|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
558-851 |
7.11e-62 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 213.66 E-value: 7.11e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 558 LDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGHTEVVSALLYAGVKV 637
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 638 DCADADSRTALRAAAWGGHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLDHGAEVNHEDVDGRTALSVA 717
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 718 alcvpASKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVV 797
Cdd:COG0666 161 -----AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIV 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 62988328 798 NTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDENHRDDAGWTPL 851
Cdd:COG0666 236 KLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
629-917 |
9.03e-60 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 207.50 E-value: 9.03e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 629 ALLYAGVKVDCADADSRTALRAAAWGGHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLDHGAEVNHEDV 708
Cdd:COG0666 6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 709 DGRTALSVAAlcvpaSKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAA 788
Cdd:COG0666 86 GGNTLLHAAA-----RNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 789 ASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRLICEALIE 868
Cdd:COG0666 161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 62988328 869 QGARTNEIDNDGRIPFILASQEGHYDCVQILLENKSNIDQRGYDGRNAL 917
Cdd:COG0666 241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
833-1102 |
4.60e-59 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 205.57 E-value: 4.60e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 833 LLDRGLDENHRDDAGWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIPFILASQEGHYDCVQILLENKSNIDQRGYD 912
Cdd:COG0666 7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 913 GRNALRVAALEGHRDIVELLFSHGADVNCKDADGRPTLYILALENQLTMAEYFLENGANVEASDAEGRTALHVSCWQGHM 992
Cdd:COG0666 87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 993 EMVQVLIAYHADVNAADNEKRSALQSAAWQGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQEGHIDVVQVLLEHGADPN 1072
Cdd:COG0666 167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246
|
250 260 270
....*....|....*....|....*....|
gi 62988328 1073 HADQFGRTAMRVAAKNGHSQIIKLLEKYGA 1102
Cdd:COG0666 247 AKDKDGLTALLLAAAAGAALIVKLLLLALL 276
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
531-818 |
5.45e-58 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 202.49 E-value: 5.45e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 531 LLDNGASVNQCDSNGRTLLANAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLIGCGANINHTDQD 610
Cdd:COG0666 7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 611 GWTALRSAAWGGHTEVVSALLYAGVKVDCADADSRTALRAAAWGGHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHR 690
Cdd:COG0666 87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 691 EIVEHLLDHGAEVNHEDVDGRTALSVAalcvpASKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEG 770
Cdd:COG0666 167 EIVKLLLEAGADVNARDNDGETPLHLA-----AENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 62988328 771 GADVDHTDNNGRTPLLAAASMGHASVVNTLLFWGAAVDSIDSEGRTVL 818
Cdd:COG0666 242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
861-1102 |
1.63e-56 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 198.25 E-value: 1.63e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 861 LICEALIEQGARTNEIDNDGRIPFILASQEGHYDCVQILLENKSNIDQRGYDGRNALRVAALEGHRDIVELLFSHGADVN 940
Cdd:COG0666 2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 941 CKDADGRPTLYILALENQLTMAEYFLENGANVEASDAEGRTALHVSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSAA 1020
Cdd:COG0666 82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 1021 WQGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQEGHIDVVQVLLEHGADPNHADQFGRTAMRVAAKNGHSQIIKLLEKY 1100
Cdd:COG0666 162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
|
..
gi 62988328 1101 GA 1102
Cdd:COG0666 242 GA 243
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
728-1016 |
1.13e-54 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 192.86 E-value: 1.13e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 728 ASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLLFWGAAV 807
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 808 DSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIPFILA 887
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 888 SQEGHYDCVQILLENKSNIDQRGYDGRNALRVAALEGHRDIVELLFSHGADVNCKDADGRPTLYILALENQLTMAEYFLE 967
Cdd:COG0666 161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 62988328 968 NGANVEASDAEGRTALHVSCWQGHMEMVQVLIAYHADVNAADNEKRSAL 1016
Cdd:COG0666 241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
495-752 |
2.57e-54 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 191.71 E-value: 2.57e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 495 EVLQLLVKAGAHVNSEDDRTSCIVRQALEREDSIRTLLDNGASVNQCDSNGRTLLANAAYSGSLDVVNLLVSRGADLEIE 574
Cdd:COG0666 37 LLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNAR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 575 DAHGHTPLTLAARQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGHTEVVSALLYAGVKVDCADADSRTALRAAAWG 654
Cdd:COG0666 117 DKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAEN 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 655 GHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLDHGAEVNHEDVDGRTALSVAALcvpasKGHASVVSLL 734
Cdd:COG0666 197 GHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAA-----AGAALIVKLL 271
|
250
....*....|....*...
gi 62988328 735 IDRGAEVDHCDKDGMTPL 752
Cdd:COG0666 272 LLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
707-983 |
7.61e-54 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 190.55 E-value: 7.61e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 707 DVDGRTALSVAALCVPASKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLL 786
Cdd:COG0666 13 AALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 787 AAASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRLICEAL 866
Cdd:COG0666 93 AAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 867 IEQGARTNEIDNDGRIPFILASQEGHYDCVQILLENKSNIDQRGYDGRNALRVAALEGHRDIVELLFSHGADVNCKDADG 946
Cdd:COG0666 173 LEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDG 252
|
250 260 270
....*....|....*....|....*....|....*..
gi 62988328 947 RPTLYILALENQLTMAEYFLENGANVEASDAEGRTAL 983
Cdd:COG0666 253 LTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
804-1082 |
1.60e-53 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 189.39 E-value: 1.60e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 804 GAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIP 883
Cdd:COG0666 11 LLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 884 FILASQEGHYDCVQILLENKSNIDQRGYDGRNALRVAALEGHRDIVELLFSHGADVNCKDADGRPTLYILALENQLTMAE 963
Cdd:COG0666 91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 964 YFLENGANVEASDAEGRTALHVSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSAAWQGHVKVVQLLIEHGAVVDHTCN 1043
Cdd:COG0666 171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250
|
250 260 270
....*....|....*....|....*....|....*....
gi 62988328 1044 QGATALCIAAQEGHIDVVQVLLEHGADPNHADQFGRTAM 1082
Cdd:COG0666 251 DGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
761-1049 |
1.32e-52 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 186.70 E-value: 1.32e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 761 VDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDE 840
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 841 NHRDDAGWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIPFILASQEGHYDCVQILLENKSNIDQRGYDGRNALRVA 920
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 921 ALEGHRDIVELLFSHGADVNCKDADGRPTLYILALENQLTMAEYFLENGANVEASDAEGRTALHVSCWQGHMEMVQVLIA 1000
Cdd:COG0666 161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 62988328 1001 YHADVNAADNEKRSALQSAAWQGHVKVVQLLIEHGAVVDHTCNQGATAL 1049
Cdd:COG0666 241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
443-714 |
8.95e-50 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 178.61 E-value: 8.95e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 443 QAKNLTPLEAQEFALHLINSNLQLETAELALWMIWNGTPVRDSLSTLIPKEQEVLQLLVKAGAHVNSEDDRTSCIVRQAL 522
Cdd:COG0666 16 LLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 523 E--REDSIRTLLDNGASVNQCDSNGRTLLANAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLIGC 600
Cdd:COG0666 96 RngDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 601 GANINHTDQDGWTALRSAAWGGHTEVVSALLYAGVKVDCADADSRTALRAAAWGGHEDIVLNLLQHGAEVNKADNEGRTA 680
Cdd:COG0666 176 GADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTA 255
|
250 260 270
....*....|....*....|....*....|....
gi 62988328 681 LIAAAYMGHREIVEHLLDHGAEVNHEDVDGRTAL 714
Cdd:COG0666 256 LLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
625-907 |
1.27e-36 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 145.55 E-value: 1.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 625 EVVSALLYAGVKVDCADADSRTALRAAAWGGHE---DIVLNLLQHGAEVNKADNEGRTALIAaaYMGH---REIVEHLLD 698
Cdd:PHA03095 28 EEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEkvkDIVRLLLEAGADVNAPERCGFTPLHL--YLYNattLDVIKLLIK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 699 HGAEVNHEDVDGRTALSVAaLCVPASkgHASVVSLLIDRGAEVDHCDKDGMTPL--LVAAYEGHVDVVDLLLEGGADVDH 776
Cdd:PHA03095 106 AGADVNAKDKVGRTPLHVY-LSGFNI--NPKVIRLLLRKGADVNALDLYGMTPLavLLKSRNANVELLRLLIDAGADVYA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 777 TDNNGRTPL--LAAASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVE--VVRTLLDRGLDENHRDDAGWTPLH 852
Cdd:PHA03095 183 VDDRFRSLLhhHLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLH 262
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 62988328 853 MAAFEGHRLICEALIEQGARTNEIDNDGRIPFILASQEGHYDCVQILLENKSNID 907
Cdd:PHA03095 263 YAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAE 317
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
524-836 |
2.68e-32 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 132.46 E-value: 2.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 524 REDSIRTLLDNGASVNQCDSNGRTLLA---NAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHT-KVVNCLIG 599
Cdd:PHA03095 26 TVEEVRRLLAAGADVNFRGEYGKTPLHlylHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 600 CGANINHTDQDGWTALrsaawggHTevvsallYAGVKvdcadadsRTalraaawggHEDIVLNLLQHGAEVNKADNEGRT 679
Cdd:PHA03095 106 AGADVNAKDKVGRTPL-------HV-------YLSGF--------NI---------NPKVIRLLLRKGADVNALDLYGMT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 680 ALiaAAYMGHR----EIVEHLLDHGAEVNHEDVDGRTALSVAALCVpasKGHASVVSLLIDRGAEVDHCDKDGMTPLLVA 755
Cdd:PHA03095 155 PL--AVLLKSRnanvELLRLLIDAGADVYAVDDRFRSLLHHHLQSF---KPRARIVRELIRAGCDPAATDMLGNTPLHSM 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 756 AYEGHVD--VVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRTL 833
Cdd:PHA03095 230 ATGSSCKrsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAA 309
|
...
gi 62988328 834 LDR 836
Cdd:PHA03095 310 LAK 312
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
558-900 |
1.16e-31 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 133.65 E-value: 1.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 558 LDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGHTEVVSALLYAGVKV 637
Cdd:PHA02876 158 LLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNI 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 638 DCADADSRTALRaaawggHEDIVLNLLQH--GAEVNKADNEGRTALIAAAYMGH-REIVEHLLDHGAEVNHEDVDGRTAL 714
Cdd:PHA02876 238 NKNDLSLLKAIR------NEDLETSLLLYdaGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 715 SVAalcvpASKGHASV-VSLLIDRGAEVDHCDKDGMTPLLVAA-YEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMG 792
Cdd:PHA02876 312 YLM-----AKNGYDTEnIRTLIMLGADVNAADRLYITPLHQAStLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRN 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 793 HASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEV-VRTLLDRGLDENHRDDAGWTPLHMAAFEGHRL-ICEALIEQG 870
Cdd:PHA02876 387 NVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVNSKNKDLSTPLHYACKKNCKLdVIEMLLDNG 466
|
330 340 350
....*....|....*....|....*....|
gi 62988328 871 ARTNEIDNDGRIPFILASqeGHYDCVQILL 900
Cdd:PHA02876 467 ADVNAINIQNQYPLLIAL--EYHGIVNILL 494
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
686-1014 |
1.35e-29 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 123.92 E-value: 1.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 686 YMGHREIVEHLLDHGAEVNHEDVDGRTALSVAALcvpaSKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVD 765
Cdd:PHA02874 10 YSGDIEAIEKIIKNKGNCINISVDETTTPLIDAI----RSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 766 LLLEGGADvdhtdnngrTPLLAAASMgHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDENHRDD 845
Cdd:PHA02874 86 LLIDNGVD---------TSILPIPCI-EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 846 AGWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIPFILASQEGHYDCVQILLENKSNIDQRGYDGRNALRVAALEgH 925
Cdd:PHA02874 156 NGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIH-N 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 926 RDIVELLFSHgADVNCKDADG-RPTLYILALENQLTMAEYFLENGANVEASDAEGRTALHVSC-WQGHMEMVQVLIAYHA 1003
Cdd:PHA02874 235 RSAIELLINN-ASINDQDIDGsTPLHHAINPPCDIDIIDILLYHKADISIKDNKGENPIDTAFkYINKDPVIKDIIANAV 313
|
330
....*....|.
gi 62988328 1004 DVNAADNEKRS 1014
Cdd:PHA02874 314 LIKEADKLKDS 324
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
763-1102 |
1.07e-27 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 120.94 E-value: 1.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 763 VVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDENH 842
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINK 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 843 RDDAGWTPLHMAAFEGHRLiceaLIEQGARTNEIDNDGRIPFILASQEGHYD-CVQILLENKSNIDQRGYDGRNALRVAA 921
Cdd:PHA02876 240 NDLSLLKAIRNEDLETSLL----LYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMA 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 922 LEGH-RDIVELLFSHGADVNCKDadgrpTLYILALENQLTMAEY------FLENGANVEASDAEGRTALHVSCWQGHMEM 994
Cdd:PHA02876 316 KNGYdTENIRTLIMLGADVNAAD-----RLYITPLHQASTLDRNkdivitLLELGANVNARDYCDKTPIHYAAVRNNVVI 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 995 VQVLIAYHADVNAADNEKRSALQSAAWQGHVKV-VQLLIEHGAVVDHTCNQGATALCIAAQEG-HIDVVQVLLEHGADPN 1072
Cdd:PHA02876 391 INTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVN 470
|
330 340 350
....*....|....*....|....*....|
gi 62988328 1073 HADQFGRTAMRVAAknGHSQIIKLLEKYGA 1102
Cdd:PHA02876 471 AINIQNQYPLLIAL--EYHGIVNILLHYGA 498
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
480-717 |
1.50e-27 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 118.20 E-value: 1.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 480 TPVRDSLSTLIPKEQEVLQLLVKAGAHVNSeddRTSC-------IVRQAlEREDSIRTLLDNGASVNQCDSNGRTLLAna 552
Cdd:PHA03095 49 TPLHLYLHYSSEKVKDIVRLLLEAGADVNA---PERCgftplhlYLYNA-TTLDVIKLLIKAGADVNAKDKVGRTPLH-- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 553 AYSGSL----DVVNLLVSRGADLEIEDAHGHTPLT--LAARQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGHT-- 624
Cdd:PHA03095 123 VYLSGFninpKVIRLLLRKGADVNALDLYGMTPLAvlLKSRNANVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPra 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 625 EVVSALLYAGVKVDCADADSRTALRAAAWGGHED--IVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLDHGAE 702
Cdd:PHA03095 203 RIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGAD 282
|
250
....*....|....*
gi 62988328 703 VNHEDVDGRTALSVA 717
Cdd:PHA03095 283 INAVSSDGNTPLSLM 297
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
557-851 |
3.22e-27 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 117.05 E-value: 3.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 557 SLDVVNLLVSRGADLEIEDAHGHTPLTLAARQGH---TKVVNCLIGCGANINHTDQDGWTALRSAAWGGHTE-VVSALLY 632
Cdd:PHA03095 26 TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 633 AGVKVDCADADSRTALRAAAWGG--HEDIVLNLLQHGAEVNKADNEGRTALiaAAYMGHR----EIVEHLLDHGAEVNHE 706
Cdd:PHA03095 106 AGADVNAKDKVGRTPLHVYLSGFniNPKVIRLLLRKGADVNALDLYGMTPL--AVLLKSRnanvELLRLLIDAGADVYAV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 707 DVDGRTALSVAALCVpasKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVD--VVDLLLEGGADVDHTDNNGRTP 784
Cdd:PHA03095 184 DDRFRSLLHHHLQSF---KPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTP 260
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62988328 785 LLAAAsmghasvvntllfwgaavdsidsegrtvlsiasAQGNVEVVRTLLDRGLDENHRDDAGWTPL 851
Cdd:PHA03095 261 LHYAA---------------------------------VFNNPRACRRLIALGADINAVSSDGNTPL 294
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
862-1103 |
7.06e-26 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 112.45 E-value: 7.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 862 ICEALIEQGARTNEIDNDGRIPFILASQEGHydcvqillenksnidqrgydgrNALRVaaleghRDIVELLFSHGADVNC 941
Cdd:PHA03100 50 VVKILLDNGADINSSTKNNSTPLHYLSNIKY----------------------NLTDV------KEIVKLLLEYGANVNA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 942 KDADGRPTLYILALE--NQLTMAEYFLENGANVEASDAEGRTALH--VSCWQGHMEMVQVLIAYHADVNAADNekrsalq 1017
Cdd:PHA03100 102 PDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHlyLESNKIDLKILKLLIDKGVDINAKNR------- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 1018 saawqghvkvVQLLIEHGAVVDHTCNQGATALCIAAQEGHIDVVQVLLEHGADPNHADQFGRTAMRVAAKNGHSQIIKLL 1097
Cdd:PHA03100 175 ----------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLL 244
|
....*.
gi 62988328 1098 EKYGAS 1103
Cdd:PHA03100 245 LNNGPS 250
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
658-983 |
1.04e-24 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 109.73 E-value: 1.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 658 DIVLNLLQHGAEVNKADNEGRTALiaAAYMGHR-----EIVEHLLDHGAEVNHEDVDGRTALSvaalCVPASKGHASVVS 732
Cdd:PHA03095 28 EEVRRLLAAGADVNFRGEYGKTPL--HLYLHYSsekvkDIVRLLLEAGADVNAPERCGFTPLH----LYLYNATTLDVIK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 733 LLIDRGAEVDHCDKDGMTPLLV--AAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASV--VNTLLFWGAAVD 808
Cdd:PHA03095 102 LLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVY 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 809 SIDSEGRTVLSI--ASAQGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHrliCEALIEQgartneidndgriPFIL 886
Cdd:PHA03095 182 AVDDRFRSLLHHhlQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSS---CKRSLVL-------------PLLI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 887 AsqeghydcvqillenksnidqrgydgrnalrvaaleghrdivellfshGADVNCKDADGRPTLYILALENQLTMAEYFL 966
Cdd:PHA03095 246 A------------------------------------------------GISINARNRYGQTPLHYAAVFNNPRACRRLI 277
|
330
....*....|....*..
gi 62988328 967 ENGANVEASDAEGRTAL 983
Cdd:PHA03095 278 ALGADINAVSSDGNTPL 294
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
820-1095 |
1.93e-24 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 108.57 E-value: 1.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 820 IASAQGNVEVVRTLLDRGLDENHRDDAGWTPLH--MAAFEGHRL-ICEALIEQGARTNEIDNDGRIPFIL----ASQEgh 892
Cdd:PHA03095 20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHlyLHYSSEKVKdIVRLLLEAGADVNAPERCGFTPLHLylynATTL-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 893 yDCVQILLENKSNIDQRGYDGRNALRV--AALEGHRDIVELLFSHGADVNCKDADGRPTLYILALENQLTMA--EYFLEN 968
Cdd:PHA03095 98 -DVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVEllRLLIDA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 969 GANVEASDAEGRTALHVscwqgHME-------MVQVLIAYHADVNAADNEKRSALQSAAWQGHVK--VVQLLIEHGAVVD 1039
Cdd:PHA03095 177 GADVYAVDDRFRSLLHH-----HLQsfkprarIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISIN 251
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 62988328 1040 HTCNQGATALCIAAQEGHIDVVQVLLEHGADPNHADQFGRTAMRVAAKNGHSQIIK 1095
Cdd:PHA03095 252 ARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVR 307
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
625-842 |
2.66e-24 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 107.44 E-value: 2.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 625 EVVSALLYAGVKVDCADADSRTALRAAAWGGHE-----DIVLNLLQHGAEVNKADNEGRTALIAAAY--MGHREIVEHLL 697
Cdd:PHA03100 49 DVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISkkSNSYSIVEYLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 698 DHGAEVNHEDVDGRTALSVAALCVPASKghaSVVSLLIDRGAEVDHCDKdgmtpllvaayeghvdvVDLLLEGGADVDHT 777
Cdd:PHA03100 129 DNGANVNIKNSDGENLLHLYLESNKIDL---KILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIK 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62988328 778 DNNGRTPLLAAASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDENH 842
Cdd:PHA03100 189 DVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
606-797 |
1.74e-23 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 108.03 E-value: 1.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 606 HTDQDGWTALRSAAWGGHTEVVSALLYAGVKVDCADADSRTALRAAAWGGHEDIVLNLLQHGAEVNKADNEGRTALIAAA 685
Cdd:PLN03192 520 HDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAI 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 686 YMGHREIVeHLLDHGAEVNHEDVDGRTalsvaaLCVPASKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVD 765
Cdd:PLN03192 600 SAKHHKIF-RILYHFASISDPHAAGDL------LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVR 672
|
170 180 190
....*....|....*....|....*....|....*...
gi 62988328 766 LLLEGGADVDHTD-NNGRTP-----LLAAASMGHASVV 797
Cdd:PLN03192 673 LLIMNGADVDKANtDDDFSPtelreLLQKRELGHSITI 710
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
492-788 |
5.96e-22 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 100.81 E-value: 5.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 492 KEQEVLQLLVKA-GAHVNSEDDRTSCIVRQALEREDS--IRTLLDNGASVNQCDSNGRTLLANAAYSGSLDVVNLLVSRG 568
Cdd:PHA02874 12 GDIEAIEKIIKNkGNCINISVDETTTPLIDAIRSGDAkiVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 569 ADLEIedahghtpltLAARQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGHTEVVSALLYAGVKVDCADADSRTAL 648
Cdd:PHA02874 92 VDTSI----------LPIPCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 649 RAAAWGGHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLDHGAEVNHEDVDGRTALSVAALcvpaskGHA 728
Cdd:PHA02874 162 HIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII------HNR 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62988328 729 SVVSLLIDrGAEVDHCDKDGMTPLLVA-AYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAA 788
Cdd:PHA02874 236 SAIELLIN-NASINDQDIDGSTPLHHAiNPPCDIDIIDILLYHKADISIKDNKGENPIDTA 295
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
983-1075 |
9.49e-22 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 90.95 E-value: 9.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 983 LHVSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSAAWQGHVKVVQLLIEHGAVVDhtCNQGATALCIAAQEGHIDVVQ 1062
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 62988328 1063 VLLEHGADPNHAD 1075
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
826-1044 |
1.75e-21 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 98.97 E-value: 1.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 826 NVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRL-----ICEALIEQGARTNEIDNDGRIP-FILASQE-GHYDCVQI 898
Cdd:PHA03100 47 NIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLtdvkeIVKLLLEYGANVNAPDNNGITPlLYAISKKsNSYSIVEY 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 899 LLENKSNIDQRGYDGRNALRVAALEGHRD--IVELLFSHGADVNCKDAdgrptlyilalenqltmAEYFLENGANVEASD 976
Cdd:PHA03100 127 LLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKD 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62988328 977 AEGRTALHVSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSAAWQGHVKVVQLLIEHGAVVDHTCNQ 1044
Cdd:PHA03100 190 VYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
851-943 |
3.23e-21 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 89.40 E-value: 3.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 851 LHMAAFEGHRLICEALIEQGARTNEIDNDGRIPFILASQEGHYDCVQILLENKsNIDQRGYdGRNALRVAALEGHRDIVE 930
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKDN-GRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 62988328 931 LLFSHGADVNCKD 943
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
718-940 |
2.08e-20 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 95.44 E-value: 2.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 718 ALCVPASKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVV 797
Cdd:PHA02875 5 ALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 798 NTLLFWGA-AVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRLICEALIEQGARTNEI 876
Cdd:PHA02875 85 EELLDLGKfADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62988328 877 DNDGRIPFILASQEGHYDCVQILLENKSNIDQRGYDGRNALRVAALEGHR-DIVELLFSHGADVN 940
Cdd:PHA02875 165 DCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKiDIVRLFIKRGADCN 229
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
761-945 |
9.13e-20 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 96.09 E-value: 9.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 761 VDVVDLLLEGGADvdHTDNNGRTPLLAAASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDE 840
Cdd:PLN03192 507 LNVGDLLGDNGGE--HDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNV 584
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 841 NHRDDAGWTPLHMAAFEGHRLICEALiEQGARTNEIDNDGRIpFILASQEGHYDCVQILLENKSNIDQRGYDGRNALRVA 920
Cdd:PLN03192 585 HIRDANGNTALWNAISAKHHKIFRIL-YHFASISDPHAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVA 662
|
170 180
....*....|....*....|....*
gi 62988328 921 ALEGHRDIVELLFSHGADVNCKDAD 945
Cdd:PLN03192 663 MAEDHVDMVRLLIMNGADVDKANTD 687
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
752-844 |
5.04e-19 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 83.24 E-value: 5.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 752 LLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLLfwgAAVDS-IDSEGRTVLSIASAQGNVEVV 830
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL---EHADVnLKDNGRTALHYAARSGHLEIV 77
|
90
....*....|....
gi 62988328 831 RTLLDRGLDENHRD 844
Cdd:pfam12796 78 KLLLEKGADINVKD 91
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
891-1104 |
5.16e-19 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 91.21 E-value: 5.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 891 GHYDCVQILLENKSNIDQRGYDGRNALRVAALEGHRDIVELLFSHGADVNCKDADGRPTLYILALENQLTMAEYFLEngA 970
Cdd:PHA02875 13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLD--L 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 971 NVEASDA---EGRTALHVSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSAAWQGHVKVVQLLIEHGAVVDHTCNQGAT 1047
Cdd:PHA02875 91 GKFADDVfykDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCT 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62988328 1048 ALCIAAQEGHIDVVQVLLEHGADPNHadqFGR----TAMRVAAKNGHSQIIKLLEKYGASS 1104
Cdd:PHA02875 171 PLIIAMAKGDIAICKMLLDSGANIDY---FGKngcvAALCYAIENNKIDIVRLFIKRGADC 228
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
618-707 |
5.78e-19 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 82.86 E-value: 5.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 618 AAWGGHTEVVSALLYAGVKVDCADADSRTALRAAAWGGHEDIVLNLLQHgAEVNKADNeGRTALIAAAYMGHREIVEHLL 697
Cdd:pfam12796 4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLL 81
|
90
....*....|
gi 62988328 698 DHGAEVNHED 707
Cdd:pfam12796 82 EKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
818-909 |
6.37e-19 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 82.86 E-value: 6.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 818 LSIASAQGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRLICEALIEQGARtnEIDNDGRIPFILASQEGHYDCVQ 897
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78
|
90
....*....|..
gi 62988328 898 ILLENKSNIDQR 909
Cdd:pfam12796 79 LLLEKGADINVK 90
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
582-674 |
7.44e-19 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 82.86 E-value: 7.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 582 LTLAARQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGHTEVVSALLyAGVKVDCADaDSRTALRAAAWGGHEDIVL 661
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 62988328 662 NLLQHGAEVNKAD 674
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
824-1121 |
1.12e-18 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 92.05 E-value: 1.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 824 QGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIPFILASQEGHYDCVQILLENK 903
Cdd:PHA02876 155 QDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNR 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 904 SNIDQRGYDGRNALRVAALEGH------------------------------RDIVELLFSHGADVNCKDADGRPTLYIL 953
Cdd:PHA02876 235 SNINKNDLSLLKAIRNEDLETSlllydagfsvnsiddckntplhhasqapslSRLVPKLLERGADVNAKNIKGETPLYLM 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 954 A-----LENQLTMaeyfLENGANVEASDAEGRTALH-VSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSAAWQGHVKV 1027
Cdd:PHA02876 315 AkngydTENIRTL----IMLGADVNAADRLYITPLHqASTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVI 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 1028 VQLLIEHGAVVDHTCNQGATALCIA-AQEGHIDVVQVLLEHGADPNHADQFGRTAMRVAAKNG-HSQIIKLLEKygassl 1105
Cdd:PHA02876 391 INTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLD------ 464
|
330
....*....|....*.
gi 62988328 1106 NGCSPSPVHTMEQKPL 1121
Cdd:PHA02876 465 NGADVNAINIQNQYPL 480
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
524-746 |
1.19e-18 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 90.49 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 524 REDSIRTLLDNGASVNQCDSNGRTLL---ANAAYSGS--LDVVNLLVSRGADLEIEDAHGHTPLTLAA--RQGHTKVVNC 596
Cdd:PHA03100 47 NIDVVKILLDNGADINSSTKNNSTPLhylSNIKYNLTdvKEIVKLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEY 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 597 LIGCGANINHTDQDGWTALRSAAWGGH--TEVVSALLYAGVKVDCADAdsrtalraaawgghediVLNLLQHGAEVNKAD 674
Cdd:PHA03100 127 LLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKD 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62988328 675 NEGRTALIAAAYMGHREIVEHLLDHGAEVNHEDVDGRTALSVAALcvpasKGHASVVSLLIDRGAEVDHCDK 746
Cdd:PHA03100 190 VYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAIL-----NNNKEIFKLLLNNGPSIKTIIE 256
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
724-1087 |
1.33e-18 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 90.41 E-value: 1.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 724 SKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLLFW 803
Cdd:PHA02874 11 SGDIEAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 804 GaaVDSidsegrTVLSIASAqgNVEVVRTLLDRGLDENHRDDAGWTPLHMAafeghrlicealieqgartneIDNdgrip 883
Cdd:PHA02874 91 G--VDT------SILPIPCI--EKDMIKTILDCGIDVNIKDAELKTFLHYA---------------------IKK----- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 884 filasqeghydcvqillenksnidqrgydgrnalrvaaleGHRDIVELLFSHGADVNCKDADGRPTLYILALENQLTMAE 963
Cdd:PHA02874 135 ----------------------------------------GDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIK 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 964 YFLENGANVEASDAEGRTALHVSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSAAWQGHvKVVQLLIEHGAVVDHTCN 1043
Cdd:PHA02874 175 LLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLINNASINDQDID 253
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 62988328 1044 qGATALCIAAQ-EGHIDVVQVLLEHGADPNHADQFGRTAMRVAAK 1087
Cdd:PHA02874 254 -GSTPLHHAINpPCDIDIIDILLYHKADISIKDNKGENPIDTAFK 297
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
959-1102 |
1.49e-18 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 87.70 E-value: 1.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 959 LTMAEYFLENGANVEASDAEGRTALHVSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSAAWQGHVKVVQLLIEHGAVV 1038
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62988328 1039 DHTCNQGATALCIAAQEGHIDVVQVLLEHGADPNHADQFGRTAMRVAAKNGHSQIIKLLEKYGA 1102
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGA 144
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
723-811 |
3.60e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 80.55 E-value: 3.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 723 ASKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEgGADVDHTDnNGRTPLLAAASMGHASVVNTLLF 802
Cdd:pfam12796 5 AKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVKLLLE 82
|
....*....
gi 62988328 803 WGAAVDSID 811
Cdd:pfam12796 83 KGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
648-742 |
4.59e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 80.55 E-value: 4.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 648 LRAAAWGGHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLDHgAEVNHEDvDGRTALSVAalcvpASKGH 727
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYA-----ARSGH 73
|
90
....*....|....*
gi 62988328 728 ASVVSLLIDRGAEVD 742
Cdd:pfam12796 74 LEIVKLLLEKGADIN 88
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
549-641 |
8.40e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 79.77 E-value: 8.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 549 LANAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLIGCgANINHTDqDGWTALRSAAWGGHTEVVS 628
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 62988328 629 ALLYAGVKVDCAD 641
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
950-1041 |
9.91e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 79.39 E-value: 9.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 950 LYILALENQLTMAEYFLENGANVEASDAEGRTALHVSCWQGHMEMVQVLIAyHADVNAADNeKRSALQSAAWQGHVKVVQ 1029
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVK 78
|
90
....*....|..
gi 62988328 1030 LLIEHGAVVDHT 1041
Cdd:pfam12796 79 LLLEKGADINVK 90
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
917-1009 |
1.31e-17 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 79.00 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 917 LRVAALEGHRDIVELLFSHGADVNCKDADGRPTLYILALENQLTMAEYFLENgANVEASDaEGRTALHVSCWQGHMEMVQ 996
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 62988328 997 VLIAYHADVNAAD 1009
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
896-1114 |
1.34e-17 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 87.77 E-value: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 896 VQILLENKSNIDQRGYDGRNALRV---AALEGHRDIVELLFSHGADVNCKDADG-RPTLYILALENQLTMAEYFLENGAN 971
Cdd:PHA03095 30 VRRLLAAGADVNFRGEYGKTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGfTPLHLYLYNATTLDVIKLLIKAGAD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 972 VEASDAEGRTALHVsCWQG---HMEMVQVLIAYHADVNAADNEKRSALQ-----SAAwqgHVKVVQLLIEHGAVVDHTCN 1043
Cdd:PHA03095 110 VNAKDKVGRTPLHV-YLSGfniNPKVIRLLLRKGADVNALDLYGMTPLAvllksRNA---NVELLRLLIDAGADVYAVDD 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62988328 1044 QGATALCIAAQEGHID--VVQVLLEHGADPNHADQFGRTAMRVAAKNG---HSQIIKLLEKyGAS--SLNGCSPSPVH 1114
Cdd:PHA03095 186 RFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATGSsckRSLVLPLLIA-GISinARNRYGQTPLH 262
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
1016-1103 |
1.42e-17 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 79.00 E-value: 1.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 1016 LQSAAWQGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQEGHIDVVQVLLEHgADPNHADQfGRTAMRVAAKNGHSQIIK 1095
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
|
....*...
gi 62988328 1096 LLEKYGAS 1103
Cdd:pfam12796 79 LLLEKGAD 86
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
826-1087 |
2.87e-17 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 86.47 E-value: 2.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 826 NVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIpfilaSQEGHYDCVQI---LLEN 902
Cdd:PHA02878 49 NLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFYTLVAI-----KDAFNNRNVEIfkiILTN 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 903 KSN---------IDQRGYDGrnalrvaALEGhrDIVELLFSHGADVNCKDADGRPTLYILALENQLT-MAEYFLENGANV 972
Cdd:PHA02878 124 RYKniqtidlvyIDKKSKDD-------IIEA--EITKLLLSYGADINMKDRHKGNTALHYATENKDQrLTELLLSYGANV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 973 EASDAEGRTALHVSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSAAwqGHVK---VVQLLIEHGAVVD-HTCNQGATA 1048
Cdd:PHA02878 195 NIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISV--GYCKdydILKLLLEHGVDVNaKSYILGLTA 272
|
250 260 270
....*....|....*....|....*....|....*....
gi 62988328 1049 LCIAAQEGhiDVVQVLLEHGADPNHADQFGRTAMRVAAK 1087
Cdd:PHA02878 273 LHSSIKSE--RKLKLLLEYGADINSLNSYKLTPLSSAVK 309
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
963-1119 |
5.75e-17 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 86.85 E-value: 5.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 963 EYFLENGANVEASDAEGRTALHVSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSAAWQGHVKVVQLLIEHGAVVD-HT 1041
Cdd:PLN03192 542 EELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDpHA 621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 1042 cnqGATALCIAAQEGHIDVVQVLLEHGADPNHADQFGRTAMRVAAKNGHSQIIKLLEKYGAS-----SLNGCSPSPVHTM 1116
Cdd:PLN03192 622 ---AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADvdkanTDDDFSPTELREL 698
|
...
gi 62988328 1117 EQK 1119
Cdd:PLN03192 699 LQK 701
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
659-925 |
1.24e-16 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 85.69 E-value: 1.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 659 IVLNLLQHGAEVNKADnegrtaliaaaymghreiVEHLLdhgAEVNHEDVDGRTALSVAALcvpASKGHASVVSLLIDRG 738
Cdd:PLN03192 493 ILKNFLQHHKELHDLN------------------VGDLL---GDNGGEHDDPNMASNLLTV---ASTGNAALLEELLKAK 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 739 AEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLLFWGAAVDSidSEGRTVL 818
Cdd:PLN03192 549 LDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDP--HAAGDLL 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 819 SIASAQGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRLICEALIEQGARTNEIDND------------------G 880
Cdd:PLN03192 627 CTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDddfsptelrellqkrelgH 706
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 62988328 881 RIPFILASQEGHYDCVQILLENKSNIDQRGYDGRNALRVAALEGH 925
Cdd:PLN03192 707 SITIVDSVPADEPDLGRDGGSRPGRLQGTSSDNQCRPRVSIYKGH 751
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
544-773 |
1.39e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 83.89 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 544 NGRTLLANAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGH 623
Cdd:PHA02875 1 MDQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 624 TEVVSALLYAGVKV-DCADADSRTALRAAAWGGHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLDHGAE 702
Cdd:PHA02875 81 VKAVEELLDLGKFAdDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKAC 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62988328 703 VNHEDVDGRTALSVAalcvpASKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGH-VDVVDLLLEGGAD 773
Cdd:PHA02875 161 LDIEDCCGCTPLIIA-----MAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNkIDIVRLFIKRGAD 227
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
645-874 |
7.78e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 81.58 E-value: 7.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 645 RTALRAAAWGGHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLDHGAEVNHEDVDGRTALSVAALcvpas 724
Cdd:PHA02875 3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVE----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 725 KGHASVVSLLIDRGAEVDHC-DKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLLFW 803
Cdd:PHA02875 78 EGDVKAVEELLDLGKFADDVfYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDH 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62988328 804 GAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRL-ICEALIEQGARTN 874
Cdd:PHA02875 158 KACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIdIVRLFIKRGADCN 229
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
730-1010 |
1.36e-15 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 81.42 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 730 VVSLLIDRGAEVDHCDKDGMTPLL-----VAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLLFW- 803
Cdd:PHA02798 53 IVKLFINLGANVNGLDNEYSTPLCtilsnIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLFMi 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 804 --GAAVDSIDSEGRTVLSIASAQGN---VEVVRTLLDRGLDEN-HRDDAGWTPLH-MAAFEGHRL---ICEALIEQGART 873
Cdd:PHA02798 133 enGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINtHNNKEKYDTLHcYFKYNIDRIdadILKLFVDNGFII 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 874 NEIDNDGRIPFIlasqeghyDCVQILLENKSNIDqrgydgrnalrvaaleghRDIVELLFSHgADVNCKDADGRPTLYIL 953
Cdd:PHA02798 213 NKENKSHKKKFM--------EYLNSLLYDNKRFK------------------KNILDFIFSY-IDINQVDELGFNPLYYS 265
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 62988328 954 ALENQLTMAEYFLENGANVEASDAEGRTALHVSCWQGHMEMVQVLIAYHADVNAADN 1010
Cdd:PHA02798 266 VSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKPNKNTISY 322
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
549-824 |
5.29e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 79.54 E-value: 5.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 549 LANAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLAA----RQGHTKVVNCLIGCgaNINHTDQdgwtALRSAAWGGHT 624
Cdd:PHA02878 41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICkepnKLGMKEMIRSINKC--SVFYTLV----AIKDAFNNRNV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 625 EVVSALLYAGVKVDCADADSRTALRAAAWGGHEDIVLNLLQHGAEVNKAD-NEGRTALIAAAYMGHREIVEHLLDHGAEV 703
Cdd:PHA02878 115 EIFKIILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 704 NHEDVDGRTALSVAAlcvpaSKGHASVVSLLIDRGAEVDHCDKDGMTPLLVA-AYEGHVDVVDLLLEGGADVDHTDN-NG 781
Cdd:PHA02878 195 NIPDKTNNSPLHHAV-----KHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYiLG 269
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 62988328 782 RTPLlaAASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQ 824
Cdd:PHA02878 270 LTAL--HSSIKSERKLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
526-608 |
1.51e-14 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 70.53 E-value: 1.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 526 DSIRTLLDNGASVNQCDSNGRTLLANAAYSGSLDVVNLLVSRgADLEIEDaHGHTPLTLAARQGHTKVVNCLIGCGANIN 605
Cdd:pfam12796 11 ELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADIN 88
|
...
gi 62988328 606 HTD 608
Cdd:pfam12796 89 VKD 91
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
815-1072 |
2.40e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 76.95 E-value: 2.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 815 RTVLSIASAQGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIPFILASQEGHYD 894
Cdd:PHA02875 3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 895 CVQILLENKSNIDQRGY-DGRNALRVAALEGHRDIVELLFSHGADVNCKDADGRptlyilalenqltmaeyflenganve 973
Cdd:PHA02875 83 AVEELLDLGKFADDVFYkDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKF-------------------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 974 asdaegrTALHVSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSAAWQGHVKVVQLLIEHGAVVDHTCNQG-ATALCIA 1052
Cdd:PHA02875 137 -------SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYA 209
|
250 260
....*....|....*....|
gi 62988328 1053 AQEGHIDVVQVLLEHGADPN 1072
Cdd:PHA02875 210 IENNKIDIVRLFIKRGADCN 229
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
915-1094 |
3.86e-14 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 77.60 E-value: 3.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 915 NALRVAALeGHRDIVELLFSHGADVNCKDADGRPTLYILALENQLTMAEYFLENGANVEASDAEGRTALHVSCWQGHMEM 994
Cdd:PLN03192 528 NLLTVAST-GNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKI 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 995 VQVLiaYHADVNAADNEKRSALQSAAWQGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQEGHIDVVQVLLEHGADPNHA 1074
Cdd:PLN03192 607 FRIL--YHFASISDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKA 684
|
170 180
....*....|....*....|....*.
gi 62988328 1075 ---DQFGRTAMRVAAKN---GHSQII 1094
Cdd:PLN03192 685 ntdDDFSPTELRELLQKrelGHSITI 710
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
495-634 |
5.83e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 75.86 E-value: 5.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 495 EVLQLLVKAGAHVNSEDDRTSCIVRQALERE----DSIRTLLDNGASVNQCDSNGRTLLANAAYSGS--LDVVNLLVSRG 568
Cdd:PHA03100 87 EIVKLLLEYGANVNAPDNNGITPLLYAISKKsnsySIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 569 ADLEIE----------------DAHGHTPLTLAARQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGHTEVVSALLY 632
Cdd:PHA03100 167 VDINAKnrvnyllsygvpinikDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLN 246
|
..
gi 62988328 633 AG 634
Cdd:PHA03100 247 NG 248
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
851-1115 |
1.09e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 75.00 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 851 LHMAAFEGHRLICEALIEQgaRTNEID---NDGRIPFILASQEGHYDCVQILLENKSNIDQRGYDGRNALRVAALEGHRD 927
Cdd:PHA02874 5 LRMCIYSGDIEAIEKIIKN--KGNCINisvDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 928 IVELLFSHGADVNckdadgrpTLYILALENQltMAEYFLENGANVEASDAEGRTALHVSCWQGHMEMVQVLIAYHADVNA 1007
Cdd:PHA02874 83 IIKLLIDNGVDTS--------ILPIPCIEKD--MIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 1008 ADNekrsalqsaawqghvkvvqlliehgavvdhtcnQGATALCIAAQEGHIDVVQVLLEHGADPNHADQFGRTAMRVAAK 1087
Cdd:PHA02874 153 EDD---------------------------------NGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAE 199
|
250 260 270
....*....|....*....|....*....|
gi 62988328 1088 NGHSQIIKLLEKYGASSLNGCSP--SPVHT 1115
Cdd:PHA02874 200 YGDYACIKLLIDHGNHIMNKCKNgfTPLHN 229
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
495-609 |
1.70e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 74.32 E-value: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 495 EVLQLLVKAGAHVNSEDdrtscivrqaleredSIRTLLDNGASVNQCDSNGRTLLANAAYSGSLDVVNLLVSRGADLEIE 574
Cdd:PHA03100 157 KILKLLIDKGVDINAKN---------------RVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLV 221
|
90 100 110
....*....|....*....|....*....|....*
gi 62988328 575 DAHGHTPLTLAARQGHTKVVNCLIGCGANINHTDQ 609
Cdd:PHA03100 222 NKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
751-1034 |
5.68e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 72.99 E-value: 5.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 751 PLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAA-------------ASMGHASVVNTLLFWGAAVDSIDSEGRTV 817
Cdd:PHA02878 40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIIckepnklgmkemiRSINKCSVFYTLVAIKDAFNNRNVEIFKI 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 818 LSIASAQGN------------------VEVVRTLLDRGLDENHRD-DAGWTPLHMAAFEGHRLICEALIEQGARTNEIDN 878
Cdd:PHA02878 120 ILTNRYKNIqtidlvyidkkskddiieAEITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDK 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 879 DGRIPFILASQEGHYDCVQILLENKSNIDQRGYDGRNALRVAALE-GHRDIVELLFSHGADVNCKDadgrptlYILALen 957
Cdd:PHA02878 200 TNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKS-------YILGL-- 270
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62988328 958 qltmaeyflenganveasdaegrTALHVSCwqgHMEMV-QVLIAYHADVNAADNEKRSALQSAAWQGH-VKVVQLLIEH 1034
Cdd:PHA02878 271 -----------------------TALHSSI---KSERKlKLLLEYGADINSLNSYKLTPLSSAVKQYLcINIGRILISN 323
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
526-740 |
1.26e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 71.56 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 526 DSIRTLLDNGASVNQCDSNGRTLLANAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLIGCGANIN 605
Cdd:PHA02875 16 DIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 606 HT-DQDGWTALRSAAWGGHTEVVSALLYAGVKVDCADADSRTALRAAAWGGHEDIVLNLLQHGAEVNKADNEGRTALIAA 684
Cdd:PHA02875 96 DVfYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 62988328 685 AYMGHREIVEHLLDHGAEVNHEDVDGrtalSVAALCVPASKGHASVVSLLIDRGAE 740
Cdd:PHA02875 176 MAKGDIAICKMLLDSGANIDYFGKNG----CVAALCYAIENNKIDIVRLFIKRGAD 227
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
748-801 |
3.45e-12 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 62.29 E-value: 3.45e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 62988328 748 GMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLL 801
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
495-631 |
3.57e-12 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 70.44 E-value: 3.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 495 EVLQLLVKAGAHVNSEDDRTSCIVRQALE----REDSIRTLLDNGASVNQCDSNGRTLLANAAYSGS---LDVVNLLVsR 567
Cdd:PHA03095 168 ELLRLLIDAGADVYAVDDRFRSLLHHHLQsfkpRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSckrSLVLPLLI-A 246
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62988328 568 GADLEIEDAHGHTPLTLAARQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGHTEVVSALL 631
Cdd:PHA03095 247 GISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
864-1093 |
4.80e-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: 4.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 864 EALIEQGARTNEIdndgriPFILASQEGHYDCVQILLENKS-NIDQRGYDGRNALRVAALEGHRDIVELLfshgadvnck 942
Cdd:cd22192 7 ELHLLQQKRISES------PLLLAAKENDVQAIKKLLKCPScDLFQRGALGETALHVAALYDNLEAAVVL---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 943 dADGRPTLYILALENQLtmaeYflenganveasdaEGRTALHVSCWQGHMEMVQVLIAYHADVNAAdnekRSA------- 1015
Cdd:cd22192 71 -MEAAPELVNEPMTSDL----Y-------------QGETALHIAVVNQNLNLVRELIARGADVVSP----RATgtffrpg 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 1016 -----------LQSAAWQGHVKVVQLLIEHGA----------VVDH--TCNQGATALC-----IAAQEGHIDvvQVLLEH 1067
Cdd:cd22192 129 pknliyygehpLSFAACVGNEEIVRLLIEHGAdiraqdslgnTVLHilVLQPNKTFACqmydlILSYDKEDD--LQPLDL 206
|
250 260
....*....|....*....|....*.
gi 62988328 1068 gaDPNHAdqfGRTAMRVAAKNGHSQI 1093
Cdd:cd22192 207 --VPNNQ---GLTPFKLAAKEGNIVM 227
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
1047-1097 |
1.94e-11 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 60.37 E-value: 1.94e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 62988328 1047 TALCIAAQEGHIDVVQVLLEHGADPNHADQFGRTAMRVAAKNGHSQIIKLL 1097
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
497-649 |
2.87e-11 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 68.36 E-value: 2.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 497 LQLLVKAG--AHVNSEDDRTSCIVRQALEREDSIRTLLDNGASVNQCDSNGRTLLANAAYSGSLDVVNLLVSRGAdleIE 574
Cdd:PLN03192 541 LEELLKAKldPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFAS---IS 617
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62988328 575 DAH-GHTPLTLAARQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGHTEVVSALLYAGVKVDCADAD---SRTALR 649
Cdd:PLN03192 618 DPHaAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDddfSPTELR 696
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
706-801 |
4.75e-11 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 67.23 E-value: 4.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 706 EDVDGRTA--LSVAaLCVPASKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRT 783
Cdd:PTZ00322 72 EVIDPVVAhmLTVE-LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKT 150
|
90
....*....|....*...
gi 62988328 784 PLLAAASMGHASVVNTLL 801
Cdd:PTZ00322 151 PLELAEENGFREVVQLLS 168
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
759-987 |
8.56e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 65.78 E-value: 8.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 759 GHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGl 838
Cdd:PHA02875 13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 839 deNHRDDA----GWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIPFILASQEGHYDCVQILLENKSNIDQRGYDGR 914
Cdd:PHA02875 92 --KFADDVfykdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGC 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62988328 915 NALRVAALEGHRDIVELLFSHGADVNCKDADGRPTLYILALE-NQLTMAEYFLENGAN---VEASDAEGRTALHVSC 987
Cdd:PHA02875 170 TPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIEnNKIDIVRLFIKRGADcniMFMIEGEECTILDMIC 246
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
764-850 |
1.13e-10 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 66.07 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 764 VDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRtLLDRGLDENHR 843
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ-LLSRHSQCHFE 176
|
....*..
gi 62988328 844 DDAGWTP 850
Cdd:PTZ00322 177 LGANAKP 183
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
1028-1130 |
1.48e-10 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 65.69 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 1028 VQLLIEHGAVVDHTCNQGATALCIAAQEGHIDVVQVLLEHGADPNHADQFGRTAMRVAAKNGHSQIIKLLEKYGASSLNG 1107
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFEL 177
|
90 100
....*....|....*....|...
gi 62988328 1108 CSPSPVHTMEQKPLQSLSSKVQS 1130
Cdd:PTZ00322 178 GANAKPDSFTGKPPSLEDSPISS 200
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
814-867 |
4.95e-10 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 56.51 E-value: 4.95e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 62988328 814 GRTVLSIASAQGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRLICEALI 867
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
528-719 |
7.02e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 63.36 E-value: 7.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 528 IRTLLDNGASVNQCDSN-GRTLLANAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLIGCGANINH 606
Cdd:PHA02878 150 TKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 607 TDQDGWTALrsaawggHTEVVSALLYagvkvdcadadsrtalraaawggheDIVLNLLQHGAEVN-KADNEGRTALIAAa 685
Cdd:PHA02878 230 RDKCGNTPL-------HISVGYCKDY-------------------------DILKLLLEHGVDVNaKSYILGLTALHSS- 276
|
170 180 190
....*....|....*....|....*....|....
gi 62988328 686 yMGHREIVEHLLDHGAEVNHEDVDGRTALSVAAL 719
Cdd:PHA02878 277 -IKSERKLKLLLEYGADINSLNSYKLTPLSSAVK 309
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
889-1114 |
8.93e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 63.16 E-value: 8.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 889 QEGHYDCVQILLENKSNIDQRGYDGRNALRVAALEGHRDIVELLFSHGADVNCKDADGRPTLYILALENQLTMAEYFLEN 968
Cdd:PHA02876 154 QQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDN 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 969 GANVEASDAEGRTALHvscwqgHMEMVQVLIAYHA--DVNAADNEKRSALQSAAWQGHV-KVVQLLIEHGAVVDHTCNQG 1045
Cdd:PHA02876 234 RSNINKNDLSLLKAIR------NEDLETSLLLYDAgfSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKG 307
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62988328 1046 ATALCIAAQEGH-IDVVQVLLEHGADPNHADQFGRTAMRVAAKNGHSQ--IIKLLEkYGA--SSLNGCSPSPVH 1114
Cdd:PHA02876 308 ETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKdiVITLLE-LGAnvNARDYCDKTPIH 380
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
1013-1065 |
9.72e-10 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 55.36 E-value: 9.72e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 62988328 1013 RSALQSAAWQGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQEGHIDVVQVLL 1065
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
580-761 |
1.40e-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: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 580 TPLTLAARQGHTKVVNCLIGCganiNHTD-----QDGWTALRSAAWGGHTEVVSAL---------------LYAGVkvdc 639
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLLKC----PSCDlfqrgALGETALHVAALYDNLEAAVVLmeaapelvnepmtsdLYQGE---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 640 adadsrTALRAAAWGGHEDIVLNLLQHGAEVNKADNEG------RTALIA--------AAYMGHREIVEHLLDHGAEVNH 705
Cdd:cd22192 91 ------TALHIAVVNQNLNLVRELIARGADVVSPRATGtffrpgPKNLIYygehplsfAACVGNEEIVRLLIEHGADIRA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62988328 706 EDVDGRTALSVAALcvPASKGHASVVSLLI------DRGAEVDHC-DKDGMTPLLVAAYEGHV 761
Cdd:cd22192 165 QDSLGNTVLHILVL--QPNKTFACQMYDLIlsydkeDDLQPLDLVpNNQGLTPFKLAAKEGNI 225
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
979-1032 |
1.70e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 54.97 E-value: 1.70e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 62988328 979 GRTALHVSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSAAWQGHVKVVQLLI 1032
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
808-900 |
1.95e-09 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 62.22 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 808 DSIDSEGRTVLSIA----SAQGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIP 883
Cdd:PTZ00322 72 EVIDPVVAHMLTVElcqlAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTP 151
|
90
....*....|....*..
gi 62988328 884 FILASQEGHYDCVQILL 900
Cdd:PTZ00322 152 LELAEENGFREVVQLLS 168
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
691-945 |
2.18e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 61.82 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 691 EIVEHLLDHGAEVNHEDVDGRTALSVAALcVPASKGHASVVSLLIDRgaEVDHCDKDGMTpllvAAYEGHVDVVDLLLEG 770
Cdd:PHA02878 51 DVVKSLLTRGHNVNQPDHRDLTPLHIICK-EPNKLGMKEMIRSINKC--SVFYTLVAIKD----AFNNRNVEIFKIILTN 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 771 GADVDHTDNNGRTPLLAAASMGHASVVNTLLFWGAAVDSID-SEGRTVLSIASAQGNVEVVRTLLDRGLDENHRDDAGWT 849
Cdd:PHA02878 124 RYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNS 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 850 PLHMAAFEGHRLICEALIEQGARTNEIDNDGRIPF-ILASQEGHYDCVQILLENKSNIDQRGY-DGRNALRVAALEghRD 927
Cdd:PHA02878 204 PLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLhISVGYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKS--ER 281
|
250
....*....|....*...
gi 62988328 928 IVELLFSHGADVNCKDAD 945
Cdd:PHA02878 282 KLKLLLEYGADINSLNSY 299
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
624-907 |
2.52e-09 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 61.39 E-value: 2.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 624 TEVVSALLYAGVKVDCADADSRTAL-----RAAAWGGHEDIVLNLLQHGAEVNKADNEGRT---ALIAAAYMGHREIVEH 695
Cdd:PHA02798 51 TDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETplyCLLSNGYINNLEILLF 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 696 LLDHGAEVNHEDVDGRTALSVAalcvpASKGHA---SVVSLLIDRGAEVD-HCDKDGMTPLLVAAYEG----HVDVVDLL 767
Cdd:PHA02798 131 MIENGADTTLLDKDGFTMLQVY-----LQSNHHidiEIIKLLLEKGVDINtHNNKEKYDTLHCYFKYNidriDADILKLF 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 768 LEGGADVDHTDNNGRTPLLaaasmghaSVVNTLLFWGAAVDSidsegrtvlsiasaqgnveVVRTLLDRGLDENHRDDAG 847
Cdd:PHA02798 206 VDNGFIINKENKSHKKKFM--------EYLNSLLYDNKRFKK-------------------NILDFIFSYIDINQVDELG 258
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 848 WTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIPFILASQEGHYDCVQILLENKSNID 907
Cdd:PHA02798 259 FNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKPNKN 318
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
927-1113 |
2.62e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 61.43 E-value: 2.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 927 DIVELLFSHGADVNCKDADGRPTLYILALE-NQLTMAE-----------------------------------YF----- 965
Cdd:PHA02878 51 DVVKSLLTRGHNVNQPDHRDLTPLHIICKEpNKLGMKEmirsinkcsvfytlvaikdafnnrnveifkiiltnRYkniqt 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 966 -----------------------LENGANVEASDAE-GRTALHVSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSAAW 1021
Cdd:PHA02878 131 idlvyidkkskddiieaeitkllLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVK 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 1022 QGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQE-GHIDVVQVLLEHGADPN-HADQFGRTAMRVAAKNghSQIIKLLEK 1099
Cdd:PHA02878 211 HYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNaKSYILGLTALHSSIKS--ERKLKLLLE 288
|
250
....*....|....*.
gi 62988328 1100 YGA--SSLNGCSPSPV 1113
Cdd:PHA02878 289 YGAdiNSLNSYKLTPL 304
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
783-999 |
4.92e-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: 4.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 783 TPLLAAASMGHASVVNTLLfwgaAVDSID-----SEGRTVLSIASAQGNVEVVRTLLD--RGL-DENHRDD--AGWTPLH 852
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLL----KCPSCDlfqrgALGETALHVAALYDNLEAAVVLMEaaPELvNEPMTSDlyQGETALH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 853 MAAFEGHRLICEALIEQGARTneidndgripfILASQEGHYdcvqiLLENKSNIdqrGYDGRNALRVAALEGHRDIVELL 932
Cdd:cd22192 95 IAVVNQNLNLVRELIARGADV-----------VSPRATGTF-----FRPGPKNL---IYYGEHPLSFAACVGNEEIVRLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 933 FSHGADVNCKDADGRPTLYILALENQLT----MAEYFLenganveASDAEGR-------------TALHVSCWQGHMEMV 995
Cdd:cd22192 156 IEHGADIRAQDSLGNTVLHILVLQPNKTfacqMYDLIL-------SYDKEDDlqpldlvpnnqglTPFKLAAKEGNIVMF 228
|
....
gi 62988328 996 QVLI 999
Cdd:cd22192 229 QHLV 232
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
578-631 |
5.39e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 53.43 E-value: 5.39e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 62988328 578 GHTPLTLAARQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGHTEVVSALL 631
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
645-697 |
6.00e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 53.43 E-value: 6.00e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 62988328 645 RTALRAAAWGGHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLL 697
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
592-801 |
9.13e-09 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 59.68 E-value: 9.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 592 KVVNCLIGCGANINHTDQDGWTALRSAAWGGHTEVVSALLYAGVKVDCADADSRTALRAAAwgGHEDIVLN----LLQHG 667
Cdd:PHA02946 53 RFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLS--GTDDEVIErinlLVQYG 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 668 AEVNKA-DNEGRTALIAAAYMGHReIVEHLLDHGAEVNHEDVDGRTALSVAALcvpASKGHASVVSLLIDRGAEVDHCDK 746
Cdd:PHA02946 131 AKINNSvDEEGCGPLLACTDPSER-VFKKIMSIGFEARIVDKFGKNHIHRHLM---SDNPKASTISWMMKLGISPSKPDH 206
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 62988328 747 DGMTPLLVAAYE--GHVDVVDLLLEgGADVDHTDNNGRTPL-LAAASMGHASVVNTLL 801
Cdd:PHA02946 207 DGNTPLHIVCSKtvKNVDIINLLLP-STDVNKQNKFGDSPLtLLIKTLSPAHLINKLL 263
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
946-999 |
1.11e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 52.66 E-value: 1.11e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 62988328 946 GRPTLYILALENQLTMAEYFLENGANVEASDAEGRTALHVSCWQGHMEMVQVLI 999
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
710-768 |
1.39e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 52.28 E-value: 1.39e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 62988328 710 GRTALSVAAlcvpaSKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVDLLL 768
Cdd:pfam13637 1 ELTALHAAA-----ASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
528-600 |
2.04e-08 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 58.76 E-value: 2.04e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62988328 528 IRTLLDNGASVNQCDSNGRTLLANAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLIGC 600
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
927-1097 |
2.32e-08 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 58.31 E-value: 2.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 927 DIVELLFSHGADVNCKDAD-GRPTLYILA----LENQLTMAEYFLENGANVEASDAEGRTALHvscwqghmemvqvliay 1001
Cdd:PHA02798 52 DIVKLFINLGANVNGLDNEySTPLCTILSnikdYKHMLDIVKILIENGADINKKNSDGETPLY----------------- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 1002 hadvnaadnekrsALQSAAWQGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQEGH---IDVVQVLLEHGADPN-HADQF 1077
Cdd:PHA02798 115 -------------CLLSNGYINNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINtHNNKE 181
|
170 180
....*....|....*....|....
gi 62988328 1078 GRTAMRVAAKNGHSQ----IIKLL 1097
Cdd:PHA02798 182 KYDTLHCYFKYNIDRidadILKLF 205
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
844-948 |
2.42e-08 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 58.76 E-value: 2.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 844 DDAGWTPLHMAAFE-------GHRLICEALIEQGARTNEIDNDGRIPFILASQEGHYDCVQILLENKSNIDQRGYDGRNA 916
Cdd:PTZ00322 72 EVIDPVVAHMLTVElcqlaasGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTP 151
|
90 100 110
....*....|....*....|....*....|..
gi 62988328 917 LRVAALEGHRDIVELLFSHGADVNCKDADGRP 948
Cdd:PTZ00322 152 LELAEENGFREVVQLLSRHSQCHFELGANAKP 183
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
962-1034 |
2.46e-08 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 58.76 E-value: 2.46e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62988328 962 AEYFLENGANVEASDAEGRTALHVSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSAAWQGHVKVVQLLIEH 1034
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
480-639 |
2.66e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 58.08 E-value: 2.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 480 TPVRDSLSTLIPKEQEVLQLLVKAGAHVNSEDDRTSCIVRQALEREDSIRTLLDNGASVNQCDSNGRTLLANAAYSGSLD 559
Cdd:PHA02875 70 SELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIK 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 560 VVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLIGCGANINHTDQDG-WTALRSAAWGGHTEVVSALLYAGvkVD 638
Cdd:PHA02875 150 GIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRG--AD 227
|
.
gi 62988328 639 C 639
Cdd:PHA02875 228 C 228
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
929-1001 |
3.67e-08 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 57.99 E-value: 3.67e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62988328 929 VELLFSHGADVNCKDADGRPTLYILALENQLTMAEYFLENGANVEASDAEGRTALHVSCWQGHMEMVQVLIAY 1001
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
955-1110 |
4.37e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 57.31 E-value: 4.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 955 LENQLTMAEYFLENGANVEASDAEGRTALHVSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSAAWQGHVKVVQLLIEH 1034
Cdd:PHA02875 11 LFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 1035 GAVVDHTC-NQGATALCIAAQEGHIDVVQVLLEHGADPNHADQFGRTAMRVAAKNGHSQIIKLLEKYGAsSLN-----GC 1108
Cdd:PHA02875 91 GKFADDVFyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKA-CLDiedccGC 169
|
..
gi 62988328 1109 SP 1110
Cdd:PHA02875 170 TP 171
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
549-631 |
4.99e-08 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 57.60 E-value: 4.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 549 LANAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGHTEVVS 628
Cdd:PTZ00322 86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165
|
...
gi 62988328 629 ALL 631
Cdd:PTZ00322 166 LLS 168
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
710-903 |
8.06e-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: 8.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 710 GRTALSVAALcvpasKGHASVVSLLIDRGAEV--DHCDKD---GMTPLLVAAYEGHVDVVDLLLEGGADVdhtdNNGRtp 784
Cdd:cd22192 51 GETALHVAAL-----YDNLEAAVVLMEAAPELvnEPMTSDlyqGETALHIAVVNQNLNLVRELIARGADV----VSPR-- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 785 llAAASMGHASVVNTLLFwgaavdsidseGRTVLSIASAQGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRLI-C 863
Cdd:cd22192 120 --ATGTFFRPGPKNLIYY-----------GEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFaC 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 62988328 864 EA---LIEQGARTNEI------DNDGRIPFILASQEGHYDCVQILLENK 903
Cdd:cd22192 187 QMydlILSYDKEDDLQpldlvpNNQGLTPFKLAAKEGNIVMFQHLVQKR 235
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
959-1114 |
1.25e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 56.04 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 959 LTMAEYFLENGANVEASDAEGRTALHVSCWQGHMEMVQVLIA------------------YHADVNAA--------DNEK 1012
Cdd:PHA02878 50 LDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRsinkcsvfytlvaikdafNNRNVEIFkiiltnryKNIQ 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 1013 RSAL-----QSAAWQGHVKVVQLLIEHGAVVD-HTCNQGATALCIAAQEGHIDVVQVLLEHGADPNHADQFGRTAMRVAA 1086
Cdd:PHA02878 130 TIDLvyidkKSKDDIIEAEITKLLLSYGADINmKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAV 209
|
170 180 190
....*....|....*....|....*....|
gi 62988328 1087 KNGHSQIIKLLEKYGASS--LNGCSPSPVH 1114
Cdd:PHA02878 210 KHYNKPIVHILLENGASTdaRDKCGNTPLH 239
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
807-964 |
1.57e-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: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 807 VDSIDSEGRTVLSIASAQGNVEVVRTLLdrgLDENHRDDAGWTPLHMAAFEGHRlICEALI---EQGAR-------TNEI 876
Cdd:TIGR00870 45 INCPDRLGRSALFVAAIENENLELTELL---LNLSCRGAVGDTLLHAISLEYVD-AVEAILlhlLAAFRksgplelANDQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 877 DND----GRIPFILASQEGHYDCVQILLENKSNIDQRG--------------YDGRNALRVAALEGHRDIVELLFSHGAD 938
Cdd:TIGR00870 121 YTSeftpGITALHLAAHRQNYEIVKLLLERGASVPARAcgdffvksqgvdsfYHGESPLNAAACLGSPSIVALLSEDPAD 200
|
170 180
....*....|....*....|....*.
gi 62988328 939 VNCKDADGRPTLYILALENQLTmAEY 964
Cdd:TIGR00870 201 ILTADSLGNTLLHLLVMENEFK-AEY 225
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
789-866 |
1.90e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 55.67 E-value: 1.90e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62988328 789 ASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRLICEAL 866
Cdd:PTZ00322 90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
847-900 |
2.21e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 48.81 E-value: 2.21e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 62988328 847 GWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIPFILASQEGHYDCVQILL 900
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| TRPV1-4 |
cd22193 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ... |
885-1066 |
2.98e-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: 2.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 885 ILASQEGHYDCVQILL---ENKSNIDQ--------RGYDGRNALRVAALEGHRDIVELLFSHGADVNC-------KDADG 946
Cdd:cd22193 37 LLNLNPGTNDTIRILLdiaEKTDNLKRfinaeytdEYYEGQTALHIAIERRQGDIVALLVENGADVHAhakgrffQPKYQ 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 947 RPTLY-------ILALENQLTMAEYFLENG---ANVEASDAEGRTALHvscwqghmemvqvliayhADVNAADNEK-RSA 1015
Cdd:cd22193 117 GEGFYfgelplsLAACTNQPDIVQYLLENEhqpADIEAQDSRGNTVLH------------------ALVTVADNTKeNTK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 62988328 1016 LQSAAWQGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQEGHIDVVQVLLE 1066
Cdd:cd22193 179 FVTRMYDMILIRGAKLCPTVELEEIRNNDGLTPLQLAAKMGKIEILKYILQ 229
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
1002-1104 |
3.61e-07 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 54.87 E-value: 3.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 1002 HADVNAADNekrsaLQSAAWQGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQEGHIDVVQVLLEHGADPNHADQFGRTA 1081
Cdd:PLN03192 520 HDDPNMASN-----LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTA 594
|
90 100
....*....|....*....|...
gi 62988328 1082 MRVAAKNGHSQIIKLLEKYGASS 1104
Cdd:PLN03192 595 LWNAISAKHHKIFRILYHFASIS 617
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
805-854 |
4.39e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 48.11 E-value: 4.39e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 62988328 805 AAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDENHRDDAGWTPLHMA 854
Cdd:pfam13857 7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| TRPV1 |
cd22196 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ... |
911-984 |
6.18e-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: 6.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 911 YDGRNALRVAALEGHRDIVELLFSHGADVNC-------KDADGRPTLY-------ILALENQLTMAEYFLEN---GANVE 973
Cdd:cd22196 92 YKGQTALHIAIERRNMHLVELLVQNGADVHArasgeffKKKKGGPGFYfgelplsLAACTNQLDIVKFLLENphsPADIS 171
|
90
....*....|.
gi 62988328 974 ASDAEGRTALH 984
Cdd:cd22196 172 ARDSMGNTVLH 182
|
|
| Semenogelin |
pfam05474 |
Semenogelin; This family consists of several mammalian secreted seminal proteins including ... |
1210-1403 |
7.03e-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: 7.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 1210 HNLSFTEQIQQHSlprsRSRQSIVSPSSTTQSLGQSHNSPSSEFEWSQVKPSLKsTKASKGGKSENSAKSGSA------- 1282
Cdd:pfam05474 268 HQTKNLSQDQEHG----RKAHKISYPSSRTEERQLHHGEKSVQKDVSKGSISIQ-TEEKIHGKSQNQVTIHSQdqehghk 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 1283 -GKKAKQSNSSQPKVLEYEMTQFdRRGPIAKSGTAAPPKQMPAESQCKIMIPSAQQEIGRSQQQFLIHQQSGEQKKRNG- 1360
Cdd:pfam05474 343 eNKISYQSSSTEERHLNCGEKGI-QKGVSKGSISIQTEEQIHGKSQNQVRIPSQAQEYGHKENKISYQSSSTEERRLNSg 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 62988328 1361 --------------IMTNPNYHLQSNQvflgRVSVPRTMQDRGHQEVLEGYPSSETE 1403
Cdd:pfam05474 422 ekdvqkgvskgsisIQTEEKIHGKSQN----QVTIPSQDQEHGHKENKMSYQSSSTE 474
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
992-1101 |
7.66e-07 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 53.30 E-value: 7.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 992 MEMVQVLIAYHADVNAADNEKRSALQS-----AAWQGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQEGHIDVVQVLL- 1065
Cdd:PHA02798 51 TDIVKLFINLGANVNGLDNEYSTPLCTilsniKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLf 130
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 62988328 1066 --EHGADPNHADQFGRTAMRVAAKNGHS---QIIKLLEKYG 1101
Cdd:PHA02798 131 miENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKG 171
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
619-713 |
8.67e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 53.75 E-value: 8.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 619 AWGGHTEVVSALLYAGVKVDCADADSRTALRAAAWGGHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLD 698
Cdd:PTZ00322 90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
|
90
....*....|....*
gi 62988328 699 HGAEvnHEDVDGRTA 713
Cdd:PTZ00322 170 HSQC--HFELGANAK 182
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
611-664 |
9.80e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 46.88 E-value: 9.80e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 62988328 611 GWTALRSAAWGGHTEVVSALLYAGVKVDCADADSRTALRAAAWGGHEDIVLNLL 664
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
1031-1085 |
1.05e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 46.96 E-value: 1.05e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 62988328 1031 LIEHGAV-VDHTCNQGATALCIAAQEGHIDVVQVLLEHGADPNHADQFGRTAMRVA 1085
Cdd:pfam13857 1 LLEHGPIdLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
677-735 |
2.56e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 45.73 E-value: 2.56e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 62988328 677 GRTALIAAAYMGHREIVEHLLDHGAEVNHEDVDGRTALSVAalcvpASKGHASVVSLLI 735
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFA-----ASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
887-932 |
2.88e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 45.73 E-value: 2.88e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 62988328 887 ASQEGHYDCVQILLENKSNIDQRGYDGRNALRVAALEGHRDIVELL 932
Cdd:pfam13637 8 AAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
663-717 |
2.92e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 45.80 E-value: 2.92e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 62988328 663 LLQHG-AEVNKADNEGRTALIAAAYMGHREIVEHLLDHGAEVNHEDVDGRTALSVA 717
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
913-966 |
3.12e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 45.73 E-value: 3.12e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 62988328 913 GRNALRVAALEGHRDIVELLFSHGADVNCKDADGRPTLYILALENQLTMAEYFL 966
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
884-1086 |
3.54e-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: 3.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 884 FILASQEGHYDCVQILLEN--KSNIDQRGYDGRNALRVAALEG-HRDIVELLFSHgadvNCKDADGRPTLYILALENQ-- 958
Cdd:TIGR00870 21 FLPAAERGDLASVYRDLEEpkKLNINCPDRLGRSALFVAAIENeNLELTELLLNL----SCRGAVGDTLLHAISLEYVda 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 959 -----LTMAEYFLENGANVEASD------AEGRTALHVSCWQGHMEMVQVLIAYHADVNAA---DNEKRSALQSAAWQGh 1024
Cdd:TIGR00870 97 veailLHLLAAFRKSGPLELANDqytsefTPGITALHLAAHRQNYEIVKLLLERGASVPARacgDFFVKSQGVDSFYHG- 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62988328 1025 vkvvqlliEHgavvdhtcnqgatALCIAAQEGHIDVVQVLLEHGADPNHADQFGRTAMRVAA 1086
Cdd:TIGR00870 176 --------ES-------------PLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLV 216
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
654-973 |
3.76e-06 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 51.21 E-value: 3.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 654 GGHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLDHGAEVNHEDVDGRTALSVAAlcvPASKGHASVVSL 733
Cdd:PHA02946 49 GLDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLS---GTDDEVIERINL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 734 LIDRGAEVDH-CDKDGMTPLLvAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLA--AASMGHASVVNTLLFWGAAVDSI 810
Cdd:PHA02946 126 LVQYGAKINNsVDEEGCGPLL-ACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRhlMSDNPKASTISWMMKLGISPSKP 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 811 DSEGRTVLSIASAQ--GNVEVVRTLLDrGLDENHRDDAGWTPLHMAAfegHRLICEALIEQGARTNEIDNDGRIPFILAS 888
Cdd:PHA02946 205 DHDGNTPLHIVCSKtvKNVDIINLLLP-STDVNKQNKFGDSPLTLLI---KTLSPAHLINKLLSTSNVITDQTVNICIFY 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 889 QEGhyDCVQILlenksNIDQRGYDGRNaLRVAALEGHRDIVELLFSHgaDVNCKDAdgrptLYILALENQLTMAEYFLEN 968
Cdd:PHA02946 281 DRD--DVLEII-----NDKGKQYDSTD-FKMAVEVGSIRCVKYLLDN--DIICEDA-----MYYAVLSEYETMVDYLLFN 345
|
....*
gi 62988328 969 GANVE 973
Cdd:PHA02946 346 HFSVD 350
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
966-1019 |
4.11e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 45.42 E-value: 4.11e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 62988328 966 LENG-ANVEASDAEGRTALHVSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSA 1019
Cdd:pfam13857 2 LEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
747-779 |
4.51e-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: 44.59 E-value: 4.51e-06
10 20 30
....*....|....*....|....*....|....
gi 62988328 747 DGMTPLLVAAYE-GHVDVVDLLLEGGADVDHTDN 779
Cdd:pfam00023 1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
839-1066 |
4.89e-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: 4.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 839 DENHRDDAGWTPLHMAAFEGH--RLICEALIEQGARtneiDNDGRIPFILASQEGHYdcvqillenksnidqrgYDGRNA 916
Cdd:cd21882 18 SAYQRGATGKTCLHKAALNLNdgVNEAIMLLLEAAP----DSGNPKELVNAPCTDEF-----------------YQGQTA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 917 LRVAALEGHRDIVELLFSHGADVN---CKDA---DGRPTLY-------ILALENQLTMAEYFLENG---ANVEASDAEGR 980
Cdd:cd21882 77 LHIAIENRNLNLVRLLVENGADVSaraTGRFfrkSPGNLFYfgelplsLAACTNQEEIVRLLLENGaqpAALEAQDSLGN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 981 TALHVscwqghmemvQVLIAYhadvNAADNEKRSalqsaawqghVKVVQLLIEHGAVVDHTC-------NQGATALCIAA 1053
Cdd:cd21882 157 TVLHA----------LVLQAD----NTPENSAFV----------CQMYNLLLSYGAHLDPTQqleeipnHQGLTPLKLAA 212
|
250
....*....|...
gi 62988328 1054 QEGHIDVVQVLLE 1066
Cdd:cd21882 213 VEGKIVMFQHILQ 225
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
526-801 |
5.44e-06 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 50.60 E-value: 5.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 526 DSIRTLLDNGASVNQCDSNGR----TLLAN-AAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTlaarqghtkvvnCLIGC 600
Cdd:PHA02798 52 DIVKLFINLGANVNGLDNEYStplcTILSNiKDYKHMLDIVKILIENGADINKKNSDGETPLY------------CLLSN 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 601 GAnINhtdqdgwtalrsaawggHTEVVSALLYAGVKVDCADADSRTALRAAAWGGHE---DIVLNLLQHGAEVNKADN-E 676
Cdd:PHA02798 120 GY-IN-----------------NLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDINTHNNkE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 677 GRTALiaAAYMGHR------EIVEHLLDHGAEVNHEDVDGRTAL--SVAALCVPASKGHASVVSLLIdrgAEVDHCDKD- 747
Cdd:PHA02798 182 KYDTL--HCYFKYNidridaDILKLFVDNGFIINKENKSHKKKFmeYLNSLLYDNKRFKKNILDFIF---SYIDINQVDe 256
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 62988328 748 -GMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLL 801
Cdd:PHA02798 257 lGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSIL 311
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
513-565 |
1.03e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 44.19 E-value: 1.03e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 62988328 513 RTSCIVRQA-LEREDSIRTLLDNGASVNQCDSNGRTLLANAAYSGSLDVVNLLV 565
Cdd:pfam13637 1 ELTALHAAAaSGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
545-598 |
1.17e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 43.80 E-value: 1.17e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 62988328 545 GRTLLANAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLI 598
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
531-585 |
1.25e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 43.87 E-value: 1.25e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 62988328 531 LLDNG-ASVNQCDSNGRTLLANAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLA 585
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
978-1010 |
1.27e-05 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 43.43 E-value: 1.27e-05
10 20 30
....*....|....*....|....*....|....
gi 62988328 978 EGRTALHVSCWQ-GHMEMVQVLIAYHADVNAADN 1010
Cdd:pfam00023 1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
734-785 |
2.34e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 43.10 E-value: 2.34e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 62988328 734 LIDRG-AEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPL 785
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
896-957 |
2.88e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 48.74 E-value: 2.88e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62988328 896 VQILLENKSNIDQRGYDGRNALRVAALEGHRDIVELLFSHGADVNCKDADGRpTLYILALEN 957
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGK-TPLELAEEN 158
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
1044-1072 |
2.93e-05 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 42.19 E-value: 2.93e-05
10 20
....*....|....*....|....*....
gi 62988328 1044 QGATALCIAAQEGHIDVVQVLLEHGADPN 1072
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
676-707 |
2.99e-05 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 42.28 E-value: 2.99e-05
10 20 30
....*....|....*....|....*....|...
gi 62988328 676 EGRTAL-IAAAYMGHREIVEHLLDHGAEVNHED 707
Cdd:pfam00023 1 DGNTPLhLAAGRRGNLEIVKLLLSKGADVNARD 33
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
1046-1102 |
3.38e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 48.36 E-value: 3.38e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 62988328 1046 ATALCIAAQEGHIDVVQVLLEHGADPNHADQFGRTAMRVAAKNGHSQIIKLLEKYGA 1102
Cdd:PTZ00322 83 TVELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGA 139
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
1044-1075 |
3.68e-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: 3.68e-05
10 20 30
....*....|....*....|....*....|...
gi 62988328 1044 QGATALCIAA-QEGHIDVVQVLLEHGADPNHAD 1075
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
1025-1102 |
5.06e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 47.35 E-value: 5.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 1025 VKVVQLLIEHGAVVDHTCNQGATALCIAAQEGHI-----DVVQVLLEHGADPNHADQFGRTAMRVAA--KNGHSQIIKLL 1097
Cdd:PHA03100 48 IDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYL 127
|
....*
gi 62988328 1098 EKYGA 1102
Cdd:PHA03100 128 LDNGA 132
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
747-775 |
6.11e-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: 41.42 E-value: 6.11e-05
10 20
....*....|....*....|....*....
gi 62988328 747 DGMTPLLVAAYEGHVDVVDLLLEGGADVD 775
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
830-1097 |
6.20e-05 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 47.36 E-value: 6.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 830 VRTLLDRGLDENHRDDAGWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIP--FILASQEGHYDCVQILLENKSNID 907
Cdd:PHA02946 55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPlyYLSGTDDEVIERINLLVQYGAKIN 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 908 QRGYDGRNALRVAALEGHRDIVELLFSHGADVNCKDADGRPTL--YILALENQLTMAEYFLENGANVEASDAEGRTALHV 985
Cdd:PHA02946 135 NSVDEEGCGPLLACTDPSERVFKKIMSIGFEARIVDKFGKNHIhrHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHI 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 986 SCWQ--GHMEMVQVLIAyHADVNAADNEKRSALQ---SAAWQGHVkVVQLLIEHGAVVDHTCNqgataLCIAAQEGhiDV 1060
Cdd:PHA02946 215 VCSKtvKNVDIINLLLP-STDVNKQNKFGDSPLTlliKTLSPAHL-INKLLSTSNVITDQTVN-----ICIFYDRD--DV 285
|
250 260 270
....*....|....*....|....*....|....*..
gi 62988328 1061 VQVLLEHGadpnhaDQFGRTAMRVAAKNGHSQIIKLL 1097
Cdd:PHA02946 286 LEIINDKG------KQYDSTDFKMAVEVGSIRCVKYL 316
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
495-613 |
6.27e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 45.58 E-value: 6.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 495 EVLQLLVKAGAHVN--SEDDRTSCI-----VRQALErEDSIRTLLDNGASVNQCDSNGRTLLAN--AAYSGSLDVVNLLV 565
Cdd:PHA02859 67 EILKFLIENGADVNfkTRDNNLSALhhylsFNKNVE-PEILKILIDSGSSITEEDEDGKNLLHMymCNFNVRINVIKLLI 145
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 62988328 566 SRGADLEIEDAHG----HTPLTLAARQghtKVVNCLIGCGANINHTDQDGWT 613
Cdd:PHA02859 146 DSGVSFLNKDFDNnnilYSYILFHSDK---KIFDFLTSLGIDINETNKSGYN 194
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
766-821 |
8.47e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 41.56 E-value: 8.47e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 62988328 766 LLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIA 821
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
676-704 |
1.05e-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: 40.65 E-value: 1.05e-04
10 20
....*....|....*....|....*....
gi 62988328 676 EGRTALIAAAYMGHREIVEHLLDHGAEVN 704
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
747-776 |
1.13e-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: 1.13e-04
10 20 30
....*....|....*....|....*....|
gi 62988328 747 DGMTPLLVAAYEGHVDVVDLLLEGGADVDH 776
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
663-734 |
1.15e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 46.82 E-value: 1.15e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62988328 663 LLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLDHGAEVNHEDVDGRTALSVAalcvpASKGHASVVSLL 734
Cdd:PTZ00322 101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA-----EENGFREVVQLL 167
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
577-605 |
1.25e-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: 1.25e-04
10 20
....*....|....*....|....*....
gi 62988328 577 HGHTPLTLAARQGHTKVVNCLIGCGANIN 605
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
978-1007 |
1.38e-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: 1.38e-04
10 20 30
....*....|....*....|....*....|
gi 62988328 978 EGRTALHVSCWQGHMEMVQVLIAYHADVNA 1007
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
899-954 |
1.48e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 40.79 E-value: 1.48e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 62988328 899 LLENKS-NIDQRGYDGRNALRVAALEGHRDIVELLFSHGADVNCKDADGrPTLYILA 954
Cdd:pfam13857 1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEG-LTALDLA 56
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
584-674 |
1.55e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 46.43 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 584 LAArQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGHTEVVSALLYAGVKVDCADADSRTALRAAAWGGHEDIVLNL 663
Cdd:PTZ00322 89 LAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
|
90
....*....|.
gi 62988328 664 LQHGAEVNKAD 674
Cdd:PTZ00322 168 SRHSQCHFELG 178
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
497-609 |
1.93e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 45.72 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 497 LQLLVKAGAHVNSEDDRTSCIVRQALEREDSIRTLLDNGASVNQCDSNGRTLLANA-AYSGSLDVVNLLVSRGADLEIED 575
Cdd:PHA02874 206 IKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIELLINNASINDQDIDGSTPLHHAiNPPCDIDIIDILLYHKADISIKD 285
|
90 100 110
....*....|....*....|....*....|....*
gi 62988328 576 AHGHTPLTLAARQ-GHTKVVNCLIGCGANINHTDQ 609
Cdd:PHA02874 286 NKGENPIDTAFKYiNKDPVIKDIIANAVLIKEADK 320
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
978-1007 |
2.44e-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: 2.44e-04
10 20 30
....*....|....*....|....*....|
gi 62988328 978 EGRTALHVSCWQGHMEMVQVLIAYHADVNA 1007
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
710-857 |
2.65e-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: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 710 GRTALSVAALcvpasKGHASVVSLLIDRGAEVD-------------HCDKDGMTPLLVAAYEGHVDVVDLLLEGGAD--- 773
Cdd:cd21882 73 GQTALHIAIE-----NRNLNLVRLLVENGADVSaratgrffrkspgNLFYFGELPLSLAACTNQEEIVRLLLENGAQpaa 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 774 VDHTDNNGRTPLLAAASMGHASVVNT---------LLFWGAAVDSIDS-------EGRTVLSIASAQGNVEVVRTLLDRG 837
Cdd:cd21882 148 LEAQDSLGNTVLHALVLQADNTPENSafvcqmynlLLSYGAHLDPTQQleeipnhQGLTPLKLAAVEGKIVMFQHILQRE 227
|
170 180
....*....|....*....|....*.
gi 62988328 838 LDENH----RDDAGWT--PLHMAAFE 857
Cdd:cd21882 228 FSGPYqplsRKFTEWTygPVTSSLYD 253
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
691-862 |
2.73e-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: 45.52 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 691 EIVEHLL----DHG-------AEVNHEDVDGRTALSVAAlcvpaSKGHASVVSLLIDRGAEVDHCDKD------------ 747
Cdd:cd22194 111 EIVRILLafaeENGildrfinAEYTEEAYEGQTALNIAI-----ERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegf 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 748 --GMTPLLVAAYEGHVDVVDLLLEggadvdhtdnNGRTPLLAAASMGhasvvNTLLFwgAAVD-SIDSEGRTVLSIasaQ 824
Cdd:cd22194 186 yfGETPLALAACTNQPEIVQLLME----------KESTDITSQDSRG-----NTVLH--ALVTvAEDSKTQNDFVK---R 245
|
170 180 190
....*....|....*....|....*....|....*...
gi 62988328 825 GNVEVVRTLLDRGLdENHRDDAGWTPLHMAAFEGHRLI 862
Cdd:cd22194 246 MYDMILLKSENKNL-ETIRNNEGLTPLQLAAKMGKAEI 282
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
658-784 |
2.79e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 43.65 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 658 DIVLNLLQHGAEVN-KADNEGRTALiaAAYMGHR-----EIVEHLLDHGAEVNHEDVDGRTALSVaALCVPASKghASVV 731
Cdd:PHA02859 67 EILKFLIENGADVNfKTRDNNLSAL--HHYLSFNknvepEILKILIDSGSSITEEDEDGKNLLHM-YMCNFNVR--INVI 141
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 62988328 732 SLLIDRGAEVDHCDKDGmTPLLVAAYEGHVD--VVDLLLEGGADVDHTDNNGRTP 784
Cdd:PHA02859 142 KLLIDSGVSFLNKDFDN-NNILYSYILFHSDkkIFDFLTSLGIDINETNKSGYNC 195
|
|
| PHA02989 |
PHA02989 |
ankyrin repeat protein; Provisional |
492-717 |
2.85e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222954 [Multi-domain] Cd Length: 494 Bit Score: 45.12 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 492 KEQEVLQLLVKAGAHVNSED-DRTSCIV----RQALEREDSIRTLLDNGASVNQC-DSNGRTLLAN--AAYSGSLDVVNL 563
Cdd:PHA02989 86 KIKKIVKLLLKFGADINLKTfNGVSPIVcfiyNSNINNCDMLRFLLSKGINVNDVkNSRGYNLLHMylESFSVKKDVIKI 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 564 LVSRGAD-LEIEDAHGHTPLTLAARQG----HTKVVNCLIGCGANINHTDQdgwtalrsaawgGHTEVVSALLyagvkvd 638
Cdd:PHA02989 166 LLSFGVNlFEKTSLYGLTPMNIYLRNDidviSIKVIKYLIKKGVNIETNNN------------GSESVLESFL------- 226
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62988328 639 cadaDSRTALRAaawggHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLDHGAEVNHEDVDGRTALSVA 717
Cdd:PHA02989 227 ----DNNKILSK-----KEFKVLNFILKYIKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYA 296
|
|
| TRPV2 |
cd22197 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ... |
885-1066 |
2.89e-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: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 885 ILASQEGHYDCVQILLEnksnIDQRG---------------YDGRNALRVAALEGHRDIVELLFSHGADVNCKDAD---- 945
Cdd:cd22197 55 VLNLQDGVNACIMPLLE----IDKDSgnpkplvnaqctdeyYRGHSALHIAIEKRSLQCVKLLVENGADVHARACGrffq 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 946 ---------GRPTLYILALENQLTMAEYFLENG---ANVEASDAEGRTALhvscwqghmemvqvliayHADVNAADN-EK 1012
Cdd:cd22197 131 kkqgtcfyfGELPLSLAACTKQWDVVNYLLENPhqpASLQAQDSLGNTVL------------------HALVMIADNsPE 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 62988328 1013 RSALQSAAWQGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQEGHIDVVQVLLE 1066
Cdd:cd22197 193 NSALVIKMYDGLLQAGARLCPTVQLEEISNHEGLTPLKLAAKEGKIEIFRHILQ 246
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
499-577 |
3.38e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 44.66 E-value: 3.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 499 LLVKAGAHVNSEDDRTSCIVRQAL--EREDSIRTLLDNGASVNQCDSNGRTLLANAAYSGSLDVVNLLVSRGADLEIEDA 576
Cdd:PHA03100 177 YLLSYGVPINIKDVYGFTPLHYAVynNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
|
.
gi 62988328 577 H 577
Cdd:PHA03100 257 T 257
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
912-941 |
3.54e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 39.11 E-value: 3.54e-04
10 20 30
....*....|....*....|....*....|
gi 62988328 912 DGRNALRVAALEGHRDIVELLFSHGADVNC 941
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
959-1095 |
3.77e-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: 45.13 E-value: 3.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 959 LTMAEyflENG-------ANVEASDAEGRTALHVSCWQGHMEMVQVLIAYHADVNAAD-----NEK---------RSALQ 1017
Cdd:cd22194 117 LAFAE---ENGildrfinAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAkgvffNPKykhegfyfgETPLA 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 1018 SAAWQGHVKVVQLLIEH----GAVVDHTCNQGATALCIAAQ--EGHIDVV-----QVLLEHG-----ADPNHAdqfGRTA 1081
Cdd:cd22194 194 LAACTNQPEIVQLLMEKestdITSQDSRGNTVLHALVTVAEdsKTQNDFVkrmydMILLKSEnknleTIRNNE---GLTP 270
|
170
....*....|....
gi 62988328 1082 MRVAAKNGHSQIIK 1095
Cdd:cd22194 271 LQLAAKMGKAEILK 284
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
577-608 |
3.77e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 39.19 E-value: 3.77e-04
10 20 30
....*....|....*....|....*....|...
gi 62988328 577 HGHTPLTLAA-RQGHTKVVNCLIGCGANINHTD 608
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
847-878 |
5.76e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 38.42 E-value: 5.76e-04
10 20 30
....*....|....*....|....*....|...
gi 62988328 847 GWTPLHMAA-FEGHRLICEALIEQGARTNEIDN 878
Cdd:pfam00023 2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
720-858 |
6.10e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 42.88 E-value: 6.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 720 CVPASKGHASVVSLLIDRGAEVDHCDKD-GMTPL---LVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPL---LAAASMg 792
Cdd:PHA02859 58 CLEKDKVNVEILKFLIENGADVNFKTRDnNLSALhhyLSFNKNVEPEILKILIDSGSSITEEDEDGKNLLhmyMCNFNV- 136
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62988328 793 HASVVNTLLFWGAAVDSIDSEGRTVL-SIASAQGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEG 858
Cdd:PHA02859 137 RINVIKLLIDSGVSFLNKDFDNNNILySYILFHSDKKIFDFLTSLGIDINETNKSGYNCYDLIKFRN 203
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
912-943 |
6.23e-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: 6.23e-04
10 20 30
....*....|....*....|....*....|...
gi 62988328 912 DGRNALRVAALE-GHRDIVELLFSHGADVNCKD 943
Cdd:pfam00023 1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
709-746 |
6.54e-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: 6.54e-04
10 20 30
....*....|....*....|....*....|....*...
gi 62988328 709 DGRTALSVAAlcvpASKGHASVVSLLIDRGAEVDHCDK 746
Cdd:pfam00023 1 DGNTPLHLAA----GRRGNLEIVKLLLSKGADVNARDK 34
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
696-755 |
7.02e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 38.87 E-value: 7.02e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62988328 696 LLDHG-AEVNHEDVDGRTALSVAAlcvpaSKGHASVVSLLIDRGAEVDHCDKDGMTPLLVA 755
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAA-----KYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
577-606 |
7.19e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 38.39 E-value: 7.19e-04
10 20 30
....*....|....*....|....*....|
gi 62988328 577 HGHTPLTLAARQGHTKVVNCLIGCGANINH 606
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
908-1084 |
8.03e-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: 8.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 908 QRGYDGRNALRVAAL---EGHRDIVELLFshgadvnckDADgRPTLYILALENQLTMAEYFlenganveasdaEGRTALH 984
Cdd:cd21882 21 QRGATGKTCLHKAALnlnDGVNEAIMLLL---------EAA-PDSGNPKELVNAPCTDEFY------------QGQTALH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 985 VSCWQGHMEMVQVLIAYHADVNAADNekrsalqSAAWQGHvkvvqlliehgavvDHTCNQ-GATALCIAAQEGHIDVVQV 1063
Cdd:cd21882 79 IAIENRNLNLVRLLVENGADVSARAT-------GRFFRKS--------------PGNLFYfGELPLSLAACTNQEEIVRL 137
|
170 180
....*....|....*....|....
gi 62988328 1064 LLEHGADP---NHADQFGRTAMRV 1084
Cdd:cd21882 138 LLENGAQPaalEAQDSLGNTVLHA 161
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
481-573 |
9.20e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 43.44 E-value: 9.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 481 PVRDSLSTL----IPKEQEVLQLLVKAGAHVNSED--DRTSCIVRQALEREDSIRTLLDNGASVNQCDSNGR-TLLANAA 553
Cdd:PHA02875 131 PNTDKFSPLhlavMMGDIKGIELLIDHKACLDIEDccGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAI 210
|
90 100
....*....|....*....|
gi 62988328 554 YSGSLDVVNLLVSRGADLEI 573
Cdd:PHA02875 211 ENNKIDIVRLFIKRGADCNI 230
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
676-705 |
9.56e-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: 9.56e-04
10 20 30
....*....|....*....|....*....|
gi 62988328 676 EGRTALIAAAYMGHREIVEHLLDHGAEVNH 705
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
826-940 |
1.13e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 42.11 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 826 NVEVVRTLLDRGLDENHR-DDAGWTPLHmaafegHRL---------ICEALIEQGARTNEIDNDGRIPF--ILASQEGHY 893
Cdd:PHA02859 65 NVEILKFLIENGADVNFKtRDNNLSALH------HYLsfnknvepeILKILIDSGSSITEEDEDGKNLLhmYMCNFNVRI 138
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 62988328 894 DCVQILLENKSNIDQRGYDGRNALRVAAL-EGHRDIVELLFSHGADVN 940
Cdd:PHA02859 139 NVIKLLIDSGVSFLNKDFDNNNILYSYILfHSDKKIFDFLTSLGIDIN 186
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
912-941 |
1.53e-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: 1.53e-03
10 20 30
....*....|....*....|....*....|
gi 62988328 912 DGRNALRVAALEGHRDIVELLFSHGADVNC 941
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
22-195 |
1.65e-03 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433025 [Multi-domain] Cd Length: 167 Bit Score: 40.95 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 22 QFYCREWVFHKLQHCLQeksnccnsAVNAPSLVMnsgnnasgvsgkgaawgVLLVGGPGSGKTALCTELLwpsspaslqR 101
Cdd:pfam13191 1 RLVGREEELEQLLDALD--------RVRSGRPPS-----------------VLLTGEAGTGKTTLLRELL---------R 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 102 GLHRQALAFHFCKAQD-------SDTLCVGGFIRGLVAQIcRSGLLQGYEDKLRDPAVQSLLQPGECERNPAEAFKRCVL 174
Cdd:pfam13191 47 ALERDGGYFLRGKCDEnlpysplLEALTREGLLRQLLDEL-ESSLLEAWRAALLEALAPVPELPGDLAERLLDLLLRLLD 125
|
170 180
....*....|....*....|.
gi 62988328 175 LPllgmKPPQQSLYLLVDSVD 195
Cdd:pfam13191 126 LL----ARGERPLVLVLDDLQ 142
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
1026-1110 |
1.66e-03 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 42.73 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 1026 KVVQLLIEHGAVVDHTCNQGATALCIAAQEGHIDVVQVLLEHGADPNHADQFGRTAMRVAAKNGHSQI--IKLLEKYGAS 1103
Cdd:PHA02946 53 RFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIerINLLVQYGAK 132
|
90
....*....|..
gi 62988328 1104 SLN-----GCSP 1110
Cdd:PHA02946 133 INNsvdeeGCGP 144
|
|
| PHA02795 |
PHA02795 |
ankyrin-like protein; Provisional |
538-589 |
1.81e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165157 [Multi-domain] Cd Length: 437 Bit Score: 42.67 E-value: 1.81e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 62988328 538 VNQCDSNGRTLLANAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLAARQG 589
Cdd:PHA02795 214 INQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRG 265
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
710-869 |
2.45e-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: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 710 GRTALSVAALCVpaSKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGH-----------VDVVDLLLEGGADVdHTD 778
Cdd:cd21882 26 GKTCLHKAALNL--NDGVNEAIMLLLEAAPDSGNPKELVNAPCTDEFYQGQtalhiaienrnLNLVRLLVENGADV-SAR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 779 NNGRT--------------PLLAAASMGHASVVNTLLFWG---AAVDSIDSEGRTVLSIASAQGNVEVVRTLL------- 834
Cdd:cd21882 103 ATGRFfrkspgnlfyfgelPLSLAACTNQEEIVRLLLENGaqpAALEAQDSLGNTVLHALVLQADNTPENSAFvcqmynl 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 62988328 835 ----DRGLDE--------NHRddaGWTPLHMAAFEGHRLICEALIEQ 869
Cdd:cd21882 183 llsyGAHLDPtqqleeipNHQ---GLTPLKLAAVEGKIVMFQHILQR 226
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
833-887 |
2.93e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 37.33 E-value: 2.93e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 62988328 833 LLDRG-LDENHRDDAGWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIPFILA 887
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
780-811 |
3.38e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 36.50 E-value: 3.38e-03
10 20 30
....*....|....*....|....*....|...
gi 62988328 780 NGRTPL-LAAASMGHASVVNTLLFWGAAVDSID 811
Cdd:pfam00023 1 DGNTPLhLAAGRRGNLEIVKLLLSKGADVNARD 33
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
545-615 |
3.60e-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: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 545 GRTLLANAAYSGSLDVVNLLVSRGADLEIEDA--------------HGHTPLTLAARQGHTKVVNCLIGCGANINHTDQD 610
Cdd:cd22192 89 GETALHIAVVNQNLNLVRELIARGADVVSPRAtgtffrpgpknliyYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168
|
....*
gi 62988328 611 GWTAL 615
Cdd:cd22192 169 GNTVL 173
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
492-588 |
4.34e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 41.40 E-value: 4.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 492 KEQEVLQLLVKAGAHVNSEDDRTSCIVRQALE--REDSIRTLLDNGASVNQCDSNGRTLL-------------------- 549
Cdd:PHA02878 179 KDQRLTELLLSYGANVNIPDKTNNSPLHHAVKhyNKPIVHILLENGASTDARDKCGNTPLhisvgyckdydilklllehg 258
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 62988328 550 --ANAAYS-----------GSLDVVNLLVSRGADLEIEDAHGHTPLTLAARQ 588
Cdd:PHA02878 259 vdVNAKSYilgltalhssiKSERKLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
1025-1101 |
5.13e-03 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 41.39 E-value: 5.13e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62988328 1025 VKVVQLLIEHGAvvDHTCNQGATALCIAAQEGHIDVVQVLLEHGADPNHADQFGRTAMRVAAKNGHSQIIKLLEKYG 1101
Cdd:PLN03192 507 LNVGDLLGDNGG--EHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA 581
|
|
| PHA02795 |
PHA02795 |
ankyrin-like protein; Provisional |
992-1100 |
5.13e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165157 [Multi-domain] Cd Length: 437 Bit Score: 41.13 E-value: 5.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 992 MEMVQVLIAYHADVNAADNEKRSALQSAAWQGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQEG--------HIDVVQV 1063
Cdd:PHA02795 201 LEIYKLCIPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRGsviarretHLKILEI 280
|
90 100 110
....*....|....*....|....*....|....*..
gi 62988328 1064 LLEhgaDPNHADQFGRTAMRVAAKNghSQIIKLLEKY 1100
Cdd:PHA02795 281 LLR---EPLSIDCIKLAILNNTIEN--HDVIKLCIKY 312
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
847-871 |
5.50e-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: 5.50e-03
10 20
....*....|....*....|....*
gi 62988328 847 GWTPLHMAAFEGHRLICEALIEQGA 871
Cdd:pfam13606 2 GNTPLHLAARNGRLEIVKLLLENGA 26
|
|
| PHA02795 |
PHA02795 |
ankyrin-like protein; Provisional |
708-812 |
5.94e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165157 [Multi-domain] Cd Length: 437 Bit Score: 40.75 E-value: 5.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 708 VDGRTALSVAALCVPASKghasvvsllidrgaEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLA 787
Cdd:PHA02795 195 VDEPTVLEIYKLCIPYIE--------------DINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDV 260
|
90 100 110
....*....|....*....|....*....|...
gi 62988328 788 AASMG--------HASVVNTLLFWGAAVDSIDS 812
Cdd:PHA02795 261 AVDRGsviarretHLKILEILLREPLSIDCIKL 293
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
493-584 |
6.36e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 39.80 E-value: 6.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 493 EQEVLQLLVKAGAHVNSEDDRTSCIVRQALE----REDSIRTLLDNGASVNQCDSNGRTLLAN-AAYSGSLDVVNLLVSR 567
Cdd:PHA02859 102 EPEILKILIDSGSSITEEDEDGKNLLHMYMCnfnvRINVIKLLIDSGVSFLNKDFDNNNILYSyILFHSDKKIFDFLTSL 181
|
90
....*....|....*..
gi 62988328 568 GADLEIEDAHGHTPLTL 584
Cdd:PHA02859 182 GIDINETNKSGYNCYDL 198
|
|
| PHA02716 |
PHA02716 |
CPXV016; CPX019; EVM010; Provisional |
682-852 |
6.57e-03 |
|
CPXV016; CPX019; EVM010; Provisional
Pssm-ID: 165089 [Multi-domain] Cd Length: 764 Bit Score: 41.05 E-value: 6.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 682 IAAAYMGHR----EIVEHLLDHGAEVNHEDVDGRTALSVAALCVPASkghASVVSLLIDRGAEVDHCDKDGMTPLLvaAY 757
Cdd:PHA02716 180 ILHAYLGNMyvdiDILEWLCNNGVNVNLQNNHLITPLHTYLITGNVC---ASVIKKIIELGGDMDMKCVNGMSPIM--TY 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 758 EGHVDVVDLLLEgGADVDHTDNNGRT--PLLAAASMGHA-----SVVNTLLFWGAAVDSIDSEGRTVLS--IASAQGNVE 828
Cdd:PHA02716 255 IINIDNINPEIT-NIYIESLDGNKVKniPMILHSYITLArnidiSVVYSFLQPGVKLHYKDSAGRTCLHqyILRHNISTD 333
|
170 180
....*....|....*....|....
gi 62988328 829 VVRTLLDRGLDENHRDDAGWTPLH 852
Cdd:PHA02716 334 IIKLLHEYGNDLNEPDNIGNTVLH 357
|
|
| PHA02795 |
PHA02795 |
ankyrin-like protein; Provisional |
669-777 |
6.70e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165157 [Multi-domain] Cd Length: 437 Bit Score: 40.75 E-value: 6.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 669 EVNKADNEGRTALIAAAYMGHREIVEHLLDHGAEVNHEDVDGRTALSVA---ALCVPASKGHASVVSLLIDRGAEVDhCD 745
Cdd:PHA02795 213 DINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAvdrGSVIARRETHLKILEILLREPLSID-CI 291
|
90 100 110
....*....|....*....|....*....|..
gi 62988328 746 KdgmTPLLVAAYEGHvDVVDLLLEGGADVDHT 777
Cdd:PHA02795 292 K---LAILNNTIENH-DVIKLCIKYFMMVDYS 319
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
927-1047 |
6.84e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 39.42 E-value: 6.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 927 DIVELLFSHGADVNCKDADGRPTL---YILALEN-QLTMAEYFLENGANVEASDAEGRTALHV--SCWQGHMEMVQVLIA 1000
Cdd:PHA02859 67 EILKFLIENGADVNFKTRDNNLSAlhhYLSFNKNvEPEILKILIDSGSSITEEDEDGKNLLHMymCNFNVRINVIKLLID 146
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 62988328 1001 YHADVNAADNEKRSALQS-AAWQGHVKVVQLLIEHGAVVDHTCNQGAT 1047
Cdd:PHA02859 147 SGVSFLNKDFDNNNILYSyILFHSDKKIFDFLTSLGIDINETNKSGYN 194
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
879-907 |
6.96e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 35.64 E-value: 6.96e-03
10 20
....*....|....*....|....*....
gi 62988328 879 DGRIPFILASQEGHYDCVQILLENKSNID 907
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
|
|
| TRPV2 |
cd22197 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ... |
710-843 |
7.15e-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: 40.99 E-value: 7.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 710 GRTALSVAAlcvpaSKGHASVVSLLIDRGAEV-------------DHCDKDGMTPLLVAAYEGHVDVVDLLLEGGAD--- 773
Cdd:cd22197 94 GHSALHIAI-----EKRSLQCVKLLVENGADVharacgrffqkkqGTCFYFGELPLSLAACTKQWDVVNYLLENPHQpas 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 774 VDHTDNNGRTPLLAAASMGHASVVNT---------LLFWGAAVDS-------IDSEGRTVLSIASAQGNVEVVRTLLDRG 837
Cdd:cd22197 169 LQAQDSLGNTVLHALVMIADNSPENSalvikmydgLLQAGARLCPtvqleeiSNHEGLTPLKLAAKEGKIEIFRHILQRE 248
|
....*.
gi 62988328 838 LDENHR 843
Cdd:cd22197 249 FSGPYQ 254
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
865-1066 |
7.72e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411978 [Multi-domain] Cd Length: 680 Bit Score: 40.90 E-value: 7.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 865 ALIEQGARTNEIdndgrIPFILASQEGHyDCVQILLEnkSNIDQRGYDGRNALRVAALEGHRDIVELLFSHGADVNCKdA 944
Cdd:cd22194 101 ALLNINENTKEI-----VRILLAFAEEN-GILDRFIN--AEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAH-A 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 945 DGR---PT------------LYILALENQLTMAEYFLENGANVEAS-DAEGRTALhvscwqghmemvqvliayHADVNAA 1008
Cdd:cd22194 172 KGVffnPKykhegfyfgetpLALAACTNQPEIVQLLMEKESTDITSqDSRGNTVL------------------HALVTVA 233
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62988328 1009 DNekrsalqSAAWQGHVKVV--QLLIEHG--AVVDHTCNQGATALCIAAQEGHIDVVQVLLE 1066
Cdd:cd22194 234 ED-------SKTQNDFVKRMydMILLKSEnkNLETIRNNEGLTPLQLAAKMGKAEILKYILS 288
|
|
| PHA02716 |
PHA02716 |
CPXV016; CPX019; EVM010; Provisional |
730-941 |
7.79e-03 |
|
CPXV016; CPX019; EVM010; Provisional
Pssm-ID: 165089 [Multi-domain] Cd Length: 764 Bit Score: 40.67 E-value: 7.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 730 VVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHV--DVVDLLLEGGADVDHTDNNGRTPLLAaaSMGHASVVNTLLFwGAAV 807
Cdd:PHA02716 194 ILEWLCNNGVNVNLQNNHLITPLHTYLITGNVcaSVIKKIIELGGDMDMKCVNGMSPIMT--YIINIDNINPEIT-NIYI 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 808 DSIDSEGRT------VLSIASAQG-NVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEgHRL---ICEALIEQGARTNEID 877
Cdd:PHA02716 271 ESLDGNKVKnipmilHSYITLARNiDISVVYSFLQPGVKLHYKDSAGRTCLHQYILR-HNIstdIIKLLHEYGNDLNEPD 349
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62988328 878 NDGRIpfILASQEGHYDCVQILlenKSNIDqrgydgrNALRVaaleghrDIVELLFSHGAD---VNC 941
Cdd:PHA02716 350 NIGNT--VLHTYLSMLSVVNIL---DPETD-------NDIRL-------DVIQCLISLGADitaVNC 397
|
|
| PHA02989 |
PHA02989 |
ankyrin repeat protein; Provisional |
894-985 |
8.55e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222954 [Multi-domain] Cd Length: 494 Bit Score: 40.49 E-value: 8.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 894 DCVQILLENKSNIDQRGYDGR---NALRVAALEGH--RDIVELLFSHGADVNCKDADGRPTLYILALE---NQLTMAEYF 965
Cdd:PHA02989 51 KIVKLLIDNGADVNYKGYIETplcAVLRNREITSNkiKKIVKLLLKFGADINLKTFNGVSPIVCFIYNsniNNCDMLRFL 130
|
90 100
....*....|....*....|.
gi 62988328 966 LENGANV-EASDAEGRTALHV 985
Cdd:PHA02989 131 LSKGINVnDVKNSRGYNLLHM 151
|
|
| PHA02716 |
PHA02716 |
CPXV016; CPX019; EVM010; Provisional |
729-851 |
8.55e-03 |
|
CPXV016; CPX019; EVM010; Provisional
Pssm-ID: 165089 [Multi-domain] Cd Length: 764 Bit Score: 40.67 E-value: 8.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 729 SVVSLLIDRGAEVDHCDKDGMTPL--LVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMghASVVNTLlfwgaa 806
Cdd:PHA02716 298 SVVYSFLQPGVKLHYKDSAGRTCLhqYILRHNISTDIIKLLHEYGNDLNEPDNIGNTVLHTYLSM--LSVVNIL------ 369
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90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 62988328 807 vdsiDSEGRTVLsiasaqgNVEVVRTLLDRGLDENHRDDAGWTPL 851
Cdd:PHA02716 370 ----DPETDNDI-------RLDVIQCLISLGADITAVNCLGYTPL 403
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|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
645-675 |
9.51e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 35.34 E-value: 9.51e-03
10 20 30
....*....|....*....|....*....|..
gi 62988328 645 RTAL-RAAAWGGHEDIVLNLLQHGAEVNKADN 675
Cdd:pfam00023 3 NTPLhLAAGRRGNLEIVKLLLSKGADVNARDK 34
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
1064-1103 |
9.74e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 35.79 E-value: 9.74e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 62988328 1064 LLEHG-ADPNHADQFGRTAMRVAAKNGHSQIIKLLEKYGAS 1103
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVD 41
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