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Conserved domains on  [gi|2131006785|ref|XP_044890140|]
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serine/threonine-protein phosphatase 6 regulatory ankyrin repeat subunit B isoform X2 [Felis catus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
76-365 6.75e-52

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 184.39  E-value: 6.75e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785   76 AEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSV 155
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  156 NVSDRGGRTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAA 235
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  236 ASNGQINVVKHLLNLGVEIDEINIYGNTALHLACYNGQDAVVNELTDYGANVNQPNNSGFTPLHFAAASTHGALcLELLV 315
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI-VKLLL 239

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 2131006785  316 NNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPL 365
Cdd:COG0666    240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
532-789 6.44e-38

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.94  E-value: 6.44e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  532 NAHENSEELERARELKEKEAALCLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNNGFEESDSGATksPL 611
Cdd:COG0666     14 ALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNT--LL 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  612 HLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASIFVKDNvTKRTPLHASVINGHTLCLR 691
Cdd:COG0666     92 HAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN-DGNTPLHLAAANGNLEIVK 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  692 LLLEI-ADnpeaIDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALHRGIMTGHEECVQMLLEQEVSIL 770
Cdd:COG0666    171 LLLEAgAD----VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246

                          250
                   ....*....|....*....
gi 2131006785  771 CKDSRGRTPLHYAAARGHA 789
Cdd:COG0666    247 AKDKDGLTALLLAAAAGAA 265
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
690-1016 3.06e-34

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.54  E-value: 3.06e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  690 LRLLLEIADNPEAIDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALHRGIMTGHEECVQMLLEQEVSI 769
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  770 LCKDSRGRTPLHYAAARGHATWLSELLQmalSEEDCSFKDNQGYTPLHWACYNGNENCIEVLLEQkcfrtfignpftplh 849
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLE---AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA--------------- 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  850 caiindhencaslllGAIdssiVNCRDDKGRTPLHAAAFADHVECLQLLLRHSAEVNAADNSGKTALMMAAENGQAGAVD 929
Cdd:COG0666    143 ---------------GAD----VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  930 ILVNsAQADLTVKDKDLNTSLHLASSKGHEKCALLILDKIQDeslINARNNALQTPLHVAARNGLKVVVEELLAKGACVL 1009
Cdd:COG0666    204 LLLE-AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD---LNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLA 279


                   ....*..
gi 2131006785 1010 AIDENGI 1016
Cdd:COG0666    280 AALLDLL 286
PHA03095 super family cl33707
ankyrin-like protein; Provisional
 234-515 1.79e-25

ankyrin-like protein; Provisional


The actual alignment was detected with superfamily member PHA03095:

Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 111.27  E-value: 1.79e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  234 AAASNGQINVVKHLLNLGVEIDEINIYGNTALH--LACYNGQDA-VVNELTDYGANVNQPNNSGFTPLHFAAASTHGALC 310
Cdd:PHA03095    20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHlyLHYSSEKVKdIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDV 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  311 LELLVNNGADVNIQSKDGKSPLH--MTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGH---ELLiNTLITSGA 385
Cdd:PHA03095   100 IKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanvELL-RLLIDAGA 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  386 DTAKCGIHSMFPLHLAALNAHSDccrkllssgqkYSIVslfsnEHVLSAGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQ 465
Cdd:PHA03095   179 DVYAVDDRFRSLLHHHLQSFKPR-----------ARIV-----RELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVLP 242

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2131006785  466 --SSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVNETDDWGRTAL 515
Cdd:PHA03095   243 llIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294
Ank_4 pfam13637
Ankyrin repeats (many copies);
32-83 2.19e-06

Ankyrin repeats (many copies);


:

Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.73  E-value: 2.19e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2131006785   32 PPLVQAIFSGDPEEIRMLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLI 83
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
76-365 6.75e-52

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 184.39  E-value: 6.75e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785   76 AEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSV 155
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  156 NVSDRGGRTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAA 235
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  236 ASNGQINVVKHLLNLGVEIDEINIYGNTALHLACYNGQDAVVNELTDYGANVNQPNNSGFTPLHFAAASTHGALcLELLV 315
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI-VKLLL 239

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 2131006785  316 NNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPL 365
Cdd:COG0666    240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA03095 PHA03095
ankyrin-like protein; Provisional
 108-381 5.11e-39

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 152.10  E-value: 5.11e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  108 SEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSS---VNVSDRGGRTALHHAALNGHVE-MVNLLLA 183
Cdd:PHA03095    26 TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIVRLLLEAgadVNAPERCGFTPLHLYLYNATTLdVIKLLIK 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  184 KGANINAFDKKDRRALHwaAYMG----HLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINV--VKHLLNLGVEIDEI 257
Cdd:PHA03095   106 AGADVNAKDKVGRTPLH--VYLSgfniNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVYAV 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  258 NIYGNTALHLACYNGQD--AVVNELTDYGANVNQPNNSGFTPLHFAAA-STHGALCLELLVNNGADVNIQSKDGKSPLHM 334
Cdd:PHA03095   184 DDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHSMATgSSCKRSLVLPLLIAGISINARNRYGQTPLHY 263

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 2131006785  335 TAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLI 381
Cdd:PHA03095   264 AAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
532-789 6.44e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.94  E-value: 6.44e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  532 NAHENSEELERARELKEKEAALCLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNNGFEESDSGATksPL 611
Cdd:COG0666     14 ALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNT--LL 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  612 HLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASIFVKDNvTKRTPLHASVINGHTLCLR 691
Cdd:COG0666     92 HAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN-DGNTPLHLAAANGNLEIVK 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  692 LLLEI-ADnpeaIDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALHRGIMTGHEECVQMLLEQEVSIL 770
Cdd:COG0666    171 LLLEAgAD----VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246

                          250
                   ....*....|....*....
gi 2131006785  771 CKDSRGRTPLHYAAARGHA 789
Cdd:COG0666    247 AKDKDGLTALLLAAAAGAA 265
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
690-1016 3.06e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.54  E-value: 3.06e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  690 LRLLLEIADNPEAIDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALHRGIMTGHEECVQMLLEQEVSI 769
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  770 LCKDSRGRTPLHYAAARGHATWLSELLQmalSEEDCSFKDNQGYTPLHWACYNGNENCIEVLLEQkcfrtfignpftplh 849
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLE---AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA--------------- 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  850 caiindhencaslllGAIdssiVNCRDDKGRTPLHAAAFADHVECLQLLLRHSAEVNAADNSGKTALMMAAENGQAGAVD 929
Cdd:COG0666    143 ---------------GAD----VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  930 ILVNsAQADLTVKDKDLNTSLHLASSKGHEKCALLILDKIQDeslINARNNALQTPLHVAARNGLKVVVEELLAKGACVL 1009
Cdd:COG0666    204 LLLE-AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD---LNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLA 279


                   ....*..
gi 2131006785 1010 AIDENGI 1016
Cdd:COG0666    280 AALLDLL 286
PHA03095 PHA03095
ankyrin-like protein; Provisional
 234-515 1.79e-25

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 111.27  E-value: 1.79e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  234 AAASNGQINVVKHLLNLGVEIDEINIYGNTALH--LACYNGQDA-VVNELTDYGANVNQPNNSGFTPLHFAAASTHGALC 310
Cdd:PHA03095    20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHlyLHYSSEKVKdIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDV 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  311 LELLVNNGADVNIQSKDGKSPLH--MTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGH---ELLiNTLITSGA 385
Cdd:PHA03095   100 IKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanvELL-RLLIDAGA 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  386 DTAKCGIHSMFPLHLAALNAHSDccrkllssgqkYSIVslfsnEHVLSAGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQ 465
Cdd:PHA03095   179 DVYAVDDRFRSLLHHHLQSFKPR-----------ARIV-----RELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVLP 242

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2131006785  466 --SSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVNETDDWGRTAL 515
Cdd:PHA03095   243 llIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294
Ank_2 pfam12796
Ankyrin repeats (3 copies);
166-258 2.61e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.40  E-value: 2.61e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  166 LHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHgAEVTCKDkKGYTPLHAAASNGQINVVK 245
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 2131006785  246 HLLNLGVEIDEIN 258
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 377-704 2.86e-21

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 98.56  E-value: 2.86e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  377 INTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRkllssgqkysIVSLfsnehVLSAGFEIDTPDKFGRTCLHAAAAGG 456
Cdd:PHA03095    30 VRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKD----------IVRL-----LLEAGADVNAPERCGFTPLHLYLYNA 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  457 NVE-CIKLLQSSGADFHKKDKCGRTPLH-YAA-ANCHFHCIETLVTTGANVNETDDWGRTALHYAAASdmdRNKTIlgna 533
Cdd:PHA03095    95 TTLdVIKLLIKAGADVNAKDKVGRTPLHvYLSgFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKS---RNANV---- 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  534 henseelerarELkekeaalcLEFLLQNDANPSIRDKEGYNSIHYAAAYGH--RQCLELLLERTNNGFEESDSGATksPL 611
Cdd:PHA03095   168 -----------EL--------LRLLIDAGADVYAVDDRFRSLLHHHLQSFKprARIVRELIRAGCDPAATDMLGNT--PL 226

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  612 HLAAYNGHHQALEV--LLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASIFVKDNvTKRTPLHASVINGHTLC 689
Cdd:PHA03095   227 HSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSS-DGNTPLSLMVRNNNGRA 305

                          330
                   ....*....|....*
gi 2131006785  690 LRLLLEIADNPEAID 704
Cdd:PHA03095   306 VRAALAKNPSAETVA 320
Ank_2 pfam12796
Ankyrin repeats (3 copies);
644-740 2.82e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.55  E-value: 2.82e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  644 LDLAAFKGHTECVEALINQGASIFVKDNvTKRTPLHASVINGHTLCLRLLLEIADnpeaIDVKDaKGQTPLMLAVAYGHI 723
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDK-NGRTALHLAAKNGHLEIVKLLLEHAD----VNLKD-NGRTALHYAARSGHL 74

                           90
                   ....*....|....*..
gi 2131006785  724 DAVSLLLEKEANVDAVD 740
Cdd:pfam12796   75 EIVKLLLEKGADINVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 657-1006 6.08e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 89.35  E-value: 6.08e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  657 EALINQGASIFVKDnVTKRTPLHASVINGHTLCLRLLLEIADNPEAIDVKDAkgqTPLMLAVAYGHIDAVSLLLEKEANV 736
Cdd:PHA02876   162 EMLLEGGADVNAKD-IYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDL---SVLECAVDSKNIDTIKAIIDNRSNI 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  737 DAVDImgctALHRGIMTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAargHATWLSELLQMALSE-EDCSFKDNQGYTP 815
Cdd:PHA02876   238 NKNDL----SLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHAS---QAPSLSRLVPKLLERgADVNAKNIKGETP 310

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  816 LHWACYNG--NENCIEVLLEQKCFRTFIGNPFTPLHCAIINDHENCASLLLGAIDSSiVNCRDDKGRTPLHAAAFADHVE 893
Cdd:PHA02876   311 LYLMAKNGydTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVITLLELGAN-VNARDYCDKTPIHYAAVRNNVV 389

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  894 CLQLLLRHSAEVNAADNSGKTALMMA-AENGQAGAVDILVNSAqADLTVKDKDLNTSLHLASSKgheKCAL----LILDK 968
Cdd:PHA02876   390 IINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRG-ANVNSKNKDLSTPLHYACKK---NCKLdvieMLLDN 465

                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 2131006785  969 IQDESLINARNnalQTPLHVAArnGLKVVVEELLAKGA 1006
Cdd:PHA02876   466 GADVNAINIQN---QYPLLIAL--EYHGIVNILLHYGA 498
Ank_2 pfam12796
Ankyrin repeats (3 copies);
816-909 3.16e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.85  E-value: 3.16e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  816 LHWACYNGNENCIEVLLEQKC-FRTFIGNPFTPLHCAIINDHENCASLLLGAIDSSIvncrDDKGRTPLHAAAFADHVEC 894
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGAdANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL----KDNGRTALHYAARSGHLEI 76

                           90
                   ....*....|....*
gi 2131006785  895 LQLLLRHSAEVNAAD 909
Cdd:pfam12796   77 VKLLLEKGADINVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 96-303 1.80e-16

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: 84.29  E-value: 1.80e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785   96 WLTPLHRAVASRSEEAVQVLIK-HSADVNARDKNWQTPLHVAAANKAVKCAEVII---PLLssVNV---SD-RGGRTALH 167
Cdd:cd22192     17 SESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMeaaPEL--VNEpmtSDlYQGETALH 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  168 HAALNGHVEMVNLLLAKGANIN------AFDKKDRRAL-----H---WAAYMGHLDVVALLINHGAEVTCKDKKGYTPLH 233
Cdd:cd22192     95 IAVVNQNLNLVRELIARGADVVspratgTFFRPGPKNLiyygeHplsFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2131006785  234 AAASNGQINVVKH----LLNLGVEIDEINIYgntalhlacyngqdavvneltdyganvNQPNNSGFTPLHFAAA 303
Cdd:cd22192    175 ILVLQPNKTFACQmydlILSYDKEDDLQPLD---------------------------LVPNNQGLTPFKLAAK 221
Ank_2 pfam12796
Ankyrin repeats (3 copies);
449-569 3.13e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.07  E-value: 3.13e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  449 LHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTgANVNETDDwGRTALHYAAASdmdrnkt 528
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARS------- 71

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2131006785  529 ilgnaheNSEElerarelkekeaalCLEFLLQNDANPSIRD 569
Cdd:pfam12796   72 -------GHLE--------------IVKLLLEKGADINVKD 91
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 71-302 1.09e-10

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: 65.87  E-value: 1.09e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785   71 AFLGDAEIIELLILSGARVNAK-------DNMWLTPLHRAVA-SRSEEAVQVLIKHSADVNARDknwqTPLHVAAANKAV 142
Cdd:TIGR00870   20 AFLPAAERGDLASVYRDLEEPKklnincpDRLGRSALFVAAIeNENLELTELLLNLSCRGAVGD----TLLHAISLEYVD 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  143 KCAEVIIPLLSS---------VNVSDRG----GRTALHHAALNGHVEMVNLLLAKGANINA------FDKKDRRA----- 198
Cdd:TIGR00870   96 AVEAILLHLLAAfrksgplelANDQYTSeftpGITALHLAAHRQNYEIVKLLLERGASVPAracgdfFVKSQGVDsfyhg 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  199 ---LHWAAYMGHLDVVALLINHGAEVTCKDKKGytplhaaasngqiNVVKHLLNLGVEideiNIYGNTALHLACYngqda 275
Cdd:TIGR00870  176 espLNAAACLGSPSIVALLSEDPADILTADSLG-------------NTLLHLLVMENE----FKAEYEELSCQMY----- 233

                          250       260       270
                   ....*....|....*....|....*....|....
gi 2131006785  276 vvNELTDYGANVNQ-------PNNSGFTPLHFAA 302
Cdd:TIGR00870  234 --NFALSLLDKLRDskeleviLNHQGLTPLKLAA 265
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 578-797 4.72e-09

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 60.41  E-value: 4.72e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  578 YAAAYGHRQCLELLL--ERTNNgFEESDSGATKspLHLAAYNGHHQALEVLLQS---LVDLDIRDE--KGRTALDLAAFK 650
Cdd:cd22192     23 LAAKENDVQAIKKLLkcPSCDL-FQRGALGETA--LHVAALYDNLEAAVVLMEAapeLVNEPMTSDlyQGETALHIAVVN 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  651 GHTECVEALINQGAsifvkDNVTKRTPLHASVINGHTLCLRllleiadnpeaidvkdakGQTPLMLAVAYGHIDAVSLLL 730
Cdd:cd22192    100 QNLNLVRELIARGA-----DVVSPRATGTFFRPGPKNLIYY------------------GEHPLSFAACVGNEEIVRLLI 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2131006785  731 EKEANVDAVDIMGCTALHRGIMTGHEECV-QM---LLEQEVSI------LCKDSRGRTPLHYAAARGHATWLSELLQ 797
Cdd:cd22192    157 EHGADIRAQDSLGNTVLHILVLQPNKTFAcQMydlILSYDKEDdlqpldLVPNNQGLTPFKLAAKEGNIVMFQHLVQ 233
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 296-483 3.99e-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: 57.33  E-value: 3.99e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  296 TPLhFAAASTHGALCLE-LLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGE-----IDCVDKDGNTPLHVAA 369
Cdd:cd22192     19 SPL-LLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElvnepMTSDLYQGETALHIAV 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  370 RYGHELLINTLITSGADTAK---CGihSMFPLHLAALnahsdccrkllssgqkysivsLFSNEHVLSagfeidtpdkFgr 446
Cdd:cd22192     98 VNQNLNLVRELIARGADVVSpraTG--TFFRPGPKNL---------------------IYYGEHPLS----------F-- 142

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 2131006785  447 tclhaAAAGGNVECIKLLQSSGADFHKKDKCGRTPLH 483
Cdd:cd22192    143 -----AACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 760-1003 4.93e-08

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: 57.40  E-value: 4.93e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  760 QMLLE-QEVSILCKDSRGRTPLHYAAARGHATWLSELLQmalseedcsFKDNQGY---TPLHWACYNGNENCIEVLLEQK 835
Cdd:TIGR00870   35 RDLEEpKKLNINCPDRLGRSALFVAAIENENLELTELLL---------NLSCRGAvgdTLLHAISLEYVDAVEAILLHLL 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  836 CFRTFIGNPF--------------TPLHCAIINDHENCASLLL--GAIDSSIVNCRDDK----------GRTPLHAAAFA 889
Cdd:TIGR00870  106 AAFRKSGPLElandqytseftpgiTALHLAAHRQNYEIVKLLLerGASVPARACGDFFVksqgvdsfyhGESPLNAAACL 185

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  890 DHVECLQLLLRHSAEVNAADNSGKTALMMAAEngqagavdilvnsaQADLTVKDKDLNTSLHLAsskghekcALLILDKI 969
Cdd:TIGR00870  186 GSPSIVALLSEDPADILTADSLGNTLLHLLVM--------------ENEFKAEYEELSCQMYNF--------ALSLLDKL 243

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 2131006785  970 QD-ESLINARNNALQTPLHVAARNGLKVVVEELLA 1003
Cdd:TIGR00870  244 RDsKELEVILNHQGLTPLKLAAKEGRIVLFRLKLA 278
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 814-1004 6.23e-07

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: 53.48  E-value: 6.23e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  814 TPLHWACYNGNENCIEVLLeqKCFRTfigNPF-------TPLHCAIINDHENCASLLLGAiDSSIVN--CRDD--KGRTP 882
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLL--KCPSC---DLFqrgalgeTALHVAALYDNLEAAVVLMEA-APELVNepMTSDlyQGETA 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  883 LHAAAFADHVECLQLLLRHSAEVNAADNS--------------GKTALMMAAENGQAGAVDILVNSAqADLTVKDKDLNT 948
Cdd:cd22192     93 LHIAVVNQNLNLVRELIARGADVVSPRATgtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHG-ADIRAQDSLGNT 171

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2131006785  949 SLHLASSKGHEKCA------LLILDKIQDE-SLINARNNALQTPLHVAARNGLKVVVEELLAK 1004
Cdd:cd22192    172 VLHILVLQPNKTFAcqmydlILSYDKEDDLqPLDLVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
Ank_4 pfam13637
Ankyrin repeats (many copies);
32-83 2.19e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.73  E-value: 2.19e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2131006785   32 PPLVQAIFSGDPEEIRMLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLI 83
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 162-190 3.39e-06

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: 44.50  E-value: 3.39e-06
                            10        20
                    ....*....|....*....|....*....
gi 2131006785   162 GRTALHHAALNGHVEMVNLLLAKGANINA 190
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 609-853 5.30e-06

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 50.46  E-value: 5.30e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  609 SPLHLAAYNGHHQALEVLLQSLvdlDIRDEKGRTALdLAAFKGHTECVEALIN--------QGASIFVKDNVTKR----- 675
Cdd:TIGR00870   54 SALFVAAIENENLELTELLLNL---SCRGAVGDTLL-HAISLEYVDAVEAILLhllaafrkSGPLELANDQYTSEftpgi 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  676 TPLHASVINGHTLCLRLLLEI-ADNPEAIDVKDAK----------GQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGC 744
Cdd:TIGR00870  130 TALHLAAHRQNYEIVKLLLERgASVPARACGDFFVksqgvdsfyhGESPLNAAACLGSPSIVALLSEDPADILTADSLGN 209

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  745 TALHRGIMtgheECVQMLLEQEVSILCKDsrgrtplhYAaarghatwLSELLQMALSEEDCSFKDNQGYTPLHWACYNGN 824
Cdd:TIGR00870  210 TLLHLLVM----ENEFKAEYEELSCQMYN--------FA--------LSLLDKLRDSKELEVILNHQGLTPLKLAAKEGR 269

                          250       260       270
                   ....*....|....*....|....*....|
gi 2131006785  825 ENCIEVLLEQKCF-RTFIGNPFTPLHCAII 853
Cdd:TIGR00870  270 IVLFRLKLAIKYKqKKFVAWPNGQQLLSLY 299
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 878-907 5.47e-04

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.34  E-value: 5.47e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 2131006785   878 KGRTPLHAAAFADHVECLQLLLRHSAEVNA 907
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 478-506 5.92e-04

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.34  E-value: 5.92e-04
                            10        20
                    ....*....|....*....|....*....
gi 2131006785   478 GRTPLHYAAANCHFHCIETLVTTGANVNE 506
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 30-94 1.69e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 42.34  E-value: 1.69e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2131006785   30 GFPPLVQAIFSGDPEEIRMLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDN 94
Cdd:PHA03100   192 GFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 709-738 2.66e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.41  E-value: 2.66e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 2131006785   709 KGQTPLMLAVAYGHIDAVSLLLEKEANVDA 738
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 354-516 3.97e-03

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 41.22  E-value: 3.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  354 IDCVDKDGNTPLHVAARYG-HELLINTLITSGA-----DTAkcgihsmfpLHLAALNAHSDC--CRKLLSSGQKYSIVSL 425
Cdd:TIGR00870   45 INCPDRLGRSALFVAAIENeNLELTELLLNLSCrgavgDTL---------LHAISLEYVDAVeaILLHLLAAFRKSGPLE 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  426 FSNEHVLSAGFeidtpdkFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKC--------------GRTPLHYAAANCHF 491
Cdd:TIGR00870  116 LANDQYTSEFT-------PGITALHLAAHRQNYEIVKLLLERGASVPARACGdffvksqgvdsfyhGESPLNAAACLGSP 188

                          170       180
                   ....*....|....*....|....*
gi 2131006785  492 HCIETLVTTGANVNETDDWGRTALH 516
Cdd:TIGR00870  189 SIVALLSEDPADILTADSLGNTLLH 213
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
76-365 6.75e-52

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 184.39  E-value: 6.75e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785   76 AEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSV 155
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  156 NVSDRGGRTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAA 235
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  236 ASNGQINVVKHLLNLGVEIDEINIYGNTALHLACYNGQDAVVNELTDYGANVNQPNNSGFTPLHFAAASTHGALcLELLV 315
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI-VKLLL 239

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 2131006785  316 NNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPL 365
Cdd:COG0666    240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
24-298 4.68e-50

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 178.99  E-value: 4.68e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785   24 FHRQCEGFPPLVQAIFSGDPEEIRMLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRA 103
Cdd:COG0666     15 LLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAA 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  104 VASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHVEMVNLLLA 183
Cdd:COG0666     95 ARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLE 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  184 KGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINIYGNT 263
Cdd:COG0666    175 AGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLT 254

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 2131006785  264 ALHLACYNGQDAVVNELTDYGANVNQPNNSGFTPL 298
Cdd:COG0666    255 ALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
44-329 4.87e-50

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 178.99  E-value: 4.87e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785   44 EEIRMLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVN 123
Cdd:COG0666      2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  124 ARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAA 203
Cdd:COG0666     82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  204 YMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINIYGNTALHLACYNGQDAVVNELTDY 283
Cdd:COG0666    162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 2131006785  284 GANVNQPNNSGFTPLHFAAASTHGALCLELLVNNGADVNIQSKDGK 329
Cdd:COG0666    242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
PHA03095 PHA03095
ankyrin-like protein; Provisional
 108-381 5.11e-39

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 152.10  E-value: 5.11e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  108 SEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSS---VNVSDRGGRTALHHAALNGHVE-MVNLLLA 183
Cdd:PHA03095    26 TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIVRLLLEAgadVNAPERCGFTPLHLYLYNATTLdVIKLLIK 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  184 KGANINAFDKKDRRALHwaAYMG----HLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINV--VKHLLNLGVEIDEI 257
Cdd:PHA03095   106 AGADVNAKDKVGRTPLH--VYLSgfniNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVYAV 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  258 NIYGNTALHLACYNGQD--AVVNELTDYGANVNQPNNSGFTPLHFAAA-STHGALCLELLVNNGADVNIQSKDGKSPLHM 334
Cdd:PHA03095   184 DDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHSMATgSSCKRSLVLPLLIAGISINARNRYGQTPLHY 263

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 2131006785  335 TAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLI 381
Cdd:PHA03095   264 AAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
PHA03095 PHA03095
ankyrin-like protein; Provisional
 44-332 7.28e-39

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 151.72  E-value: 7.28e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785   44 EEIRMLIHKTEDVNALDSEKRTPLHVaaFLG-----DAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAV-QVLIK 117
Cdd:PHA03095    28 EEVRRLLAAGADVNFRGEYGKTPLHL--YLHyssekVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDViKLLIK 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  118 HSADVNARDKNWQTPLHVAAANKAVkcaeviipllssvnvsdrggrtalhhaalngHVEMVNLLLAKGANINAFDKKDRR 197
Cdd:PHA03095   106 AGADVNAKDKVGRTPLHVYLSGFNI-------------------------------NPKVIRLLLRKGADVNALDLYGMT 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  198 ALHwaAYMGH----LDVVALLINHGAEVTCKDKKGYTPLHAAASNGQIN--VVKHLLNLGVEIDEINIYGNTALHLACYN 271
Cdd:PHA03095   155 PLA--VLLKSrnanVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATG 232

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2131006785  272 G--QDAVVNELTDYGANVNQPNNSGFTPLHFAAASTHGALCLELLvNNGADVNIQSKDGKSPL 332
Cdd:PHA03095   233 SscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLI-ALGADINAVSSDGNTPL 294
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
532-789 6.44e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.94  E-value: 6.44e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  532 NAHENSEELERARELKEKEAALCLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNNGFEESDSGATksPL 611
Cdd:COG0666     14 ALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNT--LL 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  612 HLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASIFVKDNvTKRTPLHASVINGHTLCLR 691
Cdd:COG0666     92 HAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN-DGNTPLHLAAANGNLEIVK 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  692 LLLEI-ADnpeaIDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALHRGIMTGHEECVQMLLEQEVSIL 770
Cdd:COG0666    171 LLLEAgAD----VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246

                          250
                   ....*....|....*....
gi 2131006785  771 CKDSRGRTPLHYAAARGHA 789
Cdd:COG0666    247 AKDKDGLTALLLAAAAGAA 265
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
555-835 1.10e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 140.47  E-value: 1.10e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  555 LEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNNGFEESDSGATKSPLHLAAYNGHHQALEVLLQSLVDLD 634
Cdd:COG0666      2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  635 IRDEKGRTALDLAAFKGHTECVEALINQGASIFVKDNvTKRTPLHASVINGHTLCLRLLLEI-ADnpeaIDVKDAKGQTP 713
Cdd:COG0666     82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDK-DGETPLHLAAYNGNLEIVKLLLEAgAD----VNAQDNDGNTP 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  714 LMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALHRGIMTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGHATWLS 793
Cdd:COG0666    157 LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVK 236

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 2131006785  794 ELLQMALSEEDcsfKDNQGYTPLHWACYNGNENCIEVLLEQK 835
Cdd:COG0666    237 LLLEAGADLNA---KDKDGLTALLLAAAAGAALIVKLLLLAL 275
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
175-547 1.17e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 140.47  E-value: 1.17e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  175 VEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEI 254
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  255 DEINIYGNTALHLACYNGQDAVVNELTDYGANVNQPNNSGFTPLHFAAASTHGALcLELLVNNGADVNIQskdgksplhm 334
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI-VKLLLEAGADVNAQ---------- 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  335 tavhgrftrsqtliqnggeidcvDKDGNTPLHVAARYGHELLINTLITSGADtakcgihsmfplhlaalnahsdccrkll 414
Cdd:COG0666    150 -----------------------DNDGNTPLHLAAANGNLEIVKLLLEAGAD---------------------------- 178

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  415 ssgqkysivslfsnehvlsagfeIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCI 494
Cdd:COG0666    179 -----------------------VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIV 235

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2131006785  495 ETLVTTGANVNETDDWGRTALHYAAASDMDRNKTILGNAHENSEELERARELK 547
Cdd:COG0666    236 KLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 77-323 4.35e-36

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 142.50  E-value: 4.35e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785   77 EIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAV-----KCAEVIIPL 151
Cdd:PHA03100    16 KNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEY 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  152 LSSVNVSDRGGRTALHHAALN--GHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGH--LDVVALLINHGAEVTCKDKk 227
Cdd:PHA03100    96 GANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKNR- 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  228 gytplhaaasngqinvVKHLLNLGVEIDEINIYGNTALHLACYNGQDAVVNELTDYGANVNQPNNSGFTPLHFAAASTHG 307
Cdd:PHA03100   175 ----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNK 238

                          250
                   ....*....|....*.
gi 2131006785  308 ALcLELLVNNGADVNI 323
Cdd:PHA03100   239 EI-FKLLLNNGPSIKT 253
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
658-982 1.10e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 137.39  E-value: 1.10e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  658 ALINQGASIFVKDNVTKRTPLHASVINGHTLCLRLLLEIADNpeaIDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVD 737
Cdd:COG0666      5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLA---LALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  738 AVDIMGCTALHRGIMTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGHATWLSELLQmalSEEDCSFKDNQGYTPLH 817
Cdd:COG0666     82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLE---AGADVNAQDNDGNTPLH 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  818 WACYNGNENCIEVLLEQkcfrtfignpftplhcaiindhencaslllGAIdssiVNCRDDKGRTPLHAAAFADHVECLQL 897
Cdd:COG0666    159 LAAANGNLEIVKLLLEA------------------------------GAD----VNARDNDGETPLHLAAENGHLEIVKL 204

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  898 LLRHSAEVNAADNSGKTALMMAAENGQAGAVDILVNsAQADLTVKDKDLNTSLHLASSKGHEKCALLILDKIQDESLINA 977
Cdd:COG0666    205 LLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE-AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283


                   ....*
gi 2131006785  978 RNNAL 982
Cdd:COG0666    284 DLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
690-1016 3.06e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.54  E-value: 3.06e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  690 LRLLLEIADNPEAIDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALHRGIMTGHEECVQMLLEQEVSI 769
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  770 LCKDSRGRTPLHYAAARGHATWLSELLQmalSEEDCSFKDNQGYTPLHWACYNGNENCIEVLLEQkcfrtfignpftplh 849
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLE---AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA--------------- 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  850 caiindhencaslllGAIdssiVNCRDDKGRTPLHAAAFADHVECLQLLLRHSAEVNAADNSGKTALMMAAENGQAGAVD 929
Cdd:COG0666    143 ---------------GAD----VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  930 ILVNsAQADLTVKDKDLNTSLHLASSKGHEKCALLILDKIQDeslINARNNALQTPLHVAARNGLKVVVEELLAKGACVL 1009
Cdd:COG0666    204 LLLE-AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD---LNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLA 279


                   ....*..
gi 2131006785 1010 AIDENGI 1016
Cdd:COG0666    280 AALLDLL 286
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 48-386 8.71e-34

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 139.43  E-value: 8.71e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785   48 MLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDK 127
Cdd:PHA02876   163 MLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDL 242

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  128 NwqtpLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHV-EMVNLLLAKGANINAFDKKDRRALHWAAYMG 206
Cdd:PHA02876   243 S----LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAKNG 318

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  207 H-LDVVALLINHGAEVTCKDKKGYTPLHAAAS-NGQINVVKHLLNLGVEIDEINIYGNTALHLACYNGQDAVVNELTDYG 284
Cdd:PHA02876   319 YdTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYG 398

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  285 ANVNQPNNSGFTPLHFAAASTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHG-RFTRSQTLIQNGGEIDCVDKDGNT 363
Cdd:PHA02876   399 ADIEALSQKIGTALHFALCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQY 478

                          330       340
                   ....*....|....*....|...
gi 2131006785  364 PLHVAarYGHELLINTLITSGAD 386
Cdd:PHA02876   479 PLLIA--LEYHGIVNILLHYGAE 499
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
588-866 4.56e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 130.07  E-value: 4.56e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  588 LELLLERTNNGFEESDSGATKSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASIF 667
Cdd:COG0666      2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  668 VKDNvTKRTPLHASVINGHTLCLRLLLEIADNpeaIDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTAL 747
Cdd:COG0666     82 AKDD-GGNTLLHAAARNGDLEIVKLLLEAGAD---VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPL 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  748 HRGIMTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGHATWLSELLQmalSEEDCSFKDNQGYTPLHWACYNGNENC 827
Cdd:COG0666    158 HLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLE---AGADVNAKDNDGKTALDLAAENGNLEI 234

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 2131006785  828 IEVLLEQKCFRTFIGNP-FTPLHCAIINDHENCASLLLGA 866
Cdd:COG0666    235 VKLLLEAGADLNAKDKDgLTALLLAAAAGAALIVKLLLLA 274
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 38-389 9.96e-33

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 132.78  E-value: 9.96e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785   38 IFSGDPEEIRMLI-HKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLI 116
Cdd:PHA02874     9 IYSGDIEAIEKIIkNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  117 KHSADVNArdknwqtplhvaaankavkcaeVIIPLLSSvnvsdrggrtalhhaalnghvEMVNLLLAKGANINAFDKKDR 196
Cdd:PHA02874    89 DNGVDTSI----------------------LPIPCIEK---------------------DMIKTILDCGIDVNIKDAELK 125

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  197 RALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINIYGNTALHLACYNGQDAV 276
Cdd:PHA02874   126 TFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYAC 205

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  277 VNELTDYGANVNQPNNSGFTPLHfaAASTHGALCLELLVNNgADVNIQSKDGKSPLHMtAVHGRFTRS--QTLIQNGGEI 354
Cdd:PHA02874   206 IKLLIDHGNHIMNKCKNGFTPLH--NAIIHNRSAIELLINN-ASINDQDIDGSTPLHH-AINPPCDIDiiDILLYHKADI 281

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 2131006785  355 DCVDKDGNTPLHVAARYGH------ELLINTLITSGADTAK 389
Cdd:PHA02874   282 SIKDNKGENPIDTAFKYINkdpvikDIIANAVLIKEADKLK 322
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
311-644 1.21e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 128.53  E-value: 1.21e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  311 LELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGADTAKC 390
Cdd:COG0666      4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  391 GIHSMFPLHLAALNAHSDCCRKLLSsgqkysivslfsnehvlsAGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGAD 470
Cdd:COG0666     84 DDGGNTLLHAAARNGDLEIVKLLLE------------------AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGAD 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  471 FHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVNETDDWGRTALHYAaasdmdrnktilgnAHENSEELerarelkeke 550
Cdd:COG0666    146 VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLA--------------AENGHLEI---------- 201

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  551 aalcLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNNGFEESDSGATksPLHLAAYNGHHQALEVLLQSL 630
Cdd:COG0666    202 ----VKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLT--ALLLAAAAGAALIVKLLLLAL 275

                          330
                   ....*....|....
gi 2131006785  631 VDLDIRDEKGRTAL 644
Cdd:COG0666    276 LLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
514-780 1.07e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 125.84  E-value: 1.07e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  514 ALHYAAASDMDRNKTILGNAHENSEELERARELKEKEAALCLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLE 593
Cdd:COG0666     29 ALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLE 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  594 RTNNGFEESDSGATksPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASIFVKDNvT 673
Cdd:COG0666    109 AGADVNARDKDGET--PLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN-D 185

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  674 KRTPLHASVINGHTLCLRLLLE-IADnpeaIDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALHRGIM 752
Cdd:COG0666    186 GETPLHLAAENGHLEIVKLLLEaGAD----VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAA 261

                          250       260
                   ....*....|....*....|....*...
gi 2131006785  753 TGHEECVQMLLEQEVSILCKDSRGRTPL 780
Cdd:COG0666    262 AGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 78-407 1.23e-31

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 132.88  E-value: 1.23e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785   78 IIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVNV 157
Cdd:PHA02876   160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINK 239

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  158 SDrggrTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLD-VVALLINHGAEVTCKDKKGYTPLHAAA 236
Cdd:PHA02876   240 ND----LSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMA 315

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  237 SNG-QINVVKHLLNLGVEIDEINIYGNTALHLACY--NGQDAVVNeLTDYGANVNQPNNSGFTPLHFAAAStHGALCLEL 313
Cdd:PHA02876   316 KNGyDTENIRTLIMLGADVNAADRLYITPLHQASTldRNKDIVIT-LLELGANVNARDYCDKTPIHYAAVR-NNVVIINT 393

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  314 LVNNGADVNIQSKDGKSPLHMtAVHGR--FTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHEL-LINTLITSGADTAKC 390
Cdd:PHA02876   394 LLDYGADIEALSQKIGTALHF-ALCGTnpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKLdVIEMLLDNGADVNAI 472

                          330
                   ....*....|....*..
gi 2131006785  391 GIHSMFPLhLAALNAHS 407
Cdd:PHA02876   473 NIQNQYPL-LIALEYHG 488
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
432-709 1.30e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 125.84  E-value: 1.30e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  432 LSAGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVNETDDWG 511
Cdd:COG0666     41 LLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDG 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  512 RTALHYAAasdmdrnktilgnaHENSEELerarelkekeaalcLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELL 591
Cdd:COG0666    121 ETPLHLAA--------------YNGNLEI--------------VKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  592 LERTNNGFEESDSGATksPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASIFVKDN 671
Cdd:COG0666    173 LEAGADVNARDNDGET--PLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 2131006785  672 VTKRTPLHASVINGHTLCLRLLLEIADNPEAIDVKDAK 709
Cdd:COG0666    251 DGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
425-747 4.83e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 121.21  E-value: 4.83e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  425 LFSNEHVLSAGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANV 504
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  505 NETDDWGRTALHYAAASdmdrnktilgnaheNSEELerarelkekeaalcLEFLLQNDANPSIRDKEGYNSIHYAAAYGH 584
Cdd:COG0666     81 NAKDDGGNTLLHAAARN--------------GDLEI--------------VKLLLEAGADVNARDKDGETPLHLAAYNGN 132

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  585 RQCLELLLERTNNGFEESDSGATksPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGA 664
Cdd:COG0666    133 LEIVKLLLEAGADVNAQDNDGNT--PLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA 210

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  665 SIFVKDNvTKRTPLHASVINGHTLCLRLLLEIADNPEAidvKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGC 744
Cdd:COG0666    211 DVNAKDN-DGKTALDLAAENGNLEIVKLLLEAGADLNA---KDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLL 286


                   ...
gi 2131006785  745 TAL 747
Cdd:COG0666    287 TLL 289
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 145-505 5.02e-28

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 121.32  E-value: 5.02e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  145 AEVIIPLLSSVNVSDRGGRTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCK 224
Cdd:PHA02876   161 AEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKN 240

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  225 DkkgyTPLHAAASNGQINVVKHLLNLGVEIDEINIYGNTALHLACYNGQ-DAVVNELTDYGANVNQPNNSGFTPLHFAAA 303
Cdd:PHA02876   241 D----LSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAK 316

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  304 STHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQ-TLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLIT 382
Cdd:PHA02876   317 NGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIViTLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLD 396

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  383 SGADtakcgihsmfplhLAALNahsdccrkllssgqkysivslfsnehvlsagfeidtpDKFGrTCLHAAAAGGN-VECI 461
Cdd:PHA02876   397 YGAD-------------IEALS-------------------------------------QKIG-TALHFALCGTNpYMSV 425

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 2131006785  462 KLLQSSGADFHKKDKCGRTPLHYAAA-NCHFHCIETLVTTGANVN 505
Cdd:PHA02876   426 KTLIDRGANVNSKNKDLSTPLHYACKkNCKLDVIEMLLDNGADVN 470
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 34-287 5.98e-28

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 121.32  E-value: 5.98e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785   34 LVQAIFSGDPEEIRMLIHKTEDVNALDSEKRTPLHVAAFLGD-AEIIELLILSGARVNAKDNMWLTPLH-RAVASRSEEA 111
Cdd:PHA02876   244 LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYlMAKNGYDTEN 323

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  112 VQVLIKHSADVNARDKNWQTPLHVAAANKAVKcaEVIIPLL---SSVNVSDRGGRTALHHAALNGHVEMVNLLLAKGANI 188
Cdd:PHA02876   324 IRTLIMLGADVNAADRLYITPLHQASTLDRNK--DIVITLLelgANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADI 401

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  189 NAFDKKDRRALHWAAY-MGHLDVVALLINHGAEVTCKDKKGYTPLH-AAASNGQINVVKHLLNLGVEIDEINIYGNTALH 266
Cdd:PHA02876   402 EALSQKIGTALHFALCgTNPYMSVKTLIDRGANVNSKNKDLSTPLHyACKKNCKLDVIEMLLDNGADVNAINIQNQYPLL 481

                          250       260
                   ....*....|....*....|.
gi 2131006785  267 LACynGQDAVVNELTDYGANV 287
Cdd:PHA02876   482 IAL--EYHGIVNILLHYGAEL 500
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 97-375 1.81e-26

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 114.59  E-value: 1.81e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785   97 LTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVA--AANKavkcaEVIIPLLSSVNVSDRG-GRTALHHAALNG 173
Cdd:PHA02878    38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIIckEPNK-----LGMKEMIRSINKCSVFyTLVAIKDAFNNR 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  174 HVEMVNLLLakganINAFDKK---DRRALHWAAYMGHLD--VVALLINHGAEVTCKDK-KGYTPLHAAASNGQINVVKHL 247
Cdd:PHA02878   113 NVEIFKIIL-----TNRYKNIqtiDLVYIDKKSKDDIIEaeITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELL 187

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  248 LNLGVEIDEINIYGNTALHLACYNGQDAVVNELTDYGANVNQPNNSGFTPLHFAAASTHGALCLELLVNNGADVNIQSK- 326
Cdd:PHA02878   188 LSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDYDILKLLLEHGVDVNAKSYi 267

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2131006785  327 DGKSPLHMTAVHGRFTRsqTLIQNGGEIDCVDKDGNTPLHVAA--RYGHEL 375
Cdd:PHA02878   268 LGLTALHSSIKSERKLK--LLLEYGADINSLNSYKLTPLSSAVkqYLCINI 316
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 50-260 1.20e-25

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 111.30  E-value: 1.20e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785   50 IHKTEDVN-ALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLH-----RAVASRSEEAVQVLIKHSADVN 123
Cdd:PHA03100    21 IIMEDDLNdYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGANVN 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  124 ARDKNWQTPLHVAAANKavKCAEVIIPLLSS----VNVSDRGGRTALHHAALNGHV--EMVNLLLAKGANINAFDK---- 193
Cdd:PHA03100   101 APDNNGITPLLYAISKK--SNSYSIVEYLLDnganVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKNRvnyl 178

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2131006785  194 ---------KDRR---ALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINIY 260
Cdd:PHA03100   179 lsygvpiniKDVYgftPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
PHA03095 PHA03095
ankyrin-like protein; Provisional
 234-515 1.79e-25

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 111.27  E-value: 1.79e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  234 AAASNGQINVVKHLLNLGVEIDEINIYGNTALH--LACYNGQDA-VVNELTDYGANVNQPNNSGFTPLHFAAASTHGALC 310
Cdd:PHA03095    20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHlyLHYSSEKVKdIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDV 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  311 LELLVNNGADVNIQSKDGKSPLH--MTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGH---ELLiNTLITSGA 385
Cdd:PHA03095   100 IKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanvELL-RLLIDAGA 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  386 DTAKCGIHSMFPLHLAALNAHSDccrkllssgqkYSIVslfsnEHVLSAGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQ 465
Cdd:PHA03095   179 DVYAVDDRFRSLLHHHLQSFKPR-----------ARIV-----RELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVLP 242

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2131006785  466 --SSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVNETDDWGRTAL 515
Cdd:PHA03095   243 llIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 214-505 3.57e-24

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 106.67  E-value: 3.57e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  214 LINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINIYGNTALHLAC---YNGQDAV--VNELTDYGANVN 288
Cdd:PHA03100    21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSnikYNLTDVKeiVKLLLEYGANVN 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  289 QPNNSGFTPLHFAAASTHGALCL-ELLVNNGADVNIQSKDGKSPLHMtavhgrFTRSqtliqnggeiDCVDKDgntplhv 367
Cdd:PHA03100   101 APDNNGITPLLYAISKKSNSYSIvEYLLDNGANVNIKNSDGENLLHL------YLES----------NKIDLK------- 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  368 aaryghelLINTLITSGADtakcgihsmfplhlaaLNAhsdCCRkllssgqkysiVSLFsnehvLSAGFEIDTPDKFGRT 447
Cdd:PHA03100   158 --------ILKLLIDKGVD----------------INA---KNR-----------VNYL-----LSYGVPINIKDVYGFT 194

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2131006785  448 CLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVN 505
Cdd:PHA03100   195 PLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 44-317 1.20e-22

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 103.04  E-value: 1.20e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785   44 EEIRMLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIK------ 117
Cdd:PHA02878    18 KYIEYIDHTENYSTSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRsinkcs 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  118 ------------HSADVNA-------RDKNWQTP--LHVAAANKAVKCAEVIIPLL----SSVNVSDR-GGRTALHHAAL 171
Cdd:PHA02878    98 vfytlvaikdafNNRNVEIfkiiltnRYKNIQTIdlVYIDKKSKDDIIEAEITKLLlsygADINMKDRhKGNTALHYATE 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  172 NGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASN-GQINVVKHLLNL 250
Cdd:PHA02878   178 NKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEH 257

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2131006785  251 GVEID-EINIYGNTALHLACYNGQdaVVNELTDYGANVNQPNNSGFTPLHFAAASTHGALCLELLVNN 317
Cdd:PHA02878   258 GVDVNaKSYILGLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPLSSAVKQYLCINIGRILISN 323
PHA03095 PHA03095
ankyrin-like protein; Provisional
 30-257 2.00e-21

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 98.94  E-value: 2.00e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785   30 GFPPLVQAIFSGDPEE-IRMLIHKTEDVNALDSEKRTPLHV--AAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVAS 106
Cdd:PHA03095    83 GFTPLHLYLYNATTLDvIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKS 162

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  107 R--SEEAVQVLIKHSADVNARDKNWQTPLHVAAAN--KAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHVEMVNL-- 180
Cdd:PHA03095   163 RnaNVELLRLLIDAGADVYAVDDRFRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlp 242

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2131006785  181 LLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEI 257
Cdd:PHA03095   243 LLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETV 319
Ank_2 pfam12796
Ankyrin repeats (3 copies);
166-258 2.61e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.40  E-value: 2.61e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  166 LHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHgAEVTCKDkKGYTPLHAAASNGQINVVK 245
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 2131006785  246 HLLNLGVEIDEIN 258
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 377-704 2.86e-21

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 98.56  E-value: 2.86e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  377 INTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRkllssgqkysIVSLfsnehVLSAGFEIDTPDKFGRTCLHAAAAGG 456
Cdd:PHA03095    30 VRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKD----------IVRL-----LLEAGADVNAPERCGFTPLHLYLYNA 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  457 NVE-CIKLLQSSGADFHKKDKCGRTPLH-YAA-ANCHFHCIETLVTTGANVNETDDWGRTALHYAAASdmdRNKTIlgna 533
Cdd:PHA03095    95 TTLdVIKLLIKAGADVNAKDKVGRTPLHvYLSgFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKS---RNANV---- 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  534 henseelerarELkekeaalcLEFLLQNDANPSIRDKEGYNSIHYAAAYGH--RQCLELLLERTNNGFEESDSGATksPL 611
Cdd:PHA03095   168 -----------EL--------LRLLIDAGADVYAVDDRFRSLLHHHLQSFKprARIVRELIRAGCDPAATDMLGNT--PL 226

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  612 HLAAYNGHHQALEV--LLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASIFVKDNvTKRTPLHASVINGHTLC 689
Cdd:PHA03095   227 HSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSS-DGNTPLSLMVRNNNGRA 305

                          330
                   ....*....|....*
gi 2131006785  690 LRLLLEIADNPEAID 704
Cdd:PHA03095   306 VRAALAKNPSAETVA 320
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 345-647 9.70e-21

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 96.57  E-value: 9.70e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  345 QTLIQNGGE-IDCVDKDGNTPLHVAARYGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSGQKYSIV 423
Cdd:PHA02874    18 EKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSIL 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  424 SL--FSNEHV---LSAGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLV 498
Cdd:PHA02874    98 PIpcIEKDMIktiLDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLL 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  499 TTGANVNETDDWGRTALHYAAasdmdrnktilgnahenseelerarelkEKEAALCLEFLLQNDANPSIRDKEGYNSIHY 578
Cdd:PHA02874   178 EKGAYANVKDNNGESPLHNAA----------------------------EYGDYACIKLLIDHGNHIMNKCKNGFTPLHN 229

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2131006785  579 AAAYgHRQCLELLLerTNNGFEESD-SGATksPLHLA-AYNGHHQALEVLLQSLVDLDIRDEKGRTALDLA 647
Cdd:PHA02874   230 AIIH-NRSAIELLI--NNASINDQDiDGST--PLHHAiNPPCDIDIIDILLYHKADISIKDNKGENPIDTA 295
Ank_2 pfam12796
Ankyrin repeats (3 copies);
199-291 1.03e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.48  E-value: 1.03e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  199 LHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNlGVEIDEINiYGNTALHLACYNGQDAVVN 278
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 2131006785  279 ELTDYGANVNQPN 291
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 419-704 1.03e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 96.27  E-value: 1.03e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  419 KYSIVSLFSNEHVLSAGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHF--HCIET 496
Cdd:PHA03100     9 KSRIIKVKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltDVKEI 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  497 ---LVTTGANVNETDDWGRTALHYAAASDMDRNKTIlgnahenseelerarelkekeaalclEFLLQNDANPSIRDKEGY 573
Cdd:PHA03100    89 vklLLEYGANVNAPDNNGITPLLYAISKKSNSYSIV--------------------------EYLLDNGANVNIKNSDGE 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  574 NSIHYAAAYGHR--QCLELLLERTNNgfeesdsgatksplhLAAYNghhqALEVLLQSLVDLDIRDEKGRTALDLAAFKG 651
Cdd:PHA03100   143 NLLHLYLESNKIdlKILKLLIDKGVD---------------INAKN----RVNYLLSYGVPINIKDVYGFTPLHYAVYNN 203

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2131006785  652 HTECVEALINQGASIFVKDNVTKrTPLHASVINGHTLCLRLLLEIADNPEAID 704
Cdd:PHA03100   204 NPEFVKYLLDLGANPNLVNKYGD-TPLHIAILNNNKEIFKLLLNNGPSIKTII 255
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 204-736 1.35e-20

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 97.83  E-value: 1.35e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  204 YMGHLDVVALLIN-----HGAEvTCKDKK-GYTPLHAAASNGQINVVKHLLNLGVEIDEINIYG-NTALHLACY--NGQD 274
Cdd:PHA02876    12 RGNCIDILSAIDNydlhkHGAN-QCENESiPFTAIHQALQLRQIDIVEEIIQQNPELIYITDHKcHSTLHTICIipNVMD 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  275 AVVNELTDYGANVNQPNNSGFTPLHfaaasTHGALCLELLVN--NGADVNIqSKDGKSPLHMTAVHGRFTR-----SQTL 347
Cdd:PHA02876    91 IVISLTLDCDIILDIKYASIILNKH-----KLDEACIHILKEaiSGNDIHY-DKINESIEYMKLIKERIQQdelliAEML 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  348 IQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLLS-----SGQKYSI 422
Cdd:PHA02876   165 LEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDnrsniNKNDLSL 244

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  423 VSLFSNEH------VLSAGFEIDTPDKFGRTCLHAAAAGGNVECI--KLLQsSGADFHKKDKCGRTPLHYAAANCH-FHC 493
Cdd:PHA02876   245 LKAIRNEDletsllLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLvpKLLE-RGADVNAKNIKGETPLYLMAKNGYdTEN 323

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  494 IETLVTTGANVNETDDWGRTALHyaAASDMDRNKTILGNahenseelerarelkekeaalclefLLQNDANPSIRDKEGY 573
Cdd:PHA02876   324 IRTLIMLGADVNAADRLYITPLH--QASTLDRNKDIVIT-------------------------LLELGANVNARDYCDK 376

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  574 NSIHYAAAYGHRQCLELLLertnngfeesDSGAtksplhlaaynghhqalevllqslvDLDIRDEKGRTALDLAAFKGHT 653
Cdd:PHA02876   377 TPIHYAAVRNNVVIINTLL----------DYGA-------------------------DIEALSQKIGTALHFALCGTNP 421

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  654 -ECVEALINQGASIFVKdNVTKRTPLHASVINGHTL-CLRLLLEIADNPEAIDVKDakgQTPLMLAVAYGHIdaVSLLLE 731
Cdd:PHA02876   422 yMSVKTLIDRGANVNSK-NKDLSTPLHYACKKNCKLdVIEMLLDNGADVNAINIQN---QYPLLIALEYHGI--VNILLH 495


                   ....*
gi 2131006785  732 KEANV 736
Cdd:PHA02876   496 YGAEL 500
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 70-288 1.14e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 92.75  E-value: 1.14e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785   70 AAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVII 149
Cdd:PHA02875     9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  150 PLLSSVN-VSDRGGRTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKG 228
Cdd:PHA02875    89 DLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCG 168

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2131006785  229 YTPLHAAASNGQINVVKHLLNLGVEIDEINIYGN-TALHLACYNGQDAVVNELTDYGANVN 288
Cdd:PHA02875   169 CTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADCN 229
Ank_2 pfam12796
Ankyrin repeats (3 copies);
133-225 1.76e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.01  E-value: 1.76e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  133 LHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHVEMVNLLLAKgANINAFDkKDRRALHWAAYMGHLDVVA 212
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 2131006785  213 LLINHGAEVTCKD 225
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 611-909 2.62e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 88.87  E-value: 2.62e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  611 LHLAAYNGHHQALEVLLQSLVD-LDIRDEKGRTALDLAAFKGHTECVEALINQGASI-FVKDNVTKrtPLHASVINGHTL 688
Cdd:PHA02874     5 LRMCIYSGDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADInHINTKIPH--PLLTAIKIGAHD 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  689 CLRLLLE--------------------IADNPEAIDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALH 748
Cdd:PHA02874    83 IIKLLIDngvdtsilpipciekdmiktILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIH 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  749 RGIMTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGHATWLSELLQmalSEEDCSFKDNQGYTPLHWACYNgNENCI 828
Cdd:PHA02874   163 IAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLID---HGNHIMNKCKNGFTPLHNAIIH-NRSAI 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  829 EVLLEQKCFRTFIGNPFTPLHCAIIN--DHENCASLLLGAIDSSIvncRDDKGRTPLHAA-AFADHVECLQLLLRHSAEV 905
Cdd:PHA02874   239 ELLINNASINDQDIDGSTPLHHAINPpcDIDIIDILLYHKADISI---KDNKGENPIDTAfKYINKDPVIKDIIANAVLI 315


                   ....
gi 2131006785  906 NAAD 909
Cdd:PHA02874   316 KEAD 319
Ank_2 pfam12796
Ankyrin repeats (3 copies);
644-740 2.82e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.55  E-value: 2.82e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  644 LDLAAFKGHTECVEALINQGASIFVKDNvTKRTPLHASVINGHTLCLRLLLEIADnpeaIDVKDaKGQTPLMLAVAYGHI 723
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDK-NGRTALHLAAKNGHLEIVKLLLEHAD----VNLKD-NGRTALHYAARSGHL 74

                           90
                   ....*....|....*..
gi 2131006785  724 DAVSLLLEKEANVDAVD 740
Cdd:pfam12796   75 EIVKLLLEKGADINVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 657-1006 6.08e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 89.35  E-value: 6.08e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  657 EALINQGASIFVKDnVTKRTPLHASVINGHTLCLRLLLEIADNPEAIDVKDAkgqTPLMLAVAYGHIDAVSLLLEKEANV 736
Cdd:PHA02876   162 EMLLEGGADVNAKD-IYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDL---SVLECAVDSKNIDTIKAIIDNRSNI 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  737 DAVDImgctALHRGIMTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAargHATWLSELLQMALSE-EDCSFKDNQGYTP 815
Cdd:PHA02876   238 NKNDL----SLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHAS---QAPSLSRLVPKLLERgADVNAKNIKGETP 310

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  816 LHWACYNG--NENCIEVLLEQKCFRTFIGNPFTPLHCAIINDHENCASLLLGAIDSSiVNCRDDKGRTPLHAAAFADHVE 893
Cdd:PHA02876   311 LYLMAKNGydTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVITLLELGAN-VNARDYCDKTPIHYAAVRNNVV 389

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  894 CLQLLLRHSAEVNAADNSGKTALMMA-AENGQAGAVDILVNSAqADLTVKDKDLNTSLHLASSKgheKCAL----LILDK 968
Cdd:PHA02876   390 IINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRG-ANVNSKNKDLSTPLHYACKK---NCKLdvieMLLDN 465

                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 2131006785  969 IQDESLINARNnalQTPLHVAArnGLKVVVEELLAKGA 1006
Cdd:PHA02876   466 GADVNAINIQN---QYPLLIAL--EYHGIVNILLHYGA 498
Ank_2 pfam12796
Ankyrin repeats (3 copies);
67-192 7.77e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.39  E-value: 7.77e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785   67 LHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHsADVNARDKnwqtplhvaaankavkcae 146
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN------------------- 60

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2131006785  147 viipllssvnvsdrgGRTALHHAALNGHVEMVNLLLAKGANINAFD 192
Cdd:pfam12796   61 ---------------GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 691-1006 1.22e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 87.39  E-value: 1.22e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  691 RLLLEIADnpeaIDVKDAKGQTPLMLAVAYGH---IDAVSLLLEKEANVDAVDIMGCTALHRGIMTGHEE-CVQMLLEQE 766
Cdd:PHA03095    32 RLLAAGAD----VNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAG 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  767 VSILCKDSRGRTPLH-YAA-ARGHATWLSELLQMALSEEDCsfkDNQGYTPLHwaCYNGNENC----IEVLLEQKCF--- 837
Cdd:PHA03095   108 ADVNAKDKVGRTPLHvYLSgFNINPKVIRLLLRKGADVNAL---DLYGMTPLA--VLLKSRNAnvelLRLLIDAGADvya 182

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  838 RTFIGNpfTPLH--CAIINDHENCASLLLGAIDSsiVNCRDDKGRTPLHAAAFADHVECLQL--LLRHSAEVNAADNSGK 913
Cdd:PHA03095   183 VDDRFR--SLLHhhLQSFKPRARIVRELIRAGCD--PAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQ 258

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  914 TALMMAAENGQAGAVDILVNsAQADLTVKDKDLNTSLHLASSKGHEKCALLILDKIQDESLINARNNALQTPLHVAARNG 993
Cdd:PHA03095   259 TPLHYAAVFNNPRACRRLIA-LGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAATLNTASVAGGDIPSDA 337

                          330
                   ....*....|...
gi 2131006785  994 LKVVVEELLAKGA 1006
Cdd:PHA03095   338 TRLCVAKVVLRGA 350
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 177-638 1.94e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 87.81  E-value: 1.94e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  177 MVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNlgveiDE 256
Cdd:PHA02876   160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIID-----NR 234

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  257 INIYGNTALHLACYNGQDAVVNELT-DYGANVNQPNNSGFTPLHFAAASTHGALCLELLVNNGADVNIQSKDGKSPLHMT 335
Cdd:PHA02876   235 SNINKNDLSLLKAIRNEDLETSLLLyDAGFSVNSIDDCKNTPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLM 314

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  336 AVHGRFTRS-QTLIQNGGEIDCVDKDGNTPLHVAAryghellintlitsgadtakcgihsmfplhlaalnahsdccrkll 414
Cdd:PHA02876   315 AKNGYDTENiRTLIMLGADVNAADRLYITPLHQAS--------------------------------------------- 349

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  415 ssgqkysivslfsnehvlsagfeidTPDKFGRTClhaaaaggnvecIKLLQSsGADFHKKDKCGRTPLHYAAANCHFHCI 494
Cdd:PHA02876   350 -------------------------TLDRNKDIV------------ITLLEL-GANVNARDYCDKTPIHYAAVRNNVVII 391

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  495 ETLVTTGANVNETDDWGRTALHYAAASD---MDRNKTILGNAHENSEELERARELKEKEAALC----LEFLLQNDANPSI 567
Cdd:PHA02876   392 NTLLDYGADIEALSQKIGTALHFALCGTnpyMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCkldvIEMLLDNGADVNA 471

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2131006785  568 RDKEgyNSIHYAAAYGHRQCLELLLertNNGFEESDSGATKSPLHLAAYNGHHQALEVLLQSLVDLDIRDE 638
Cdd:PHA02876   472 INIQ--NQYPLLIALEYHGIVNILL---HYGAELRDSRVLHKSLNDNMFSFRYIIAHICIQDFIRHDIRNE 537
Ank_2 pfam12796
Ankyrin repeats (3 copies);
816-909 3.16e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.85  E-value: 3.16e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  816 LHWACYNGNENCIEVLLEQKC-FRTFIGNPFTPLHCAIINDHENCASLLLGAIDSSIvncrDDKGRTPLHAAAFADHVEC 894
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGAdANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL----KDNGRTALHYAARSGHLEI 76

                           90
                   ....*....|....*
gi 2131006785  895 LQLLLRHSAEVNAAD 909
Cdd:pfam12796   77 VKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
611-704 3.76e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.46  E-value: 3.76e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  611 LHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQgasIFVKDNVTKRTPLHASVINGHTLCL 690
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLEIV 77

                           90
                   ....*....|....
gi 2131006785  691 RLLLEIADNPEAID 704
Cdd:pfam12796   78 KLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
678-773 3.99e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.46  E-value: 3.99e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  678 LHASVINGHTLCLRLLLEiadNPEAIDVKDAKGQTPLMLAVAYGHIDAVSLLLEKeANVDAVDiMGCTALHRGIMTGHEE 757
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLE---NGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLE 75

                           90
                   ....*....|....*.
gi 2131006785  758 CVQMLLEQEVSILCKD 773
Cdd:pfam12796   76 IVKLLLEKGADINVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 760-1018 5.61e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 86.27  E-value: 5.61e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  760 QMLLEQEVSILCKDSRGRTPLHYAAARGHATWLSELLQMAlseEDCSFKDNQGYTPLHWACYNGNENCIEVLLEQkcfRT 839
Cdd:PHA02876   162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYG---ADVNIIALDDLSVLECAVDSKNIDTIKAIIDN---RS 235

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  840 FIGNPFTPLHCAIINDHENCASLLLGAIDSsiVNCRDDKGRTPLHAAAFADHVECL-QLLLRHSAEVNAADNSGKTALMM 918
Cdd:PHA02876   236 NINKNDLSLLKAIRNEDLETSLLLYDAGFS--VNSIDDCKNTPLHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLYL 313

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  919 AAENGQAGAVDILVNSAQADLTVKDKDLNTSLHLASSKGHEKCALLILdkIQDESLINARNNALQTPLHVAARNGLKVVV 998
Cdd:PHA02876   314 MAKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVITL--LELGANVNARDYCDKTPIHYAAVRNNVVII 391

                          250       260
                   ....*....|....*....|
gi 2131006785  999 EELLAKGACVLAIDENgIGT 1018
Cdd:PHA02876   392 NTLLDYGADIEALSQK-IGT 410
PHA03095 PHA03095
ankyrin-like protein; Provisional
 656-929 1.09e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 84.31  E-value: 1.09e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  656 VEALINQGASIFVKDNVtKRTPLHASVINGHTLCLRLLLEIADNPEAIDVKDAKGQTPLMLAVAYGH-IDAVSLLLEKEA 734
Cdd:PHA03095    30 VRRLLAAGADVNFRGEY-GKTPLHLYLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGA 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  735 NVDAVDIMGCTALH---RGiMTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGHATwlSELLQMALSE-EDCSFKDN 810
Cdd:PHA03095   109 DVNAKDKVGRTPLHvylSG-FNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNAN--VELLRLLIDAgADVYAVDD 185

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  811 QGYTPLHWAC--YNGNENCIEVLLEQKC---FRTFIGNpfTPLHCAIIndHENCASLLLGA--IDSSIVNCRDDKGRTPL 883
Cdd:PHA03095   186 RFRSLLHHHLqsFKPRARIVRELIRAGCdpaATDMLGN--TPLHSMAT--GSSCKRSLVLPllIAGISINARNRYGQTPL 261

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 2131006785  884 H-AAAFADHVECLQlLLRHSAEVNAADNSGKTALMMAAENGQAGAVD 929
Cdd:PHA03095   262 HyAAVFNNPRACRR-LIALGADINAVSSDGNTPLSLMVRNNNGRAVR 307
Ank_2 pfam12796
Ankyrin repeats (3 copies);
34-126 1.51e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.92  E-value: 1.51e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785   34 LVQAIFSGDPEEIRMLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLiLSGARVNAKDNMWlTPLHRAVASRSEEAVQ 113
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL-LEHADVNLKDNGR-TALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 2131006785  114 VLIKHSADVNARD 126
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 172-585 1.76e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 83.47  E-value: 1.76e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  172 NGHVEMV-NLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNL 250
Cdd:PHA02874    11 SGDIEAIeKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDN 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  251 GVEideiniygNTALHLACYNGQdaVVNELTDYGANVNQPNNSGFTPLHFAAASthGAL-CLELLVNNGADVNIQSKDGK 329
Cdd:PHA02874    91 GVD--------TSILPIPCIEKD--MIKTILDCGIDVNIKDAELKTFLHYAIKK--GDLeSIKMLFEYGADVNIEDDNGC 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  330 SPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGhellintlitsgadtakcgihsmfplhlaalnahsdc 409
Cdd:PHA02874   159 YPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYG------------------------------------- 201

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  410 crkllssgqkysivslfsnehvlsagfeidtpdkfgrtclhaaaaggNVECIKLLQSSGADFHKKDKCGRTPLHYAAanC 489
Cdd:PHA02874   202 -----------------------------------------------DYACIKLLIDHGNHIMNKCKNGFTPLHNAI--I 232

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  490 HFHCIETLVTTGANVNETDDWGRTALHYAAASDMDRNktilgnahenseelerarelkekeaalCLEFLLQNDANPSIRD 569
Cdd:PHA02874   233 HNRSAIELLINNASINDQDIDGSTPLHHAINPPCDID---------------------------IIDILLYHKADISIKD 285

                          410
                   ....*....|....*.
gi 2131006785  570 KEGYNSIHYAAAYGHR 585
Cdd:PHA02874   286 NKGENPIDTAFKYINK 301
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 96-303 1.80e-16

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: 84.29  E-value: 1.80e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785   96 WLTPLHRAVASRSEEAVQVLIK-HSADVNARDKNWQTPLHVAAANKAVKCAEVII---PLLssVNV---SD-RGGRTALH 167
Cdd:cd22192     17 SESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMeaaPEL--VNEpmtSDlYQGETALH 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  168 HAALNGHVEMVNLLLAKGANIN------AFDKKDRRAL-----H---WAAYMGHLDVVALLINHGAEVTCKDKKGYTPLH 233
Cdd:cd22192     95 IAVVNQNLNLVRELIARGADVVspratgTFFRPGPKNLiyygeHplsFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2131006785  234 AAASNGQINVVKH----LLNLGVEIDEINIYgntalhlacyngqdavvneltdyganvNQPNNSGFTPLHFAAA 303
Cdd:cd22192    175 ILVLQPNKTFACQmydlILSYDKEDDLQPLD---------------------------LVPNNQGLTPFKLAAK 221
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 555-765 2.77e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 82.35  E-value: 2.77e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  555 LEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLerTNNGFEESDSGATKSPLHLAAYNGHHQALEVLLQS--LVD 632
Cdd:PHA02875    18 ARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLM--KHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLgkFAD 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  633 lDIRDEKGRTALDLAAFKGHTECVEALINQGASIFVKdNVTKRTPLHASVINGHTLCLRLLLeiaDNPEAIDVKDAKGQT 712
Cdd:PHA02875    96 -DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIP-NTDKFSPLHLAVMMGDIKGIELLI---DHKACLDIEDCCGCT 170

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2131006785  713 PLMLAVAYGHIDAVSLLLEKEANVDAVDIMGC-TALHRGIMTGHEECVQMLLEQ 765
Cdd:PHA02875   171 PLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKR 224
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 42-192 4.88e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 82.24  E-value: 4.88e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785   42 DPEEIRMLIHKTEDVNALDSEK-RTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSA 120
Cdd:PHA02878   146 EAEITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2131006785  121 DVNARDKNWQTPLHVAAAnkAVKCAEVIIPLL---SSVNV-SDRGGRTALHHAALNGHVemVNLLLAKGANINAFD 192
Cdd:PHA02878   226 STDARDKCGNTPLHISVG--YCKDYDILKLLLehgVDVNAkSYILGLTALHSSIKSERK--LKLLLEYGADINSLN 297
Ank_2 pfam12796
Ankyrin repeats (3 copies);
576-670 5.06e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.38  E-value: 5.06e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  576 IHYAAAYGHRQCLELLLERTNNGFEESDSGATksPLHLAAYNGHHQALEVLLQSlVDLDIRDEkGRTALDLAAFKGHTEC 655
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRT--ALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEI 76

                           90
                   ....*....|....*
gi 2131006785  656 VEALINQGASIFVKD 670
Cdd:pfam12796   77 VKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
747-836 9.08e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 73.61  E-value: 9.08e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  747 LHRGIMTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGHATWLSELLQMALSEEdcsfkDNQGYTPLHWACYNGNEN 826
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL-----KDNGRTALHYAARSGHLE 75

                           90
                   ....*....|
gi 2131006785  827 CIEVLLEQKC 836
Cdd:pfam12796   76 IVKLLLEKGA 85
Ank_2 pfam12796
Ankyrin repeats (3 copies);
883-979 1.14e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 73.23  E-value: 1.14e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  883 LHAAAFADHVECLQLLLRHSAEVNAADNSGKTALMMAAENGQAGAVDILVNSAQADLTVKDKdlnTSLHLASSKGHEKCA 962
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR---TALHYAARSGHLEIV 77

                           90
                   ....*....|....*..
gi 2131006785  963 LLILDKIQDeslINARN 979
Cdd:pfam12796   78 KLLLEKGAD---INVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
449-569 3.13e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.07  E-value: 3.13e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  449 LHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTgANVNETDDwGRTALHYAAASdmdrnkt 528
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARS------- 71

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2131006785  529 ilgnaheNSEElerarelkekeaalCLEFLLQNDANPSIRD 569
Cdd:pfam12796   72 -------GHLE--------------IVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 723-1015 3.24e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 79.68  E-value: 3.24e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  723 IDAVSLLLEKEANVDAVDIMGCTALHRGIMTGHEEC---VQMLLEQEVSILCKDSRGRTPLHYaaarghatwlseLLQMA 799
Cdd:PHA03095    27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLHL------------YLYNA 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  800 LSEE----------DCSFKDNQGYTPLHwACYNG---NENCIEVLLEQKcfrtfignpftplhcaiindhencaslllga 866
Cdd:PHA03095    95 TTLDvikllikagaDVNAKDKVGRTPLH-VYLSGfniNPKVIRLLLRKG------------------------------- 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  867 IDssiVNCRDDKGRTPLHA---AAFADhVECLQLLLRHSAEVNAADNSGKTALMMAAEN--GQAGAVDILVnSAQADLTV 941
Cdd:PHA03095   143 AD---VNALDLYGMTPLAVllkSRNAN-VELLRLLIDAGADVYAVDDRFRSLLHHHLQSfkPRARIVRELI-RAGCDPAA 217

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2131006785  942 KDKDLNTSLHLASSKGHEKcALLILDKIQDESLINARNNALQTPLHVAARNGLKVVVEELLAKGACVLAIDENG 1015
Cdd:PHA03095   218 TDMLGNTPLHSMATGSSCK-RSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDG 290
PHA02798 PHA02798
ankyrin-like protein; Provisional
 100-386 3.35e-15

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 79.88  E-value: 3.35e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  100 LHRAvaSRSEEAVQVLIKHSADVNARDKNWQTPLhvaaankavkCAeviipLLSsvNVSDrggrtalhhaaLNGHVEMVN 179
Cdd:PHA02798    44 LQRD--SPSTDIVKLFINLGANVNGLDNEYSTPL----------CT-----ILS--NIKD-----------YKHMLDIVK 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  180 LLLAKGANINAFDKKDRRALHWA---AYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNG---QINVVKHLLNLGVE 253
Cdd:PHA02798    94 ILIENGADINKKNSDGETPLYCLlsnGYINNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNhhiDIEIIKLLLEKGVD 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  254 IDEI-NIYGNTALHlaCY-----NGQDA-VVNELTDYGANVNQPNNSgftplhfaAASTHGALCLELLVNNG-------- 318
Cdd:PHA02798   174 INTHnNKEKYDTLH--CYfkyniDRIDAdILKLFVDNGFIINKENKS--------HKKKFMEYLNSLLYDNKrfkknild 243

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2131006785  319 ---ADVNIQSKD--GKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGAD 386
Cdd:PHA02798   244 fifSYIDINQVDelGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKPN 316
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 607-950 3.56e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 80.49  E-value: 3.56e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  607 TKSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASIFVKD---------------- 670
Cdd:PHA02876   178 CITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDlsllkairnedletsl 257

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  671 ------------NVTKRTPLHASVingHTLCL-RLLLEIADNPEAIDVKDAKGQTPLMLAVAYGH-IDAVSLLLEKEANV 736
Cdd:PHA02876   258 llydagfsvnsiDDCKNTPLHHAS---QAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADV 334

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  737 DAVDIMGCTALHRG-IMTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGHATWLSELLQMALSEEDCSFKDNqgyTP 815
Cdd:PHA02876   335 NAADRLYITPLHQAsTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIG---TA 411

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  816 LHWACYNgnencievlleqkcfrtfiGNPFTPLHcAIINDHENcaslllgaidssiVNCRDDKGRTPLHAAAFAD-HVEC 894
Cdd:PHA02876   412 LHFALCG-------------------TNPYMSVK-TLIDRGAN-------------VNSKNKDLSTPLHYACKKNcKLDV 458

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2131006785  895 LQLLLRHSAEVNAADNSGKTALMMAAenGQAGAVDILVNSAQA--DLTVKDKDLNTSL 950
Cdd:PHA02876   459 IEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGAElrDSRVLHKSLNDNM 514
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 589-771 4.19e-15

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 80.30  E-value: 4.19e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  589 ELLLERTnngfEESDSGATKSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASIFV 668
Cdd:PLN03192   511 DLLGDNG----GEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHI 586

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  669 KDnVTKRTPLHASVINGHTLCLRLLLEIA--DNPEAidvkdakGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTA 746
Cdd:PLN03192   587 RD-ANGNTALWNAISAKHHKIFRILYHFAsiSDPHA-------AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATA 658

                          170       180
                   ....*....|....*....|....*
gi 2131006785  747 LHRGIMTGHEECVQMLLEQEVSILC 771
Cdd:PLN03192   659 LQVAMAEDHVDMVRLLIMNGADVDK 683
Ank_2 pfam12796
Ankyrin repeats (3 copies);
398-508 8.28e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.92  E-value: 8.28e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  398 LHLAALNAHSDCCRKLLSSGqkysivslfsnehvlsagFEIDTPDKFGRTCLHAAAAGGNVECIKLLqSSGADFHKKDKc 477
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENG------------------ADANLQDKNGRTALHLAAKNGHLEIVKLL-LEHADVNLKDN- 60

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2131006785  478 GRTPLHYAAANCHFHCIETLVTTGANVNETD 508
Cdd:pfam12796   61 GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 20-189 9.39e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 77.72  E-value: 9.39e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785   20 GAFPFHRQCEGFPPLVQAIFSGDPEEIRMLIHKTEDVNALDSEK-RTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLT 98
Cdd:PHA02875    58 GAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDgMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFS 137

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785   99 PLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVN-VSDRGGRTALHHAALNGHVEM 177
Cdd:PHA02875   138 PLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDyFGKNGCVAALCYAIENNKIDI 217

                          170
                   ....*....|..
gi 2131006785  178 VNLLLAKGANIN 189
Cdd:PHA02875   218 VRLFIKRGADCN 229
Ank_2 pfam12796
Ankyrin repeats (3 copies);
714-788 9.49e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.53  E-value: 9.49e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2131006785  714 LMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALHRGIMTGHEECVQMLLEQEvsILCKDSRGRTPLHYAAARGH 788
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA--DVNLKDNGRTALHYAARSGH 73
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 678-948 3.15e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 76.24  E-value: 3.15e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  678 LHASVINGHTLCLRLLLE--IADNPEAIDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALHRGIMTGH 755
Cdd:PHA03100     1 LYSYIVLTKSRIIKVKNIkyIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  756 E-----ECVQMLLEQEVSILCKDSRGRTPLHYAAAR--GHATWLSELLQMALseeDCSFKDNQGYTPLHWA--CYNGNEN 826
Cdd:PHA03100    81 NltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGA---NVNIKNSDGENLLHLYleSNKIDLK 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  827 CIEVLLEqkcfrtfignpftplHCAIINDHENCASLLLGAIDssiVNCRDDKGRTPLHAAAFADHVECLQLLLRHSAEVN 906
Cdd:PHA03100   158 ILKLLID---------------KGVDINAKNRVNYLLSYGVP---INIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPN 219

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 2131006785  907 AADNSGKTALMMAAENGQAGAVDILVNSAQADLTV-------KDKDLNT 948
Cdd:PHA03100   220 LVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIietllyfKDKDLNT 268
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 195-430 3.54e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 76.18  E-value: 3.54e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  195 DRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVeIDEINIYG-NTALHLACYNGQ 273
Cdd:PHA02875     2 DQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGA-IPDVKYPDiESELHDAVEEGD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  274 DAVVNELTDYGANVNQP-NNSGFTPLHFAAASTHGALcLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGG 352
Cdd:PHA02875    81 VKAVEELLDLGKFADDVfYKDGMTPLHLATILKKLDI-MKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKA 159

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2131006785  353 EIDCVDKDGNTPLHVAARYGHELLINTLITSGADTAKCGIHSMFPLHLAAL-NAHSDCCRKLLSSGQKYSIVSLFSNEH 430
Cdd:PHA02875   160 CLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIeNNKIDIVRLFIKRGADCNIMFMIEGEE 238
Ank_2 pfam12796
Ankyrin repeats (3 copies);
780-864 7.56e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.22  E-value: 7.56e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  780 LHYAAARGHATWLSELLQmalSEEDCSFKDNQGYTPLHWACYNGNENCIEVLLEQKCFRtFIGNPFTPLHCAIINDHENC 859
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLE---NGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN-LKDNGRTALHYAARSGHLEI 76


                   ....*
gi 2131006785  860 ASLLL 864
Cdd:pfam12796   77 VKLLL 81
Ank_2 pfam12796
Ankyrin repeats (3 copies);
554-637 6.08e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.52  E-value: 6.08e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  554 CLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNngFEESDSGATksPLHLAAYNGHHQALEVLLQSLVDL 633
Cdd:pfam12796   12 LVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRT--ALHYAARSGHLEIVKLLLEKGADI 87


                   ....
gi 2131006785  634 DIRD 637
Cdd:pfam12796   88 NVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 429-783 9.16e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 72.40  E-value: 9.16e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  429 EHVLSAGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVNetd 508
Cdd:PHA02876   162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNIN--- 238

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  509 dwgrtalhyaaasdmdRNKTILGNAHENsEELERArelkekeaalclefLLQNDANPSIRDKEGYNSihyaaayghrqcl 588
Cdd:PHA02876   239 ----------------KNDLSLLKAIRN-EDLETS--------------LLLYDAGFSVNSIDDCKN------------- 274

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  589 elllertnngfeesdsgatkSPLHLAAYNGHHQAL-EVLLQSLVDLDIRDEKGRTALDLAAFKGH-TECVEALINQGASI 666
Cdd:PHA02876   275 --------------------TPLHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADV 334

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  667 FVKDNVTKrTPLH-ASVINGHTLCLRLLLEIADNpeaIDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGCT 745
Cdd:PHA02876   335 NAADRLYI-TPLHqASTLDRNKDIVITLLELGAN---VNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGT 410

                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 2131006785  746 ALHRGIM-TGHEECVQMLLEQEVSILCKDSRGRTPLHYA 783
Cdd:PHA02876   411 ALHFALCgTNPYMSVKTLIDRGANVNSKNKDLSTPLHYA 449
PHA02798 PHA02798
ankyrin-like protein; Provisional
 77-295 1.09e-12

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 71.79  E-value: 1.09e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785   77 EIIELLILSGARVNAKDNMWLTPLHRAVASRSE-----EAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPL 151
Cdd:PHA02798    52 DIVKLFINLGANVNGLDNEYSTPLCTILSNIKDykhmlDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLFM 131

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  152 L---SSVNVSDRGGRTALHHAALNGH---VEMVNLLLAKGANINAFDKKDR-RALHwaAYMGH------LDVVALLINHG 218
Cdd:PHA02798   132 IengADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINTHNNKEKyDTLH--CYFKYnidridADILKLFVDNG 209

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  219 ---------------------------------------AEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINI 259
Cdd:PHA02798   210 fiinkenkshkkkfmeylnsllydnkrfkknildfifsyIDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITE 289

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 2131006785  260 YGNTALHLACYNGQDAVVNELTDYGANVNQPNNSGF 295
Cdd:PHA02798   290 LGNTCLFTAFENESKFIFNSILNKKPNKNTISYTYY 325
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 70-223 1.13e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 72.59  E-value: 1.13e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785   70 AAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVII 149
Cdd:PLN03192   532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY 611

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2131006785  150 PLLSSVNVSDRGgrTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTC 223
Cdd:PLN03192   612 HFASISDPHAAG--DLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDK 683
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 331-650 2.70e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 70.29  E-value: 2.70e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  331 PLHMtAVHGR-FTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSgadTAKCGIHSmfplhlaALNAHSDC 409
Cdd:PHA02878    40 PLHQ-AVEARnLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRS---INKCSVFY-------TLVAIKDA 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  410 CRKLLSSGQKYSIVSLFSNEHVLSAgFEIDTPDKFGRTclhaaaaggNVECIKLLQSSGADFHKKDK-CGRTPLHYAAAN 488
Cdd:PHA02878   109 FNNRNVEIFKIILTNRYKNIQTIDL-VYIDKKSKDDII---------EAEITKLLLSYGADINMKDRhKGNTALHYATEN 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  489 CHFHCIETLVTTGANVNETDDWGRTALHYAAASdmdRNKTIlgnahenseelerarelkekeaalcLEFLLQNDANPSIR 568
Cdd:PHA02878   179 KDQRLTELLLSYGANVNIPDKTNNSPLHHAVKH---YNKPI-------------------------VHILLENGASTDAR 230

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  569 DKEGYNSIHYAAAY-GHRQCLELLLER-TNNGFEESDSGATksPLHLAAYNghHQALEVLLQSLVDLDIRDEKGRTALDL 646
Cdd:PHA02878   231 DKCGNTPLHISVGYcKDYDILKLLLEHgVDVNAKSYILGLT--ALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSS 306


                   ....
gi 2131006785  647 AAFK 650
Cdd:PHA02878   307 AVKQ 310
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 276-505 3.57e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 69.63  E-value: 3.57e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  276 VVNELTDYGANVNQPNNSGFTPLHFAAaSTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEI- 354
Cdd:PHA02875    17 IARRLLDIGINPNFEIYDGISPIKLAM-KFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAd 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  355 DCVDKDGNTPLHVAARYGHELLINTLITSGADTakcgihsmfplhlaalnahsdccrkllssgqkysivslfsnehvlsa 434
Cdd:PHA02875    96 DVFYKDGMTPLHLATILKKLDIMKLLIARGADP----------------------------------------------- 128

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2131006785  435 gfEIDTPDKFgrTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVN 505
Cdd:PHA02875   129 --DIPNTDKF--SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANID 195
Ank_2 pfam12796
Ankyrin repeats (3 copies);
916-1012 4.57e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.21  E-value: 4.57e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  916 LMMAAENGQAGAVDILVNSaQADLTVKDKDLNTSLHLASSKGHEKCALLILDKIQdeslINARNNAlQTPLHVAARNGLK 995
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLEN-GADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD----VNLKDNG-RTALHYAARSGHL 74

                           90
                   ....*....|....*..
gi 2131006785  996 VVVEELLAKGACVLAID 1012
Cdd:pfam12796   75 EIVKLLLEKGADINVKD 91
Ank_4 pfam13637
Ankyrin repeats (many copies);
162-215 4.61e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 61.91  E-value: 4.61e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2131006785  162 GRTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLI 215
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 558-835 5.33e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 69.67  E-value: 5.33e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  558 LLQNDANPSIRDKEGYNSIHYAAAYGHRQCLE---LLLERTNNGFEESDSGATksPLHLAAYNGHHQA-LEVLLQSLVDL 633
Cdd:PHA03095    33 LLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDivrLLLEAGADVNAPERCGFT--PLHLYLYNATTLDvIKLLIKAGADV 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  634 DIRDEKGRTALD--LAAFKGHTECVEALINQGASIFVKDNvTKRTPLHASVINgHTLC---LRLLLEIADNPEAidvKDA 708
Cdd:PHA03095   111 NAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDL-YGMTPLAVLLKS-RNANvelLRLLIDAGADVYA---VDD 185

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  709 KGQTPLMLAVAYGHIDA--VSLLLEKEANVDAVDIMGCTALHrgIMTGHEEC----VQMLLEQEVSILCKDSRGRTPLHY 782
Cdd:PHA03095   186 RFRSLLHHHLQSFKPRAriVRELIRAGCDPAATDMLGNTPLH--SMATGSSCkrslVLPLLIAGISINARNRYGQTPLHY 263

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2131006785  783 AAARGHATWLSELLQMAlseEDCSFKDNQGYTPLHWACYNGNENCIEVLLEQK 835
Cdd:PHA03095   264 AAVFNNPRACRRLIALG---ADINAVSSDGNTPLSLMVRNNNGRAVRAALAKN 313
Ank_2 pfam12796
Ankyrin repeats (3 copies);
365-475 8.45e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.44  E-value: 8.45e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  365 LHVAARYGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSGQKYSIVSlfsnehvlsagfeidtpdkf 444
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN-------------------- 60

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2131006785  445 GRTCLHAAAAGGNVECIKLLQSSGADFHKKD 475
Cdd:pfam12796   61 GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 255-522 8.55e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 68.75  E-value: 8.55e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  255 DEINIYGNTALHLACYNGQDAVVNELTDYGANVNQPNNSGFTPLHFAAASTHGALCLELL-VNNGADVNIQSKDGKSPLH 333
Cdd:PHA02878    31 TSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIrSINKCSVFYTLVAIKDAFN 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  334 MTAVH-------GRFTRSQTLiqNGGEIDCVDKDGNTPLHVaaryghellINTLITSGADTAKCGIHSM-FPLHLAALNA 405
Cdd:PHA02878   111 NRNVEifkiiltNRYKNIQTI--DLVYIDKKSKDDIIEAEI---------TKLLLSYGADINMKDRHKGnTALHYATENK 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  406 HSDCCRKLLSSGQkysivslfsnehvlsagfEIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYA 485
Cdd:PHA02878   180 DQRLTELLLSYGA------------------NVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIS 241

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 2131006785  486 AANC-HFHCIETLVTTGANVN-ETDDWGRTALHYAAASD 522
Cdd:PHA02878   242 VGYCkDYDILKLLLEHGVDVNaKSYILGLTALHSSIKSE 280
Ank_4 pfam13637
Ankyrin repeats (many copies);
196-248 8.97e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 61.14  E-value: 8.97e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2131006785  196 RRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLL 248
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
445-498 1.83e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.98  E-value: 1.83e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2131006785  445 GRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLV 498
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 783-949 2.65e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 67.97  E-value: 2.65e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  783 AAARGHATWLSELLQMALseeDCSFKDNQGYTPLHWACYNGNENCIEVLLEQKC---FRTFIGNpfTPLHCAIINDHENC 859
Cdd:PLN03192   532 VASTGNAALLEELLKAKL---DPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACnvhIRDANGN--TALWNAISAKHHKI 606

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  860 ASLLLGAIDSSIVNCRDDKgrtpLHAAAFADHVECLQLLLRHSAEVNAADNSGKTALMMAAENGQAGAVDILV-NSAQAD 938
Cdd:PLN03192   607 FRILYHFASISDPHAAGDL----LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLImNGADVD 682

                          170
                   ....*....|.
gi 2131006785  939 LTVKDKDLNTS 949
Cdd:PLN03192   683 KANTDDDFSPT 693
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 172-297 3.11e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 64.07  E-value: 3.11e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  172 NGHVEMVNLLLAKGANINAFDKKDRRAL--HWAAYMGHL--DVVALLINHGAEVTCKDKKGYTPLHAAASNG--QINVVK 245
Cdd:PHA02859    63 KVNVEILKFLIENGADVNFKTRDNNLSAlhHYLSFNKNVepEILKILIDSGSSITEEDEDGKNLLHMYMCNFnvRINVIK 142

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2131006785  246 HLLNLGVEIDEINIYGNTALH-LACYNGQDAVVNELTDYGANVNQPNNSGFTP 297
Cdd:PHA02859   143 LLIDSGVSFLNKDFDNNNILYsYILFHSDKKIFDFLTSLGIDINETNKSGYNC 195
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 188-485 5.41e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 66.44  E-value: 5.41e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  188 INAFDKKDRRA----------LHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEI 257
Cdd:PHA02878    20 IEYIDHTENYStsaslipfipLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVF 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  258 NIYgnTALHLACYNGQDAVVNE-LTDYGANVNQPNNSGFTPLHFAAASThgALCLELLVNNGADVNIQSKD-GKSPLHMT 335
Cdd:PHA02878   100 YTL--VAIKDAFNNRNVEIFKIiLTNRYKNIQTIDLVYIDKKSKDDIIE--AEITKLLLSYGADINMKDRHkGNTALHYA 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  336 AVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGADT---AKCGihsMFPLHLAAlnahsdccrk 412
Cdd:PHA02878   176 TENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTdarDKCG---NTPLHISV---------- 242

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2131006785  413 llSSGQKYSIVSLfsnehVLSAGFEIDTPDKF-GRTCLHAAAAGGNVecIKLLQSSGADFHKKDKCGRTPLHYA 485
Cdd:PHA02878   243 --GYCKDYDILKL-----LLEHGVDVNAKSYIlGLTALHSSIKSERK--LKLLLEYGADINSLNSYKLTPLSSA 307
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 481-718 6.16e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 66.06  E-value: 6.16e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  481 PLHYAAANCHFHCIETLVTTGANVNETDDWGRTALH--------------------------YAAASDM--DRN----KT 528
Cdd:PHA02878    40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHiickepnklgmkemirsinkcsvfytLVAIKDAfnNRNveifKI 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  529 ILGNAHENSEELErARELKEKEAALCLE-----FLLQNDANPSIRDKEGYNS-IHYAAAYGHRQCLELLLERTNNgfEES 602
Cdd:PHA02878   120 ILTNRYKNIQTID-LVYIDKKSKDDIIEaeitkLLLSYGADINMKDRHKGNTaLHYATENKDQRLTELLLSYGAN--VNI 196

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  603 DSGATKSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLA-AFKGHTECVEALINQGASIFVKDNVTKRTPLHAS 681
Cdd:PHA02878   197 PDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYILGLTALHSS 276

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 2131006785  682 VINGHTlcLRLLLEIADNPEAIdvkDAKGQTPLMLAV 718
Cdd:PHA02878   277 IKSERK--LKLLLEYGADINSL---NSYKLTPLSSAV 308
Ank_2 pfam12796
Ankyrin repeats (3 copies);
265-358 6.42e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.74  E-value: 6.42e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  265 LHLACYNGQDAVVNELTDYGANVNQPNNSGFTPLHFAAASTHGAlCLELLVNNgADVNIQSkDGKSPLHMTAVHGRFTRS 344
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLE-IVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77

                           90
                   ....*....|....
gi 2131006785  345 QTLIQNGGEIDCVD 358
Cdd:pfam12796   78 KLLLEKGADINVKD 91
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 71-302 1.09e-10

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: 65.87  E-value: 1.09e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785   71 AFLGDAEIIELLILSGARVNAK-------DNMWLTPLHRAVA-SRSEEAVQVLIKHSADVNARDknwqTPLHVAAANKAV 142
Cdd:TIGR00870   20 AFLPAAERGDLASVYRDLEEPKklnincpDRLGRSALFVAAIeNENLELTELLLNLSCRGAVGD----TLLHAISLEYVD 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  143 KCAEVIIPLLSS---------VNVSDRG----GRTALHHAALNGHVEMVNLLLAKGANINA------FDKKDRRA----- 198
Cdd:TIGR00870   96 AVEAILLHLLAAfrksgplelANDQYTSeftpGITALHLAAHRQNYEIVKLLLERGASVPAracgdfFVKSQGVDsfyhg 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  199 ---LHWAAYMGHLDVVALLINHGAEVTCKDKKGytplhaaasngqiNVVKHLLNLGVEideiNIYGNTALHLACYngqda 275
Cdd:TIGR00870  176 espLNAAACLGSPSIVALLSEDPADILTADSLG-------------NTLLHLLVMENE----FKAEYEELSCQMY----- 233

                          250       260       270
                   ....*....|....*....|....*....|....
gi 2131006785  276 vvNELTDYGANVNQ-------PNNSGFTPLHFAA 302
Cdd:TIGR00870  234 --NFALSLLDKLRDskeleviLNHQGLTPLKLAA 265
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 175-337 1.29e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 65.01  E-value: 1.29e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  175 VEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVtcKD---KKGYTPLHAAASNGQINVVKHLLNLG 251
Cdd:PHA02875    48 SEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFA--DDvfyKDGMTPLHLATILKKLDIMKLLIARG 125

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  252 VEIDEINIYGNTALHLACYNGQDAVVNELTDYGANVNQPNNSGFTPLHFAAASTHGALClELLVNNGADVNIQSKDGKSP 331
Cdd:PHA02875   126 ADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAIC-KMLLDSGANIDYFGKNGCVA 204


                   ....*.
gi 2131006785  332 LHMTAV 337
Cdd:PHA02875   205 ALCYAI 210
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 803-1014 1.43e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 64.69  E-value: 1.43e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  803 EDCSFKDNqgYTPLHWACYNGNENCIEVLLEQKCF-RTFIGNPFTPLH-----CAIINDHENCASLLL--GAIdssiVNC 874
Cdd:PHA03100    28 NDYSYKKP--VLPLYLAKEARNIDVVKILLDNGADiNSSTKNNSTPLHylsniKYNLTDVKEIVKLLLeyGAN----VNA 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  875 RDDKGRTPLHAAAFA--DHVECLQLLLRHSAEVNAADNSGKTALMMAAENG------------------QAGAVDILVNS 934
Cdd:PHA03100   102 PDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNkidlkilkllidkgvdinAKNRVNYLLSY 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  935 AqADLTVKDKDLNTSLHLASSKGHEKCALLILDKIQDeslINARNNALQTPLHVAARNGLKVVVEELLAKGACVLAIDEN 1014
Cdd:PHA03100   182 G-VPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGAN---PNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
Ank_2 pfam12796
Ankyrin repeats (3 copies);
332-422 2.30e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.20  E-value: 2.30e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  332 LHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGAdtAKCGIHSMFPLHLAALNAHSDCCR 411
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|.
gi 2131006785  412 KLLSSGQKYSI 422
Cdd:pfam12796   79 LLLEKGADINV 89
Ank_4 pfam13637
Ankyrin repeats (many copies);
712-763 5.24e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.13  E-value: 5.24e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2131006785  712 TPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALHRGIMTGHEECVQMLL 763
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 205-396 1.24e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 62.58  E-value: 1.24e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  205 MGHLDVVALLINHGAEVTckDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINIYGNTALHLACYNGQDAVVNELTDYG 284
Cdd:PLN03192   504 LHDLNVGDLLGDNGGEHD--DPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA 581

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  285 ANVNQPNNSGFTPLHFAAASTHGALcLELLVNNGADVNIQSkdGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTP 364
Cdd:PLN03192   582 CNVHIRDANGNTALWNAISAKHHKI-FRILYHFASISDPHA--AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATA 658

                          170       180       190
                   ....*....|....*....|....*....|..
gi 2131006785  365 LHVAARYGHELLINTLITSGADTAKCGIHSMF 396
Cdd:PLN03192   659 LQVAMAEDHVDMVRLLIMNGADVDKANTDDDF 690
Ank_4 pfam13637
Ankyrin repeats (many copies);
609-660 1.55e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.59  E-value: 1.55e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2131006785  609 SPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALI 660
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 166-248 1.63e-09

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 61.84  E-value: 1.63e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  166 LHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVK 245
Cdd:PTZ00322    86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165


                   ...
gi 2131006785  246 HLL 248
Cdd:PTZ00322   166 LLS 168
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 169-327 1.72e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 62.19  E-value: 1.72e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  169 AALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLL 248
Cdd:PLN03192   532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY 611

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2131006785  249 NLGvEIDEINIYGNTaLHLACYNGQDAVVNELTDYGANVNQPNNSGFTPLHFAAASTHGALcLELLVNNGADVNIQSKD 327
Cdd:PLN03192   612 HFA-SISDPHAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDM-VRLLIMNGADVDKANTD 687
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 129-381 2.57e-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: 61.18  E-value: 2.57e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  129 WQTPLHVAAANKAVKCaevIIPLL--SSVNVSDRG--GRTALHHAALNGHVEMVNLLLakganinafdkkdrralhwaay 204
Cdd:cd22192     17 SESPLLLAAKENDVQA---IKKLLkcPSCDLFQRGalGETALHVAALYDNLEAAVVLM---------------------- 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  205 mghlDVVALLINHgaEVTCkdkkgytplhaaasngqinvvkhllnlgveideiNIY-GNTALHLACYNGQDAVVNELTDY 283
Cdd:cd22192     72 ----EAAPELVNE--PMTS----------------------------------DLYqGETALHIAVVNQNLNLVRELIAR 111

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  284 GANVNQPNNSG--FT------------PLHFAAASTHGALcLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLI- 348
Cdd:cd22192    112 GADVVSPRATGtfFRpgpknliyygehPLSFAACVGNEEI-VRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFACQMYd 190

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 2131006785  349 --------QNGGEIDCV-DKDGNTPLHVAARYGHELLINTLI 381
Cdd:cd22192    191 lilsydkeDDLQPLDLVpNNQGLTPFKLAAKEGNIVMFQHLV 232
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 814-1044 2.79e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 60.75  E-value: 2.79e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  814 TPLHWACYNGNENCIEVLLEQKCFRTFIG-NPFTPLHCAI-INDHENCASLLLGAIDSSI-------------------- 871
Cdd:PHA02874    37 TPLIDAIRSGDAKIVELFIKHGADINHINtKIPHPLLTAIkIGAHDIIKLLIDNGVDTSIlpipciekdmiktildcgid 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  872 VNCRDDKGRTPLHAAAFADHVECLQLLLRHSAEVNAADNSGKTALMMAAENGQAGAVDILVNSAqADLTVKDKDLNTSLH 951
Cdd:PHA02874   117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKG-AYANVKDNNGESPLH 195

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  952 LASSKGHEKCALLILDkiQDESLINARNNALqTPLHVAARNGLKVVveELLAKGACVLAIDENGigtSSPCLFlrshtpA 1031
Cdd:PHA02874   196 NAAEYGDYACIKLLID--HGNHIMNKCKNGF-TPLHNAIIHNRSAI--ELLINNASINDQDIDG---STPLHH------A 261

                          250
                   ....*....|...
gi 2131006785 1032 LACAPNKDVADCL 1044
Cdd:PHA02874   262 INPPCDIDIIDIL 274
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 77-339 2.89e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 60.91  E-value: 2.89e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785   77 EIIELLILSGARVNAKDNMwLTPL-----HRAVAS-RSEEAVQVLIKHSADVNARDKNWQTPlhvaaankavkcaevIIP 150
Cdd:PHA02989    51 KIVKLLIDNGADVNYKGYI-ETPLcavlrNREITSnKIKKIVKLLLKFGADINLKTFNGVSP---------------IVC 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  151 LLSSVNVSDrggrtalhhaalnghVEMVNLLLAKGANINafDKKDRRA---LH--WAAYMGHLDVVALLINHGAEV-TCK 224
Cdd:PHA02989   115 FIYNSNINN---------------CDMLRFLLSKGINVN--DVKNSRGynlLHmyLESFSVKKDVIKILLSFGVNLfEKT 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  225 DKKGYTP----LHAAASNGQINVVKHLLNLGVEIDEINIYGNTAL------HLACYNGQDAVVNELTDYgANVNQPNNSG 294
Cdd:PHA02989   178 SLYGLTPmniyLRNDIDVISIKVIKYLIKKGVNIETNNNGSESVLesfldnNKILSKKEFKVLNFILKY-IKINKKDKKG 256

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 2131006785  295 FTPLhFAAASTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHG 339
Cdd:PHA02989   257 FNPL-LISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHG 300
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 675-787 3.02e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 60.39  E-value: 3.02e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  675 RTPLHASVINGHTLCLRLLLEIadNPEAIDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALHRGIMTG 754
Cdd:PHA02875    69 ESELHDAVEEGDVKAVEELLDL--GKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMG 146

                           90       100       110
                   ....*....|....*....|....*....|...
gi 2131006785  755 HEECVQMLLEQEVSILCKDSRGRTPLHYAAARG 787
Cdd:PHA02875   147 DIKGIELLIDHKACLDIEDCCGCTPLIIAMAKG 179
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 578-797 4.72e-09

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 60.41  E-value: 4.72e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  578 YAAAYGHRQCLELLL--ERTNNgFEESDSGATKspLHLAAYNGHHQALEVLLQS---LVDLDIRDE--KGRTALDLAAFK 650
Cdd:cd22192     23 LAAKENDVQAIKKLLkcPSCDL-FQRGALGETA--LHVAALYDNLEAAVVLMEAapeLVNEPMTSDlyQGETALHIAVVN 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  651 GHTECVEALINQGAsifvkDNVTKRTPLHASVINGHTLCLRllleiadnpeaidvkdakGQTPLMLAVAYGHIDAVSLLL 730
Cdd:cd22192    100 QNLNLVRELIARGA-----DVVSPRATGTFFRPGPKNLIYY------------------GEHPLSFAACVGNEEIVRLLI 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2131006785  731 EKEANVDAVDIMGCTALHRGIMTGHEECV-QM---LLEQEVSI------LCKDSRGRTPLHYAAARGHATWLSELLQ 797
Cdd:cd22192    157 EHGADIRAQDSLGNTVLHILVLQPNKTFAcQMydlILSYDKEDdlqpldLVPNNQGLTPFKLAAKEGNIVMFQHLVQ 233
PHA03095 PHA03095
ankyrin-like protein; Provisional
 42-186 4.79e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 60.04  E-value: 4.79e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785   42 DPEEIRMLIHKTEDVNALDSEKRTPLHVAAFLGD--AEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHS 119
Cdd:PHA03095   201 RARIVRELIRAGCDPAATDMLGNTPLHSMATGSSckRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALG 280

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2131006785  120 ADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVNVSDRggrtALHHAALNGHV-------EMVNLLLAKGA 186
Cdd:PHA03095   281 ADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAA----TLNTASVAGGDipsdatrLCVAKVVLRGA 350
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 33-136 4.97e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 59.89  E-value: 4.97e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785   33 PLVQAIFSGDPEEIRMLIHKTEDVNALDSEKRTPLHVA-AFLGDAEIIELLILSGARVNAKDNMW-LTPLHRAVasRSEE 110
Cdd:PHA02878   204 PLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYILgLTALHSSI--KSER 281

                           90       100
                   ....*....|....*....|....*.
gi 2131006785  111 AVQVLIKHSADVNARDKNWQTPLHVA 136
Cdd:PHA02878   282 KLKLLLEYGADINSLNSYKLTPLSSA 307
PHA02946 PHA02946
ankyin-like protein; Provisional
 345-593 5.26e-09

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 60.07  E-value: 5.26e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  345 QTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGADTAKCGIHSMFPLHL-------------------AALNA 405
Cdd:PHA02946    56 EELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYlsgtddevierinllvqygAKINN 135

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  406 HSD--CCRKLLSSGQKYSIVSlfsnEHVLSAGFEIDTPDKFGRTCLHAAAAGGN--VECIKLLQSSGADFHKKDKCGRTP 481
Cdd:PHA02946   136 SVDeeGCGPLLACTDPSERVF----KKIMSIGFEARIVDKFGKNHIHRHLMSDNpkASTISWMMKLGISPSKPDHDGNTP 211

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  482 LHYAAANCHFHC-IETLVTTGANVNETDDWGRTALHYAAASdmdrnktiLGNAHENSEELERARELKEKEAALCLeFLLQ 560
Cdd:PHA02946   212 LHIVCSKTVKNVdIINLLLPSTDVNKQNKFGDSPLTLLIKT--------LSPAHLINKLLSTSNVITDQTVNICI-FYDR 282

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 2131006785  561 NDANPSIRDK-EGYNSIHY--AAAYGHRQCLELLLE 593
Cdd:PHA02946   283 DDVLEIINDKgKQYDSTDFkmAVEVGSIRCVKYLLD 318
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 711-932 7.57e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 59.23  E-value: 7.57e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  711 QTPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALHRGIMTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGHAT 790
Cdd:PHA02875     3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  791 WLSELLQMALSEEDCSFKDnqGYTPLHWACYNGNENCIEVLLEQKCfRTFIGNP--FTPLHCAIINDHENCASLLLGaiD 868
Cdd:PHA02875    83 AVEELLDLGKFADDVFYKD--GMTPLHLATILKKLDIMKLLIARGA-DPDIPNTdkFSPLHLAVMMGDIKGIELLID--H 157

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2131006785  869 SSIVNCRDDKGRTPLHAAAFADHVECLQLLLRHSAEVNAADNSGKTALM-MAAENGQAGAVDILV 932
Cdd:PHA02875   158 KACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcYAIENNKIDIVRLFI 222
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 732-1012 1.05e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 59.12  E-value: 1.05e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  732 KEANVDAVDIMGCTALHRGIMTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGHATWLSELLQMALseedcsfKDNQ 811
Cdd:PHA02878    26 TENYSTSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSIN-------KCSV 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  812 GYT--PLHWACYNGNENCIEVLLEQKcfrtFIGNpftplhcAIINDHENCASLLLGAIDSSI----------VNCRD-DK 878
Cdd:PHA02878    99 FYTlvAIKDAFNNRNVEIFKIILTNR----YKNI-------QTIDLVYIDKKSKDDIIEAEItklllsygadINMKDrHK 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  879 GRTPLHAAAFADHVECLQLLLRHSAEVNAADNSGKTALMMAAENGQAGAVDILVNSAqADLTVKDKDLNTSLHLASSKGH 958
Cdd:PHA02878   168 GNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENG-ASTDARDKCGNTPLHISVGYCK 246

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2131006785  959 EKCALLILdkIQDESLINARNNALQ-TPLHVAARNGLKVVVeeLLAKGACVLAID 1012
Cdd:PHA02878   247 DYDILKLL--LEHGVDVNAKSYILGlTALHSSIKSERKLKL--LLEYGADINSLN 297
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 642-824 1.31e-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: 1.31e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  642 TALDLAAFKGHTECVEALI-NQGASIFVKDNVTKrTPLHASVINGHTLCLRLLLEIAdnPEAIDVKDA----KGQTPLML 716
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGE-TALHVAALYDNLEAAVVLMEAA--PELVNEPMTsdlyQGETALHI 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  717 AVAYGHIDAVSLLLEKEANVDAVDIMGcTALHRGI---------------MTGHEECVQMLLEQEVSILCKDSRGRTPLH 781
Cdd:cd22192     96 AVVNQNLNLVRELIARGADVVSPRATG-TFFRPGPknliyygehplsfaaCVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 2131006785  782 YAAARGHATWLSEL--LQMALSEEDCS-----FKDNQGYTPLHWACYNGN 824
Cdd:cd22192    175 ILVLQPNKTFACQMydLILSYDKEDDLqpldlVPNNQGLTPFKLAAKEGN 224
PHA02946 PHA02946
ankyin-like protein; Provisional
 75-334 1.70e-08

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 58.14  E-value: 1.70e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785   75 DAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKavkcAEVIipllss 154
Cdd:PHA02946    51 DERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTD----DEVI------ 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  155 vnvsdrggrtalhhaalnghvEMVNLLLAKGANINafdkkdrralhwaaymghldvvallinhgaevTCKDKKGYTPLHA 234
Cdd:PHA02946   121 ---------------------ERINLLVQYGAKIN--------------------------------NSVDEEGCGPLLA 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  235 AASNGQiNVVKHLLNLGVEIDEINIYGNTAL--HLACYNGQDAVVNELTDYGANVNQPNNSGFTPLHFAAASTHGALCLE 312
Cdd:PHA02946   148 CTDPSE-RVFKKIMSIGFEARIVDKFGKNHIhrHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCSKTVKNVDII 226

                          250       260
                   ....*....|....*....|..
gi 2131006785  313 LLVNNGADVNIQSKDGKSPLHM 334
Cdd:PHA02946   227 NLLLPSTDVNKQNKFGDSPLTL 248
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 609-779 1.75e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.08  E-value: 1.75e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  609 SPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGAsiFVKDNVTKR--TPLHASVINGH 686
Cdd:PHA02875    37 SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK--FADDVFYKDgmTPLHLATILKK 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  687 TLCLRLLLEIADNPeaiDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALHRGIMTGHEECVQMLLEQE 766
Cdd:PHA02875   115 LDIMKLLIARGADP---DIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSG 191

                          170
                   ....*....|...
gi 2131006785  767 VSIlckDSRGRTP 779
Cdd:PHA02875   192 ANI---DYFGKNG 201
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 33-169 1.82e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 58.05  E-value: 1.82e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785   33 PLVQAIFSGDPEEIRMLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVA-SRSeeA 111
Cdd:PHA02874   160 PIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIhNRS--A 237

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2131006785  112 VQVLIkHSADVNARDKNWQTPLHVAAankAVKCAEVIIPLL----SSVNVSDRGGRTALHHA 169
Cdd:PHA02874   238 IELLI-NNASINDQDIDGSTPLHHAI---NPPCDIDIIDILlyhkADISIKDNKGENPIDTA 295
Ank_4 pfam13637
Ankyrin repeats (many copies);
478-520 1.94e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.51  E-value: 1.94e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 2131006785  478 GRTPLHYAAANCHFHCIETLVTTGANVNETDDWGRTALHYAAA 520
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAAS 43
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 451-666 2.14e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 58.34  E-value: 2.14e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  451 AAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVNETDDWGRTALHYAAASDMDRNKTIL 530
Cdd:PLN03192   531 TVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  531 gnahenseelerarelkekeaalclefllqndanpsirdkegynsIHYAAAyghrqclelllertnngfeeSDSGATKSP 610
Cdd:PLN03192   611 ---------------------------------------------YHFASI--------------------SDPHAAGDL 625

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2131006785  611 LHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASI 666
Cdd:PLN03192   626 LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
Ank_4 pfam13637
Ankyrin repeats (many copies);
131-182 3.39e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.74  E-value: 3.39e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2131006785  131 TPLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHVEMVNLLL 182
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 130-304 3.84e-08

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: 57.58  E-value: 3.84e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  130 QTPLHVAAANKAVKCAEVIIPLLSSVNVSDRG--------------GRTALHHAALNGHVEMVNLLLAKGANINA----- 190
Cdd:cd21882     27 KTCLHKAALNLNDGVNEAIMLLLEAAPDSGNPkelvnapctdefyqGQTALHIAIENRNLNLVRLLVENGADVSAratgr 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  191 FDKKDRR--------ALHWAAYMGHLDVVALLINHGAE---VTCKDKKGYTPLHAAasngqinvvkhllnlgVEIDEiNI 259
Cdd:cd21882    107 FFRKSPGnlfyfgelPLSLAACTNQEEIVRLLLENGAQpaaLEAQDSLGNTVLHAL----------------VLQAD-NT 169

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2131006785  260 YGNTALHLACYNGqdavvneLTDYGANVNQ-------PNNSGFTPLHFAAAS 304
Cdd:cd21882    170 PENSAFVCQMYNL-------LLSYGAHLDPtqqleeiPNHQGLTPLKLAAVE 214
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 296-483 3.99e-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: 57.33  E-value: 3.99e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  296 TPLhFAAASTHGALCLE-LLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGE-----IDCVDKDGNTPLHVAA 369
Cdd:cd22192     19 SPL-LLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElvnepMTSDLYQGETALHIAV 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  370 RYGHELLINTLITSGADTAK---CGihSMFPLHLAALnahsdccrkllssgqkysivsLFSNEHVLSagfeidtpdkFgr 446
Cdd:cd22192     98 VNQNLNLVRELIARGADVVSpraTG--TFFRPGPKNL---------------------IYYGEHPLS----------F-- 142

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 2131006785  447 tclhaAAAGGNVECIKLLQSSGADFHKKDKCGRTPLH 483
Cdd:cd22192    143 -----AACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
Ank_4 pfam13637
Ankyrin repeats (many copies);
96-149 4.04e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.74  E-value: 4.04e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2131006785   96 WLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVII 149
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 99-272 4.54e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 54.83  E-value: 4.54e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785   99 PLHRAVASRSEEAVQVLIKHSADVNardKNWQTPLHVAAANKAV--KCAEVIIPLLSSVNVSDRG-GRTALHH-AALNGH 174
Cdd:PHA02859    24 PLFYYVEKDDIEGVKKWIKFVNDCN---DLYETPIFSCLEKDKVnvEILKFLIENGADVNFKTRDnNLSALHHyLSFNKN 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  175 V--EMVNLLLAKGANINAFDKKDRRALHwaAYMGH----LDVVALLINHGAEVTCKDKKGYTPLHA-AASNGQINVVKHL 247
Cdd:PHA02859   101 VepEILKILIDSGSSITEEDEDGKNLLH--MYMCNfnvrINVIKLLIDSGVSFLNKDFDNNNILYSyILFHSDKKIFDFL 178

                          170       180
                   ....*....|....*....|....*
gi 2131006785  248 LNLGVEIDEINIYGNTALHLACYNG 272
Cdd:PHA02859   179 TSLGIDINETNKSGYNCYDLIKFRN 203
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 362-516 4.61e-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: 57.33  E-value: 4.61e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  362 NTPLHVAARYGHELLINTLITS-GADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSgqkysiVSLFSNEHVLSAGFEidt 440
Cdd:cd22192     18 ESPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLMEA------APELVNEPMTSDLYQ--- 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  441 pdkfGRTCLHAAAAGGNVECIKLLQSSGAD----------FHKKDKC----GRTPLHYAAANCHFHCIETLVTTGANVNE 506
Cdd:cd22192     89 ----GETALHIAVVNQNLNLVRELIARGADvvspratgtfFRPGPKNliyyGEHPLSFAACVGNEEIVRLLIEHGADIRA 164

                          170
                   ....*....|
gi 2131006785  507 TDDWGRTALH 516
Cdd:cd22192    165 QDSLGNTVLH 174
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 67-348 4.64e-08

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 57.23  E-value: 4.64e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785   67 LHvaAFLG----DAEIIELLILSGARVNAKDNMWLTPLHRAV--ASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANK 140
Cdd:PHA02716   181 LH--AYLGnmyvDIDILEWLCNNGVNVNLQNNHLITPLHTYLitGNVCASVIKKIIELGGDMDMKCVNGMSPIMTYIINI 258

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  141 AVKCAEVI----------------------IPLLSSVNVS---------------DRGGRTALHHAAL--NGHVEMVNLL 181
Cdd:PHA02716   259 DNINPEITniyiesldgnkvknipmilhsyITLARNIDISvvysflqpgvklhykDSAGRTCLHQYILrhNISTDIIKLL 338

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  182 LAKGANINAFDKKDRRALHwaAYMG----------------HLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQ----- 240
Cdd:PHA02716   339 HEYGNDLNEPDNIGNTVLH--TYLSmlsvvnildpetdndiRLDVIQCLISLGADITAVNCLGYTPLTSYICTAQnymyy 416

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  241 -----------INVVKH--LLNLGVEIDEiniyGNTALH--LACYN-GQDAVVNELTDYG----------ANVNQPNN-- 292
Cdd:PHA02716   417 diidclisdkvLNMVKHriLQDLLIRVDD----TPCIIHhiIAKYNiPTDLYTDEYEPYDstkihdvyhcAIIERYNNav 492

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2131006785  293 ---SGFTPLHFAAASTHGAL----CLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLI 348
Cdd:PHA02716   493 cetSGMTPLHVSIISHTNANivmdSFVYLLSIQYNINIPTKNGVTPLMLTMRNNRLSGHQWYI 555
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 760-1003 4.93e-08

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: 57.40  E-value: 4.93e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  760 QMLLE-QEVSILCKDSRGRTPLHYAAARGHATWLSELLQmalseedcsFKDNQGY---TPLHWACYNGNENCIEVLLEQK 835
Cdd:TIGR00870   35 RDLEEpKKLNINCPDRLGRSALFVAAIENENLELTELLL---------NLSCRGAvgdTLLHAISLEYVDAVEAILLHLL 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  836 CFRTFIGNPF--------------TPLHCAIINDHENCASLLL--GAIDSSIVNCRDDK----------GRTPLHAAAFA 889
Cdd:TIGR00870  106 AAFRKSGPLElandqytseftpgiTALHLAAHRQNYEIVKLLLerGASVPARACGDFFVksqgvdsfyhGESPLNAAACL 185

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  890 DHVECLQLLLRHSAEVNAADNSGKTALMMAAEngqagavdilvnsaQADLTVKDKDLNTSLHLAsskghekcALLILDKI 969
Cdd:TIGR00870  186 GSPSIVALLSEDPADILTADSLGNTLLHLLVM--------------ENEFKAEYEELSCQMYNF--------ALSLLDKL 243

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 2131006785  970 QD-ESLINARNNALQTPLHVAARNGLKVVVEELLA 1003
Cdd:TIGR00870  244 RDsKELEVILNHQGLTPLKLAAKEGRIVLFRLKLA 278
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 862-938 6.00e-08

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.83  E-value: 6.00e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2131006785  862 LLLGAIDSsivNCRDDKGRTPLHAAAFADHVECLQLLLRHSAEVNAADNSGKTALMMAAENGQAGAVDILVNSAQAD 938
Cdd:PTZ00322   101 LLTGGADP---NCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCH 174
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 34-119 7.76e-08

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.45  E-value: 7.76e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785   34 LVQAIFSGDPEEIRMLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQ 113
Cdd:PTZ00322    86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165


                   ....*.
gi 2131006785  114 VLIKHS 119
Cdd:PTZ00322   166 LLSRHS 171
Ank_4 pfam13637
Ankyrin repeats (many copies);
879-932 1.01e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.58  E-value: 1.01e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2131006785  879 GRTPLHAAAFADHVECLQLLLRHSAEVNAADNSGKTALMMAAENGQAGAVDILV 932
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
228-273 1.01e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.58  E-value: 1.01e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2131006785  228 GYTPLHAAASNGQINVVKHLLNLGVEIDEINIYGNTALHLACYNGQ 273
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGN 46
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 33-193 1.70e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 52.90  E-value: 1.70e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785   33 PLVQAIFSGDPEEIRMLIHKTEDVNALDsekRTPLH--VAAFLGDAEIIELLILSGARVNAK---DNmwLTPLHRAVA-- 105
Cdd:PHA02859    24 PLFYYVEKDDIEGVKKWIKFVNDCNDLY---ETPIFscLEKDKVNVEILKFLIENGADVNFKtrdNN--LSALHHYLSfn 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  106 -SRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAevIIPLLSSVNVS----DRGGRTALH-HAALNGHVEMVN 179
Cdd:PHA02859    99 kNVEPEILKILIDSGSSITEEDEDGKNLLHMYMCNFNVRIN--VIKLLIDSGVSflnkDFDNNNILYsYILFHSDKKIFD 176

                          170
                   ....*....|....
gi 2131006785  180 LLLAKGANINAFDK 193
Cdd:PHA02859   177 FLTSLGIDINETNK 190
Ank_4 pfam13637
Ankyrin repeats (many copies);
745-788 1.85e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.81  E-value: 1.85e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2131006785  745 TALHRGIMTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGH 788
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGN 46
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 303-372 1.97e-07

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 55.29  E-value: 1.97e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  303 ASTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYG 372
Cdd:PTZ00322    90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENG 159
Ank_5 pfam13857
Ankyrin repeats (many copies);
214-268 2.32e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.50  E-value: 2.32e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2131006785  214 LINHG-AEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINIYGNTALHLA 268
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
64-116 3.49e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.04  E-value: 3.49e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2131006785   64 RTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLI 116
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 91-220 3.80e-07

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.13  E-value: 3.80e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785   91 AKDNMWLTPLHRAVasrSEEAVQVLIKHSADVNArdknwqtpLHVAAANKAVKcAEVIIPLLSSVNVSDRGGRTALHHAA 170
Cdd:PTZ00322    56 ATENKDATPDHNLT---TEEVIDPVVAHMLTVEL--------CQLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIAC 123

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2131006785  171 LNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAE 220
Cdd:PTZ00322   124 ANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQC 173
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 712-1015 5.51e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.43  E-value: 5.51e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  712 TPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALHRGIMTGHEECVQMLLEQEV--SILckdsrgrtPLHYAAARGHA 789
Cdd:PHA02874    37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVdtSIL--------PIPCIEKDMIK 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  790 TWLSellqmalSEEDCSFKDNQGYTPLHWACYNGNENCIEVLLEQKcfrtfignpftplhcaiindhencaslllgaids 869
Cdd:PHA02874   109 TILD-------CGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYG---------------------------------- 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  870 SIVNCRDDKGRTPLHAAAFADHVECLQLLLRHSAEVNAADNSGKTALMMAAENGQAGAVDILVNSAqADLTVKDKDLNTS 949
Cdd:PHA02874   148 ADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHG-NHIMNKCKNGFTP 226

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2131006785  950 LHLASSKGHEKCALLIldkiqDESLINARNNALQTPLHVAARNGLKV-VVEELLAKGACVLAIDENG 1015
Cdd:PHA02874   227 LHNAIIHNRSAIELLI-----NNASINDQDIDGSTPLHHAINPPCDIdIIDILLYHKADISIKDNKG 288
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 814-1004 6.23e-07

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: 53.48  E-value: 6.23e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  814 TPLHWACYNGNENCIEVLLeqKCFRTfigNPF-------TPLHCAIINDHENCASLLLGAiDSSIVN--CRDD--KGRTP 882
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLL--KCPSC---DLFqrgalgeTALHVAALYDNLEAAVVLMEA-APELVNepMTSDlyQGETA 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  883 LHAAAFADHVECLQLLLRHSAEVNAADNS--------------GKTALMMAAENGQAGAVDILVNSAqADLTVKDKDLNT 948
Cdd:cd22192     93 LHIAVVNQNLNLVRELIARGADVVSPRATgtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHG-ADIRAQDSLGNT 171

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2131006785  949 SLHLASSKGHEKCA------LLILDKIQDE-SLINARNNALQTPLHVAARNGLKVVVEELLAK 1004
Cdd:cd22192    172 VLHILVLQPNKTFAcqmydlILSYDKEDDLqPLDLVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 576-835 6.55e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 53.35  E-value: 6.55e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  576 IHYAAAYGHRQCLELLLERTNNGFEESDSGATksPLHLAAYNGHHQALEVLLQSLVDLDIRDEKgrTALDLAAFKGHTEC 655
Cdd:PHA02878    41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLT--PLHIICKEPNKLGMKEMIRSINKCSVFYTL--VAIKDAFNNRNVEI 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  656 VEA-LINQGASIFVKDNVTKRTPLHASVINghTLCLRLLLEI-ADnpeaIDVKDA-KGQTPLMLAVAYGHIDAVSLLLEK 732
Cdd:PHA02878   117 FKIiLTNRYKNIQTIDLVYIDKKSKDDIIE--AEITKLLLSYgAD----INMKDRhKGNTALHYATENKDQRLTELLLSY 190

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  733 EANVDAVDIMGCTALHRGIMTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGHATwlsELLQMALSEEDCSFKDN-- 810
Cdd:PHA02878   191 GANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDY---DILKLLLEHGVDVNAKSyi 267

                          250       260
                   ....*....|....*....|....*
gi 2131006785  811 QGYTPLHWACYngNENCIEVLLEQK 835
Cdd:PHA02878   268 LGLTALHSSIK--SERKLKLLLEYG 290
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 876-1008 6.77e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 53.72  E-value: 6.77e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  876 DDKGRTPLHAAAFADHVECLQLLLRHSAEVNAADNSGKTALMMAAENGQAGAVDILVNSAQADLTVKDKDLntsLHLASS 955
Cdd:PLN03192   555 DSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAGDL---LCTAAK 631

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2131006785  956 KGHekcaLLILDKIQDESL-INARNNALQTPLHVAARNGLKVVVEELLAKGACV 1008
Cdd:PLN03192   632 RND----LTAMKELLKQGLnVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
Ank_4 pfam13637
Ankyrin repeats (many copies);
846-899 8.87e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.88  E-value: 8.87e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2131006785  846 TPLHCAIINDHENCASLLLGAidSSIVNCRDDKGRTPLHAAAFADHVECLQLLL 899
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEK--GADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 44-182 8.92e-07

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.98  E-value: 8.92e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785   44 EEIRMLIHKTEDVNALDSEKRTPLHVAAflgDAEIIELLILsgarvnakdNMWLTPLHRAVASRSEEAVQVLIKHSADVN 123
Cdd:PTZ00322    42 EEIARIDTHLEALEATENKDATPDHNLT---TEEVIDPVVA---------HMLTVELCQLAASGDAVGARILLTGGADPN 109

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2131006785  124 ARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHVEMVNLLL 182
Cdd:PTZ00322   110 CRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 347-515 9.04e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 53.33  E-value: 9.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  347 LIQNGGEIDCVDKDGNtpLHVAARYGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSGQKYSIVSLF 426
Cdd:PLN03192   513 LGDNGGEHDDPNMASN--LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDAN 590

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  427 SNE---HVLSAG----FEI-------DTPDKFGrTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFH 492
Cdd:PLN03192   591 GNTalwNAISAKhhkiFRIlyhfasiSDPHAAG-DLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVD 669

                          170       180
                   ....*....|....*....|....*.
gi 2131006785  493 CIETLVTTGANV---NETDDWGRTAL 515
Cdd:PLN03192   670 MVRLLIMNGADVdkaNTDDDFSPTEL 695
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 211-283 1.07e-06

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.98  E-value: 1.07e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2131006785  211 VALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINIYGNTALHLACYNGQDAVVNELTDY 283
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
Ank_4 pfam13637
Ankyrin repeats (many copies);
32-83 2.19e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.73  E-value: 2.19e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2131006785   32 PPLVQAIFSGDPEEIRMLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLI 83
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 231-390 2.24e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 49.82  E-value: 2.24e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  231 PLHAAASNGQINVVKHLLNLgveIDEINIYGNTALHlACYNGQDAVVNE---LTDYGANVN-QPNNSGFTPLHFAAASTH 306
Cdd:PHA02859    24 PLFYYVEKDDIEGVKKWIKF---VNDCNDLYETPIF-SCLEKDKVNVEIlkfLIENGADVNfKTRDNNLSALHHYLSFNK 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  307 GAL--CLELLVNNGADVNIQSKDGKSPLH--MTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLI-NTLI 381
Cdd:PHA02859   100 NVEpeILKILIDSGSSITEEDEDGKNLLHmyMCNFNVRINVIKLLIDSGVSFLNKDFDNNNILYSYILFHSDKKIfDFLT 179


                   ....*....
gi 2131006785  382 TSGADTAKC 390
Cdd:PHA02859   180 SLGIDINET 188
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 311-515 2.35e-06

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 51.84  E-value: 2.35e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  311 LELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRS--QTLIQNGGEIDCVDKDGNTPLH---VAARYGHELLINTLITSGA 385
Cdd:PHA02716   195 LEWLCNNGVNVNLQNNHLITPLHTYLITGNVCASviKKIIELGGDMDMKCVNGMSPIMtyiINIDNINPEITNIYIESLD 274

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  386 DTAKCGIHSMFPLHLAalnahsdccrklLSSGQKYSIVslfsnEHVLSAGFEIDTPDKFGRTCLHAAAAGGNV--ECIKL 463
Cdd:PHA02716   275 GNKVKNIPMILHSYIT------------LARNIDISVV-----YSFLQPGVKLHYKDSAGRTCLHQYILRHNIstDIIKL 337

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2131006785  464 LQSSGADFHKKDKCGRTPLH-YAAANCHFH-------------CIETLVTTGANVNETDDWGRTAL 515
Cdd:PHA02716   338 LHEYGNDLNEPDNIGNTVLHtYLSMLSVVNildpetdndirldVIQCLISLGADITAVNCLGYTPL 403
Ank_4 pfam13637
Ankyrin repeats (many copies);
776-832 3.18e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.34  E-value: 3.18e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2131006785  776 GRTPLHYAAARGHatwlSELLQMAL-SEEDCSFKDNQGYTPLHWACYNGNENCIEVLL 832
Cdd:pfam13637    1 ELTALHAAAASGH----LELLRLLLeKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 920-1037 3.29e-06

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.44  E-value: 3.29e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  920 AENGQAGAVDILVNSAqADLTVKDKDLNTSLHLASSKGHEKCALLILDKIQDESLINARNNalqTPLHVAARNGLKVVVE 999
Cdd:PTZ00322    90 AASGDAVGARILLTGG-ADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGK---TPLELAEENGFREVVQ 165

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2131006785 1000 ELLAKGACVLAIDENGIG---TSSPCLFLRShtPALACAPN 1037
Cdd:PTZ00322   166 LLSRHSQCHFELGANAKPdsfTGKPPSLEDS--PISSHHPD 204
Ank_4 pfam13637
Ankyrin repeats (many copies);
261-315 3.37e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.34  E-value: 3.37e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2131006785  261 GNTALHLACYNGQDAVVNELTDYGANVNQPNNSGFTPLHFAAASTHGAlCLELLV 315
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVE-VLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 162-190 3.39e-06

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: 44.50  E-value: 3.39e-06
                            10        20
                    ....*....|....*....|....*....
gi 2131006785   162 GRTALHHAALNGHVEMVNLLLAKGANINA 190
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 429-550 3.49e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 51.41  E-value: 3.49e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  429 EHVLSAGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPL-------HYAAANCHFHC-------- 493
Cdd:PLN03192   542 EELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnaisakHHKIFRILYHFasisdpha 621

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  494 ----------------IETLVTTGANVNETDDWGRTALHYAAASD---------MDRNKTILGNAHENSEELERARELKE 548
Cdd:PLN03192   622 agdllctaakrndltaMKELLKQGLNVDSEDHQGATALQVAMAEDhvdmvrlliMNGADVDKANTDDDFSPTELRELLQK 701


                   ..
gi 2131006785  549 KE 550
Cdd:PLN03192   702 RE 703
Ank_4 pfam13637
Ankyrin repeats (many copies);
330-381 3.98e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.96  E-value: 3.98e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2131006785  330 SPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLI 381
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02946 PHA02946
ankyin-like protein; Provisional
 42-232 4.49e-06

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 50.44  E-value: 4.49e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785   42 DPEEIRMLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSE--EAVQVLIKHS 119
Cdd:PHA02946    51 DERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEviERINLLVQYG 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  120 ADV-NARDKNWQTPLhVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAAL--NGHVEMVNLLLAKGANINAFDKKDR 196
Cdd:PHA02946   131 AKInNSVDEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMsdNPKASTISWMMKLGISPSKPDHDGN 209

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 2131006785  197 RALH--WAAYMGHLDVVALLINhGAEVTCKDKKGYTPL 232
Cdd:PHA02946   210 TPLHivCSKTVKNVDIINLLLP-STDVNKQNKFGDSPL 246
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 453-522 4.71e-06

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.67  E-value: 4.71e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  453 AAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVNETDDWGRTALHYAAASD 522
Cdd:PTZ00322    90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENG 159
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 609-853 5.30e-06

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 50.46  E-value: 5.30e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  609 SPLHLAAYNGHHQALEVLLQSLvdlDIRDEKGRTALdLAAFKGHTECVEALIN--------QGASIFVKDNVTKR----- 675
Cdd:TIGR00870   54 SALFVAAIENENLELTELLLNL---SCRGAVGDTLL-HAISLEYVDAVEAILLhllaafrkSGPLELANDQYTSEftpgi 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  676 TPLHASVINGHTLCLRLLLEI-ADNPEAIDVKDAK----------GQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGC 744
Cdd:TIGR00870  130 TALHLAAHRQNYEIVKLLLERgASVPARACGDFFVksqgvdsfyhGESPLNAAACLGSPSIVALLSEDPADILTADSLGN 209

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  745 TALHRGIMtgheECVQMLLEQEVSILCKDsrgrtplhYAaarghatwLSELLQMALSEEDCSFKDNQGYTPLHWACYNGN 824
Cdd:TIGR00870  210 TLLHLLVM----ENEFKAEYEELSCQMYN--------FA--------LSLLDKLRDSKELEVILNHQGLTPLKLAAKEGR 269

                          250       260       270
                   ....*....|....*....|....*....|
gi 2131006785  825 ENCIEVLLEQKCF-RTFIGNPFTPLHCAII 853
Cdd:TIGR00870  270 IVLFRLKLAIKYKqKKFVAWPNGQQLLSLY 299
Ank_5 pfam13857
Ankyrin repeats (many copies);
180-235 5.46e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.64  E-value: 5.46e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2131006785  180 LLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAA 235
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 547-733 5.85e-06

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 50.40  E-value: 5.85e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  547 KEKEAALCLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLE---RTNNGFEESDSGATKSPLHLAAYNGHHQAL 623
Cdd:cd22192     26 KENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEaapELVNEPMTSDLYQGETALHIAVVNQNLNLV 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  624 EVLLQSLVDLD--------IRDEK------GRTALDLAAFKGHTECVEALINQGASIFVKDNVTKrTPLHASVINGHTL- 688
Cdd:cd22192    106 RELIARGADVVspratgtfFRPGPknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGN-TVLHILVLQPNKTf 184

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2131006785  689 -C----LRLLLEIADNPEAID-VKDAKGQTPLMLAVAYGHIDAVSLLLEKE 733
Cdd:cd22192    185 aCqmydLILSYDKEDDLQPLDlVPNNQGLTPFKLAAKEGNIVMFQHLVQKR 235
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 162-193 7.45e-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: 7.45e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2131006785  162 GRTALHHAAL-NGHVEMVNLLLAKGANINAFDK 193
Cdd:pfam00023    2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
Ank_4 pfam13637
Ankyrin repeats (many copies);
397-464 7.46e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.19  E-value: 7.46e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2131006785  397 PLHLAALNAHSDCCRKLLSSGqkysivslfsnehvlsagFEIDTPDKFGRTCLHAAAAGGNVECIKLL 464
Cdd:pfam13637    4 ALHAAAASGHLELLRLLLEKG------------------ADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank_4 pfam13637
Ankyrin repeats (many copies);
572-627 8.64e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.19  E-value: 8.64e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2131006785  572 GYNSIHYAAAYGHRQCLELLLERTNNGFEESDSGATksPLHLAAYNGHHQALEVLL 627
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGET--ALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
640-694 9.08e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.80  E-value: 9.08e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2131006785  640 GRTALDLAAFKGHTECVEALINQGASIFVKDNvTKRTPLHASVINGHTLCLRLLL 694
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDG-NGETALHFAASNGNVEVLKLLL 54
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 583-822 1.03e-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: 1.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  583 GHRQCLELLLerTNNGFEESDSGatKSPLHLAAYNGHHQALE---VLLQS---------LVDLDIRDE--KGRTALDLAA 648
Cdd:cd21882      6 GLLECLRWYL--TDSAYQRGATG--KTCLHKAALNLNDGVNEaimLLLEAapdsgnpkeLVNAPCTDEfyQGQTALHIAI 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  649 FKGHTECVEALINQGASIFVKDNVT--KRTPLHASVINGHTLCL----------RLLLEIADNPEAIDVKDAKGQTPLml 716
Cdd:cd21882     82 ENRNLNLVRLLVENGADVSARATGRffRKSPGNLFYFGELPLSLaactnqeeivRLLLENGAQPAALEAQDSLGNTVL-- 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  717 avaygHIdavsLLLEKEANVDAVDIMgcTALHRGIMTGHEECVQMLLEQEVSilckDSRGRTPLHYAAARGHATWLSELL 796
Cdd:cd21882    160 -----HA----LVLQADNTPENSAFV--CQMYNLLLSYGAHLDPTQQLEEIP----NHQGLTPLKLAAVEGKIVMFQHIL 224

                          250       260
                   ....*....|....*....|....*....
gi 2131006785  797 QMALSE--EDCSFKDNQ-GYTPLHWACYN 822
Cdd:cd21882    225 QREFSGpyQPLSRKFTEwTYGPVTSSLYD 253
PHA02791 PHA02791
ankyrin-like protein; Provisional
 790-985 1.06e-05

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 48.50  E-value: 1.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  790 TWLSELLQMALSEEDCSFKDNQGYTPLHWACYNGNENCIEVLLEQKCFRTFIGNPFtPLH-CAIINDHENCASLLLGAID 868
Cdd:PHA02791     8 TWKSKQLKSFLSSKDAFKADVHGHSALYYAIADNNVRLVCTLLNAGALKNLLENEF-PLHqAATLEDTKIVKILLFSGMD 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  869 SSIVncrDDKGRTPLHAAAFADHVECLQLLLRHSAEVNAADNSG-KTALMMAAENGQAGAVDILVNSAQA--DLTVkdkd 945
Cdd:PHA02791    87 DSQF---DDKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTGwKTSFYHAVMLNDVSIVSYFLSEIPStfDLAI---- 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 2131006785  946 LNTSLHLASSKGHEKCALLILDKIQDeslINARNNALQTP 985
Cdd:PHA02791   160 LLSCIHITIKNGHVDMMILLLDYMTS---TNTNNSLLFIP 196
Ank_4 pfam13637
Ankyrin repeats (many copies);
675-730 2.03e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.03  E-value: 2.03e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2131006785  675 RTPLHASVINGHTLCLRLLLEiadNPEAIDVKDAKGQTPLMLAVAYGHIDAVSLLL 730
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLE---KGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 162-190 2.06e-05

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 42.24  E-value: 2.06e-05
                           10        20
                   ....*....|....*....|....*....
gi 2131006785  162 GRTALHHAALNGHVEMVNLLLAKGANINA 190
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02798 PHA02798
ankyrin-like protein; Provisional
 653-922 2.33e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 48.29  E-value: 2.33e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  653 TECVEALINQGASIFVKDNvTKRTPLHA--SVINGHTLCLRLLLEIADNPEAIDVKDAKGQTPLMLAVAYGHIDA---VS 727
Cdd:PHA02798    51 TDIVKLFINLGANVNGLDN-EYSTPLCTilSNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNleiLL 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  728 LLLEKEANVDAVDIMGCTALHRGIMTGHE---ECVQMLLEQEVSIlckdsrgrtplhyaaaRGHATWlsellqmalseed 804
Cdd:PHA02798   130 FMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDI----------------NTHNNK------------- 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  805 csfkdnQGYTPLHwaCY-NGNENCIEV-LLEQKCFRTFIGNPFTPLH--------CAIINDHENCASLLLGAIDSSI-VN 873
Cdd:PHA02798   181 ------EKYDTLH--CYfKYNIDRIDAdILKLFVDNGFIINKENKSHkkkfmeylNSLLYDNKRFKKNILDFIFSYIdIN 252

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 2131006785  874 CRDDKGRTPLHAAAFADHVECLQLLLRHSAEVNAADNSGKTALMMAAEN 922
Cdd:PHA02798   253 QVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFEN 301
Ank_5 pfam13857
Ankyrin repeats (many copies);
115-169 2.52e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.72  E-value: 2.52e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2131006785  115 LIKH-SADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHA 169
Cdd:pfam13857    1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
154-202 2.68e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.72  E-value: 2.68e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2131006785  154 SVNVSDRGGRTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWA 202
Cdd:pfam13857    8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 829-1004 2.74e-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: 48.34  E-value: 2.74e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  829 EVLLEQKCFRTFIGNPF--------TPLHCAIINDHEN---CASLLLGAIDSS-----IVN--CRDD--KGRTPLHAAAF 888
Cdd:cd21882      3 ELLGLLECLRWYLTDSAyqrgatgkTCLHKAALNLNDGvneAIMLLLEAAPDSgnpkeLVNapCTDEfyQGQTALHIAIE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  889 ADHVECLQLLLRHSAEVNAADNS-------------GKTALMMAAENGQAGAVDILV-NSAQ-ADLTVKDKDLNTSLH-- 951
Cdd:cd21882     83 NRNLNLVRLLVENGADVSARATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLeNGAQpAALEAQDSLGNTVLHal 162

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2131006785  952 -LASSKGHEKCA--------LLILDKIQD--ESLINARNNALQTPLHVAARNGLKVVVEELLAK 1004
Cdd:cd21882    163 vLQADNTPENSAfvcqmynlLLSYGAHLDptQQLEEIPNHQGLTPLKLAAVEGKIVMFQHILQR 226
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 684-763 3.03e-05

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.97  E-value: 3.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  684 NGHTLCLRLLLEIADNPeaiDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALHRGIMTGHEECVQMLL 763
Cdd:PTZ00322    92 SGDAVGARILLTGGADP---NCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
Ank_5 pfam13857
Ankyrin repeats (many copies);
51-103 3.16e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 3.16e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2131006785   51 HKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRA 103
Cdd:pfam13857    4 HGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 878-910 3.61e-05

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 41.51  E-value: 3.61e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2131006785  878 KGRTPLHAAA-FADHVECLQLLLRHSAEVNAADN 910
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 878-993 3.70e-05

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: 47.83  E-value: 3.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  878 KGRTPLHAAAFADHVECLQLLLRHSAEVNAADNS--------------GKTALMMAAENGQAGAVDILVNSAQADLTVKD 943
Cdd:cd22194    140 EGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEIVQLLMEKESTDITSQD 219

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2131006785  944 KDLNTSLHL-----ASSKGHEKCALLILDKI----QDESLINARNNALQTPLHVAARNG 993
Cdd:cd22194    220 SRGNTVLHAlvtvaEDSKTQNDFVKRMYDMIllksENKNLETIRNNEGLTPLQLAAKMG 278
Ank_5 pfam13857
Ankyrin repeats (many copies);
463-518 4.38e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 4.38e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2131006785  463 LLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVNETDDWGRTALHYA 518
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 162-304 4.77e-05

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: 47.49  E-value: 4.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  162 GRTALHHAALN---GHVEMVNLLL---AKGANINAF------DK--KDRRALHWAAYMGHLDVVALLINHGAEVTC---- 223
Cdd:cd22196     47 GKTCLLKAMLNlhnGQNDTISLLLdiaEKTGNLKEFvnaaytDSyyKGQTALHIAIERRNMHLVELLVQNGADVHArasg 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  224 ------KDKKGY----TPLHAAASNGQINVVKHLLN---LGVEIDEINIYGNTALHL---ACYNGQD------AVVNELT 281
Cdd:cd22196    127 effkkkKGGPGFyfgeLPLSLAACTNQLDIVKFLLEnphSPADISARDSMGNTVLHAlveVADNTPEntkfvtKMYNEIL 206

                          170       180       190
                   ....*....|....*....|....*....|
gi 2131006785  282 DYGANVNQ-------PNNSGFTPLHFAAAS 304
Cdd:cd22196    207 ILGAKIRPllkleeiTNKKGLTPLKLAAKT 236
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 691-823 5.81e-05

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: 47.06  E-value: 5.81e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  691 RLLLEIADNPEAIDV--------KDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDA---------VDIMGC-----TALH 748
Cdd:cd22194    114 RILLAFAEENGILDRfinaeyteEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAhakgvffnpKYKHEGfyfgeTPLA 193

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  749 RGIMTGHEECVQMLLEQE-VSILCKDSRGRTPLHYAA-----ARGHATWLSELLQMAL----SEEDCSFKDNQGYTPLHW 818
Cdd:cd22194    194 LAACTNQPEIVQLLMEKEsTDITSQDSRGNTVLHALVtvaedSKTQNDFVKRMYDMILlkseNKNLETIRNNEGLTPLQL 273


                   ....*
gi 2131006785  819 ACYNG 823
Cdd:cd22194    274 AAKMG 278
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 360-520 6.73e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 46.52  E-value: 6.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  360 DGNTPLHVAARYGHELLINTLITSGA--DTAKCGIHSmfPLHLAALNAHSDCCRKLLSSGQkysivslfsnehvlsagFE 437
Cdd:PHA02875    34 DGISPIKLAMKFRDSEAIKLLMKHGAipDVKYPDIES--ELHDAVEEGDVKAVEELLDLGK-----------------FA 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  438 IDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVNETDDWGRTALHY 517
Cdd:PHA02875    95 DDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLII 174


                   ...
gi 2131006785  518 AAA 520
Cdd:PHA02875   175 AMA 177
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 162-302 6.77e-05

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: 47.06  E-value: 6.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  162 GRTALHHAALNGHVEMVNLLLAKGANINA------FDKKDRR--------ALHWAAYMGHLDVVALLINHGAE-VTCKDK 226
Cdd:cd22194    141 GQTALNIAIERRQGDIVKLLIAKGADVNAhakgvfFNPKYKHegfyfgetPLALAACTNQPEIVQLLMEKESTdITSQDS 220

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  227 KGYTPLHAAA-----SNGQINVVKHLLnlgveiDEIniygntalHLACYNgqdavvneltdygANVNQ-PNNSGFTPLHF 300
Cdd:cd22194    221 RGNTVLHALVtvaedSKTQNDFVKRMY------DMI--------LLKSEN-------------KNLETiRNNEGLTPLQL 273


                   ..
gi 2131006785  301 AA 302
Cdd:cd22194    274 AA 275
Ank_5 pfam13857
Ankyrin repeats (many copies);
280-334 7.89e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.56  E-value: 7.89e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2131006785  280 LTDYGANVNQPNNSGFTPLHFAAasTHGAL-CLELLVNNGADVNIQSKDGKSPLHM 334
Cdd:pfam13857    2 LEHGPIDLNRLDGEGYTPLHVAA--KYGALeIVRVLLAYGVDLNLKDEEGLTALDL 55
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 646-730 8.07e-05

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.82  E-value: 8.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  646 LAAfKGHTECVEALINQGASIFVKDnVTKRTPLHASVINGHTLCLRLLLEIADNPEAIDvKDakGQTPLMLAVAYGHIDA 725
Cdd:PTZ00322    89 LAA-SGDAVGARILLTGGADPNCRD-YDGRTPLHIACANGHVQVVRVLLEFGADPTLLD-KD--GKTPLELAEENGFREV 163


                   ....*
gi 2131006785  726 VSLLL 730
Cdd:PTZ00322   164 VQLLS 168
Ank_5 pfam13857
Ankyrin repeats (many copies);
696-748 8.54e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.18  E-value: 8.54e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2131006785  696 IADNPEAIDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALH 748
Cdd:pfam13857    2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 332-421 9.41e-05

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.43  E-value: 9.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  332 LHMTAVH-------GRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGADTAKCGIHSMFPLHLAALN 404
Cdd:PTZ00322    79 AHMLTVElcqlaasGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEEN 158

                           90
                   ....*....|....*..
gi 2131006785  405 AHSDCCRKLLSSGQKYS 421
Cdd:PTZ00322   159 GFREVVQLLSRHSQCHF 175
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 233-336 1.14e-04

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.43  E-value: 1.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  233 HAAASNGQINVvKHLLNLGVEIDEINIYGNTALHLACYNGQDAVVNELTDYGANVNQPNNSGFTPLHFAAASTHGALcLE 312
Cdd:PTZ00322    88 QLAASGDAVGA-RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREV-VQ 165

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2131006785  313 LLV-------NNGADVNIQSKDGK------SPLHMTA 336
Cdd:PTZ00322   166 LLSrhsqchfELGANAKPDSFTGKppsledSPISSHH 202
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 183-369 1.26e-04

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 46.23  E-value: 1.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  183 AKGANINAFDKKDRRALHWAAYMG-HLDVVALLINHGAEVtckdKKGYTPLHAAaSNGQINVVKHLLNLGVEIDEiniyG 261
Cdd:TIGR00870   40 PKKLNINCPDRLGRSALFVAAIENeNLELTELLLNLSCRG----AVGDTLLHAI-SLEYVDAVEAILLHLLAAFR----K 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  262 NTALHLAcyNGQDavvneLTDYGAnvnqpnnsGFTPLHFAAaSTHGALCLELLVNNGADVNIQSKDG---KSPLHMTAVH 338
Cdd:TIGR00870  111 SGPLELA--NDQY-----TSEFTP--------GITALHLAA-HRQNYEIVKLLLERGASVPARACGDffvKSQGVDSFYH 174

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 2131006785  339 GRFTRS-----------QTLIQNGGEIDCVDKDGNTPLHVAA 369
Cdd:TIGR00870  175 GESPLNaaaclgspsivALLSEDPADILTADSLGNTLLHLLV 216
Ank_4 pfam13637
Ankyrin repeats (many copies);
361-414 1.31e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.72  E-value: 1.31e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2131006785  361 GNTPLHVAARYGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLL 414
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02946 PHA02946
ankyin-like protein; Provisional
 178-464 1.44e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 45.82  E-value: 1.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  178 VNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLH-AAASNGQInvvkhllnlgveIDE 256
Cdd:PHA02946    55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYyLSGTDDEV------------IER 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  257 INIygntalhlacyngqdavvneLTDYGANVNQP-NNSGFTPLhfAAASTHGALCLELLVNNGADVNIQSKDGKSPLH-- 333
Cdd:PHA02946   123 INL--------------------LVQYGAKINNSvDEEGCGPL--LACTDPSERVFKKIMSIGFEARIVDKFGKNHIHrh 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  334 MTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLH-VAARYGHELLINTLITSGADTAKCGIHSMFPLHLAALN-AHSDCCR 411
Cdd:PHA02946   181 LMSDNPKASTISWMMKLGISPSKPDHDGNTPLHiVCSKTVKNVDIINLLLPSTDVNKQNKFGDSPLTLLIKTlSPAHLIN 260

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  412 KLLSSG-----QKYSIVSLFSNEHVLsagfEI--DTPDKFGRTCLHAAAAGGNVECIKLL 464
Cdd:PHA02946   261 KLLSTSnvitdQTVNICIFYDRDDVL----EIinDKGKQYDSTDFKMAVEVGSIRCVKYL 316
Ank_5 pfam13857
Ankyrin repeats (many copies);
866-919 1.56e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.41  E-value: 1.56e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2131006785  866 AIDSSIVNCRDDKGRTPLHAAAFADHVECLQLLLRHSAEVNAADNSGKTALMMA 919
Cdd:pfam13857    3 EHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 227-256 1.84e-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: 1.84e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 2131006785   227 KGYTPLHAAASNGQINVVKHLLNLGVEIDE 256
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
554-592 1.85e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.34  E-value: 1.85e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2131006785  554 CLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLL 592
Cdd:pfam13637   16 LLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
897-953 1.89e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.41  E-value: 1.89e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2131006785  897 LLLRHSAEVNAADNSGKTALMMAAENGQAGAVDILVNsAQADLTVKDKDLNTSLHLA 953
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLA-YGVDLNLKDEEGLTALDLA 56
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 398-516 2.01e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 45.26  E-value: 2.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  398 LHLAALNAHS---DCCRKLLSSGQKYSIVSLFSNEHVLSAGFEidtpdkfGRTCLHAAAAGGNVECIKLLQSSGADFH-- 472
Cdd:cd21882     30 LHKAALNLNDgvnEAIMLLLEAAPDSGNPKELVNAPCTDEFYQ-------GQTALHIAIENRNLNLVRLLVENGADVSar 102

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2131006785  473 ------KKDKC-----GRTPLHYAAANCHFHCIETLVTTG---ANVNETDDWGRTALH 516
Cdd:cd21882    103 atgrffRKSPGnlfyfGELPLSLAACTNQEEIVRLLLENGaqpAALEAQDSLGNTVLH 160
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 294-326 2.04e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.58  E-value: 2.04e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2131006785  294 GFTPLHFAAASTHGALCLELLVNNGADVNIQSK 326
Cdd:pfam00023    2 GNTPLHLAAGRRGNLEIVKLLLSKGADVNARDK 34
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 709-740 2.43e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.19  E-value: 2.43e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2131006785  709 KGQTPLMLAVA-YGHIDAVSLLLEKEANVDAVD 740
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 260-288 3.03e-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: 3.03e-04
                            10        20
                    ....*....|....*....|....*....
gi 2131006785   260 YGNTALHLACYNGQDAVVNELTDYGANVN 288
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank_5 pfam13857
Ankyrin repeats (many copies);
609-647 3.55e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.64  E-value: 3.55e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2131006785  609 SPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLA 647
Cdd:pfam13857   18 TPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
258-301 4.20e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 4.20e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2131006785  258 NIYGNTALHLACYNGQDAVVNELTDYGANVNQPNNSGFTPLHFA 301
Cdd:pfam13857   13 DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 445-594 4.80e-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: 44.08  E-value: 4.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  445 GRTCLHAAAAGGNVECIKLLQSSGADFH----------KKDKC---GRTPLHYAAANCHFHCIETLVTTG---ANVNETD 508
Cdd:cd22197     94 GHSALHIAIEKRSLQCVKLLVENGADVHaracgrffqkKQGTCfyfGELPLSLAACTKQWDVVNYLLENPhqpASLQAQD 173

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  509 DWGRTALHYAAasdmdrnkTILGNAHENSEELERA-RELKEKEAALCLEFLLQndanpSIRDKEGYNSIHYAAAYGHRQC 587
Cdd:cd22197    174 SLGNTVLHALV--------MIADNSPENSALVIKMyDGLLQAGARLCPTVQLE-----EISNHEGLTPLKLAAKEGKIEI 240


                   ....*..
gi 2131006785  588 LELLLER 594
Cdd:cd22197    241 FRHILQR 247
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 478-509 4.88e-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: 4.88e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2131006785  478 GRTPLHYAAANC-HFHCIETLVTTGANVNETDD 509
Cdd:pfam00023    2 GNTPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 258-335 5.37e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 43.43  E-value: 5.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  258 NIYGNTALHLACYNGQDAVVNeLTDYGANVNQ-PNNSGFTPLHFAAasTHGAL-CLELLVNNGADVNIQSKDGKSPLHMT 335
Cdd:PHA02884    68 NSKTNPLIYAIDCDNDDAAKL-LIRYGADVNRyAEEAKITPLYISV--LHGCLkCLEILLSYGADINIQTNDMVTPIELA 144
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 878-907 5.47e-04

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.34  E-value: 5.47e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 2131006785   878 KGRTPLHAAAFADHVECLQLLLRHSAEVNA 907
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
296-348 5.64e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.79  E-value: 5.64e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2131006785  296 TPLHFAAASTHGAlCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLI 348
Cdd:pfam13637    3 TALHAAAASGHLE-LLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 914-1008 5.90e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 43.85  E-value: 5.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  914 TALMMAAENGQAGAVDILVNSAQADLTVKDKDLNTSLHLASSKGHEKCALLILDkiQDESLIN-ARNNAL---QTPLHVA 989
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNePMTSDLyqgETALHIA 96

                           90
                   ....*....|....*....
gi 2131006785  990 ARNGLKVVVEELLAKGACV 1008
Cdd:cd22192     97 VVNQNLNLVRELIARGADV 115
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 478-506 5.92e-04

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.34  E-value: 5.92e-04
                            10        20
                    ....*....|....*....|....*....
gi 2131006785   478 GRTPLHYAAANCHFHCIETLVTTGANVNE 506
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 77-249 6.05e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 43.98  E-value: 6.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785   77 EIIELLI-----------LSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKN-WQTPLHvaaankavkc 144
Cdd:cd22194    111 EIVRILLafaeengildrFINAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGvFFNPKY---------- 180

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  145 aeviipllssvnvSDRG---GRTALHHAALNGHVEMVNLLLAKGANINAF-DKKDRRALHwAAYM------GHLDVV--- 211
Cdd:cd22194    181 -------------KHEGfyfGETPLALAACTNQPEIVQLLMEKESTDITSqDSRGNTVLH-ALVTvaedskTQNDFVkrm 246

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 2131006785  212 --ALLINHGAEV--TCKDKKGYTPLHAAASNGQINVVKHLLN 249
Cdd:cd22194    247 ydMILLKSENKNleTIRNNEGLTPLQLAAKMGKAEILKYILS 288
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 235-372 6.42e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 43.98  E-value: 6.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  235 AASNGqinVVKHLLNlgVEIDEINIYGNTALHLACYNGQDAVVNELTDYGANVN--------QP--NNSGF----TPLHF 300
Cdd:cd22194    120 AEENG---ILDRFIN--AEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNahakgvffNPkyKHEGFyfgeTPLAL 194

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  301 AAASTHGALcLELLVNNGADvNIQSKD--GKSPLHMTAVHGRFTRSQT-----------LIQNGGEIDCV-DKDGNTPLH 366
Cdd:cd22194    195 AACTNQPEI-VQLLMEKEST-DITSQDsrGNTVLHALVTVAEDSKTQNdfvkrmydmilLKSENKNLETIrNNEGLTPLQ 272


                   ....*.
gi 2131006785  367 VAARYG 372
Cdd:cd22194    273 LAAKMG 278
Ank_5 pfam13857
Ankyrin repeats (many copies);
728-783 6.48e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.87  E-value: 6.48e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2131006785  728 LLLEKEANVDAVDIMGCTALHRGIMTGHEECVQMLLEQEVSILCKDSRGRTPLHYA 783
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 784-913 6.68e-04

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.73  E-value: 6.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  784 AARGHATWLSELLQmalSEEDCSFKDNQGYTPLHWACYNGNENCIEVLLEqkcfrtfignpftplhcaiindhencasll 863
Cdd:PTZ00322    90 AASGDAVGARILLT---GGADPNCRDYDGRTPLHIACANGHVQVVRVLLE------------------------------ 136

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2131006785  864 LGAiDSSIVncrDDKGRTPLHAAAFADHVECLQLLLRHSAEVNAADNSGK 913
Cdd:PTZ00322   137 FGA-DPTLL---DKDGKTPLELAEENGFREVVQLLSRHSQCHFELGANAK 182
Ank_5 pfam13857
Ankyrin repeats (many copies);
437-485 6.94e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.87  E-value: 6.94e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2131006785  437 EIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYA 485
Cdd:pfam13857    8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 715-807 7.73e-04

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.73  E-value: 7.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  715 MLAVAYGHIDA------VSLLLEKEANVDAVDIMGCTALHRGIMTGHEECVQMLLE--QEVSILCKDsrGRTPLHYAAAR 786
Cdd:PTZ00322    81 MLTVELCQLAAsgdavgARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEfgADPTLLDKD--GKTPLELAEEN 158

                           90       100
                   ....*....|....*....|.
gi 2131006785  787 GhatwLSELLQMALSEEDCSF 807
Cdd:PTZ00322   159 G----FREVVQLLSRHSQCHF 175
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 260-292 7.83e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.04  E-value: 7.83e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2131006785  260 YGNTALHLACY-NGQDAVVNELTDYGANVNQPNN 292
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 884-978 7.99e-04

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.35  E-value: 7.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  884 HAAAFADHVEcLQLLLRHSAEVNAADNSGKTALMMAAENGQAGAVDILVNSAqADLTVKDKDLNTSLHLASSKGHEKCAL 963
Cdd:PTZ00322    88 QLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFG-ADPTLLDKDGKTPLELAEENGFREVVQ 165

                           90
                   ....*....|....*
gi 2131006785  964 LILDKIQDESLINAR 978
Cdd:PTZ00322   166 LLSRHSQCHFELGAN 180
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 851-1047 8.47e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 43.06  E-value: 8.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  851 AIINDHENCASLLLgaiDSSI-VNCRDDKGRTPLHAAAFADHVECLQLLLRHSAEVNAADNSGKTALMMAAENGQAGAVD 929
Cdd:PHA02875     9 AILFGELDIARRLL---DIGInPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVE 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  930 ILVNSAQADLTVKDKDLNTSLHLASSKGHEKCALLILDKIQDESLINARNNalqTPLHVAARNGLKVVVEELLAKGACVL 1009
Cdd:PHA02875    86 ELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKF---SPLHLAVMMGDIKGIELLIDHKACLD 162

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 2131006785 1010 AidENGIGtsspclflrsHTPALACAPNKDVADCLALI 1047
Cdd:PHA02875   163 I--EDCCG----------CTPLIIAMAKGDIAICKMLL 188
Ank_5 pfam13857
Ankyrin repeats (many copies);
87-136 8.97e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.48  E-value: 8.97e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2131006785   87 ARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVA 136
Cdd:pfam13857    7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 227-256 9.49e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.62  E-value: 9.49e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 2131006785  227 KGYTPLHAAASNGQINVVKHLLNLGVEIDE 256
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 62-248 9.92e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 43.33  E-value: 9.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785   62 EKRTPLHVAAFLGDAEIIELLILSGARVNAKDN-------------MWLTPLHRAVASRSEEAVQVLIKHSAD---VNAR 125
Cdd:cd21882     72 QGQTALHIAIENRNLNLVRLLVENGADVSARATgrffrkspgnlfyFGELPLSLAACTNQEEIVRLLLENGAQpaaLEAQ 151

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  126 DKNWQTPLH--VAAANKAVKCAEVIIpllssvnvsdrggrtalhhaalnghvEMVNLLLAKGANINafdkkdrralhwaa 203
Cdd:cd21882    152 DSLGNTVLHalVLQADNTPENSAFVC--------------------------QMYNLLLSYGAHLD-------------- 191

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2131006785  204 ymgHLDVVALLINHgaevtckdkKGYTPLHAAASNGQINVVKHLL 248
Cdd:cd21882    192 ---PTQQLEEIPNH---------QGLTPLKLAAVEGKIVMFQHIL 224
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 608-659 1.12e-03

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.96  E-value: 1.12e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2131006785  608 KSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEAL 659
Cdd:PTZ00322   116 RTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 64-94 1.17e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 37.27  E-value: 1.17e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 2131006785   64 RTPLHVAA-FLGDAEIIELLILSGARVNAKDN 94
Cdd:pfam00023    3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 431-488 1.18e-03

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.96  E-value: 1.18e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2131006785  431 VLSAGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAAN 488
Cdd:PTZ00322   101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEEN 158
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 445-594 1.45e-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: 42.82  E-value: 1.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  445 GRTCLHAAAAGGNVECIKLLQSSGAD---------FHKKDK-----CGRTPLHYAAANCHFHCIETLVTTGA-NVNETDD 509
Cdd:cd22194    141 GQTALNIAIERRQGDIVKLLIAKGADvnahakgvfFNPKYKhegfyFGETPLALAACTNQPEIVQLLMEKEStDITSQDS 220

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  510 WGRTALH--YAAASDMDRNKTILGNAHEnseELERARELKEKEAalclefllqndanpsIRDKEGYNSIHYAAAYGHRQC 587
Cdd:cd22194    221 RGNTVLHalVTVAEDSKTQNDFVKRMYD---MILLKSENKNLET---------------IRNNEGLTPLQLAAKMGKAEI 282


                   ....*..
gi 2131006785  588 LELLLER 594
Cdd:cd22194    283 LKYILSR 289
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 811-833 1.57e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.80  E-value: 1.57e-03
                            10        20
                    ....*....|....*....|...
gi 2131006785   811 QGYTPLHWACYNGNENCIEVLLE 833
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLD 23
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 709-738 1.65e-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: 36.85  E-value: 1.65e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 2131006785  709 KGQTPLMLAVAYGHIDAVSLLLEKEANVDA 738
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 198-226 1.65e-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. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.88  E-value: 1.65e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 2131006785  198 ALHWAAYM-GHLDVVALLINHGAEVTCKDK 226
Cdd:pfam00023    5 PLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 30-94 1.69e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 42.34  E-value: 1.69e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2131006785   30 GFPPLVQAIFSGDPEEIRMLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDN 94
Cdd:PHA03100   192 GFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
PHA02795 PHA02795
ankyrin-like protein; Provisional
 146-223 1.71e-03

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 42.29  E-value: 1.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  146 EVIIPLLSSVNVSDRGGRTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMG--------HLDVVALLINH 217
Cdd:PHA02795   205 KLCIPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRGsviarretHLKILEILLRE 284


                   ....*.
gi 2131006785  218 GAEVTC 223
Cdd:PHA02795   285 PLSIDC 290
PHA02791 PHA02791
ankyrin-like protein; Provisional
 24-259 1.82e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 41.57  E-value: 1.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785   24 FHRQCEGFPPLVQAIFSGDPEEIRMLIHKTEDVNALDSEkrTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRA 103
Cdd:PHA02791    24 FKADVHGHSALYYAIADNNVRLVCTLLNAGALKNLLENE--FPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYA 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  104 VASRSEEAVQVLIKhsadvnardKNWQTPLHvaaankavkcaeviipllssvnvSDRGGRTALHHAALNGHVEMVNLLLA 183
Cdd:PHA02791   102 VDSGNMQTVKLFVK---------KNWRLMFY-----------------------GKTGWKTSFYHAVMLNDVSIVSYFLS 149

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2131006785  184 KGAniNAFDKKDRRA-LHWAAYMGHLDVVALLINHGAEVTCKDKKGYTP-LHAAASNGQINVVKHLLNLGVEIDEINI 259
Cdd:PHA02791   150 EIP--STFDLAILLScIHITIKNGHVDMMILLLDYMTSTNTNNSLLFIPdIKLAIDNKDLEMLQALFKYDINIYSVNL 225
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 639-671 1.88e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.88  E-value: 1.88e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2131006785  639 KGRTALDLAAFK-GHTECVEALINQGASIFVKDN 671
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 445-473 2.12e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.41  E-value: 2.12e-03
                            10        20
                    ....*....|....*....|....*....
gi 2131006785   445 GRTCLHAAAAGGNVECIKLLQSSGADFHK 473
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 360-386 2.12e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.41  E-value: 2.12e-03
                            10        20
                    ....*....|....*....|....*..
gi 2131006785   360 DGNTPLHVAARYGHELLINTLITSGAD 386
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 162-302 2.26e-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: 42.15  E-value: 2.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  162 GRTALHHAALNGHVEMVNLLLAKGANINA------FDKKDRRALhwaaYMGHLdvvallinhgaevtckdkkgytPLHAA 235
Cdd:cd22197     94 GHSALHIAIEKRSLQCVKLLVENGADVHAracgrfFQKKQGTCF----YFGEL----------------------PLSLA 147

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  236 ASNGQINVVKHLLNLGVE---IDEINIYGNTALHLACYNGQDAVVN---------ELTDYGANVNQ-------PNNSGFT 296
Cdd:cd22197    148 ACTKQWDVVNYLLENPHQpasLQAQDSLGNTVLHALVMIADNSPENsalvikmydGLLQAGARLCPtvqleeiSNHEGLT 227


                   ....*.
gi 2131006785  297 PLHFAA 302
Cdd:cd22197    228 PLKLAA 233
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 669-781 2.48e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 41.70  E-value: 2.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  669 KDNVTKRTPLHASVIN---GHTLCLRLLLEIAD---------NPEAIDVKdAKGQTPLMLAVAYGHIDAVSLLLEKEANV 736
Cdd:cd22193     24 TESSTGKTCLMKALLNlnpGTNDTIRILLDIAEktdnlkrfiNAEYTDEY-YEGQTALHIAIERRQGDIVALLVENGADV 102

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2131006785  737 DAVD--------------IMGCTALHRGIMTGHEECVQMLLE---QEVSILCKDSRGRTPLH 781
Cdd:cd22193    103 HAHAkgrffqpkyqgegfYFGELPLSLAACTNQPDIVQYLLEnehQPADIEAQDSRGNTVLH 164
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 162-304 2.66e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 41.70  E-value: 2.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  162 GRTALHHAALNGHVEMVNLLLAKGANINA------FDKKDRRA--------LHWAAYMGHLDVVALLINHG---AEVTCK 224
Cdd:cd22193     76 GQTALHIAIERRQGDIVALLVENGADVHAhakgrfFQPKYQGEgfyfgelpLSLAACTNQPDIVQYLLENEhqpADIEAQ 155

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  225 DKKGYTPLHAAasngqinvvkhllnlgVEIDEiNIYGNTALHLACYNGqdavvneLTDYGANVNQP-------NNSGFTP 297
Cdd:cd22193    156 DSRGNTVLHAL----------------VTVAD-NTKENTKFVTRMYDM-------ILIRGAKLCPTveleeirNNDGLTP 211


                   ....*..
gi 2131006785  298 LHFAAAS 304
Cdd:cd22193    212 LQLAAKM 218
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 709-738 2.66e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.41  E-value: 2.66e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 2131006785   709 KGQTPLMLAVAYGHIDAVSLLLEKEANVDA 738
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 65-143 2.76e-03

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 41.99  E-value: 2.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785   65 TPLHVAAFLGDAEIIELLILSGARVNAKDN--MWLT------------PLHRAVASRSEEAVQVLIKHSADVNARDKNWQ 130
Cdd:TIGR00870  130 TALHLAAHRQNYEIVKLLLERGASVPARACgdFFVKsqgvdsfyhgesPLNAAACLGSPSIVALLSEDPADILTADSLGN 209

                           90
                   ....*....|...
gi 2131006785  131 TPLHVAAANKAVK 143
Cdd:TIGR00870  210 TLLHLLVMENEFK 222
Ank_5 pfam13857
Ankyrin repeats (many copies);
767-819 3.29e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.94  E-value: 3.29e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2131006785  767 VSILCKDSRGRTPLHYAAARGHATWLSELLQMalsEEDCSFKDNQGYTPLHWA 819
Cdd:pfam13857    7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAY---GVDLNLKDEEGLTALDLA 56
PHA02798 PHA02798
ankyrin-like protein; Provisional
 494-751 3.58e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 41.36  E-value: 3.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  494 IETLVTTGANVNETDDWGRTALHyaaasdmdrnkTILGNAhenseelerareLKEKEAALCLEFLLQNDANPSIRDKEGY 573
Cdd:PHA02798    54 VKLFINLGANVNGLDNEYSTPLC-----------TILSNI------------KDYKHMLDIVKILIENGADINKKNSDGE 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  574 NSIHYAAAYGHRQCLELLLERTNNGFEES-DSGATKSPLHLAAYNGHHQALEV---LLQSLVDLD-IRDEKGRTALDlAA 648
Cdd:PHA02798   111 TPLYCLLSNGYINNLEILLFMIENGADTTlLDKDGFTMLQVYLQSNHHIDIEIiklLLEKGVDINtHNNKEKYDTLH-CY 189

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  649 FKGHTECVEA-----LINQGASIFVKDNVTKRTpLHASVINGHTLCLRLLLEIADNPEA-IDV--KDAKGQTPLMLAVAY 720
Cdd:PHA02798   190 FKYNIDRIDAdilklFVDNGFIINKENKSHKKK-FMEYLNSLLYDNKRFKKNILDFIFSyIDInqVDELGFNPLYYSVSH 268

                          250       260       270
                   ....*....|....*....|....*....|.
gi 2131006785  721 GHIDAVSLLLEKEANVDAVDIMGCTALHRGI 751
Cdd:PHA02798   269 NNRKIFEYLLQLGGDINIITELGNTCLFTAF 299
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 198-223 3.79e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.03  E-value: 3.79e-03
                            10        20
                    ....*....|....*....|....*.
gi 2131006785   198 ALHWAAYMGHLDVVALLINHGAEVTC 223
Cdd:smart00248    5 PLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 354-516 3.97e-03

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 41.22  E-value: 3.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  354 IDCVDKDGNTPLHVAARYG-HELLINTLITSGA-----DTAkcgihsmfpLHLAALNAHSDC--CRKLLSSGQKYSIVSL 425
Cdd:TIGR00870   45 INCPDRLGRSALFVAAIENeNLELTELLLNLSCrgavgDTL---------LHAISLEYVDAVeaILLHLLAAFRKSGPLE 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  426 FSNEHVLSAGFeidtpdkFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKC--------------GRTPLHYAAANCHF 491
Cdd:TIGR00870  116 LANDQYTSEFT-------PGITALHLAAHRQNYEIVKLLLERGASVPARACGdffvksqgvdsfyhGESPLNAAACLGSP 188

                          170       180
                   ....*....|....*....|....*
gi 2131006785  492 HCIETLVTTGANVNETDDWGRTALH 516
Cdd:TIGR00870  189 SIVALLSEDPADILTADSLGNTLLH 213
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 211-340 4.25e-03

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.04  E-value: 4.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  211 VALLINHGAEVTCKDKKGYTPLHAAASNGQIN-VVKHLLNlgVEIDEINIYGntalhlacyngqDAV-VNELTDYGANVN 288
Cdd:PTZ00322    44 IARIDTHLEALEATENKDATPDHNLTTEEVIDpVVAHMLT--VELCQLAASG------------DAVgARILLTGGADPN 109

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2131006785  289 QPNNSGFTPLHFAAASTHGALcLELLVNNGADVNIQSKDGKSPLHMTAVHGR 340
Cdd:PTZ00322   110 CRDYDGRTPLHIACANGHVQV-VRVLLEFGADPTLLDKDGKTPLELAEENGF 160
PHA02791 PHA02791
ankyrin-like protein; Provisional
 166-297 4.64e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 40.41  E-value: 4.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  166 LHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGY-TPLHAAASNGQINVV 244
Cdd:PHA02791    65 LHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTGWkTSFYHAVMLNDVSIV 144

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2131006785  245 KHLLNLGVEIDEINIYgNTALHLACYNGQDAVVNELTDYGANVNQPNNSGFTP 297
Cdd:PHA02791   145 SYFLSEIPSTFDLAIL-LSCIHITIKNGHVDMMILLLDYMTSTNTNNSLLFIP 196
Ank_4 pfam13637
Ankyrin repeats (many copies);
947-993 4.73e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.48  E-value: 4.73e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 2131006785  947 NTSLHLASSKGHEKCALLILDKIQDeslINARNNALQTPLHVAARNG 993
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGAD---INAVDGNGETALHFAASNG 45
Ank_5 pfam13857
Ankyrin repeats (many copies);
313-368 4.78e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.17  E-value: 4.78e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2131006785  313 LLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVA 368
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 445-476 5.71e-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: 5.71e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2131006785  445 GRTCLHAAAA-GGNVECIKLLQSSGADFHKKDK 476
Cdd:pfam00023    2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 98-127 5.94e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.34  E-value: 5.94e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 2131006785   98 TPLHRAVASR-SEEAVQVLIKHSADVNARDK 127
Cdd:pfam00023    4 TPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 639-668 6.39e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.26  E-value: 6.39e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 2131006785   639 KGRTALDLAAFKGHTECVEALINQGASIFV 668
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 77-217 6.48e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 39.97  E-value: 6.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785   77 EIIELLILSGARVNAK----DNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQ-TPLHVAAANKAVKCAEVIIPL 151
Cdd:PHA02884    47 DIIDAILKLGADPEAPfplsENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLHGCLKCLEILLSY 126

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2131006785  152 LSSVNVSDRGGRTALHHAALNGHVEMVNLLlaKGANINAFDKKDRRalhwaaYMGHLDVVALLINH 217
Cdd:PHA02884   127 GADINIQTNDMVTPIELALMICNNFLAFMI--CDNEISNFYKHPKK------ILINFDILKILVSH 184
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 477-506 7.20e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.93  E-value: 7.20e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 2131006785  477 CGRTPLHYAAANCHFHCIETLVTTGANVNE 506
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 890-966 7.32e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 40.62  E-value: 7.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  890 DHVECLQLLLRHSAEVNA-------ADNSGK-------TALMMAAENGQAGAVDILVNsAQADLTVKDKDLNTSLHLASS 955
Cdd:PLN03192   489 DNVVILKNFLQHHKELHDlnvgdllGDNGGEhddpnmaSNLLTVASTGNAALLEELLK-AKLDPDIGDSKGRTPLHIAAS 567

                           90
                   ....*....|.
gi 2131006785  956 KGHEKCALLIL 966
Cdd:PLN03192   568 KGYEDCVLVLL 578
PHA02795 PHA02795
ankyrin-like protein; Provisional
 701-774 8.21e-03

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 39.98  E-value: 8.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  701 EAIDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALHRGIMTG--------HEECVQMLLEQEVSILCK 772
Cdd:PHA02795   212 EDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRGsviarretHLKILEILLREPLSIDCI 291


                   ..
gi 2131006785  773 DS 774
Cdd:PHA02795   292 KL 293
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 260-288 8.26e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.93  E-value: 8.26e-03
                           10        20
                   ....*....|....*....|....*....
gi 2131006785  260 YGNTALHLACYNGQDAVVNELTDYGANVN 288
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
Ank_5 pfam13857
Ankyrin repeats (many copies);
558-614 8.56e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.79  E-value: 8.56e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2131006785  558 LLQND-ANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNNGFEESDSGATksPLHLA 614
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLT--ALDLA 56
PHA02743 PHA02743
Viral ankyrin protein; Provisional
 175-294 9.65e-03

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 38.26  E-value: 9.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131006785  175 VEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVV---ALLINHGAEVTCKDKK-GYTPLHAAASNGQINVVKHLL-N 249
Cdd:PHA02743    37 MEVAPFISGDGHLLHRYDHHGRQCTHMVAWYDRANAVmkiELLVNMGADINARELGtGNTLLHIAASTKNYELAEWLCrQ 116

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2131006785  250 LGVEIDEINIYGNTALHLAcYNGQDAVVNE-LTDYGANVNQPNNSG 294
Cdd:PHA02743   117 LGVNLGAINYQHETAYHIA-YKMRDRRMMEiLRANGAVCDDPLSIG 161
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 878-907 9.67e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.93  E-value: 9.67e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 2131006785  878 KGRTPLHAAAFADHVECLQLLLRHSAEVNA 907
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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