|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
558-851 |
6.57e-63 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 216.36 E-value: 6.57e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 558 LDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGHTEVVSALLYAGVKV 637
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 638 DCADADSRTALRAAAWGGHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLDHGAEVNHEDVDGRTALSVA 717
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 718 alcvpASKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVV 797
Cdd:COG0666 161 -----AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIV 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 568921145 798 NTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDESHRDDAGWTPL 851
Cdd:COG0666 236 KLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
629-917 |
2.87e-60 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 209.04 E-value: 2.87e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 629 ALLYAGVKVDCADADSRTALRAAAWGGHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLDHGAEVNHEDV 708
Cdd:COG0666 6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 709 DGRTALSVAAlcvpaSKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAA 788
Cdd:COG0666 86 GGNTLLHAAA-----RNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 789 ASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDESHRDDAGWTPLHMAAFEGHRLICEALIE 868
Cdd:COG0666 161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 568921145 869 QGARTNEIDNDGRIPFILASQEGHYDCVQILLENKSNIDQRGYDGRNAL 917
Cdd:COG0666 241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
833-1102 |
4.46e-60 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 208.27 E-value: 4.46e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 833 LLDRGLDESHRDDAGWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIPFILASQEGHYDCVQILLENKSNIDQRGYD 912
Cdd:COG0666 7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 913 GRNALRVAALEGHRDIVELLFSHGADVNYKDADGRPTLYILALENQLTMAEYFLENGANVEASDAEGRTALHVSCWQGHV 992
Cdd:COG0666 87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 993 EMVRVLIACHADVNAADNEKRSALQSAAWQGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQEGHVDVVQVLLEHGADPN 1072
Cdd:COG0666 167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246
|
250 260 270
....*....|....*....|....*....|
gi 568921145 1073 HADQFGRTAMRVAAKNGHSQIIKLLEKYGA 1102
Cdd:COG0666 247 AKDKDGLTALLLAAAAGAALIVKLLLLALL 276
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
531-818 |
3.21e-59 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 205.96 E-value: 3.21e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 531 LLDNGASVNQCDSNGRTLLANAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLIGCGANINHTDQD 610
Cdd:COG0666 7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 611 GWTALRSAAWGGHTEVVSALLYAGVKVDCADADSRTALRAAAWGGHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHR 690
Cdd:COG0666 87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 691 EIVEHLLDHGAEVNHEDVDGRTALSVAalcvpASKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEG 770
Cdd:COG0666 167 EIVKLLLEAGADVNARDNDGETPLHLA-----AENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 568921145 771 GADVDHTDNNGRTPLLAAASMGHASVVNTLLFWGAAVDSIDSEGRTVL 818
Cdd:COG0666 242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
861-1102 |
4.20e-58 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 202.49 E-value: 4.20e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 861 LICEALIEQGARTNEIDNDGRIPFILASQEGHYDCVQILLENKSNIDQRGYDGRNALRVAALEGHRDIVELLFSHGADVN 940
Cdd:COG0666 2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 941 YKDADGRPTLYILALENQLTMAEYFLENGANVEASDAEGRTALHVSCWQGHVEMVRVLIACHADVNAADNEKRSALQSAA 1020
Cdd:COG0666 82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 1021 WQGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQEGHVDVVQVLLEHGADPNHADQFGRTAMRVAAKNGHSQIIKLLEKY 1100
Cdd:COG0666 162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
|
..
gi 568921145 1101 GA 1102
Cdd:COG0666 242 GA 243
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
495-752 |
9.93e-56 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 195.94 E-value: 9.93e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 495 EVLQLLIRAGAHVNSEDDHTSCIVRQALEREDSIRTLLDNGASVNQCDSNGRTLLANAAYSGSLDVVNLLVSRGADLEIE 574
Cdd:COG0666 37 LLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNAR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 575 DAHGHTPLTLAARQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGHTEVVSALLYAGVKVDCADADSRTALRAAAWG 654
Cdd:COG0666 117 DKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAEN 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 655 GHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLDHGAEVNHEDVDGRTALSVAALcvpasKGHASVVSLL 734
Cdd:COG0666 197 GHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAA-----AGAALIVKLL 271
|
250
....*....|....*...
gi 568921145 735 IDRGAEVDHCDKDGMTPL 752
Cdd:COG0666 272 LLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
728-1016 |
3.77e-54 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 191.32 E-value: 3.77e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 728 ASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLLFWGAAV 807
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 808 DSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDESHRDDAGWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIPFILA 887
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 888 SQEGHYDCVQILLENKSNIDQRGYDGRNALRVAALEGHRDIVELLFSHGADVNYKDADGRPTLYILALENQLTMAEYFLE 967
Cdd:COG0666 161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 568921145 968 NGANVEASDAEGRTALHVSCWQGHVEMVRVLIACHADVNAADNEKRSAL 1016
Cdd:COG0666 241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
707-983 |
5.92e-54 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 190.55 E-value: 5.92e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 707 DVDGRTALSVAALCVPASKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLL 786
Cdd:COG0666 13 AALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 787 AAASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDESHRDDAGWTPLHMAAFEGHRLICEAL 866
Cdd:COG0666 93 AAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 867 IEQGARTNEIDNDGRIPFILASQEGHYDCVQILLENKSNIDQRGYDGRNALRVAALEGHRDIVELLFSHGADVNYKDADG 946
Cdd:COG0666 173 LEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDG 252
|
250 260 270
....*....|....*....|....*....|....*..
gi 568921145 947 RPTLYILALENQLTMAEYFLENGANVEASDAEGRTAL 983
Cdd:COG0666 253 LTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
761-1049 |
6.68e-53 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 187.85 E-value: 6.68e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 761 VDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDE 840
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 841 SHRDDAGWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIPFILASQEGHYDCVQILLENKSNIDQRGYDGRNALRVA 920
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 921 ALEGHRDIVELLFSHGADVNYKDADGRPTLYILALENQLTMAEYFLENGANVEASDAEGRTALHVSCWQGHVEMVRVLIA 1000
Cdd:COG0666 161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 568921145 1001 CHADVNAADNEKRSALQSAAWQGHVKVVQLLIEHGAVVDHTCNQGATAL 1049
Cdd:COG0666 241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
443-714 |
4.33e-51 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 182.46 E-value: 4.33e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 443 QARNLTPLEAQEFALHLINSNLQLEPAELALWMIWNGTPVKDSLSTLIPKEQEVLQLLIRAGAHVNSEDDHTSCIVRQAL 522
Cdd:COG0666 16 LLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 523 E--REDSIRTLLDNGASVNQCDSNGRTLLANAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLIGC 600
Cdd:COG0666 96 RngDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 601 GANINHTDQDGWTALRSAAWGGHTEVVSALLYAGVKVDCADADSRTALRAAAWGGHEDIVLNLLQHGAEVNKADNEGRTA 680
Cdd:COG0666 176 GADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTA 255
|
250 260 270
....*....|....*....|....*....|....
gi 568921145 681 LIAAAYMGHREIVEHLLDHGAEVNHEDVDGRTAL 714
Cdd:COG0666 256 LLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
625-907 |
1.12e-35 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 142.47 E-value: 1.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 625 EVVSALLYAGVKVDCADADSRTALRAAAWGGHE---DIVLNLLQHGAEVNKADNEGRTALIAaaYMGH---REIVEHLLD 698
Cdd:PHA03095 28 EEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEkvkDIVRLLLEAGADVNAPERCGFTPLHL--YLYNattLDVIKLLIK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 699 HGAEVNHEDVDGRTALSVAaLCVPASkgHASVVSLLIDRGAEVDHCDKDGMTPL--LVAAYEGHVDVVDLLLEGGADVDH 776
Cdd:PHA03095 106 AGADVNAKDKVGRTPLHVY-LSGFNI--NPKVIRLLLRKGADVNALDLYGMTPLavLLKSRNANVELLRLLIDAGADVYA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 777 TDNNGRTPL--LAAASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVE--VVRTLLDRGLDESHRDDAGWTPLH 852
Cdd:PHA03095 183 VDDRFRSLLhhHLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLH 262
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 568921145 853 MAAFEGHRLICEALIEQGARTNEIDNDGRIPFILASQEGHYDCVQILLENKSNID 907
Cdd:PHA03095 263 YAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAE 317
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
558-900 |
6.13e-31 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 131.34 E-value: 6.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 558 LDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGHTEVVSALLYAGVKV 637
Cdd:PHA02876 158 LLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNI 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 638 DCADADSRTALRaaawggHEDIVLNLLQH--GAEVNKADNEGRTALIAAAYMGH-REIVEHLLDHGAEVNHEDVDGRTAL 714
Cdd:PHA02876 238 NKNDLSLLKAIR------NEDLETSLLLYdaGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 715 SVAalcvpASKGHASV-VSLLIDRGAEVDHCDKDGMTPLLVAA-YEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMG 792
Cdd:PHA02876 312 YLM-----AKNGYDTEnIRTLIMLGADVNAADRLYITPLHQAStLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRN 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 793 HASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEV-VRTLLDRGLDESHRDDAGWTPLHMAAFEGHRL-ICEALIEQG 870
Cdd:PHA02876 387 NVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVNSKNKDLSTPLHYACKKNCKLdVIEMLLDNG 466
|
330 340 350
....*....|....*....|....*....|
gi 568921145 871 ARTNEIDNDGRIPFILASqeGHYDCVQILL 900
Cdd:PHA02876 467 ADVNAINIQNQYPLLIAL--EYHGIVNILL 494
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
524-801 |
2.73e-30 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 126.68 E-value: 2.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 524 REDSIRTLLDNGASVNQCDSNGRTLLA---NAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHT-KVVNCLIG 599
Cdd:PHA03095 26 TVEEVRRLLAAGADVNFRGEYGKTPLHlylHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 600 CGANINHTDQDGWTALrSAAWGG---HTEVVSALLYAGVKVDCADADSRTALRAAAWGGHEDI-VLNLL-QHGAEVNKAD 674
Cdd:PHA03095 106 AGADVNAKDKVGRTPL-HVYLSGfniNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVeLLRLLiDAGADVYAVD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 675 NEGRTAL-IAAAYMGHRE-IVEHLLDHGAEVNHEDVDGRTALSVAALcvpASKGHASVVSLLIDRGAEVDHCDKDGMTPL 752
Cdd:PHA03095 185 DRFRSLLhHHLQSFKPRArIVRELIRAGCDPAATDMLGNTPLHSMAT---GSSCKRSLVLPLLIAGISINARNRYGQTPL 261
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 568921145 753 LVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLL 801
Cdd:PHA03095 262 HYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
686-986 |
5.14e-28 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 118.91 E-value: 5.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 686 YMGHREIVEHLLDHGAEVNHEDVDGRTALSVAALcvpaSKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVD 765
Cdd:PHA02874 10 YSGDIEAIEKIIKNKGNCINISVDETTTPLIDAI----RSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 766 LLLEGGADvdhtdnngrTPLLAAASMgHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDESHRDD 845
Cdd:PHA02874 86 LLIDNGVD---------TSILPIPCI-EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 846 AGWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIPFILASQEGHYDCVQILLENKSNIDQRGYDGRNALRVAALEgH 925
Cdd:PHA02874 156 NGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIH-N 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568921145 926 RDIVELLFSHgADVNYKDADG-RPTLYILALENQLTMAEYFLENGANVEASDAEGRTALHVS 986
Cdd:PHA02874 235 RSAIELLINN-ASINDQDIDGsTPLHHAINPPCDIDIIDILLYHKADISIKDNKGENPIDTA 295
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
480-717 |
3.49e-27 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 117.05 E-value: 3.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 480 TPVKDSLSTLIPKEQEVLQLLIRAGAHVNSEDD------HtsCIVRQAlEREDSIRTLLDNGASVNQCDSNGRTLLanAA 553
Cdd:PHA03095 49 TPLHLYLHYSSEKVKDIVRLLLEAGADVNAPERcgftplH--LYLYNA-TTLDVIKLLIKAGADVNAKDKVGRTPL--HV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 554 YSGSL----DVVNLLVSRGADLEIEDAHGHTPLT--LAARQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGHT--E 625
Cdd:PHA03095 124 YLSGFninpKVIRLLLRKGADVNALDLYGMTPLAvlLKSRNANVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPraR 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 626 VVSALLYAGVKVDCADADSRTALRAAAWGGHED--IVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLDHGAEV 703
Cdd:PHA03095 204 IVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADI 283
|
250
....*....|....
gi 568921145 704 NHEDVDGRTALSVA 717
Cdd:PHA03095 284 NAVSSDGNTPLSLM 297
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
557-851 |
1.44e-26 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 115.12 E-value: 1.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 557 SLDVVNLLVSRGADLEIEDAHGHTPLTLAARQGH---TKVVNCLIGCGANINHTDQDGWTALRSAAWGGHTE-VVSALLY 632
Cdd:PHA03095 26 TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 633 AGVKVDCADADSRTALRAAAWGG--HEDIVLNLLQHGAEVNKADNEGRTALiaAAYMGHR----EIVEHLLDHGAEVNHE 706
Cdd:PHA03095 106 AGADVNAKDKVGRTPLHVYLSGFniNPKVIRLLLRKGADVNALDLYGMTPL--AVLLKSRnanvELLRLLIDAGADVYAV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 707 DVDGRTALSVAALCVpasKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVD--VVDLLLEGGADVDHTDNNGRTP 784
Cdd:PHA03095 184 DDRFRSLLHHHLQSF---KPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTP 260
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568921145 785 LLAAAsmghasvvntllfwgaavdsidsegrtvlsiasAQGNVEVVRTLLDRGLDESHRDDAGWTPL 851
Cdd:PHA03095 261 LHYAA---------------------------------VFNNPRACRRLIALGADINAVSSDGNTPL 294
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
763-1102 |
6.58e-26 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 115.16 E-value: 6.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 763 VVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDESH 842
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINK 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 843 RDDAGWTPLHMAAFEGHRLiceaLIEQGARTNEIDNDGRIPFILASQEGHYD-CVQILLENKSNIDQRGYDGRNALRVAA 921
Cdd:PHA02876 240 NDLSLLKAIRNEDLETSLL----LYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMA 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 922 LEGH-RDIVELLFSHGADVNYKDadgrpTLYILALENQLTMAEY------FLENGANVEASDAEGRTALHVSCWQGHVEM 994
Cdd:PHA02876 316 KNGYdTENIRTLIMLGADVNAAD-----RLYITPLHQASTLDRNkdivitLLELGANVNARDYCDKTPIHYAAVRNNVVI 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 995 VRVLIACHADVNAADNEKRSALQSAAWQGHVKV-VQLLIEHGAVVDHTCNQGATALCIAAQEG-HVDVVQVLLEHGADPN 1072
Cdd:PHA02876 391 INTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVN 470
|
330 340 350
....*....|....*....|....*....|
gi 568921145 1073 HADQFGRTAMRVAAknGHSQIIKLLEKYGA 1102
Cdd:PHA02876 471 AINIQNQYPLLIAL--EYHGIVNILLHYGA 498
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
658-1010 |
1.05e-25 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 112.43 E-value: 1.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 658 DIVLNLLQHGAEVNKADNEGRTALiaAAYMGHR-----EIVEHLLDHGAEVNHEDVDGRTALSvaalCVPASKGHASVVS 732
Cdd:PHA03095 28 EEVRRLLAAGADVNFRGEYGKTPL--HLYLHYSsekvkDIVRLLLEAGADVNAPERCGFTPLH----LYLYNATTLDVIK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 733 LLIDRGAEVDHCDKDGMTPLLV--AAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASV--VNTLLFWGAAVD 808
Cdd:PHA03095 102 LLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVY 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 809 SIDSEGRTVLSI--ASAQGNVEVVRTLLDRGLDESHRDDAGWTPLHMAAFEGHrliCEALIEQgartneidndgriPFIL 886
Cdd:PHA03095 182 AVDDRFRSLLHHhlQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSS---CKRSLVL-------------PLLI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 887 AsqeghydcvqillenksnidqrgydgrnalrvaaleghrdivellfshGADVNYKDADGRPTLYILALENQLTMAEYFL 966
Cdd:PHA03095 246 A------------------------------------------------GISINARNRYGQTPLHYAAVFNNPRACRRLI 277
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 568921145 967 ENGANVEASDAEGRTALHVSCWQGHVEMVRVLIACHADVNAADN 1010
Cdd:PHA03095 278 ALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAA 321
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
862-1103 |
9.59e-25 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 108.98 E-value: 9.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 862 ICEALIEQGARTNEIDNDGRIPFILASQEGHydcvqillenksnidqrgydgrNALRVaaleghRDIVELLFSHGADVNY 941
Cdd:PHA03100 50 VVKILLDNGADINSSTKNNSTPLHYLSNIKY----------------------NLTDV------KEIVKLLLEYGANVNA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 942 KDADGRPTLYILALE--NQLTMAEYFLENGANVEASDAEGRTALH--VSCWQGHVEMVRVLIACHADVNAADNekrsalq 1017
Cdd:PHA03100 102 PDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHlyLESNKIDLKILKLLIDKGVDINAKNR------- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 1018 saawqghvkvVQLLIEHGAVVDHTCNQGATALCIAAQEGHVDVVQVLLEHGADPNHADQFGRTAMRVAAKNGHSQIIKLL 1097
Cdd:PHA03100 175 ----------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLL 244
|
....*.
gi 568921145 1098 EKYGAS 1103
Cdd:PHA03100 245 LNNGPS 250
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
625-842 |
5.69e-24 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 106.67 E-value: 5.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 625 EVVSALLYAGVKVDCADADSRTALRAAAWGGHE-----DIVLNLLQHGAEVNKADNEGRTALIAAAY--MGHREIVEHLL 697
Cdd:PHA03100 49 DVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISkkSNSYSIVEYLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 698 DHGAEVNHEDVDGRTALSVAALCVPASKghaSVVSLLIDRGAEVDHCDKdgmtpllvaayeghvdvVDLLLEGGADVDHT 777
Cdd:PHA03100 129 DNGANVNIKNSDGENLLHLYLESNKIDL---KILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIK 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568921145 778 DNNGRTPLLAAASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDESH 842
Cdd:PHA03100 189 DVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
820-1095 |
6.14e-24 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 107.03 E-value: 6.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 820 IASAQGNVEVVRTLLDRGLDESHRDDAGWTPLH--MAAFEGHRL-ICEALIEQGARTNEIDNDGRIPFIL----ASQEgh 892
Cdd:PHA03095 20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHlyLHYSSEKVKdIVRLLLEAGADVNAPERCGFTPLHLylynATTL-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 893 yDCVQILLENKSNIDQRGYDGRNALRV--AALEGHRDIVELLFSHGADVNYKDADGRPTLYILALENQLTMA--EYFLEN 968
Cdd:PHA03095 98 -DVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVEllRLLIDA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 969 GANVEASDAEGRTALHVscwqgHVE-------MVRVLIACHADVNAADNEKRSALQSAAWQGHVK--VVQLLIEHGAVVD 1039
Cdd:PHA03095 177 GADVYAVDDRFRSLLHH-----HLQsfkprarIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISIN 251
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 568921145 1040 HTCNQGATALCIAAQEGHVDVVQVLLEHGADPNHADQFGRTAMRVAAKNGHSQIIK 1095
Cdd:PHA03095 252 ARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVR 307
|
|
| 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 568921145 606 HTDQDGWTALRSAAWGGHTEVVSALLYAGVKVDCADADSRTALRAAAWGGHEDIVLNLLQHGAEVNKADNEGRTALIAAA 685
Cdd:PLN03192 520 HDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAI 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 686 YMGHREIVeHLLDHGAEVNHEDVDGRTalsvaaLCVPASKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVD 765
Cdd:PLN03192 600 SAKHHKIF-RILYHFASISDPHAAGDL------LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVR 672
|
170 180 190
....*....|....*....|....*....|....*...
gi 568921145 766 LLLEGGADVDHTD-NNGRTP-----LLAAASMGHASVV 797
Cdd:PLN03192 673 LLIMNGADVDKANtDDDFSPtelreLLQKRELGHSITI 710
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
554-854 |
1.03e-22 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 103.12 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 554 YSGSLDVV-NLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGHTEVVSALLY 632
Cdd:PHA02874 10 YSGDIEAIeKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLID 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 633 AGVK-----VDCADadsrtalraaawgghEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLDHGAEVNHED 707
Cdd:PHA02874 90 NGVDtsilpIPCIE---------------KDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIED 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 708 VDGRTALSVAalcvpASKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLA 787
Cdd:PHA02874 155 DNGCYPIHIA-----IKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHN 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568921145 788 AasMGHASVVNTLLFWGAAVDSIDSEGRTVLSIA-SAQGNVEVVRTLLDRGLDESHRDDAGWTPLHMA 854
Cdd:PHA02874 230 A--IIHNRSAIELLINNASINDQDIDGSTPLHHAiNPPCDIDIIDILLYHKADISIKDNKGENPIDTA 295
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
983-1075 |
3.16e-22 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 92.10 E-value: 3.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 983 LHVSCWQGHVEMVRVLIACHADVNAADNEKRSALQSAAWQGHVKVVQLLIEHGAVVDhtCNQGATALCIAAQEGHVDVVQ 1062
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 568921145 1063 VLLEHGADPNHAD 1075
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
526-788 |
7.07e-22 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 100.42 E-value: 7.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 526 DSIRT--------LLDNGASVNQCDSNGRTLLANAAYSGSLDVVNLLVSRGADLEIedahghtpltLAARQGHTKVVNCL 597
Cdd:PHA02874 41 DAIRSgdakivelFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSI----------LPIPCIEKDMIKTI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 598 IGCGANINHTDQDGWTALRSAAWGGHTEVVSALLYAGVKVDCADADSRTALRAAAWGGHEDIVLNLLQHGAEVNKADNEG 677
Cdd:PHA02874 111 LDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 678 RTALIAAAYMGHREIVEHLLDHGAEVNHEDVDGRTALSVAALcvpaskGHASVVSLLIDrGAEVDHCDKDGMTPLLVA-A 756
Cdd:PHA02874 191 ESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII------HNRSAIELLIN-NASINDQDIDGSTPLHHAiN 263
|
250 260 270
....*....|....*....|....*....|..
gi 568921145 757 YEGHVDVVDLLLEGGADVDHTDNNGRTPLLAA 788
Cdd:PHA02874 264 PPCDIDIIDILLYHKADISIKDNKGENPIDTA 295
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
851-943 |
1.87e-21 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 90.18 E-value: 1.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 851 LHMAAFEGHRLICEALIEQGARTNEIDNDGRIPFILASQEGHYDCVQILLENKsNIDQRGYdGRNALRVAALEGHRDIVE 930
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKDN-GRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 568921145 931 LLFSHGADVNYKD 943
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
826-1044 |
2.60e-21 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 98.58 E-value: 2.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 826 NVEVVRTLLDRGLDESHRDDAGWTPLHMAAFEGHRL-----ICEALIEQGARTNEIDNDGRIP-FILASQE-GHYDCVQI 898
Cdd:PHA03100 47 NIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLtdvkeIVKLLLEYGANVNAPDNNGITPlLYAISKKsNSYSIVEY 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 899 LLENKSNIDQRGYDGRNALRVAALEGHRD--IVELLFSHGADVNYKDAdgrptlyilalenqltmAEYFLENGANVEASD 976
Cdd:PHA03100 127 LLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKD 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568921145 977 AEGRTALHVSCWQGHVEMVRVLIACHADVNAADNEKRSALQSAAWQGHVKVVQLLIEHGAVVDHTCNQ 1044
Cdd:PHA03100 190 VYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
718-940 |
3.39e-20 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 95.06 E-value: 3.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 718 ALCVPASKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVV 797
Cdd:PHA02875 5 ALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 798 NTLLFWGA-AVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDESHRDDAGWTPLHMAAFEGHRLICEALIEQGARTNEI 876
Cdd:PHA02875 85 EELLDLGKfADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568921145 877 DNDGRIPFILASQEGHYDCVQILLENKSNIDQRGYDGRNALRVAALEGHR-DIVELLFSHGADVN 940
Cdd:PHA02875 165 DCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKiDIVRLFIKRGADCN 229
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
891-1104 |
2.39e-19 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 92.36 E-value: 2.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 891 GHYDCVQILLENKSNIDQRGYDGRNALRVAALEGHRDIVELLFSHGADVNYKDADGRPTLYILALENQLTMAEYFLEngA 970
Cdd:PHA02875 13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLD--L 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 971 NVEASDA---EGRTALHVSCWQGHVEMVRVLIACHADVNAADNEKRSALQSAAWQGHVKVVQLLIEHGAVVDHTCNQGAT 1047
Cdd:PHA02875 91 GKFADDVfykDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCT 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568921145 1048 ALCIAAQEGHVDVVQVLLEHGADPNHadqFGR----TAMRVAAKNGHSQIIKLLEKYGASS 1104
Cdd:PHA02875 171 PLIIAMAKGDIAICKMLLDSGANIDY---FGKngcvAALCYAIENNKIDIVRLFIKRGADC 228
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
618-707 |
3.12e-19 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 83.63 E-value: 3.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 618 AAWGGHTEVVSALLYAGVKVDCADADSRTALRAAAWGGHEDIVLNLLQHgAEVNKADNeGRTALIAAAYMGHREIVEHLL 697
Cdd:pfam12796 4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLL 81
|
90
....*....|
gi 568921145 698 DHGAEVNHED 707
Cdd:pfam12796 82 EKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
582-674 |
4.14e-19 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 83.24 E-value: 4.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 582 LTLAARQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGHTEVVSALLyAGVKVDCADaDSRTALRAAAWGGHEDIVL 661
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 568921145 662 NLLQHGAEVNKAD 674
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
959-1102 |
6.96e-19 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 88.86 E-value: 6.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 959 LTMAEYFLENGANVEASDAEGRTALHVSCWQGHVEMVRVLIACHADVNAADNEKRSALQSAAWQGHVKVVQLLIEHGAVV 1038
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568921145 1039 DHTCNQGATALCIAAQEGHVDVVQVLLEHGADPNHADQFGRTAMRVAAKNGHSQIIKLLEKYGA 1102
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGA 144
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
824-1114 |
1.01e-18 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 92.43 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 824 QGNVEVVRTLLDRGLDESHRDDAGWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIPFILASQEGHYDCVQILLENK 903
Cdd:PHA02876 155 QDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNR 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 904 SNIDQRGYDGRNALRVAALEGHRdiveLLFSHGADVN-YKDADGRPTLYILALENQLTMAEYFLENGANVEASDAEGRTA 982
Cdd:PHA02876 235 SNINKNDLSLLKAIRNEDLETSL----LLYDAGFSVNsIDDCKNTPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETP 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 983 LHVSCWQGH-VEMVRVLIACHADVNAADNEKRSALQSAAWQGHVK-VVQLLIEHGAVVDHTCNQGATALCIAAQEGHVDV 1060
Cdd:PHA02876 311 LYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKdIVITLLELGANVNARDYCDKTPIHYAAVRNNVVI 390
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 568921145 1061 VQVLLEHGADPNHADQFGRTAMRVA--AKNGHSQIIKLLEKyGA--SSLNGCSPSPVH 1114
Cdd:PHA02876 391 INTLLDYGADIEALSQKIGTALHFAlcGTNPYMSVKTLIDR-GAnvNSKNKDLSTPLH 447
|
|
| 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 568921145 524 REDSIRTLLDNGASVNQCDSNGRTLL---ANAAYSGS--LDVVNLLVSRGADLEIEDAHGHTPLTLAA--RQGHTKVVNC 596
Cdd:PHA03100 47 NIDVVKILLDNGADINSSTKNNSTPLhylSNIKYNLTdvKEIVKLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEY 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 597 LIGCGANINHTDQDGWTALRSAAWGGH--TEVVSALLYAGVKVDCADAdsrtalraaawgghediVLNLLQHGAEVNKAD 674
Cdd:PHA03100 127 LLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKD 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568921145 675 NEGRTALIAAAYMGHREIVEHLLDHGAEVNHEDVDGRTALSVAALcvpasKGHASVVSLLIDRGAEVDHCDK 746
Cdd:PHA03100 190 VYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAIL-----NNNKEIFKLLLNNGPSIKTIIE 256
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
950-1041 |
1.62e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 81.70 E-value: 1.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 950 LYILALENQLTMAEYFLENGANVEASDAEGRTALHVSCWQGHVEMVRVLIAcHADVNAADNeKRSALQSAAWQGHVKVVQ 1029
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVK 78
|
90
....*....|..
gi 568921145 1030 LLIEHGAVVDHT 1041
Cdd:pfam12796 79 LLLEKGADINVK 90
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
818-909 |
1.84e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 81.70 E-value: 1.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 818 LSIASAQGNVEVVRTLLDRGLDESHRDDAGWTPLHMAAFEGHRLICEALIEQGARtnEIDNDGRIPFILASQEGHYDCVQ 897
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78
|
90
....*....|..
gi 568921145 898 ILLENKSNIDQR 909
Cdd:pfam12796 79 LLLEKGADINVK 90
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
752-844 |
2.02e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 81.32 E-value: 2.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 752 LLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLLfwgAAVDS-IDSEGRTVLSIASAQGNVEVV 830
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL---EHADVnLKDNGRTALHYAARSGHLEIV 77
|
90
....*....|....
gi 568921145 831 RTLLDRGLDESHRD 844
Cdd:pfam12796 78 KLLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
723-811 |
2.06e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 81.32 E-value: 2.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 723 ASKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEgGADVDHTDnNGRTPLLAAASMGHASVVNTLLF 802
Cdd:pfam12796 5 AKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVKLLLE 82
|
....*....
gi 568921145 803 WGAAVDSID 811
Cdd:pfam12796 83 KGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
648-742 |
2.37e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 81.32 E-value: 2.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 648 LRAAAWGGHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLDHgAEVNHEDvDGRTALSVAalcvpASKGH 727
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYA-----ARSGH 73
|
90
....*....|....*
gi 568921145 728 ASVVSLLIDRGAEVD 742
Cdd:pfam12796 74 LEIVKLLLEKGADIN 88
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
761-945 |
2.59e-18 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 91.08 E-value: 2.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 761 VDVVDLLLEGGADvdHTDNNGRTPLLAAASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDE 840
Cdd:PLN03192 507 LNVGDLLGDNGGE--HDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNV 584
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 841 SHRDDAGWTPLHMAAFEGHRLICEALiEQGARTNEIDNDGRIpFILASQEGHYDCVQILLENKSNIDQRGYDGRNALRVA 920
Cdd:PLN03192 585 HIRDANGNTALWNAISAKHHKIFRIL-YHFASISDPHAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVA 662
|
170 180
....*....|....*....|....*
gi 568921145 921 ALEGHRDIVELLFSHGADVNYKDAD 945
Cdd:PLN03192 663 MAEDHVDMVRLLIMNGADVDKANTD 687
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
549-641 |
5.00e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 80.16 E-value: 5.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 549 LANAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLIGCgANINHTDqDGWTALRSAAWGGHTEVVS 628
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 568921145 629 ALLYAGVKVDCAD 641
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
896-1114 |
5.79e-18 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 88.54 E-value: 5.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 896 VQILLENKSNIDQRGYDGRNALRV---AALEGHRDIVELLFSHGADVNYKDADG-RPTLYILALENQLTMAEYFLENGAN 971
Cdd:PHA03095 30 VRRLLAAGADVNFRGEYGKTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGfTPLHLYLYNATTLDVIKLLIKAGAD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 972 VEASDAEGRTALHVsCWQG---HVEMVRVLIACHADVNAADNEKRSALQ-----SAAwqgHVKVVQLLIEHGAVVDHTCN 1043
Cdd:PHA03095 110 VNAKDKVGRTPLHV-YLSGfniNPKVIRLLLRKGADVNALDLYGMTPLAvllksRNA---NVELLRLLIDAGADVYAVDD 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568921145 1044 QGATALCIAAQEGHVD--VVQVLLEHGADPNHADQFGRTAMRVAAKNG---HSQIIKLLEKyGAS--SLNGCSPSPVH 1114
Cdd:PHA03095 186 RFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATGSsckRSLVLPLLIA-GISinARNRYGQTPLH 262
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
1016-1103 |
7.91e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 79.77 E-value: 7.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 1016 LQSAAWQGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQEGHVDVVQVLLEHgADPNHADQfGRTAMRVAAKNGHSQIIK 1095
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
|
....*...
gi 568921145 1096 LLEKYGAS 1103
Cdd:pfam12796 79 LLLEKGAD 86
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
917-1009 |
8.89e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 79.77 E-value: 8.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 917 LRVAALEGHRDIVELLFSHGADVNYKDADGRPTLYILALENQLTMAEYFLENgANVEASDaEGRTALHVSCWQGHVEMVR 996
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 568921145 997 VLIACHADVNAAD 1009
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
849-1087 |
2.46e-17 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 86.56 E-value: 2.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 849 TPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIPFILASQEGHYDCVQILLENksnidqrGYDgRNALRVAALEghRDI 928
Cdd:PHA02874 37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDN-------GVD-TSILPIPCIE--KDM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 929 VELLFSHGADVNYKDADGRPTLYILALENQLTMAEYFLENGANVEASDAEGRTALHVSCWQGHVEMVRVLIACHADVNAA 1008
Cdd:PHA02874 107 IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVK 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 1009 DNEKRSALQSAAWQGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQEGH------------------------------- 1057
Cdd:PHA02874 187 DNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRsaiellinnasindqdidgstplhhainppc 266
|
250 260 270
....*....|....*....|....*....|.
gi 568921145 1058 -VDVVQVLLEHGADPNHADQFGRTAMRVAAK 1087
Cdd:PHA02874 267 dIDIIDILLYHKADISIKDNKGENPIDTAFK 297
|
|
| 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 568921145 544 NGRTLLANAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGH 623
Cdd:PHA02875 1 MDQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 624 TEVVSALLYAGVKV-DCADADSRTALRAAAWGGHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLDHGAE 702
Cdd:PHA02875 81 VKAVEELLDLGKFAdDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKAC 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568921145 703 VNHEDVDGRTALSVAalcvpASKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGH-VDVVDLLLEGGAD 773
Cdd:PHA02875 161 LDIEDCCGCTPLIIA-----MAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNkIDIVRLFIKRGAD 227
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
659-925 |
1.96e-16 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 85.30 E-value: 1.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 659 IVLNLLQHGAEVNKADnegrtaliaaaymghreiVEHLLdhgAEVNHEDVDGRTALSVAALcvpASKGHASVVSLLIDRG 738
Cdd:PLN03192 493 ILKNFLQHHKELHDLN------------------VGDLL---GDNGGEHDDPNMASNLLTV---ASTGNAALLEELLKAK 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 739 AEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLLFWGAAVDSidSEGRTVL 818
Cdd:PLN03192 549 LDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDP--HAAGDLL 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 819 SIASAQGNVEVVRTLLDRGLDESHRDDAGWTPLHMAAFEGHRLICEALIEQGARTNEIDND------------------G 880
Cdd:PLN03192 627 CTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDddfsptelrellqkrelgH 706
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 568921145 881 RIPFILASQEGHYDCVQILLENKSNIDQRGYDGRNALRVAALEGH 925
Cdd:PLN03192 707 SITIVDSVPADEPDLGRDGGSRPGRLQGTSSDNQCRPRVSIYKGH 751
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
963-1119 |
2.49e-16 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 84.92 E-value: 2.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 963 EYFLENGANVEASDAEGRTALHVSCWQGHVEMVRVLIACHADVNAADNEKRSALQSAAWQGHVKVVQLLIEHGAVVD-HT 1041
Cdd:PLN03192 542 EELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDpHA 621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 1042 cnqGATALCIAAQEGHVDVVQVLLEHGADPNHADQFGRTAMRVAAKNGHSQIIKLLEKYGAS-----SLNGCSPSPVHTM 1116
Cdd:PLN03192 622 ---AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADvdkanTDDDFSPTELREL 698
|
...
gi 568921145 1117 EQK 1119
Cdd:PLN03192 699 LQK 701
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
826-1087 |
2.44e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 80.69 E-value: 2.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 826 NVEVVRTLLDRGLDESHRDDAGWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIpfilaSQEGHYDCVQI---LLEN 902
Cdd:PHA02878 49 NLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFYTLVAI-----KDAFNNRNVEIfkiILTN 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 903 KSN---------IDQRGYDGrnalrvaALEGhrDIVELLFSHGADVNYKDADGRPTLYILALENQLT-MAEYFLENGANV 972
Cdd:PHA02878 124 RYKniqtidlvyIDKKSKDD-------IIEA--EITKLLLSYGADINMKDRHKGNTALHYATENKDQrLTELLLSYGANV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 973 EASDAEGRTALHVSCWQGHVEMVRVLIACHADVNAADNEKRSALQSAAwqGHVK---VVQLLIEHGAVVD-HTCNQGATA 1048
Cdd:PHA02878 195 NIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISV--GYCKdydILKLLLEHGVDVNaKSYILGLTA 272
|
250 260 270
....*....|....*....|....*....|....*....
gi 568921145 1049 LCIAAQEGhvDVVQVLLEHGADPNHADQFGRTAMRVAAK 1087
Cdd:PHA02878 273 LHSSIKSE--RKLKLLLEYGADINSLNSYKLTPLSSAVK 309
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
645-874 |
3.43e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 79.65 E-value: 3.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 645 RTALRAAAWGGHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLDHGAEVNHEDVDGRTALSVAALcvpas 724
Cdd:PHA02875 3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVE----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 725 KGHASVVSLLIDRGAEVDHC-DKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLLFW 803
Cdd:PHA02875 78 EGDVKAVEELLDLGKFADDVfYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDH 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568921145 804 GAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDESHRDDAGWTPLHMAAFEGHRL-ICEALIEQGARTN 874
Cdd:PHA02875 158 KACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIdIVRLFIKRGADCN 229
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
730-983 |
3.68e-15 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 79.88 E-value: 3.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 730 VVSLLIDRGAEVDHCDKDGMTPLL-----VAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLLFW- 803
Cdd:PHA02798 53 IVKLFINLGANVNGLDNEYSTPLCtilsnIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLFMi 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 804 --GAAVDSIDSEGRTVLSIASAQGN---VEVVRTLLDRGLD-ESHRDDAGWTPLH-MAAFEGHRL---ICEALIEQGART 873
Cdd:PHA02798 133 enGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDiNTHNNKEKYDTLHcYFKYNIDRIdadILKLFVDNGFII 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 874 NEIDNDGRIPFIlasqeghyDCVQILLENKSNIDqrgydgrnalrvaaleghRDIVELLFSHgADVNYKDADGRPTLYIL 953
Cdd:PHA02798 213 NKENKSHKKKFM--------EYLNSLLYDNKRFK------------------KNILDFIFSY-IDINQVDELGFNPLYYS 265
|
250 260 270
....*....|....*....|....*....|
gi 568921145 954 ALENQLTMAEYFLENGANVEASDAEGRTAL 983
Cdd:PHA02798 266 VSHNNRKIFEYLLQLGGDINIITELGNTCL 295
|
|
| 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 568921145 549 LANAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLAA----RQGHTKVVNCLIGCgaNINHTDQdgwtALRSAAWGGHT 624
Cdd:PHA02878 41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICkepnKLGMKEMIRSINKC--SVFYTLV----AIKDAFNNRNV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 625 EVVSALLYAGVKVDCADADSRTALRAAAWGGHEDIVLNLLQHGAEVNKAD-NEGRTALIAAAYMGHREIVEHLLDHGAEV 703
Cdd:PHA02878 115 EIFKIILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 704 NHEDVDGRTALSVAAlcvpaSKGHASVVSLLIDRGAEVDHCDKDGMTPLLVA-AYEGHVDVVDLLLEGGADVDHTDN-NG 781
Cdd:PHA02878 195 NIPDKTNNSPLHHAV-----KHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYiLG 269
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 568921145 782 RTPLlaAASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQ 824
Cdd:PHA02878 270 LTAL--HSSIKSERKLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
891-1115 |
6.33e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 78.85 E-value: 6.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 891 GHYDCVQILLENKSNIDQRGYDGRNALRVAALE-GHRDIVELLFSHGADVNYKDAD-GRPTLYILALENQlTMAEYFLEN 968
Cdd:PHA02874 12 GDIEAIEKIIKNKGNCINISVDETTTPLIDAIRsGDAKIVELFIKHGADINHINTKiPHPLLTAIKIGAH-DIIKLLIDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 969 GANVeasdaegrTALHVSCWQGhvEMVRVLIACHADVNAADNEKRSALQSAAWQGHVKVVQLLIEHGAVVDHTCNQGATA 1048
Cdd:PHA02874 91 GVDT--------SILPIPCIEK--DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568921145 1049 LCIAAQEGHVDVVQVLLEHGADPNHADQFGRTAMRVAAKNGHSQIIKLLEKYGASSLNGCSP--SPVHT 1115
Cdd:PHA02874 161 IHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNgfTPLHN 229
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
526-608 |
9.11e-15 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 70.92 E-value: 9.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 526 DSIRTLLDNGASVNQCDSNGRTLLANAAYSGSLDVVNLLVSRgADLEIEDaHGHTPLTLAARQGHTKVVNCLIGCGANIN 605
Cdd:pfam12796 11 ELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADIN 88
|
...
gi 568921145 606 HTD 608
Cdd:pfam12796 89 VKD 91
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
915-1094 |
1.78e-14 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 78.76 E-value: 1.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 915 NALRVAALeGHRDIVELLFSHGADVNYKDADGRPTLYILALENQLTMAEYFLENGANVEASDAEGRTALHVSCWQGHVEM 994
Cdd:PLN03192 528 NLLTVAST-GNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKI 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 995 VRVLIACHADVN---AADnekrsALQSAAWQGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQEGHVDVVQVLLEHGADP 1071
Cdd:PLN03192 607 FRILYHFASISDphaAGD-----LLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
|
170 180
....*....|....*....|....*....
gi 568921145 1072 NHA---DQFGRTAMRVAAKN---GHSQII 1094
Cdd:PLN03192 682 DKAntdDDFSPTELRELLQKrelGHSITI 710
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
862-1072 |
2.21e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 76.95 E-value: 2.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 862 ICEALIEQGARTNEIDNDGRIPFILASQEGHYDCVQILLENKSNIDQRGYDGRNALRVAALEGHRDIVELLFSHGA---D 938
Cdd:PHA02875 17 IARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKfadD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 939 VNYKDadGRPTLYILALENQLTMAEYFLENGANVEASDAEGRTALHVSCWQGHVEMVRVLIACHADVNAADNEKRSALQS 1018
Cdd:PHA02875 97 VFYKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLII 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568921145 1019 AAWQGHVKVVQLLIEHGAVVDHTCNQG-ATALCIAAQEGHVDVVQVLLEHGADPN 1072
Cdd:PHA02875 175 AMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCN 229
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
495-609 |
2.24e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 73.93 E-value: 2.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 495 EVLQLLIRAGAHVNSEDdhtscivrqaleredSIRTLLDNGASVNQCDSNGRTLLANAAYSGSLDVVNLLVSRGADLEIE 574
Cdd:PHA03100 157 KILKLLIDKGVDINAKN---------------RVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLV 221
|
90 100 110
....*....|....*....|....*....|....*
gi 568921145 575 DAHGHTPLTLAARQGHTKVVNCLIGCGANINHTDQ 609
Cdd:PHA03100 222 NKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
495-634 |
2.38e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 73.93 E-value: 2.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 495 EVLQLLIRAGAHVNSEDDHTSCIVRQALERE----DSIRTLLDNGASVNQCDSNGRTLLANAAYSGS--LDVVNLLVSRG 568
Cdd:PHA03100 87 EIVKLLLEYGANVNAPDNNGITPLLYAISKKsnsySIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 569 ADLEIE----------------DAHGHTPLTLAARQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGHTEVVSALLY 632
Cdd:PHA03100 167 VDINAKnrvnyllsygvpinikDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLN 246
|
..
gi 568921145 633 AG 634
Cdd:PHA03100 247 NG 248
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
526-740 |
1.25e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 71.56 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 526 DSIRTLLDNGASVNQCDSNGRTLLANAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLIGCGANIN 605
Cdd:PHA02875 16 DIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 606 HT-DQDGWTALRSAAWGGHTEVVSALLYAGVKVDCADADSRTALRAAAWGGHEDIVLNLLQHGAEVNKADNEGRTALIAA 684
Cdd:PHA02875 96 DVfYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 568921145 685 AYMGHREIVEHLLDHGAEVNHEDVDGrtalSVAALCVPASKGHASVVSLLIDRGAE 740
Cdd:PHA02875 176 MAKGDIAICKMLLDSGANIDYFGKNG----CVAALCYAIENNKIDIVRLFIKRGAD 227
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
748-801 |
3.09e-12 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 62.68 E-value: 3.09e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 568921145 748 GMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLL 801
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
759-987 |
3.14e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 70.41 E-value: 3.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 759 GHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGl 838
Cdd:PHA02875 13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 839 deSHRDDA----GWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIPFILASQEGHYDCVQILLENKSNIDQRGYDGR 914
Cdd:PHA02875 92 --KFADDVfykdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGC 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568921145 915 NALRVAALEGHRDIVELLFSHGADVNYKDADGRPTLYILALE-NQLTMAEYFLENGAN---VEASDAEGRTALHVSC 987
Cdd:PHA02875 170 TPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIEnNKIDIVRLFIKRGADcniMFMIEGEECTILDMIC 246
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
1047-1097 |
1.66e-11 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 60.37 E-value: 1.66e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 568921145 1047 TALCIAAQEGHVDVVQVLLEHGADPNHADQFGRTAMRVAAKNGHSQIIKLL 1097
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
864-1093 |
2.47e-11 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 68.12 E-value: 2.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 864 EALIEQGARTNEIdndgriPFILASQEGHYDCVQILLENKS-NIDQRGYDGRNALRVAALEGHRDIVELLfshgadvnyk 942
Cdd:cd22192 7 ELHLLQQKRISES------PLLLAAKENDVQAIKKLLKCPScDLFQRGALGETALHVAALYDNLEAAVVL---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 943 dADGRPTLYILALENQLtmaeYflenganveasdaEGRTALHVSCWQGHVEMVRVLIACHADVNAAdnekRSA------- 1015
Cdd:cd22192 71 -MEAAPELVNEPMTSDL----Y-------------QGETALHIAVVNQNLNLVRELIARGADVVSP----RATgtffrpg 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 1016 -----------LQSAAWQGHVKVVQLLIEHGA----------VVDH--TCNQGATALC-----IAAQEGHVDvvQVLLEH 1067
Cdd:cd22192 129 pknliyygehpLSFAACVGNEEIVRLLIEHGAdiraqdslgnTVLHilVLQPNKTFACqmydlILSYDKEDD--LQPLDL 206
|
250 260
....*....|....*....|....*.
gi 568921145 1068 gaDPNHAdqfGRTAMRVAAKNGHSQI 1093
Cdd:cd22192 207 --VPNNQ---GLTPFKLAAKEGNIVM 227
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
706-801 |
5.29e-11 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 67.23 E-value: 5.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 706 EDVDGRTA--LSVAaLCVPASKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRT 783
Cdd:PTZ00322 72 EVIDPVVAhmLTVE-LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKT 150
|
90
....*....|....*...
gi 568921145 784 PLLAAASMGHASVVNTLL 801
Cdd:PTZ00322 151 PLELAEENGFREVVQLLS 168
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
1028-1128 |
8.05e-11 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 66.85 E-value: 8.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 1028 VQLLIEHGAVVDHTCNQGATALCIAAQEGHVDVVQVLLEHGADPNHADQFGRTAMRVAAKNGHSQIIKLLEKYGASSLNG 1107
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFEL 177
|
90 100
....*....|....*....|...
gi 568921145 1108 CSPSPVHTMEQKPP--QSAPSKM 1128
Cdd:PTZ00322 178 GANAKPDSFTGKPPslEDSPISS 200
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
751-1034 |
8.16e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 66.06 E-value: 8.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 751 PLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAA-------------ASMGHASVVNTLLFWGAAVDSIDSEGRTV 817
Cdd:PHA02878 40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIIckepnklgmkemiRSINKCSVFYTLVAIKDAFNNRNVEIFKI 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 818 LSIASAQGN------------------VEVVRTLLDRGLDESHRD-DAGWTPLHMAAFEGHRLICEALIEQGARTNEIDN 878
Cdd:PHA02878 120 ILTNRYKNIqtidlvyidkkskddiieAEITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDK 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 879 DGRIPFILASQEGHYDCVQILLENKSNIDQRGYDGRNALRVAALE-GHRDIVELLFSHGADVNYKDadgrptlYILALen 957
Cdd:PHA02878 200 TNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKS-------YILGL-- 270
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568921145 958 qltmaeyflenganveasdaegrTALHVSCwqgHVEMV-RVLIACHADVNAADNEKRSALQSAAWQGH-VKVVQLLIEH 1034
Cdd:PHA02878 271 -----------------------TALHSSI---KSERKlKLLLEYGADINSLNSYKLTPLSSAVKQYLcINIGRILISN 323
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
497-649 |
1.47e-10 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 66.04 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 497 LQLLIRAG--AHVNSEDDHTSCIVRQALEREDSIRTLLDNGASVNQCDSNGRTLLANAAYSGSLDVVNLLVSRGAdleIE 574
Cdd:PLN03192 541 LEELLKAKldPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFAS---IS 617
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568921145 575 DAH-GHTPLTLAARQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGHTEVVSALLYAGVKVDCADAD---SRTALR 649
Cdd:PLN03192 618 DPHaAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDddfSPTELR 696
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
764-850 |
1.65e-10 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 65.69 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 764 VDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRtLLDRGLDESHR 843
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ-LLSRHSQCHFE 176
|
....*..
gi 568921145 844 DDAGWTP 850
Cdd:PTZ00322 177 LGANAKP 183
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
1013-1065 |
5.78e-10 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 56.13 E-value: 5.78e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 568921145 1013 RSALQSAAWQGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQEGHVDVVQVLL 1065
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
528-719 |
7.01e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 63.36 E-value: 7.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 528 IRTLLDNGASVNQCDSN-GRTLLANAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLIGCGANINH 606
Cdd:PHA02878 150 TKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 607 TDQDGWTALrsaawggHTEVVSALLYagvkvdcadadsrtalraaawggheDIVLNLLQHGAEVN-KADNEGRTALIAAa 685
Cdd:PHA02878 230 RDKCGNTPL-------HISVGYCKDY-------------------------DILKLLLEHGVDVNaKSYILGLTALHSS- 276
|
170 180 190
....*....|....*....|....*....|....
gi 568921145 686 yMGHREIVEHLLDHGAEVNHEDVDGRTALSVAAL 719
Cdd:PHA02878 277 -IKSERKLKLLLEYGADINSLNSYKLTPLSSAVK 309
|
|
| 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 568921145 580 TPLTLAARQGHTKVVNCLIGCganiNHTD-----QDGWTALRSAAWGGHTEVVSAL---------------LYAGVkvdc 639
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLLKC----PSCDlfqrgALGETALHVAALYDNLEAAVVLmeaapelvnepmtsdLYQGE---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 640 adadsrTALRAAAWGGHEDIVLNLLQHGAEVNKADNEG------RTALIA--------AAYMGHREIVEHLLDHGAEVNH 705
Cdd:cd22192 91 ------TALHIAVVNQNLNLVRELIARGADVVSPRATGtffrpgPKNLIYygehplsfAACVGNEEIVRLLIEHGADIRA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568921145 706 EDVDGRTALSVAALcvPASKGHASVVSLLI------DRGAEVDHC-DKDGMTPLLVAAYEGHV 761
Cdd:cd22192 165 QDSLGNTVLHILVL--QPNKTFACQMYDLIlsydkeDDLQPLDLVpNNQGLTPFKLAAKEGNI 225
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
889-1114 |
1.41e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 62.77 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 889 QEGHYDCVQILLENKSNIDQRGYDGRNALRVAALEGHRDIVELLFSHGADVNYKDADGRPTLYILALENQLTMAEYFLEN 968
Cdd:PHA02876 154 QQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDN 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 969 GANVEASDAEGRTALHvscwQGHVEMVRVLIACHADVNAADNEKRSALQSAAWQGHV-KVVQLLIEHGAVVDHTCNQGAT 1047
Cdd:PHA02876 234 RSNINKNDLSLLKAIR----NEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGET 309
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568921145 1048 ALCIAAQEGH-VDVVQVLLEHGADPNHADQFGRTAMRVAAKNGHSQ--IIKLLEkYGA--SSLNGCSPSPVH 1114
Cdd:PHA02876 310 PLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKdiVITLLE-LGAnvNARDYCDKTPIH 380
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
814-867 |
2.14e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 54.59 E-value: 2.14e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 568921145 814 GRTVLSIASAQGNVEVVRTLLDRGLDESHRDDAGWTPLHMAAFEGHRLICEALI 867
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
578-631 |
4.78e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 53.43 E-value: 4.78e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 568921145 578 GHTPLTLAARQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGHTEVVSALL 631
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
979-1032 |
4.88e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 53.43 E-value: 4.88e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 568921145 979 GRTALHVSCWQGHVEMVRVLIACHADVNAADNEKRSALQSAAWQGHVKVVQLLI 1032
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
645-697 |
5.49e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 53.43 E-value: 5.49e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 568921145 645 RTALRAAAWGGHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLL 697
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
946-999 |
7.01e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 53.05 E-value: 7.01e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 568921145 946 GRPTLYILALENQLTMAEYFLENGANVEASDAEGRTALHVSCWQGHVEMVRVLI 999
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
592-801 |
9.11e-09 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 59.68 E-value: 9.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 592 KVVNCLIGCGANINHTDQDGWTALRSAAWGGHTEVVSALLYAGVKVDCADADSRTALRAAAwgGHEDIVLN----LLQHG 667
Cdd:PHA02946 53 RFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLS--GTDDEVIErinlLVQYG 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 668 AEVNKA-DNEGRTALIAAAYMGHReIVEHLLDHGAEVNHEDVDGRTALSVAALcvpASKGHASVVSLLIDRGAEVDHCDK 746
Cdd:PHA02946 131 AKINNSvDEEGCGPLLACTDPSER-VFKKIMSIGFEARIVDKFGKNHIHRHLM---SDNPKASTISWMMKLGISPSKPDH 206
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568921145 747 DGMTPLLVAAYE--GHVDVVDLLLEgGADVDHTDNNGRTPL-LAAASMGHASVVNTLL 801
Cdd:PHA02946 207 DGNTPLHIVCSKtvKNVDIINLLLP-STDVNKQNKFGDSPLtLLIKTLSPAHLINKLL 263
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
808-900 |
1.23e-08 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 59.53 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 808 DSIDSEGRTVLSIA----SAQGNVEVVRTLLDRGLDESHRDDAGWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIP 883
Cdd:PTZ00322 72 EVIDPVVAHMLTVElcqlAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTP 151
|
90
....*....|....*..
gi 568921145 884 FILASQEGHYDCVQILL 900
Cdd:PTZ00322 152 LELAEENGFREVVQLLS 168
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
710-768 |
1.25e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 52.28 E-value: 1.25e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 568921145 710 GRTALSVAAlcvpaSKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVDLLL 768
Cdd:pfam13637 1 ELTALHAAA-----ASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
962-1034 |
1.43e-08 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 59.53 E-value: 1.43e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568921145 962 AEYFLENGANVEASDAEGRTALHVSCWQGHVEMVRVLIACHADVNAADNEKRSALQSAAWQGHVKVVQLLIEH 1034
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
483-801 |
1.45e-08 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 59.08 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 483 KDSLSTlipkeqEVLQLLIRAGAHVNSEDDHTS---CIVRQALERE----DSIRTLLDNGASVNQCDSNGRT----LLAN 551
Cdd:PHA02798 46 RDSPST------DIVKLFINLGANVNGLDNEYStplCTILSNIKDYkhmlDIVKILIENGADINKKNSDGETplycLLSN 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 552 AaYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHT---KVVNCLIGCGANIN-HTDQDGWTALRSaawgghtevv 627
Cdd:PHA02798 120 G-YINNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDINtHNNKEKYDTLHC---------- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 628 sallYAGVKVDCADADsrtalraaawgghedIVLNLLQHGAEVNKADNEGRTALIaaaymghrEIVEHLLDHGAEVNHED 707
Cdd:PHA02798 189 ----YFKYNIDRIDAD---------------ILKLFVDNGFIINKENKSHKKKFM--------EYLNSLLYDNKRFKKNI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 708 VDgrtalsvaalcvpaskghasvvslLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLA 787
Cdd:PHA02798 242 LD------------------------FIFSYIDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFT 297
|
330
....*....|....
gi 568921145 788 AASMGHASVVNTLL 801
Cdd:PHA02798 298 AFENESKFIFNSIL 311
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
624-907 |
1.70e-08 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 58.69 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 624 TEVVSALLYAGVKVDCADADSRTAL-----RAAAWGGHEDIVLNLLQHGAEVNKADNEGRT---ALIAAAYMGHREIVEH 695
Cdd:PHA02798 51 TDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETplyCLLSNGYINNLEILLF 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 696 LLDHGAEVNHEDVDGRTALSVAalcvpASKGHA---SVVSLLIDRGAEVD-HCDKDGMTPLLVAAYEG----HVDVVDLL 767
Cdd:PHA02798 131 MIENGADTTLLDKDGFTMLQVY-----LQSNHHidiEIIKLLLEKGVDINtHNNKEKYDTLHCYFKYNidriDADILKLF 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 768 LEGGADVDHTDNNGRTPLLaaasmghaSVVNTLLFWGAAVDSidsegrtvlsiasaqgnveVVRTLLDRGLDESHRDDAG 847
Cdd:PHA02798 206 VDNGFIINKENKSHKKKFM--------EYLNSLLYDNKRFKK-------------------NILDFIFSYIDINQVDELG 258
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 848 WTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIPFILASQEGHYDCVQILLENKSNID 907
Cdd:PHA02798 259 FNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKPNKN 318
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
691-945 |
1.86e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 58.74 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 691 EIVEHLLDHGAEVNHEDVDGRTALSVAALcVPASKGHASVVSLLIDRgaEVDHCDKDGMTpllvAAYEGHVDVVDLLLEG 770
Cdd:PHA02878 51 DVVKSLLTRGHNVNQPDHRDLTPLHIICK-EPNKLGMKEMIRSINKC--SVFYTLVAIKD----AFNNRNVEIFKIILTN 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 771 GADVDHTDNNGRTPLLAAASMGHASVVNTLLFWGAAVDSID-SEGRTVLSIASAQGNVEVVRTLLDRGLDESHRDDAGWT 849
Cdd:PHA02878 124 RYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNS 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 850 PLHMAAFEGHRLICEALIEQGARTNEIDNDGRIPF-ILASQEGHYDCVQILLENKSNIDQRGY-DGRNALRVAALEghRD 927
Cdd:PHA02878 204 PLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLhISVGYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKS--ER 281
|
250
....*....|....*...
gi 568921145 928 IVELLFSHGADVNYKDAD 945
Cdd:PHA02878 282 KLKLLLEYGADINSLNSY 299
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
783-962 |
2.07e-08 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 58.87 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 783 TPLLAAASMGHASVVNTLLfwgaAVDSID-----SEGRTVLSIASAQGNVEVVRTLLD--RGL-DESHRDD--AGWTPLH 852
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLL----KCPSCDlfqrgALGETALHVAALYDNLEAAVVLMEaaPELvNEPMTSDlyQGETALH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 853 MAAFEGHRLICEALIEQGARTneidndgripfILASQEGHYdcvqiLLENKSNIdqrGYDGRNALRVAALEGHRDIVELL 932
Cdd:cd22192 95 IAVVNQNLNLVRELIARGADV-----------VSPRATGTF-----FRPGPKNL---IYYGEHPLSFAACVGNEEIVRLL 155
|
170 180 190
....*....|....*....|....*....|
gi 568921145 933 FSHGADVNYKDADGRPTLYILALENQLTMA 962
Cdd:cd22192 156 IEHGADIRAQDSLGNTVLHILVLQPNKTFA 185
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
528-600 |
2.25e-08 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 58.76 E-value: 2.25e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568921145 528 IRTLLDNGASVNQCDSNGRTLLANAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLIGC 600
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
844-948 |
2.63e-08 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 58.37 E-value: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 844 DDAGWTPLHMAAFE-------GHRLICEALIEQGARTNEIDNDGRIPFILASQEGHYDCVQILLENKSNIDQRGYDGRNA 916
Cdd:PTZ00322 72 EVIDPVVAHMLTVElcqlaasGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTP 151
|
90 100 110
....*....|....*....|....*....|..
gi 568921145 917 LRVAALEGHRDIVELLFSHGADVNYKDADGRP 948
Cdd:PTZ00322 152 LELAEENGFREVVQLLSRHSQCHFELGANAKP 183
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
497-639 |
2.63e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 58.08 E-value: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 497 LQLLIRAGAHVNS---EDDHTSCIVRQALEREDSIRTLLDNGASVNQCDSNGRTLLANAAYSGSLDVVNLLVSRGADLEI 573
Cdd:PHA02875 84 VEELLDLGKFADDvfyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDI 163
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568921145 574 EDAHGHTPLTLAARQGHTKVVNCLIGCGANINHTDQDG-WTALRSAAWGGHTEVVSALLYAGvkVDC 639
Cdd:PHA02875 164 EDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRG--ADC 228
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
549-631 |
5.47e-08 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 57.60 E-value: 5.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 549 LANAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGHTEVVS 628
Cdd:PTZ00322 86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165
|
...
gi 568921145 629 ALL 631
Cdd:PTZ00322 166 LLS 168
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
927-1097 |
6.51e-08 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 56.77 E-value: 6.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 927 DIVELLFSHGADVNYKDAD-GRPTLYILA----LENQLTMAEYFLENGANVEASDAEGRTALHvscwqghvemvrvliac 1001
Cdd:PHA02798 52 DIVKLFINLGANVNGLDNEySTPLCTILSnikdYKHMLDIVKILIENGADINKKNSDGETPLY----------------- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 1002 hadvnaadnekrsALQSAAWQGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQEGH---VDVVQVLLEHGADPN-HADQF 1077
Cdd:PHA02798 115 -------------CLLSNGYINNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINtHNNKE 181
|
170 180
....*....|....*....|....
gi 568921145 1078 GRTAMRVAAKNGHSQ----IIKLL 1097
Cdd:PHA02798 182 KYDTLHCYFKYNIDRidadILKLF 205
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
789-866 |
7.37e-08 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 57.22 E-value: 7.37e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568921145 789 ASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDESHRDDAGWTPLHMAAFEGHRLICEAL 866
Cdd:PTZ00322 90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
710-903 |
8.76e-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: 56.56 E-value: 8.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 710 GRTALSVAALcvpasKGHASVVSLLIDRGAEV--DHCDKD---GMTPLLVAAYEGHVDVVDLLLEGGADVdhtdNNGRtp 784
Cdd:cd22192 51 GETALHVAAL-----YDNLEAAVVLMEAAPELvnEPMTSDlyqGETALHIAVVNQNLNLVRELIARGADV----VSPR-- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 785 llAAASMGHASVVNTLLFwgaavdsidseGRTVLSIASAQGNVEVVRTLLDRGLDESHRDDAGWTPLHMAAFEGHRLI-C 863
Cdd:cd22192 120 --ATGTFFRPGPKNLIYY-----------GEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFaC 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568921145 864 EA---LIEQGARTNEI------DNDGRIPFILASQEGHYDCVQILLENK 903
Cdd:cd22192 187 QMydlILSYDKEDDLQpldlvpNNQGLTPFKLAAKEGNIVMFQHLVQKR 235
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
955-1110 |
1.10e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 56.15 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 955 LENQLTMAEYFLENGANVEASDAEGRTALHVSCWQGHVEMVRVLIACHADVNAADNEKRSALQSAAWQGHVKVVQLLIEH 1034
Cdd:PHA02875 11 LFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 1035 GAVVDHTC-NQGATALCIAAQEGHVDVVQVLLEHGADPNHADQFGRTAMRVAAKNGHSQIIKLLEKYGAsSLN-----GC 1108
Cdd:PHA02875 91 GKFADDVFyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKA-CLDiedccGC 169
|
..
gi 568921145 1109 SP 1110
Cdd:PHA02875 170 TP 171
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
847-900 |
2.02e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 48.81 E-value: 2.02e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 568921145 847 GWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIPFILASQEGHYDCVQILL 900
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| TRPV1 |
cd22196 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ... |
911-984 |
2.27e-07 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411980 [Multi-domain] Cd Length: 649 Bit Score: 55.58 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 911 YDGRNALRVAALEGHRDIVELLFSHGADVN-------YKDADGRPTLY-------ILALENQLTMAEYFLEN---GANVE 973
Cdd:cd22196 92 YKGQTALHIAIERRNMHLVELLVQNGADVHarasgefFKKKKGGPGFYfgelplsLAACTNQLDIVKFLLENphsPADIS 171
|
90
....*....|.
gi 568921145 974 ASDAEGRTALH 984
Cdd:cd22196 172 ARDSMGNTVLH 182
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
807-964 |
2.36e-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: 55.47 E-value: 2.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 807 VDSIDSEGRTVLSIASAQGNVEVVRTLLdrgLDESHRDDAGWTPLHMAAFEGHRlICEALI---EQGAR-------TNEI 876
Cdd:TIGR00870 45 INCPDRLGRSALFVAAIENENLELTELL---LNLSCRGAVGDTLLHAISLEYVD-AVEAILlhlLAAFRksgplelANDQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 877 DND----GRIPFILASQEGHYDCVQILLENKSNIDQRG--------------YDGRNALRVAALEGHRDIVELLFSHGAD 938
Cdd:TIGR00870 121 YTSeftpGITALHLAAHRQNYEIVKLLLERGASVPARAcgdffvksqgvdsfYHGESPLNAAACLGSPSIVALLSEDPAD 200
|
170 180
....*....|....*....|....*.
gi 568921145 939 VNYKDADGRPTLYILALENQLTmAEY 964
Cdd:TIGR00870 201 ILTADSLGNTLLHLLVMENEFK-AEY 225
|
|
| TRPV1-4 |
cd22193 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ... |
885-1066 |
2.78e-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: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 885 ILASQEGHYDCVQILL---ENKSNIDQ--------RGYDGRNALRVAALEGHRDIVELLFSHGADVN-------YKDADG 946
Cdd:cd22193 37 LLNLNPGTNDTIRILLdiaEKTDNLKRfinaeytdEYYEGQTALHIAIERRQGDIVALLVENGADVHahakgrfFQPKYQ 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 947 RPTLY-------ILALENQLTMAEYFLENG---ANVEASDAEGRTALHvscwqghvemvrvliachADVNAADNEK-RSA 1015
Cdd:cd22193 117 GEGFYfgelplsLAACTNQPDIVQYLLENEhqpADIEAQDSRGNTVLH------------------ALVTVADNTKeNTK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568921145 1016 LQSAAWQGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQEGHVDVVQVLLE 1066
Cdd:cd22193 179 FVTRMYDMILIRGAKLCPTVELEEIRNNDGLTPLQLAAKMGKIEILKYILQ 229
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
1002-1104 |
2.89e-07 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 55.26 E-value: 2.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 1002 HADVNAADNekrsaLQSAAWQGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQEGHVDVVQVLLEHGADPNHADQFGRTA 1081
Cdd:PLN03192 520 HDDPNMASN-----LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTA 594
|
90 100
....*....|....*....|...
gi 568921145 1082 MRVAAKNGHSQIIKLLEKYGASS 1104
Cdd:PLN03192 595 LWNAISAKHHKIFRILYHFASIS 617
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
557-839 |
7.32e-07 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 53.69 E-value: 7.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 557 SLDVVNLLVSRGADLEIEDAHGHTPL-TLAARQGHTK----VVNCLIGCGANINHTDQDGWTALrsaawgghtevvSALL 631
Cdd:PHA02798 50 STDIVKLFINLGANVNGLDNEYSTPLcTILSNIKDYKhmldIVKILIENGADINKKNSDGETPL------------YCLL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 632 YAGvkvdcadadsrtalraaaWGGHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHR---EIVEHLLDHGAEVN-HED 707
Cdd:PHA02798 118 SNG------------------YINNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDINtHNN 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 708 VDGRTALSvAALCVPASKGHASVVSLLIDRGAEVDHCDK-------DGMTPLLVAAYEGHVDVVDLLLEGgADVDHTDNN 780
Cdd:PHA02798 180 KEKYDTLH-CYFKYNIDRIDADILKLFVDNGFIINKENKshkkkfmEYLNSLLYDNKRFKKNILDFIFSY-IDINQVDEL 257
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 568921145 781 GRTPLLAAASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLD 839
Cdd:PHA02798 258 GFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKPN 316
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
611-664 |
8.87e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 47.27 E-value: 8.87e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 568921145 611 GWTALRSAAWGGHTEVVSALLYAGVKVDCADADSRTALRAAAWGGHEDIVLNLL 664
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
619-713 |
9.51e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 53.36 E-value: 9.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 619 AWGGHTEVVSALLYAGVKVDCADADSRTALRAAAWGGHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLD 698
Cdd:PTZ00322 90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
|
90
....*....|....*
gi 568921145 699 HGAEvnHEDVDGRTA 713
Cdd:PTZ00322 170 HSQC--HFELGANAK 182
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
1031-1085 |
9.70e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 46.96 E-value: 9.70e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 568921145 1031 LIEHGAV-VDHTCNQGATALCIAAQEGHVDVVQVLLEHGADPNHADQFGRTAMRVA 1085
Cdd:pfam13857 1 LLEHGPIdLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
992-1101 |
2.06e-06 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 52.14 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 992 VEMVRVLIACHADVNAADNEKRSALQS-----AAWQGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQEGHVDVVQVLL- 1065
Cdd:PHA02798 51 TDIVKLFINLGANVNGLDNEYSTPLCTilsniKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLf 130
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 568921145 1066 --EHGADPNHADQFGRTAMRVAAKNGHS---QIIKLLEKYG 1101
Cdd:PHA02798 131 miENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKG 171
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
677-735 |
2.32e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 46.11 E-value: 2.32e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 568921145 677 GRTALIAAAYMGHREIVEHLLDHGAEVNHEDVDGRTALSVAalcvpASKGHASVVSLLI 735
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFA-----ASNGNVEVLKLLL 54
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
663-717 |
2.35e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 46.19 E-value: 2.35e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 568921145 663 LLQHG-AEVNKADNEGRTALIAAAYMGHREIVEHLLDHGAEVNHEDVDGRTALSVA 717
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
887-932 |
2.69e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 45.73 E-value: 2.69e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 568921145 887 ASQEGHYDCVQILLENKSNIDQRGYDGRNALRVAALEGHRDIVELL 932
Cdd:pfam13637 8 AAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
805-854 |
2.88e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 45.80 E-value: 2.88e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 568921145 805 AAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDESHRDDAGWTPLHMA 854
Cdd:pfam13857 7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
929-1001 |
3.72e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 51.44 E-value: 3.72e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568921145 929 VELLFSHGADVNYKDADGRPTLYILALENQLTMAEYFLENGANVEASDAEGRTALHVSCWQGHVEMVRVLIAC 1001
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
913-966 |
3.94e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 45.34 E-value: 3.94e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 568921145 913 GRNALRVAALEGHRDIVELLFSHGADVNYKDADGRPTLYILALENQLTMAEYFL 966
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
747-779 |
3.96e-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: 3.96e-06
10 20 30
....*....|....*....|....*....|....
gi 568921145 747 DGMTPLLVAAYE-GHVDVVDLLLEGGADVDHTDN 779
Cdd:pfam00023 1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
884-1086 |
4.29e-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: 51.24 E-value: 4.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 884 FILASQEGHYDCVQILLEN--KSNIDQRGYDGRNALRVAALEG-HRDIVELLFSHGADVNYKDAdgrpTLYILALENQ-- 958
Cdd:TIGR00870 21 FLPAAERGDLASVYRDLEEpkKLNINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAVGDT----LLHAISLEYVda 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 959 -----LTMAEYFLENGANVEASD------AEGRTALHVSCWQGHVEMVRVLIACHADVNAA---DNEKRSALQSAAWQGh 1024
Cdd:TIGR00870 97 veailLHLLAAFRKSGPLELANDqytsefTPGITALHLAAHRQNYEIVKLLLERGASVPARacgDFFVKSQGVDSFYHG- 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568921145 1025 vkvvqlliEHgavvdhtcnqgatALCIAAQEGHVDVVQVLLEHGADPNHADQFGRTAMRVAA 1086
Cdd:TIGR00870 176 --------ES-------------PLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLV 216
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
966-1019 |
4.66e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 45.03 E-value: 4.66e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 568921145 966 LENG-ANVEASDAEGRTALHVSCWQGHVEMVRVLIACHADVNAADNEKRSALQSA 1019
Cdd:pfam13857 2 LEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
513-565 |
6.83e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 44.57 E-value: 6.83e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 568921145 513 HTSCIVRQA-LEREDSIRTLLDNGASVNQCDSNGRTLLANAAYSGSLDVVNLLV 565
Cdd:pfam13637 1 ELTALHAAAaSGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
978-1010 |
7.64e-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: 43.82 E-value: 7.64e-06
10 20 30
....*....|....*....|....*....|....
gi 568921145 978 EGRTALHVSCWQ-GHVEMVRVLIACHADVNAADN 1010
Cdd:pfam00023 1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
989-1123 |
8.41e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 50.45 E-value: 8.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 989 QGHVEMVRVLIACHADVNAADNEKRSALQSAAWQGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQEGHVDVVQVLLEHG 1068
Cdd:PHA02876 155 QDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNR 234
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 568921145 1069 ADPNHADqfgrTAMRVAAKNGHSQIIKLLEKYGAS--SLNGCSPSPVHTMEQKPPQS 1123
Cdd:PHA02876 235 SNINKND----LSLLKAIRNEDLETSLLLYDAGFSvnSIDDCKNTPLHHASQAPSLS 287
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
531-585 |
1.03e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 44.26 E-value: 1.03e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 568921145 531 LLDNG-ASVNQCDSNGRTLLANAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLA 585
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
545-598 |
1.09e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 44.19 E-value: 1.09e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 568921145 545 GRTLLANAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLI 598
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
839-1066 |
1.37e-05 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).
Pssm-ID: 411975 [Multi-domain] Cd Length: 600 Bit Score: 49.49 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 839 DESHRDDAGWTPLHMAAFEGH--RLICEALIEQGARtneiDNDGRIPFILASQEGHYdcvqillenksnidqrgYDGRNA 916
Cdd:cd21882 18 SAYQRGATGKTCLHKAALNLNdgVNEAIMLLLEAAP----DSGNPKELVNAPCTDEF-----------------YQGQTA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 917 LRVAALEGHRDIVELLFSHGADVNYK------DADGRPTLY-------ILALENQLTMAEYFLENG---ANVEASDAEGR 980
Cdd:cd21882 77 LHIAIENRNLNLVRLLVENGADVSARatgrffRKSPGNLFYfgelplsLAACTNQEEIVRLLLENGaqpAALEAQDSLGN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 981 TALHVSCWQGHVEMVRVLIACHadvnaadnekrsalqsaawqghvkVVQLLIEHGAVVDHTC-------NQGATALCIAA 1053
Cdd:cd21882 157 TVLHALVLQADNTPENSAFVCQ------------------------MYNLLLSYGAHLDPTQqleeipnHQGLTPLKLAA 212
|
250
....*....|...
gi 568921145 1054 QEGHVDVVQVLLE 1066
Cdd:cd21882 213 VEGKIVMFQHILQ 225
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
781-834 |
1.79e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 43.42 E-value: 1.79e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 568921145 781 GRTPLLAAASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRTLL 834
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
734-785 |
1.94e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 43.49 E-value: 1.94e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 568921145 734 LIDRG-AEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPL 785
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
1044-1075 |
2.16e-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: 42.66 E-value: 2.16e-05
10 20 30
....*....|....*....|....*....|...
gi 568921145 1044 QGATALCIAA-QEGHVDVVQVLLEHGADPNHAD 1075
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
676-707 |
2.63e-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: 2.63e-05
10 20 30
....*....|....*....|....*....|...
gi 568921145 676 EGRTAL-IAAAYMGHREIVEHLLDHGAEVNHED 707
Cdd:pfam00023 1 DGNTPLhLAAGRRGNLEIVKLLLSKGADVNARD 33
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
1046-1102 |
2.70e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 48.74 E-value: 2.70e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 568921145 1046 ATALCIAAQEGHVDVVQVLLEHGADPNHADQFGRTAMRVAAKNGHSQIIKLLEKYGA 1102
Cdd:PTZ00322 83 TVELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGA 139
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
1025-1102 |
3.28e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 48.12 E-value: 3.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 1025 VKVVQLLIEHGAVVDHTCNQGATALCIAAQEGHV-----DVVQVLLEHGADPNHADQFGRTAMRVAA--KNGHSQIIKLL 1097
Cdd:PHA03100 48 IDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYL 127
|
....*
gi 568921145 1098 EKYGA 1102
Cdd:PHA03100 128 LDNGA 132
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
896-957 |
3.35e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 48.36 E-value: 3.35e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568921145 896 VQILLENKSNIDQRGYDGRNALRVAALEGHRDIVELLFSHGADVNYKDADGRpTLYILALEN 957
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGK-TPLELAEEN 158
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
654-935 |
3.76e-05 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 48.13 E-value: 3.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 654 GGHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLDHGAEVNHEDVDGRTALSVAAlcvPASKGHASVVSL 733
Cdd:PHA02946 49 GLDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLS---GTDDEVIERINL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 734 LIDRGAEVDH-CDKDGMTPLLvAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLA--AASMGHASVVNTLLFWGAAVDSI 810
Cdd:PHA02946 126 LVQYGAKINNsVDEEGCGPLL-ACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRhlMSDNPKASTISWMMKLGISPSKP 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 811 DSEGRTVLSIASAQ--GNVEVVRTLLDrGLDESHRDDAGWTPLHM--AAFEGHRLICEALIEQGARTNE----------- 875
Cdd:PHA02946 205 DHDGNTPLHIVCSKtvKNVDIINLLLP-STDVNKQNKFGDSPLTLliKTLSPAHLINKLLSTSNVITDQtvnicifydrd 283
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 876 -----IDNDGR----IPFILASQEGHYDCVQILLENKSNIDqrgydgrNALRVAALEGHRDIVE-LLFSH 935
Cdd:PHA02946 284 dvleiINDKGKqydsTDFKMAVEVGSIRCVKYLLDNDIICE-------DAMYYAVLSEYETMVDyLLFNH 346
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
495-613 |
3.95e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 46.35 E-value: 3.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 495 EVLQLLIRAGAHVN--SEDDHTSCI-----VRQALErEDSIRTLLDNGASVNQCDSNGRTLLAN--AAYSGSLDVVNLLV 565
Cdd:PHA02859 67 EILKFLIENGADVNfkTRDNNLSALhhylsFNKNVE-PEILKILIDSGSSITEEDEDGKNLLHMymCNFNVRINVIKLLI 145
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 568921145 566 SRGADLEIEDAHG----HTPLTLAARQghtKVVNCLIGCGANINHTDQDGWT 613
Cdd:PHA02859 146 DSGVSFLNKDFDNnnilYSYILFHSDK---KIFDFLTSLGIDINETNKSGYN 194
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
1044-1072 |
4.00e-05 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 41.80 E-value: 4.00e-05
10 20
....*....|....*....|....*....
gi 568921145 1044 QGATALCIAAQEGHVDVVQVLLEHGADPN 1072
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
747-775 |
4.82e-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: 4.82e-05
10 20
....*....|....*....|....*....
gi 568921145 747 DGMTPLLVAAYEGHVDVVDLLLEGGADVD 775
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
766-821 |
7.08e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 41.95 E-value: 7.08e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 568921145 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 |
8.68e-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: 40.65 E-value: 8.68e-05
10 20
....*....|....*....|....*....
gi 568921145 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 |
9.50e-05 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 40.70 E-value: 9.50e-05
10 20 30
....*....|....*....|....*....|
gi 568921145 747 DGMTPLLVAAYEGHVDVVDLLLEGGADVDH 776
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
577-605 |
1.04e-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: 1.04e-04
10 20
....*....|....*....|....*....
gi 568921145 577 HGHTPLTLAARQGHTKVVNCLIGCGANIN 605
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
663-734 |
1.31e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 46.43 E-value: 1.31e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568921145 663 LLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLDHGAEVNHEDVDGRTALSVAalcvpASKGHASVVSLL 734
Cdd:PTZ00322 101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA-----EENGFREVVQLL 167
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
978-1007 |
1.39e-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: 1.39e-04
10 20 30
....*....|....*....|....*....|
gi 568921145 978 EGRTALHVSCWQGHVEMVRVLIACHADVNA 1007
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
584-674 |
1.67e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 46.04 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 584 LAArQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGHTEVVSALLYAGVKVDCADADSRTALRAAAWGGHEDIVLNL 663
Cdd:PTZ00322 89 LAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
|
90
....*....|.
gi 568921145 664 LQHGAEVNKAD 674
Cdd:PTZ00322 168 SRHSQCHFELG 178
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
691-862 |
1.97e-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: 45.90 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 691 EIVEHLL----DHG-------AEVNHEDVDGRTALSVAAlcvpaSKGHASVVSLLIDRGAEVDHCDKD------------ 747
Cdd:cd22194 111 EIVRILLafaeENGildrfinAEYTEEAYEGQTALNIAI-----ERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegf 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 748 --GMTPLLVAAYEGHVDVVDLLLEggadvdhtdnNGRTPLLAAASMGhasvvNTLLFwgAAVD-SIDSEGRTVLSIasaQ 824
Cdd:cd22194 186 yfGETPLALAACTNQPEIVQLLME----------KESTDITSQDSRG-----NTVLH--ALVTvAEDSKTQNDFVK---R 245
|
170 180 190
....*....|....*....|....*....|....*...
gi 568921145 825 GNVEVVRTLLDRGLdESHRDDAGWTPLHMAAFEGHRLI 862
Cdd:cd22194 246 MYDMILLKSENKNL-ETIRNNEGLTPLQLAAKMGKAEI 282
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
710-857 |
2.27e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).
Pssm-ID: 411975 [Multi-domain] Cd Length: 600 Bit Score: 45.64 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 710 GRTALSVAALcvpasKGHASVVSLLIDRGAEVD-------------HCDKDGMTPLLVAAYEGHVDVVDLLLEGGAD--- 773
Cdd:cd21882 73 GQTALHIAIE-----NRNLNLVRLLVENGADVSaratgrffrkspgNLFYFGELPLSLAACTNQEEIVRLLLENGAQpaa 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 774 VDHTDNNGRTPLLAAASMGHASVVNT---------LLFWGAAVDSIDS-------EGRTVLSIASAQGNVEVVRTLLDRG 837
Cdd:cd21882 148 LEAQDSLGNTVLHALVLQADNTPENSafvcqmynlLLSYGAHLDPTQQleeipnhQGLTPLKLAAVEGKIVMFQHILQRE 227
|
170 180
....*....|....*....|....*.
gi 568921145 838 LDESH----RDDAGWT--PLHMAAFE 857
Cdd:cd21882 228 FSGPYqplsRKFTEWTygPVTSSLYD 253
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
899-954 |
2.28e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 40.41 E-value: 2.28e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 568921145 899 LLENKS-NIDQRGYDGRNALRVAALEGHRDIVELLFSHGADVNYKDADGrPTLYILA 954
Cdd:pfam13857 1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEG-LTALDLA 56
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
978-1007 |
2.74e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 39.49 E-value: 2.74e-04
10 20 30
....*....|....*....|....*....|
gi 568921145 978 EGRTALHVSCWQGHVEMVRVLIACHADVNA 1007
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| 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 568921145 658 DIVLNLLQHGAEVN-KADNEGRTALiaAAYMGHR-----EIVEHLLDHGAEVNHEDVDGRTALSVaALCVPASKghASVV 731
Cdd:PHA02859 67 EILKFLIENGADVNfKTRDNNLSAL--HHYLSFNknvepEILKILIDSGSSITEEDEDGKNLLHM-YMCNFNVR--INVI 141
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 568921145 732 SLLIDRGAEVDHCDKDGmTPLLVAAYEGHVD--VVDLLLEGGADVDHTDNNGRTP 784
Cdd:PHA02859 142 KLLIDSGVSFLNKDFDN-NNILYSYILFHSDkkIFDFLTSLGIDINETNKSGYNC 195
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
577-608 |
3.25e-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: 3.25e-04
10 20 30
....*....|....*....|....*....|...
gi 568921145 577 HGHTPLTLAA-RQGHTKVVNCLIGCGANINHTD 608
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
499-577 |
3.35e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 44.66 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 499 LLIRAGAHVNSEDD------HTSCIVrqalEREDSIRTLLDNGASVNQCDSNGRTLLANAAYSGSLDVVNLLVSRGADLE 572
Cdd:PHA03100 177 YLLSYGVPINIKDVygftplHYAVYN----NNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
|
....*
gi 568921145 573 IEDAH 577
Cdd:PHA03100 253 TIIET 257
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
912-941 |
3.60e-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: 3.60e-04
10 20 30
....*....|....*....|....*....|
gi 568921145 912 DGRNALRVAALEGHRDIVELLFSHGADVNY 941
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
481-573 |
4.65e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 44.21 E-value: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 481 PVKDSLSTL----IPKEQEVLQLLIRAGAHVNSED--DHTSCIVRQALEREDSIRTLLDNGASVNQCDSNGR-TLLANAA 553
Cdd:PHA02875 131 PNTDKFSPLhlavMMGDIKGIELLIDHKACLDIEDccGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAI 210
|
90 100
....*....|....*....|
gi 568921145 554 YSGSLDVVNLLVSRGADLEI 573
Cdd:PHA02875 211 ENNKIDIVRLFIKRGADCNI 230
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
497-609 |
4.65e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 44.57 E-value: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 497 LQLLIRAGAHVNSEDDHTSCIVRQALEREDSIRTLLDNGASVNQCDSNGRTLLANA-AYSGSLDVVNLLVSRGADLEIED 575
Cdd:PHA02874 206 IKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIELLINNASINDQDIDGSTPLHHAiNPPCDIDIIDILLYHKADISIKD 285
|
90 100 110
....*....|....*....|....*....|....*
gi 568921145 576 AHGHTPLTLAARQ-GHTKVVNCLIGCGANINHTDQ 609
Cdd:PHA02874 286 NKGENPIDTAFKYiNKDPVIKDIIANAVLIKEADK 320
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
847-878 |
5.01e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 38.81 E-value: 5.01e-04
10 20 30
....*....|....*....|....*....|...
gi 568921145 847 GWTPLHMAA-FEGHRLICEALIEQGARTNEIDN 878
Cdd:pfam00023 2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
|
|
| TRPV2 |
cd22197 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ... |
885-1066 |
5.37e-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: 44.46 E-value: 5.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 885 ILASQEGHYDCVQILLEnksnIDQRG---------------YDGRNALRVAALEGHRDIVELLFSHGADVNYKdADGR-- 947
Cdd:cd22197 55 VLNLQDGVNACIMPLLE----IDKDSgnpkplvnaqctdeyYRGHSALHIAIEKRSLQCVKLLVENGADVHAR-ACGRff 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 948 -------------PtLYILALENQLTMAEYFLENG---ANVEASDAEGRTALhvscwqghvemvrvliacHADVNAADN- 1010
Cdd:cd22197 130 qkkqgtcfyfgelP-LSLAACTKQWDVVNYLLENPhqpASLQAQDSLGNTVL------------------HALVMIADNs 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 568921145 1011 EKRSALQSAAWQGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQEGHVDVVQVLLE 1066
Cdd:cd22197 191 PENSALVIKMYDGLLQAGARLCPTVQLEEISNHEGLTPLKLAAKEGKIEIFRHILQ 246
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
709-746 |
5.75e-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: 5.75e-04
10 20 30
....*....|....*....|....*....|....*...
gi 568921145 709 DGRTALSVAAlcvpASKGHASVVSLLIDRGAEVDHCDK 746
Cdd:pfam00023 1 DGNTPLHLAA----GRRGNLEIVKLLLSKGADVNARDK 34
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
696-755 |
5.75e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 39.25 E-value: 5.75e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568921145 696 LLDHG-AEVNHEDVDGRTALSVAAlcvpaSKGHASVVSLLIDRGAEVDHCDKDGMTPLLVA 755
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAA-----KYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02989 |
PHA02989 |
ankyrin repeat protein; Provisional |
495-717 |
5.90e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222954 [Multi-domain] Cd Length: 494 Bit Score: 44.35 E-value: 5.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 495 EVLQLLIRAGAHVNSED--DHTSCIVRQALEREDS-----IRTLLDNGASVNQCDSNGRTLLANAAYS---GSLDVVNLL 564
Cdd:PHA02989 51 KIVKLLIDNGADVNYKGyiETPLCAVLRNREITSNkikkiVKLLLKFGADINLKTFNGVSPIVCFIYNsniNNCDMLRFL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 565 VSRGADL-EIEDAHGHTPLTLAARQGHTK--VVNCLIGCGANI-NHTDQDGWTA----LRSAAWGGHTEVVSALLYAGVK 636
Cdd:PHA02989 131 LSKGINVnDVKNSRGYNLLHMYLESFSVKkdVIKILLSFGVNLfEKTSLYGLTPmniyLRNDIDVISIKVIKYLIKKGVN 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 637 VDCADADSRTALRA-----AAWGGHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLDHGAEVNHEDVDGR 711
Cdd:PHA02989 211 IETNNNGSESVLESfldnnKILSKKEFKVLNFILKYIKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGD 290
|
....*.
gi 568921145 712 TALSVA 717
Cdd:PHA02989 291 TVLTYA 296
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
577-606 |
6.14e-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: 6.14e-04
10 20 30
....*....|....*....|....*....|
gi 568921145 577 HGHTPLTLAARQGHTKVVNCLIGCGANINH 606
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
912-943 |
6.60e-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: 6.60e-04
10 20 30
....*....|....*....|....*....|...
gi 568921145 912 DGRNALRVAALE-GHRDIVELLFSHGADVNYKD 943
Cdd:pfam00023 1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
676-705 |
7.84e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 38.01 E-value: 7.84e-04
10 20 30
....*....|....*....|....*....|
gi 568921145 676 EGRTALIAAAYMGHREIVEHLLDHGAEVNH 705
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| PHA02989 |
PHA02989 |
ankyrin repeat protein; Provisional |
492-697 |
1.04e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222954 [Multi-domain] Cd Length: 494 Bit Score: 43.19 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 492 KEQEVLQLLIRAGAHVNSED-DHTSCIV----RQALEREDSIRTLLDNGASVNQC-DSNGRTLLAN--AAYSGSLDVVNL 563
Cdd:PHA02989 86 KIKKIVKLLLKFGADINLKTfNGVSPIVcfiyNSNINNCDMLRFLLSKGINVNDVkNSRGYNLLHMylESFSVKKDVIKI 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 564 LVSRGAD-LEIEDAHGHTPLTLAARQG----HTKVVNCLIGCGANINHTDQDGWTALRS------AAWGGHTEVVSALLy 632
Cdd:PHA02989 166 LLSFGVNlFEKTSLYGLTPMNIYLRNDidviSIKVIKYLIKKGVNIETNNNGSESVLESfldnnkILSKKEFKVLNFIL- 244
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568921145 633 AGVKVDCADADSRTALRAAAWGGHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLL 697
Cdd:PHA02989 245 KYIKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNRIL 309
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
1026-1110 |
1.49e-03 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 42.73 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 1026 KVVQLLIEHGAVVDHTCNQGATALCIAAQEGHVDVVQVLLEHGADPNHADQFGRTAMRVAAKNGHSQI--IKLLEKYGAS 1103
Cdd:PHA02946 53 RFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIerINLLVQYGAK 132
|
90
....*....|..
gi 568921145 1104 SLN-----GCSP 1110
Cdd:PHA02946 133 INNsvdeeGCGP 144
|
|
| PHA02989 |
PHA02989 |
ankyrin repeat protein; Provisional |
493-801 |
1.53e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222954 [Multi-domain] Cd Length: 494 Bit Score: 42.81 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 493 EQEVLQLLIRAGAHVNSEDDHTSCIVRQaLEREDS----IRTLLDNGASVNQ---CDSNGRTLLANAAYSGSL--DVVNL 563
Cdd:PHA02989 15 DKNALEFLLRTGFDVNEEYRGNSILLLY-LKRKDVkikiVKLLIDNGADVNYkgyIETPLCAVLRNREITSNKikKIVKL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 564 LVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCL---IGCGANINHT-DQDGWTALRSAAWGG--HTEVVSALLYAGVKV 637
Cdd:PHA02989 94 LLKFGADINLKTFNGVSPIVCFIYNSNINNCDMLrflLSKGINVNDVkNSRGYNLLHMYLESFsvKKDVIKILLSFGVNL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 638 DCADADSRTA-----LRAAAWGGHEDIVLNLLQHGAEVNKADNegrtaliaaaymGHREIVEHLLDhgaevNHEDVdgrt 712
Cdd:PHA02989 174 FEKTSLYGLTpmniyLRNDIDVISIKVIKYLIKKGVNIETNNN------------GSESVLESFLD-----NNKIL---- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 713 alsvaalcvpaSKGHASVVSLLIDRgAEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMG 792
Cdd:PHA02989 233 -----------SKKEFKVLNFILKY-IKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHG 300
|
....*....
gi 568921145 793 HASVVNTLL 801
Cdd:PHA02989 301 NIDMLNRIL 309
|
|
| PHA02795 |
PHA02795 |
ankyrin-like protein; Provisional |
538-589 |
1.66e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165157 [Multi-domain] Cd Length: 437 Bit Score: 42.67 E-value: 1.66e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 568921145 538 VNQCDSNGRTLLANAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLAARQG 589
Cdd:PHA02795 214 INQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRG 265
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
908-1084 |
1.74e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).
Pssm-ID: 411975 [Multi-domain] Cd Length: 600 Bit Score: 42.94 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 908 QRGYDGRNALRVAAL---EGHRDIVELLFshgadvnykDADgRPTLYILALENQLTMAEYFlenganveasdaEGRTALH 984
Cdd:cd21882 21 QRGATGKTCLHKAALnlnDGVNEAIMLLL---------EAA-PDSGNPKELVNAPCTDEFY------------QGQTALH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 985 VSCWQGHVEMVRVLIACHADVNAADNekrsalqSAAWQGHvkvvqlliehgavvDHTCNQ-GATALCIAAQEGHVDVVQV 1063
Cdd:cd21882 79 IAIENRNLNLVRLLVENGADVSARAT-------GRFFRKS--------------PGNLFYfGELPLSLAACTNQEEIVRL 137
|
170 180
....*....|....*....|....
gi 568921145 1064 LLEHGADP---NHADQFGRTAMRV 1084
Cdd:cd21882 138 LLENGAQPaalEAQDSLGNTVLHA 161
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
912-940 |
1.90e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 37.24 E-value: 1.90e-03
10 20
....*....|....*....|....*....
gi 568921145 912 DGRNALRVAALEGHRDIVELLFSHGADVN 940
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
959-1095 |
2.03e-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: 42.44 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 959 LTMAEyflENG-------ANVEASDAEGRTALHVSCWQGHVEMVRVLIACHADVNAAD-----NEK---------RSALQ 1017
Cdd:cd22194 117 LAFAE---ENGildrfinAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAkgvffNPKykhegfyfgETPLA 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 1018 SAAWQGHVKVVQLLIEH----GAVVDHTCNQGATALCIAAQ--EGHVDVV-----QVLLEHG-----ADPNHAdqfGRTA 1081
Cdd:cd22194 194 LAACTNQPEIVQLLMEKestdITSQDSRGNTVLHALVTVAEdsKTQNDFVkrmydMILLKSEnknleTIRNNE---GLTP 270
|
170
....*....|....
gi 568921145 1082 MRVAAKNGHSQIIK 1095
Cdd:cd22194 271 LQLAAKMGKAEILK 284
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
720-858 |
2.39e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 40.96 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 720 CVPASKGHASVVSLLIDRGAEVDHCDKD-GMTPL---LVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPL---LAAASMg 792
Cdd:PHA02859 58 CLEKDKVNVEILKFLIENGADVNFKTRDnNLSALhhyLSFNKNVEPEILKILIDSGSSITEEDEDGKNLLhmyMCNFNV- 136
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568921145 793 HASVVNTLLFWGAAVDSIDSEGRTVL-SIASAQGNVEVVRTLLDRGLDESHRDDAGWTPLHMAAFEG 858
Cdd:PHA02859 137 RINVIKLLIDSGVSFLNKDFDNNNILySYILFHSDKKIFDFLTSLGIDINETNKSGYNCYDLIKFRN 203
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
22-195 |
2.45e-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: 40.18 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 22 QFYCREWVFHKLQHCLQekwsccsgpataqslvgnagnnaSAISGKGASwgVLLVGGPGSGKTALCTELLwpsspaslqR 101
Cdd:pfam13191 1 RLVGREEELEQLLDALD-----------------------RVRSGRPPS--VLLTGEAGTGKTTLLRELL---------R 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 102 GLHRQALAFHFCKAQD-------SDTLCVGGFIRGLVAQIcQSGLLQGYEDKLRDPAVQSLLEPGECERNPAEAFKRCVL 174
Cdd:pfam13191 47 ALERDGGYFLRGKCDEnlpysplLEALTREGLLRQLLDEL-ESSLLEAWRAALLEALAPVPELPGDLAERLLDLLLRLLD 125
|
170 180
....*....|....*....|.
gi 568921145 175 LPLLGMKPppqsLYLLVDSVD 195
Cdd:pfam13191 126 LLARGERP----LVLVLDDLQ 142
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
492-588 |
2.55e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 42.17 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 492 KEQEVLQLLIRAGAHVNSEDDHTSCIVRQALE--REDSIRTLLDNGASVNQCDSNGRTLL-------------------- 549
Cdd:PHA02878 179 KDQRLTELLLSYGANVNIPDKTNNSPLHHAVKhyNKPIVHILLENGASTDARDKCGNTPLhisvgyckdydilklllehg 258
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 568921145 550 --ANAAYS-----------GSLDVVNLLVSRGADLEIEDAHGHTPLTLAARQ 588
Cdd:PHA02878 259 vdVNAKSYilgltalhssiKSERKLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
780-811 |
3.03e-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: 3.03e-03
10 20 30
....*....|....*....|....*....|...
gi 568921145 780 NGRTPL-LAAASMGHASVVNTLLFWGAAVDSID 811
Cdd:pfam00023 1 DGNTPLhLAAGRRGNLEIVKLLLSKGADVNARD 33
|
|
| PHA02795 |
PHA02795 |
ankyrin-like protein; Provisional |
927-1041 |
3.33e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165157 [Multi-domain] Cd Length: 437 Bit Score: 41.52 E-value: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 927 DIVELLFSHGADVNYKDADGRPTLYILALENQLTMAEYFLENGANVEASDAEGRTALHVSCWQG--------HVEMVRVL 998
Cdd:PHA02795 202 EIYKLCIPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRGsviarretHLKILEIL 281
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 568921145 999 IACHADVNAAdnekRSALQSAAWQGHvKVVQLLIEHGAVVDHT 1041
Cdd:PHA02795 282 LREPLSIDCI----KLAILNNTIENH-DVIKLCIKYFMMVDYS 319
|
|
| PHA02716 |
PHA02716 |
CPXV016; CPX019; EVM010; Provisional |
729-851 |
3.41e-03 |
|
CPXV016; CPX019; EVM010; Provisional
Pssm-ID: 165089 [Multi-domain] Cd Length: 764 Bit Score: 41.82 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 729 SVVSLLIDRGAEVDHCDKDGMTPL--LVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMghASVVNTLlfwgaa 806
Cdd:PHA02716 298 SVVYSFLQPGVKLHYKDSAGRTCLhqYILRHNISTDIIKLLHEYGNDLNEPDNIGNTVLHTYLSM--LSVVNIL------ 369
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 568921145 807 vdsiDSEGRTVLsiasaqgNVEVVRTLLDRGLDESHRDDAGWTPL 851
Cdd:PHA02716 370 ----DPETDNDI-------RLDVIQCLISLGADITAVNCLGYTPL 403
|
|
| 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 568921145 545 GRTLLANAAYSGSLDVVNLLVSRGADLEIEDA--------------HGHTPLTLAARQGHTKVVNCLIGCGANINHTDQD 610
Cdd:cd22192 89 GETALHIAVVNQNLNLVRELIARGADVVSPRAtgtffrpgpknliyYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168
|
....*
gi 568921145 611 GWTAL 615
Cdd:cd22192 169 GNTVL 173
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
1025-1101 |
3.80e-03 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 41.78 E-value: 3.80e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568921145 1025 VKVVQLLIEHGAvvDHTCNQGATALCIAAQEGHVDVVQVLLEHGADPNHADQFGRTAMRVAAKNGHSQIIKLLEKYG 1101
Cdd:PLN03192 507 LNVGDLLGDNGG--EHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA 581
|
|
| TRPV2 |
cd22197 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ... |
710-843 |
4.58e-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: 41.38 E-value: 4.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 710 GRTALSVAAlcvpaSKGHASVVSLLIDRGAEV-------------DHCDKDGMTPLLVAAYEGHVDVVDLLLEGGAD--- 773
Cdd:cd22197 94 GHSALHIAI-----EKRSLQCVKLLVENGADVharacgrffqkkqGTCFYFGELPLSLAACTKQWDVVNYLLENPHQpas 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 774 VDHTDNNGRTPLLAAASMGHASVVNT---------LLFWGAAVDS-------IDSEGRTVLSIASAQGNVEVVRTLLDRG 837
Cdd:cd22197 169 LQAQDSLGNTVLHALVMIADNSPENSalvikmydgLLQAGARLCPtvqleeiSNHEGLTPLKLAAKEGKIEIFRHILQRE 248
|
....*.
gi 568921145 838 LDESHR 843
Cdd:cd22197 249 FSGPYQ 254
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
847-871 |
4.65e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 36.08 E-value: 4.65e-03
|
| TRPV2 |
cd22197 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ... |
748-858 |
4.91e-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: 41.38 E-value: 4.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 748 GMTPLLVAAYEGHVDVVDLLLEGGADVdHTDNNGR--------------TPLLAAASMGHASVVNTLL---FWGAAVDSI 810
Cdd:cd22197 94 GHSALHIAIEKRSLQCVKLLVENGADV-HARACGRffqkkqgtcfyfgeLPLSLAACTKQWDVVNYLLenpHQPASLQAQ 172
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568921145 811 DSEGRTVLS----IA-SAQGNVEVVRTLLDRGLDESHRDD-----------AGWTPLHMAAFEG 858
Cdd:cd22197 173 DSLGNTVLHalvmIAdNSPENSALVIKMYDGLLQAGARLCptvqleeisnhEGLTPLKLAAKEG 236
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
710-869 |
5.05e-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: 41.40 E-value: 5.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 710 GRTALSVAALCVpaSKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGH-----------VDVVDLLLEGGADVdHTD 778
Cdd:cd21882 26 GKTCLHKAALNL--NDGVNEAIMLLLEAAPDSGNPKELVNAPCTDEFYQGQtalhiaienrnLNLVRLLVENGADV-SAR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 779 NNGRT--------------PLLAAASMGHASVVNTLLFWG---AAVDSIDSEGRTVLSIASAQGNVEVVRTLL------- 834
Cdd:cd21882 103 ATGRFfrkspgnlfyfgelPLSLAACTNQEEIVRLLLENGaqpAALEAQDSLGNTVLHALVLQADNTPENSAFvcqmynl 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 568921145 835 ----DRGLD-----ESHRDDAGWTPLHMAAFEGHRLICEALIEQ 869
Cdd:cd21882 183 llsyGAHLDptqqlEEIPNHQGLTPLKLAAVEGKIVMFQHILQR 226
|
|
| PHA02795 |
PHA02795 |
ankyrin-like protein; Provisional |
658-812 |
5.49e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165157 [Multi-domain] Cd Length: 437 Bit Score: 41.13 E-value: 5.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 658 DIVLNLLQHGAEVNKAdnEGRTALIAAAYMGHREIVEHLLDHGA----EVNHE-----------DVDGRTALSVAALCVP 722
Cdd:PHA02795 132 DIVDFMVDHGAVIYKI--ECLNAYFRGICKKESSVVEFILNCGIpdenDVKLDlykiiqytrgfLVDEPTVLEIYKLCIP 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 723 ASKghasvvsllidrgaEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMG--------HA 794
Cdd:PHA02795 210 YIE--------------DINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRGsviarretHL 275
|
170
....*....|....*...
gi 568921145 795 SVVNTLLFWGAAVDSIDS 812
Cdd:PHA02795 276 KILEILLREPLSIDCIKL 293
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
879-907 |
5.71e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 35.64 E-value: 5.71e-03
10 20
....*....|....*....|....*....
gi 568921145 879 DGRIPFILASQEGHYDCVQILLENKSNID 907
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
|
|
| PHA02795 |
PHA02795 |
ankyrin-like protein; Provisional |
669-777 |
6.30e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165157 [Multi-domain] Cd Length: 437 Bit Score: 40.75 E-value: 6.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 669 EVNKADNEGRTALIAAAYMGHREIVEHLLDHGAEVNHEDVDGRTALSVA---ALCVPASKGHASVVSLLIDRGAEVDhCD 745
Cdd:PHA02795 213 DINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAvdrGSVIARRETHLKILEILLREPLSID-CI 291
|
90 100 110
....*....|....*....|....*....|..
gi 568921145 746 KdgmTPLLVAAYEGHvDVVDLLLEGGADVDHT 777
Cdd:PHA02795 292 K---LAILNNTIENH-DVIKLCIKYFMMVDYS 319
|
|
| PHA02989 |
PHA02989 |
ankyrin repeat protein; Provisional |
894-1094 |
6.66e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222954 [Multi-domain] Cd Length: 494 Bit Score: 40.88 E-value: 6.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 894 DCVQILLENKSNIDQRGYDGR---NALRVAALEGH--RDIVELLFSHGADVNYKDADGRPTLYILALE---NQLTMAEYF 965
Cdd:PHA02989 51 KIVKLLIDNGADVNYKGYIETplcAVLRNREITSNkiKKIVKLLLKFGADINLKTFNGVSPIVCFIYNsniNNCDMLRFL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 966 LENGANV-EASDAEGRTALHV---SCWQG-------------------------------------HVEMVRVLIACHAD 1004
Cdd:PHA02989 131 LSKGINVnDVKNSRGYNLLHMyleSFSVKkdvikillsfgvnlfektslygltpmniylrndidviSIKVIKYLIKKGVN 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 1005 VNAADNEKRSALQS------AAWQGHVKVVQLLIEHgAVVDHTCNQGATALCIAAQEGHVDVVQVLLEHGADPNHADQFG 1078
Cdd:PHA02989 211 IETNNNGSESVLESfldnnkILSKKEFKVLNFILKY-IKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDG 289
|
250
....*....|....*.
gi 568921145 1079 RTAMRVAAKNGHSQII 1094
Cdd:PHA02989 290 DTVLTYAIKHGNIDML 305
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
1064-1103 |
8.22e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 36.17 E-value: 8.22e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 568921145 1064 LLEHG-ADPNHADQFGRTAMRVAAKNGHSQIIKLLEKYGAS 1103
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVD 41
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
645-675 |
8.44e-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: 8.44e-03
10 20 30
....*....|....*....|....*....|..
gi 568921145 645 RTAL-RAAAWGGHEDIVLNLLQHGAEVNKADN 675
Cdd:pfam00023 3 NTPLhLAAGRRGNLEIVKLLLSKGADVNARDK 34
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
826-940 |
8.58e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 39.42 E-value: 8.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 826 NVEVVRTLLDRGLDESHR-DDAGWTPLHmaafegHRL---------ICEALIEQGARTNEIDNDGRIPF--ILASQEGHY 893
Cdd:PHA02859 65 NVEILKFLIENGADVNFKtRDNNLSALH------HYLsfnknvepeILKILIDSGSSITEEDEDGKNLLhmYMCNFNVRI 138
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 568921145 894 DCVQILLENKSNIDQRGYDGRNALRVAAL-EGHRDIVELLFSHGADVN 940
Cdd:PHA02859 139 NVIKLLIDSGVSFLNKDFDNNNILYSYILfHSDKKIFDFLTSLGIDIN 186
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
493-584 |
8.73e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 39.42 E-value: 8.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921145 493 EQEVLQLLIRAGAHVNSEDDHTSCIVRQALE----REDSIRTLLDNGASVNQCDSNGRTLLAN-AAYSGSLDVVNLLVSR 567
Cdd:PHA02859 102 EPEILKILIDSGSSITEEDEDGKNLLHMYMCnfnvRINVIKLLIDSGVSFLNKDFDNNNILYSyILFHSDKKIFDFLTSL 181
|
90
....*....|....*..
gi 568921145 568 GADLEIEDAHGHTPLTL 584
Cdd:PHA02859 182 GIDINETNKSGYNCYDL 198
|
|
|