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Conserved domains on  [gi|2092232601|ref|XP_043396930|]
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serine/threonine-protein phosphatase 6 regulatory ankyrin repeat subunit A isoform X2 [Chelonia mydas]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 13837771)

ankyrin (ANK) repeat domain-containing protein may be involved in mediating protein-protein interactions

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
54-343 2.44e-48

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 173.99  E-value: 2.44e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601   54 AEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNV 133
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  134 NVSDRAGRTALHHAAFSGHVEMVSLLLSRGANINAFDKKDRRAIHWGAYMGHIEVVKLLVTHGAEVTCKDKKSYTPLHAA 213
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  214 ASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGANVNQMNERGFTPLHFAAASTHGALCLELLV 293
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 2092232601  294 cNGADVNMKSKDGKTPLHMTAIHGRFSRSQTIIQNGAEIDCEDKNGNTPL 343
Cdd:COG0666    241 -AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
521-777 6.97e-38

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.94  E-value: 6.97e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  521 LELIASETPLDVLMETSGTDMLNDSDNRAPISPLHLAAYHGHHQALEVLVQSLLDLDVRNNNGRTPLDLAAFKGHVECVD 600
Cdd:COG0666     25 LLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVK 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  601 VLINQGASILVKDYVvKRTPIHAAATNGHSECLRLLIGNaepqNA-VDIQDGNGQTPLMLSVLNGHTDCVYSLLNKGANV 679
Cdd:COG0666    105 LLLEAGADVNARDKD-GETPLHLAAYNGNLEIVKLLLEA----GAdVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADV 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  680 DAKDKWGRTALHRGAVTGHEECVEALLQHGAKSLLRDCRGRTPIHLSAACGHIGVLGALLQSAtsvdAVPAIADNHGYTS 759
Cdd:COG0666    180 NARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG----ADLNAKDKDGLTA 255

                          250
                   ....*....|....*...
gi 2092232601  760 LHWACYNGHDSCVELLLE 777
Cdd:COG0666    256 LLLAAAAGAALIVKLLLL 273
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
746-981 8.06e-34

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 132.00  E-value: 8.06e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  746 DAVPAIADNHGYTSLHWACYNGHDSCVELLLEQEVFQKMEGNS-FSPLHCAVINDNEGAAEMLIDtLGAgIVNSTDAKGR 824
Cdd:COG0666     44 LLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGgNTLLHAAARNGDLEIVKLLLE-AGA-DVNARDKDGE 121

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  825 TPLHAAAFTDHVECLQLLLSHNAQVNAVDSSGKTPLMMAAENGQTNTVEVLVSsAKADLTLQDSSKNTALHLACSKGHET 904
Cdd:COG0666    122 TPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLE-AGADVNARDNDGETPLHLAAENGHLE 200

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2092232601  905 SALLILEKITDrnlINATNAALQTPLHVAARNGLTVVVQELLGKGASVLAVDENGYTPALACAPNKDVADCLALILA 981
Cdd:COG0666    201 IVKLLLEAGAD---VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLA 274
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
225-503 2.73e-33

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 130.46  E-value: 2.73e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  225 LLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGANVNQMNERGFTPLHFAAASTHGALCLELLVCNGADVNMKSK 304
Cdd:COG0666      6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  305 DGKTPLHMTAIHGRFSRSQTIIQNGAEIDCEDKNGNTPLHIAARYGHELLINTLITSGADTAKRGVHGMFPLHLAALSGF 384
Cdd:COG0666     86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  385 SDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGADFNKKDKFGRTPLHYAAANCNYQCLFALVGSGASV 464
Cdd:COG0666    166 LEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADL 245

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 2092232601  465 NDLDERGCTPLHYAAASDTDGKCLEYLLRNDANPGIRDK 503
Cdd:COG0666    246 NAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLD 284
Ank_4 pfam13637
Ankyrin repeats (many copies);
10-61 1.55e-05

Ankyrin repeats (many copies);


:

Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.42  E-value: 1.55e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2092232601   10 PLLVQAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLI 61
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
54-343 2.44e-48

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 173.99  E-value: 2.44e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601   54 AEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNV 133
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  134 NVSDRAGRTALHHAAFSGHVEMVSLLLSRGANINAFDKKDRRAIHWGAYMGHIEVVKLLVTHGAEVTCKDKKSYTPLHAA 213
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  214 ASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGANVNQMNERGFTPLHFAAASTHGALCLELLV 293
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 2092232601  294 cNGADVNMKSKDGKTPLHMTAIHGRFSRSQTIIQNGAEIDCEDKNGNTPL 343
Cdd:COG0666    241 -AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA03095 PHA03095
ankyrin-like protein; Provisional
 22-310 6.18e-41

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 157.88  E-value: 6.18e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601   22 DEVRALIFKKEDVNFQDNEKRTPLHAaaYLG-----DAEIIELLILSGARVNAKDSKWLTPLHRAV-ASCSEDAVQVLLK 95
Cdd:PHA03095    28 EEVRRLLAAGADVNFRGEYGKTPLHL--YLHyssekVKDIVRLLLEAGADVNAPERCGFTPLHLYLyNATTLDVIKLLIK 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601   96 HSADVNARDKNWQTPLHIAAANKAVkcaealvpllsnvnvsdragrtalhhaafsgHVEMVSLLLSRGANINAFDKKDRR 175
Cdd:PHA03095   106 AGADVNAKDKVGRTPLHVYLSGFNI-------------------------------NPKVIRLLLRKGADVNALDLYGMT 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  176 AIHwgAYMGH----IEVVKLLVTHGAEVTCKDKKSYTPLHAAASSGMIS--VVKYLLDLGVDMNEPNAYGNTPLHVACYN 249
Cdd:PHA03095   155 PLA--VLLKSrnanVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATG 232

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2092232601  250 G--QDVVVNELIDCGANVNQMNERGFTPLHFAAASTHGALCLELLVCnGADVNMKSKDGKTPL 310
Cdd:PHA03095   233 SscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIAL-GADINAVSSDGNTPL 294
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
521-777 6.97e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.94  E-value: 6.97e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  521 LELIASETPLDVLMETSGTDMLNDSDNRAPISPLHLAAYHGHHQALEVLVQSLLDLDVRNNNGRTPLDLAAFKGHVECVD 600
Cdd:COG0666     25 LLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVK 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  601 VLINQGASILVKDYVvKRTPIHAAATNGHSECLRLLIGNaepqNA-VDIQDGNGQTPLMLSVLNGHTDCVYSLLNKGANV 679
Cdd:COG0666    105 LLLEAGADVNARDKD-GETPLHLAAYNGNLEIVKLLLEA----GAdVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADV 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  680 DAKDKWGRTALHRGAVTGHEECVEALLQHGAKSLLRDCRGRTPIHLSAACGHIGVLGALLQSAtsvdAVPAIADNHGYTS 759
Cdd:COG0666    180 NARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG----ADLNAKDKDGLTA 255

                          250
                   ....*....|....*...
gi 2092232601  760 LHWACYNGHDSCVELLLE 777
Cdd:COG0666    256 LLLAAAAGAALIVKLLLL 273
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
746-981 8.06e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 132.00  E-value: 8.06e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  746 DAVPAIADNHGYTSLHWACYNGHDSCVELLLEQEVFQKMEGNS-FSPLHCAVINDNEGAAEMLIDtLGAgIVNSTDAKGR 824
Cdd:COG0666     44 LLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGgNTLLHAAARNGDLEIVKLLLE-AGA-DVNARDKDGE 121

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  825 TPLHAAAFTDHVECLQLLLSHNAQVNAVDSSGKTPLMMAAENGQTNTVEVLVSsAKADLTLQDSSKNTALHLACSKGHET 904
Cdd:COG0666    122 TPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLE-AGADVNARDNDGETPLHLAAENGHLE 200

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2092232601  905 SALLILEKITDrnlINATNAALQTPLHVAARNGLTVVVQELLGKGASVLAVDENGYTPALACAPNKDVADCLALILA 981
Cdd:COG0666    201 IVKLLLEAGAD---VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLA 274
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
225-503 2.73e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 130.46  E-value: 2.73e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  225 LLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGANVNQMNERGFTPLHFAAASTHGALCLELLVCNGADVNMKSK 304
Cdd:COG0666      6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  305 DGKTPLHMTAIHGRFSRSQTIIQNGAEIDCEDKNGNTPLHIAARYGHELLINTLITSGADTAKRGVHGMFPLHLAALSGF 384
Cdd:COG0666     86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  385 SDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGADFNKKDKFGRTPLHYAAANCNYQCLFALVGSGASV 464
Cdd:COG0666    166 LEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADL 245

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 2092232601  465 NDLDERGCTPLHYAAASDTDGKCLEYLLRNDANPGIRDK 503
Cdd:COG0666    246 NAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLD 284
PHA03095 PHA03095
ankyrin-like protein; Provisional
 219-475 4.49e-31

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 128.22  E-value: 4.49e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  219 ISVVKYLLDLGVDMNEPNAYGNTPLHV--ACYNGQDV-VVNELIDCGANVNQMNERGFTPLHFAAASTHGALCLELLVCN 295
Cdd:PHA03095    27 VEEVRRLLAAGADVNFRGEYGKTPLHLylHYSSEKVKdIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDVIKLLIKA 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  296 GADVNMKSKDGKTPLH--MTAIHGRFSRSQTIIQNGAEIDCEDKNGNTPLHIAARYGH---ELLiNTLITSGADTAKRGV 370
Cdd:PHA03095   107 GADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanvELL-RLLIDAGADVYAVDD 185

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  371 HGMFPLHLAALS--GFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLL--NTGADFNKKDKFGRTPLHYAA 446
Cdd:PHA03095   186 RFRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVLPllIAGISINARNRYGQTPLHYAA 265

                          250       260       270
                   ....*....|....*....|....*....|
gi 2092232601  447 ANCNyQCLFA-LVGSGASVNDLDERGCTPL 475
Cdd:PHA03095   266 VFNN-PRACRrLIALGADINAVSSDGNTPL 294
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 554-863 5.85e-21

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 96.96  E-value: 5.85e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  554 LHLAAYHGHHQALEVLVQS---LLDLDVRNNNgrTPLDLAAFKGHVECVDVLINQGASILVKDYVVKRtPIHAAATNGHS 630
Cdd:PHA02874     5 LRMCIYSGDIEAIEKIIKNkgnCINISVDETT--TPLIDAIRSGDAKIVELFIKHGADINHINTKIPH-PLLTAIKIGAH 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  631 ECLRLLIGNAEPQNAVDIQDGNGQTplmlsvlnghtdcVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVEALLQHGA 710
Cdd:PHA02874    82 DIIKLLIDNGVDTSILPIPCIEKDM-------------IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGA 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  711 KSLLRDCRGRTPIHLSAACGHIGVLGALLQSAtsvdAVPAIADNHGYTSLHWACYNGHDSCVELLLEQ--EVFQKMEgNS 788
Cdd:PHA02874   149 DVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKG----AYANVKDNNGESPLHNAAEYGDYACIKLLIDHgnHIMNKCK-NG 223

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2092232601  789 FSPLHCAVINdNEGAAEMLIDTlgaGIVNSTDAKGRTPLH-AAAFTDHVECLQLLLSHNAQVNAVDSSGKTPLMMA 863
Cdd:PHA02874   224 FTPLHNAIIH-NRSAIELLINN---ASINDQDIDGSTPLHhAINPPCDIDIIDILLYHKADISIKDNKGENPIDTA 295
Ank_2 pfam12796
Ankyrin repeats (3 copies);
78-170 3.89e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.94  E-value: 3.89e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601   78 LHRAVASCSEDAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLsNVNVSDRaGRTALHHAAFSGHVEMVS 157
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKDN-GRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 2092232601  158 LLLSRGANINAFD 170
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 653-982 9.76e-19

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 90.47  E-value: 9.76e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  653 GQTPLMLSVLNGHTDC---VYSLLNKGANVDAKDKWGRTALH---RGAVTghEECVEALLQHGAKSLLRDCRGRTPIH-- 724
Cdd:PHA03095    47 GKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLHlylYNATT--LDVIKLLIKAGADVNAKDKVGRTPLHvy 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  725 LSAACGHIGVLGALLQSATSVDAVpaiaDNHGYTSLHwACYNGHDSCVELLleqevfqkmegnsfsplhcavindnegaa 804
Cdd:PHA03095   125 LSGFNINPKVIRLLLRKGADVNAL----DLYGMTPLA-VLLKSRNANVELL----------------------------- 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  805 EMLIDTlGAGIVNsTDAKGRTPLH--AAAFTDHVECLQLLLSHNAQVNAVDSSGKTPLMMAAengqtntvevLVSSAKAD 882
Cdd:PHA03095   171 RLLIDA-GADVYA-VDDRFRSLLHhhLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMA----------TGSSCKRS 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  883 LTLQdsskntalhlacskghetsallILEKITDrnlINATNAALQTPLHVAARNGLTVVVQELLGKGASVLAVDENGYTP 962
Cdd:PHA03095   239 LVLP----------------------LLIAGIS---INARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTP 293

                          330       340
                   ....*....|....*....|
gi 2092232601  963 ALACAPNKDVaDCLALILAT 982
Cdd:PHA03095   294 LSLMVRNNNG-RAVRAALAK 312
Ank_2 pfam12796
Ankyrin repeats (3 copies);
621-716 4.07e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.16  E-value: 4.07e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  621 IHAAATNGHSECLRLLIgnaEPQNAVDIQDGNGQTPLMLSVLNGHTDCVYSLLNKgANVDAKDKwGRTALHRGAVTGHEE 700
Cdd:pfam12796    1 LHLAAKNGNLELVKLLL---ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLE 75

                           90
                   ....*....|....*.
gi 2092232601  701 CVEALLQHGAKSLLRD 716
Cdd:pfam12796   76 IVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
827-920 1.11e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.92  E-value: 1.11e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  827 LHAAAFTDHVECLQLLLSHNAQVNAVDSSGKTPLMMAAENGQTNTVEVLVSSAKADLTLQDsskNTALHLACSKGHETSA 906
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNG---RTALHYAARSGHLEIV 77

                           90
                   ....*....|....
gi 2092232601  907 LLILEKITDRNLIN 920
Cdd:pfam12796   78 KLLLEKGADINVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 74-281 2.28e-14

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: 77.36  E-value: 2.28e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601   74 WLTPLHRAVASCSEDAVQVLLK-HSADVNARDKNWQTPLHIAAANKAVKCAEAL---VPLLSNVNV-SD-RAGRTALHHA 147
Cdd:cd22192     17 SESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLmeaAPELVNEPMtSDlYQGETALHIA 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  148 AFSGHVEMVSLLLSRGANIN-------AFDKKDRRAIHWGAYmghievvkllvthgaevtckdkksytPLHAAASSGMIS 220
Cdd:cd22192     97 VVNQNLNLVRELIARGADVVspratgtFFRPGPKNLIYYGEH--------------------------PLSFAACVGNEE 150

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2092232601  221 VVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDC----GANVNQM------NERGFTPLHFAAA 281
Cdd:cd22192    151 IVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFACQMYDLilsyDKEDDLQpldlvpNNQGLTPFKLAAK 221
Ank_2 pfam12796
Ankyrin repeats (3 copies);
310-402 5.20e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.60  E-value: 5.20e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  310 LHMTAIHGRFSRSQTIIQNGAEIDCEDKNGNTPLHIAARYGHELLINTLITSGAdtAKRGVHGMFPLHLAALSGFSDCCR 389
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 2092232601  390 KLLSSGFDIDTPD 402
Cdd:pfam12796   79 LLLEKGADINVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 274-480 7.12e-10

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: 63.11  E-value: 7.12e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  274 TPLhFAAASTHGALCLE-LLVCNGADVNMKSKDGKTPLHMTAIHGRFSRSQTIIQNGAE-----IDCEDKNGNTPLHIAA 347
Cdd:cd22192     19 SPL-LLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElvnepMTSDLYQGETALHIAV 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  348 RYGHELLINTLITSGADTAKRGVHGMFplhlaalsgFSDCCRKLLSsgfdidtpddFGRTCLHAAAAGGNLECLNLLLNT 427
Cdd:cd22192     98 VNQNLNLVRELIARGADVVSPRATGTF---------FRPGPKNLIY----------YGEHPLSFAACVGNEEIVRLLIEH 158

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2092232601  428 GADFNKKDKFGRTPLHYAA--ANCNYQC-----LFALVGSGASVNdLD----ERGCTPLHYAAA 480
Cdd:cd22192    159 GADIRAQDSLGNTVLHILVlqPNKTFACqmydlILSYDKEDDLQP-LDlvpnNQGLTPFKLAAK 221
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 585-725 9.21e-10

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 62.72  E-value: 9.21e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  585 TPLDLAAFKGHVECVDVLINQGASILVKDYVVKRTPIHAAATNGHSECLRLLIGNA-----EPQNAVDIQdgnGQTPLML 659
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAApelvnEPMTSDLYQ---GETALHI 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  660 SVLNGHTDCVYSLLNKGANV--------------DAKDKWGRTALHRGAVTGHEECVEALLQHGAKSLLRDCRGRTPIHL 725
Cdd:cd22192     96 AVVNQNLNLVRELIARGADVvspratgtffrpgpKNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 822-948 1.76e-08

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: 58.62  E-value: 1.76e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  822 KGRTPLHAAAFTDHVECLQLLLSHNAQVNAVDSS--------------GKTPLMMAAENGQTNTVEVLVSSAKADLTLQD 887
Cdd:cd22194    140 EGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEIVQLLMEKESTDITSQD 219

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  888 SSKNTALHLAC-----SKGHETSAL----LILEKITDRNLINATNAALQTPLHVAARNGLTVVVQELLGK 948
Cdd:cd22194    220 SRGNTVLHALVtvaedSKTQNDFVKrmydMILLKSENKNLETIRNNEGLTPLQLAAKMGKAEILKYILSR 289
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 28-247 5.20e-07

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 53.93  E-value: 5.20e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601   28 IFKKEDVNFQDNEKrtplhaaAYLGDAEIIELLILSGARVNAK-------DSKWLTPLHRAVA-SCSEDAVQVLLKHSAD 99
Cdd:TIGR00870    6 IVPAEESPLSDEEK-------AFLPAAERGDLASVYRDLEEPKklnincpDRLGRSALFVAAIeNENLELTELLLNLSCR 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  100 VNARDknwqTPLHIAAANKAVKCAEALVPLLSN---------VNVSDR----AGRTALHHAAFSGHVEMVSLLLSRGANI 166
Cdd:TIGR00870   79 GAVGD----TLLHAISLEYVDAVEAILLHLLAAfrksgplelANDQYTseftPGITALHLAAHRQNYEIVKLLLERGASV 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  167 NA------FDKKDRRA--------IHWGAYMGHIEVVKLLVTHGAEVTCKDKKSYTPLHAAA------------SSGMIS 220
Cdd:TIGR00870  155 PAracgdfFVKSQGVDsfyhgespLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVmenefkaeyeelSCQMYN 234

                          250       260       270
                   ....*....|....*....|....*....|.
gi 2092232601  221 VVKYLLDLGVDMNE----PNAYGNTPLHVAC 247
Cdd:TIGR00870  235 FALSLLDKLRDSKEleviLNHQGLTPLKLAA 265
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 574-797 5.29e-07

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 53.93  E-value: 5.29e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  574 LDLDVRNNNGRTPLDLAAFKG-HVECVDVLINQGASILVKDyvvkrTPIHAAATNGH---SECLRLLIGNAE----PQNA 645
Cdd:TIGR00870   43 LNINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAVGD-----TLLHAISLEYVdavEAILLHLLAAFRksgpLELA 117

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  646 VDIQDGN---GQTPLMLSVLNGHTDCVYSLLNKGANVDAKDK--------------WGRTALHRGAVTGHEECVEALLQH 708
Cdd:TIGR00870  118 NDQYTSEftpGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSED 197

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  709 GAKSLLRDCRGRTPIHLSA--------------ACGHIGV-LGALLQSATSVDAVPaiadNH-GYTSLHWACYNGHDSCV 772
Cdd:TIGR00870  198 PADILTADSLGNTLLHLLVmenefkaeyeelscQMYNFALsLLDKLRDSKELEVIL----NHqGLTPLKLAAKEGRIVLF 273

                          250       260
                   ....*....|....*....|....*.
gi 2092232601  773 ELLLEQEVFQ-KMEGNSFSPLHCAVI 797
Cdd:TIGR00870  274 RLKLAIKYKQkKFVAWPNGQQLLSLY 299
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 140-168 7.80e-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: 43.35  E-value: 7.80e-06
                            10        20
                    ....*....|....*....|....*....
gi 2092232601   140 GRTALHHAAFSGHVEMVSLLLSRGANINA 168
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
10-61 1.55e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.42  E-value: 1.55e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2092232601   10 PLLVQAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLI 61
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 391-594 2.63e-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: 45.07  E-value: 2.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  391 LLSSGFDIDTpddfGRTCLHAA-----------------AAGGNLECLNLLLNTGADFNkkdkFGRTPLHYAAANCNYQC 453
Cdd:TIGR00870   72 LLNLSCRGAV----GDTLLHAIsleyvdaveaillhllaAFRKSGPLELANDQYTSEFT----PGITALHLAAHRQNYEI 143

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  454 LFALVGSGASVndldergctplHYAAasdtdgKCLEYLlrndanpgirDKQGYNAVHYSAaygHRL----CL---ELIA- 525
Cdd:TIGR00870  144 VKLLLERGASV-----------PARA------CGDFFV----------KSQGVDSFYHGE---SPLnaaaCLgspSIVAl 193

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2092232601  526 -SETPLDVLMETS-GTDMLN----DSDNRAPISPLHLAAYHGHHQALEVLVQSLLDLDVRNNNGRTPLDLAAFKG 594
Cdd:TIGR00870  194 lSEDPADILTADSlGNTLLHllvmENEFKAEYEELSCQMYNFALSLLDKLRDSKELEVILNHQGLTPLKLAAKEG 268
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 822-851 4.23e-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: 4.23e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 2092232601   822 KGRTPLHAAAFTDHVECLQLLLSHNAQVNA 851
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 582-609 1.05e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.57  E-value: 1.05e-03
                            10        20
                    ....*....|....*....|....*...
gi 2092232601   582 NGRTPLDLAAFKGHVECVDVLINQGASI 609
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 338-364 1.19e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.18  E-value: 1.19e-03
                            10        20
                    ....*....|....*....|....*..
gi 2092232601   338 NGNTPLHIAARYGHELLINTLITSGAD 364
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 818-946 1.25e-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: 42.76  E-value: 1.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  818 STDAKGRTPLHAAAFTDHVECLQLLLSHNAQVNA------------VDS--SGKTPLMMAAENGQTNTVEvLVSSAKADL 883
Cdd:TIGR00870  123 SEFTPGITALHLAAHRQNYEIVKLLLERGASVPAracgdffvksqgVDSfyHGESPLNAAACLGSPSIVA-LLSEDPADI 201

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2092232601  884 TLQDSSKNTALHL------------ACSKGHETSALLILEKITD-RNLINATNAALQTPLHVAARNGLTVVVQELL 946
Cdd:TIGR00870  202 LTADSLGNTLLHLlvmenefkaeyeELSCQMYNFALSLLDKLRDsKELEVILNHQGLTPLKLAAKEGRIVLFRLKL 277
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 15-79 4.99e-03

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 40.77  E-value: 4.99e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2092232601   15 AIFNGDPDEVRALIFKKEDVN--------FQDNEKRT------PLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLH 79
Cdd:cd22192     96 AVVNQNLNLVRELIARGADVVspratgtfFRPGPKNLiyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
54-343 2.44e-48

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 173.99  E-value: 2.44e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601   54 AEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNV 133
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  134 NVSDRAGRTALHHAAFSGHVEMVSLLLSRGANINAFDKKDRRAIHWGAYMGHIEVVKLLVTHGAEVTCKDKKSYTPLHAA 213
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  214 ASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGANVNQMNERGFTPLHFAAASTHGALCLELLV 293
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 2092232601  294 cNGADVNMKSKDGKTPLHMTAIHGRFSRSQTIIQNGAEIDCEDKNGNTPL 343
Cdd:COG0666    241 -AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
11-276 6.83e-48

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 172.83  E-value: 6.83e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601   11 LLVQAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAV 90
Cdd:COG0666     24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIV 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601   91 QVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHVEMVSLLLSRGANINAFD 170
Cdd:COG0666    104 KLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  171 KKDRRAIHWGAYMGHIEVVKLLVTHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNG 250
Cdd:COG0666    184 NDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAG 263

                          250       260
                   ....*....|....*....|....*.
gi 2092232601  251 QDVVVNELIDCGANVNQMNERGFTPL 276
Cdd:COG0666    264 AALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
10-243 5.46e-47

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 170.13  E-value: 5.46e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601   10 PLLVQAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDA 89
Cdd:COG0666     56 LLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI 135

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601   90 VQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHVEMVSLLLSRGANINAF 169
Cdd:COG0666    136 VKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAK 215

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2092232601  170 DKKDRRAIHWGAYMGHIEVVKLLVTHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPL 243
Cdd:COG0666    216 DNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
22-292 7.80e-47

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 169.75  E-value: 7.80e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601   22 DEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQVLLKHSADVN 101
Cdd:COG0666      2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  102 ARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHVEMVSLLLSRGANINAFDKKDRRAIHWGA 181
Cdd:COG0666     82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  182 YMGHIEVVKLLVTHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDC 261
Cdd:COG0666    162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241

                          250       260       270
                   ....*....|....*....|....*....|.
gi 2092232601  262 GANVNQMNERGFTPLHFAAASTHGALCLELL 292
Cdd:COG0666    242 GADLNAKDKDGLTALLLAAAAGAALIVKLLL 272
PHA03095 PHA03095
ankyrin-like protein; Provisional
 22-310 6.18e-41

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 157.88  E-value: 6.18e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601   22 DEVRALIFKKEDVNFQDNEKRTPLHAaaYLG-----DAEIIELLILSGARVNAKDSKWLTPLHRAV-ASCSEDAVQVLLK 95
Cdd:PHA03095    28 EEVRRLLAAGADVNFRGEYGKTPLHL--YLHyssekVKDIVRLLLEAGADVNAPERCGFTPLHLYLyNATTLDVIKLLIK 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601   96 HSADVNARDKNWQTPLHIAAANKAVkcaealvpllsnvnvsdragrtalhhaafsgHVEMVSLLLSRGANINAFDKKDRR 175
Cdd:PHA03095   106 AGADVNAKDKVGRTPLHVYLSGFNI-------------------------------NPKVIRLLLRKGADVNALDLYGMT 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  176 AIHwgAYMGH----IEVVKLLVTHGAEVTCKDKKSYTPLHAAASSGMIS--VVKYLLDLGVDMNEPNAYGNTPLHVACYN 249
Cdd:PHA03095   155 PLA--VLLKSrnanVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATG 232

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2092232601  250 G--QDVVVNELIDCGANVNQMNERGFTPLHFAAASTHGALCLELLVCnGADVNMKSKDGKTPL 310
Cdd:PHA03095   233 SscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIAL-GADINAVSSDGNTPL 294
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 23-301 4.92e-38

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 147.89  E-value: 4.92e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601   23 EVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLH-----RAVASCSEDAVQVLLKHS 97
Cdd:PHA03100    17 NIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYG 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601   98 ADVNARDKNWQTPLHIAAANKavkcaealvpllsnvnvsdragrtalhhaafSGHVEMVSLLLSRGANINAFDKKDRRAI 177
Cdd:PHA03100    97 ANVNAPDNNGITPLLYAISKK-------------------------------SNSYSIVEYLLDNGANVNIKNSDGENLL 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  178 HWGAYMGHI--EVVKLLVTHGAEVTCKDKksytplhaaassgmisvVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVV 255
Cdd:PHA03100   146 HLYLESNKIdlKILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFV 208

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 2092232601  256 NELIDCGANVNQMNERGFTPLHFAAASTHGALcLELLVCNGADVNM 301
Cdd:PHA03100   209 KYLLDLGANPNLVNKYGDTPLHIAILNNNKEI-FKLLLNNGPSIKT 253
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
521-777 6.97e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.94  E-value: 6.97e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  521 LELIASETPLDVLMETSGTDMLNDSDNRAPISPLHLAAYHGHHQALEVLVQSLLDLDVRNNNGRTPLDLAAFKGHVECVD 600
Cdd:COG0666     25 LLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVK 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  601 VLINQGASILVKDYVvKRTPIHAAATNGHSECLRLLIGNaepqNA-VDIQDGNGQTPLMLSVLNGHTDCVYSLLNKGANV 679
Cdd:COG0666    105 LLLEAGADVNARDKD-GETPLHLAAYNGNLEIVKLLLEA----GAdVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADV 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  680 DAKDKWGRTALHRGAVTGHEECVEALLQHGAKSLLRDCRGRTPIHLSAACGHIGVLGALLQSAtsvdAVPAIADNHGYTS 759
Cdd:COG0666    180 NARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG----ADLNAKDKDGLTA 255

                          250
                   ....*....|....*...
gi 2092232601  760 LHWACYNGHDSCVELLLE 777
Cdd:COG0666    256 LLLAAAAGAALIVKLLLL 273
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
186-475 9.86e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 140.47  E-value: 9.86e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  186 IEVVKLLVTHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGANV 265
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  266 NQMNERGFTPLHFAAASTHGALcLELLVCNGADVNMKSKDGKTPLHMTAIHGRFSRSQTIIQNGAEIDCEDKNGNTPLHI 345
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEI-VKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  346 AARYGHELLINTLITSGADTAKRGVHGMFPLHLAALSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLL 425
Cdd:COG0666    160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 2092232601  426 NTGADFNKKDKFGRTPLHYAAANCNYQCLFALVGSGASVNDLDERGCTPL 475
Cdd:COG0666    240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
633-963 1.26e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 140.09  E-value: 1.26e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  633 LRLLIGNAEPQNAVDIQDGNGQTPLMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVEALLQHGAKS 712
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  713 LLRDCRGRTPIHLSAACGHIGVLGALLQSATSVDAVpaiaDNHGYTSLHWACYNGHDSCVELLLEQevfqkmegnsfspl 792
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNAR----DKDGETPLHLAAYNGNLEIVKLLLEA-------------- 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  793 hcavindneGAAemlidtlgagiVNSTDAKGRTPLHAAAFTDHVECLQLLLSHNAQVNAVDSSGKTPLMMAAENGQTNTV 872
Cdd:COG0666    143 ---------GAD-----------VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  873 EVLVsSAKADLTLQDSSKNTALHLACSKGHETSALLILEKITDrnlINATNAALQTPLHVAARNGLTVVVQELLGKGASV 952
Cdd:COG0666    203 KLLL-EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD---LNAKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278

                          330
                   ....*....|.
gi 2092232601  953 LAVDENGYTPA 963
Cdd:COG0666    279 AAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
507-754 1.54e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 140.09  E-value: 1.54e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  507 NAVHYSAAYGHRLCLELIASETPLDVLMETSGTDMLNDSDNRAPISPLHLAAYHGHHQALEVLVQSLLDLDVRNNNGRTP 586
Cdd:COG0666     44 LLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETP 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  587 LDLAAFKGHVECVDVLINQGASILVKDYVvKRTPIHAAATNGHSECLRLLIGNaepqNA-VDIQDGNGQTPLMLSVLNGH 665
Cdd:COG0666    124 LHLAAYNGNLEIVKLLLEAGADVNAQDND-GNTPLHLAAANGNLEIVKLLLEA----GAdVNARDNDGETPLHLAAENGH 198

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  666 TDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVEALLQHGAKSLLRDCRGRTPIHLSAACGHIGVLGALLQSATSV 745
Cdd:COG0666    199 LEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278


                   ....*....
gi 2092232601  746 DAVPAIADN 754
Cdd:COG0666    279 AAALLDLLT 287
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 22-364 2.88e-36

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 147.13  E-value: 2.88e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601   22 DEVR---ALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQVLLKHSA 98
Cdd:PHA02876   156 DELLiaeMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRS 235

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601   99 DVNARDKNwqtpLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHV-EMVSLLLSRGANINAFDKKDRRAI 177
Cdd:PHA02876   236 NINKNDLS----LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPL 311

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  178 HWGAYMGH-IEVVKLLVTHGAEVTCKDKKSYTPLHAAAS-SGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVV 255
Cdd:PHA02876   312 YLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVII 391

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  256 NELIDCGANVNQMNERGFTPLHFAAASTHGALCLELLVCNGADVNMKSKDGKTPLHMTAIHG-RFSRSQTIIQNGAEIDC 334
Cdd:PHA02876   392 NTLLDYGADIEALSQKIGTALHFALCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNA 471

                          330       340       350
                   ....*....|....*....|....*....|
gi 2092232601  335 EDKNGNTPLHIAarYGHELLINTLITSGAD 364
Cdd:PHA02876   472 INIQNQYPLLIA--LEYHGIVNILLHYGAE 499
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 16-367 3.42e-34

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 137.02  E-value: 3.42e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601   16 IFNGDPDEVRALIFKKED-VNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQVLL 94
Cdd:PHA02874     9 IYSGDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601   95 KHSADVNARDknwqtplhiaaankavkcaealVPLLSNvnvsdragrtalhhaafsghvEMVSLLLSRGANINAFDKKDR 174
Cdd:PHA02874    89 DNGVDTSILP----------------------IPCIEK---------------------DMIKTILDCGIDVNIKDAELK 125

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  175 RAIHWGAYMGHIEVVKLLVTHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVV 254
Cdd:PHA02874   126 TFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYAC 205

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  255 VNELIDCGANVNQMNERGFTPLHfaAASTHGALCLELLVcNGADVNMKSKDGKTPLHMtAIHGRFSRS--QTIIQNGAEI 332
Cdd:PHA02874   206 IKLLIDHGNHIMNKCKNGFTPLH--NAIIHNRSAIELLI-NNASINDQDIDGSTPLHH-AINPPCDIDiiDILLYHKADI 281

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 2092232601  333 DCEDKNGNTPLHIAARYGH------ELLINTLITSGADTAK 367
Cdd:PHA02874   282 SIKDNKGENPIDTAFKYINkdpvikDIIANAVLIKEADKLK 322
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
746-981 8.06e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 132.00  E-value: 8.06e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  746 DAVPAIADNHGYTSLHWACYNGHDSCVELLLEQEVFQKMEGNS-FSPLHCAVINDNEGAAEMLIDtLGAgIVNSTDAKGR 824
Cdd:COG0666     44 LLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGgNTLLHAAARNGDLEIVKLLLE-AGA-DVNARDKDGE 121

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  825 TPLHAAAFTDHVECLQLLLSHNAQVNAVDSSGKTPLMMAAENGQTNTVEVLVSsAKADLTLQDSSKNTALHLACSKGHET 904
Cdd:COG0666    122 TPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLE-AGADVNARDNDGETPLHLAAENGHLE 200

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2092232601  905 SALLILEKITDrnlINATNAALQTPLHVAARNGLTVVVQELLGKGASVLAVDENGYTPALACAPNKDVADCLALILA 981
Cdd:COG0666    201 IVKLLLEAGAD---VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLA 274
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
540-778 1.31e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 131.61  E-value: 1.31e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  540 DMLNDSDNRAPISPLHLAAYHGHHQALEVLVQSLLDLDVRNNNGRTPLDLAAFKGHVECVDVLINQGASILVKDYVvKRT 619
Cdd:COG0666     11 LLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG-GNT 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  620 PIHAAATNGHSECLRLLIGNAEPqnaVDIQDGNGQTPLMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHE 699
Cdd:COG0666     90 LLHAAARNGDLEIVKLLLEAGAD---VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2092232601  700 ECVEALLQHGAKSLLRDCRGRTPIHLSAACGHIGVLGALLQSatsvDAVPAIADNHGYTSLHWACYNGHDSCVELLLEQ 778
Cdd:COG0666    167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA----GADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
225-503 2.73e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 130.46  E-value: 2.73e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  225 LLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGANVNQMNERGFTPLHFAAASTHGALCLELLVCNGADVNMKSK 304
Cdd:COG0666      6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  305 DGKTPLHMTAIHGRFSRSQTIIQNGAEIDCEDKNGNTPLHIAARYGHELLINTLITSGADTAKRGVHGMFPLHLAALSGF 384
Cdd:COG0666     86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  385 SDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGADFNKKDKFGRTPLHYAAANCNYQCLFALVGSGASV 464
Cdd:COG0666    166 LEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADL 245

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 2092232601  465 NDLDERGCTPLHYAAASDTDGKCLEYLLRNDANPGIRDK 503
Cdd:COG0666    246 NAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLD 284
PHA03095 PHA03095
ankyrin-like protein; Provisional
 86-359 4.18e-33

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 134.38  E-value: 4.18e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601   86 SEDAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLL---SNVNVSDRAGRTALH-HAAFSGHVEMVSLLLS 161
Cdd:PHA03095    26 TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIVRLLLeagADVNAPERCGFTPLHlYLYNATTLDVIKLLIK 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  162 RGANINAFDKKDRRAIHwgAYMG----HIEVVKLLVTHGAEVTCKDKKSYTPLHAAASSGMISV--VKYLLDLGVDMNEP 235
Cdd:PHA03095   106 AGADVNAKDKVGRTPLH--VYLSgfniNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVYAV 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  236 NAYGNTPLHVACYNGQD--VVVNELIDCGANVNQMNERGFTPLHFAAA-STHGALCLELLVCNGADVNMKSKDGKTPLHM 312
Cdd:PHA03095   184 DDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHSMATgSSCKRSLVLPLLIAGISINARNRYGQTPLHY 263

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 2092232601  313 TAIHGR---FSRsqtIIQNGAEIDCEDKNGNTPLHIAARYGHELLINTLI 359
Cdd:PHA03095   264 AAVFNNpraCRR---LIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
746-981 1.69e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 128.15  E-value: 1.69e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  746 DAVPAIADNHGYTSLHWACYNGHDSCVELLLEQEVFQKMEGNSFSPLHCAVINDNEGAAEMLIDTLGAgIVNSTDAKGRT 825
Cdd:COG0666     11 LLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGA-DINAKDDGGNT 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  826 PLHAAAFTDHVECLQLLLSHNAQVNAVDSSGKTPLMMAAENGQTNTVEVLVSsAKADLTLQDSSKNTALHLACSKGHETS 905
Cdd:COG0666     90 LLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLE-AGADVNAQDNDGNTPLHLAAANGNLEI 168

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2092232601  906 ALLILEKITDrnlINATNAALQTPLHVAARNGLTVVVQELLGKGASVLAVDENGYTPALACAPNKDVADCLALILA 981
Cdd:COG0666    169 VKLLLEAGAD---VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
391-723 5.25e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 126.61  E-value: 5.25e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  391 LLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGADFNKKDKFGRTPLHYAAANCNYQCLFALVGSGASVNDLDER 470
Cdd:COG0666      7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  471 GCTPLHYAAASDtDGKCLEYLLRNDANPGIRDKQGYnavhysaayghrlcleliasetpldvlmetsgtdmlndsdnrap 550
Cdd:COG0666     87 GNTLLHAAARNG-DLEIVKLLLEAGADVNARDKDGE-------------------------------------------- 121

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  551 iSPLHLAAYHGHHQALEVLVQSLLDLDVRNNNGRTPLDLAAFKGHVECVDVLINQGASILVKDYVvKRTPIHAAATNGHS 630
Cdd:COG0666    122 -TPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDND-GETPLHLAAENGHL 199

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  631 ECLRLLIGNaepqNA-VDIQDGNGQTPLMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVEALLQHG 709
Cdd:COG0666    200 EIVKLLLEA----GAdVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLAL 275

                          330
                   ....*....|....
gi 2092232601  710 AKSLLRDCRGRTPI 723
Cdd:COG0666    276 LLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
263-525 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 2092232601  263 ANVNQMNERGFTPLHFAAASTHGALCLELLVCNGADVNMKSKDGKTPLHMTAIHGRFSRSQTIIQNGAEIDCEDKNGNTP 342
Cdd:COG0666     11 LLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTL 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  343 LHIAARYGHELLINTLITSGADTAKRGVHGMFPLHLAALSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLN 422
Cdd:COG0666     91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  423 LLLNTGADFNKKDKFGRTPLHYAAANCNYQCLFALVGSGASVNDLDERGCTPLHYAAASDtDGKCLEYLLRNDANPGIRD 502
Cdd:COG0666    171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENG-NLEIVKLLLEAGADLNAKD 249

                          250       260
                   ....*....|....*....|...
gi 2092232601  503 KQGYNAVHYSAAYGHRLCLELIA 525
Cdd:COG0666    250 KDGLTALLLAAAAGAALIVKLLL 272
PHA03095 PHA03095
ankyrin-like protein; Provisional
 186-454 1.72e-31

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 129.37  E-value: 1.72e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  186 IEVVKLLVTHGAEVTCKDKKSYTPLHAAASSGM---ISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDV-VVNELIDC 261
Cdd:PHA03095    27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKA 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  262 GANVNQMNERGFTPLH--FAAASTHgALCLELLVCNGADVNMKSKDGKTPLHMTAIHGRFSRS--QTIIQNGAEIDCEDK 337
Cdd:PHA03095   107 GADVNAKDKVGRTPLHvyLSGFNIN-PKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVEllRLLIDAGADVYAVDD 185

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  338 NGNTPLHIAARYGH--ELLINTLITSGADTAKRGVHGMFPLHLAALsgFSDCCR----KLLSSGFDIDTPDDFGRTCLHA 411
Cdd:PHA03095   186 RFRSLLHHHLQSFKprARIVRELIRAGCDPAATDMLGNTPLHSMAT--GSSCKRslvlPLLIAGISINARNRYGQTPLHY 263

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 2092232601  412 AAAGGNLECLNLLLNTGADFNKKDKFGRTPLHYAAANCNYQCL 454
Cdd:PHA03095   264 AAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAV 306
PHA03095 PHA03095
ankyrin-like protein; Provisional
 219-475 4.49e-31

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 128.22  E-value: 4.49e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  219 ISVVKYLLDLGVDMNEPNAYGNTPLHV--ACYNGQDV-VVNELIDCGANVNQMNERGFTPLHFAAASTHGALCLELLVCN 295
Cdd:PHA03095    27 VEEVRRLLAAGADVNFRGEYGKTPLHLylHYSSEKVKdIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDVIKLLIKA 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  296 GADVNMKSKDGKTPLH--MTAIHGRFSRSQTIIQNGAEIDCEDKNGNTPLHIAARYGH---ELLiNTLITSGADTAKRGV 370
Cdd:PHA03095   107 GADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanvELL-RLLIDAGADVYAVDD 185

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  371 HGMFPLHLAALS--GFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLL--NTGADFNKKDKFGRTPLHYAA 446
Cdd:PHA03095   186 RFRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVLPllIAGISINARNRYGQTPLHYAA 265

                          250       260       270
                   ....*....|....*....|....*....|
gi 2092232601  447 ANCNyQCLFA-LVGSGASVNDLDERGCTPL 475
Cdd:PHA03095   266 VFNN-PRACRrLIALGADINAVSSDGNTPL 294
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
352-690 2.51e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 121.98  E-value: 2.51e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  352 ELLINTLITSGADTAKRGVHGMFPLHLAALSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGADF 431
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  432 NKKDKFGRTPLHYAAANCNYQCLFALVGSGASVNDLDERGCTPLHYAAASDtDGKCLEYLLRNDANPGIRDKQGYnavhy 511
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNG-NLEIVKLLLEAGADVNAQDNDGN----- 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  512 saayghrlcleliasetpldvlmetsgtdmlndsdnrapiSPLHLAAYHGHHQALEVLVQSLLDLDVRNNNGRTPLDLAA 591
Cdd:COG0666    155 ----------------------------------------TPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAA 194

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  592 FKGHVECVDVLINQGASILVKDYvVKRTPIHAAATNGHSECLRLLIGNAEpqnAVDIQDGNGQTPLMLSVLNGHTDCVYS 671
Cdd:COG0666    195 ENGHLEIVKLLLEAGADVNAKDN-DGKTALDLAAENGNLEIVKLLLEAGA---DLNAKDKDGLTALLLAAAAGAALIVKL 270

                          330
                   ....*....|....*....
gi 2092232601  672 LLNKGANVDAKDKWGRTAL 690
Cdd:COG0666    271 LLLALLLLAAALLDLLTLL 289
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 75-353 7.81e-27

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 115.75  E-value: 7.81e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601   75 LTPLHRAVASCSEDAVQVLLKHSADVNARDKNWQTPLHIA--AANKavkcaEALVPLLSNVNvSDRAGRT--ALHHAAFS 150
Cdd:PHA02878    38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIIckEPNK-----LGMKEMIRSIN-KCSVFYTlvAIKDAFNN 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  151 GHVEMV-SLLLSRGANINAFDKKDRRAIHWGAYMgHIEVVKLLVTHGAEVTCKDK-KSYTPLHAAASSGMISVVKYLLDL 228
Cdd:PHA02878   112 RNVEIFkIILTNRYKNIQTIDLVYIDKKSKDDII-EAEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSY 190

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  229 GVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGANVNQMNERGFTPLHFAAASTHGALCLELLVCNGADVNMKSK-DGK 307
Cdd:PHA02878   191 GANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDYDILKLLLEHGVDVNAKSYiLGL 270

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 2092232601  308 TPLHMtAIHGRfSRSQTIIQNGAEIDCEDKNGNTPLHIAA--RYGHEL 353
Cdd:PHA02878   271 TALHS-SIKSE-RKLKLLLEYGADINSLNSYKLTPLSSAVkqYLCINI 316
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 186-400 2.24e-26

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 113.22  E-value: 2.24e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  186 IEVVKLLVTHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLH---VACYNGQDVV--VNELID 260
Cdd:PHA03100    15 VKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsNIKYNLTDVKeiVKLLLE 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  261 CGANVNQMNERGFTPLHFAAASTHGALCL-ELLVCNGADVNMKSKDGKTPLHMTA--IHGRFSRSQTIIQNGAEIDCE-- 335
Cdd:PHA03100    95 YGANVNAPDNNGITPLLYAISKKSNSYSIvEYLLDNGANVNIKNSDGENLLHLYLesNKIDLKILKLLIDKGVDINAKnr 174

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2092232601  336 --------------DKNGNTPLHIAARYGHELLINTLITSGADTAKRGVHGMFPLHLAALSGFSDCCRKLLSSGFDIDT 400
Cdd:PHA03100   175 vnyllsygvpinikDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 10-270 3.45e-26

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 112.84  E-value: 3.45e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601   10 PLLVQAIFN-GDPDEVRALIFKKE-DVNFQDNEKRTPLHAAAY--LGDAEIIELLILSGARVNAKDSKWLTPLHRAVASC 85
Cdd:PHA03100    73 HYLSNIKYNlTDVKEIVKLLLEYGaNVNAPDNNGITPLLYAISkkSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESN 152

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601   86 SEDavqvllkhsadvnardknwqtplhiaaankavkcaealvpllsnvnvsdragrtalhhaafsghVEMVSLLLSRGAN 165
Cdd:PHA03100   153 KID----------------------------------------------------------------LKILKLLIDKGVD 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  166 INAfdkKDRraihwgaymghievVKLLVTHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHV 245
Cdd:PHA03100   169 INA---KNR--------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHI 231

                          250       260
                   ....*....|....*....|....*
gi 2092232601  246 ACYNGQDVVVNELIDCGANVNQMNE 270
Cdd:PHA03100   232 AILNNNKEIFKLLLNNGPSIKTIIE 256
PHA03095 PHA03095
ankyrin-like protein; Provisional
 254-605 6.46e-26

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 112.81  E-value: 6.46e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  254 VVNELIDCGANVNQMNERGFTPLHFAAASTHGAL--CLELLVCNGADVNMKSKDGKTPLHMTAIHgrfsrSQTI------ 325
Cdd:PHA03095    29 EVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdIVRLLLEAGADVNAPERCGFTPLHLYLYN-----ATTLdvikll 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  326 IQNGAEIDCEDKNGNTPLHIAAR--YGHELLINTLITSGADTAKRGVHGMFPLHlaALSGFSDCC----RKLLSSGFDID 399
Cdd:PHA03095   104 IKAGADVNAKDKVGRTPLHVYLSgfNINPKVIRLLLRKGADVNALDLYGMTPLA--VLLKSRNANvellRLLIDAGADVY 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  400 TPDDFGRTCLHaaaaggnleclnlllnTGADFNKKdkfgrtplhyaaancNYQCLFALVGSGASVNDLDERGCTPLHYAA 479
Cdd:PHA03095   182 AVDDRFRSLLH----------------HHLQSFKP---------------RARIVRELIRAGCDPAATDMLGNTPLHSMA 230

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  480 asdTDGKCLEYLLRNdanpgirdkqgynavhysaayghrlcleLIASetpldvlmetsGTDMlnDSDNRAPISPLHLAAY 559
Cdd:PHA03095   231 ---TGSSCKRSLVLP----------------------------LLIA-----------GISI--NARNRYGQTPLHYAAV 266

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 2092232601  560 HGHHQALEVLVQSLLDLDVRNNNGRTPLDLAAFKGHVECVDVLINQ 605
Cdd:PHA03095   267 FNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAK 312
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 241-543 4.15e-24

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 106.59  E-value: 4.15e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  241 TPLHVACYNGQDVVVNELIDCGANVNQMNERGFTPLhFAAASTHGALCLELLVCNGADVNMkskdgktpLHMTAIHGRFS 320
Cdd:PHA02874    37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPL-LTAIKIGAHDIIKLLIDNGVDTSI--------LPIPCIEKDMI 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  321 RsqTIIQNGAEIDCEDKNGNTPLHIAARYGHELLINTLITSGADTAKRGVHGMFPLHLAALSGFSDCCRKLLSSGFDIDT 400
Cdd:PHA02874   108 K--TILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANV 185

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  401 PDDFGRTCLHAAAAGGNLECLNLLLNTGADFNKKDKFGRTPLHYAAanCNYQCLFALVGSGASVNDLDERGCTPLHYAAA 480
Cdd:PHA02874   186 KDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI--IHNRSAIELLINNASINDQDIDGSTPLHHAIN 263

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2092232601  481 SDTDGKCLEYLLRNDANPGIRDKQGYNAVHYSAAYGHRLCL--ELIASETPLDVLMETSGTDMLN 543
Cdd:PHA02874   264 PPCDIDIIDILLYHKADISIKDNKGENPIDTAFKYINKDPVikDIIANAVLIKEADKLKDSDFLE 328
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
774-979 4.64e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 97.72  E-value: 4.64e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  774 LLLEQEVFQKMEGNSFSPLHCAVINDNEGAAEMLIDTLGAGIVNSTDAKGRTPLHAAAFTDHVECLQLLLSHNAQVNAVD 853
Cdd:COG0666      5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  854 SSGKTPLMMAAENGQTNTVEVLVsSAKADLTLQDSSKNTALHLACSKGHETSALLILEKITDrnlINATNAALQTPLHVA 933
Cdd:COG0666     85 DGGNTLLHAAARNGDLEIVKLLL-EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGAD---VNAQDNDGNTPLHLA 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2092232601  934 ARNGLTVVVQELLGKGASVLAVDENGYTPALACAPNKDVADCLALI 979
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLL 206
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 155-512 5.57e-22

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 102.06  E-value: 5.57e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  155 MVSLLLSRGANINAFDKKDRRAIHWGAYMGHIEVVKLLVTHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNE 234
Cdd:PHA02876   160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINK 239

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  235 P-----NAYGNTPLHVACYngqdvvvneLIDCGANVNQMNERGFTPLHFAAASTHGALCLELLVCNGADVNMKSKDGKTP 309
Cdd:PHA02876   240 NdlsllKAIRNEDLETSLL---------LYDAGFSVNSIDDCKNTPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETP 310

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  310 LHMTAIHGRFSRS-QTIIQNGAEIDCEDKNGNTPLHIAAryghellintlitsgadtakrgvhgmfplhlaALSGFSDCC 388
Cdd:PHA02876   311 LYLMAKNGYDTENiRTLIMLGADVNAADRLYITPLHQAS--------------------------------TLDRNKDIV 358

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  389 RKLLSsgfdidtpddfgrtclhaaaaggnleclnlllnTGADFNKKDKFGRTPLHYAAANCNYQCLFALVGSGASVNDLD 468
Cdd:PHA02876   359 ITLLE---------------------------------LGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALS 405

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 2092232601  469 ERGCTPLHYAAASDTDGKCLEYLLRNDANPGIRDKQGYNAVHYS 512
Cdd:PHA02876   406 QKIGTALHFALCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYA 449
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 30-317 4.12e-21

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 98.03  E-value: 4.12e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601   30 KKEDVNFQDNEKRT---------PLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQVLLK----- 95
Cdd:PHA02878    17 LKYIEYIDHTENYStsaslipfiPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRsinkc 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601   96 -------------HSADVNA-------RDKNWQTP--LHIAAANKAVKCAEALVPLL----SNVNVSDR-AGRTALHHAA 148
Cdd:PHA02878    97 svfytlvaikdafNNRNVEIfkiiltnRYKNIQTIdlVYIDKKSKDDIIEAEITKLLlsygADINMKDRhKGNTALHYAT 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  149 FSGHVEMVSLLLSRGANINAFDKKDRRAIHWGAYMGHIEVVKLLVTHGAEVTCKDKKSYTPLHAAASSGM-ISVVKYLLD 227
Cdd:PHA02878   177 ENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKdYDILKLLLE 256

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  228 LGVDMN-EPNAYGNTPLHVACYNGQdvVVNELIDCGANVNQMNERGFTPLHFAAASTHGALCLELLVCNGADVNMKSKDG 306
Cdd:PHA02878   257 HGVDVNaKSYILGLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPLSSAVKQYLCINIGRILISNICLLKRIKPDI 334

                          330
                   ....*....|....*
gi 2092232601  307 KTPL----HMTAIHG 317
Cdd:PHA02878   335 KNSEgfidNMDCITS 349
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 554-863 5.85e-21

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 96.96  E-value: 5.85e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  554 LHLAAYHGHHQALEVLVQS---LLDLDVRNNNgrTPLDLAAFKGHVECVDVLINQGASILVKDYVVKRtPIHAAATNGHS 630
Cdd:PHA02874     5 LRMCIYSGDIEAIEKIIKNkgnCINISVDETT--TPLIDAIRSGDAKIVELFIKHGADINHINTKIPH-PLLTAIKIGAH 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  631 ECLRLLIGNAEPQNAVDIQDGNGQTplmlsvlnghtdcVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVEALLQHGA 710
Cdd:PHA02874    82 DIIKLLIDNGVDTSILPIPCIEKDM-------------IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGA 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  711 KSLLRDCRGRTPIHLSAACGHIGVLGALLQSAtsvdAVPAIADNHGYTSLHWACYNGHDSCVELLLEQ--EVFQKMEgNS 788
Cdd:PHA02874   149 DVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKG----AYANVKDNNGESPLHNAAEYGDYACIKLLIDHgnHIMNKCK-NG 223

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2092232601  789 FSPLHCAVINdNEGAAEMLIDTlgaGIVNSTDAKGRTPLH-AAAFTDHVECLQLLLSHNAQVNAVDSSGKTPLMMA 863
Cdd:PHA02874   224 FTPLHNAIIH-NRSAIELLINN---ASINDQDIDGSTPLHhAINPPCDIDIIDILLYHKADISIKDNKGENPIDTA 295
Ank_2 pfam12796
Ankyrin repeats (3 copies);
78-170 3.89e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.94  E-value: 3.89e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601   78 LHRAVASCSEDAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLsNVNVSDRaGRTALHHAAFSGHVEMVS 157
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKDN-GRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 2092232601  158 LLLSRGANINAFD 170
Cdd:pfam12796   79 LLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
9-144 4.33e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 91.94  E-value: 4.33e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601    9 QPLLVQAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSED 88
Cdd:COG0666    154 NTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLE 233

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2092232601   89 AVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTAL 144
Cdd:COG0666    234 IVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
12-104 5.07e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.86  E-value: 5.07e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601   12 LVQAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLiLSGARVNAKDSKWlTPLHRAVASCSEDAVQ 91
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL-LEHADVNLKDNGR-TALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 2092232601   92 VLLKHSADVNARD 104
Cdd:pfam12796   79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
111-203 5.70e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.47  E-value: 5.70e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  111 LHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHVEMVSLLLSRgANINAFDkKDRRAIHWGAYMGHIEVVK 190
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 2092232601  191 LLVTHGAEVTCKD 203
Cdd:pfam12796   79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
177-269 5.76e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.47  E-value: 5.76e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  177 IHWGAYMGHIEVVKLLVTHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDlGVDMNEPNaYGNTPLHVACYNGQDVVVN 256
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 2092232601  257 ELIDCGANVNQMN 269
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 653-982 9.76e-19

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 90.47  E-value: 9.76e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  653 GQTPLMLSVLNGHTDC---VYSLLNKGANVDAKDKWGRTALH---RGAVTghEECVEALLQHGAKSLLRDCRGRTPIH-- 724
Cdd:PHA03095    47 GKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLHlylYNATT--LDVIKLLIKAGADVNAKDKVGRTPLHvy 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  725 LSAACGHIGVLGALLQSATSVDAVpaiaDNHGYTSLHwACYNGHDSCVELLleqevfqkmegnsfsplhcavindnegaa 804
Cdd:PHA03095   125 LSGFNINPKVIRLLLRKGADVNAL----DLYGMTPLA-VLLKSRNANVELL----------------------------- 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  805 EMLIDTlGAGIVNsTDAKGRTPLH--AAAFTDHVECLQLLLSHNAQVNAVDSSGKTPLMMAAengqtntvevLVSSAKAD 882
Cdd:PHA03095   171 RLLIDA-GADVYA-VDDRFRSLLHhhLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMA----------TGSSCKRS 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  883 LTLQdsskntalhlacskghetsallILEKITDrnlINATNAALQTPLHVAARNGLTVVVQELLGKGASVLAVDENGYTP 962
Cdd:PHA03095   239 LVLP----------------------LLIAGIS---INARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTP 293

                          330       340
                   ....*....|....*....|
gi 2092232601  963 ALACAPNKDVaDCLALILAT 982
Cdd:PHA03095   294 LSLMVRNNNG-RAVRAALAK 312
Ank_2 pfam12796
Ankyrin repeats (3 copies);
210-302 1.87e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 81.32  E-value: 1.87e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  210 LHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCgANVNqMNERGFTPLHFAAASTHGAlCL 289
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVN-LKDNGRTALHYAARSGHLE-IV 77

                           90
                   ....*....|...
gi 2092232601  290 ELLVCNGADVNMK 302
Cdd:pfam12796   78 KLLLEKGADINVK 90
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 42-304 2.70e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 88.51  E-value: 2.70e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601   42 RTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQVLLKHSADVNARDKNWQTPLHIAAANKAVK 121
Cdd:PHA02875     3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  122 CAEALvpLLSNVNVSD---RAGRTALHHAAFSGHVEMVSLLLSRGANINAFDKKDRRAIHWGAYMGHIEVVKLLVTHGAE 198
Cdd:PHA02875    83 AVEEL--LDLGKFADDvfyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKAC 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  199 VTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDmnePNAYGNTP-LHVACY---NGQDVVVNELIDCGANVNQMnergft 274
Cdd:PHA02875   161 LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGAN---IDYFGKNGcVAALCYaieNNKIDIVRLFIKRGADCNIM------ 231

                          250       260       270
                   ....*....|....*....|....*....|
gi 2092232601  275 plhfaaASTHGALCLELLVCNGADVNMKSK 304
Cdd:PHA02875   232 ------FMIEGEECTILDMICNMCTNLESE 255
Ank_2 pfam12796
Ankyrin repeats (3 copies);
621-716 4.07e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.16  E-value: 4.07e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  621 IHAAATNGHSECLRLLIgnaEPQNAVDIQDGNGQTPLMLSVLNGHTDCVYSLLNKgANVDAKDKwGRTALHRGAVTGHEE 700
Cdd:pfam12796    1 LHLAAKNGNLELVKLLL---ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLE 75

                           90
                   ....*....|....*.
gi 2092232601  701 CVEALLQHGAKSLLRD 716
Cdd:pfam12796   76 IVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
587-683 4.27e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.16  E-value: 4.27e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  587 LDLAAFKGHVECVDVLINQGASILVKDyVVKRTPIHAAATNGHSECLRLLIGNAEPQNavdiqDGNGQTPLMLSVLNGHT 666
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQD-KNGRTALHLAAKNGHLEIVKLLLEHADVNL-----KDNGRTALHYAARSGHL 74

                           90
                   ....*....|....*..
gi 2092232601  667 DCVYSLLNKGANVDAKD 683
Cdd:pfam12796   75 EIVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 389-748 4.12e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 85.46  E-value: 4.12e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  389 RKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECL---NLLLNTGADFNKKDKFGRTPLH-YAAANCNYQCLFALVGSGASV 464
Cdd:PHA03095    31 RRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKdivRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADV 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  465 NDLDERGCTPLH-YAAASDTDGKCLEYLLRNDANPGIRDKqgynavhysaaYGHrlcleliaseTPLDVLMETSGTDMln 543
Cdd:PHA03095   111 NAKDKVGRTPLHvYLSGFNINPKVIRLLLRKGADVNALDL-----------YGM----------TPLAVLLKSRNANV-- 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  544 dsdnrapisplhlaayhghhQALEVLVQSLLDLDVRNNNGRTPLD--LAAFKGHVECVDVLINQGASILVKDyVVKRTPI 621
Cdd:PHA03095   168 --------------------ELLRLLIDAGADVYAVDDRFRSLLHhhLQSFKPRARIVRELIRAGCDPAATD-MLGNTPL 226

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  622 HAAATngHSECLRLLIGNaepqnavdiqdgngqtplmlsvlnghtdcvysLLNKGANVDAKDKWGRTALHRGAVTGHEEC 701
Cdd:PHA03095   227 HSMAT--GSSCKRSLVLP--------------------------------LLIAGISINARNRYGQTPLHYAAVFNNPRA 272

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 2092232601  702 VEALLQHGAKSLLRDCRGRTPIHLSAACGHIGVLGALLQSATSVDAV 748
Cdd:PHA03095   273 CRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETV 319
Ank_2 pfam12796
Ankyrin repeats (3 copies);
827-920 1.11e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.92  E-value: 1.11e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  827 LHAAAFTDHVECLQLLLSHNAQVNAVDSSGKTPLMMAAENGQTNTVEVLVSSAKADLTLQDsskNTALHLACSKGHETSA 906
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNG---RTALHYAARSGHLEIV 77

                           90
                   ....*....|....
gi 2092232601  907 LLILEKITDRNLIN 920
Cdd:pfam12796   78 KLLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 11-193 1.78e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 83.09  E-value: 1.78e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601   11 LLVQAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAV 90
Cdd:PHA02874   127 FLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACI 206

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601   91 QVLLKHSADVNARDKNWQTPLHIAAA-NKAVkcaealVPLLSN---VNVSDRAGRTALHHA-AFSGHVEMVSLLLSRGAN 165
Cdd:PHA02874   207 KLLIDHGNHIMNKCKNGFTPLHNAIIhNRSA------IELLINnasINDQDIDGSTPLHHAiNPPCDIDIIDILLYHKAD 280

                          170       180
                   ....*....|....*....|....*....
gi 2092232601  166 INAFDKKDRRAIHWG-AYMGHIEVVKLLV 193
Cdd:PHA02874   281 ISIKDNKGENPIDTAfKYINKDPVIKDII 309
Ank_2 pfam12796
Ankyrin repeats (3 copies);
657-747 2.73e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.15  E-value: 2.73e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  657 LMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVEALLQHGAKSLlrDCRGRTPIHLSAACGHIGVLG 736
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|.
gi 2092232601  737 ALLQSATSVDA 747
Cdd:pfam12796   79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
554-647 2.89e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.77  E-value: 2.89e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  554 LHLAAYHGHHQALEVLVQSLLDLDVRNNNGRTPLDLAAFKGHVECVDVLINQGAsilVKDYVVKRTPIHAAATNGHSECL 633
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD---VNLKDNGRTALHYAARSGHLEIV 77

                           90
                   ....*....|....
gi 2092232601  634 RLLIGNAEPQNAVD 647
Cdd:pfam12796   78 KLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 427-684 3.63e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 82.02  E-value: 3.63e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  427 TGADFNKKDKFGRTPLHYAA-----ANCNYQCLFALVGSGASVNDLDERGCTPLHYAAASD-TDGKCLEYLLRNDANPGI 500
Cdd:PHA03100    57 NGADINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKKsNSYSIVEYLLDNGANVNI 136

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  501 RDKQGYNAVHYSAAYGHRlclELIASETPLDvlmetSGTDMlnDSDNRapisplhlaayhghhqaLEVLVQSLLDLDVRN 580
Cdd:PHA03100   137 KNSDGENLLHLYLESNKI---DLKILKLLID-----KGVDI--NAKNR-----------------VNYLLSYGVPINIKD 189

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  581 NNGRTPLDLAAFKGHVECVDVLINQGASIlvkdyvvkrtpihaaatnghseclrllignaepqNAVDIqdgNGQTPLMLS 660
Cdd:PHA03100   190 VYGFTPLHYAVYNNNPEFVKYLLDLGANP----------------------------------NLVNK---YGDTPLHIA 232

                          250       260
                   ....*....|....*....|....
gi 2092232601  661 VLNGHTDCVYSLLNKGANVDAKDK 684
Cdd:PHA03100   233 ILNNNKEIFKLLLNNGPSIKTIIE 256
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 428-865 4.87e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 83.19  E-value: 4.87e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  428 GADFNKKDKFGRTPLHYAAANCNYQCLFALVGSGASVNDLDERGCTPLHYAAASDtDGKCLEYLLRNDANPGIRDKQGYN 507
Cdd:PHA02876   168 GADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSK-NIDTIKAIIDNRSNINKNDLSLLK 246

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  508 AVHYSAAyghrlcleliasETPLDVLMETSGTDMLNDSDNrapiSPLHLAAyhgHHQALEVLVQSLL----DLDVRNNNG 583
Cdd:PHA02876   247 AIRNEDL------------ETSLLLYDAGFSVNSIDDCKN----TPLHHAS---QAPSLSRLVPKLLergaDVNAKNIKG 307

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  584 RTPLDLAAFKGH-VECVDVLINQGASILVKDYVVKrTPIHAAATnghseclrllignaepqnavdiqdgngqtplmlsvL 662
Cdd:PHA02876   308 ETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYI-TPLHQAST-----------------------------------L 351

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  663 NGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVEALLQHGAKsllrdcrgrtpihLSAACGHIGvlgallqsa 742
Cdd:PHA02876   352 DRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGAD-------------IEALSQKIG--------- 409

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  743 tsvdavpaiadnhgyTSLHWACYNghdscvellleqevfqkmeGNSFSplhcavindnegAAEMLIDTlGAGiVNSTDAK 822
Cdd:PHA02876   410 ---------------TALHFALCG-------------------TNPYM------------SVKTLIDR-GAN-VNSKNKD 441

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....
gi 2092232601  823 GRTPLHAAAFTD-HVECLQLLLSHNAQVNAVDSSGKTPLMMAAE 865
Cdd:PHA02876   442 LSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIALE 485
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 8-220 9.69e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 82.03  E-value: 9.69e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601    8 EQPLLVQAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLG-DAEIIELLILSGARVNAKDSKWLTPLHRAVASCS 86
Cdd:PHA02876   308 ETPLYLMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNN 387

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601   87 EDAVQVLLKHSADVNARDKNWQTPLHIA-AANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSG-HVEMVSLLLSRGA 164
Cdd:PHA02876   388 VVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGA 467

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2092232601  165 NINAFDKKDRRAIHWGayMGHIEVVKLLVTHGAEVtcKDKKSytpLHAAASSGMIS 220
Cdd:PHA02876   468 DVNAINIQNQYPLLIA--LEYHGIVNILLHYGAEL--RDSRV---LHKSLNDNMFS 516
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 209-523 1.13e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 81.08  E-value: 1.13e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  209 PLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIdcgANVNQmNERGFTplhFAAASThgalc 288
Cdd:PHA02878    40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMI---RSINK-CSVFYT---LVAIKD----- 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  289 lellVCNGADVNMKSkdgktplhmTAIHGRFSRSQTIiqNGAEIDCEDKNGNTPLHIaaryghellINTLITSGADTAKR 368
Cdd:PHA02878   108 ----AFNNRNVEIFK---------IILTNRYKNIQTI--DLVYIDKKSKDDIIEAEI---------TKLLLSYGADINMK 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  369 GVH-GMFPLHLAALSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGADFNKKDKFGRTPLHYAAA 447
Cdd:PHA02878   164 DRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVG 243

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2092232601  448 NC-NYQCLFALVGSGASVNDLDE-RGCTPLHYAAASDtdgKCLEYLLRNDANPGIRDkqGYNAVHYSAAYGHRLCLEL 523
Cdd:PHA02878   244 YCkDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSE---RKLKLLLEYGADINSLN--SYKLTPLSSAVKQYLCINI 316
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 33-198 1.14e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 80.42  E-value: 1.14e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601   33 DVNFQDneKRTPLHAAAYLGDAEIIELLILSGARVN-AKDSKWLTPLHRAVASCSEDAVQVLLKHSADVNARDKNWQTPL 111
Cdd:PHA02875    62 DVKYPD--IESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPL 139

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  112 HIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHVEMVSLLLSRGANINAFDKK-DRRAIHWGAYMGHIEVVK 190
Cdd:PHA02875   140 HLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNgCVAALCYAIENNKIDIVR 219


                   ....*...
gi 2092232601  191 LLVTHGAE 198
Cdd:PHA02875   220 LFIKRGAD 227
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 24-195 1.24e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 81.08  E-value: 1.24e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601   24 VRALIFKKEDVNFQDNEK-RTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQVLLKHSADVNA 102
Cdd:PHA02878   150 TKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  103 RDKNWQTPLHIAAAnkAVKCAEALVPLL---SNVNV-SDRAGRTALHHAAFSGHVemVSLLLSRGANINA--FDKKDRRA 176
Cdd:PHA02878   230 RDKCGNTPLHISVG--YCKDYDILKLLLehgVDVNAkSYILGLTALHSSIKSERK--LKLLLEYGADINSlnSYKLTPLS 305

                          170
                   ....*....|....*....
gi 2092232601  177 IHWGAYMGhIEVVKLLVTH 195
Cdd:PHA02878   306 SAVKQYLC-INIGRILISN 323
Ank_2 pfam12796
Ankyrin repeats (3 copies);
760-853 2.30e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.46  E-value: 2.30e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  760 LHWACYNGHDSCVELLLEQEV-FQKMEGNSFSPLHCAVINDNEGAAEMLIDTLGAGIVNstdaKGRTPLHAAAFTDHVEC 838
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGAdANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD----NGRTALHYAARSGHLEI 76

                           90
                   ....*....|....*
gi 2092232601  839 LQLLLSHNAQVNAVD 853
Cdd:pfam12796   77 VKLLLEKGADINVKD 91
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 30-201 3.26e-15

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 80.68  E-value: 3.26e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601   30 KKEDVNFQDNEKRTPLHAAAYL------GDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQVLLKHSADVNAR 103
Cdd:PLN03192   508 NVGDLLGDNGGEHDDPNMASNLltvastGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIR 587

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  104 DKNWQTPLHIAAANKAVKCAEALVPLLSnvnVSD-RAGRTALHHAAFSGHVEMVSLLLSRGANINAFDKKDRRAIHWGAY 182
Cdd:PLN03192   588 DANGNTALWNAISAKHHKIFRILYHFAS---ISDpHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMA 664

                          170
                   ....*....|....*....
gi 2092232601  183 MGHIEVVKLLVTHGAEVTC 201
Cdd:PLN03192   665 EDHVDMVRLLIMNGADVDK 683
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 672-957 3.43e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 80.11  E-value: 3.43e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  672 LLNKGANVDAKDKWGRTALHRGAVTGHEECVEALLQHGAKSLLRDCRGRTPIHLSAacghigvlgallqSATSVDAVPAI 751
Cdd:PHA02876   164 LLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAV-------------DSKNIDTIKAI 230

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  752 ADNHgytslhwacynghdscvellleqevfQKMEGNSFSPLHcAVINDNEGAAEMLIDtlgAGI-VNSTDAKGRTPLHAA 830
Cdd:PHA02876   231 IDNR--------------------------SNINKNDLSLLK-AIRNEDLETSLLLYD---AGFsVNSIDDCKNTPLHHA 280

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  831 AFTDHVECL-QLLLSHNAQVNAVDSSGKTPLMMAAENG-QTNTVEVLVSSAkADLTLQDSSKNTALHLACSKGHETSALL 908
Cdd:PHA02876   281 SQAPSLSRLvPKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLG-ADVNAADRLYITPLHQASTLDRNKDIVI 359

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 2092232601  909 ILEKITDRnlINATNAALQTPLHVAARNGLTVVVQELLGKGASVLAVDE 957
Cdd:PHA02876   360 TLLELGAN--VNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQ 406
PHA02798 PHA02798
ankyrin-like protein; Provisional
 55-318 6.03e-15

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 78.72  E-value: 6.03e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601   55 EIIELLILSGARVNAKDSKWLTPLHRAVASCSE-----DAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPL 129
Cdd:PHA02798    52 DIVKLFINLGANVNGLDNEYSTPLCTILSNIKDykhmlDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLFM 131

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  130 LSN---VNVSDRAGRTALHHAAFSGH---VEMVSLLLSRGANINAFDkkdrraiHWGAYmghievvkllvthgAEVTCKD 203
Cdd:PHA02798   132 IENgadTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINTHN-------NKEKY--------------DTLHCYF 190

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  204 KKSYTPLHAaassgmiSVVKYLLDLGVDMNEPNAYGNTP----LHVACYNGQDVVVN--ELIDCGANVNQMNERGFTPLH 277
Cdd:PHA02798   191 KYNIDRIDA-------DILKLFVDNGFIINKENKSHKKKfmeyLNSLLYDNKRFKKNilDFIFSYIDINQVDELGFNPLY 263

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 2092232601  278 FAAASTHGALClELLVCNGADVNMKSKDGKTPLhMTAIHGR 318
Cdd:PHA02798   264 YSVSHNNRKIF-EYLLQLGGDINIITELGNTCL-FTAFENE 302
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 531-710 1.43e-14

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 78.37  E-value: 1.43e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  531 DVLMETSGTDmlndsDNRAPISPLHLAAYHGHHQALEVLVQSLLDLDVRNNNGRTPLDLAAFKGHVECVDVLINQGASIL 610
Cdd:PLN03192   511 DLLGDNGGEH-----DDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVH 585

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  611 VKDyVVKRTPIHAAATNGHSECLRLLIGNA---EPQNAVDIqdgngqtpLMLSVLNGHTDCVYSLLNKGANVDAKDKWGR 687
Cdd:PLN03192   586 IRD-ANGNTALWNAISAKHHKIFRILYHFAsisDPHAAGDL--------LCTAAKRNDLTAMKELLKQGLNVDSEDHQGA 656

                          170       180
                   ....*....|....*....|...
gi 2092232601  688 TALHRGAVTGHEECVEALLQHGA 710
Cdd:PLN03192   657 TALQVAMAEDHVDMVRLLIMNGA 679
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 74-281 2.28e-14

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: 77.36  E-value: 2.28e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601   74 WLTPLHRAVASCSEDAVQVLLK-HSADVNARDKNWQTPLHIAAANKAVKCAEAL---VPLLSNVNV-SD-RAGRTALHHA 147
Cdd:cd22192     17 SESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLmeaAPELVNEPMtSDlYQGETALHIA 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  148 AFSGHVEMVSLLLSRGANIN-------AFDKKDRRAIHWGAYmghievvkllvthgaevtckdkksytPLHAAASSGMIS 220
Cdd:cd22192     97 VVNQNLNLVRELIARGADVVspratgtFFRPGPKNLIYYGEH--------------------------PLSFAACVGNEE 150

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2092232601  221 VVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDC----GANVNQM------NERGFTPLHFAAA 281
Cdd:cd22192    151 IVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFACQMYDLilsyDKEDDLQpldlvpNNQGLTPFKLAAK 221
PHA03095 PHA03095
ankyrin-like protein; Provisional
 17-168 3.00e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 76.60  E-value: 3.00e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601   17 FNGDPDEVRALIFKKEDVNFQDNEKRTPLHaaAYLG----DAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDA--V 90
Cdd:PHA03095   128 FNINPKVIRLLLRKGADVNALDLYGMTPLA--VLLKsrnaNVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRAriV 205

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601   91 QVLLKHSADVNARDKNWQTPLHIAAANKAVKcAEALVPLLSN---VNVSDRAGRTALHHAAFSGHVEMVSLLLSRGANIN 167
Cdd:PHA03095   206 RELIRAGCDPAATDMLGNTPLHSMATGSSCK-RSLVLPLLIAgisINARNRYGQTPLHYAAVFNNPRACRRLIALGADIN 284


                   .
gi 2092232601  168 A 168
Cdd:PHA03095   285 A 285
Ank_2 pfam12796
Ankyrin repeats (3 copies);
310-402 5.20e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.60  E-value: 5.20e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  310 LHMTAIHGRFSRSQTIIQNGAEIDCEDKNGNTPLHIAARYGHELLINTLITSGAdtAKRGVHGMFPLHLAALSGFSDCCR 389
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 2092232601  390 KLLSSGFDIDTPD 402
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 772-958 1.11e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 74.32  E-value: 1.11e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  772 VELLLEQ--EVFQKMEGNSfSPLH-----CAVINDNEGAAEMLIDtLGAgIVNSTDAKGRTPLHAAAFT--DHVECLQLL 842
Cdd:PHA03100    51 VKILLDNgaDINSSTKNNS-TPLHylsniKYNLTDVKEIVKLLLE-YGA-NVNAPDNNGITPLLYAISKksNSYSIVEYL 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  843 LSHNAQVNAVDSSGKTPLMMAAENGQ--TNTVEVLVSSaKADLTLQDSSK----------------NTALHLACSKGHET 904
Cdd:PHA03100   128 LDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDK-GVDINAKNRVNyllsygvpinikdvygFTPLHYAVYNNNPE 206

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2092232601  905 SALLILEKITDRNLINATNaalQTPLHVAARNGLTVVVQELLGKGASVLAVDEN 958
Cdd:PHA03100   207 FVKYLLDLGANPNLVNKYG---DTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 765-969 1.40e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 73.93  E-value: 1.40e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  765 YNGHDSCVELLLEQEVFQKMEGNSFS------PLHCAVINDNEGAAEMLIDTlGAGIvNSTDAKGRTPLH-----AAAFT 833
Cdd:PHA03100     6 VLTKSRIIKVKNIKYIIMEDDLNDYSykkpvlPLYLAKEARNIDVVKILLDN-GADI-NSSTKNNSTPLHylsniKYNLT 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  834 DHVECLQLLLSHNAQVNAVDSSGKTPLMMAAEN--GQTNTVEVLVSSAkADLTLQDSSKNTALHLACSKGHETSAL--LI 909
Cdd:PHA03100    84 DVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNG-ANVNIKNSDGENLLHLYLESNKIDLKIlkLL 162

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2092232601  910 LEKITDRNL-------------INATNAALQTPLHVAARNGLTVVVQELLGKGASVLAVDENGYTPA-LACAPN 969
Cdd:PHA03100   163 IDKGVDINAknrvnyllsygvpINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLhIAILNN 236
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 352-740 1.72e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 74.71  E-value: 1.72e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  352 ELLI-NTLITSGADTAKRGVHGMFPLHLAALSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGAD 430
Cdd:PHA02876   157 ELLIaEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSN 236

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  431 FNKKDkfgrTPLHYAAANCNYQCLFALVGSGASVNDLDERGCTPLHYAAASDTDGKCLEYLLRNDANPGIRDKQGynavh 510
Cdd:PHA02876   237 INKND----LSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLVPKLLERGADVNAKNIKG----- 307

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  511 ysaayghrlcleliasETPLdVLMETSGTDMLNdsdnrapisplhlaayhghhqaLEVLVQSLLDLDVRNNNGRTPLDLA 590
Cdd:PHA02876   308 ----------------ETPL-YLMAKNGYDTEN----------------------IRTLIMLGADVNAADRLYITPLHQA 348

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  591 A-FKGHVECVDVLINQGASILVKDYvVKRTPIHAAATNGHSECLRLLIGNAEPQNAVDIQDGN-------GQTPLMlsvl 662
Cdd:PHA02876   349 StLDRNKDIVITLLELGANVNARDY-CDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTalhfalcGTNPYM---- 423

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2092232601  663 nghtdCVYSLLNKGANVDAKDKWGRTALHRGAVTGHE-ECVEALLQHGAKSLLRDCRGRTPihLSAACGHIGVLGALLQ 740
Cdd:PHA02876   424 -----SVKTLIDRGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAINIQNQYP--LLIALEYHGIVNILLH 495
PHA03095 PHA03095
ankyrin-like protein; Provisional
 18-214 2.10e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 73.91  E-value: 2.10e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601   18 NGDPDEVRALIFKKEDVNFQDNEKRTPLH--AAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQV--L 93
Cdd:PHA03095   164 NANVELLRLLIDAGADVYAVDDRFRSLLHhhLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpL 243

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601   94 LKHSADVNARDKNWQTPLHIAAA-NKAVKCAEaLVPLLSNVNVSDRAGRTALHHAAFSGHVEMVSLLLSRGANINAFDKK 172
Cdd:PHA03095   244 LIAGISINARNRYGQTPLHYAAVfNNPRACRR-LIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAAT 322

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2092232601  173 DRRAIHWGAYMG----HIEVVKLLVTHGAEVtckDKKSYTPLHAAA 214
Cdd:PHA03095   323 LNTASVAGGDIPsdatRLCVAKVVLRGAFSL---LPEPIRAYHADF 365
Ank_2 pfam12796
Ankyrin repeats (3 copies);
860-956 3.69e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.91  E-value: 3.69e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  860 LMMAAENGQTNTVEVLVSSaKADLTLQDSSKNTALHLACSKGHETSALLILEKItDRNLINATNaalqTPLHVAARNGLT 939
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLEN-GADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKDNGR----TALHYAARSGHL 74

                           90
                   ....*....|....*..
gi 2092232601  940 VVVQELLGKGASVLAVD 956
Cdd:pfam12796   75 EIVKLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 540-748 3.95e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 72.78  E-value: 3.95e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  540 DMLNDSDNRAPISPLHLAAYHGHHQALEVLVQSLLDLDVRNNNGRTPLDLAAFKGHV-----ECVDVLINQGASILVKDY 614
Cdd:PHA03100    25 DDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDN 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  615 VvKRTPIHAAATN--GHSECLRLLIGNAEPQNAVDiqdGNGQTPLMLSVLNGHTDC------------------VYSLLN 674
Cdd:PHA03100   105 N-GITPLLYAISKksNSYSIVEYLLDNGANVNIKN---SDGENLLHLYLESNKIDLkilkllidkgvdinaknrVNYLLS 180

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2092232601  675 KGANVDAKDKWGRTALHRGAVTGHEECVEALLQHGAKSLLRDCRGRTPIHLSAACGHIGVLGALLQSATSVDAV 748
Cdd:PHA03100   181 YGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTI 254
Ank_2 pfam12796
Ankyrin repeats (3 copies);
243-336 4.52e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.91  E-value: 4.52e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  243 LHVACYNGQDVVVNELIDCGANVNQMNERGFTPLHFAAASTHGALCLELLvcNGADVNMKSkDGKTPLHMTAIHGRFSRS 322
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL--EHADVNLKD-NGRTALHYAARSGHLEIV 77

                           90
                   ....*....|....
gi 2092232601  323 QTIIQNGAEIDCED 336
Cdd:pfam12796   78 KLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
376-468 5.50e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.52  E-value: 5.50e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  376 LHLAALSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTgADFNKKDKfGRTPLHYAAANCNYQCLF 455
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 2092232601  456 ALVGSGASVNDLD 468
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 655-854 1.46e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 70.85  E-value: 1.46e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  655 TPLMLSVLNGHT-----DCVYSLLNKGANVDAKDKWGRTALHRGAVT--GHEECVEALLQHGAKSLLRDCRGRTPIHLSA 727
Cdd:PHA03100    70 TPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYL 149

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  728 ACGHI--GVLGALLQSATSVDA-----------VPA-IADNHGYTSLHWACYNGHDSCVELLLEqevfqkmegnsfsplh 793
Cdd:PHA03100   150 ESNKIdlKILKLLIDKGVDINAknrvnyllsygVPInIKDVYGFTPLHYAVYNNNPEFVKYLLD---------------- 213

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2092232601  794 cavindnegaaemlidtLGAGIvNSTDAKGRTPLHAAAFTDHVECLQLLLSHNAQVNAVDS 854
Cdd:PHA03100   214 -----------------LGANP-NLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
PHA02798 PHA02798
ankyrin-like protein; Provisional
 186-412 1.75e-12

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 71.02  E-value: 1.75e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  186 IEVVKLLVTHGAEVTCKDKKSYTPLHAAASS-----GMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGqdvVVNEL-- 258
Cdd:PHA02798    51 TDIVKLFINLGANVNGLDNEYSTPLCTILSNikdykHMLDIVKILIENGADINKKNSDGETPLYCLLSNG---YINNLei 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  259 ----IDCGANVNQMNERGFTPLHFAAASTHGAL--CLELLVCNGADVNMKS-KDGKTPLHmTAIHGRFSR-----SQTII 326
Cdd:PHA02798   128 llfmIENGADTTLLDKDGFTMLQVYLQSNHHIDieIIKLLLEKGVDINTHNnKEKYDTLH-CYFKYNIDRidadiLKLFV 206

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  327 QNGAEIDCEDKNGNTPLhiaARYGHELLINT---------LITSGADTAKRGVHGMFPLHLAALSGFSDCCRKLLSSGFD 397
Cdd:PHA02798   207 DNGFIINKENKSHKKKF---MEYLNSLLYDNkrfkknildFIFSYIDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGD 283

                          250
                   ....*....|....*
gi 2092232601  398 IDTPDDFGRTCLHAA 412
Cdd:PHA02798   284 INIITELGNTCLFTA 298
Ank_2 pfam12796
Ankyrin repeats (3 copies);
276-364 3.68e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.21  E-value: 3.68e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  276 LHFAAASTHgALCLELLVCNGADVNMKSKDGKTPLHMTAIHGRFSRSQTIIQNgAEIDCEDkNGNTPLHIAARYGHELLI 355
Cdd:pfam12796    1 LHLAAKNGN-LELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77


                   ....*....
gi 2092232601  356 NTLITSGAD 364
Cdd:pfam12796   78 KLLLEKGAD 86
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 600-952 4.31e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 70.09  E-value: 4.31e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  600 DVLINQGASILVKDyVVKRTPIHAAATNGHSECLRLLIGNAEPQNAVDIqdgNGQTPLMLSVLNGHTDCVYSLLNKGANV 679
Cdd:PHA02876   162 EMLLEGGADVNAKD-IYCITPIHYAAERGNAKMVNLLLSYGADVNIIAL---DDLSVLECAVDSKNIDTIKAIIDNRSNI 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  680 DAKDkwgrtaLHRGAVTGHEECVEALLQHGAK---SLLRDCRGrTPIHLSAACGHIGVL-GALLQSATSVDAvpaiADNH 755
Cdd:PHA02876   238 NKND------LSLLKAIRNEDLETSLLLYDAGfsvNSIDDCKN-TPLHHASQAPSLSRLvPKLLERGADVNA----KNIK 306

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  756 GYTSLHWACYNGHDS--CVELLLEQEVFQKMEGNSFSPLHCAVINDNEGAAEMLIDTLGAGiVNSTDAKGRTPLHAAAFT 833
Cdd:PHA02876   307 GETPLYLMAKNGYDTenIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVITLLELGAN-VNARDYCDKTPIHYAAVR 385

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  834 DHVECLQLLLSHNAQVNAVDSSGKTPLMMA--AENGQTnTVEVLVSSAkADLTLQDSSKNTALHLACSKGHETSAL-LIL 910
Cdd:PHA02876   386 NNVVIINTLLDYGADIEALSQKIGTALHFAlcGTNPYM-SVKTLIDRG-ANVNSKNKDLSTPLHYACKKNCKLDVIeMLL 463

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|..
gi 2092232601  911 EKITDRNLINATNaalQTPLHVAArnGLTVVVQELLGKGASV 952
Cdd:PHA02876   464 DNGADVNAINIQN---QYPLLIAL--EYHGIVNILLHYGAEL 500
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 310-690 7.71e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 68.84  E-value: 7.71e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  310 LHMTAIHGRFSRSQTIIQN-GAEIDCEDKNGNTPLHIAARYGHELLINTLITSGADTAKRGVHGMFPLHLAALSGFSDCC 388
Cdd:PHA02874     5 LRMCIYSGDIEAIEKIIKNkGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDII 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  389 RKLLSSGFDI------DTPDDFGRTCLHaaaaggnleclnlllnTGADFNKKDKFGRTPLHYAAANCNYQCLFALVGSGA 462
Cdd:PHA02874    85 KLLIDNGVDTsilpipCIEKDMIKTILD----------------CGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGA 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  463 SVNDLDERGCTPLHyaaasdtdgkcleyllrndanpgirdkqgynavhysaayghrlcleliasetpldvlmetsgtdml 542
Cdd:PHA02874   149 DVNIEDDNGCYPIH------------------------------------------------------------------ 162

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  543 ndsdnrapisplhLAAYHGHHQALEVLVQSLLDLDVRNNNGRTPLDLAAFKGHVECVDVLINQGASILVKdyvVKR--TP 620
Cdd:PHA02874   163 -------------IAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNK---CKNgfTP 226

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2092232601  621 IHAAATNGHSeCLRLLIGNAepqnAVDIQDGNGQTPLMLSV-LNGHTDCVYSLLNKGANVDAKDKWGRTAL 690
Cdd:PHA02874   227 LHNAIIHNRS-AIELLINNA----SINDQDIDGSTPLHHAInPPCDIDIIDILLYHKADISIKDNKGENPI 292
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 670-969 1.17e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 68.94  E-value: 1.17e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  670 YSLLNKGANVDAKDKWGRTALHRGAVTGHEECVEALLQHGAKSL-LRDCRGRTPIHlsAACGHIGVLGALLQSATSVDAV 748
Cdd:PHA02876    25 YDLHKHGANQCENESIPFTAIHQALQLRQIDIVEEIIQQNPELIyITDHKCHSTLH--TICIIPNVMDIVISLTLDCDII 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  749 PAIAdnhgYTSLHWACYNGHDSCVELLleqevfqkMEGNSFSPLHCAVIN---------------DNEGAAEMLIDtlGA 813
Cdd:PHA02876   103 LDIK----YASIILNKHKLDEACIHIL--------KEAISGNDIHYDKINesieymklikeriqqDELLIAEMLLE--GG 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  814 GIVNSTDAKGRTPLHAAAFTDHVECLQLLLSHNAQVNAVDSSGKTPLMMAAENGQTNTVEVLVSSA----KADLTLQDSS 889
Cdd:PHA02876   169 ADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRsninKNDLSLLKAI 248

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  890 KNTALhlacskghETSALLILEKITdrnlINATNAALQTPLHVAARN-GLTVVVQELLGKGASVLAVDENGYTPALACAP 968
Cdd:PHA02876   249 RNEDL--------ETSLLLYDAGFS----VNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKGETPLYLMAK 316


                   .
gi 2092232601  969 N 969
Cdd:PHA02876   317 N 317
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 213-399 1.42e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 67.71  E-value: 1.42e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  213 AASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGA--NVNQMNERgfTPLHFAAASTHGALCLE 290
Cdd:PHA02875     9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAipDVKYPDIE--SELHDAVEEGDVKAVEE 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  291 LLVCNGADVNMKSKDGKTPLHMTAIHGRFSRSQTIIQNGAEIDCEDKNGNTPLHIAARYGHELLINTLITSGADTAKRGV 370
Cdd:PHA02875    87 LLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDC 166

                          170       180
                   ....*....|....*....|....*....
gi 2092232601  371 HGMFPLHLAALSGFSDCCRKLLSSGFDID 399
Cdd:PHA02875   167 CGCTPLIIAMAKGDIAICKMLLDSGANID 195
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 573-778 1.46e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 67.71  E-value: 1.46e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  573 LLDLDVRNN----NGRTPLDLAAFKGHVECVDVLINQGASILVKdYVVKRTPIHAAATNGHSECLRLLIGNAEPQNAVDI 648
Cdd:PHA02875    21 LLDIGINPNfeiyDGISPIKLAMKFRDSEAIKLLMKHGAIPDVK-YPDIESELHDAVEEGDVKAVEELLDLGKFADDVFY 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  649 QDGNgqTPLMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVEALLQHGAKSLLRDCRGRTPIHLSAA 728
Cdd:PHA02875   100 KDGM--TPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMA 177

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 2092232601  729 CGHIGVLGALLQSATSVDAVpaiADNHGYTSLHWACYNGHDSCVELLLEQ 778
Cdd:PHA02875   178 KGDIAICKMLLDSGANIDYF---GKNGCVAALCYAIENNKIDIVRLFIKR 224
Ank_4 pfam13637
Ankyrin repeats (many copies);
140-193 2.11e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.98  E-value: 2.11e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2092232601  140 GRTALHHAAFSGHVEMVSLLLSRGANINAFDKKDRRAIHWGAYMGHIEVVKLLV 193
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 805-976 3.49e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 66.53  E-value: 3.49e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  805 EMLIDTLGAGI-VNSTDAKGRTPLHAAAFTDHVECLQLLLSHNAQVNAVDSSGKTPLMMAAENGQTNTVEVLVSSAkADL 883
Cdd:PHA02874   105 DMIKTILDCGIdVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKG-AYA 183

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  884 TLQDSSKNTALHLACSKGHETSALLILEKITdrNLINATNAALqTPLHVAARNGLTVVvqELLGKGASVLAVDENGYTP- 962
Cdd:PHA02874   184 NVKDNNGESPLHNAAEYGDYACIKLLIDHGN--HIMNKCKNGF-TPLHNAIIHNRSAI--ELLINNASINDQDIDGSTPl 258

                          170
                   ....*....|....*.
gi 2092232601  963 --ALACAPNKDVADCL 976
Cdd:PHA02874   259 hhAINPPCDIDIIDIL 274
Ank_4 pfam13637
Ankyrin repeats (many copies);
552-603 8.56e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.05  E-value: 8.56e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2092232601  552 SPLHLAAYHGHHQALEVLVQSLLDLDVRNNNGRTPLDLAAFKGHVECVDVLI 603
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 542-777 8.98e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 65.67  E-value: 8.98e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  542 LNDSDNRApISPLHLAAYHGHHQALEVLVQSLLDLDVrnNNGRTPLDLAAFKGHVECVD-VLINQGASILVKDYVVKRTP 620
Cdd:PHA02878    63 VNQPDHRD-LTPLHIICKEPNKLGMKEMIRSINKCSV--FYTLVAIKDAFNNRNVEIFKiILTNRYKNIQTIDLVYIDKK 139

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  621 IHAAATNghSECLRLLIGNAEPQNAVDIQDGNgqTPLMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEE 700
Cdd:PHA02878   140 SKDDIIE--AEITKLLLSYGADINMKDRHKGN--TALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKP 215

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2092232601  701 CVEALLQHGAKSLLRDCRGRTPIHLSAA-CGHIGVLGALLQSATSVDAVPAIAdnhGYTSLHWACYNghDSCVELLLE 777
Cdd:PHA02878   216 IVHILLENGASTDARDKCGNTPLHISVGyCKDYDILKLLLEHGVDVNAKSYIL---GLTALHSSIKS--ERKLKLLLE 288
Ank_2 pfam12796
Ankyrin repeats (3 copies);
442-526 3.39e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 57.82  E-value: 3.39e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  442 LHYAAANCNYQCLFALVGSGASVNDLDERGCTPLHYAAASDTDgKCLEYLLRNdANPGIRDkQGYNAVHYSAAYGHRLCL 521
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHL-EIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77


                   ....*
gi 2092232601  522 ELIAS 526
Cdd:pfam12796   78 KLLLE 82
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 629-838 5.42e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 63.73  E-value: 5.42e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  629 HSECLRLLIGNAEPQNAVDIQDGNGQTPLMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVEALLQH 708
Cdd:PLN03192   501 HKELHDLNVGDLLGDNGGEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKH 580

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  709 GAKSLLRDCRGRTPIHLSAACGH-------------------------------IGVLGALLQSATSVDAvpaiADNHGY 757
Cdd:PLN03192   581 ACNVHIRDANGNTALWNAISAKHhkifrilyhfasisdphaagdllctaakrndLTAMKELLKQGLNVDS----EDHQGA 656

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  758 TSLHWACYNGHDSCVELLLEQ--EVFQKMEGNSFSPLHC-AVINDNE-GAAEMLIDTLGAGIVNSTDAKGRTPLHAAAFT 833
Cdd:PLN03192   657 TALQVAMAEDHVDMVRLLIMNgaDVDKANTDDDFSPTELrELLQKRElGHSITIVDSVPADEPDLGRDGGSRPGRLQGTS 736


                   ....*
gi 2092232601  834 DHVEC 838
Cdd:PLN03192   737 SDNQC 741
Ank_4 pfam13637
Ankyrin repeats (many copies);
207-251 5.49e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.74  E-value: 5.49e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2092232601  207 YTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQ 251
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGN 46
Ank_2 pfam12796
Ankyrin repeats (3 copies);
475-580 6.71e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 56.66  E-value: 6.71e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  475 LHYAAASDtDGKCLEYLLRNDANPGIRDKQGYNAVHYSAAYGHRLCLELIASETPLDvlMETSGTdmlndsdnrapiSPL 554
Cdd:pfam12796    1 LHLAAKNG-NLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN--LKDNGR------------TAL 65

                           90       100
                   ....*....|....*....|....*.
gi 2092232601  555 HLAAYHGHHQALEVLVQSLLDLDVRN 580
Cdd:pfam12796   66 HYAARSGHLEIVKLLLEKGADINVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 274-480 7.12e-10

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: 63.11  E-value: 7.12e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  274 TPLhFAAASTHGALCLE-LLVCNGADVNMKSKDGKTPLHMTAIHGRFSRSQTIIQNGAE-----IDCEDKNGNTPLHIAA 347
Cdd:cd22192     19 SPL-LLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElvnepMTSDLYQGETALHIAV 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  348 RYGHELLINTLITSGADTAKRGVHGMFplhlaalsgFSDCCRKLLSsgfdidtpddFGRTCLHAAAAGGNLECLNLLLNT 427
Cdd:cd22192     98 VNQNLNLVRELIARGADVVSPRATGTF---------FRPGPKNLIY----------YGEHPLSFAACVGNEEIVRLLIEH 158

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2092232601  428 GADFNKKDKFGRTPLHYAA--ANCNYQC-----LFALVGSGASVNdLD----ERGCTPLHYAAA 480
Cdd:cd22192    159 GADIRAQDSLGNTVLHILVlqPNKTFACqmydlILSYDKEDDLQP-LDlvpnNQGLTPFKLAAK 221
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 585-725 9.21e-10

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 62.72  E-value: 9.21e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  585 TPLDLAAFKGHVECVDVLINQGASILVKDYVVKRTPIHAAATNGHSECLRLLIGNA-----EPQNAVDIQdgnGQTPLML 659
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAApelvnEPMTSDLYQ---GETALHI 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  660 SVLNGHTDCVYSLLNKGANV--------------DAKDKWGRTALHRGAVTGHEECVEALLQHGAKSLLRDCRGRTPIHL 725
Cdd:cd22192     96 AVVNQNLNLVRELIARGADVvspratgtffrpgpKNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175
Ank_4 pfam13637
Ankyrin repeats (many copies);
74-127 9.31e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.36  E-value: 9.31e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2092232601   74 WLTPLHRAVASCSEDAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALV 127
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 183-374 1.22e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 62.58  E-value: 1.22e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  183 MGHIEVVKLLVTHGAEVTckDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCG 262
Cdd:PLN03192   504 LHDLNVGDLLGDNGGEHD--DPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA 581

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  263 ANVNQMNERGFTPLHFAAASTHGALCLELLVCNGADVNMKSKDgktPLHMTAIHGRFSRSQTIIQNGAEIDCEDKNGNTP 342
Cdd:PLN03192   582 CNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAGD---LLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATA 658

                          170       180       190
                   ....*....|....*....|....*....|..
gi 2092232601  343 LHIAARYGHELLINTLITSGADTAKRGVHGMF 374
Cdd:PLN03192   659 LQVAMAEDHVDMVRLLIMNGADVDKANTDDDF 690
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 690-962 1.75e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 61.43  E-value: 1.75e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  690 LHRGAVTGHEECVEALLQHGAKSLLRDCRGRTPIHLsaACGHIGVLGA--LLQSATSVDAvpaiadNHGYTSLHWACYNG 767
Cdd:PHA02878    41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHI--ICKEPNKLGMkeMIRSINKCSV------FYTLVAIKDAFNNR 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  768 HDSCVELLLeqevFQKMEGNSFSPLHCAVINDNEGAAEMLIDTL----GAGIVNSTDAKGRTPLHAAAFTDHVECLQLLL 843
Cdd:PHA02878   113 NVEIFKIIL----TNRYKNIQTIDLVYIDKKSKDDIIEAEITKLllsyGADINMKDRHKGNTALHYATENKDQRLTELLL 188

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  844 SHNAQVNAVDSSGKTPLMMAAENGQTNTVEVLVSSAkADLTLQDSSKNTALHLACSKGHETSAL-LILEKITDrnlINAT 922
Cdd:PHA02878   189 SYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENG-ASTDARDKCGNTPLHISVGYCKDYDILkLLLEHGVD---VNAK 264

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 2092232601  923 NAALQ-TPLHVAARNglTVVVQELLGKGASVLAVDENGYTP 962
Cdd:PHA02878   265 SYILGlTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTP 303
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 296-500 1.93e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.16  E-value: 1.93e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  296 GADVNMKSKDGKTPLHMTAihgRFSRSQTI---IQNGAEIDCEDKNGNTPLHIAARYGHELLINTLITSGA---DTAKRg 369
Cdd:PHA02875    25 GINPNFEIYDGISPIKLAM---KFRDSEAIkllMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKfadDVFYK- 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  370 vHGMFPLHLAALSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGADFNKKDKFGRTPLHYAAANC 449
Cdd:PHA02875   101 -DGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKG 179

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2092232601  450 NYQCLFALVGSGASVNDLDERGCTPLHYAAASDTDGKCLEYLLRNDANPGI 500
Cdd:PHA02875   180 DIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGADCNI 230
PHA02946 PHA02946
ankyin-like protein; Provisional
 49-276 2.01e-09

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 61.22  E-value: 2.01e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601   49 AYLG----DAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQVLLKHSADVNARDKNWQTPLH-IAAANKAVkca 123
Cdd:PHA02946    43 AYCGikglDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYyLSGTDDEV--- 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  124 ealvpllsnvnvsdragrtalhhaafsghVEMVSLLLSRGANINAFDKKDRRAIHWGAYMGHIEVVKLLVTHGAEVTCKD 203
Cdd:PHA02946   120 -----------------------------IERINLLVQYGAKINNSVDEEGCGPLLACTDPSERVFKKIMSIGFEARIVD 170

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2092232601  204 K--KSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNG-QDVVVNELIDCGANVNQMNERGFTPL 276
Cdd:PHA02946   171 KfgKNHIHRHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCSKTvKNVDIINLLLPSTDVNKQNKFGDSPL 246
Ank_4 pfam13637
Ankyrin repeats (many copies);
174-226 2.58e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.82  E-value: 2.58e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2092232601  174 RRAIHWGAYMGHIEVVKLLVTHGAEVTCKDKKSYTPLHAAASSGMISVVKYLL 226
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 208-345 2.83e-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: 2.83e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  208 TPLHAAASSGMISVVKYLLDL-GVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGAN-VNQ-MNE---RGFTPLHFAAA 281
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEpMTSdlyQGETALHIAVV 98

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2092232601  282 STHGALcLELLVCNGADVN---------MKSKD-----GKTPLHMTAIHGRFSRSQTIIQNGAEIDCEDKNGNTPLHI 345
Cdd:cd22192     99 NQNLNL-VRELIARGADVVspratgtffRPGPKnliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175
Ank_4 pfam13637
Ankyrin repeats (many copies);
823-876 3.96e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.43  E-value: 3.96e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2092232601  823 GRTPLHAAAFTDHVECLQLLLSHNAQVNAVDSSGKTPLMMAAENGQTNTVEVLV 876
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02798 PHA02798
ankyrin-like protein; Provisional
 254-478 4.37e-09

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 60.23  E-value: 4.37e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  254 VVNELIDCGANVNQMNERGFTPLHFAAAS----THGALCLELLVCNGADVNMKSKDGKTPLHMTAIHGRFSRSQTI---I 326
Cdd:PHA02798    53 IVKLFINLGANVNGLDNEYSTPLCTILSNikdyKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILlfmI 132

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  327 QNGAEIDCEDKNGNTPLHIAARYGHEL---LINTLITSGADTAKRG-------VHGMFPLHLAALSgfSDCCRKLLSSGF 396
Cdd:PHA02798   133 ENGADTTLLDKDGFTMLQVYLQSNHHIdieIIKLLLEKGVDINTHNnkekydtLHCYFKYNIDRID--ADILKLFVDNGF 210

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  397 DIDTPDDFGRTCLHAAAAGGNLECLNLLLN------TGADFNKKDKFGRTPLHYAAANCNYQCLFALVGSGASVNDLDER 470
Cdd:PHA02798   211 IINKENKSHKKKFMEYLNSLLYDNKRFKKNildfifSYIDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITEL 290


                   ....*...
gi 2092232601  471 GCTPLHYA 478
Cdd:PHA02798   291 GNTCLFTA 298
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 55-327 5.45e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 59.75  E-value: 5.45e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601   55 EIIELLILSGARVNAKdSKWLTPL-----HRAVASCS-EDAVQVLLKHSADVNARDKNWQTPlhiaaankavkcaeaLVP 128
Cdd:PHA02989    51 KIVKLLIDNGADVNYK-GYIETPLcavlrNREITSNKiKKIVKLLLKFGADINLKTFNGVSP---------------IVC 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  129 LLSNVNVSDragrtalhhaafsghVEMVSLLLSRGANINafDKKDRRA-----IHWGAYMGHIEVVKLLVTHGaeVTCKD 203
Cdd:PHA02989   115 FIYNSNINN---------------CDMLRFLLSKGINVN--DVKNSRGynllhMYLESFSVKKDVIKILLSFG--VNLFE 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  204 KKSY---TPLHAAASSGM----ISVVKYLLDLGVDMNEPNAYGNTPL------HVACYNGQDVVVNeLIDCGANVNQMNE 270
Cdd:PHA02989   176 KTSLyglTPMNIYLRNDIdvisIKVIKYLIKKGVNIETNNNGSESVLesfldnNKILSKKEFKVLN-FILKYIKINKKDK 254

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2092232601  271 RGFTPLHFAAASTHGALCLELLVCnGADVNMKSKDGKTPLHMTAIHGRFSRSQTIIQ 327
Cdd:PHA02989   255 KGFNPLLISAKVDNYEAFNYLLKL-GDDIYNVSKDGDTVLTYAIKHGNIDMLNRILQ 310
Ank_4 pfam13637
Ankyrin repeats (many copies);
109-160 6.66e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.66  E-value: 6.66e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2092232601  109 TPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHVEMVSLLL 160
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 72-250 7.01e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 57.14  E-value: 7.01e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601   72 SKWLTPLHRAVASCSEDAVQvllKHSADVNARDKNWQTPLHIAAANKAV--KCAEALVPLLSNVNVSDRA-GRTALHH-A 147
Cdd:PHA02859    19 YRYCNPLFYYVEKDDIEGVK---KWIKFVNDCNDLYETPIFSCLEKDKVnvEILKFLIENGADVNFKTRDnNLSALHHyL 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  148 AFSGHV--EMVSLLLSRGANINAFDKKDRRAIHwgAYMGH----IEVVKLLVTHGAEVTCKDKK------SYTPLHAAAS 215
Cdd:PHA02859    96 SFNKNVepEILKILIDSGSSITEEDEDGKNLLH--MYMCNfnvrINVIKLLIDSGVSFLNKDFDnnnilySYILFHSDKK 173

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 2092232601  216 sgmisVVKYLLDLGVDMNEPNAYGNTPLHVACYNG 250
Cdd:PHA02859   174 -----IFDFLTSLGIDINETNKSGYNCYDLIKFRN 203
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 33-276 9.53e-09

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 59.54  E-value: 9.53e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601   33 DVNFQDNEKRTP-LHAaaYLG----DAEIIELLILSGARVNAKDSKWLTPLHRAV--ASCSEDAVQVLLKHSADVNARDK 105
Cdd:PHA02716   168 NLNYVCKKTGYGiLHA--YLGnmyvDIDILEWLCNNGVNVNLQNNHLITPLHTYLitGNVCASVIKKIIELGGDMDMKCV 245

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  106 NWQTPLHIAAANkavkcAEALVPLLSNVNVSDRAGRTALHHAafsghvEMVSLLLSRGANINafdkkdrraihwgaymgh 185
Cdd:PHA02716   246 NGMSPIMTYIIN-----IDNINPEITNIYIESLDGNKVKNIP------MILHSYITLARNID------------------ 296

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  186 IEVVKLLVTHGAEVTCKDKKSYTPLHAAASSGMIS--VVKYLLDLGVDMNEPNAYGNTPLH--------VACYNGQ---D 252
Cdd:PHA02716   297 ISVVYSFLQPGVKLHYKDSAGRTCLHQYILRHNIStdIIKLLHEYGNDLNEPDNIGNTVLHtylsmlsvVNILDPEtdnD 376

                          250       260
                   ....*....|....*....|....*..
gi 2092232601  253 V---VVNELIDCGANVNQMNERGFTPL 276
Cdd:PHA02716   377 IrldVIQCLISLGADITAVNCLGYTPL 403
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 22-106 1.18e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 58.52  E-value: 1.18e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601   22 DEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQVLLKHSADVN 101
Cdd:PHA03100   173 NRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252


                   ....*
gi 2092232601  102 ARDKN 106
Cdd:PHA03100   253 TIIET 257
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 809-890 1.69e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 58.76  E-value: 1.69e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  809 DTLGAGIV-------NSTDAKGRTPLHAAAFTDHVECLQLLLSHNAQVNAVDSSGKTPLMMAAENGQTNTVEVLVSSAKA 881
Cdd:PTZ00322    94 DAVGARILltggadpNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQC 173


                   ....*....
gi 2092232601  882 DLTLQDSSK 890
Cdd:PTZ00322   174 HFELGANAK 182
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 822-948 1.76e-08

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: 58.62  E-value: 1.76e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  822 KGRTPLHAAAFTDHVECLQLLLSHNAQVNAVDSS--------------GKTPLMMAAENGQTNTVEVLVSSAKADLTLQD 887
Cdd:cd22194    140 EGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEIVQLLMEKESTDITSQD 219

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  888 SSKNTALHLAC-----SKGHETSAL----LILEKITDRNLINATNAALQTPLHVAARNGLTVVVQELLGK 948
Cdd:cd22194    220 SRGNTVLHALVtvaedSKTQNDFVKrmydMILLKSENKNLETIRNNEGLTPLQLAAKMGKAEILKYILSR 289
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 445-693 2.04e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 58.34  E-value: 2.04e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  445 AAANCNYQCLFALVGSGASVNDLDERGCTPLHYAAASDTDgKCLEYLLRNDANPGIRDKQGYNAVHYSAAYGHrlcleli 524
Cdd:PLN03192   532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYE-DCVLVLLKHACNVHIRDANGNTALWNAISAKH------- 603

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  525 asETPLDVLMETSGTdmlndSDNRAPISPLHLAAYHGHHQALEVLVQSLLDLDVRNNNGRTPLDLAAFKGHVECVDVLIN 604
Cdd:PLN03192   604 --HKIFRILYHFASI-----SDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIM 676

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  605 QGASIlvkdyvvkrtpIHAAATNGHS-ECLRLLIGNAEPQNAVDIQDGNGQTPLMLSVLNGHTDCvySLLNKGANvdaKD 683
Cdd:PLN03192   677 NGADV-----------DKANTDDDFSpTELRELLQKRELGHSITIVDSVPADEPDLGRDGGSRPG--RLQGTSSD---NQ 740

                          250
                   ....*....|
gi 2092232601  684 KWGRTALHRG 693
Cdd:PLN03192   741 CRPRVSIYKG 750
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 802-962 2.77e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 57.96  E-value: 2.77e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  802 GAAEMLIDTLGAGI-VNSTDAKGRTPLHAAAFTDHVECLQLLLSHNAQVNAVDSSGKTPLMMAAENGQTNTVEVLVSSAK 880
Cdd:PLN03192   536 GNAALLEELLKAKLdPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFAS 615

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  881 AdltlqdSSKNTALHLACSKGHETSaLLILEKITDRNL-INATNAALQTPLHVAARNGLTVVVQELLGKGASVLAVD-EN 958
Cdd:PLN03192   616 I------SDPHAAGDLLCTAAKRND-LTAMKELLKQGLnVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANtDD 688


                   ....
gi 2092232601  959 GYTP 962
Cdd:PLN03192   689 DFSP 692
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 279-433 2.84e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 57.96  E-value: 2.84e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  279 AAASTHGALCLELLVCNGADVNMKSKDGKTPLHMTAIHGRFSRSQTIIQNGAEIDCEDKNGNTPLHIAARYGHELLINTL 358
Cdd:PLN03192   531 TVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2092232601  359 --ITSGADTAKRGVhgmfPLHLAALSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGADFNK 433
Cdd:PLN03192   611 yhFASISDPHAAGD----LLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDK 683
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 147-305 3.10e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 57.96  E-value: 3.10e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  147 AAFSGHVEMVSLLLSRGANINAFDKKDRRAIHWGAYMGHIEVVKLLVTHGAEVTCKDKKSYTPLHAAASSGMISVVKYLL 226
Cdd:PLN03192   532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY 611

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2092232601  227 DLGvDMNEPNAYGNTpLHVACYNGQDVVVNELIDCGANVNQMNERGFTPLHFAAASTHGALcLELLVCNGADVNMKSKD 305
Cdd:PLN03192   612 HFA-SISDPHAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDM-VRLLIMNGADVDKANTD 687
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 189-261 3.55e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.60  E-value: 3.55e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2092232601  189 VKLLVTHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDC 261
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
Ank_4 pfam13637
Ankyrin repeats (many copies);
42-94 4.04e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.35  E-value: 4.04e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2092232601   42 RTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQVLL 94
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 144-226 4.75e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.22  E-value: 4.75e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  144 LHHAAFSGHVEMVSLLLSRGANINAFDKKDRRAIHWGAYMGHIEVVKLLVTHGAEVTCKDKKSYTPLHAAASSGMISVVK 223
Cdd:PTZ00322    86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165


                   ...
gi 2092232601  224 YLL 226
Cdd:PTZ00322   166 LLS 168
PHA02946 PHA02946
ankyin-like protein; Provisional
 134-312 4.76e-08

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 56.60  E-value: 4.76e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  134 NVSDRAGRTALHHAAFSGHVEMVSLLLSRGANINAFDKKDRRAIHW--GAYMGHIEVVKLLVTHGAEVTCK-DKKSYTPL 210
Cdd:PHA02946    66 NETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYlsGTDDEVIERINLLVQYGAKINNSvDEEGCGPL 145

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  211 HAAASSGMiSVVKYLLDLGVDMNEPNAYGNTPLH--VACYNGQDVVVNELIDCGANVNQMNERGFTPLHFAAASTHGALC 288
Cdd:PHA02946   146 LACTDPSE-RVFKKIMSIGFEARIVDKFGKNHIHrhLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCSKTVKNVD 224

                          170       180
                   ....*....|....*....|....
gi 2092232601  289 LELLVCNGADVNMKSKDGKTPLHM 312
Cdd:PHA02946   225 IINLLLPSTDVNKQNKFGDSPLTL 248
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 792-948 5.05e-08

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 56.94  E-value: 5.05e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  792 LHCAVINDNEGAAEMLIDTlGAGIVN----STDAKGRTPLHAAAFTDHVECLQLLLSHNAQVNAVDSSG----------- 856
Cdd:cd22192     55 LHVAALYDNLEAAVVLMEA-APELVNepmtSDLYQGETALHIAVVNQNLNLVRELIARGADVVSPRATGtffrpgpknli 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  857 ---KTPLMMAAENGQTNTVEVLVSSAkADLTLQDSSKNTALHLACSKGHETSA------LLILEK-ITDRNLINATNAAL 926
Cdd:cd22192    134 yygEHPLSFAACVGNEEIVRLLIEHG-ADIRAQDSLGNTVLHILVLQPNKTFAcqmydlILSYDKeDDLQPLDLVPNNQG 212

                          170       180
                   ....*....|....*....|..
gi 2092232601  927 QTPLHVAARNGLTVVVQELLGK 948
Cdd:cd22192    213 LTPFKLAAKEGNIVMFQHLVQK 234
Ank_4 pfam13637
Ankyrin repeats (many copies);
583-637 6.72e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.97  E-value: 6.72e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2092232601  583 GRTPLDLAAFKGHVECVDVLINQGASILVKDYvVKRTPIHAAATNGHSECLRLLI 637
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDG-NGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 2-167 6.99e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 56.15  E-value: 6.99e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601    2 VFLKLREQPLLVQAIFNgDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLIlsgarvnakdskwltplhra 81
Cdd:PHA02875    97 VFYKDGMTPLHLATILK-KLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLI-------------------- 155

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601   82 vascsedavqvllKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVN-VSDRAGRTALHHAAFSGHVEMVSLLL 160
Cdd:PHA02875   156 -------------DHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDyFGKNGCVAALCYAIENNKIDIVRLFI 222


                   ....*..
gi 2092232601  161 SRGANIN 167
Cdd:PHA02875   223 KRGADCN 229
Ank_4 pfam13637
Ankyrin repeats (many copies);
438-492 8.75e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.58  E-value: 8.75e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2092232601  438 GRTPLHYAAANCNYQCLFALVGSGASVNDLDERGCTPLHYAAASDtDGKCLEYLL 492
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNG-NVEVLKLLL 54
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 206-378 1.54e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 53.28  E-value: 1.54e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  206 SYT-PLHAAASSGMISVVKYLLDLgvdMNEPNAYGNTPLHvACYNGQDVVVNE---LIDCGANVN-QMNERGFTPLHFAA 280
Cdd:PHA02859    20 RYCnPLFYYVEKDDIEGVKKWIKF---VNDCNDLYETPIF-SCLEKDKVNVEIlkfLIENGADVNfKTRDNNLSALHHYL 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  281 ASTHGAL--CLELLVCNGADVNMKSKDGKTPLH--MTAIHGRFSRSQTIIQNGAEIDCEDKNGNTPLHIAARYGHELLI- 355
Cdd:PHA02859    96 SFNKNVEpeILKILIDSGSSITEEDEDGKNLLHmyMCNFNVRINVIKLLIDSGVSFLNKDFDNNNILYSYILFHSDKKIf 175

                          170       180
                   ....*....|....*....|...
gi 2092232601  356 NTLITSGADTAKRGVHGMFPLHL 378
Cdd:PHA02859   176 DFLTSLGIDINETNKSGYNCYDL 198
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 817-979 1.55e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.00  E-value: 1.55e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  817 NSTDAKGRTPLHAAAFTDHVECLQLLLSHNAQVNAVDSSGKTPLMMAAENGQTNTVEVLVSSAK--ADLTLQDSskNTAL 894
Cdd:PHA02875    29 NFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKfaDDVFYKDG--MTPL 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  895 HLAC-SKGHETSALLILEKiTDRNLINATNAalqTPLHVAARNGLTVVVQELLGKGASVLAVDENGYTPALACAPNKDVA 973
Cdd:PHA02875   107 HLATiLKKLDIMKLLIARG-ADPDIPNTDKF---SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIA 182


                   ....*.
gi 2092232601  974 DCLALI 979
Cdd:PHA02875   183 ICKMLL 188
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 758-878 1.63e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.00  E-value: 1.63e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  758 TSLHWACYNGHDSCVELLLE-----QEVFQKmEGNSfsPLHCAVINDNEGAAEMLIDTLGAGIVNSTDAKgrTPLHAAAF 832
Cdd:PHA02875    70 SELHDAVEEGDVKAVEELLDlgkfaDDVFYK-DGMT--PLHLATILKKLDIMKLLIARGADPDIPNTDKF--SPLHLAVM 144

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2092232601  833 TDHVECLQLLLSHNAQVNAVDSSGKTPLMMAAENGQTNTVEVLVSS 878
Cdd:PHA02875   145 MGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDS 190
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 787-981 2.61e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 54.23  E-value: 2.61e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  787 NSFSPLHCAVINDNEGAAEMLIDTLGAGIVNSTDAkgRTPLHAAAFTDHVECLQLLLSHNAQVNAV-DSSGKTPLMMAAE 865
Cdd:PHA02875    34 DGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDI--ESELHDAVEEGDVKAVEELLDLGKFADDVfYKDGMTPLHLATI 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  866 NGQTNTVEVLVSSaKADLTLQDSSKNTALHLACSKGHETSALLILEKitdRNLINATNAALQTPLHVAARNGLTVVVQEL 945
Cdd:PHA02875   112 LKKLDIMKLLIAR-GADPDIPNTDKFSPLHLAVMMGDIKGIELLIDH---KACLDIEDCCGCTPLIIAMAKGDIAICKML 187

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 2092232601  946 LGKGASVLAVDENGYTPALACAPNKDVADCLALILA 981
Cdd:PHA02875   188 LDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIK 223
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 84-161 2.69e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.52  E-value: 2.69e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601   84 SCSEDAV--QVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHVEMVSLLLS 161
Cdd:PTZ00322    90 AASGDAVgaRILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
Ank_4 pfam13637
Ankyrin repeats (many copies);
308-359 3.42e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.04  E-value: 3.42e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2092232601  308 TPLHMTAIHGRFSRSQTIIQNGAEIDCEDKNGNTPLHIAARYGHELLINTLI 359
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 792-962 5.04e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.43  E-value: 5.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  792 LHCAVINDNEGAAEMLIDtLGAGiVNSTDAKGRTPLHAAAFTDHVECLQLLLSHNAQVNAVDSSGKTPLMMAAENGQTNT 871
Cdd:PHA02874   128 LHYAIKKGDLESIKMLFE-YGAD-VNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYAC 205

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  872 VEVLVSSAkADLTLQDSSKNTALHLACSkgHETSALLILekITDRNlINATNAALQTPLHVAARNGLTV-VVQELLGKGA 950
Cdd:PHA02874   206 IKLLIDHG-NHIMNKCKNGFTPLHNAII--HNRSAIELL--INNAS-INDQDIDGSTPLHHAINPPCDIdIIDILLYHKA 279

                          170
                   ....*....|..
gi 2092232601  951 SVLAVDENGYTP 962
Cdd:PHA02874   280 DISIKDNKGENP 291
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 552-741 5.14e-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: 53.86  E-value: 5.14e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  552 SPLHLAAYHGHHQALE-VLVQSLLDLDVRNNNGRTPLDLAAFKGHVECVDVLINqGASILVK-----DYVVKRTPIHAAA 625
Cdd:cd22192     19 SPLLLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME-AAPELVNepmtsDLYQGETALHIAV 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  626 TNGHSECLRLLIG-NAEPQNA------VDIQDGN----GQTPLMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALHRGA 694
Cdd:cd22192     98 VNQNLNLVRELIArGADVVSPratgtfFRPGPKNliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILV 177

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2092232601  695 VTGHEECV----------EALLQHGAKSLLRDCRGRTPIHLSAACGHIGVLGALLQS 741
Cdd:cd22192    178 LQPNKTFAcqmydlilsyDKEDDLQPLDLVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 28-247 5.20e-07

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 53.93  E-value: 5.20e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601   28 IFKKEDVNFQDNEKrtplhaaAYLGDAEIIELLILSGARVNAK-------DSKWLTPLHRAVA-SCSEDAVQVLLKHSAD 99
Cdd:TIGR00870    6 IVPAEESPLSDEEK-------AFLPAAERGDLASVYRDLEEPKklnincpDRLGRSALFVAAIeNENLELTELLLNLSCR 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  100 VNARDknwqTPLHIAAANKAVKCAEALVPLLSN---------VNVSDR----AGRTALHHAAFSGHVEMVSLLLSRGANI 166
Cdd:TIGR00870   79 GAVGD----TLLHAISLEYVDAVEAILLHLLAAfrksgplelANDQYTseftPGITALHLAAHRQNYEIVKLLLERGASV 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  167 NA------FDKKDRRA--------IHWGAYMGHIEVVKLLVTHGAEVTCKDKKSYTPLHAAA------------SSGMIS 220
Cdd:TIGR00870  155 PAracgdfFVKSQGVDsfyhgespLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVmenefkaeyeelSCQMYN 234

                          250       260       270
                   ....*....|....*....|....*....|.
gi 2092232601  221 VVKYLLDLGVDMNE----PNAYGNTPLHVAC 247
Cdd:TIGR00870  235 FALSLLDKLRDSKEleviLNHQGLTPLKLAA 265
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 574-797 5.29e-07

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 53.93  E-value: 5.29e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  574 LDLDVRNNNGRTPLDLAAFKG-HVECVDVLINQGASILVKDyvvkrTPIHAAATNGH---SECLRLLIGNAE----PQNA 645
Cdd:TIGR00870   43 LNINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAVGD-----TLLHAISLEYVdavEAILLHLLAAFRksgpLELA 117

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  646 VDIQDGN---GQTPLMLSVLNGHTDCVYSLLNKGANVDAKDK--------------WGRTALHRGAVTGHEECVEALLQH 708
Cdd:TIGR00870  118 NDQYTSEftpGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSED 197

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  709 GAKSLLRDCRGRTPIHLSA--------------ACGHIGV-LGALLQSATSVDAVPaiadNH-GYTSLHWACYNGHDSCV 772
Cdd:TIGR00870  198 PADILTADSLGNTLLHLLVmenefkaeyeelscQMYNFALsLLDKLRDSKELEVIL----NHqGLTPLKLAAKEGRIVLF 273

                          250       260
                   ....*....|....*....|....*.
gi 2092232601  773 ELLLEQEVFQ-KMEGNSFSPLHCAVI 797
Cdd:TIGR00870  274 RLKLAIKYKQkKFVAWPNGQQLLSLY 299
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 652-875 6.44e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 53.07  E-value: 6.44e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  652 NGQTPLMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVEALLQHGakSLLRDC---RGRTPIHLSAA 728
Cdd:PHA02875    34 DGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLG--KFADDVfykDGMTPLHLATI 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  729 CGHIGVLGALLQSAtsvdAVPAIADNHGYTSLHWACYNGHDSCVELLLEQEVFQKME-GNSFSPLHCAVINDNEGAAEML 807
Cdd:PHA02875   112 LKKLDIMKLLIARG----ADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEdCCGCTPLIIAMAKGDIAICKML 187

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2092232601  808 IDTlGAGIvnstDAKGRTP----LHAAAFTDHVECLQLLLSHNAQVNavdssgktpLMMAAENGQTNTVEVL 875
Cdd:PHA02875   188 LDS-GANI----DYFGKNGcvaaLCYAIENNKIDIVRLFIKRGADCN---------IMFMIEGEECTILDMI 245
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 858-952 6.76e-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: 6.76e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  858 TPLMMAAENGQTNTVEVLVSSAKADLTLQDSSKNTALHLACSKGHETSALLILEkiTDRNLIN-ATNAAL---QTPLHVA 933
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNePMTSDLyqgETALHIA 96

                           90
                   ....*....|....*....
gi 2092232601  934 ARNGLTVVVQELLGKGASV 952
Cdd:cd22192     97 VVNQNLNLVRELIARGADV 115
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 281-350 7.50e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.36  E-value: 7.50e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  281 ASTHGALCLELLVCNGADVNMKSKDGKTPLHMTAIHGRFSRSQTIIQNGAEIDCEDKNGNTPLHIAARYG 350
Cdd:PTZ00322    90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENG 159
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 767-951 7.53e-07

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: 53.35  E-value: 7.53e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  767 GHDSCVELLLEQEVFQKMEGNSfSPLHCAVINDNEGAAEMLIDTLGAG--------IVNS--TDA--KGRTPLHAAAFTD 834
Cdd:cd21882      6 GLLECLRWYLTDSAYQRGATGK-TCLHKAALNLNDGVNEAIMLLLEAApdsgnpkeLVNApcTDEfyQGQTALHIAIENR 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  835 HVECLQLLLSHNAQVNAVDSS-------------GKTPLMMAAENGQTNTVEVLV--SSAKADLTLQDSSKNTALH---L 896
Cdd:cd21882     85 NLNLVRLLVENGADVSARATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLenGAQPAALEAQDSLGNTVLHalvL 164

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2092232601  897 ACSKGHETSA--------LLILEKITD--RNLINATNAALQTPLHVAARNGLTVVVQELLGKGAS 951
Cdd:cd21882    165 QADNTPENSAfvcqmynlLLSYGAHLDptQQLEEIPNHQGLTPLKLAAVEGKIVMFQHILQREFS 229
Ank_4 pfam13637
Ankyrin repeats (many copies);
655-706 7.71e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.88  E-value: 7.71e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2092232601  655 TPLMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVEALL 706
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
618-673 2.02e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.73  E-value: 2.02e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2092232601  618 RTPIHAAATNGHSECLRLLIGNAEPqnaVDIQDGNGQTPLMLSVLNGHTDCVYSLL 673
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGAD---INAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 214-320 2.63e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.44  E-value: 2.63e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  214 ASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGANVNQMNERGFTPLHFAAASTHGALCLELLV 293
Cdd:PTZ00322    90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2092232601  294 CNGADVNM------KSKDGKTPLH----MTAIHGRFS 320
Cdd:PTZ00322   170 HSQCHFELganakpDSFTGKPPSLedspISSHHPDFS 206
Ank_4 pfam13637
Ankyrin repeats (many copies);
686-739 2.71e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.34  E-value: 2.71e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2092232601  686 GRTALHRGAVTGHEECVEALLQHGAKSLLRDCRGRTPIHLSAACGHIGVLGALL 739
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 12-97 2.79e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.44  E-value: 2.79e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601   12 LVQAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQ 91
Cdd:PTZ00322    86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165


                   ....*.
gi 2092232601   92 VLLKHS 97
Cdd:PTZ00322   166 LLSRHS 171
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 803-980 2.85e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 51.12  E-value: 2.85e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  803 AAEMLIDTLGAGIVNSTDaKGRTPLHAAAFTDHVECLQLLLSHNAQVNAVDSSGKTPLMMAAENGQTNTVEVLVSS---- 878
Cdd:PHA02874    16 AIEKIIKNKGNCINISVD-ETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNgvdt 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  879 ------------------AKADLTLQDSSKNTALHLACSKGHETSALLILEKITDRNlINATNAALqtPLHVAARNGLTV 940
Cdd:PHA02874    95 silpipciekdmiktildCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVN-IEDDNGCY--PIHIAIKHNFFD 171

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 2092232601  941 VVQELLGKGASVLAVDENGYTPALACAPNKDVAdCLALIL 980
Cdd:PHA02874   172 IIKLLLEKGAYANVKDNNGESPLHNAAEYGDYA-CIKLLI 210
PHA02798 PHA02798
ankyrin-like protein; Provisional
 646-866 2.93e-06

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 50.99  E-value: 2.93e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  646 VDIQDGNGQTPL--MLSVL---NGHTDCVYSLLNKGANVDAKDKWGRTA----LHRGAVTgHEECVEALLQHGAKSLLRD 716
Cdd:PHA02798    64 VNGLDNEYSTPLctILSNIkdyKHMLDIVKILIENGADINKKNSDGETPlyclLSNGYIN-NLEILLFMIENGADTTLLD 142

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  717 CRGRTPIHLSAACGH---IGVLGALLQSATSVDAvpaIADNHGYTSLHwaCYNGHD-SCVE-----LLLEQEVFQKMEGN 787
Cdd:PHA02798   143 KDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINT---HNNKEKYDTLH--CYFKYNiDRIDadilkLFVDNGFIINKENK 217

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  788 S----FSPLHCAVINDNEGAAEMLIDTLGAGI-VNSTDAKGRTPLHAAAFTDHVECLQLLLSHNAQVNAVDSSGKTPLMM 862
Cdd:PHA02798   218 ShkkkFMEYLNSLLYDNKRFKKNILDFIFSYIdINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFT 297


                   ....
gi 2092232601  863 AAEN 866
Cdd:PHA02798   298 AFEN 301
Ank_5 pfam13857
Ankyrin repeats (many copies);
191-246 3.30e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.03  E-value: 3.30e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2092232601  191 LLVTHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVA 246
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 108-259 4.66e-06

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 50.65  E-value: 4.66e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  108 QTPLHIAAANKAVKCAEALVPLLSNVNVSDRA--------------GRTALHHAAFSGHVEMVSLLLSRGANINA----- 168
Cdd:cd21882     27 KTCLHKAALNLNDGVNEAIMLLLEAAPDSGNPkelvnapctdefyqGQTALHIAIENRNLNLVRLLVENGADVSAratgr 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  169 -FDKKDRRAIHWG-------AYMGHIEVVKLLVTHGAE---VTCKDKKSYTPLHA---------AASSGMISVVKYLLDL 228
Cdd:cd21882    107 fFRKSPGNLFYFGelplslaACTNQEEIVRLLLENGAQpaaLEAQDSLGNTVLHAlvlqadntpENSAFVCQMYNLLLSY 186

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 2092232601  229 G------VDMNE-PNAYGNTPLHVACYNGQDVVVNELI 259
Cdd:cd21882    187 GahldptQQLEEiPNHQGLTPLKLAAVEGKIVMFQHIL 224
Ank_4 pfam13637
Ankyrin repeats (many copies);
405-458 4.98e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 4.98e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2092232601  405 GRTCLHAAAAGGNLECLNLLLNTGADFNKKDKFGRTPLHYAAANCNYQCLFALV 458
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 140-171 5.33e-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: 5.33e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2092232601  140 GRTALHHAAFS-GHVEMVSLLLSRGANINAFDK 171
Cdd:pfam00023    2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
Ank_4 pfam13637
Ankyrin repeats (many copies);
375-416 5.65e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 5.65e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 2092232601  375 PLHLAALSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGG 416
Cdd:pfam13637    4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNG 45
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 289-475 5.78e-06

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 50.30  E-value: 5.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  289 LELLVCNGADVNMKSKDGKTPLHMTAIHGRFSRS--QTIIQNGAEIDCEDKNGNTPLH---IAARYGHELLINTLITSGA 363
Cdd:PHA02716   195 LEWLCNNGVNVNLQNNHLITPLHTYLITGNVCASviKKIIELGGDMDMKCVNGMSPIMtyiINIDNINPEITNIYIESLD 274

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  364 DTAKRGVHGMFPLHLAALSGFS-DCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECL--NLLLNTGADFNKKDKFGRT 440
Cdd:PHA02716   275 GNKVKNIPMILHSYITLARNIDiSVVYSFLQPGVKLHYKDSAGRTCLHQYILRHNISTDiiKLLHEYGNDLNEPDNIGNT 354

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 2092232601  441 PLHYAAA--------------NCNYQCLFALVGSGASVNDLDERGCTPL 475
Cdd:PHA02716   355 VLHTYLSmlsvvnildpetdnDIRLDVIQCLISLGADITAVNCLGYTPL 403
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 140-168 7.80e-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: 43.35  E-value: 7.80e-06
                            10        20
                    ....*....|....*....|....*....
gi 2092232601   140 GRTALHHAAFSGHVEMVSLLLSRGANINA 168
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 809-980 7.88e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 49.87  E-value: 7.88e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  809 DTLGAGIVNSTDAKGRTPLHAAAFTDHVECLQLLLSHNAQVNAVDSSGKTPLMMAAENGQTNTVEVLVSSAkADLTLQDS 888
Cdd:PLN03192   511 DLLGDNGGEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA-CNVHIRDA 589

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  889 SKNTALHLACSKGHETsALLILEKItdrnlinatnAALQTP------LHVAARNGLTVVVQELLGKGASVLAVDENGYTp 962
Cdd:PLN03192   590 NGNTALWNAISAKHHK-IFRILYHF----------ASISDPhaagdlLCTAAKRNDLTAMKELLKQGLNVDSEDHQGAT- 657

                          170
                   ....*....|....*...
gi 2092232601  963 ALACAPNKDVADCLALIL 980
Cdd:PLN03192   658 ALQVAMAEDHVDMVRLLI 675
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 43-179 8.73e-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: 49.63  E-value: 8.73e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601   43 TPLHAAAYLGDAEIIELLILSGARVNA---------KDSKWLT-----PLHRAVASCSEDAVQVLLKHSADVNARDKNWQ 108
Cdd:cd22192     91 TALHIAVVNQNLNLVRELIARGADVVSpratgtffrPGPKNLIyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGN 170

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  109 TPLHIAA--ANKAVKCAE-----ALVPLLSNVNVS---DRAGRTALHHAAFSGHVEMVSLLLSRganinafdkkdRRAIH 178
Cdd:cd22192    171 TVLHILVlqPNKTFACQMydlilSYDKEDDLQPLDlvpNNQGLTPFKLAAKEGNIVMFQHLVQK-----------RRHIQ 239


                   .
gi 2092232601  179 W 179
Cdd:cd22192    240 W 240
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 52-126 9.00e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.90  E-value: 9.00e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2092232601   52 GDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEAL 126
Cdd:PTZ00322    93 GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 625-708 9.55e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.51  E-value: 9.55e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  625 ATNGHSECLRLLI-GNAEPqnavDIQDGNGQTPLMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVE 703
Cdd:PTZ00322    90 AASGDAVGARILLtGGADP----NCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165


                   ....*
gi 2092232601  704 ALLQH 708
Cdd:PTZ00322   166 LLSRH 170
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 727-876 9.75e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 49.87  E-value: 9.75e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  727 AACGHIGVLGALLQSATSVDavpaIADNHGYTSLHWACYNGHDSCVELLLEQEV---FQKMEGNS-------------FS 790
Cdd:PLN03192   533 ASTGNAALLEELLKAKLDPD----IGDSKGRTPLHIAASKGYEDCVLVLLKHACnvhIRDANGNTalwnaisakhhkiFR 608

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  791 PL-HCAVINDNEGAAEMLIdtlgagivnstdakgrtplhAAAFTDHVECLQLLLSHNAQVNAVDSSGKTPLMMAAENGQT 869
Cdd:PLN03192   609 ILyHFASISDPHAAGDLLC--------------------TAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHV 668


                   ....*..
gi 2092232601  870 NTVEVLV 876
Cdd:PLN03192   669 DMVRLLI 675
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 325-404 9.80e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.51  E-value: 9.80e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  325 IIQNGAEIDCEDKNGNTPLHIAARYGHELLINTLITSGADTAKRGVHGMFPLHLAALSGFSDCCRKLLS---SGFDIDT- 400
Cdd:PTZ00322   101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRhsqCHFELGAn 180


                   ....*.
gi 2092232601  401 --PDDF 404
Cdd:PTZ00322   181 akPDSF 186
Ank_4 pfam13637
Ankyrin repeats (many copies);
239-293 9.89e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.80  E-value: 9.89e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2092232601  239 GNTPLHVACYNGQDVVVNELIDCGANVNQMNERGFTPLHFAAASTHGAlCLELLV 293
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVE-VLKLLL 54
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 234-350 1.08e-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: 49.37  E-value: 1.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  234 EPNAYGNTPLHVACYNGQDVVVNELIDCGANVN----------QMNERGF----TPLHFAAASTHGALcLELLVCNGAD- 298
Cdd:cd22194    136 EEAYEGQTALNIAIERRQGDIVKLLIAKGADVNahakgvffnpKYKHEGFyfgeTPLALAACTNQPEI-VQLLMEKESTd 214

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2092232601  299 VNMKSKDGKTPLHMTAIHGRFSRSQT--IIQNGAEI--DCEDKN--------GNTPLHIAARYG 350
Cdd:cd22194    215 ITSQDSRGNTVLHALVTVAEDSKTQNdfVKRMYDMIllKSENKNletirnneGLTPLQLAAKMG 278
Ank_5 pfam13857
Ankyrin repeats (many copies);
93-147 1.17e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.49  E-value: 1.17e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2092232601   93 LLKH-SADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHA 147
Cdd:pfam13857    1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
790-843 1.25e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.42  E-value: 1.25e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2092232601  790 SPLHCAVINDNEGAAEMLIDTlGAgIVNSTDAKGRTPLHAAAFTDHVECLQLLL 843
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEK-GA-DINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 190-359 1.46e-05

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 48.86  E-value: 1.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  190 KLLVTHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDM-NEP---NAY-GNTPLHVACYNGQDVVVNELIDCGAN 264
Cdd:cd22192     35 KLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELvNEPmtsDLYqGETALHIAVVNQNLNLVRELIARGAD 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  265 VNQMNERG--FT------------PLHFAAASTHGALcLELLVCNGADVNMKSKDGKTPLHMtaihgrfsrsqTIIQNGA 330
Cdd:cd22192    115 VVSPRATGtfFRpgpknliyygehPLSFAACVGNEEI-VRLLIEHGADIRAQDSLGNTVLHI-----------LVLQPNK 182

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 2092232601  331 EIDCE--------DKNGN-------------TPLHIAARYGHELLINTLI 359
Cdd:cd22192    183 TFACQmydlilsyDKEDDlqpldlvpnnqglTPFKLAAKEGNIVMFQHLV 232
Ank_4 pfam13637
Ankyrin repeats (many copies);
10-61 1.55e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.42  E-value: 1.55e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2092232601   10 PLLVQAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLI 61
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 864-959 1.84e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.74  E-value: 1.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  864 AENGQTNTVEVLVSSAkADLTLQDSSKNTALHLACSKGHETSALLILEKITDRNLINATNaalQTPLHVAARNGLTVVVQ 943
Cdd:PTZ00322    90 AASGDAVGARILLTGG-ADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDG---KTPLELAEENGFREVVQ 165

                           90
                   ....*....|....*.
gi 2092232601  944 ELLGKGASVLAVDENG 959
Cdd:PTZ00322   166 LLSRHSQCHFELGANA 181
Ank_4 pfam13637
Ankyrin repeats (many copies);
756-808 1.97e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.03  E-value: 1.97e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2092232601  756 GYTSLHWACYNGHDSCVELLLEQEV-FQKMEGNSFSPLHCAVINDNEGAAEMLI 808
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGAdINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
258-312 2.15e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.72  E-value: 2.15e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2092232601  258 LIDCG-ANVNQMNERGFTPLHFAAasTHGAL-CLELLVCNGADVNMKSKDGKTPLHM 312
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAA--KYGALeIVRVLLAYGVDLNLKDEEGLTALDL 55
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 219-478 2.28e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 48.20  E-value: 2.28e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  219 ISVVKYLLDLGVDMNEpnAYGNTPLHVACYNGQDV---VVNELIDCGANVNQmneRGF--TPL-----HFAAASTHGALC 288
Cdd:PHA02989    16 KNALEFLLRTGFDVNE--EYRGNSILLLYLKRKDVkikIVKLLIDNGADVNY---KGYieTPLcavlrNREITSNKIKKI 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  289 LELLVCNGADVNMKSKDGKTPLhMTAIHG---------RFsrsqtIIQNGAEI-DCEDKNGNTPLHIaarYGHELLINT- 357
Cdd:PHA02989    91 VKLLLKFGADINLKTFNGVSPI-VCFIYNsninncdmlRF-----LLSKGINVnDVKNSRGYNLLHM---YLESFSVKKd 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  358 ----LITSGADT-AKRGVHGMFPLHLAALSGFS----DCCRKLLSSGFDIDTPDDFGRTCLHAAAagGNLECLNLLLNTG 428
Cdd:PHA02989   162 vikiLLSFGVNLfEKTSLYGLTPMNIYLRNDIDvisiKVIKYLIKKGVNIETNNNGSESVLESFL--DNNKILSKKEFKV 239

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2092232601  429 ADF-------NKKDKFGRTPLHYAAANCNYQCLFALVGSGASVNDLDERGCTPLHYA 478
Cdd:PHA02989   240 LNFilkyikiNKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYA 296
PHA02946 PHA02946
ankyin-like protein; Provisional
 390-510 2.42e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 48.13  E-value: 2.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  390 KLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGADFNKKDKFGRTPLHYAAANCN--YQCLFALVGSGASVND- 466
Cdd:PHA02946    57 ELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKINNs 136

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2092232601  467 LDERGCTPLhyAAASDTDGKCLEYLLRNDANPGIRDKQGYNAVH 510
Cdd:PHA02946   137 VDEEGCGPL--LACTDPSERVFKKIMSIGFEARIVDKFGKNHIH 178
Ank_5 pfam13857
Ankyrin repeats (many copies);
643-691 2.75e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.72  E-value: 2.75e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2092232601  643 QNAVDIQDGNGQTPLMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALH 691
Cdd:pfam13857    6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 528-657 3.20e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 47.68  E-value: 3.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  528 TPLDVLMETSGTDMLN---------DSDNRAPISPLHLAAYHGHHQALEVLVQSLLDLDVRNNNGRTPLDLAAFKGHVEC 598
Cdd:PHA02875   104 TPLHLATILKKLDIMKlliargadpDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAI 183

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2092232601  599 VDVLINQGASIlvkDYVVKRTPIHA---AATNGHSECLRLLIGNAEPQNAVDIQDGNGQTPL 657
Cdd:PHA02875   184 CKMLLDSGANI---DYFGKNGCVAAlcyAIENNKIDIVRLFIKRGADCNIMFMIEGEECTIL 242
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 378-597 3.22e-05

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 47.95  E-value: 3.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  378 LAALSGFSDCCRKLLSSgfDIDTPDDFGRTCLHAAA---AGGNLECLNLLLNTGADFNKKDKF-----------GRTPLH 443
Cdd:cd21882      1 LEELLGLLECLRWYLTD--SAYQRGATGKTCLHKAAlnlNDGVNEAIMLLLEAAPDSGNPKELvnapctdefyqGQTALH 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  444 YAAANCNYQCLFALVGSGASVND------LDERGCT-------PLHYAAASDTDgKCLEYLLRNDANP---GIRDKQGYN 507
Cdd:cd21882     79 IAIENRNLNLVRLLVENGADVSAratgrfFRKSPGNlfyfgelPLSLAACTNQE-EIVRLLLENGAQPaalEAQDSLGNT 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  508 AVHysaayghrlCLELIASETPLDVLMETSGTDMLndsdnrapispLHLAAYHGHHQALEvlvqslldlDVRNNNGRTPL 587
Cdd:cd21882    158 VLH---------ALVLQADNTPENSAFVCQMYNLL-----------LSYGAHLDPTQQLE---------EIPNHQGLTPL 208

                          250
                   ....*....|
gi 2092232601  588 DLAAFKGHVE 597
Cdd:cd21882    209 KLAAVEGKIV 218
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 555-660 3.74e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.59  E-value: 3.74e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  555 HLAAyHGHHQALEVLVQSLLDLDVRNNNGRTPLDLAAFKGHVECVDVLINQGA--SILVKDyvvKRTPIHAAATNGHSEC 632
Cdd:PTZ00322    88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGAdpTLLDKD---GKTPLELAEENGFREV 163

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2092232601  633 LRLLIG----------NAEPQNAVDIQDGNGQTPLMLS 660
Cdd:PTZ00322   164 VQLLSRhsqchfelgaNAKPDSFTGKPPSLEDSPISSH 201
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 140-168 3.86e-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: 41.47  E-value: 3.86e-05
                           10        20
                   ....*....|....*....|....*....
gi 2092232601  140 GRTALHHAAFSGHVEMVSLLLSRGANINA 168
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 377-493 3.94e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.59  E-value: 3.94e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  377 HLAALSGFSDccrKLLSSGFDIDTPDDFGRTCLHAA-------AAGGNLECLNLLLNTGADFNKKDKFGRTPLHYAAANC 449
Cdd:PTZ00322    50 HLEALEATEN---KDATPDHNLTTEEVIDPVVAHMLtvelcqlAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANG 126

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2092232601  450 NYQCLFALVGSGASVNDLDERGCTPLHYAAASDTdGKCLEYLLR 493
Cdd:PTZ00322   127 HVQVVRVLLEFGADPTLLDKDGKTPLELAEENGF-REVVQLLSR 169
Ank_4 pfam13637
Ankyrin repeats (many copies);
274-326 4.91e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.88  E-value: 4.91e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2092232601  274 TPLHFAAASTHGAlCLELLVCNGADVNMKSKDGKTPLHMTAIHGRFSRSQTII 326
Cdd:pfam13637    3 TALHAAAASGHLE-LLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 694-776 6.19e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.20  E-value: 6.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  694 AVTGHEECVEALLQHGAKSLLRDCRGRTPIHLSAACGHIGVLGALLQsatsVDAVPAIADNHGYTSLHWACYNGHDSCVE 773
Cdd:PTZ00322    90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLE----FGADPTLLDKDGKTPLELAEENGFREVVQ 165


                   ...
gi 2092232601  774 LLL 776
Cdd:PTZ00322   166 LLS 168
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 822-853 6.44e-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: 40.74  E-value: 6.44e-05
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2092232601  822 KGRTPLHAAA-FTDHVECLQLLLSHNAQVNAVD 853
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 238-266 6.68e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 40.65  E-value: 6.68e-05
                            10        20
                    ....*....|....*....|....*....
gi 2092232601   238 YGNTPLHVACYNGQDVVVNELIDCGANVN 266
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank_4 pfam13637
Ankyrin repeats (many copies);
339-392 8.59e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.11  E-value: 8.59e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2092232601  339 GNTPLHIAARYGHELLINTLITSGADTAKRGVHGMFPLHLAALSGFSDCCRKLL 392
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02946 PHA02946
ankyin-like protein; Provisional
 255-442 9.21e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 46.20  E-value: 9.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  255 VNELIDCGANVNQMNERGFTPLHFAAASTHGALcLELLVCNGADVNMKSKDGKTPLHMTAIHGR--FSRSQTIIQNGAEI 332
Cdd:PHA02946    55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRI-VAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKI 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  333 DCE-DKNGNTPLhIAARYGHELLINTLITSGADT------AKRGVHgmfpLHLAALSGFSDCCRKLLSSGFDIDTPDDFG 405
Cdd:PHA02946   134 NNSvDEEGCGPL-LACTDPSERVFKKIMSIGFEArivdkfGKNHIH----RHLMSDNPKASTISWMMKLGISPSKPDHDG 208

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 2092232601  406 RTCLHAAAAGGNLECLN-LLLNTGADFNKKDKFGRTPL 442
Cdd:PHA02946   209 NTPLHIVCSKTVKNVDIiNLLLPSTDVNKQNKFGDSPL 246
Ank_5 pfam13857
Ankyrin repeats (many copies);
812-863 1.18e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.79  E-value: 1.18e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2092232601  812 GAGIVNSTDAKGRTPLHAAAFTDHVECLQLLLSHNAQVNAVDSSGKTPLMMA 863
Cdd:pfam13857    5 GPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 377-471 1.32e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.04  E-value: 1.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  377 HLAAlSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGADFNKKDKFGRTPLHYAAANCNYQCLFA 456
Cdd:PTZ00322    88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166

                           90
                   ....*....|....*
gi 2092232601  457 LVGSGASVNDLDERG 471
Cdd:PTZ00322   167 LSRHSQCHFELGANA 181
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 816-948 1.81e-04

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: 45.57  E-value: 1.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  816 VNS--TDA--KGRTPLHAAAFTDHVECLQLLLSHNAQVNAVDSS--------------GKTPLMMAAENGQTNTVEVLVS 877
Cdd:cd22196     83 VNAayTDSyyKGQTALHIAIERRNMHLVELLVQNGADVHARASGeffkkkkggpgfyfGELPLSLAACTNQLDIVKFLLE 162

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  878 S--AKADLTLQDSSKNTALHLACS---------------------KGHETSALLILEKITDRNLInatnaalqTPLHVAA 934
Cdd:cd22196    163 NphSPADISARDSMGNTVLHALVEvadntpentkfvtkmyneiliLGAKIRPLLKLEEITNKKGL--------TPLKLAA 234

                          170
                   ....*....|....
gi 2092232601  935 RNGLTVVVQELLGK 948
Cdd:cd22196    235 KTGKIGIFAYILGR 248
Ank_5 pfam13857
Ankyrin repeats (many copies);
225-279 1.82e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.41  E-value: 1.82e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2092232601  225 LLDLG-VDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGANVNQMNERGFTPLHFA 279
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 238-270 2.18e-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: 2.18e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2092232601  238 YGNTPLHVACY-NGQDVVVNELIDCGANVNQMNE 270
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 391-594 2.63e-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: 45.07  E-value: 2.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  391 LLSSGFDIDTpddfGRTCLHAA-----------------AAGGNLECLNLLLNTGADFNkkdkFGRTPLHYAAANCNYQC 453
Cdd:TIGR00870   72 LLNLSCRGAV----GDTLLHAIsleyvdaveaillhllaAFRKSGPLELANDQYTSEFT----PGITALHLAAHRQNYEI 143

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  454 LFALVGSGASVndldergctplHYAAasdtdgKCLEYLlrndanpgirDKQGYNAVHYSAaygHRL----CL---ELIA- 525
Cdd:TIGR00870  144 VKLLLERGASV-----------PARA------CGDFFV----------KSQGVDSFYHGE---SPLnaaaCLgspSIVAl 193

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2092232601  526 -SETPLDVLMETS-GTDMLN----DSDNRAPISPLHLAAYHGHHQALEVLVQSLLDLDVRNNNGRTPLDLAAFKG 594
Cdd:TIGR00870  194 lSEDPADILTADSlGNTLLHllvmENEFKAEYEELSCQMYNFALSLLDKLRDSKELEVILNHQGLTPLKLAAKEG 268
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 639-739 2.64e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.89  E-value: 2.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  639 NAEPQNAVDiqdgngQTPL-MLSV------LNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVEALLQHGAK 711
Cdd:PTZ00322    67 NLTTEEVID------PVVAhMLTVelcqlaASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGAD 140

                           90       100
                   ....*....|....*....|....*...
gi 2092232601  712 SLLRDCRGRTPIHLSAACGHIGVLGALL 739
Cdd:PTZ00322   141 PTLLDKDGKTPLELAEENGFREVVQLLS 168
Ank_5 pfam13857
Ankyrin repeats (many copies);
32-81 3.58e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.64  E-value: 3.58e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2092232601   32 EDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRA 81
Cdd:pfam13857    7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 652-684 3.89e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.81  E-value: 3.89e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2092232601  652 NGQTPLMLSVL-NGHTDCVYSLLNKGANVDAKDK 684
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 140-282 3.92e-04

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: 44.41  E-value: 3.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  140 GRTALHHAAFSGHVEMVSLLLSRGANINA------FDKKDRRAihwGAYMGHIevvkllvthgaevtckdkksytPLHAA 213
Cdd:cd22196     94 GQTALHIAIERRNMHLVELLVQNGADVHArasgefFKKKKGGP---GFYFGEL----------------------PLSLA 148

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  214 ASSGMISVVKYLLD---LGVDMNEPNAYGNTPLHVACYNGQDVVVN---------ELIDCGANVNQM-------NERGFT 274
Cdd:cd22196    149 ACTNQLDIVKFLLEnphSPADISARDSMGNTVLHALVEVADNTPENtkfvtkmynEILILGAKIRPLlkleeitNKKGLT 228


                   ....*...
gi 2092232601  275 PLHFAAAS 282
Cdd:cd22196    229 PLKLAAKT 236
Ank_5 pfam13857
Ankyrin repeats (many copies);
429-478 3.95e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 3.95e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2092232601  429 ADFNKKDKFGRTPLHYAAANCNYQCLFALVGSGASVNDLDERGCTPLHYA 478
Cdd:pfam13857    7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 470-503 3.97e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.81  E-value: 3.97e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2092232601  470 RGCTPLHYAAASDTDGKCLEYLLRNDANPGIRDK 503
Cdd:pfam00023    1 DGNTPLHLAAGRRGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 207-234 3.99e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.72  E-value: 3.99e-04
                            10        20
                    ....*....|....*....|....*...
gi 2092232601   207 YTPLHAAASSGMISVVKYLLDLGVDMNE 234
Cdd:smart00248    3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 822-937 4.08e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 44.46  E-value: 4.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  822 KGRTPLHAAAFTDHVECLQLLLSHNAQVNAVDSS-------------GKTPLMMAAENGQTNTVEVLVSSA--KADLTLQ 886
Cdd:cd22197     93 RGHSALHIAIEKRSLQCVKLLVENGADVHARACGrffqkkqgtcfyfGELPLSLAACTKQWDVVNYLLENPhqPASLQAQ 172

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2092232601  887 DSSKNTALH---LACSKGHETSALL------ILEKITDRN----LINATNAALQTPLHVAARNG 937
Cdd:cd22197    173 DSLGNTVLHalvMIADNSPENSALVikmydgLLQAGARLCptvqLEEISNHEGLTPLKLAAKEG 236
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 822-851 4.23e-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: 4.23e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 2092232601   822 KGRTPLHAAAFTDHVECLQLLLSHNAQVNA 851
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
65-114 4.36e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 4.36e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2092232601   65 ARVNAKDSKWLTPLHRAVASCSEDAVQVLLKHSADVNARDKNWQTPLHIA 114
Cdd:pfam13857    7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 55-195 5.29e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 43.43  E-value: 5.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601   55 EIIELLILSGARVNAK----DSKWLTPLHRAVASCSEDAVQVLLKHSADVNARDKNWQ-TPLHIAAANKAVKCAEALVPL 129
Cdd:PHA02884    47 DIIDAILKLGADPEAPfplsENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLHGCLKCLEILLSY 126

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2092232601  130 LSNVNVSDRAGRTALHHAAFSGHVEMVSLLlsRGANINAFDKKDRRaihwgaYMGHIEVVKLLVTH 195
Cdd:PHA02884   127 GADINIQTNDMVTPIELALMICNNFLAFMI--CDNEISNFYKHPKK------ILINFDILKILVSH 184
Ank_5 pfam13857
Ankyrin repeats (many copies);
540-590 6.09e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.87  E-value: 6.09e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2092232601  540 DMLNDSDNRAPISPLHLAAYHGHHQALEVLVQSLLDLDVRNNNGRTPLDLA 590
Cdd:pfam13857    6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 140-280 6.37e-04

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 43.59  E-value: 6.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  140 GRTALHHAAFSGHVEMVSLLLSRGANINA------FDKKDRraiHWGAYMGHievvkllvthgaevtckdkksyTPLHAA 213
Cdd:cd22194    141 GQTALNIAIERRQGDIVKLLIAKGADVNAhakgvfFNPKYK---HEGFYFGE----------------------TPLALA 195

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  214 ASSGMISVVKYLLDlgvdmNEPNAY------GNTPLH----VA-CYNGQDVVVNELIDC------GANVNQM-NERGFTP 275
Cdd:cd22194    196 ACTNQPEIVQLLME-----KESTDItsqdsrGNTVLHalvtVAeDSKTQNDFVKRMYDMillkseNKNLETIrNNEGLTP 270


                   ....*
gi 2092232601  276 LHFAA 280
Cdd:cd22194    271 LQLAA 275
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 31-249 6.60e-04

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: 43.64  E-value: 6.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601   31 KEDVN--FQDNEKR--TPLHAAAYLGDAEIIELLILSGARVNA------------KDSKWLTPLHRAVASCSE--DAVQV 92
Cdd:cd22196     80 KEFVNaaYTDSYYKgqTALHIAIERRNMHLVELLVQNGADVHArasgeffkkkkgGPGFYFGELPLSLAACTNqlDIVKF 159

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601   93 LLKHS---ADVNARDKNWQTPLHiaaankavkcaeALVPLLSNvnvsdragrtALHHAAFSghVEMVSLLLSRGANINAF 169
Cdd:cd22196    160 LLENPhspADISARDSMGNTVLH------------ALVEVADN----------TPENTKFV--TKMYNEILILGAKIRPL 215

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  170 DKkdrraihwgaymghIEvvkllvthgaEVTckDKKSYTPLHAAASSGMISVVKYLldLGVDMNEPN-----------AY 238
Cdd:cd22196    216 LK--------------LE----------EIT--NKKGLTPLKLAAKTGKIGIFAYI--LGREIKEPEcrhlsrkftewAY 267

                          250
                   ....*....|.
gi 2092232601  239 GntPLHVACYN 249
Cdd:cd22196    268 G--PVHSSLYD 276
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 187-337 6.93e-04

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 43.59  E-value: 6.93e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  187 EVVKLLVTHG-----------AEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMN--------------EPNAYGNT 241
Cdd:cd22194    111 EIVRILLAFAeengildrfinAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNahakgvffnpkykhEGFYFGET 190

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  242 PLHV-ACYNGQDVVVNELIDCGANVNQMNERGFTPLHFAA-----ASTHGALCLE-----LLVCNGADVN-MKSKDGKTP 309
Cdd:cd22194    191 PLALaACTNQPEIVQLLMEKESTDITSQDSRGNTVLHALVtvaedSKTQNDFVKRmydmiLLKSENKNLEtIRNNEGLTP 270

                          170       180
                   ....*....|....*....|....*...
gi 2092232601  310 LHMTAIHGRFSRSQTIIqnGAEIDCEDK 337
Cdd:cd22194    271 LQLAAKMGKAEILKYIL--SREIKEKPN 296
PHA02795 PHA02795
ankyrin-like protein; Provisional
 127-168 7.19e-04

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 43.45  E-value: 7.19e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 2092232601  127 VPLLSNVNVSDRAGRTALHHAAFSGHVEMVSLLLSRGANINA 168
Cdd:PHA02795   208 IPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNA 249
PHA02946 PHA02946
ankyin-like protein; Provisional
 289-475 7.23e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 43.50  E-value: 7.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  289 LELLVCNGADVNMKSKDGKTPLHMTAIHGRFSRSQTIIQNGAEIDCEDKNGNTPLHIAARYGHELL--INTLITSGADTA 366
Cdd:PHA02946    55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIerINLLVQYGAKIN 134

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  367 KR-GVHGMFPLhLAALSGFSDCCRKLLSSGFDIDTPDDFGRTCLHA--AAAGGNLECLNLLLNTGADFNKKDKFGRTPLH 443
Cdd:PHA02946   135 NSvDEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRhlMSDNPKASTISWMMKLGISPSKPDHDGNTPLH 213

                          170       180       190
                   ....*....|....*....|....*....|...
gi 2092232601  444 YAAANCNYQC-LFALVGSGASVNDLDERGCTPL 475
Cdd:PHA02946   214 IVCSKTVKNVdIINLLLPSTDVNKQNKFGDSPL 246
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 473-675 7.37e-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: 43.46  E-value: 7.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  473 TPLHYAAaSDTDGKCLEYLLR-NDANPGIRDKQGYNAVHYSAAYGHRLCLELIASETPLDVLMETSgtdmlndSDNRAPI 551
Cdd:cd22192     19 SPLLLAA-KENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMT-------SDLYQGE 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  552 SPLHLAAYHGHhqalEVLVQSLLD--LDVRNNN----------------GRTPLDLAAFKGHVECVDVLINQGASILVKD 613
Cdd:cd22192     91 TALHIAVVNQN----LNLVRELIArgADVVSPRatgtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQD 166

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2092232601  614 YvVKRTPIHAAAT--NGHSECLRL-LIGNAEP---QNAVD-IQDGNGQTPLMLSVLNGHTDCVYSLLNK 675
Cdd:cd22192    167 S-LGNTVLHILVLqpNKTFACQMYdLILSYDKeddLQPLDlVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
Ank_4 pfam13637
Ankyrin repeats (many copies);
719-776 7.71e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.41  E-value: 7.71e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2092232601  719 GRTPIHLSAACGHIGVLGALLQSATSVDAVpaiaDNHGYTSLHWACYNGHDSCVELLL 776
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAV----DGNGETALHFAASNGNVEVLKLLL 54
PHA02798 PHA02798
ankyrin-like protein; Provisional
 814-920 7.97e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 43.28  E-value: 7.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  814 GIVNSTDAKGRTPL-----HAAAFTDHVECLQLLLSHNAQVNAVDSSGKTPLMMAAENGQTNTVEVLVSSAK--ADLTLQ 886
Cdd:PHA02798    62 ANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLFMIEngADTTLL 141

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2092232601  887 DSSKNTALHLACSKGHETSALLI---LEKITDRNLIN 920
Cdd:PHA02798   142 DKDGFTMLQVYLQSNHHIDIEIIkllLEKGVDINTHN 178
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 221-313 9.30e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 42.66  E-value: 9.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  221 VVKYLLDLGVDMNEP-----NAYgNTPLHVACYNGQDVVVNELIDCGANVNQM-NERGFTPLHFAAasTHGAL-CLELLV 293
Cdd:PHA02884    48 IIDAILKLGADPEAPfplseNSK-TNPLIYAIDCDNDDAAKLLIRYGADVNRYaEEAKITPLYISV--LHGCLkCLEILL 124

                           90       100
                   ....*....|....*....|
gi 2092232601  294 CNGADVNMKSKDGKTPLHMT 313
Cdd:PHA02884   125 SYGADINIQTNDMVTPIELA 144
Ank_5 pfam13857
Ankyrin repeats (many copies);
917-962 9.87e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.10  E-value: 9.87e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2092232601  917 NLINATNAALQTPLHVAARNGLTVVVQELLGKGASVLAVDENGYTP 962
Cdd:pfam13857    7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTA 52
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 582-613 1.02e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 37.65  E-value: 1.02e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2092232601  582 NGRTPLDLAAFK-GHVECVDVLINQGASILVKD 613
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 582-609 1.05e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.57  E-value: 1.05e-03
                            10        20
                    ....*....|....*....|....*...
gi 2092232601   582 NGRTPLDLAAFKGHVECVDVLINQGASI 609
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 238-266 1.06e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.24  E-value: 1.06e-03
                           10        20
                   ....*....|....*....|....*....
gi 2092232601  238 YGNTPLHVACYNGQDVVVNELIDCGANVN 266
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 566-760 1.16e-03

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 42.98  E-value: 1.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  566 LEVLVQSLLDLDVRNNNGRTPLDLAAFKGHVeCVDVL---INQGASILVKdYVVKRTPIHAAATNghseclrllIGNAEP 642
Cdd:PHA02716   195 LEWLCNNGVNVNLQNNHLITPLHTYLITGNV-CASVIkkiIELGGDMDMK-CVNGMSPIMTYIIN---------IDNINP 263

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  643 Q--NA-VDIQDGNGQT--PLMLSVL-----NGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGH--EECVEALLQHGA 710
Cdd:PHA02716   264 EitNIyIESLDGNKVKniPMILHSYitlarNIDISVVYSFLQPGVKLHYKDSAGRTCLHQYILRHNisTDIIKLLHEYGN 343

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2092232601  711 KSLLRDCRGRTPIH--LSAACG------------HIGVLGALLQSATSVDAVpaiaDNHGYTSL 760
Cdd:PHA02716   344 DLNEPDNIGNTVLHtyLSMLSVvnildpetdndiRLDVIQCLISLGADITAV----NCLGYTPL 403
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 338-364 1.19e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.18  E-value: 1.19e-03
                            10        20
                    ....*....|....*....|....*..
gi 2092232601   338 NGNTPLHIAARYGHELLINTLITSGAD 364
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 818-946 1.25e-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: 42.76  E-value: 1.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  818 STDAKGRTPLHAAAFTDHVECLQLLLSHNAQVNA------------VDS--SGKTPLMMAAENGQTNTVEvLVSSAKADL 883
Cdd:TIGR00870  123 SEFTPGITALHLAAHRQNYEIVKLLLERGASVPAracgdffvksqgVDSfyHGESPLNAAACLGSPSIVA-LLSEDPADI 201

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2092232601  884 TLQDSSKNTALHL------------ACSKGHETSALLILEKITD-RNLINATNAALQTPLHVAARNGLTVVVQELL 946
Cdd:TIGR00870  202 LTADSLGNTLLHLlvmenefkaeyeELSCQMYNFALSLLDKLRDsKELEVILNHQGLTPLKLAAKEGRIVLFRLKL 277
Ank_5 pfam13857
Ankyrin repeats (many copies);
462-511 1.26e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.10  E-value: 1.26e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2092232601  462 ASVNDLDERGCTPLHYAA---ASDtdgkCLEYLLRNDANPGIRDKQGYNAVHY 511
Cdd:pfam13857    7 IDLNRLDGEGYTPLHVAAkygALE----IVRVLLAYGVDLNLKDEEGLTALDL 55
Ank_5 pfam13857
Ankyrin repeats (many copies);
291-346 1.30e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.71  E-value: 1.30e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2092232601  291 LLVCNGADVNMKSKDGKTPLHMTAIHGRFSRSQTIIQNGAEIDCEDKNGNTPLHIA 346
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 271-304 1.32e-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: 1.32e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2092232601  271 RGFTPLHFAAASTHGALCLELLVCNGADVNMKSK 304
Cdd:pfam00023    1 DGNTPLHLAAGRRGNLEIVKLLLSKGADVNARDK 34
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 379-517 1.38e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 42.55  E-value: 1.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  379 AALSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGADFNKKDKFGRTPLhYAAANCNYQCLFALV 458
Cdd:PLN03192   532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTAL-WNAISAKHHKIFRIL 610

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2092232601  459 GSGASVNDLDERG---CTplhyaAASDTDGKCLEYLLRNDANPGIRDKQGYNAVHYSAAYGH 517
Cdd:PLN03192   611 YHFASISDPHAAGdllCT-----AAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDH 667
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 325-482 1.42e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 42.55  E-value: 1.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  325 IIQNGAEIDceDKNGNTPLHIAARYGHELLINTLITSGADTAKRGVHGMFPLHLAALSGFSDCCRKLLSSGFDIDTPDDF 404
Cdd:PLN03192   513 LGDNGGEHD--DPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDAN 590

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  405 GRTCLHAAAAGGNLEClnlllntgadFNKKDKFGRTP--------LHYAAANCNYQCLFALVGSGASVNDLDERGCTPLH 476
Cdd:PLN03192   591 GNTALWNAISAKHHKI----------FRILYHFASISdphaagdlLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQ 660


                   ....*.
gi 2092232601  477 YAAASD 482
Cdd:PLN03192   661 VAMAED 666
Ank_4 pfam13637
Ankyrin repeats (many copies);
858-903 1.66e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.64  E-value: 1.66e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2092232601  858 TPLMMAAENGQTNTVEVLVSSaKADLTLQDSSKNTALHLACSKGHE 903
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEK-GADINAVDGNGETALHFAASNGNV 47
PHA02946 PHA02946
ankyin-like protein; Provisional
 222-378 1.75e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 41.96  E-value: 1.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  222 VKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGANVNQMNERGFTPLHFAAAS------------THGAL-- 287
Cdd:PHA02946    55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTddevierinllvQYGAKin 134

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  288 -------CLELLVCN-------------GADVNMKSKDGKTPL--HMTAIHGRFSRSQTIIQNGAEIDCEDKNGNTPLHI 345
Cdd:PHA02946   135 nsvdeegCGPLLACTdpservfkkimsiGFEARIVDKFGKNHIhrHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHI 214

                          170       180       190
                   ....*....|....*....|....*....|....
gi 2092232601  346 A-ARYGHELLINTLITSGADTAKRGVHGMFPLHL 378
Cdd:PHA02946   215 VcSKTVKNVDIINLLLPSTDVNKQNKFGDSPLTL 248
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 822-946 2.17e-03

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 42.09  E-value: 2.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  822 KGRTPLHAAAFTDHVECLQLLLSHNAQVNAVDSS--------------GKTPLMMAAENGQTNTVEVLVSSA--KADLTL 885
Cdd:cd22193     75 EGQTALHIAIERRQGDIVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLSLAACTNQPDIVQYLLENEhqPADIEA 154

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  886 QDSSKNTALH------------------------LACSKGHETSAlliLEKITDRNLInatnaalqTPLHVAARNGLTVV 941
Cdd:cd22193    155 QDSRGNTVLHalvtvadntkentkfvtrmydmilIRGAKLCPTVE---LEEIRNNDGL--------TPLQLAAKMGKIEI 223


                   ....*
gi 2092232601  942 VQELL 946
Cdd:cd22193    224 LKYIL 228
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 42-71 2.24e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.50  E-value: 2.24e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 2092232601   42 RTPLHAAAY-LGDAEIIELLILSGARVNAKD 71
Cdd:pfam00023    3 NTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
Ank_4 pfam13637
Ankyrin repeats (many copies);
891-946 2.26e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.25  E-value: 2.26e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2092232601  891 NTALHLACSKGHETSALLILEKITDrnlINATNAALQTPLHVAARNGLTVVVQELL 946
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGAD---INAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 344-416 2.95e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.42  E-value: 2.95e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2092232601  344 HIAARyGHELLINTLITSGADTAKRGVHGMFPLHLAALSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGG 416
Cdd:PTZ00322    88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENG 159
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 428-510 3.79e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 39.80  E-value: 3.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  428 GADFNKKDK-FGRTPLHYAAA---NCNYQCLFALVGSGASVNDLDERGCTPLH-YAAASDTDGKCLEYLLRNDANPGIRD 502
Cdd:PHA02859    76 GADVNFKTRdNNLSALHHYLSfnkNVEPEILKILIDSGSSITEEDEDGKNLLHmYMCNFNVRINVIKLLIDSGVSFLNKD 155


                   ....*...
gi 2092232601  503 KQGYNAVH 510
Cdd:PHA02859   156 FDNNNILY 163
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 76-105 3.89e-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: 35.73  E-value: 3.89e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 2092232601   76 TPLHRAVASC-SEDAVQVLLKHSADVNARDK 105
Cdd:pfam00023    4 TPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 612-724 4.06e-03

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 41.02  E-value: 4.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  612 KDYVVKRTPIHAAATN---GHSECLRLLIgNAEPQNAVDIQDGN---------GQTPLMLSVLNGHTDCVYSLLNKGANV 679
Cdd:cd21882     21 QRGATGKTCLHKAALNlndGVNEAIMLLL-EAAPDSGNPKELVNapctdefyqGQTALHIAIENRNLNLVRLLVENGADV 99

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2092232601  680 DAK------DKWGRTALHRG-------AVTGHEECVEALLQHGAK---SLLRDCRGRTPIH 724
Cdd:cd21882    100 SARatgrffRKSPGNLFYFGelplslaACTNQEEIVRLLLENGAQpaaLEAQDSLGNTVLH 160
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 137-247 4.08e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 39.09  E-value: 4.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  137 DRAGRTALHHAAFSGHVemVSLLLSRGANINA-------FDKKDRRAIHWGAYMGHI---EVVKLLVTHGAEVTCKDKK- 205
Cdd:PHA02736    14 DIEGENILHYLCRNGGV--TDLLAFKNAISDEnrylvleYNRHGKQCVHIVSNPDKAdpqEKLKLLMEWGADINGKERVf 91

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2092232601  206 SYTPLHAAASSGMISVVKYLLDL-GVDMNEPNAYGNTPLHVAC 247
Cdd:PHA02736    92 GNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVAC 134
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 55-249 4.29e-03

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 40.90  E-value: 4.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601   55 EIIELLI-----------LSGARVNAKDSKWLTPLHRAVASCSEDAVQVLLKHSADVNARDKN------WQ--------T 109
Cdd:cd22194    111 EIVRILLafaeengildrFINAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkYKhegfyfgeT 190

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  110 PLHIAAANKAVKCAEALVPLLS-NVNVSDRAGRTALH-----------HAAFSGHVEMVSLLLSRGANINAF-DKKDRRA 176
Cdd:cd22194    191 PLALAACTNQPEIVQLLMEKEStDITSQDSRGNTVLHalvtvaedsktQNDFVKRMYDMILLKSENKNLETIrNNEGLTP 270

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2092232601  177 IHWGAYMGHIEVVKLLVthGAEVTCKDKKSYTPLHAAASSGMISVVKYllDL-GVDMNEPNAYgntpLHVACYN 249
Cdd:cd22194    271 LQLAAKMGKAEILKYIL--SREIKEKPNRSLSRKFTDWAYGPVSSSLY--DLtNVDTTTDNSV----LEIIVYN 336
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 652-681 4.30e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.64  E-value: 4.30e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 2092232601   652 NGQTPLMLSVLNGHTDCVYSLLNKGANVDA 681
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 618-724 4.71e-03

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 40.90  E-value: 4.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  618 RTPIHAAATNGhseCLRLLIgNAEPQNavdiQDGNGQTPLMLSVLNGHTDCVYSLLNKGANVDAKDK------------- 684
Cdd:cd22194    114 RILLAFAEENG---ILDRFI-NAEYTE----EAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKgvffnpkykhegf 185

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2092232601  685 -WGRTALHRGAVTGHEECVEALLQHGAKSL-LRDCRGRTPIH 724
Cdd:cd22194    186 yFGETPLALAACTNQPEIVQLLMEKESTDItSQDSRGNTVLH 227
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 15-79 4.99e-03

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 40.77  E-value: 4.99e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2092232601   15 AIFNGDPDEVRALIFKKEDVN--------FQDNEKRT------PLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLH 79
Cdd:cd22192     96 AVVNQNLNLVRELIARGADVVspratgtfFRPGPKNLiyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
PHA02791 PHA02791
ankyrin-like protein; Provisional
 752-921 5.22e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 40.03  E-value: 5.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  752 ADNHGYTSLHWACYNGHDSCVELLLEQEVFQKMEGNSFsPLHCAVINDNEGAAEMLidtLGAGIVNST-DAKGRTPLHAA 830
Cdd:PHA02791    26 ADVHGHSALYYAIADNNVRLVCTLLNAGALKNLLENEF-PLHQAATLEDTKIVKIL---LFSGMDDSQfDDKGNTALYYA 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  831 AFTDHVECLQLLLSHNAQVNAVDSSG-KTPLMMAAENGQTNTVEVLVSSAKADLTLqdSSKNTALHLACSKGHETSALLI 909
Cdd:PHA02791   102 VDSGNMQTVKLFVKKNWRLMFYGKTGwKTSFYHAVMLNDVSIVSYFLSEIPSTFDL--AILLSCIHITIKNGHVDMMILL 179

                          170
                   ....*....|..
gi 2092232601  910 LEKITDRNLINA 921
Cdd:PHA02791   180 LDYMTSTNTNNS 191
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 438-466 5.95e-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: 5.95e-03
                            10        20
                    ....*....|....*....|....*....
gi 2092232601   438 GRTPLHYAAANCNYQCLFALVGSGASVND 466
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
842-897 6.88e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.79  E-value: 6.88e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2092232601  842 LLSH-NAQVNAVDSSGKTPLMMAAENGQTNTVEVLVsSAKADLTLQDSSKNTALHLA 897
Cdd:pfam13857    1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLL-AYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
473-523 6.94e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 35.71  E-value: 6.94e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2092232601  473 TPLHYAAASDtDGKCLEYLLRNDANPGIRDKQGYNAVHYSAAYGHRLCLEL 523
Cdd:pfam13637    3 TALHAAAASG-HLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKL 52
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 249-383 7.19e-03

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: 40.17  E-value: 7.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  249 NGQDVVVNELIDCGANVNQMNE-----------RGFTPLHFAAASTHGALcLELLVCNGADVN----------MKSKD-- 305
Cdd:cd22196     60 NGQNDTISLLLDIAEKTGNLKEfvnaaytdsyyKGQTALHIAIERRNMHL-VELLVQNGADVHarasgeffkkKKGGPgf 138

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601  306 --GKTPLHMTAIHGRFSRSQTIIQN---GAEIDCEDKNGNTPLHIAARYGHELLINT---------LITSGAD------- 364
Cdd:cd22196    139 yfGELPLSLAACTNQLDIVKFLLENphsPADISARDSMGNTVLHALVEVADNTPENTkfvtkmyneILILGAKirpllkl 218

                          170       180
                   ....*....|....*....|..
gi 2092232601  365 ---TAKRgvhGMFPLHLAALSG 383
Cdd:cd22196    219 eeiTNKK---GLTPLKLAAKTG 237
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 338-364 8.01e-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: 8.01e-03
                           10        20
                   ....*....|....*....|....*..
gi 2092232601  338 NGNTPLHIAARYGHELLINTLITSGAD 364
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGAD 27
Ank_5 pfam13857
Ankyrin repeats (many copies);
159-213 8.89e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.40  E-value: 8.89e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2092232601  159 LLSRG-ANINAFDKKDRRAIHWGAYMGHIEVVKLLVTHGAEVTCKDKKSYTPLHAA 213
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 338-364 9.15e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.96  E-value: 9.15e-03
                           10        20
                   ....*....|....*....|....*...
gi 2092232601  338 NGNTPLHIAA-RYGHELLINTLITSGAD 364
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGAD 28
PHA02791 PHA02791
ankyrin-like protein; Provisional
 40-167 9.77e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 39.25  E-value: 9.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092232601   40 EKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQVLLKHSADVNARDKN-WQTPL-HIAAAN 117
Cdd:PHA02791    60 ENEFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTgWKTSFyHAVMLN 139

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2092232601  118 KAVKCAEALVPLLSNVNVSDRAgrTALHHAAFSGHVEMVSLLLSRGANIN 167
Cdd:PHA02791   140 DVSIVSYFLSEIPSTFDLAILL--SCIHITIKNGHVDMMILLLDYMTSTN 187
 
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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