 91 ------TALHIAVVNQNLNLVRELIARGADVVSPRATGtffrpgPKNLIYygehplsfAACVGNEEIVRLLIEHGADIRA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 268607595 527 EDVDGRTALSVAALcvPASKGHASVVSLLI------DRGAEVDHC-DKDGMTPLLVAAYEGHV 582
Cdd:cd22192 165 QDSLGNTVLHILVL--QPNKTFACQMYDLIlsydkeDDLQPLDLVpNNQGLTPFKLAAKEGNI 225
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
800-853 |
1.64e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 54.59 E-value: 1.64e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 268607595 800 GRTALHVSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSAAWQGHVKVVQLLI 853
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
512-766 |
1.86e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 61.82 E-value: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 512 EIVEHLLDHGAEVNHEDVDGRTALSVAALcVPASKGHASVVSLLIDRgaEVDHCDKDGMTpllvAAYEGHVDVVDLLLEG 591
Cdd:PHA02878 51 DVVKSLLTRGHNVNQPDHRDLTPLHIICK-EPNKLGMKEMIRSINKC--SVFYTLVAIKD----AFNNRNVEIFKIILTN 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 592 GADVDHTDNNGRTPLLAAASMGHASVVNTLLFWGAAVDSID-SEGRTVLSIASAQGNVEVVRTLLDRGLDENHRDDAGWT 670
Cdd:PHA02878 124 RYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNS 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 671 PLHMAAFEGHRLICEALIEQGARTNEIDNDGRIPF-ILASQEGHYDCVQILLENKSNIDQRGY-DGRNALRVAALEghRD 748
Cdd:PHA02878 204 PLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLhISVGYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKS--ER 281
|
250
....*....|....*...
gi 268607595 749 IVELLFSHGADVNCKDAD 766
Cdd:PHA02878 282 KLKLLLEYGADINSLNSY 299
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
629-721 |
1.93e-09 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 61.84 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 629 DSIDSEGRTVLSIA----SAQGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIP 704
Cdd:PTZ00322 72 EVIDPVVAHMLTVElcqlAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTP 151
|
90
....*....|....*..
gi 268607595 705 FILASQEGHYDCVQILL 721
Cdd:PTZ00322 152 LELAEENGFREVVQLLS 168
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
445-728 |
2.14e-09 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 61.39 E-value: 2.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 445 TEVVSALLYAGVKVDCADADSRTAL-----RAAAWGGHEDIVLNLLQHGAEVNKADNEGRT---ALIAAAYMGHREIVEH 516
Cdd:PHA02798 51 TDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETplyCLLSNGYINNLEILLF 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 517 LLDHGAEVNHEDVDGRTALSVAalcvpASKGHA---SVVSLLIDRGAEVD-HCDKDGMTPLLVAAYEG----HVDVVDLL 588
Cdd:PHA02798 131 MIENGADTTLLDKDGFTMLQVY-----LQSNHHidiEIIKLLLEKGVDINtHNNKEKYDTLHCYFKYNidriDADILKLF 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 589 LEGGADVDHTDNNGRTPLLaaasmghaSVVNTLLFWGAAVDSidsegrtvlsiasaqgnveVVRTLLDRGLDENHRDDAG 668
Cdd:PHA02798 206 VDNGFIINKENKSHKKKFM--------EYLNSLLYDNKRFKK-------------------NILDFIFSYIDINQVDELG 258
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 669 WTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIPFILASQEGHYDCVQILLENKSNID 728
Cdd:PHA02798 259 FNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKPNKN 318
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
748-934 |
2.23e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 61.43 E-value: 2.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 748 DIVELLFSHGADVNCKDADGRPTLYILALE-NQLTMAE-----------------------------------YF----- 786
Cdd:PHA02878 51 DVVKSLLTRGHNVNQPDHRDLTPLHIICKEpNKLGMKEmirsinkcsvfytlvaikdafnnrnveifkiiltnRYkniqt 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 787 -----------------------LENGANVEASDAE-GRTALHVSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSAAW 842
Cdd:PHA02878 131 idlvyidkkskddiieaeitkllLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVK 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 843 QGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQE-GHIDVVQVLLEHGADPN-HADQFGRTAMRVAAKNghSQIIKLLEK 920
Cdd:PHA02878 211 HYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNaKSYILGLTALHSSIKS--ERKLKLLLE 288
|
250
....*....|....*.
gi 268607595 921 YGA--SSLNGCSPSPV 934
Cdd:PHA02878 289 YGAdiNSLNSYKLTPL 304
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
604-820 |
4.18e-09 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 60.80 E-value: 4.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 604 TPLLAAASMGHASVVNTLLfwgaAVDSID-----SEGRTVLSIASAQGNVEVVRTLLD--RGL-DENHRDD--AGWTPLH 673
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLL----KCPSCDlfqrgALGETALHVAALYDNLEAAVVLMEaaPELvNEPMTSDlyQGETALH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 674 MAAFEGHRLICEALIEQGARTneidndgripfILASQEGHYdcvqiLLENKSNIdqrGYDGRNALRVAALEGHRDIVELL 753
Cdd:cd22192 95 IAVVNQNLNLVRELIARGADV-----------VSPRATGTF-----FRPGPKNL---IYYGEHPLSFAACVGNEEIVRLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 754 FSHGADVNCKDADGRPTLYILALENQLT----MAEYFLenganveASDAEGR-------------TALHVSCWQGHMEMV 816
Cdd:cd22192 156 IEHGADIRAQDSLGNTVLHILVLQPNKTfacqMYDLIL-------SYDKEDDlqpldlvpnnqglTPFKLAAKEGNIVMF 228
|
....
gi 268607595 817 QVLI 820
Cdd:cd22192 229 QHLV 232
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
399-452 |
5.35e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 53.05 E-value: 5.35e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 268607595 399 GHTPLTLAARQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGHTEVVSALL 452
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
466-518 |
5.73e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 53.05 E-value: 5.73e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 268607595 466 RTALRAAAWGGHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLL 518
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
413-622 |
8.71e-09 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 59.30 E-value: 8.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 413 KVVNCLIGCGANINHTDQDGWTALRSAAWGGHTEVVSALLYAGVKVDCADADSRTALRAAAwgGHEDIVLN----LLQHG 488
Cdd:PHA02946 53 RFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLS--GTDDEVIErinlLVQYG 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 489 AEVNKA-DNEGRTALIAAAYMGHReIVEHLLDHGAEVNHEDVDGRTALSVAALcvpASKGHASVVSLLIDRGAEVDHCDK 567
Cdd:PHA02946 131 AKINNSvDEEGCGPLLACTDPSER-VFKKIMSIGFEARIVDKFGKNHIHRHLM---SDNPKASTISWMMKLGISPSKPDH 206
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 268607595 568 DGMTPLLVAAYE--GHVDVVDLLLEgGADVDHTDNNGRTPL-LAAASMGHASVVNTLL 622
Cdd:PHA02946 207 DGNTPLHIVCSKtvKNVDIINLLLP-STDVNKQNKFGDSPLtLLIKTLSPAHLINKLL 263
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
767-820 |
1.08e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 52.28 E-value: 1.08e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 268607595 767 GRPTLYILALENQLTMAEYFLENGANVEASDAEGRTALHVSCWQGHMEMVQVLI 820
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
531-589 |
1.37e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 51.89 E-value: 1.37e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 268607595 531 GRTALSVAAlcvpaSKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVDLLL 589
Cdd:pfam13637 1 ELTALHAAA-----ASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
748-918 |
1.98e-08 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 58.31 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 748 DIVELLFSHGADVNCKDAD-GRPTLYILA----LENQLTMAEYFLENGANVEASDAEGRTALHvscwqghmemvqvliay 822
Cdd:PHA02798 52 DIVKLFINLGANVNGLDNEySTPLCTILSnikdYKHMLDIVKILIENGADINKKNSDGETPLY----------------- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 823 hadvnaadnekrsALQSAAWQGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQEGH---IDVVQVLLEHGADPN-HADQF 898
Cdd:PHA02798 115 -------------CLLSNGYINNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINtHNNKE 181
|
170 180
....*....|....*....|....
gi 268607595 899 GRTAMRVAAKNGHSQ----IIKLL 918
Cdd:PHA02798 182 KYDTLHCYFKYNIDRidadILKLF 205
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
349-421 |
2.13e-08 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 58.76 E-value: 2.13e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 268607595 349 IRTLLDNGASVNQCDSNGRTLLANAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLIGC 421
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
301-460 |
2.27e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 58.08 E-value: 2.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 301 TPVRDSLSTLIPKEQEVLQLLVKAGAHVNSEDDRTSCIVRQALEREDSIRTLLDNGASVNQCDSNGRTLLANAAYSGSLD 380
Cdd:PHA02875 70 SELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIK 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 381 VVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLIGCGANINHTDQDG-WTALRSAAWGGHTEVVSALLYAGvkVD 459
Cdd:PHA02875 150 GIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRG--AD 227
|
.
gi 268607595 460 C 460
Cdd:PHA02875 228 C 228
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
783-855 |
2.59e-08 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 58.37 E-value: 2.59e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 268607595 783 AEYFLENGANVEASDAEGRTALHVSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSAAWQGHVKVVQLLIEH 855
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
665-769 |
2.59e-08 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 58.37 E-value: 2.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 665 DDAGWTPLHMAAFE-------GHRLICEALIEQGARTNEIDNDGRIPFILASQEGHYDCVQILLENKSNIDQRGYDGRNA 737
Cdd:PTZ00322 72 EVIDPVVAHMLTVElcqlaasGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTP 151
|
90 100 110
....*....|....*....|....*....|..
gi 268607595 738 LRVAALEGHRDIVELLFSHGADVNCKDADGRP 769
Cdd:PTZ00322 152 LELAEENGFREVVQLLSRHSQCHFELGANAKP 183
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
776-931 |
3.73e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 57.31 E-value: 3.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 776 LENQLTMAEYFLENGANVEASDAEGRTALHVSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSAAWQGHVKVVQLLIEH 855
Cdd:PHA02875 11 LFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 856 GAVVDHTC-NQGATALCIAAQEGHIDVVQVLLEHGADPNHADQFGRTAMRVAAKNGHSQIIKLLEKYGAsSLN-----GC 929
Cdd:PHA02875 91 GKFADDVFyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKA-CLDiedccGC 169
|
..
gi 268607595 930 SP 931
Cdd:PHA02875 170 TP 171
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
750-822 |
3.93e-08 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 57.60 E-value: 3.93e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 268607595 750 VELLFSHGADVNCKDADGRPTLYILALENQLTMAEYFLENGANVEASDAEGRTALHVSCWQGHMEMVQVLIAY 822
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
370-452 |
5.12e-08 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 57.22 E-value: 5.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 370 LANAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGHTEVVS 449
Cdd:PTZ00322 86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165
|
...
gi 268607595 450 ALL 452
Cdd:PTZ00322 166 LLS 168
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
531-724 |
6.86e-08 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 56.94 E-value: 6.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 531 GRTALSVAALcvpasKGHASVVSLLIDRGAEV--DHCDKD---GMTPLLVAAYEGHVDVVDLLLEGGADVdhtdNNGRtp 605
Cdd:cd22192 51 GETALHVAAL-----YDNLEAAVVLMEAAPELvnEPMTSDlyqGETALHIAVVNQNLNLVRELIARGADV----VSPR-- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 606 llAAASMGHASVVNTLLFwgaavdsidseGRTVLSIASAQGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRLI-C 684
Cdd:cd22192 120 --ATGTFFRPGPKNLIYY-----------GEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFaC 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 268607595 685 EA---LIEQGARTNEI------DNDGRIPFILASQEGHYDCVQILLENK 724
Cdd:cd22192 187 QMydlILSYDKEDDLQpldlvpNNQGLTPFKLAAKEGNIVMFQHLVQKR 235
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
780-935 |
1.07e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 56.04 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 780 LTMAEYFLENGANVEASDAEGRTALHVSCWQGHMEMVQVLIA------------------YHADVNAA--------DNEK 833
Cdd:PHA02878 50 LDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRsinkcsvfytlvaikdafNNRNVEIFkiiltnryKNIQ 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 834 RSAL-----QSAAWQGHVKVVQLLIEHGAVVD-HTCNQGATALCIAAQEGHIDVVQVLLEHGADPNHADQFGRTAMRVAA 907
Cdd:PHA02878 130 TIDLvyidkKSKDDIIEAEITKLLLSYGADINmKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAV 209
|
170 180 190
....*....|....*....|....*....|
gi 268607595 908 KNGHSQIIKLLEKYGASS--LNGCSPSPVH 935
Cdd:PHA02878 210 KHYNKPIVHILLENGASTdaRDKCGNTPLH 239
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
628-785 |
1.34e-07 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 56.24 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 628 VDSIDSEGRTVLSIASAQGNVEVVRTLLdrgLDENHRDDAGWTPLHMAAFEGHRlICEALI---EQGAR-------TNEI 697
Cdd:TIGR00870 45 INCPDRLGRSALFVAAIENENLELTELL---LNLSCRGAVGDTLLHAISLEYVD-AVEAILlhlLAAFRksgplelANDQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 698 DND----GRIPFILASQEGHYDCVQILLENKSNIDQRG--------------YDGRNALRVAALEGHRDIVELLFSHGAD 759
Cdd:TIGR00870 121 YTSeftpGITALHLAAHRQNYEIVKLLLERGASVPARAcgdffvksqgvdsfYHGESPLNAAACLGSPSIVALLSEDPAD 200
|
170 180
....*....|....*....|....*.
gi 268607595 760 VNCKDADGRPTLYILALENQLTmAEY 785
Cdd:TIGR00870 201 ILTADSLGNTLLHLLVMENEFK-AEY 225
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
610-687 |
1.97e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 55.29 E-value: 1.97e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 268607595 610 ASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRLICEAL 687
Cdd:PTZ00322 90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
668-721 |
2.17e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 48.81 E-value: 2.17e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 268607595 668 GWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIPFILASQEGHYDCVQILL 721
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| TRPV1-4 |
cd22193 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ... |
706-887 |
2.54e-07 |
|
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: 55.19 E-value: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 706 ILASQEGHYDCVQILL---ENKSNIDQ--------RGYDGRNALRVAALEGHRDIVELLFSHGADVNC-------KDADG 767
Cdd:cd22193 37 LLNLNPGTNDTIRILLdiaEKTDNLKRfinaeytdEYYEGQTALHIAIERRQGDIVALLVENGADVHAhakgrffQPKYQ 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 768 RPTLY-------ILALENQLTMAEYFLENG---ANVEASDAEGRTALHvscwqghmemvqvliayhADVNAADNEK-RSA 836
Cdd:cd22193 117 GEGFYfgelplsLAACTNQPDIVQYLLENEhqpADIEAQDSRGNTVLH------------------ALVTVADNTKeNTK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 268607595 837 LQSAAWQGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQEGHIDVVQVLLE 887
Cdd:cd22193 179 FVTRMYDMILIRGAKLCPTVELEEIRNNDGLTPLQLAAKMGKIEILKYILQ 229
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
823-925 |
3.35e-07 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 54.87 E-value: 3.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 823 HADVNAADNekrsaLQSAAWQGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQEGHIDVVQVLLEHGADPNHADQFGRTA 902
Cdd:PLN03192 520 HDDPNMASN-----LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTA 594
|
90 100
....*....|....*....|...
gi 268607595 903 MRVAAKNGHSQIIKLLEKYGASS 925
Cdd:PLN03192 595 LWNAISAKHHKIFRILYHFASIS 617
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
626-675 |
4.71e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 47.73 E-value: 4.71e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 268607595 626 AAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDENHRDDAGWTPLHMA 675
Cdd:pfam13857 7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| TRPV1 |
cd22196 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ... |
732-805 |
5.27e-07 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411980 [Multi-domain] Cd Length: 649 Bit Score: 54.04 E-value: 5.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 732 YDGRNALRVAALEGHRDIVELLFSHGADVNC-------KDADGRPTLY-------ILALENQLTMAEYFLEN---GANVE 794
Cdd:cd22196 92 YKGQTALHIAIERRNMHLVELLVQNGADVHArasgeffKKKKGGPGFYfgelplsLAACTNQLDIVKFLLENphsPADIS 171
|
90
....*....|.
gi 268607595 795 ASDAEGRTALH 805
Cdd:cd22196 172 ARDSMGNTVLH 182
|
|
| Semenogelin |
pfam05474 |
Semenogelin; This family consists of several mammalian secreted seminal proteins including ... |
1031-1224 |
6.00e-07 |
|
Semenogelin; This family consists of several mammalian secreted seminal proteins including semenogelin I and II. Freshly ejaculated human semen has the appearance of a loose gel in which the predominant structural protein components are the seminal vesicle secreted semenogelins (Sg). This family also includes seminal vesicle secretory protein 3A from mouse, which has been shown to be involved in the coagulation of semen resulting in the formation of the copulatory plug.
Pssm-ID: 368458 [Multi-domain] Cd Length: 582 Bit Score: 53.73 E-value: 6.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 1031 HNLSFTEQIQQHSlprsRSRQSIVSPSSTTQSLGQSHNSPSSEFEWSQVKPSLKsTKASKGGKSENSAKSGSA------- 1103
Cdd:pfam05474 268 HQTKNLSQDQEHG----RKAHKISYPSSRTEERQLHHGEKSVQKDVSKGSISIQ-TEEKIHGKSQNQVTIHSQdqehghk 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 1104 -GKKAKQSNSSQPKVLEYEMTQFdRRGPIAKSGTAAPPKQMPAESQCKIMIPSAQQEIGRSQQQFLIHQQSGEQKKRNG- 1181
Cdd:pfam05474 343 eNKISYQSSSTEERHLNCGEKGI-QKGVSKGSISIQTEEQIHGKSQNQVRIPSQAQEYGHKENKISYQSSSTEERRLNSg 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 268607595 1182 --------------IMTNPNYHLQSNQvflgRVSVPRTMQDRGHQEVLEGYPSSETE 1224
Cdd:pfam05474 422 ekdvqkgvskgsisIQTEEKIHGKSQN----QVTIPSQDQEHGHKENKMSYQSSSTE 474
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
813-922 |
6.54e-07 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 53.30 E-value: 6.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 813 MEMVQVLIAYHADVNAADNEKRSALQS-----AAWQGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQEGHIDVVQVLL- 886
Cdd:PHA02798 51 TDIVKLFINLGANVNGLDNEYSTPLCTilsniKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLf 130
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 268607595 887 --EHGADPNHADQFGRTAMRVAAKNGHS---QIIKLLEKYG 922
Cdd:PHA02798 131 miENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKG 171
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
440-534 |
9.16e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 53.36 E-value: 9.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 440 AWGGHTEVVSALLYAGVKVDCADADSRTALRAAAWGGHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLD 519
Cdd:PTZ00322 90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
|
90
....*....|....*
gi 268607595 520 HGAEvnHEDVDGRTA 534
Cdd:PTZ00322 170 HSQC--HFELGANAK 182
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
432-485 |
9.35e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 46.88 E-value: 9.35e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 268607595 432 GWTALRSAAWGGHTEVVSALLYAGVKVDCADADSRTALRAAAWGGHEDIVLNLL 485
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
852-906 |
1.19e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 46.57 E-value: 1.19e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 268607595 852 LIEHGAV-VDHTCNQGATALCIAAQEGHIDVVQVLLEHGADPNHADQFGRTAMRVA 906
Cdd:pfam13857 1 LLEHGPIdLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
498-556 |
2.47e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 45.73 E-value: 2.47e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 268607595 498 GRTALIAAAYMGHREIVEHLLDHGAEVNHEDVDGRTALSVAalcvpASKGHASVVSLLI 556
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFA-----ASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
708-753 |
2.81e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 45.73 E-value: 2.81e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 268607595 708 ASQEGHYDCVQILLENKSNIDQRGYDGRNALRVAALEGHRDIVELL 753
Cdd:pfam13637 8 AAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
734-787 |
2.98e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 45.34 E-value: 2.98e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 268607595 734 GRNALRVAALEGHRDIVELLFSHGADVNCKDADGRPTLYILALENQLTMAEYFL 787
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
705-907 |
3.02e-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: 51.62 E-value: 3.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 705 FILASQEGHYDCVQILLEN--KSNIDQRGYDGRNALRVAALEG-HRDIVELLFSHgadvNCKDADGRPTLYILALENQ-- 779
Cdd:TIGR00870 21 FLPAAERGDLASVYRDLEEpkKLNINCPDRLGRSALFVAAIENeNLELTELLLNL----SCRGAVGDTLLHAISLEYVda 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 780 -----LTMAEYFLENGANVEASD------AEGRTALHVSCWQGHMEMVQVLIAYHADVNAA---DNEKRSALQSAAWQGh 845
Cdd:TIGR00870 97 veailLHLLAAFRKSGPLELANDqytsefTPGITALHLAAHRQNYEIVKLLLERGASVPARacgDFFVKSQGVDSFYHG- 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 268607595 846 vkvvqlliEHgavvdhtcnqgatALCIAAQEGHIDVVQVLLEHGADPNHADQFGRTAMRVAA 907
Cdd:TIGR00870 176 --------ES-------------PLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLV 216
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
484-538 |
3.26e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 45.42 E-value: 3.26e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 268607595 484 LLQHG-AEVNKADNEGRTALIAAAYMGHREIVEHLLDHGAEVNHEDVDGRTALSVA 538
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
475-794 |
4.00e-06 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 50.82 E-value: 4.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 475 GGHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLDHGAEVNHEDVDGRTALSVAAlcvPASKGHASVVSL 554
Cdd:PHA02946 49 GLDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLS---GTDDEVIERINL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 555 LIDRGAEVDH-CDKDGMTPLLvAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLA--AASMGHASVVNTLLFWGAAVDSI 631
Cdd:PHA02946 126 LVQYGAKINNsVDEEGCGPLL-ACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRhlMSDNPKASTISWMMKLGISPSKP 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 632 DSEGRTVLSIASAQ--GNVEVVRTLLDrGLDENHRDDAGWTPLHMAAfegHRLICEALIEQGARTNEIDNDGRIPFILAS 709
Cdd:PHA02946 205 DHDGNTPLHIVCSKtvKNVDIINLLLP-STDVNKQNKFGDSPLTLLI---KTLSPAHLINKLLSTSNVITDQTVNICIFY 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 710 QEGhyDCVQILlenksNIDQRGYDGRNaLRVAALEGHRDIVELLFSHgaDVNCKDAdgrptLYILALENQLTMAEYFLEN 789
Cdd:PHA02946 281 DRD--DVLEII-----NDKGKQYDSTD-FKMAVEVGSIRCVKYLLDN--DIICEDA-----MYYAVLSEYETMVDYLLFN 345
|
....*
gi 268607595 790 GANVE 794
Cdd:PHA02946 346 HFSVD 350
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
660-887 |
4.18e-06 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).
Pssm-ID: 411975 [Multi-domain] Cd Length: 600 Bit Score: 51.03 E-value: 4.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 660 DENHRDDAGWTPLHMAAFEGH--RLICEALIEQGARtneiDNDGRIPFILASQEGHYdcvqillenksnidqrgYDGRNA 737
Cdd:cd21882 18 SAYQRGATGKTCLHKAALNLNdgVNEAIMLLLEAAP----DSGNPKELVNAPCTDEF-----------------YQGQTA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 738 LRVAALEGHRDIVELLFSHGADVN---CKDA---DGRPTLY-------ILALENQLTMAEYFLENG---ANVEASDAEGR 801
Cdd:cd21882 77 LHIAIENRNLNLVRLLVENGADVSaraTGRFfrkSPGNLFYfgelplsLAACTNQEEIVRLLLENGaqpAALEAQDSLGN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 802 TALHVscwqghmemvQVLIAYhadvNAADNEKRSalqsaawqghVKVVQLLIEHGAVVDHTC-------NQGATALCIAA 874
Cdd:cd21882 157 TVLHA----------LVLQAD----NTPENSAFV----------CQMYNLLLSYGAHLDPTQqleeipnHQGLTPLKLAA 212
|
250
....*....|...
gi 268607595 875 QEGHIDVVQVLLE 887
Cdd:cd21882 213 VEGKIVMFQHILQ 225
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
787-840 |
4.55e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 45.03 E-value: 4.55e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 268607595 787 LENG-ANVEASDAEGRTALHVSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSA 840
Cdd:pfam13857 2 LEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
347-622 |
4.65e-06 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 50.60 E-value: 4.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 347 DSIRTLLDNGASVNQCDSNGR----TLLAN-AAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTlaarqghtkvvnCLIGC 421
Cdd:PHA02798 52 DIVKLFINLGANVNGLDNEYStplcTILSNiKDYKHMLDIVKILIENGADINKKNSDGETPLY------------CLLSN 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 422 GAnINhtdqdgwtalrsaawggHTEVVSALLYAGVKVDCADADSRTALRAAAWGGHE---DIVLNLLQHGAEVNKADN-E 497
Cdd:PHA02798 120 GY-IN-----------------NLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDINTHNNkE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 498 GRTALiaAAYMGHR------EIVEHLLDHGAEVNHEDVDGRTAL--SVAALCVPASKGHASVVSLLIdrgAEVDHCDKD- 568
Cdd:PHA02798 182 KYDTL--HCYFKYNidridaDILKLFVDNGFIINKENKSHKKKFmeYLNSLLYDNKRFKKNILDFIF---SYIDINQVDe 256
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 268607595 569 -GMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLL 622
Cdd:PHA02798 257 lGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSIL 311
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
568-600 |
5.04e-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: 5.04e-06
10 20 30
....*....|....*....|....*....|....
gi 268607595 568 DGMTPLLVAAYE-GHVDVVDLLLEGGADVDHTDN 600
Cdd:pfam00023 1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
334-386 |
9.67e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 44.19 E-value: 9.67e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 268607595 334 RTSCIVRQA-LEREDSIRTLLDNGASVNQCDSNGRTLLANAAYSGSLDVVNLLV 386
Cdd:pfam13637 1 ELTALHAAAaSGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
366-419 |
1.13e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 43.80 E-value: 1.13e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 268607595 366 GRTLLANAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLI 419
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
352-406 |
1.35e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 43.87 E-value: 1.35e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 268607595 352 LLDNG-ASVNQCDSNGRTLLANAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLA 406
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
799-831 |
1.43e-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: 43.05 E-value: 1.43e-05
10 20 30
....*....|....*....|....*....|....
gi 268607595 799 EGRTALHVSCWQ-GHMEMVQVLIAYHADVNAADN 831
Cdd:pfam00023 1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
555-606 |
2.56e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 42.72 E-value: 2.56e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 268607595 555 LIDRG-AEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPL 606
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
717-778 |
2.89e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 48.36 E-value: 2.89e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 268607595 717 VQILLENKSNIDQRGYDGRNALRVAALEGHRDIVELLFSHGADVNCKDADGRpTLYILALEN 778
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGK-TPLELAEEN 158
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
497-528 |
3.25e-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: 41.89 E-value: 3.25e-05
10 20 30
....*....|....*....|....*....|...
gi 268607595 497 EGRTAL-IAAAYMGHREIVEHLLDHGAEVNHED 528
Cdd:pfam00023 1 DGNTPLhLAAGRRGNLEIVKLLLSKGADVNARD 33
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
867-923 |
3.26e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 48.36 E-value: 3.26e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 268607595 867 ATALCIAAQEGHIDVVQVLLEHGADPNHADQFGRTAMRVAAKNGHSQIIKLLEKYGA 923
Cdd:PTZ00322 83 TVELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGA 139
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
865-893 |
3.41e-05 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 41.80 E-value: 3.41e-05
10 20
....*....|....*....|....*....
gi 268607595 865 QGATALCIAAQEGHIDVVQVLLEHGADPN 893
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
865-896 |
4.12e-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: 41.51 E-value: 4.12e-05
10 20 30
....*....|....*....|....*....|...
gi 268607595 865 QGATALCIAA-QEGHIDVVQVLLEHGADPNHAD 896
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
846-923 |
4.34e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 47.35 E-value: 4.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 846 VKVVQLLIEHGAVVDHTCNQGATALCIAAQEGHI-----DVVQVLLEHGADPNHADQFGRTAMRVAA--KNGHSQIIKLL 918
Cdd:PHA03100 48 IDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYL 127
|
....*
gi 268607595 919 EKYGA 923
Cdd:PHA03100 128 LDNGA 132
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
316-434 |
5.42e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 45.58 E-value: 5.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 316 EVLQLLVKAGAHVN--SEDDRTSCI-----VRQALErEDSIRTLLDNGASVNQCDSNGRTLLAN--AAYSGSLDVVNLLV 386
Cdd:PHA02859 67 EILKFLIENGADVNfkTRDNNLSALhhylsFNKNVE-PEILKILIDSGSSITEEDEDGKNLLHMymCNFNVRINVIKLLI 145
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 268607595 387 SRGADLEIEDAHG----HTPLTLAARQghtKVVNCLIGCGANINHTDQDGWT 434
Cdd:PHA02859 146 DSGVSFLNKDFDNnnilYSYILFHSDK---KIFDFLTSLGIDINETNKSGYN 194
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
651-918 |
6.10e-05 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 46.97 E-value: 6.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 651 VRTLLDRGLDENHRDDAGWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIP--FILASQEGHYDCVQILLENKSNID 728
Cdd:PHA02946 55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPlyYLSGTDDEVIERINLLVQYGAKIN 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 729 QRGYDGRNALRVAALEGHRDIVELLFSHGADVNCKDADGRPTL--YILALENQLTMAEYFLENGANVEASDAEGRTALHV 806
Cdd:PHA02946 135 NSVDEEGCGPLLACTDPSERVFKKIMSIGFEARIVDKFGKNHIhrHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHI 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 807 SCWQ--GHMEMVQVLIAyHADVNAADNEKRSALQ---SAAWQGHVkVVQLLIEHGAVVDHTCNqgataLCIAAQEGhiDV 881
Cdd:PHA02946 215 VCSKtvKNVDIINLLLP-STDVNKQNKFGDSPLTlliKTLSPAHL-INKLLSTSNVITDQTVN-----ICIFYDRD--DV 285
|
250 260 270
....*....|....*....|....*....|....*..
gi 268607595 882 VQVLLEHGadpnhaDQFGRTAMRVAAKNGHSQIIKLL 918
Cdd:PHA02946 286 LEIINDKG------KQYDSTDFKMAVEVGSIRCVKYL 316
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
568-596 |
6.97e-05 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 41.03 E-value: 6.97e-05
10 20
....*....|....*....|....*....
gi 268607595 568 DGMTPLLVAAYEGHVDVVDLLLEGGADVD 596
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
587-642 |
8.66e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 41.56 E-value: 8.66e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 268607595 587 LLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIA 642
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
568-597 |
1.16e-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: 40.32 E-value: 1.16e-04
10 20 30
....*....|....*....|....*....|
gi 268607595 568 DGMTPLLVAAYEGHVDVVDLLLEGGADVDH 597
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
484-555 |
1.22e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 46.43 E-value: 1.22e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 268607595 484 LLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLDHGAEVNHEDVDGRTALSVAalcvpASKGHASVVSLL 555
Cdd:PTZ00322 101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA-----EENGFREVVQLL 167
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
497-525 |
1.26e-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: 1.26e-04
10 20
....*....|....*....|....*....
gi 268607595 497 EGRTALIAAAYMGHREIVEHLLDHGAEVN 525
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
398-426 |
1.50e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 39.88 E-value: 1.50e-04
10 20
....*....|....*....|....*....
gi 268607595 398 HGHTPLTLAARQGHTKVVNCLIGCGANIN 426
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
405-495 |
1.55e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 46.04 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 405 LAArQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGHTEVVSALLYAGVKVDCADADSRTALRAAAWGGHEDIVLNL 484
Cdd:PTZ00322 89 LAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
|
90
....*....|.
gi 268607595 485 LQHGAEVNKAD 495
Cdd:PTZ00322 168 SRHSQCHFELG 178
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
799-828 |
1.62e-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: 39.88 E-value: 1.62e-04
10 20 30
....*....|....*....|....*....|
gi 268607595 799 EGRTALHVSCWQGHMEMVQVLIAYHADVNA 828
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
720-775 |
1.62e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 40.79 E-value: 1.62e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 268607595 720 LLENKS-NIDQRGYDGRNALRVAALEGHRDIVELLFSHGADVNCKDADGrPTLYILA 775
Cdd:pfam13857 1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEG-LTALDLA 56
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
318-430 |
1.66e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 45.72 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 318 LQLLVKAGAHVNSEDDRTSCIVRQALEREDSIRTLLDNGASVNQCDSNGRTLLANA-AYSGSLDVVNLLVSRGADLEIED 396
Cdd:PHA02874 206 IKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIELLINNASINDQDIDGSTPLHHAiNPPCDIDIIDILLYHKADISIKD 285
|
90 100 110
....*....|....*....|....*....|....*
gi 268607595 397 AHGHTPLTLAARQ-GHTKVVNCLIGCGANINHTDQ 430
Cdd:PHA02874 286 NKGENPIDTAFKYiNKDPVIKDIIANAVLIKEADK 320
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
531-678 |
2.27e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).
Pssm-ID: 411975 [Multi-domain] Cd Length: 600 Bit Score: 45.26 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 531 GRTALSVAALcvpasKGHASVVSLLIDRGAEVD-------------HCDKDGMTPLLVAAYEGHVDVVDLLLEGGAD--- 594
Cdd:cd21882 73 GQTALHIAIE-----NRNLNLVRLLVENGADVSaratgrffrkspgNLFYFGELPLSLAACTNQEEIVRLLLENGAQpaa 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 595 VDHTDNNGRTPLLAAASMGHASVVNT---------LLFWGAAVDSIDS-------EGRTVLSIASAQGNVEVVRTLLDRG 658
Cdd:cd21882 148 LEAQDSLGNTVLHALVLQADNTPENSafvcqmynlLLSYGAHLDPTQQleeipnhQGLTPLKLAAVEGKIVMFQHILQRE 227
|
170 180
....*....|....*....|....*.
gi 268607595 659 LDENH----RDDAGWT--PLHMAAFE 678
Cdd:cd21882 228 FSGPYqplsRKFTEWTygPVTSSLYD 253
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
799-828 |
2.40e-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: 39.55 E-value: 2.40e-04
10 20 30
....*....|....*....|....*....|
gi 268607595 799 EGRTALHVSCWQGHMEMVQVLIAYHADVNA 828
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
479-605 |
2.41e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 43.65 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 479 DIVLNLLQHGAEVN-KADNEGRTALiaAAYMGHR-----EIVEHLLDHGAEVNHEDVDGRTALSVaALCVPASKghASVV 552
Cdd:PHA02859 67 EILKFLIENGADVNfKTRDNNLSAL--HHYLSFNknvepEILKILIDSGSSITEEDEDGKNLLHM-YMCNFNVR--INVI 141
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 268607595 553 SLLIDRGAEVDHCDKDGmTPLLVAAYEGHVD--VVDLLLEGGADVDHTDNNGRTP 605
Cdd:PHA02859 142 KLLIDSGVSFLNKDFDN-NNILYSYILFHSDkkIFDFLTSLGIDINETNKSGYNC 195
|
|
| PHA02989 |
PHA02989 |
ankyrin repeat protein; Provisional |
313-538 |
2.45e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222954 [Multi-domain] Cd Length: 494 Bit Score: 45.12 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 313 KEQEVLQLLVKAGAHVNSED-DRTSCIV----RQALEREDSIRTLLDNGASVNQC-DSNGRTLLAN--AAYSGSLDVVNL 384
Cdd:PHA02989 86 KIKKIVKLLLKFGADINLKTfNGVSPIVcfiyNSNINNCDMLRFLLSKGINVNDVkNSRGYNLLHMylESFSVKKDVIKI 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 385 LVSRGAD-LEIEDAHGHTPLTLAARQG----HTKVVNCLIGCGANINHTDQdgwtalrsaawgGHTEVVSALLyagvkvd 459
Cdd:PHA02989 166 LLSFGVNlFEKTSLYGLTPMNIYLRNDidviSIKVIKYLIKKGVNIETNNN------------GSESVLESFL------- 226
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 268607595 460 cadaDSRTALRAaawggHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLDHGAEVNHEDVDGRTALSVA 538
Cdd:PHA02989 227 ----DNNKILSK-----KEFKVLNFILKYIKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYA 296
|
|
| TRPV2 |
cd22197 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ... |
706-887 |
2.45e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411981 [Multi-domain] Cd Length: 640 Bit Score: 45.23 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 706 ILASQEGHYDCVQILLEnksnIDQRG---------------YDGRNALRVAALEGHRDIVELLFSHGADVNCKDAD---- 766
Cdd:cd22197 55 VLNLQDGVNACIMPLLE----IDKDSgnpkplvnaqctdeyYRGHSALHIAIEKRSLQCVKLLVENGADVHARACGrffq 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 767 ---------GRPTLYILALENQLTMAEYFLENG---ANVEASDAEGRTALhvscwqghmemvqvliayHADVNAADN-EK 833
Cdd:cd22197 131 kkqgtcfyfGELPLSLAACTKQWDVVNYLLENPhqpASLQAQDSLGNTVL------------------HALVMIADNsPE 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 268607595 834 RSALQSAAWQGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQEGHIDVVQVLLE 887
Cdd:cd22197 193 NSALVIKMYDGLLQAGARLCPTVQLEEISNHEGLTPLKLAAKEGKIEIFRHILQ 246
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
320-398 |
2.90e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 44.66 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 320 LLVKAGAHVNSEDDRTSCIVRQAL--EREDSIRTLLDNGASVNQCDSNGRTLLANAAYSGSLDVVNLLVSRGADLEIEDA 397
Cdd:PHA03100 177 YLLSYGVPINIKDVYGFTPLHYAVynNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
|
.
gi 268607595 398 H 398
Cdd:PHA03100 257 T 257
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
780-916 |
3.38e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411978 [Multi-domain] Cd Length: 680 Bit Score: 44.75 E-value: 3.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 780 LTMAEyflENG-------ANVEASDAEGRTALHVSCWQGHMEMVQVLIAYHADVNAAD-----NEK---------RSALQ 838
Cdd:cd22194 117 LAFAE---ENGildrfinAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAkgvffNPKykhegfyfgETPLA 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 839 SAAWQGHVKVVQLLIEH----GAVVDHTCNQGATALCIAAQ--EGHIDVV-----QVLLEHG-----ADPNHAdqfGRTA 902
Cdd:cd22194 194 LAACTNQPEIVQLLMEKestdITSQDSRGNTVLHALVTVAEdsKTQNDFVkrmydMILLKSEnknleTIRNNE---GLTP 270
|
170
....*....|....
gi 268607595 903 MRVAAKNGHSQIIK 916
Cdd:cd22194 271 LQLAAKMGKAEILK 284
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
398-429 |
4.06e-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: 4.06e-04
10 20 30
....*....|....*....|....*....|...
gi 268607595 398 HGHTPLTLAA-RQGHTKVVNCLIGCGANINHTD 429
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
733-762 |
4.16e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 38.72 E-value: 4.16e-04
10 20 30
....*....|....*....|....*....|
gi 268607595 733 DGRNALRVAALEGHRDIVELLFSHGADVNC 762
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
541-679 |
5.27e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 42.88 E-value: 5.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 541 CVPASKGHASVVSLLIDRGAEVDHCDKD-GMTPL---LVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPL---LAAASMg 613
Cdd:PHA02859 58 CLEKDKVNVEILKFLIENGADVNFKTRDnNLSALhhyLSFNKNVEPEILKILIDSGSSITEEDEDGKNLLhmyMCNFNV- 136
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 268607595 614 HASVVNTLLFWGAAVDSIDSEGRTVL-SIASAQGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEG 679
Cdd:PHA02859 137 RINVIKLLIDSGVSFLNKDFDNNNILySYILFHSDKKIFDFLTSLGIDINETNKSGYNCYDLIKFRN 203
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
668-699 |
6.26e-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: 6.26e-04
10 20 30
....*....|....*....|....*....|...
gi 268607595 668 GWTPLHMAA-FEGHRLICEALIEQGARTNEIDN 699
Cdd:pfam00023 2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
733-764 |
6.64e-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: 6.64e-04
10 20 30
....*....|....*....|....*....|...
gi 268607595 733 DGRNALRVAALE-GHRDIVELLFSHGADVNCKD 764
Cdd:pfam00023 1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
729-905 |
6.89e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).
Pssm-ID: 411975 [Multi-domain] Cd Length: 600 Bit Score: 43.72 E-value: 6.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 729 QRGYDGRNALRVAAL---EGHRDIVELLFshgadvnckDADgRPTLYILALENQLTMAEYFlenganveasdaEGRTALH 805
Cdd:cd21882 21 QRGATGKTCLHKAALnlnDGVNEAIMLLL---------EAA-PDSGNPKELVNAPCTDEFY------------QGQTALH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 806 VSCWQGHMEMVQVLIAYHADVNAADNekrsalqSAAWQGHvkvvqlliehgavvDHTCNQ-GATALCIAAQEGHIDVVQV 884
Cdd:cd21882 79 IAIENRNLNLVRLLVENGADVSARAT-------GRFFRKS--------------PGNLFYfGELPLSLAACTNQEEIVRL 137
|
170 180
....*....|....*....|....
gi 268607595 885 LLEHGADP---NHADQFGRTAMRV 905
Cdd:cd21882 138 LLENGAQPaalEAQDSLGNTVLHA 161
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
530-567 |
7.04e-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: 38.04 E-value: 7.04e-04
10 20 30
....*....|....*....|....*....|....*...
gi 268607595 530 DGRTALSVAAlcvpASKGHASVVSLLIDRGAEVDHCDK 567
Cdd:pfam00023 1 DGNTPLHLAA----GRRGNLEIVKLLLSKGADVNARDK 34
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
398-427 |
7.30e-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.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 38.01 E-value: 7.30e-04
10 20 30
....*....|....*....|....*....|
gi 268607595 398 HGHTPLTLAARQGHTKVVNCLIGCGANINH 427
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
517-576 |
7.46e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 38.87 E-value: 7.46e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 268607595 517 LLDHG-AEVNHEDVDGRTALSVAAlcvpaSKGHASVVSLLIDRGAEVDHCDKDGMTPLLVA 576
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAA-----KYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
302-394 |
7.91e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 43.44 E-value: 7.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 302 PVRDSLSTL----IPKEQEVLQLLVKAGAHVNSED--DRTSCIVRQALEREDSIRTLLDNGASVNQCDSNGR-TLLANAA 374
Cdd:PHA02875 131 PNTDKFSPLhlavMMGDIKGIELLIDHKACLDIEDccGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAI 210
|
90 100
....*....|....*....|
gi 268607595 375 YSGSLDVVNLLVSRGADLEI 394
Cdd:PHA02875 211 ENNKIDIVRLFIKRGADCNI 230
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
497-526 |
9.42e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 37.62 E-value: 9.42e-04
10 20 30
....*....|....*....|....*....|
gi 268607595 497 EGRTALIAAAYMGHREIVEHLLDHGAEVNH 526
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
647-761 |
9.75e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 42.11 E-value: 9.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 647 NVEVVRTLLDRGLDENHR-DDAGWTPLHmaafegHRL---------ICEALIEQGARTNEIDNDGRIPF--ILASQEGHY 714
Cdd:PHA02859 65 NVEILKFLIENGADVNFKtRDNNLSALH------HYLsfnknvepeILKILIDSGSSITEEDEDGKNLLhmYMCNFNVRI 138
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 268607595 715 DCVQILLENKSNIDQRGYDGRNALRVAAL-EGHRDIVELLFSHGADVN 761
Cdd:PHA02859 139 NVIKLLIDSGVSFLNKDFDNNNILYSYILfHSDKKIFDFLTSLGIDIN 186
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
733-762 |
1.48e-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: 37.24 E-value: 1.48e-03
10 20 30
....*....|....*....|....*....|
gi 268607595 733 DGRNALRVAALEGHRDIVELLFSHGADVNC 762
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
847-931 |
1.57e-03 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 42.35 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 847 KVVQLLIEHGAVVDHTCNQGATALCIAAQEGHIDVVQVLLEHGADPNHADQFGRTAMRVAAKNGHSQI--IKLLEKYGAS 924
Cdd:PHA02946 53 RFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIerINLLVQYGAK 132
|
90
....*....|..
gi 268607595 925 SLN-----GCSP 931
Cdd:PHA02946 133 INNsvdeeGCGP 144
|
|
| PHA02795 |
PHA02795 |
ankyrin-like protein; Provisional |
359-410 |
1.93e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165157 [Multi-domain] Cd Length: 437 Bit Score: 42.29 E-value: 1.93e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 268607595 359 VNQCDSNGRTLLANAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLAARQG 410
Cdd:PHA02795 214 INQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRG 265
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
531-690 |
2.11e-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: 42.17 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 531 GRTALSVAALCVpaSKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGH-----------VDVVDLLLEGGADVdHTD 599
Cdd:cd21882 26 GKTCLHKAALNL--NDGVNEAIMLLLEAAPDSGNPKELVNAPCTDEFYQGQtalhiaienrnLNLVRLLVENGADV-SAR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 600 NNGRT--------------PLLAAASMGHASVVNTLLFWG---AAVDSIDSEGRTVLSIASAQGNVEVVRTLL------- 655
Cdd:cd21882 103 ATGRFfrkspgnlfyfgelPLSLAACTNQEEIVRLLLENGaqpAALEAQDSLGNTVLHALVLQADNTPENSAFvcqmynl 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 268607595 656 ----DRGLDE--------NHRddaGWTPLHMAAFEGHRLICEALIEQ 690
Cdd:cd21882 183 llsyGAHLDPtqqleeipNHQ---GLTPLKLAAVEGKIVMFQHILQR 226
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
366-436 |
3.10e-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: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 366 GRTLLANAAYSGSLDVVNLLVSRGADLEIEDA--------------HGHTPLTLAARQGHTKVVNCLIGCGANINHTDQD 431
Cdd:cd22192 89 GETALHIAVVNQNLNLVRELIARGADVVSPRAtgtffrpgpknliyYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168
|
....*
gi 268607595 432 GWTAL 436
Cdd:cd22192 169 GNTVL 173
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
654-708 |
3.11e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 36.94 E-value: 3.11e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 268607595 654 LLDRG-LDENHRDDAGWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIPFILA 708
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
601-632 |
3.60e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 36.11 E-value: 3.60e-03
10 20 30
....*....|....*....|....*....|...
gi 268607595 601 NGRTPL-LAAASMGHASVVNTLLFWGAAVDSID 632
Cdd:pfam00023 1 DGNTPLhLAAGRRGNLEIVKLLLSKGADVNARD 33
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
313-409 |
3.73e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 41.40 E-value: 3.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 313 KEQEVLQLLVKAGAHVNSEDDRTSCIVRQALE--REDSIRTLLDNGASVNQCDSNGRTLL-------------------- 370
Cdd:PHA02878 179 KDQRLTELLLSYGANVNIPDKTNNSPLHHAVKhyNKPIVHILLENGASTDARDKCGNTPLhisvgyckdydilklllehg 258
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 268607595 371 --ANAAYS-----------GSLDVVNLLVSRGADLEIEDAHGHTPLTLAARQ 409
Cdd:PHA02878 259 vdVNAKSYilgltalhssiKSERKLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
846-922 |
4.48e-03 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 41.39 E-value: 4.48e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 268607595 846 VKVVQLLIEHGAvvDHTCNQGATALCIAAQEGHIDVVQVLLEHGADPNHADQFGRTAMRVAAKNGHSQIIKLLEKYG 922
Cdd:PLN03192 507 LNVGDLLGDNGG--EHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA 581
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
668-692 |
5.37e-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: 35.70 E-value: 5.37e-03
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
314-405 |
5.50e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 39.80 E-value: 5.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 314 EQEVLQLLVKAGAHVNSEDDRTSCIVRQALE----REDSIRTLLDNGASVNQCDSNGRTLLAN-AAYSGSLDVVNLLVSR 388
Cdd:PHA02859 102 EPEILKILIDSGSSITEEDEDGKNLLHMYMCnfnvRINVIKLLIDSGVSFLNKDFDNNNILYSyILFHSDKKIFDFLTSL 181
|
90
....*....|....*..
gi 268607595 389 GADLEIEDAHGHTPLTL 405
Cdd:PHA02859 182 GIDINETNKSGYNCYDL 198
|
|
| PHA02795 |
PHA02795 |
ankyrin-like protein; Provisional |
813-921 |
5.62e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165157 [Multi-domain] Cd Length: 437 Bit Score: 40.75 E-value: 5.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 813 MEMVQVLIAYHADVNAADNEKRSALQSAAWQGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQEG--------HIDVVQV 884
Cdd:PHA02795 201 LEIYKLCIPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRGsviarretHLKILEI 280
|
90 100 110
....*....|....*....|....*....|....*..
gi 268607595 885 LLEhgaDPNHADQFGRTAMRVAAKNghSQIIKLLEKY 921
Cdd:PHA02795 281 LLR---EPLSIDCIKLAILNNTIEN--HDVIKLCIKY 312
|
|
| PHA02716 |
PHA02716 |
CPXV016; CPX019; EVM010; Provisional |
503-673 |
5.65e-03 |
|
CPXV016; CPX019; EVM010; Provisional
Pssm-ID: 165089 [Multi-domain] Cd Length: 764 Bit Score: 41.05 E-value: 5.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 503 IAAAYMGHR----EIVEHLLDHGAEVNHEDVDGRTALSVAALCVPASkghASVVSLLIDRGAEVDHCDKDGMTPLLvaAY 578
Cdd:PHA02716 180 ILHAYLGNMyvdiDILEWLCNNGVNVNLQNNHLITPLHTYLITGNVC---ASVIKKIIELGGDMDMKCVNGMSPIM--TY 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 579 EGHVDVVDLLLEgGADVDHTDNNGRT--PLLAAASMGHA-----SVVNTLLFWGAAVDSIDSEGRTVLS--IASAQGNVE 649
Cdd:PHA02716 255 IINIDNINPEIT-NIYIESLDGNKVKniPMILHSYITLArnidiSVVYSFLQPGVKLHYKDSAGRTCLHqyILRHNISTD 333
|
170 180
....*....|....*....|....
gi 268607595 650 VVRTLLDRGLDENHRDDAGWTPLH 673
Cdd:PHA02716 334 IIKLLHEYGNDLNEPDNIGNTVLH 357
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
748-868 |
5.91e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 39.42 E-value: 5.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 748 DIVELLFSHGADVNCKDADGRPTL---YILALEN-QLTMAEYFLENGANVEASDAEGRTALHV--SCWQGHMEMVQVLIA 821
Cdd:PHA02859 67 EILKFLIENGADVNFKTRDNNLSAlhhYLSFNKNvEPEILKILIDSGSSITEEDEDGKNLLHMymCNFNVRINVIKLLID 146
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 268607595 822 YHADVNAADNEKRSALQS-AAWQGHVKVVQLLIEHGAVVDHTCNQGAT 868
Cdd:PHA02859 147 SGVSFLNKDFDNNNILYSyILFHSDKKIFDFLTSLGIDINETNKSGYN 194
|
|
| TRPV2 |
cd22197 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ... |
531-664 |
6.20e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411981 [Multi-domain] Cd Length: 640 Bit Score: 40.61 E-value: 6.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 531 GRTALSVAAlcvpaSKGHASVVSLLIDRGAEV-------------DHCDKDGMTPLLVAAYEGHVDVVDLLLEGGAD--- 594
Cdd:cd22197 94 GHSALHIAI-----EKRSLQCVKLLVENGADVharacgrffqkkqGTCFYFGELPLSLAACTKQWDVVNYLLENPHQpas 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 595 VDHTDNNGRTPLLAAASMGHASVVNT---------LLFWGAAVDS-------IDSEGRTVLSIASAQGNVEVVRTLLDRG 658
Cdd:cd22197 169 LQAQDSLGNTVLHALVMIADNSPENSalvikmydgLLQAGARLCPtvqleeiSNHEGLTPLKLAAKEGKIEIFRHILQRE 248
|
....*.
gi 268607595 659 LDENHR 664
Cdd:cd22197 249 FSGPYQ 254
|
|
| PHA02716 |
PHA02716 |
CPXV016; CPX019; EVM010; Provisional |
551-762 |
6.70e-03 |
|
CPXV016; CPX019; EVM010; Provisional
Pssm-ID: 165089 [Multi-domain] Cd Length: 764 Bit Score: 40.67 E-value: 6.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 551 VVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHV--DVVDLLLEGGADVDHTDNNGRTPLLAaaSMGHASVVNTLLFwGAAV 628
Cdd:PHA02716 194 ILEWLCNNGVNVNLQNNHLITPLHTYLITGNVcaSVIKKIIELGGDMDMKCVNGMSPIMT--YIINIDNINPEIT-NIYI 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 629 DSIDSEGRT------VLSIASAQG-NVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEgHRL---ICEALIEQGARTNEID 698
Cdd:PHA02716 271 ESLDGNKVKnipmilHSYITLARNiDISVVYSFLQPGVKLHYKDSAGRTCLHQYILR-HNIstdIIKLLHEYGNDLNEPD 349
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 268607595 699 NDGRIpfILASQEGHYDCVQILlenKSNIDqrgydgrNALRVaaleghrDIVELLFSHGAD---VNC 762
Cdd:PHA02716 350 NIGNT--VLHTYLSMLSVVNIL---DPETD-------NDIRL-------DVIQCLISLGADitaVNC 397
|
|
| PHA02795 |
PHA02795 |
ankyrin-like protein; Provisional |
529-633 |
7.27e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165157 [Multi-domain] Cd Length: 437 Bit Score: 40.36 E-value: 7.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 529 VDGRTALSVAALCVPASKghasvvsllidrgaEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLA 608
Cdd:PHA02795 195 VDEPTVLEIYKLCIPYIE--------------DINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDV 260
|
90 100 110
....*....|....*....|....*....|...
gi 268607595 609 AASMG--------HASVVNTLLFWGAAVDSIDS 633
Cdd:PHA02795 261 AVDRGsviarretHLKILEILLREPLSIDCIKL 293
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
686-887 |
7.35e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411978 [Multi-domain] Cd Length: 680 Bit Score: 40.51 E-value: 7.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 686 ALIEQGARTNEIdndgrIPFILASQEGHyDCVQILLEnkSNIDQRGYDGRNALRVAALEGHRDIVELLFSHGADVNCKdA 765
Cdd:cd22194 101 ALLNINENTKEI-----VRILLAFAEEN-GILDRFIN--AEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAH-A 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 766 DGR---PT------------LYILALENQLTMAEYFLENGANVEAS-DAEGRTALhvscwqghmemvqvliayHADVNAA 829
Cdd:cd22194 172 KGVffnPKykhegfyfgetpLALAACTNQPEIVQLLMEKESTDITSqDSRGNTVL------------------HALVTVA 233
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 268607595 830 DNekrsalqSAAWQGHVKVV--QLLIEHG--AVVDHTCNQGATALCIAAQEGHIDVVQVLLE 887
Cdd:cd22194 234 ED-------SKTQNDFVKRMydMILLKSEnkNLETIRNNEGLTPLQLAAKMGKAEILKYILS 288
|
|
| PHA02716 |
PHA02716 |
CPXV016; CPX019; EVM010; Provisional |
550-672 |
7.36e-03 |
|
CPXV016; CPX019; EVM010; Provisional
Pssm-ID: 165089 [Multi-domain] Cd Length: 764 Bit Score: 40.67 E-value: 7.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 550 SVVSLLIDRGAEVDHCDKDGMTPL--LVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMghASVVNTLlfwgaa 627
Cdd:PHA02716 298 SVVYSFLQPGVKLHYKDSAGRTCLhqYILRHNISTDIIKLLHEYGNDLNEPDNIGNTVLHTYLSM--LSVVNIL------ 369
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 268607595 628 vdsiDSEGRTVLsiasaqgNVEVVRTLLDRGLDENHRDDAGWTPL 672
Cdd:PHA02716 370 ----DPETDNDI-------RLDVIQCLISLGADITAVNCLGYTPL 403
|
|
| PHA02989 |
PHA02989 |
ankyrin repeat protein; Provisional |
715-806 |
7.36e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222954 [Multi-domain] Cd Length: 494 Bit Score: 40.49 E-value: 7.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 715 DCVQILLENKSNIDQRGYDGR---NALRVAALEGH--RDIVELLFSHGADVNCKDADGRPTLYILALE---NQLTMAEYF 786
Cdd:PHA02989 51 KIVKLLIDNGADVNYKGYIETplcAVLRNREITSNkiKKIVKLLLKFGADINLKTFNGVSPIVCFIYNsniNNCDMLRFL 130
|
90 100
....*....|....*....|.
gi 268607595 787 LENGANV-EASDAEGRTALHV 806
Cdd:PHA02989 131 LSKGINVnDVKNSRGYNLLHM 151
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
700-728 |
7.41e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 35.26 E-value: 7.41e-03
10 20
....*....|....*....|....*....
gi 268607595 700 DGRIPFILASQEGHYDCVQILLENKSNID 728
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
|
|
| PHA02795 |
PHA02795 |
ankyrin-like protein; Provisional |
490-598 |
7.59e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165157 [Multi-domain] Cd Length: 437 Bit Score: 40.36 E-value: 7.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607595 490 EVNKADNEGRTALIAAAYMGHREIVEHLLDHGAEVNHEDVDGRTALSVA---ALCVPASKGHASVVSLLIDRGAEVDhCD 566
Cdd:PHA02795 213 DINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAvdrGSVIARRETHLKILEILLREPLSID-CI 291
|
90 100 110
....*....|....*....|....*....|..
gi 268607595 567 KdgmTPLLVAAYEGHvDVVDLLLEGGADVDHT 598
Cdd:PHA02795 292 K---LAILNNTIENH-DVIKLCIKYFMMVDYS 319
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
466-496 |
9.94e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 34.96 E-value: 9.94e-03
10 20 30
....*....|....*....|....*....|..
gi 268607595 466 RTAL-RAAAWGGHEDIVLNLLQHGAEVNKADN 496
Cdd:pfam00023 3 NTPLhLAAGRRGNLEIVKLLLSKGADVNARDK 34
|
|
|