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Conserved domains on  [gi|160707915|ref|NP_001104253|]
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ankyrin-1 isoform 1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UPA_2 pfam17809
UPA domain; The UPA domain is conserved in UNC5, PIDD, and Ankyrins. It has a beta sandwich ...
 1277-1406 4.28e-67

UPA domain; The UPA domain is conserved in UNC5, PIDD, and Ankyrins. It has a beta sandwich structure.


:

Pssm-ID: 375346  Cd Length: 131  Bit Score: 222.35  E-value: 4.28e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  1277 VPYMAKFVIFAKMNDAREGRLRCYCMTDDKVDKTLEQHENFVEVARSRDIEVLEGMPLFAELSGNLVPVKKAAQQRSFHF 1356
Cdd:pfam17809    1 VPYLAKFVVFAKRYDPGEARLRCACMTDDGEDKTLEFHEGFTEVARSRDVEVLEGSPVSIELSGNLVPIKKKSQSRQMDF 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 160707915  1357 QSFRENRLAIPVKVRDSSREPGGFLSFLRKTMKYEDTQH-ILCHLNITMPP 1406
Cdd:pfam17809   81 KAFRENRLDGSVRVKDPSDPPKGLLSFMRDAKVDGGTVSqPLCTLNIVLPQ 131
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
209-474 4.30e-57

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 200.18  E-value: 4.30e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  209 ALHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMV 288
Cdd:COG0666    24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIV 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  289 RLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQYNAEIDDIT 368
Cdd:COG0666   104 KLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  369 LDHLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMG 448
Cdd:COG0666   184 NDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAG 263

                         250       260
                  ....*....|....*....|....*.
gi 160707915  449 HLPIVKNLLQRGASPNVSNVKVETPL 474
Cdd:COG0666   264 AALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
552-820 4.73e-57

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 200.18  E-value: 4.73e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  552 ALALLEKEASQACMTKKGFTPLHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSP 631
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  632 AWNGYTPLHIAAKQNQIEVARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQE 711
Cdd:COG0666    84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  712 GHVPVADVLIKHGVTVDATTRMGYTPLHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGA 791
Cdd:COG0666   164 GNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243

                         250       260
                  ....*....|....*....|....*....
gi 160707915  792 SPNEVSSNGTTPLAIAKRLGYISVTDVLK 820
Cdd:COG0666   244 DLNAKDKDGLTALLLAAAAGAALIVKLLL 272
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
43-339 1.14e-53

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 190.17  E-value: 1.14e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   43 ADAATSFLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAG 122
Cdd:COG0666    19 LLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNG 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  123 QDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPlavalqqghenvvahlinygtk 202
Cdd:COG0666    99 DLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTP---------------------- 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  203 gkvrlpaLHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRR 282
Cdd:COG0666   157 -------LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAEN 229

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 160707915  283 GNVIMVRLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILLDHGAPIQAKTKNGL 339
Cdd:COG0666   230 GNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLL 286
Death_ank1 cd08805
Death domain of Ankyrin-1; Death Domain (DD) of the human protein ankyrin-1 (ANK-1) and ...
 1442-1525 9.77e-51

Death domain of Ankyrin-1; Death Domain (DD) of the human protein ankyrin-1 (ANK-1) and related proteins. Ankyrins are modular proteins comprising three conserved domains, an N-terminal membrane-binding domain containing ANK repeats, a spectrin-binding domain and a C-terminal DD. ANK-1, also called ankyrin-R (for restricted), is found in brain, muscle, and erythrocytes and is thought to function in linking integral membrane proteins to the underlying cytoskeleton. It plays a critical nonredundant role in erythroid development and is associated with hereditary spherocytosis (HS), a common disorder of the red cell membrane. The small alternatively-spliced variant, sANK-1, found in striated muscle and concentrated in the sarcoplasmic reticulum (SR) binds obscurin and titin, which facilitates the anchoring of the network SR to the contractile apparatus. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


:

Pssm-ID: 260067  Cd Length: 84  Bit Score: 173.62  E-value: 9.77e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915 1442 DRVEMRMAVIREHLGLSWAELARELQFSVEDINRIRVENPNSLLDQSTALLTLWVDREGENAKMENLYTALRNIDRSEIV 1521
Cdd:cd08805     1 ERVEMKMAVIREHLGLSWAELARELQFSVEDINRIRVENPNSLLEQSTALLNLWVDREGENAKMEPLYPALYSIDRLTIV 80


                  ....
gi 160707915 1522 NMLE 1525
Cdd:cd08805    81 NILE 84
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
 952-1056 1.57e-49

Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.


:

Pssm-ID: 128514  Cd Length: 104  Bit Score: 170.99  E-value: 1.57e-49
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915    952 TGFLVSFMVDARGGSMRGSRhNGLRVVIPPRTCAAPTRITCRLVKPQKLNTPPPLAEEEGLASRIIALGPTGAQFLSPVI 1031
Cdd:smart00218    1 PSFLVSGTFDARGGRLRGPR-TGVRLIIPPGAIPQGTRYTCYLVVHKTLSTPPPLEEGETLLSPVVECGPHGALFLRPVI 79

                            90       100
                    ....*....|....*....|....*
gi 160707915   1032 VEIPHFASHGRGDRELVVLRSENGS 1056
Cdd:smart00218   80 LEVPHCASLRPRDWEIVLLRSENGG 104
Ank_2 pfam12796
Ankyrin repeats (3 copies);
441-531 9.50e-23

Ankyrin repeats (3 copies);


:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 94.03  E-value: 9.50e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   441 LHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQnkAKANAKAKDDQTPLHCAARIGHTGMVK 520
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE--HADVNLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|.
gi 160707915   521 LLLENGASPNL 531
Cdd:pfam12796   79 LLLEKGADINV 89
 
Name Accession Description Interval E-value
UPA_2 pfam17809
UPA domain; The UPA domain is conserved in UNC5, PIDD, and Ankyrins. It has a beta sandwich ...
 1277-1406 4.28e-67

UPA domain; The UPA domain is conserved in UNC5, PIDD, and Ankyrins. It has a beta sandwich structure.


Pssm-ID: 375346  Cd Length: 131  Bit Score: 222.35  E-value: 4.28e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  1277 VPYMAKFVIFAKMNDAREGRLRCYCMTDDKVDKTLEQHENFVEVARSRDIEVLEGMPLFAELSGNLVPVKKAAQQRSFHF 1356
Cdd:pfam17809    1 VPYLAKFVVFAKRYDPGEARLRCACMTDDGEDKTLEFHEGFTEVARSRDVEVLEGSPVSIELSGNLVPIKKKSQSRQMDF 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 160707915  1357 QSFRENRLAIPVKVRDSSREPGGFLSFLRKTMKYEDTQH-ILCHLNITMPP 1406
Cdd:pfam17809   81 KAFRENRLDGSVRVKDPSDPPKGLLSFMRDAKVDGGTVSqPLCTLNIVLPQ 131
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
209-474 4.30e-57

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 200.18  E-value: 4.30e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  209 ALHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMV 288
Cdd:COG0666    24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIV 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  289 RLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQYNAEIDDIT 368
Cdd:COG0666   104 KLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  369 LDHLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMG 448
Cdd:COG0666   184 NDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAG 263

                         250       260
                  ....*....|....*....|....*.
gi 160707915  449 HLPIVKNLLQRGASPNVSNVKVETPL 474
Cdd:COG0666   264 AALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
552-820 4.73e-57

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 200.18  E-value: 4.73e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  552 ALALLEKEASQACMTKKGFTPLHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSP 631
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  632 AWNGYTPLHIAAKQNQIEVARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQE 711
Cdd:COG0666    84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  712 GHVPVADVLIKHGVTVDATTRMGYTPLHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGA 791
Cdd:COG0666   164 GNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243

                         250       260
                  ....*....|....*....|....*....
gi 160707915  792 SPNEVSSNGTTPLAIAKRLGYISVTDVLK 820
Cdd:COG0666   244 DLNAKDKDGLTALLLAAAAGAALIVKLLL 272
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
43-339 1.14e-53

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 190.17  E-value: 1.14e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   43 ADAATSFLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAG 122
Cdd:COG0666    19 LLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNG 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  123 QDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPlavalqqghenvvahlinygtk 202
Cdd:COG0666    99 DLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTP---------------------- 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  203 gkvrlpaLHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRR 282
Cdd:COG0666   157 -------LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAEN 229

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 160707915  283 GNVIMVRLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILLDHGAPIQAKTKNGL 339
Cdd:COG0666   230 GNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLL 286
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
354-625 9.24e-53

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 187.85  E-value: 9.24e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  354 VRLLLQYNAEIDDITLDHLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAV 433
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  434 TESGLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKAKANAKAKDDQTPLHCAARI 513
Cdd:COG0666    84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  514 GHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALLEKEASQACMTKKGFTPLHVAAKYGKVRLAELLLEHDA 593
Cdd:COG0666   164 GNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243

                         250       260       270
                  ....*....|....*....|....*....|..
gi 160707915  594 HPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRG 625
Cdd:COG0666   244 DLNAKDKDGLTALLLAAAAGAALIVKLLLLAL 275
Death_ank1 cd08805
Death domain of Ankyrin-1; Death Domain (DD) of the human protein ankyrin-1 (ANK-1) and ...
 1442-1525 9.77e-51

Death domain of Ankyrin-1; Death Domain (DD) of the human protein ankyrin-1 (ANK-1) and related proteins. Ankyrins are modular proteins comprising three conserved domains, an N-terminal membrane-binding domain containing ANK repeats, a spectrin-binding domain and a C-terminal DD. ANK-1, also called ankyrin-R (for restricted), is found in brain, muscle, and erythrocytes and is thought to function in linking integral membrane proteins to the underlying cytoskeleton. It plays a critical nonredundant role in erythroid development and is associated with hereditary spherocytosis (HS), a common disorder of the red cell membrane. The small alternatively-spliced variant, sANK-1, found in striated muscle and concentrated in the sarcoplasmic reticulum (SR) binds obscurin and titin, which facilitates the anchoring of the network SR to the contractile apparatus. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260067  Cd Length: 84  Bit Score: 173.62  E-value: 9.77e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915 1442 DRVEMRMAVIREHLGLSWAELARELQFSVEDINRIRVENPNSLLDQSTALLTLWVDREGENAKMENLYTALRNIDRSEIV 1521
Cdd:cd08805     1 ERVEMKMAVIREHLGLSWAELARELQFSVEDINRIRVENPNSLLEQSTALLNLWVDREGENAKMEPLYPALYSIDRLTIV 80


                  ....
gi 160707915 1522 NMLE 1525
Cdd:cd08805    81 NILE 84
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
 952-1056 1.57e-49

Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.


Pssm-ID: 128514  Cd Length: 104  Bit Score: 170.99  E-value: 1.57e-49
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915    952 TGFLVSFMVDARGGSMRGSRhNGLRVVIPPRTCAAPTRITCRLVKPQKLNTPPPLAEEEGLASRIIALGPTGAQFLSPVI 1031
Cdd:smart00218    1 PSFLVSGTFDARGGRLRGPR-TGVRLIIPPGAIPQGTRYTCYLVVHKTLSTPPPLEEGETLLSPVVECGPHGALFLRPVI 79

                            90       100
                    ....*....|....*....|....*
gi 160707915   1032 VEIPHFASHGRGDRELVVLRSENGS 1056
Cdd:smart00218   80 LEVPHCASLRPRDWEIVLLRSENGG 104
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 579-792 1.96e-39

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 153.28  E-value: 1.96e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  579 YGKVRLAELLLEHDAHPNAAG-----KNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQI----- 648
Cdd:PHA03100    7 LTKSRIIKVKNIKYIIMEDDLndysyKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvk 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  649 EVARSLLQYGGSANAESVQGVTPLHLAAQE--GHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHV--PVADVLIKHG 724
Cdd:PHA03100   87 EIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKG 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  725 VTVDATTR----------------MGYTPLHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLK 788
Cdd:PHA03100  167 VDINAKNRvnyllsygvpinikdvYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLN 246


                  ....
gi 160707915  789 NGAS 792
Cdd:PHA03100  247 NGPS 250
ZU5 pfam00791
ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.
 956-1053 1.84e-37

ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.


Pssm-ID: 459941  Cd Length: 97  Bit Score: 136.12  E-value: 1.84e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   956 VSFMVDARGGSMRGSrHNGLRVVIPPRTCAAPTRITCRLVKPQKLNTPPPLAEEEGLASRIIALGPTGAQFLSPVIVEIP 1035
Cdd:pfam00791    1 VSGLVDSRGGRLVLP-NSGVSLLIPPGAIPEGTRIECYLAVNRDESSRPPLEEGETLLSPVVECGPPGLKFLKPVILEVP 79

                           90
                   ....*....|....*...
gi 160707915  1036 HFASHGRGDRELVVLRSE 1053
Cdd:pfam00791   80 HCASLRPEEWEIVLKRSD 97
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 123-468 9.58e-37

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 149.83  E-value: 9.58e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  123 QDE--VVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLI-NY 199
Cdd:PHA02876  155 QDEllIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIdNR 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  200 GTKGKVRLPALHiAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLN-VAQLLLNRGASVNFTPQNGITPLHI 278
Cdd:PHA02876  235 SNINKNDLSLLK-AIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYL 313

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  279 ASRRG-NVIMVRLLLDRGAQIETRTKDELTPLHCAA---RNGHVRISeiLLDHGAPIQAKTKNGLSPIHMAAQGDHLDCV 354
Cdd:PHA02876  314 MAKNGyDTENIRTLIMLGADVNAADRLYITPLHQAStldRNKDIVIT--LLELGANVNARDYCDKTPIHYAAVRNNVVII 391

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  355 RLLLQYNAEIDDITLDHLTPLHVAAhCGH--HRVAKVLLDKGAKPNSRALNGFTPLHIACKKN-HIRVMELLLKTGASID 431
Cdd:PHA02876  392 NTLLDYGADIEALSQKIGTALHFAL-CGTnpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVN 470

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 160707915  432 AVTESGLTPLHVAsfMGHLPIVKNLLQRGASPNVSNV 468
Cdd:PHA02876  471 AINIQNQYPLLIA--LEYHGIVNILLHYGAELRDSRV 505
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 82-300 2.86e-29

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 122.85  E-value: 2.86e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   82 LHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQD-----EVVRELVNYGANVNAQSQKGFTPLYMAAQE-- 154
Cdd:PHA03100   39 LYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKks 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  155 NHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHE--NVVAHLINYGT----KGKVRLpalhiaarnddtrtaavLLQN 228
Cdd:PHA03100  119 NSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVdinaKNRVNY-----------------LLSY 181

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 160707915  229 DPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLDRGAQIET 300
Cdd:PHA03100  182 GVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 415-625 8.63e-24

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 106.23  E-value: 8.63e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  415 NHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKA 494
Cdd:PHA02875   13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  495 -KANAKAKDDQTPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALLEKEASQACMTKKGFTPL 573
Cdd:PHA02875   93 fADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPL 172

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 160707915  574 HVAAKYGKVRLAELLLEHDAHPNAAGKNG-LTPLHVAVHHNNLDIVKLLLPRG 625
Cdd:PHA02875  173 IIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRG 225
Ank_2 pfam12796
Ankyrin repeats (3 copies);
441-531 9.50e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 94.03  E-value: 9.50e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   441 LHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQnkAKANAKAKDDQTPLHCAARIGHTGMVK 520
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE--HADVNLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|.
gi 160707915   521 LLLENGASPNL 531
Cdd:pfam12796   79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
82-172 2.01e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 93.26  E-value: 2.01e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915    82 LHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQDEVVRELVNYgANVNAQSQkGFTPLYMAAQENHLEVVK 161
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                           90
                   ....*....|.
gi 160707915   162 FLLENGANQNV 172
Cdd:pfam12796   79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
507-597 3.11e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.49  E-value: 3.11e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   507 LHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALLEKEASQacMTKKGFTPLHVAAKYGKVRLAE 586
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN--LKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|.
gi 160707915   587 LLLEHDAHPNA 597
Cdd:pfam12796   79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
375-467 4.63e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.10  E-value: 4.63e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   375 LHVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASidAVTESGLTPLHVASFMGHLPIVK 454
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 160707915   455 NLLQRGASPNVSN 467
Cdd:pfam12796   79 LLLEKGADINVKD 91
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
 1441-1527 4.97e-21

DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain present in a variety of proteins with apoptotic functions. Some (but not all) of these domains form homotypic and heterotypic dimers.


Pssm-ID: 214467 [Multi-domain]  Cd Length: 88  Bit Score: 89.01  E-value: 4.97e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   1441 TDRVEMRMAVIREH-LGLSWAELARELQFSVEDINRIRVENPNSLLDQSTALLTLWVDREGENAKMENLYTALRNIDRSE 1519
Cdd:smart00005    1 PELTRQKLAKLLDHpLGLDWRELARKLGLSEADIDQIRTEAPRDLAEQSVQLLRLWEQREGKNATLGTLLEALRKMGRDD 80


                    ....*...
gi 160707915   1520 IVNMLEGS 1527
Cdd:smart00005   81 AVELLRSE 88
Death pfam00531
Death domain;
1445-1525 2.39e-19

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 84.34  E-value: 2.39e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  1445 EMRMAVIREH---LGLSWAELARELQFSVEDINRIRVENPNsLLDQSTALLTLWVDREGENAKMENLYTALRNIDRSEIV 1521
Cdd:pfam00531    1 RKQLDRLLDPpppLGKDWRELARKLGLSENEIDEIESENPR-LRSQTYELLRLWEQREGKNATVGTLLEALRKLGRRDAA 79


                   ....
gi 160707915  1522 NMLE 1525
Cdd:pfam00531   80 EKIQ 83
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 538-714 3.16e-17

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: 87.76  E-value: 3.16e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  538 TPLHTAAREGHVDTALALLEKEASQACMTKK-GFTPLHVAAKYGKVRLAELLLEhdAHPNAAGK-------NGLTPLHVA 609
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGAlGETALHVAALYDNLEAAVVLME--AAPELVNEpmtsdlyQGETALHIA 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  610 VHHNNLDIVKLLLPRGG--------------SPHSPAWNGYTPLHIAAKQNQIEVARSLLQYGGSANAESVQGVTPLH-L 674
Cdd:cd22192    97 VVNQNLNLVRELIARGAdvvspratgtffrpGPKNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHiL 176

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 160707915  675 AAQEGHT---EMVALLLSKQANGNLG------NKSGLTPLHLVSQEGHV 714
Cdd:cd22192   177 VLQPNKTfacQMYDLILSYDKEDDLQpldlvpNNQGLTPFKLAAKEGNI 225
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 210-379 8.52e-17

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: 86.22  E-value: 8.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  210 LHIAARNDDTRTAAVLLQNdPNPDVLSK--TGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQN-----GITPLHIASRR 282
Cdd:cd22192    21 LLLAAKENDVQAIKKLLKC-PSCDLFQRgaLGETALHVAALYDNLEAAVVLMEAAPELVNEPMTsdlyqGETALHIAVVN 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  283 GNVIMVRLLLDRGAQIET---------RTKDELT-----PLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAA-- 346
Cdd:cd22192   100 QNLNLVRELIARGADVVSpratgtffrPGPKNLIyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVlq 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 160707915  347 QGDHLDC--VRLLLQYNAEIDDITLDH------LTPLHVAA 379
Cdd:cd22192   180 PNKTFACqmYDLILSYDKEDDLQPLDLvpnnqgLTPFKLAA 220
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 110-261 8.66e-13

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: 73.64  E-value: 8.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  110 KGNTALHIAALAGQDEVVRELVNYGANVNAQSQKGF--------------TPLYMAAQENHLEVVKFLLENGANqNVATE 175
Cdd:cd22194   140 EGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVFfnpkykhegfyfgeTPLALAACTNQPEIVQLLMEKEST-DITSQ 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  176 DGFTplavalqqgheNVVAHlinygtkgkvrlpALHIAARNDDTRTAAV------LLQNDPNPD---VLSKTGFTPLHIA 246
Cdd:cd22194   219 DSRG-----------NTVLH-------------ALVTVAEDSKTQNDFVkrmydmILLKSENKNletIRNNEGLTPLQLA 274

                         170
                  ....*....|....*
gi 160707915  247 AHYENLNVAQLLLNR 261
Cdd:cd22194   275 AKMGKAEILKYILSR 289
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 406-589 2.87e-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: 65.42  E-value: 2.87e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  406 TPLHIACKKNHIRVMELLLKTgASIDAVTESGL--TPLHVASFMGHLPIVKNLLQrgASPNVSNVKV-------ETPLHM 476
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKC-PSCDLFQRGALgeTALHVAALYDNLEAAVVLME--AAPELVNEPMtsdlyqgETALHI 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  477 AARAGHTEVAKYLLQNKAkanakakDDQTP---------------------LHCAARIGHTGMVKLLLENGASPNLATTA 535
Cdd:cd22192    96 AVVNQNLNLVRELIARGA-------DVVSPratgtffrpgpknliyygehpLSFAACVGNEEIVRLLIEHGADIRAQDSL 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 160707915  536 GHTPLH------TAAREGHVDTALALLEKEASQACM----TKKGFTPLHVAAKYGKVRLAELLL 589
Cdd:cd22192   169 GNTVLHilvlqpNKTFACQMYDLILSYDKEDDLQPLdlvpNNQGLTPFKLAAKEGNIVMFQHLV 232
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 139-359 1.33e-09

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: 63.18  E-value: 1.33e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   139 AQSQKGFTPlymAAQENHLEVVKFLLENGA--NQNVATEDGFTPLAVALQQG-HENVVAHLINYGTKGKVRLPALHIAAR 215
Cdd:TIGR00870   15 SDEEKAFLP---AAERGDLASVYRDLEEPKklNINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAVGDTLLHAISL 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   216 ND--------------DTRTAAVLLQNDPNPDVLSKtGFTPLHIAAHYENLNVAQLLLNRGASVN-------FTPQNGIT 274
Cdd:TIGR00870   92 EYvdaveaillhllaaFRKSGPLELANDQYTSEFTP-GITALHLAAHRQNYEIVKLLLERGASVParacgdfFVKSQGVD 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   275 -------PLHIASRRGNVIMVRLLLDRGAQIETRtkDEL--TPLHCA-------ARNGHVRIS--EILLDHGAPIQAKTK 336
Cdd:TIGR00870  171 sfyhgesPLNAAACLGSPSIVALLSEDPADILTA--DSLgnTLLHLLvmenefkAEYEELSCQmyNFALSLLDKLRDSKE 248

                          250       260       270
                   ....*....|....*....|....*....|
gi 160707915   337 -------NGLSPIHMAAQGDHLDCVRLLLQ 359
Cdd:TIGR00870  249 levilnhQGLTPLKLAAKEGRIVLFRLKLA 278
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 646-808 4.05e-09

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: 61.64  E-value: 4.05e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   646 NQIEVARSLLQYGGSANAESVQ-------GVTPLHLAAQEG-HTEMVALLLSKQANGNLGNksglTPLHLVSQEGHVPVA 717
Cdd:TIGR00870   23 PAAERGDLASVYRDLEEPKKLNincpdrlGRSALFVAAIENeNLELTELLLNLSCRGAVGD----TLLHAISLEYVDAVE 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   718 DVLI-------KHGVTVDATTRM------GYTPLHVASHYGNIKLVKFLLQHQADVNAKTK--------------LGYSP 770
Cdd:TIGR00870   99 AILLhllaafrKSGPLELANDQYtseftpGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESP 178

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 160707915   771 LHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIAK 808
Cdd:TIGR00870  179 LNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLV 216
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 420-573 6.73e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 61.04  E-value: 6.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  420 MELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKAKANAK 499
Cdd:PLN03192  541 LEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPH 620

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160707915  500 AKDDqtpLHC-AARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALLEKEASQACM-TKKGFTPL 573
Cdd:PLN03192  621 AAGD---LLCtAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAnTDDDFSPT 693
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 403-432 8.70e-07

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: 46.81  E-value: 8.70e-07
                            10        20        30
                    ....*....|....*....|....*....|
gi 160707915    403 NGFTPLHIACKKNHIRVMELLLKTGASIDA 432
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 733-762 1.58e-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: 46.04  E-value: 1.58e-06
                            10        20        30
                    ....*....|....*....|....*....|
gi 160707915    733 MGYTPLHVASHYGNIKLVKFLLQHQADVNA 762
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 143-172 2.46e-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: 45.66  E-value: 2.46e-06
                            10        20        30
                    ....*....|....*....|....*....|
gi 160707915    143 KGFTPLYMAAQENHLEVVKFLLENGANQNV 172
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 502-531 2.23e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.96  E-value: 2.23e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 160707915    502 DDQTPLHCAARIGHTGMVKLLLENGASPNL 531
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 78-261 4.54e-05

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: 48.54  E-value: 4.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915    78 GLNGLHLASKEGHVkmVVE--LLHKEIILETTTK-------------KGNTALHIAALAGQDEVVRELVNYGANVNA--- 139
Cdd:TIGR00870   82 GDTLLHAISLEYVD--AVEaiLLHLLAAFRKSGPlelandqytseftPGITALHLAAHRQNYEIVKLLLERGASVPArac 159

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   140 -------QSQKGF----TPLYMAAQENHLEVVKFLLENGANqnvatedgftPLAvALQQGheNVVAHLINYGTKGKVRLP 208
Cdd:TIGR00870  160 gdffvksQGVDSFyhgeSPLNAAACLGSPSIVALLSEDPAD----------ILT-ADSLG--NTLLHLLVMENEFKAEYE 226

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 160707915   209 ALHIA---------ARNDDTRTAAVLLQNDpnpdvlsktGFTPLHIAAHYENLNVAQLLLNR 261
Cdd:TIGR00870  227 ELSCQmynfalsllDKLRDSKELEVILNHQ---------GLTPLKLAAKEGRIVLFRLKLAI 279
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 467-590 1.05e-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: 43.98  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  467 NVKVETPLHMAARAGHTEVAKYLLQNKAKANAKAKDD--------------QTPLHCAARIGHTGMVKLLLENGASP-NL 531
Cdd:cd22194   138 AYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVffnpkykhegfyfgETPLALAACTNQPEIVQLLMEKESTDiTS 217

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 160707915  532 ATTAGHTPLH---TAAR--EGHV-------DTALALLEKEASQACMTKKGFTPLHVAAKYGKVRLAELLLE 590
Cdd:cd22194   218 QDSRGNTVLHalvTVAEdsKTQNdfvkrmyDMILLKSENKNLETIRNNEGLTPLQLAAKMGKAEILKYILS 288
 
Name Accession Description Interval E-value
UPA_2 pfam17809
UPA domain; The UPA domain is conserved in UNC5, PIDD, and Ankyrins. It has a beta sandwich ...
 1277-1406 4.28e-67

UPA domain; The UPA domain is conserved in UNC5, PIDD, and Ankyrins. It has a beta sandwich structure.


Pssm-ID: 375346  Cd Length: 131  Bit Score: 222.35  E-value: 4.28e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  1277 VPYMAKFVIFAKMNDAREGRLRCYCMTDDKVDKTLEQHENFVEVARSRDIEVLEGMPLFAELSGNLVPVKKAAQQRSFHF 1356
Cdd:pfam17809    1 VPYLAKFVVFAKRYDPGEARLRCACMTDDGEDKTLEFHEGFTEVARSRDVEVLEGSPVSIELSGNLVPIKKKSQSRQMDF 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 160707915  1357 QSFRENRLAIPVKVRDSSREPGGFLSFLRKTMKYEDTQH-ILCHLNITMPP 1406
Cdd:pfam17809   81 KAFRENRLDGSVRVKDPSDPPKGLLSFMRDAKVDGGTVSqPLCTLNIVLPQ 131
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
209-474 4.30e-57

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 200.18  E-value: 4.30e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  209 ALHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMV 288
Cdd:COG0666    24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIV 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  289 RLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQYNAEIDDIT 368
Cdd:COG0666   104 KLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  369 LDHLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMG 448
Cdd:COG0666   184 NDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAG 263

                         250       260
                  ....*....|....*....|....*.
gi 160707915  449 HLPIVKNLLQRGASPNVSNVKVETPL 474
Cdd:COG0666   264 AALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
552-820 4.73e-57

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 200.18  E-value: 4.73e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  552 ALALLEKEASQACMTKKGFTPLHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSP 631
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  632 AWNGYTPLHIAAKQNQIEVARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQE 711
Cdd:COG0666    84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  712 GHVPVADVLIKHGVTVDATTRMGYTPLHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGA 791
Cdd:COG0666   164 GNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243

                         250       260
                  ....*....|....*....|....*....
gi 160707915  792 SPNEVSSNGTTPLAIAKRLGYISVTDVLK 820
Cdd:COG0666   244 DLNAKDKDGLTALLLAAAAGAALIVKLLL 272
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
222-507 1.79e-56

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 198.25  E-value: 1.79e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  222 AAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLDRGAQIETR 301
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  302 TKDELTPLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQYNAEIDDITLDHLTPLHVAAHC 381
Cdd:COG0666    84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  382 GHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGA 461
Cdd:COG0666   164 GNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 160707915  462 SPNVSNVKVETPLHMAARAGHTEVAKYLLQNKAKANAKAKDDQTPL 507
Cdd:COG0666   244 DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
252-540 2.95e-56

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 197.87  E-value: 2.95e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  252 LNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILLDHGAPI 331
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  332 QAKTKNGLSPIHMAAQGDHLDCVRLLLQYNAEIDDITLDHLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIA 411
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  412 CKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQ 491
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 160707915  492 NKAKANAKAKDDQTPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPL 540
Cdd:COG0666   241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
417-705 7.14e-56

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 196.71  E-value: 7.14e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  417 IRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKAKA 496
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  497 NAKAKDDQTPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALLEKEASQACMTKKGFTPLHVA 576
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  577 AKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQIEVARSLLQ 656
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 160707915  657 YGGSANAESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPL 705
Cdd:COG0666   241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
154-441 1.47e-55

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 195.94  E-value: 1.47e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  154 ENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLINYGTKGKVRLPALHIAARNDDTRTAAVLLQNDPNPD 233
Cdd:COG0666     2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  234 VLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLDRGAQIETRTKDELTPLHCAA 313
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  314 RNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQYNAEIDDITLDHLTPLHVAAHCGHHRVAKVLLDK 393
Cdd:COG0666   162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 160707915  394 GAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPL 441
Cdd:COG0666   242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
518-804 5.76e-55

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 194.02  E-value: 5.76e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  518 MVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALLEKEASQACMTKKGFTPLHVAAKYGKVRLAELLLEHDAHPNA 597
Cdd:COG0666     3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  598 AGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQIEVARSLLQYGGSANAESVQGVTPLHLAAQ 677
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  678 EGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADVLIKHGVTVDATTRMGYTPLHVASHYGNIKLVKFLLQHQ 757
Cdd:COG0666   163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 160707915  758 ADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPL 804
Cdd:COG0666   243 ADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
320-606 1.15e-54

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 193.25  E-value: 1.15e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  320 ISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQYNAEIDDITLDHLTPLHVAAHCGHHRVAKVLLDKGAKPNS 399
Cdd:COG0666     3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  400 RALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAAR 479
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  480 AGHTEVAKYLLQNKAKANAKAKDDQTPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALLEKE 559
Cdd:COG0666   163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 160707915  560 ASQACMTKKGFTPLHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPL 606
Cdd:COG0666   243 ADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
58-375 1.24e-54

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 193.25  E-value: 1.24e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   58 LDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQDEVVRELVNYGANV 137
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  138 NAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPlavalqqghenvvahlinygtkgkvrlpaLHIAARND 217
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETP-----------------------------LHLAAYNG 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  218 DTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLDRGAQ 297
Cdd:COG0666   132 NLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGAD 211

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 160707915  298 IETRTKDELTPLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQYNAEIDDITLDHLTPL 375
Cdd:COG0666   212 VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
43-339 1.14e-53

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 190.17  E-value: 1.14e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   43 ADAATSFLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAG 122
Cdd:COG0666    19 LLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNG 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  123 QDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPlavalqqghenvvahlinygtk 202
Cdd:COG0666    99 DLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTP---------------------- 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  203 gkvrlpaLHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRR 282
Cdd:COG0666   157 -------LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAEN 229

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 160707915  283 GNVIMVRLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILLDHGAPIQAKTKNGL 339
Cdd:COG0666   230 GNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLL 286
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
285-560 2.08e-53

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 189.39  E-value: 2.08e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  285 VIMVRLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQYNAEI 364
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  365 DDITLDHLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVA 444
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  445 SFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKAKANAKAKDDQTPLHCAARIGHTGMVKLLLE 524
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 160707915  525 NGASPNLATTAGHTPLHTAAREGHVDTALALLEKEA 560
Cdd:COG0666   241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALL 276
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
450-724 3.27e-53

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 189.01  E-value: 3.27e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  450 LPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKAKANAKAKDDQTPLHCAARIGHTGMVKLLLENGASP 529
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  530 NLATTAGHTPLHTAAREGHVDTALALLEKEASQACMTKKGFTPLHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVA 609
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  610 VHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQIEVARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVALLLS 689
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 160707915  690 KQANGNLGNKSGLTPLHLVSQEGHVPVADVLIKHG 724
Cdd:COG0666   241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLAL 275
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
484-767 8.64e-53

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 187.85  E-value: 8.64e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  484 EVAKYLLQNKAKANAKAKDDQTPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALLEKEASQA 563
Cdd:COG0666     2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  564 CMTKKGFTPLHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAA 643
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  644 KQNQIEVARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADVLIKH 723
Cdd:COG0666   162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 160707915  724 GVTVDATTRMGYTPLHVASHYGNIKLVKFLLQHQADVNAKTKLG 767
Cdd:COG0666   242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
354-625 9.24e-53

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 187.85  E-value: 9.24e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  354 VRLLLQYNAEIDDITLDHLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAV 433
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  434 TESGLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKAKANAKAKDDQTPLHCAARI 513
Cdd:COG0666    84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  514 GHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALLEKEASQACMTKKGFTPLHVAAKYGKVRLAELLLEHDA 593
Cdd:COG0666   164 GNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243

                         250       260       270
                  ....*....|....*....|....*....|..
gi 160707915  594 HPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRG 625
Cdd:COG0666   244 DLNAKDKDGLTALLLAAAAGAALIVKLLLLAL 275
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
384-672 1.54e-52

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 187.08  E-value: 1.54e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  384 HRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASP 463
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  464 NVSNVKVETPLHMAARAGHTEVAKYLLQNKAKANAKAKDDQTPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTA 543
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  544 AREGHVDTALALLEKEASQACMTKKGFTPLHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLP 623
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 160707915  624 RGGSPHSPAWNGYTPLHIAAKQNQIEVARSLLQYGGSANAESVQGVTPL 672
Cdd:COG0666   241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
584-820 4.56e-52

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 185.54  E-value: 4.56e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  584 LAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQIEVARSLLQYGGSANA 663
Cdd:COG0666     3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  664 ESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADVLIKHGVTVDATTRMGYTPLHVASH 743
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 160707915  744 YGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIAKRLGYISVTDVLK 820
Cdd:COG0666   163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
Death_ank1 cd08805
Death domain of Ankyrin-1; Death Domain (DD) of the human protein ankyrin-1 (ANK-1) and ...
 1442-1525 9.77e-51

Death domain of Ankyrin-1; Death Domain (DD) of the human protein ankyrin-1 (ANK-1) and related proteins. Ankyrins are modular proteins comprising three conserved domains, an N-terminal membrane-binding domain containing ANK repeats, a spectrin-binding domain and a C-terminal DD. ANK-1, also called ankyrin-R (for restricted), is found in brain, muscle, and erythrocytes and is thought to function in linking integral membrane proteins to the underlying cytoskeleton. It plays a critical nonredundant role in erythroid development and is associated with hereditary spherocytosis (HS), a common disorder of the red cell membrane. The small alternatively-spliced variant, sANK-1, found in striated muscle and concentrated in the sarcoplasmic reticulum (SR) binds obscurin and titin, which facilitates the anchoring of the network SR to the contractile apparatus. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260067  Cd Length: 84  Bit Score: 173.62  E-value: 9.77e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915 1442 DRVEMRMAVIREHLGLSWAELARELQFSVEDINRIRVENPNSLLDQSTALLTLWVDREGENAKMENLYTALRNIDRSEIV 1521
Cdd:cd08805     1 ERVEMKMAVIREHLGLSWAELARELQFSVEDINRIRVENPNSLLEQSTALLNLWVDREGENAKMEPLYPALYSIDRLTIV 80


                  ....
gi 160707915 1522 NMLE 1525
Cdd:cd08805    81 NILE 84
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
 952-1056 1.57e-49

Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.


Pssm-ID: 128514  Cd Length: 104  Bit Score: 170.99  E-value: 1.57e-49
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915    952 TGFLVSFMVDARGGSMRGSRhNGLRVVIPPRTCAAPTRITCRLVKPQKLNTPPPLAEEEGLASRIIALGPTGAQFLSPVI 1031
Cdd:smart00218    1 PSFLVSGTFDARGGRLRGPR-TGVRLIIPPGAIPQGTRYTCYLVVHKTLSTPPPLEEGETLLSPVVECGPHGALFLRPVI 79

                            90       100
                    ....*....|....*....|....*
gi 160707915   1032 VEIPHFASHGRGDRELVVLRSENGS 1056
Cdd:smart00218   80 LEVPHCASLRPRDWEIVLLRSENGG 104
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-228 2.53e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 157.42  E-value: 2.53e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915    1 MAQAAKQLKKIKDIEAQALQEQKEKEESNRKRRNRSRDRKKKADAATSFLRAARSGNLDKALDHLRNGVDINTCNQNGLN 80
Cdd:COG0666    43 ALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGET 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   81 GLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVV 160
Cdd:COG0666   123 PLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 160707915  161 KFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLINYG----TKGKVRLPALHIAARNDDTRTAAVLLQN 228
Cdd:COG0666   203 KLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGadlnAKDKDGLTALLLAAAAGAALIVKLLLLA 274
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
615-819 2.04e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 152.03  E-value: 2.04e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  615 LDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQIEVARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVALLLSKQANG 694
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  695 NLGNKSGLTPLHLVSQEGHVPVADVLIKHGVTVDATTRMGYTPLHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQA 774
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 160707915  775 AQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIAKRLGYISVTDVL 819
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 579-792 1.96e-39

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 153.28  E-value: 1.96e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  579 YGKVRLAELLLEHDAHPNAAG-----KNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQI----- 648
Cdd:PHA03100    7 LTKSRIIKVKNIKYIIMEDDLndysyKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvk 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  649 EVARSLLQYGGSANAESVQGVTPLHLAAQE--GHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHV--PVADVLIKHG 724
Cdd:PHA03100   87 EIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKG 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  725 VTVDATTR----------------MGYTPLHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLK 788
Cdd:PHA03100  167 VDINAKNRvnyllsygvpinikdvYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLN 246


                  ....
gi 160707915  789 NGAS 792
Cdd:PHA03100  247 NGPS 250
ZU5 pfam00791
ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.
 956-1053 1.84e-37

ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.


Pssm-ID: 459941  Cd Length: 97  Bit Score: 136.12  E-value: 1.84e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   956 VSFMVDARGGSMRGSrHNGLRVVIPPRTCAAPTRITCRLVKPQKLNTPPPLAEEEGLASRIIALGPTGAQFLSPVIVEIP 1035
Cdd:pfam00791    1 VSGLVDSRGGRLVLP-NSGVSLLIPPGAIPEGTRIECYLAVNRDESSRPPLEEGETLLSPVVECGPPGLKFLKPVILEVP 79

                           90
                   ....*....|....*...
gi 160707915  1036 HFASHGRGDRELVVLRSE 1053
Cdd:pfam00791   80 HCASLRPEEWEIVLKRSD 97
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 123-468 9.58e-37

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 149.83  E-value: 9.58e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  123 QDE--VVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLI-NY 199
Cdd:PHA02876  155 QDEllIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIdNR 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  200 GTKGKVRLPALHiAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLN-VAQLLLNRGASVNFTPQNGITPLHI 278
Cdd:PHA02876  235 SNINKNDLSLLK-AIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYL 313

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  279 ASRRG-NVIMVRLLLDRGAQIETRTKDELTPLHCAA---RNGHVRISeiLLDHGAPIQAKTKNGLSPIHMAAQGDHLDCV 354
Cdd:PHA02876  314 MAKNGyDTENIRTLIMLGADVNAADRLYITPLHQAStldRNKDIVIT--LLELGANVNARDYCDKTPIHYAAVRNNVVII 391

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  355 RLLLQYNAEIDDITLDHLTPLHVAAhCGH--HRVAKVLLDKGAKPNSRALNGFTPLHIACKKN-HIRVMELLLKTGASID 431
Cdd:PHA02876  392 NTLLDYGADIEALSQKIGTALHFAL-CGTnpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVN 470

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 160707915  432 AVTESGLTPLHVAsfMGHLPIVKNLLQRGASPNVSNV 468
Cdd:PHA02876  471 AINIQNQYPLLIA--LEYHGIVNILLHYGAELRDSRV 505
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 225-462 6.42e-34

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 136.72  E-value: 6.42e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  225 LLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVI-----MVRLLLDRGAQIE 299
Cdd:PHA03100   21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLtdvkeIVKLLLEYGANVN 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  300 TRTKDELTPLHCAARN--GHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDH--LDCVRLLLQYNAEIDDITldhltpl 375
Cdd:PHA03100  101 APDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKN------- 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  376 hvaahcghhRVaKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKN 455
Cdd:PHA03100  174 ---------RV-NYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKL 243


                  ....*..
gi 160707915  456 LLQRGAS 462
Cdd:PHA03100  244 LLNNGPS 250
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 273-491 3.75e-33

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 134.41  E-value: 3.75e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  273 ITPLHIASRRGNVIMVRLLLDRGAQIETRTKDELTPLHCAARNGHV-----RISEILLDHGAPIQAKTKNGLSPIHMAAQ 347
Cdd:PHA03100   36 VLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAIS 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  348 G--DHLDCVRLLLQYNAEIDDITLDHLTPLHVAAHCGHH--RVAKVLLDKGAKPNsralngftplhiacKKNHIrvmELL 423
Cdd:PHA03100  116 KksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDIN--------------AKNRV---NYL 178

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 160707915  424 LKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQ 491
Cdd:PHA03100  179 LSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLN 246
PHA03095 PHA03095
ankyrin-like protein; Provisional
 149-447 5.91e-33

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 135.15  E-value: 5.91e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  149 YMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVvahlinygtKGKVRLpalhiaarnddtrtaavLLQN 228
Cdd:PHA03095   19 LLNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKV---------KDIVRL-----------------LLEA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  229 DPNPDVLSKTGFTPLHIAAHYEN-LNVAQLLLNRGASVNFTPQNGITPLHI--ASRRGNVIMVRLLLDRGAQIETRTKDE 305
Cdd:PHA03095   73 GADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYG 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  306 LTPLHCAARNGHVRIS--EILLDHGAPIQAKTKNGLSPIHMAAQG--DHLDCVRLLLQYNAEIDDITLDHLTPLHVAAHC 381
Cdd:PHA03095  153 MTPLAVLLKSRNANVEllRLLIDAGADVYAVDDRFRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSMATG 232

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 160707915  382 GHHRVAKV--LLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLhvaSFM 447
Cdd:PHA03095  233 SSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL---SLM 297
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 225-433 1.16e-32

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 133.25  E-value: 1.16e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  225 LLQNDPNPDVLSKTGFTPLHIAAHY-----ENLNVAQLLLNRGASVNFTPQNGITPLHIAS--RRGNVIMVRLLLDRGAQ 297
Cdd:PHA03100   54 LLDNGADINSSTKNNSTPLHYLSNIkynltDVKEIVKLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGAN 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  298 IETRTKDELTPLHCAARNGHV--RISEILLDHGAPIQAKTKnglspihmaaqgdhldcVRLLLQYNAEIDDITLDHLTPL 375
Cdd:PHA03100  134 VNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKDVYGFTPL 196

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 160707915  376 HVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAV 433
Cdd:PHA03100  197 HYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTI 254
PHA03095 PHA03095
ankyrin-like protein; Provisional
 252-558 5.57e-32

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 132.07  E-value: 5.57e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  252 LNVAQLLLNRGASVNFTPQNGITPLHIASRRGN---VIMVRLLLDRGAQIETRTKDELTPLHCAARNGHV-RISEILLDH 327
Cdd:PHA03095   27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKA 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  328 GAPIQAKTKNGLSPIHMAAQGD--HLDCVRLLLQYNAEIDDITLDHLTPLHVaaHCGHHRVA----KVLLDKGAKPNSRA 401
Cdd:PHA03095  107 GADVNAKDKVGRTPLHVYLSGFniNPKVIRLLLRKGADVNALDLYGMTPLAV--LLKSRNANvellRLLIDAGADVYAVD 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  402 LNGFTPLHI---ACKKNHiRVMELLLKTGASIDAVTESGLTPLHVASFMGHL--PIVKNLLQRGASPNVSNVKVETPLHM 476
Cdd:PHA03095  185 DRFRSLLHHhlqSFKPRA-RIVRELIRAGCDPAATDMLGNTPLHSMATGSSCkrSLVLPLLIAGISINARNRYGQTPLHY 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  477 AARAGHTEVAKYLLQNkakanakakddqtplhcaarightgmvklllenGASPNLATTAGHTPLHTAAREGHVDTALALL 556
Cdd:PHA03095  264 AAVFNNPRACRRLIAL---------------------------------GADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310


                  ..
gi 160707915  557 EK 558
Cdd:PHA03095  311 AK 312
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 246-465 2.35e-31

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 128.96  E-value: 2.35e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  246 AAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILL 325
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  326 DHGAPIQ-AKTKNGLSPIHMAAQGDHLDCVRLLLQYNAEIDDITLDHLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNG 404
Cdd:PHA02875   89 DLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCG 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 160707915  405 FTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLP-IVKNLLQRGASPNV 465
Cdd:PHA02875  169 CTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIdIVRLFIKRGADCNI 230
Death_ank cd08317
Death domain associated with Ankyrins; Death Domain (DD) associated with Ankyrins. Ankyrins ...
 1442-1525 3.99e-31

Death domain associated with Ankyrins; Death Domain (DD) associated with Ankyrins. Ankyrins are modular proteins comprising three conserved domains, an N-terminal membrane-binding domain containing ANK repeats, a spectrin-binding domain and a C-terminal DD. Ankyrins function as adaptor proteins and they interact, through ANK repeats, with structurally diverse membrane proteins, including ion channels/pumps, calcium release channels, and cell adhesion molecules. They play critical roles in the proper expression and membrane localization of these proteins. In mammals, this family includes ankyrin-R for restricted (or ANK1), ankyrin-B for broadly expressed (or ANK2) and ankyrin-G for general or giant (or ANK3). They are expressed in different combinations in many tissues and play non-overlapping functions. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260029  Cd Length: 84  Bit Score: 117.75  E-value: 3.99e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915 1442 DRVEMRMAVIREHLGLSWAELARELQFSVEDINRIRVENPNSLLDQSTALLTLWVDREGENAKMENLYTALRNIDRSEIV 1521
Cdd:cd08317     1 HRADLRLSDIANLLGSDWPELARELGVSEEDIDLIRSENPNSLAQQAMAMLRLWLEREGEKATGNALESALKKIGRDDIV 80


                  ....
gi 160707915 1522 NMLE 1525
Cdd:cd08317    81 EKCE 84
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
47-214 1.17e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 123.91  E-value: 1.17e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   47 TSFLRAARSGNLD--KALdhLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQD 124
Cdd:COG0666   122 TPLHLAAYNGNLEivKLL--LEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHL 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  125 EVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLINYGTKGK 204
Cdd:COG0666   200 EIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLA 279

                         170
                  ....*....|
gi 160707915  205 VRLPALHIAA 214
Cdd:COG0666   280 AALLDLLTLL 289
PHA03095 PHA03095
ankyrin-like protein; Provisional
 519-845 8.49e-30

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 125.52  E-value: 8.49e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  519 VKLLLENGASPNLATTAGHTPLHTAAREGH---VDTALALLEKEASQACMTKKGFTPLHVAAKYGKV-RLAELLLEHDAH 594
Cdd:PHA03095   30 VRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGAD 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  595 PNAAGKNGLTPLHV--AVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQIEVA--RSLLQYGGSANAESVQGVT 670
Cdd:PHA03095  110 VNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVEllRLLIDAGADVYAVDDRFRS 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  671 PLHLAAQEGHT--EMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADV--LIKHGVTVDATTRMGYTPLHVASHYGN 746
Cdd:PHA03095  190 LLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNN 269

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  747 IKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNEVSsnGTtpLAIAKRLGYISVTD-----VLKV 821
Cdd:PHA03095  270 PRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVA--AT--LNTASVAGGDIPSDatrlcVAKV 345

                         330       340
                  ....*....|....*....|....
gi 160707915  822 VTDETSVVLvSDKHRMSYPETVDE 845
Cdd:PHA03095  346 VLRGAFSLL-PEPIRAYHADFIRE 368
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 233-512 2.24e-29

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 124.22  E-value: 2.24e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  233 DVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLdrGAQIETRTKDELTPLHCA 312
Cdd:PHA02878   31 TSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMI--RSINKCSVFYTLVAIKDA 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  313 ARNGHVRISE-ILLDHGAPIQAKTkngLSPIHMAAQGDHLDC--VRLLLQYNAEIDDITLDHL-TPLHVAAHCGHHRVAK 388
Cdd:PHA02878  109 FNNRNVEIFKiILTNRYKNIQTID---LVYIDKKSKDDIIEAeiTKLLLSYGADINMKDRHKGnTALHYATENKDQRLTE 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  389 VLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVA-SFMGHLPIVKNLLQRGASPNV-S 466
Cdd:PHA02878  186 LLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAkS 265

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 160707915  467 NVKVETPLHMAARAghTEVAKYLLQNKAKANAKAKDDQTPLHCAAR 512
Cdd:PHA02878  266 YILGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAVK 309
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 82-300 2.86e-29

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 122.85  E-value: 2.86e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   82 LHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQD-----EVVRELVNYGANVNAQSQKGFTPLYMAAQE-- 154
Cdd:PHA03100   39 LYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKks 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  155 NHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHE--NVVAHLINYGT----KGKVRLpalhiaarnddtrtaavLLQN 228
Cdd:PHA03100  119 NSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVdinaKNRVNY-----------------LLSY 181

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 160707915  229 DPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLDRGAQIET 300
Cdd:PHA03100  182 GVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 289-579 8.93e-29

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 121.61  E-value: 8.93e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  289 RLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLlqynaeIDDIT 368
Cdd:PHA02874   19 KIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLL------IDNGV 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  369 LDHLTPLHvaahCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMG 448
Cdd:PHA02874   93 DTSILPIP----CIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHN 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  449 HLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKAKANAKAKDDQTPLHCAarIGHTGMVKLLLENGAS 528
Cdd:PHA02874  169 FFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA--IIHNRSAIELLINNAS 246

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 160707915  529 PNLATTAGHTPLHTAAR-EGHVDTALALLEKEASQACMTKKGFTPLHVAAKY 579
Cdd:PHA02874  247 INDQDIDGSTPLHHAINpPCDIDIIDILLYHKADISIKDNKGENPIDTAFKY 298
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 215-527 8.94e-29

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 124.79  E-value: 8.94e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  215 RNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVR----- 289
Cdd:PHA02876  154 QQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKaiidn 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  290 ------------------------LLLDRGAQIETRTKDELTPLHCAARNGHV-RISEILLDHGAPIQAKTKNGLSPIH- 343
Cdd:PHA02876  234 rsninkndlsllkairnedletslLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYl 313

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  344 MAAQGDHLDCVRLLLQYNAEIDDITLDHLTPLHVAAHCGHHR-VAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMEL 422
Cdd:PHA02876  314 MAKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKdIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINT 393

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  423 LLKTGASIDAVTESGLTPLHVAsFMGHLPI--VKNLLQRGASPNVSNVKVETPLHMAARAG-HTEVAKYLLQNKAKANAK 499
Cdd:PHA02876  394 LLDYGADIEALSQKIGTALHFA-LCGTNPYmsVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAI 472

                         330       340
                  ....*....|....*....|....*...
gi 160707915  500 AKDDQTPLHCAarIGHTGMVKLLLENGA 527
Cdd:PHA02876  473 NIQNQYPLLIA--LEYHGIVNILLHYGA 498
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 250-593 5.77e-28

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 122.48  E-value: 5.77e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  250 ENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILLDHGA 329
Cdd:PHA02876  156 DELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRS 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  330 PIQaktKNGLSPIHmAAQGDHLDCVRLLLQYNAEIDDITLDHLTPLHVAAHCGH-HRVAKVLLDKGAKPNSRALNGFTPL 408
Cdd:PHA02876  236 NIN---KNDLSLLK-AIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPL 311

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  409 HIACKKNH-IRVMELLLKTGASIDAVTESGLTPLHVASFMG-HLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVA 486
Cdd:PHA02876  312 YLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVII 391

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  487 KYLLQNKAKANAKAKDDQTPLHCAARIGHTGM-VKLLLENGASPNLATTAGHTPLHTAAREG-HVDTALALLEKEASQAC 564
Cdd:PHA02876  392 NTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNA 471

                         330       340
                  ....*....|....*....|....*....
gi 160707915  565 MTKKGFTPLHVAAKYGKVrlAELLLEHDA 593
Cdd:PHA02876  472 INIQNQYPLLIALEYHGI--VNILLHYGA 498
PHA03095 PHA03095
ankyrin-like protein; Provisional
 65-362 6.24e-28

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 119.74  E-value: 6.24e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   65 LRNGVDINTCNQNGLNGLH--LASKEGHVKMVVE-LLHKEIILETTTKKGNTALHIAALAGQDE-VVRELVNYGANVNAQ 140
Cdd:PHA03095   34 LAAGADVNFRGEYGKTPLHlyLHYSSEKVKDIVRlLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAGADVNAK 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  141 SQKGFTPL--YMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENV--VAHLINYG----TKGKVRLPALHI 212
Cdd:PHA03095  114 DKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGadvyAVDDRFRSLLHH 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  213 AARNDDTRTAAV--LLQNDPNPDVLSKTGFTPLHIAAHY---ENLNVAQLLLNrGASVNFTPQNGITPLHIASRRGNVIM 287
Cdd:PHA03095  194 HLQSFKPRARIVreLIRAGCDPAATDMLGNTPLHSMATGsscKRSLVLPLLIA-GISINARNRYGQTPLHYAAVFNNPRA 272

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 160707915  288 VRLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILLDHGAPIQ--AKTKNGLSPihmAAQGDHLDCVRLLLQYNA 362
Cdd:PHA03095  273 CRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAEtvAATLNTASV---AGGDIPSDATRLCVAKVV 346
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 145-444 2.84e-27

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 118.06  E-value: 2.84e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  145 FTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLINYGTKGKVRlpalhiaarnddtrtaav 224
Cdd:PHA02878   38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVF------------------ 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  225 llqndpNPDVLSKTGFtplhiaaHYENLNVAQLLLNRGASVNFTpqngITPLHIASRRGNVI----MVRLLLDRGAQIET 300
Cdd:PHA02878  100 ------YTLVAIKDAF-------NNRNVEIFKIILTNRYKNIQT----IDLVYIDKKSKDDIieaeITKLLLSYGADINM 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  301 RTKDEL-TPLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQYNAEIDDITLDHLTPLHVA- 378
Cdd:PHA02878  163 KDRHKGnTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISv 242

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 160707915  379 AHCGHHRVAKVLLDKGAKPNSRA-LNGFTPLHIACKKNhiRVMELLLKTGASIDAVTESGLTPLHVA 444
Cdd:PHA02878  243 GYCKDYDILKLLLEHGVDVNAKSyILGLTALHSSIKSE--RKLKLLLEYGADINSLNSYKLTPLSSA 307
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 539-812 5.28e-27

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 117.29  E-value: 5.28e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  539 PLHTAAREGHVDTALALLEKEASQACMTKKGFTPLHVAAKY-GKVRLAELLLEHDahpNAAGKNGLTPLHVAVHHNNLDI 617
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEpNKLGMKEMIRSIN---KCSVFYTLVAIKDAFNNRNVEI 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  618 VKLLLPRGGSphspawNGYT----PLHIAAKQNQIE--VARSLLQYGGSANAESV-QGVTPLHLAAQEGHTEMVALLLSK 690
Cdd:PHA02878  117 FKIILTNRYK------NIQTidlvYIDKKSKDDIIEaeITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSY 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  691 QANGNLGNKSGLTPLHLVSQEGHVPVADVLIKHGVTVDATTRMGYTPLHVASHY-GNIKLVKFLLQHQADVNAK-TKLGY 768
Cdd:PHA02878  191 GANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKsYILGL 270

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 160707915  769 SPLHQAAQQghTDIVTLLLKNGASPNEVSSNGTTPLAIA--KRLGY 812
Cdd:PHA02878  271 TALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAvkQYLCI 314
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 609-800 9.11e-27

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 115.47  E-value: 9.11e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  609 AVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQIEVARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVALLL 688
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  689 --SKQANgNLGNKSGLTPLHLVSQEGHVPVADVLIKHGVTVDATTRMGYTPLHVASHYGNIKLVKFLLQHQADVNAKTKL 766
Cdd:PHA02875   89 dlGKFAD-DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCC 167

                         170       180       190
                  ....*....|....*....|....*....|....
gi 160707915  767 GYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSNG 800
Cdd:PHA02875  168 GCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNG 201
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 571-820 2.23e-26

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 114.68  E-value: 2.23e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  571 TPLHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHS---PAWNG------------ 635
Cdd:PHA02874   37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSIlpiPCIEKdmiktildcgid 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  636 --------YTPLHIAAKQNQIEVARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHL 707
Cdd:PHA02874  117 vnikdaelKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  708 VSQEGHVPVADVLIKHGVTVDATTRMGYTPLHVASHYgNIKLVKFLLqHQADVNAKTKLGYSPLHQAAQQG-HTDIVTLL 786
Cdd:PHA02874  197 AAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIH-NRSAIELLI-NNASINDQDIDGSTPLHHAINPPcDIDIIDIL 274

                         250       260       270
                  ....*....|....*....|....*....|....
gi 160707915  787 LKNGASPNEVSSNGTTPLAIAKRlgYISVTDVLK 820
Cdd:PHA02874  275 LYHKADISIKDNKGENPIDTAFK--YINKDPVIK 306
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 576-794 3.23e-26

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 113.55  E-value: 3.23e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  576 AAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQIEVARSLL 655
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  656 QYGGSANAESVQ-GVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADVLIKHGVTVDATTRMG 734
Cdd:PHA02875   89 DLGKFADDVFYKdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCG 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 160707915  735 YTPLHVASHYGNIKLVKFLLQHQADVNAKTKLG-YSPLHQAAQQGHTDIVTLLLKNGASPN 794
Cdd:PHA02875  169 CTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCN 229
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 280-528 3.87e-26

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 113.61  E-value: 3.87e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  280 SRRGNVIMVRLLLDRGAQIETRTKDELTPLHCAARngHVRIS--EILLDHGAPIQAKTKNGLSPIH-----MAAQGDHLD 352
Cdd:PHA03100   10 SRIIKVKNIKYIIMEDDLNDYSYKKPVLPLYLAKE--ARNIDvvKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  353 CVRLLLQYNAEIDDITLDHLTPLHVAA--HCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHI--RVMELLLKTGA 428
Cdd:PHA03100   88 IVKLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGV 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  429 SIDAVTEsgltplhvasfmghlpiVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKAKANAKAKDDQTPLH 508
Cdd:PHA03100  168 DINAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLH 230

                         250       260
                  ....*....|....*....|
gi 160707915  509 CAARIGHTGMVKLLLENGAS 528
Cdd:PHA03100  231 IAILNNNKEIFKLLLNNGPS 250
Death_ank3 cd08803
Death domain of Ankyrin-3; Death Domain (DD) of the human protein ankyrin-3 (ANK-3) and ...
 1442-1525 4.57e-25

Death domain of Ankyrin-3; Death Domain (DD) of the human protein ankyrin-3 (ANK-3) and related proteins. Ankyrins are modular proteins comprising three conserved domains, an N-terminal membrane-binding domain containing ANK repeats, a spectrin-binding domain and a C-terminal DD. ANK-3, also called anykyrin-G (for general or giant), is found in neurons and at least one splice variant has been shown to be essential for propagation of action potentials as a binding partner to neurofascin and voltage-gated sodium channels. It is required for maintaining axo-dendritic polarity, and may be a genetic risk factor associated with bipolar disorder. ANK-3 may also play roles in other cell types. Mutations affecting ANK-3 pathways for Na channel localization are associated with Brugada syndrome, a potentially fatal arrythmia. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 176781  Cd Length: 84  Bit Score: 100.52  E-value: 4.57e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915 1442 DRVEMRMAVIREHLGLSWAELARELQFSVEDINRIRVENPNSLLDQSTALLTLWVDREGENAKMENLYTALRNIDRSEIV 1521
Cdd:cd08803     1 ERTDIRMAIVADHLGLSWTELARELNFSVDEINQIRVENPNSLIAQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIV 80


                  ....
gi 160707915 1522 NMLE 1525
Cdd:cd08803    81 TLLE 84
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 481-696 5.23e-25

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 110.08  E-value: 5.23e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  481 GHTEVAKYLLQNKAKANAKAKDDQTPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALLEKEA 560
Cdd:PHA02875   13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  561 -SQACMTKKGFTPLHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPL 639
Cdd:PHA02875   93 fADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPL 172

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 160707915  640 HIAAKQNQIEVARSLLQYGGSANAESVQG-VTPLHLAAQEGHTEMVALLLSKQANGNL 696
Cdd:PHA02875  173 IIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNI 230
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 121-455 7.07e-25

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 110.05  E-value: 7.07e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  121 AGQDEVVRELV-NYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLINY 199
Cdd:PHA02874   11 SGDIEAIEKIIkNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDN 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  200 GTKGKVrLPALHIaaRNDDTRTaavLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIA 279
Cdd:PHA02874   91 GVDTSI-LPIPCI--EKDMIKT---ILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIA 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  280 SRRGNVIMVRLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQgdHLDCVRLLLQ 359
Cdd:PHA02874  165 IKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLI 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  360 YNAEIDDITLDHLTPLHVAAH--CGHHrVAKVLLDKGAKPNSRALNGFTPLHIACKknHIRVMELLLKTGAsiDAVTESG 437
Cdd:PHA02874  243 NNASINDQDIDGSTPLHHAINppCDID-IIDILLYHKADISIKDNKGENPIDTAFK--YINKDPVIKDIIA--NAVLIKE 317

                         330
                  ....*....|....*...
gi 160707915  438 LTPLHVASFMGHLPIVKN 455
Cdd:PHA02874  318 ADKLKDSDFLEHIEIKDN 335
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 552-819 3.04e-24

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 110.54  E-value: 3.04e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  552 ALALLEKEASQACMTKKGFTPLHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVK------------ 619
Cdd:PHA02876  161 AEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKaiidnrsninkn 240

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  620 -----------------LLLPRGGSPHSPAWNGYTPLHIAAKQNQI-EVARSLLQYGGSANAESVQGVTPLHLAAQEGH- 680
Cdd:PHA02876  241 dlsllkairnedletslLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAKNGYd 320

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  681 TEMVALLLSKQANGNLGNKSGLTPLHLVSQ-EGHVPVADVLIKHGVTVDATTRMGYTPLHVASHYGNIKLVKFLLQHQAD 759
Cdd:PHA02876  321 TENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGAD 400

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  760 ----------------------------------VNAKTKLGYSPLHQAAQQG-HTDIVTLLLKNGASPNEVSSNGTTPL 804
Cdd:PHA02876  401 iealsqkigtalhfalcgtnpymsvktlidrganVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPL 480

                         330
                  ....*....|....*
gi 160707915  805 AIAkrLGYISVTDVL 819
Cdd:PHA02876  481 LIA--LEYHGIVNIL 493
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 155-369 5.16e-24

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 107.00  E-value: 5.16e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  155 NHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLINYGTKGKVRLPA----LHIAARNDDTRTAAVLLQ-ND 229
Cdd:PHA02875   13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDieseLHDAVEEGDVKAVEELLDlGK 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  230 PNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLDRGAQIETRTKDELTPL 309
Cdd:PHA02875   93 FADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPL 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 160707915  310 HCAARNGHVRISEILLDHGAPIQAKTKNG-LSPIHMAAQGDHLDCVRLLLQYNAEIDDITL 369
Cdd:PHA02875  173 IIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNIMFM 233
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 415-625 8.63e-24

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 106.23  E-value: 8.63e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  415 NHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKA 494
Cdd:PHA02875   13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  495 -KANAKAKDDQTPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALLEKEASQACMTKKGFTPL 573
Cdd:PHA02875   93 fADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPL 172

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 160707915  574 HVAAKYGKVRLAELLLEHDAHPNAAGKNG-LTPLHVAVHHNNLDIVKLLLPRG 625
Cdd:PHA02875  173 IIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRG 225
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 386-675 2.28e-23

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 105.43  E-value: 2.28e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  386 VAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNV 465
Cdd:PHA02874   17 IEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSI 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  466 SNVKvetplhmaarAGHTEVAKYLLQNKAKANAKAKDDQTPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAR 545
Cdd:PHA02874   97 LPIP----------CIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIK 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  546 EGHVDTALALLEKEASQACMTKKGFTPLHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNlDIVKLLLpRG 625
Cdd:PHA02874  167 HNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLI-NN 244

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 160707915  626 GSPHSPAWNGYTPLHIAAKQN-QIEVARSLLQYGGSANAESVQGVTPLHLA 675
Cdd:PHA02874  245 ASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTA 295
Death_ank2 cd08804
Death domain of Ankyrin-2; Death Domain (DD) of Ankyrin-2 (ANK-2) and related proteins. ...
 1442-1525 4.69e-23

Death domain of Ankyrin-2; Death Domain (DD) of Ankyrin-2 (ANK-2) and related proteins. Ankyrins are modular proteins comprising three conserved domains, an N-terminal membrane-binding domain containing ANK repeats, a spectrin-binding domain and a C-terminal DD. ANK-2, also called ankyrin-B (for broadly expressed), is required for proper function of the Na/Ca ion exchanger-1 in cardiomyocytes, and is thought to function in linking integral membrane proteins to the underlying cytoskeleton. Human ANK-2 is associated with "Ankyrin-B syndrome", an atypical arrythmia disorder with risk of sudden cardiac death. It also plays key roles in the brain and striated muscle. Loss of ANK-2 is associated with significant nervous system defects and sarcomere disorganization. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260066  Cd Length: 84  Bit Score: 94.77  E-value: 4.69e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915 1442 DRVEMRMAVIREHLGLSWAELARELQFSVEDINRIRVENPNSLLDQSTALLTLWVDREGENAKMENLYTALRNIDRSEIV 1521
Cdd:cd08804     1 ERTEERLAHIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLTQCLTKINRMDIV 80


                  ....
gi 160707915 1522 NMLE 1525
Cdd:cd08804    81 HLME 84
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 405-708 6.83e-23

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 104.58  E-value: 6.83e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  405 FTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNVSN--VKVETPLHMAaragH 482
Cdd:PHA02878   38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFYtlVAIKDAFNNR----N 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  483 TEVAKYLLQNKAKANAKAKDDQTPLHCAARIGHTGMVKLLLENGASPNLATTaghtplhtaareghvdtalallekeasq 562
Cdd:PHA02878  114 VEIFKIILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDR---------------------------- 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  563 acmtKKGFTPLHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIA 642
Cdd:PHA02878  166 ----HKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIS 241

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 160707915  643 AKQ-NQIEVARSLLQYGGSANAES-VQGVTPLHLAAQEghTEMVALLLSKQANGNLGNKSGLTPLHLV 708
Cdd:PHA02878  242 VGYcKDYDILKLLLEHGVDVNAKSyILGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSA 307
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 505-729 7.44e-23

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 103.59  E-value: 7.44e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  505 TPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHV-----DTALALLEKEASQACMTKKGFTPLHVAA-- 577
Cdd:PHA03100   37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAIsk 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  578 KYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVH--HNNLDIVKLLLPRGgsphspawngytplhiaAKQNQIEVARSLL 655
Cdd:PHA03100  117 KSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLEsnKIDLKILKLLIDKG-----------------VDINAKNRVNYLL 179

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 160707915  656 QYGGSANAESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADVLIKHGVTVDA 729
Cdd:PHA03100  180 SYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
Ank_2 pfam12796
Ankyrin repeats (3 copies);
441-531 9.50e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 94.03  E-value: 9.50e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   441 LHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQnkAKANAKAKDDQTPLHCAARIGHTGMVK 520
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE--HADVNLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|.
gi 160707915   521 LLLENGASPNL 531
Cdd:pfam12796   79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
82-172 2.01e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 93.26  E-value: 2.01e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915    82 LHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQDEVVRELVNYgANVNAQSQkGFTPLYMAAQENHLEVVK 161
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                           90
                   ....*....|.
gi 160707915   162 FLLENGANQNV 172
Cdd:pfam12796   79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
507-597 3.11e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.49  E-value: 3.11e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   507 LHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALLEKEASQacMTKKGFTPLHVAAKYGKVRLAE 586
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN--LKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|.
gi 160707915   587 LLLEHDAHPNA 597
Cdd:pfam12796   79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
375-467 4.63e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.10  E-value: 4.63e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   375 LHVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASidAVTESGLTPLHVASFMGHLPIVK 454
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 160707915   455 NLLQRGASPNVSN 467
Cdd:pfam12796   79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
342-432 6.45e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 91.72  E-value: 6.45e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   342 IHMAAQGDHLDCVRLLLQYNAEIDDITLDHLTPLHVAAHCGHHRVAKVLLDKGAKpnSRALNGFTPLHIACKKNHIRVME 421
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|.
gi 160707915   422 LLLKTGASIDA 432
Cdd:pfam12796   79 LLLEKGADINV 89
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 44-314 9.32e-22

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 100.42  E-value: 9.32e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   44 DAATSFLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMV--------------VELLHKEII------ 103
Cdd:PHA02874   34 ETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIkllidngvdtsilpIPCIEKDMIktildc 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  104 ---LETTTKKGNTALHIAALAGQDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTP 180
Cdd:PHA02874  114 gidVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESP 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  181 lavalqqghenvvahlinygtkgkvrlpaLHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYeNLNVAQLLLN 260
Cdd:PHA02874  194 -----------------------------LHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIH-NRSAIELLIN 243

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 160707915  261 rGASVNFTPQNGITPLHIASRRG-NVIMVRLLLDRGAQIETRTKDELTPLHCAAR 314
Cdd:PHA02874  244 -NASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAFK 297
Ank_2 pfam12796
Ankyrin repeats (3 copies);
309-400 9.34e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 91.33  E-value: 9.34e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   309 LHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQYNAEidDITLDHLTPLHVAAHCGHHRVAK 388
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 160707915   389 VLLDKGAKPNSR 400
Cdd:pfam12796   79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
705-794 1.21e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.95  E-value: 1.21e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   705 LHLVSQEGHVPVADVLIKHGVTVDATTRMGYTPLHVASHYGNIKLVKFLLQHqADVNAKTKlGYSPLHQAAQQGHTDIVT 784
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                           90
                   ....*....|
gi 160707915   785 LLLKNGASPN 794
Cdd:pfam12796   79 LLLEKGADIN 88
Ank_2 pfam12796
Ankyrin repeats (3 copies);
672-763 1.42e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.95  E-value: 1.42e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   672 LHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADVLIKHgVTVDATTRmGYTPLHVASHYGNIKLVK 751
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 160707915   752 FLLQHQADVNAK 763
Cdd:pfam12796   79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
573-663 1.69e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.56  E-value: 1.69e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   573 LHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSphSPAWNGYTPLHIAAKQNQIEVAR 652
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|.
gi 160707915   653 SLLQYGGSANA 663
Cdd:pfam12796   79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
243-334 1.96e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.56  E-value: 1.96e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   243 LHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLDRGAQieTRTKDELTPLHCAARNGHVRISE 322
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 160707915   323 ILLDHGAPIQAK 334
Cdd:pfam12796   79 LLLEKGADINVK 90
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 503-810 4.75e-21

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 98.14  E-value: 4.75e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  503 DQTPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDtALALLEKEASQACMTKKGF-TPLHVAAKYGK 581
Cdd:PHA02875    2 DQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSE-AIKLLMKHGAIPDVKYPDIeSELHDAVEEGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  582 VRLAELLLEHDAHPN-AAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQIEVARSLLQYGGS 660
Cdd:PHA02875   81 VKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKAC 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  661 ANAESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSG-LTPLHLVSQEGHVPVADVLIKHGVTVD-ATTRMG--YT 736
Cdd:PHA02875  161 LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNiMFMIEGeeCT 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 160707915  737 PLHVASHYgniklvkfllqhqaDVNAKTklgysplhQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIAKRL 810
Cdd:PHA02875  241 ILDMICNM--------------CTNLES--------EAIDALIADIAIRIHKKTIRRDEGFKNNMSTIEDKEEF 292
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
 1441-1527 4.97e-21

DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain present in a variety of proteins with apoptotic functions. Some (but not all) of these domains form homotypic and heterotypic dimers.


Pssm-ID: 214467 [Multi-domain]  Cd Length: 88  Bit Score: 89.01  E-value: 4.97e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   1441 TDRVEMRMAVIREH-LGLSWAELARELQFSVEDINRIRVENPNSLLDQSTALLTLWVDREGENAKMENLYTALRNIDRSE 1519
Cdd:smart00005    1 PELTRQKLAKLLDHpLGLDWRELARKLGLSEADIDQIRTEAPRDLAEQSVQLLRLWEQREGKNATLGTLLEALRKMGRDD 80


                    ....*...
gi 160707915   1520 IVNMLEGS 1527
Cdd:smart00005   81 AVELLRSE 88
Ank_2 pfam12796
Ankyrin repeats (3 copies);
115-202 5.43e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.02  E-value: 5.43e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   115 LHIAALAGQDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENgANQNVaTEDGFTPLAVALQQGHENVVA 194
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNL-KDNGRTALHYAARSGHLEIVK 78


                   ....*...
gi 160707915   195 HLINYGTK 202
Cdd:pfam12796   79 LLLEKGAD 86
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 115-440 7.95e-21

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 98.03  E-value: 7.95e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  115 LHIAALAGQDEVVRELVNYGANVNAQSQKGFTPLYMAAQE-------------------------------NHLEVVKFL 163
Cdd:PHA02878   41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEpnklgmkemirsinkcsvfytlvaikdafnnRNVEIFKII 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  164 LENGANQNVATEDGFTPLAVALQQGHENVVAHLINYGTKGKVRL-----PALHIAARNDDTRTAAVLLQNDPNPDVLSKT 238
Cdd:PHA02878  121 LTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDrhkgnTALHYATENKDQRLTELLLSYGANVNIPDKT 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  239 GFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRgnvimvrlLLDrgaqietrtkdeltplhcaarnghV 318
Cdd:PHA02878  201 NNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGY--------CKD------------------------Y 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  319 RISEILLDHGAPIQAK-TKNGLSPIHMAAQGDhlDCVRLLLQYNAEIDDITLDHLTPLHVAA------HCGHHRVAKVLL 391
Cdd:PHA02878  249 DILKLLLEHGVDVNAKsYILGLTALHSSIKSE--RKLKLLLEYGADINSLNSYKLTPLSSAVkqylciNIGRILISNICL 326

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 160707915  392 DKGAKPNSRALNGFTpLHIACKKNHIRVMELLLKTGASIDAVTESGLTP 440
Cdd:PHA02878  327 LKRIKPDIKNSEGFI-DNMDCITSNKRLNQIKDKCEDELNRLASIKITN 374
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 444-662 1.55e-20

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 96.60  E-value: 1.55e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  444 ASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKAKANAKAKDDQTPLHCAARIGHTGMVKLLL 523
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  524 ENGASPN-LATTAGHTPLHTAAREGHVDTALALLEKEASQACMTKKGFTPLHVAAKYGKVRLAELLLEHDAHPNAAGKNG 602
Cdd:PHA02875   89 DLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCG 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 160707915  603 LTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNG-YTPLHIAAKQNQIEVARSLLQYGGSAN 662
Cdd:PHA02875  169 CTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCN 229
Ank_2 pfam12796
Ankyrin repeats (3 copies);
474-561 3.66e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.71  E-value: 3.66e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   474 LHMAARAGHTEVAKYLLQNKAKANAKAKDDQTPLHCAARIGHTGMVKLLLENGASPNlaTTAGHTPLHTAAREGHVDTAL 553
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78


                   ....*...
gi 160707915   554 ALLEKEAS 561
Cdd:pfam12796   79 LLLEKGAD 86
Ank_2 pfam12796
Ankyrin repeats (3 copies);
639-730 5.50e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.32  E-value: 5.50e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   639 LHIAAKQNQIEVARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVALLLSKqANGNLGNKsGLTPLHLVSQEGHVPVAD 718
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 160707915   719 VLIKHGVTVDAT 730
Cdd:pfam12796   79 LLLEKGADINVK 90
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 341-610 7.90e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 94.95  E-value: 7.90e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  341 PIHMAAQGDHLDCVRLLLQYNAEIDDITLDHLTPLHVAAHCGHHRVAKVLLdkgAKPNSRAL-NGFTPLHIACKKNHIRV 419
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMI---RSINKCSVfYTLVAIKDAFNNRNVEI 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  420 MELLLKTgaSIDAVTESGLTPLHVASFMGHL--PIVKNLLQRGASPN-VSNVKVETPLHMAARAGHTEVAKYLLQNKAKA 496
Cdd:PHA02878  117 FKIILTN--RYKNIQTIDLVYIDKKSKDDIIeaEITKLLLSYGADINmKDRHKGNTALHYATENKDQRLTELLLSYGANV 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  497 NAKAKDDQTPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTA-AREGHVDTALALLEKEAS-QACMTKKGFTPLH 574
Cdd:PHA02878  195 NIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDvNAKSYILGLTALH 274

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 160707915  575 VAAKygKVRLAELLLEHDAHPNAAGKNGLTPLHVAV 610
Cdd:PHA02878  275 SSIK--SERKLKLLLEYGADINSLNSYKLTPLSSAV 308
Death cd01670
Death Domain: a protein-protein interaction domain; Death Domains (DDs) are protein-protein ...
 1450-1525 8.96e-20

Death Domain: a protein-protein interaction domain; Death Domains (DDs) are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. Structural analysis of DD-DD complexes show that the domains interact with each other in many different ways. DD-containing proteins serve as adaptors in signaling pathways and they can recruit other proteins into signaling complexes. In mammals, they are prominent components of the programmed cell death (apoptosis) pathway and are found in a number of other signaling pathways. In invertebrates, they are involved in transcriptional regulation of zygotic patterning genes in insect embryogenesis, and are components of the ToII/NF-kappaB pathway, a conserved innate immune pathway in animal cells.


Pssm-ID: 260017 [Multi-domain]  Cd Length: 79  Bit Score: 85.03  E-value: 8.96e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160707915 1450 VIREHLGLSWAELARELQFSVEDINRIRVENPNSLLDQSTALLTLWVDREGENAKMENLYTALRNIDRSEIVNMLE 1525
Cdd:cd01670     4 LVAEELGRDWKKLARKLGLSEGDIDQIEEDNRDDLKEQAYQMLERWREREGDEATLGRLIQALREIGRRDLAEKLE 79
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 581-807 1.03e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 95.90  E-value: 1.03e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  581 KVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQIEVAR-------- 652
Cdd:PHA02876  157 ELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKaiidnrsn 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  653 -------------------SLLQY--GGSANAESVQGVTPLHLAAQEGH-TEMVALLLSKQANGNLGNKSGLTPLHLVSQ 710
Cdd:PHA02876  237 inkndlsllkairnedletSLLLYdaGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAK 316

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  711 EGH-VPVADVLIKHGVTVDATTRMGYTPLHVASHYGNIK-LVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLK 788
Cdd:PHA02876  317 NGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKdIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLD 396

                         250
                  ....*....|....*....
gi 160707915  789 NGASPNEVSSNGTTPLAIA 807
Cdd:PHA02876  397 YGADIEALSQKIGTALHFA 415
Ank_2 pfam12796
Ankyrin repeats (3 copies);
210-301 1.68e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.78  E-value: 1.68e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   210 LHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTpqNGITPLHIASRRGNVIMVR 289
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD--NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 160707915   290 LLLDRGAQIETR 301
Cdd:pfam12796   79 LLLEKGADINVK 90
Death pfam00531
Death domain;
1445-1525 2.39e-19

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 84.34  E-value: 2.39e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  1445 EMRMAVIREH---LGLSWAELARELQFSVEDINRIRVENPNsLLDQSTALLTLWVDREGENAKMENLYTALRNIDRSEIV 1521
Cdd:pfam00531    1 RKQLDRLLDPpppLGKDWRELARKLGLSENEIDEIESENPR-LRSQTYELLRLWEQREGKNATVGTLLEALRKLGRRDAA 79


                   ....
gi 160707915  1522 NMLE 1525
Cdd:pfam00531   80 EKIQ 83
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 603-822 5.08e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 92.64  E-value: 5.08e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  603 LTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQ-NQI---EVARSLLQYGGSANAESVQGvtplhlAAQE 678
Cdd:PHA02878   38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEpNKLgmkEMIRSINKCSVFYTLVAIKD------AFNN 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  679 GHTEMVALLLSKQANGNlgNKSGLTPLHLVSQEGHV--PVADVLIKHGVTVDATTR-MGYTPLHVASHYGNIKLVKFLLQ 755
Cdd:PHA02878  112 RNVEIFKIILTNRYKNI--QTIDLVYIDKKSKDDIIeaEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLS 189

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 160707915  756 HQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIAkrLGYISVTDVLKVV 822
Cdd:PHA02878  190 YGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIS--VGYCKDYDILKLL 254
Ank_2 pfam12796
Ankyrin repeats (3 copies);
408-491 1.05e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.47  E-value: 1.05e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   408 LHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRgASPNVSNVKvETPLHMAARAGHTEVAK 487
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG-RTALHYAARSGHLEIVK 78


                   ....
gi 160707915   488 YLLQ 491
Cdd:pfam12796   79 LLLE 82
PHA03095 PHA03095
ankyrin-like protein; Provisional
 682-806 2.63e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 90.47  E-value: 2.63e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  682 EMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADV---LIKHGVTVDATTRMGYTPLHVASHYGN-IKLVKFLLQHQ 757
Cdd:PHA03095   28 EEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAG 107

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 160707915  758 ADVNAKTKLGYSPLHQ--AAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAI 806
Cdd:PHA03095  108 ADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAV 158
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 52-296 3.76e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 89.28  E-value: 3.76e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   52 AARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQDEVVRELV 131
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  132 NYGANVN-AQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPlavalqqghenvvahlinygtkgkvrlpaL 210
Cdd:PHA02875   89 DLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSP-----------------------------L 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  211 HIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNG-ITPLHIASRRGNVIMVR 289
Cdd:PHA02875  140 HLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVR 219


                  ....*..
gi 160707915  290 LLLDRGA 296
Cdd:PHA02875  220 LFIKRGA 226
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 351-566 7.13e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 88.51  E-value: 7.13e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  351 LDCVRLLLQYNAEIDDITLDHLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASI 430
Cdd:PHA02875   15 LDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  431 DAVT-ESGLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKAKANAKAKDDQTPLHC 509
Cdd:PHA02875   95 DDVFyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLII 174

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 160707915  510 AARIGHTGMVKLLLENGASPNLATTAGH-TPLHTAAREGHVDTALALLEKEASQACMT 566
Cdd:PHA02875  175 AMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADCNIMF 232
Ank_2 pfam12796
Ankyrin repeats (3 copies);
49-140 1.08e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.77  E-value: 1.08e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915    49 FLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMvVELLHKEIILETTTkKGNTALHIAALAGQDEVVR 128
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEI-VKLLLEHADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 160707915   129 ELVNYGANVNAQ 140
Cdd:pfam12796   79 LLLEKGADINVK 90
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 538-714 3.16e-17

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: 87.76  E-value: 3.16e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  538 TPLHTAAREGHVDTALALLEKEASQACMTKK-GFTPLHVAAKYGKVRLAELLLEhdAHPNAAGK-------NGLTPLHVA 609
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGAlGETALHVAALYDNLEAAVVLME--AAPELVNEpmtsdlyQGETALHIA 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  610 VHHNNLDIVKLLLPRGG--------------SPHSPAWNGYTPLHIAAKQNQIEVARSLLQYGGSANAESVQGVTPLH-L 674
Cdd:cd22192    97 VVNQNLNLVRELIARGAdvvspratgtffrpGPKNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHiL 176

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 160707915  675 AAQEGHT---EMVALLLSKQANGNLG------NKSGLTPLHLVSQEGHV 714
Cdd:cd22192   177 VLQPNKTfacQMYDLILSYDKEDDLQpldlvpNNQGLTPFKLAAKEGNI 225
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 646-819 3.30e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 86.20  E-value: 3.30e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  646 NQIEVARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADVLIKHGV 725
Cdd:PHA02875   13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  726 TV-DATTRMGYTPLHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPL 804
Cdd:PHA02875   93 FAdDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPL 172

                         170
                  ....*....|....*
gi 160707915  805 AIAKRLGYISVTDVL 819
Cdd:PHA02875  173 IIAMAKGDIAICKML 187
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 505-691 5.16e-17

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: 86.99  E-value: 5.16e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  505 TPLHCAARIGHTGMVKLLLENGASPNLATTA-GHTPLHTAAREGHVDTALALLE--KEASQACMTK---KGFTPLHVAAK 578
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGAlGETALHVAALYDNLEAAVVLMEaaPELVNEPMTSdlyQGETALHIAVV 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  579 YGKVRLAELLLEHDA---HPNAAG-------KN----GLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAK 644
Cdd:cd22192    99 NQNLNLVRELIARGAdvvSPRATGtffrpgpKNliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVL 178

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 160707915  645 QNQIEVARS----LLQYGGSANAESV------QGVTPLHLAAQEGHTEMVALLLSKQ 691
Cdd:cd22192   179 QPNKTFACQmydlILSYDKEDDLQPLdlvpnnQGLTPFKLAAKEGNIVMFQHLVQKR 235
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 210-379 8.52e-17

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: 86.22  E-value: 8.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  210 LHIAARNDDTRTAAVLLQNdPNPDVLSK--TGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQN-----GITPLHIASRR 282
Cdd:cd22192    21 LLLAAKENDVQAIKKLLKC-PSCDLFQRgaLGETALHVAALYDNLEAAVVLMEAAPELVNEPMTsdlyqGETALHIAVVN 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  283 GNVIMVRLLLDRGAQIET---------RTKDELT-----PLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAA-- 346
Cdd:cd22192   100 QNLNLVRELIARGADVVSpratgtffrPGPKNLIyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVlq 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 160707915  347 QGDHLDC--VRLLLQYNAEIDDITLDH------LTPLHVAA 379
Cdd:cd22192   180 PNKTFACqmYDLILSYDKEDDLQPLDLvpnnqgLTPFKLAA 220
Ank_2 pfam12796
Ankyrin repeats (3 copies);
738-819 1.14e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.69  E-value: 1.14e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   738 LHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASpnEVSSNGTTPLAIAKRLGYISVTD 817
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78


                   ..
gi 160707915   818 VL 819
Cdd:pfam12796   79 LL 80
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 644-810 2.51e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 78.57  E-value: 2.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  644 KQNQIEVARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADVLIKH 723
Cdd:PHA02876  154 QQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDN 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  724 -----------------------------GVTVDATTRMGYTPLHVASHYGNI-KLVKFLLQHQADVNAKTKLGYSPLHQ 773
Cdd:PHA02876  234 rsninkndlsllkairnedletslllydaGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYL 313

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 160707915  774 AAQQGH-TDIVTLLLKNGASPNEVSSNGTTPLAIAKRL 810
Cdd:PHA02876  314 MAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTL 351
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 110-261 8.66e-13

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: 73.64  E-value: 8.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  110 KGNTALHIAALAGQDEVVRELVNYGANVNAQSQKGF--------------TPLYMAAQENHLEVVKFLLENGANqNVATE 175
Cdd:cd22194   140 EGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVFfnpkykhegfyfgeTPLALAACTNQPEIVQLLMEKEST-DITSQ 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  176 DGFTplavalqqgheNVVAHlinygtkgkvrlpALHIAARNDDTRTAAV------LLQNDPNPD---VLSKTGFTPLHIA 246
Cdd:cd22194   219 DSRG-----------NTVLH-------------ALVTVAEDSKTQNDFVkrmydmILLKSENKNletIRNNEGLTPLQLA 274

                         170
                  ....*....|....*
gi 160707915  247 AHYENLNVAQLLLNR 261
Cdd:cd22194   275 AKMGKAEILKYILSR 289
Death_FADD cd08306
Fas-associated Death Domain protein-protein interaction domain; Death domain (DD) found in ...
 1450-1513 1.25e-12

Fas-associated Death Domain protein-protein interaction domain; Death domain (DD) found in FAS-associated via death domain (FADD). FADD is a component of the death-inducing signaling complex (DISC) and serves as an adaptor in the signaling pathway of death receptor proteins. It modulates apoptosis as well as non-apoptotic processes such as cell cycle progression, survival, innate immune signaling, and hematopoiesis. FADD contains an N-terminal DED and a C-terminal DD. Its DD interacts with the DD of the activated death receptor, FAS, and its DED recruits the initiator caspases, caspase-8 and -10, to the DISC complex via a homotypic interaction with the N-terminal DED of the caspase. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and they can recruit other proteins into signaling complexes.


Pssm-ID: 260020  Cd Length: 85  Bit Score: 65.01  E-value: 1.25e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 160707915 1450 VIREHLGLSWAELARELQFSVEDINRIRVENPNSLLDQSTALLTLWVDREGENAKMENLYTALR 1513
Cdd:cd08306     7 VICENLGRDWRQLARKLGLSETKIESISEAHPRNLREQVRQSLREWKKIKKAEATVADLIKALR 70
Ank_4 pfam13637
Ankyrin repeats (many copies);
571-622 2.28e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 63.45  E-value: 2.28e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 160707915   571 TPLHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLL 622
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
734-787 4.79e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 62.29  E-value: 4.79e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 160707915   734 GYTPLHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLL 787
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02946 PHA02946
ankyin-like protein; Provisional
 583-825 7.59e-12

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 69.70  E-value: 7.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  583 RLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQ--IEVARSLLQYGGS 660
Cdd:PHA02946   53 RFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAK 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  661 A-NAESVQGVTPLhLAAQEGHTEMVALLLSKQANGNLGNKSGLTPL--HLVSQEGHVPVADVLIKHGVTVDATTRMGYTP 737
Cdd:PHA02946  133 InNSVDEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFGKNHIhrHLMSDNPKASTISWMMKLGISPSKPDHDGNTP 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  738 LHV--ASHYGNIKLVKFLLQhQADVNAKTKLGYSPLhqaaqqghtdivTLLLKNGASPNEVSSNGTTPLAIAKRLGYISV 815
Cdd:PHA02946  212 LHIvcSKTVKNVDIINLLLP-STDVNKQNKFGDSPL------------TLLIKTLSPAHLINKLLSTSNVITDQTVNICI 278

                         250
                  ....*....|....
gi 160707915  816 ----TDVLKVVTDE 825
Cdd:PHA02946  279 fydrDDVLEIINDK 292
Ank_4 pfam13637
Ankyrin repeats (many copies);
437-490 1.18e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 61.14  E-value: 1.18e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 160707915   437 GLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLL 490
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
111-164 1.74e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 60.75  E-value: 1.74e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 160707915   111 GNTALHIAALAGQDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLL 164
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 670-806 2.37e-11

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 68.89  E-value: 2.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  670 TPLHLAAQEGHTEMVA-LLLSKQAN----GNLGNksglTPLHLVSQEGHVPVADVLIKHG---VTVDATTRM--GYTPLH 739
Cdd:cd22192    19 SPLLLAAKENDVQAIKkLLKCPSCDlfqrGALGE----TALHVAALYDNLEAAVVLMEAApelVNEPMTSDLyqGETALH 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  740 VASHYGNIKLVKFLLQHQADV------------NAKTKLGYS--PLHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLA 805
Cdd:cd22192    95 IAVVNQNLNLVRELIARGADVvspratgtffrpGPKNLIYYGehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174


                  .
gi 160707915  806 I 806
Cdd:cd22192   175 I 175
Ank_4 pfam13637
Ankyrin repeats (many copies);
406-457 2.78e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 60.37  E-value: 2.78e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 160707915   406 TPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLL 457
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 510-693 3.00e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 68.74  E-value: 3.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  510 AARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALLEkeasQACmtkkgftPLHVaakygkvrlaelll 589
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLK----HAC-------NVHI-------------- 586

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  590 eHDAHPNAAGKNGLTplhvAVHHNNLDIVkLLLPRGGSPHSpawnGYTPLHIAAKQNQIEVARSLLQYGGSANAESVQGV 669
Cdd:PLN03192  587 -RDANGNTALWNAIS----AKHHKIFRIL-YHFASISDPHA----AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGA 656

                         170       180
                  ....*....|....*....|....
gi 160707915  670 TPLHLAAQEGHTEMVALLLSKQAN 693
Cdd:PLN03192  657 TALQVAMAEDHVDMVRLLIMNGAD 680
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 253-524 5.34e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 67.46  E-value: 5.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  253 NVAQLLLNRGASVNFTPQ-NGITPLHIASRRGNVIMVRLLLDRGAQIETRTKDElTPLHCAARNGHV------RISEILL 325
Cdd:PHA02989   17 NALEFLLRTGFDVNEEYRgNSILLLYLKRKDVKIKIVKLLIDNGADVNYKGYIE-TPLCAVLRNREItsnkikKIVKLLL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  326 DHGAPIQAKTKNGLSPIHMAAQGDH---LDCVRLLLQYNAEIDDI-TLDHLTPLHVAAHCGHHR--VAKVLLDKGAKP-N 398
Cdd:PHA02989   96 KFGADINLKTFNGVSPIVCFIYNSNinnCDMLRFLLSKGINVNDVkNSRGYNLLHMYLESFSVKkdVIKILLSFGVNLfE 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  399 SRALNGFTPLHIACKKN----HIRVMELLLKTGASI---DAVTESGLTplhvaSFMGHLPI-------VKNLLQRGASPN 464
Cdd:PHA02989  176 KTSLYGLTPMNIYLRNDidviSIKVIKYLIKKGVNIetnNNGSESVLE-----SFLDNNKIlskkefkVLNFILKYIKIN 250

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  465 VSNVKVETPLHMAARAGHTEVAKYLLQNKAKANAKAKDDQTPLHCAARIGHTGMVKLLLE 524
Cdd:PHA02989  251 KKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNRILQ 310
Ank_4 pfam13637
Ankyrin repeats (many copies);
371-424 5.51e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.21  E-value: 5.51e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 160707915   371 HLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLL 424
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 43-186 5.56e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 66.91  E-value: 5.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   43 ADAATSFLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAG 122
Cdd:PHA02874  122 AELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYG 201

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 160707915  123 QDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHlEVVKFLLENgANQNVATEDGFTPLAVALQ 186
Cdd:PHA02874  202 DYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLINN-ASINDQDIDGSTPLHHAIN 263
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 607-797 7.24e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 67.59  E-value: 7.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  607 HVAVHhnNLDIVKLLLPRGGSpHSPAWNGYTPLHIAAKQNQiEVARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVAL 686
Cdd:PLN03192  501 HKELH--DLNVGDLLGDNGGE-HDDPNMASNLLTVASTGNA-ALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLV 576

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  687 LLSKQANGNLGNKSGLTPLHLVSQEGHVPVADVLIKHGVTVDATTrmGYTPLHVASHYGNIKLVKFLLQHQADVNAKTKL 766
Cdd:PLN03192  577 LLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHA--AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQ 654

                         170       180       190
                  ....*....|....*....|....*....|.
gi 160707915  767 GYSPLHQAAQQGHTDIVTLLLKNGASPNEVS 797
Cdd:PLN03192  655 GATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
Ank_4 pfam13637
Ankyrin repeats (many copies);
241-292 1.08e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.44  E-value: 1.08e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 160707915   241 TPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLL 292
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 57-202 1.54e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 66.24  E-value: 1.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   57 NLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIaALAGQDEV--VRELVNYG 134
Cdd:PHA02876  354 NKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHF-ALCGTNPYmsVKTLIDRG 432

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 160707915  135 ANVNAQSQKGFTPLYMAAQEN-HLEVVKFLLENGANQNVATEDGFTPLAVALqqGHENVVAHLINYGTK 202
Cdd:PHA02876  433 ANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGAE 499
Ank_4 pfam13637
Ankyrin repeats (many copies);
305-358 1.62e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.05  E-value: 1.62e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 160707915   305 ELTPLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLL 358
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
338-391 1.73e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.05  E-value: 1.73e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 160707915   338 GLSPIHMAAQGDHLDCVRLLLQYNAEIDDITLDHLTPLHVAAHCGHHRVAKVLL 391
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 406-589 2.87e-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: 65.42  E-value: 2.87e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  406 TPLHIACKKNHIRVMELLLKTgASIDAVTESGL--TPLHVASFMGHLPIVKNLLQrgASPNVSNVKV-------ETPLHM 476
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKC-PSCDLFQRGALgeTALHVAALYDNLEAAVVLME--AAPELVNEPMtsdlyqgETALHI 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  477 AARAGHTEVAKYLLQNKAkanakakDDQTP---------------------LHCAARIGHTGMVKLLLENGASPNLATTA 535
Cdd:cd22192    96 AVVNQNLNLVRELIARGA-------DVVSPratgtffrpgpknliyygehpLSFAACVGNEEIVRLLIEHGADIRAQDSL 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 160707915  536 GHTPLH------TAAREGHVDTALALLEKEASQACM----TKKGFTPLHVAAKYGKVRLAELLL 589
Cdd:cd22192   169 GNTVLHilvlqpNKTFACQMYDLILSYDKEDDLQPLdlvpNNQGLTPFKLAAKEGNIVMFQHLV 232
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 82-294 3.49e-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: 65.03  E-value: 3.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   82 LHLASKEGHVKMVVELL-HKEIILETTTKKGNTALHIAALAGQDEV-------VRELVNygANVNAQSQKGFTPLYMAAQ 153
Cdd:cd22192    21 LLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAavvlmeaAPELVN--EPMTSDLYQGETALHIAVV 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  154 ENHLEVVKFLLENGANQNVATEDG--FT------------PLAVALQQGHENVVAHLINYGTkgkvrlpalhiAARNDDT 219
Cdd:cd22192    99 NQNLNLVRELIARGADVVSPRATGtfFRpgpknliyygehPLSFAACVGNEEIVRLLIEHGA-----------DIRAQDS 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  220 RtaavllqndpnpdvlsktGFTPLHIAAHYENLNVA----QLLLNRGASVNFTP------QNGITPLHIASRRGNVIMVR 289
Cdd:cd22192   168 L------------------GNTVLHILVLQPNKTFAcqmyDLILSYDKEDDLQPldlvpnNQGLTPFKLAAKEGNIVMFQ 229


                  ....*
gi 160707915  290 LLLDR 294
Cdd:cd22192   230 HLVQK 234
Ank_4 pfam13637
Ankyrin repeats (many copies);
472-523 3.53e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 57.28  E-value: 3.53e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 160707915   472 TPLHMAARAGHTEVAKYLLQNKAKANAKAKDDQTPLHCAARIGHTGMVKLLL 523
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 46-200 4.61e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 64.89  E-value: 4.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   46 ATSFLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQDE 125
Cdd:PLN03192  526 ASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHK 605

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 160707915  126 VVRELVNYGANVNAQSqkGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLINYG 200
Cdd:PLN03192  606 IFRILYHFASISDPHA--AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNG 678
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 312-467 4.89e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 64.89  E-value: 4.89e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  312 AARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQY--NAEIDDITLDhlTPLHVAAHCGHHRVAKV 389
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHacNVHIRDANGN--TALWNAISAKHHKIFRI 609

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 160707915  390 LLDKGAKPNSRAlnGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNVSN 467
Cdd:PLN03192  610 LYHFASISDPHA--AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
PHA02798 PHA02798
ankyrin-like protein; Provisional
 231-477 7.59e-10

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 63.70  E-value: 7.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  231 NPDVLSKTgFTPLHIAAHYEN--LNVAQLLLNRGASVNFTPQNGITPL-----HIASRRGNVIMVRLLLDRGAQIETRTK 303
Cdd:PHA02798   29 NPNEIVNE-YSIFQKYLQRDSpsTDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNS 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  304 DELTPLHCAARNGHVRISEILL---DHGAPIQAKTKNGLSPIHMAAQGDH---LDCVRLLLQYNAEIDDIT-LDHLTPLH 376
Cdd:PHA02798  108 DGETPLYCLLSNGYINNLEILLfmiENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINTHNnKEKYDTLH 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  377 VAAHCGHHR----VAKVLLDKG---AKPN----SRALNGFTPLHIACKKNHIRVMELLLKTgASIDAVTESGLTPLHVAS 445
Cdd:PHA02798  188 CYFKYNIDRidadILKLFVDNGfiiNKENkshkKKFMEYLNSLLYDNKRFKKNILDFIFSY-IDINQVDELGFNPLYYSV 266

                         250       260       270
                  ....*....|....*....|....*....|..
gi 160707915  446 FMGHLPIVKNLLQRGASPNVSNVKVETPLHMA 477
Cdd:PHA02798  267 SHNNRKIFEYLLQLGGDINIITELGNTCLFTA 298
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 125-468 1.10e-09

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 63.39  E-value: 1.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  125 EVVRELVNYGANVNAQSQKGFTPL--YMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGhENVVAHLINY--- 199
Cdd:PHA02716  193 DILEWLCNNGVNVNLQNNHLITPLhtYLITGNVCASVIKKIIELGGDMDMKCVNGMSPIMTYIINI-DNINPEITNIyie 271

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  200 ---GTKGKVRLPALHI---AARNDDTRTAAVLLQNDPNPDVLSKTGFTPLH--IAAHYENLNVAQLLLNRGASVNFTPQN 271
Cdd:PHA02716  272 sldGNKVKNIPMILHSyitLARNIDISVVYSFLQPGVKLHYKDSAGRTCLHqyILRHNISTDIIKLLHEYGNDLNEPDNI 351

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  272 GITPLHIASRRGNVI--------------MVRLLLDRGAQIETRTKDELTPLH---CAARN-GHVRISEILldhgapIQA 333
Cdd:PHA02716  352 GNTVLHTYLSMLSVVnildpetdndirldVIQCLISLGADITAVNCLGYTPLTsyiCTAQNyMYYDIIDCL------ISD 425

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  334 KTKNGLSpiHMAAQG-----DHLDCV--RLLLQYNAEIDDITLDH----LTPLHVAAHCGhhrvakvlLDKGAKPNSRAL 402
Cdd:PHA02716  426 KVLNMVK--HRILQDllirvDDTPCIihHIIAKYNIPTDLYTDEYepydSTKIHDVYHCA--------IIERYNNAVCET 495

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160707915  403 NGFTPLHIA--CKKNHIRVME---LLLKTGASIDAVTESGLTPLHVA----SFMGHLP-IVKNLLQRgaSPNVSNV 468
Cdd:PHA02716  496 SGMTPLHVSiiSHTNANIVMDsfvYLLSIQYNINIPTKNGVTPLMLTmrnnRLSGHQWyIVKNILDK--RPNVDIV 569
Ank_4 pfam13637
Ankyrin repeats (many copies);
635-688 1.15e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.74  E-value: 1.15e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 160707915   635 GYTPLHIAAKQNQIEVARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVALLL 688
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 139-359 1.33e-09

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: 63.18  E-value: 1.33e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   139 AQSQKGFTPlymAAQENHLEVVKFLLENGA--NQNVATEDGFTPLAVALQQG-HENVVAHLINYGTKGKVRLPALHIAAR 215
Cdd:TIGR00870   15 SDEEKAFLP---AAERGDLASVYRDLEEPKklNINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAVGDTLLHAISL 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   216 ND--------------DTRTAAVLLQNDPNPDVLSKtGFTPLHIAAHYENLNVAQLLLNRGASVN-------FTPQNGIT 274
Cdd:TIGR00870   92 EYvdaveaillhllaaFRKSGPLELANDQYTSEFTP-GITALHLAAHRQNYEIVKLLLERGASVParacgdfFVKSQGVD 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   275 -------PLHIASRRGNVIMVRLLLDRGAQIETRtkDEL--TPLHCA-------ARNGHVRIS--EILLDHGAPIQAKTK 336
Cdd:TIGR00870  171 sfyhgesPLNAAACLGSPSIVALLSEDPADILTA--DSLgnTLLHLLvmenefkAEYEELSCQmyNFALSLLDKLRDSKE 248

                          250       260       270
                   ....*....|....*....|....*....|
gi 160707915   337 -------NGLSPIHMAAQGDHLDCVRLLLQ 359
Cdd:TIGR00870  249 levilnhQGLTPLKLAAKEGRIVLFRLKLA 278
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 266-363 1.53e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 62.99  E-value: 1.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  266 NFTPQNGITP--LHIAS-------RRGNVIMVRLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILLDHGAPIQAKTK 336
Cdd:PTZ00322   67 NLTTEEVIDPvvAHMLTvelcqlaASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDK 146

                          90       100
                  ....*....|....*....|....*..
gi 160707915  337 NGLSPIHMAAQGDHLDCVRLLLQYNAE 363
Cdd:PTZ00322  147 DGKTPLELAEENGFREVVQLLSRHSQC 173
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 571-807 1.93e-09

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 62.72  E-value: 1.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  571 TPLHVAAKYGKVR-LAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLprggsphspawngytplhiaakqnqiE 649
Cdd:cd22192    19 SPLLLAAKENDVQaIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLM--------------------------E 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  650 VARSLLQYggSANAESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTplhlvsqegHVPVADVLIKHGvtvda 729
Cdd:cd22192    73 AAPELVNE--PMTSDLYQGETALHIAVVNQNLNLVRELIARGADVVSPRATGTF---------FRPGPKNLIYYG----- 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  730 ttrmgYTPLHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVT----LLL-----KNGASPNEVSSN- 799
Cdd:cd22192   137 -----EHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFACqmydLILsydkeDDLQPLDLVPNNq 211


                  ....*...
gi 160707915  800 GTTPLAIA 807
Cdd:cd22192   212 GLTPFKLA 219
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 50-261 2.14e-09

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 62.34  E-value: 2.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   50 LRAARSGNLDkALDHLRNGVDINTCnQNGLNG---LHLASKEGHVKMVVELLH--KEIILETTTK---KGNTALHIAALA 121
Cdd:cd22192    22 LLAAKENDVQ-AIKKLLKCPSCDLF-QRGALGetaLHVAALYDNLEAAVVLMEaaPELVNEPMTSdlyQGETALHIAVVN 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  122 GQDEVVRELVNYGANVNAQSQKG--FT------------PLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQ 187
Cdd:cd22192   100 QNLNLVRELIARGADVVSPRATGtfFRpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQ 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  188 GHENVVAHLINygtkgkvrlpalhiaarnddtrtaaVLLQNDPNPD------VLSKTGFTPLHIAAHYENLNVAQLLLNR 261
Cdd:cd22192   180 PNKTFACQMYD-------------------------LILSYDKEDDlqpldlVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
Ank_4 pfam13637
Ankyrin repeats (many copies);
274-325 2.87e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.59  E-value: 2.87e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 160707915   274 TPLHIASRRGNVIMVRLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILL 325
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 536-694 3.58e-09

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: 61.82  E-value: 3.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  536 GHTPLHTAA---REGHVDTALALLE--------KEASQACMTK---KGFTPLHVAAKYGKVRLAELLLEH--DAHPNAAG 599
Cdd:cd21882    26 GKTCLHKAAlnlNDGVNEAIMLLLEaapdsgnpKELVNAPCTDefyQGQTALHIAIENRNLNLVRLLVENgaDVSARATG 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  600 KN-----------GLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWN---GYTPLHIAAKQNQIEVARS---------LLQ 656
Cdd:cd21882   106 RFfrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPAALEAQdslGNTVLHALVLQADNTPENSafvcqmynlLLS 185

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 160707915  657 YGGSANA----ESV---QGVTPLHLAAQEGHTEMVALLLSKQANG 694
Cdd:cd21882   186 YGAHLDPtqqlEEIpnhQGLTPLKLAAVEGKIVMFQHILQREFSG 230
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 646-808 4.05e-09

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: 61.64  E-value: 4.05e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   646 NQIEVARSLLQYGGSANAESVQ-------GVTPLHLAAQEG-HTEMVALLLSKQANGNLGNksglTPLHLVSQEGHVPVA 717
Cdd:TIGR00870   23 PAAERGDLASVYRDLEEPKKLNincpdrlGRSALFVAAIENeNLELTELLLNLSCRGAVGD----TLLHAISLEYVDAVE 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   718 DVLI-------KHGVTVDATTRM------GYTPLHVASHYGNIKLVKFLLQHQADVNAKTK--------------LGYSP 770
Cdd:TIGR00870   99 AILLhllaafrKSGPLELANDQYtseftpGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESP 178

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 160707915   771 LHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIAK 808
Cdd:TIGR00870  179 LNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLV 216
Ank_5 pfam13857
Ankyrin repeats (many copies);
390-444 5.02e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 53.89  E-value: 5.02e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 160707915   390 LLDKG-AKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVA 444
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 206-327 5.50e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 61.07  E-value: 5.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  206 RLPALHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNvAQLLLNRGASVNFTPQNGITPLHIASRRGNV 285
Cdd:PTZ00322   50 HLEALEATENKDATPDHNLTTEEVIDPVVAHMLTVELCQLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHV 128

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 160707915  286 IMVRLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILLDH 327
Cdd:PTZ00322  129 QVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 569-772 5.58e-09

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: 61.05  E-value: 5.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  569 GFTPLHVAAKY---GKVRLAELLLEHDAHPNAAGK-----------NGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPA-- 632
Cdd:cd21882    26 GKTCLHKAALNlndGVNEAIMLLLEAAPDSGNPKElvnapctdefyQGQTALHIAIENRNLNLVRLLVENGADVSARAtg 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  633 -----------WNGYTPLHIAAKQNQIEVARSLLQYGGSANAESVQ---GVTPLH-LAAQEGHTEMVALLLSKQANGNLG 697
Cdd:cd21882   106 rffrkspgnlfYFGELPLSLAACTNQEEIVRLLLENGAQPAALEAQdslGNTVLHaLVLQADNTPENSAFVCQMYNLLLS 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  698 NKSGLTPLhlvsqeghVPVADVlikhgvtvdaTTRMGYTPLHVASHYGNIKLVKFLLQHQADVNAK------TKLGYSPL 771
Cdd:cd21882   186 YGAHLDPT--------QQLEEI----------PNHQGLTPLKLAAVEGKIVMFQHILQREFSGPYQplsrkfTEWTYGPV 247


                  .
gi 160707915  772 H 772
Cdd:cd21882   248 T 248
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 420-573 6.73e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 61.04  E-value: 6.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  420 MELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKAKANAK 499
Cdd:PLN03192  541 LEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPH 620

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160707915  500 AKDDqtpLHC-AARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALLEKEASQACM-TKKGFTPL 573
Cdd:PLN03192  621 AAGD---LLCtAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAnTDDDFSPT 693
PHA02798 PHA02798
ankyrin-like protein; Provisional
 125-368 7.35e-09

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 60.62  E-value: 7.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  125 EVVRELVNYGANVNAQSQKGFTPL-----YMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLIny 199
Cdd:PHA02798   52 DIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILL-- 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  200 gtkgkvrlpalhiaarnddtrtaaVLLQNDPNPDVLSKTGFTPLHI---AAHYENLNVAQLLLNRGASVN-FTPQNGITP 275
Cdd:PHA02798  130 ------------------------FMIENGADTTLLDKDGFTMLQVylqSNHHIDIEIIKLLLEKGVDINtHNNKEKYDT 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  276 LHIASR----RGNVIMVRLLLDRGAQIETRTK-------DELTPLHCAARNGHVRISEILLDHgAPIQAKTKNGLSPIHM 344
Cdd:PHA02798  186 LHCYFKynidRIDADILKLFVDNGFIINKENKshkkkfmEYLNSLLYDNKRFKKNILDFIFSY-IDINQVDELGFNPLYY 264

                         250       260
                  ....*....|....*....|....
gi 160707915  345 AAQGDHLDCVRLLLQYNAEIDDIT 368
Cdd:PHA02798  265 SVSHNNRKIFEYLLQLGGDINIIT 288
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 387-457 8.08e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 60.68  E-value: 8.08e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 160707915  387 AKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLL 457
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 225-370 9.05e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 60.65  E-value: 9.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  225 LLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLDRGAQIETRTKD 304
Cdd:PLN03192  544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAG 623

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160707915  305 ELtpLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQYNAEIDDITLD 370
Cdd:PLN03192  624 DL--LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTD 687
Ank_4 pfam13637
Ankyrin repeats (many copies);
668-721 9.56e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.05  E-value: 9.56e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 160707915   668 GVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADVLI 721
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 514-602 9.91e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 60.30  E-value: 9.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  514 GHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALLEKEASQACMTKKGFTPLHVAAKYGKVRLAELLLEHDA 593
Cdd:PTZ00322   93 GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQ 172


                  ....*....
gi 160707915  594 HPNAAGKNG 602
Cdd:PTZ00322  173 CHFELGANA 181
PHA02946 PHA02946
ankyin-like protein; Provisional
 92-276 1.06e-08

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 59.68  E-value: 1.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   92 KMVVELLHKEIILETTTKKGNTALHIAALAGQDEVVRELVNYGANVNAQSQKGFTPLYM--AAQENHLEVVKFLLENGAN 169
Cdd:PHA02946   53 RFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYlsGTDDEVIERINLLVQYGAK 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  170 -QNVATEDGFTPLaVALQQGHENVVAHLINYGTKGKV------RLPALHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTP 242
Cdd:PHA02946  133 iNNSVDEEGCGPL-LACTDPSERVFKKIMSIGFEARIvdkfgkNHIHRHLMSDNPKASTISWMMKLGISPSKPDHDGNTP 211

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 160707915  243 LHI--AAHYENLNVAQLLLnrgASVNFTPQN--GITPL 276
Cdd:PHA02946  212 LHIvcSKTVKNVDIINLLL---PSTDVNKQNkfGDSPL 246
Ank_4 pfam13637
Ankyrin repeats (many copies);
701-754 1.11e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.05  E-value: 1.11e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 160707915   701 GLTPLHLVSQEGHVPVADVLIKHGVTVDATTRMGYTPLHVASHYGNIKLVKFLL 754
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
753-807 1.40e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 52.73  E-value: 1.40e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 160707915   753 LLQH-QADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIA 807
Cdd:pfam13857    1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
146-197 1.53e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 1.53e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 160707915   146 TPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLI 197
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Death_NMPP84 cd08318
Death domain of Nuclear Matrix Protein P84; Death domain (DD) found in the Nuclear Matrix ...
 1447-1524 1.74e-08

Death domain of Nuclear Matrix Protein P84; Death domain (DD) found in the Nuclear Matrix Protein P84 (also known as HPR1 or THOC1). HPR1/p84 resides in the nuclear matrix and is part of the THO complex, also called TREX (transcription/export) complex, which functions in mRNP biogenesis at the interface between transcription and export of mRNA from the nucleus. Mice lacking THOC1 have abnormal testis development and are sterile. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260030  Cd Length: 86  Bit Score: 53.29  E-value: 1.74e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 160707915 1447 RMAVIREHLGLSWAELARELQFSVEDINRIRvENPNSLLDQSTALLTLWVDREGENAKMENLYTALRNIDRSEIVNML 1524
Cdd:cd08318     9 QIDVLANKLGEQWKTLAPYLEMKDKDIRQIE-SDSEDMKMRAKQLLVTWQDREGAQATPEILMTALNAAGLNEIAENL 85
Ank_4 pfam13637
Ankyrin repeats (many copies);
505-556 2.20e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.89  E-value: 2.20e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 160707915   505 TPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALL 556
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
206-259 2.52e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.89  E-value: 2.52e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 160707915   206 RLPALHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLL 259
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 68-187 2.88e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 58.35  E-value: 2.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   68 GVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQD-EVVRELVNYGANVNAQSQ-KGF 145
Cdd:PHA02878  191 GANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDyDILKLLLEHGVDVNAKSYiLGL 270

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 160707915  146 TPLYMAAQENhlEVVKFLLENGANQNVATEDGFTPLAVALQQ 187
Cdd:PHA02878  271 TALHSSIKSE--RKLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 44-174 2.95e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.08  E-value: 2.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   44 DAATSFLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQ 123
Cdd:PHA02875  101 DGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGD 180

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 160707915  124 DEVVRELVNYGANVNAQSQKG-FTPLYMAAQENHLEVVKFLLENGANQNVAT 174
Cdd:PHA02875  181 IAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNIMF 232
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 510-678 4.34e-08

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 58.17  E-value: 4.34e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   510 AARIGHTGMVKLLLENGAS--PNLATTAGHTPLHTAAREGHVDTALALLEKEASQACMtkkGFTPLHVAAKyGKVRLAEL 587
Cdd:TIGR00870   24 AAERGDLASVYRDLEEPKKlnINCPDRLGRSALFVAAIENENLELTELLLNLSCRGAV---GDTLLHAISL-EYVDAVEA 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   588 LLEH--DAHP--------NAAGKN----GLTPLHVAVHHNNLDIVKLLLPRGG-------------SPHSP-AWNGYTPL 639
Cdd:TIGR00870  100 ILLHllAAFRksgplelaNDQYTSeftpGITALHLAAHRQNYEIVKLLLERGAsvparacgdffvkSQGVDsFYHGESPL 179

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 160707915   640 HIAAKQNQIEVARSLLQYGGSANAESVQGVTPLHLAAQE 678
Cdd:TIGR00870  180 NAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVME 218
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 118-265 4.53e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 58.34  E-value: 4.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  118 AALAGQDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENV----- 192
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIfrily 611

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 160707915  193 -VAHLINYGTKGKVrlpaLHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASV 265
Cdd:PLN03192  612 hFASISDPHAAGDL----LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
Ank_5 pfam13857
Ankyrin repeats (many copies);
130-184 6.16e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.81  E-value: 6.16e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 160707915   130 LVNYG-ANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVA 184
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
720-774 7.87e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.42  E-value: 7.87e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 160707915   720 LIKHG-VTVDATTRMGYTPLHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQA 774
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02798 PHA02798
ankyrin-like protein; Provisional
 125-367 8.27e-08

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 57.15  E-value: 8.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  125 EVVRELVNYGANVNAQSQKGFTPLYMAAQE---NHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHenvvahlinygt 201
Cdd:PHA02798   90 DIVKILIENGADINKKNSDGETPLYCLLSNgyiNNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNH------------ 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  202 kgkvrlpalHIaarndDTRTAAVLLQNDPNPDVLS-KTGFTPLHIAAHYE----NLNVAQLLLNRGASVN----FTPQNG 272
Cdd:PHA02798  158 ---------HI-----DIEIIKLLLEKGVDINTHNnKEKYDTLHCYFKYNidriDADILKLFVDNGFIINkenkSHKKKF 223

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  273 I---TPLHIASRRGNVIMVRLLLdrgAQIETRTKDEL--TPLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQ 347
Cdd:PHA02798  224 MeylNSLLYDNKRFKKNILDFIF---SYIDINQVDELgfNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFE 300

                         250       260
                  ....*....|....*....|
gi 160707915  348 GDHLDCVRLLLQYNAEIDDI 367
Cdd:PHA02798  301 NESKFIFNSILNKKPNKNTI 320
Ank_5 pfam13857
Ankyrin repeats (many copies);
257-312 8.68e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.42  E-value: 8.68e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 160707915   257 LLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLDRGAQIETRTKDELTPLHCA 312
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 422-490 8.85e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.22  E-value: 8.85e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 160707915  422 LLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLL 490
Cdd:PTZ00322  100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 618-689 1.11e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.83  E-value: 1.11e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 160707915  618 VKLLLPRGGSPHSPAWNGYTPLHIAAKQNQIEVARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVALLLS 689
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
Ank_5 pfam13857
Ankyrin repeats (many copies);
567-609 1.15e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.04  E-value: 1.15e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 160707915   567 KKGFTPLHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVA 609
Cdd:pfam13857   14 GEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 343-425 1.18e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.83  E-value: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  343 HMAAQGDHLDcVRLLLQYNAEIDDITLDHLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMEL 422
Cdd:PTZ00322   88 QLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                  ...
gi 160707915  423 LLK 425
Cdd:PTZ00322  167 LSR 169
Ank_4 pfam13637
Ankyrin repeats (many copies);
536-589 1.21e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.97  E-value: 1.21e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 160707915   536 GHTPLHTAAREGHVDTALALLEKEASQACMTKKGFTPLHVAAKYGKVRLAELLL 589
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 675-851 1.28e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 56.80  E-value: 1.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  675 AAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADVLIKHGVTVDATTRMGYTPLHVASHYGNIKLVKFLL 754
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY 611

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  755 QHQADVNAKTklGYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIAKRLGYISVTDVLkvVTDETSVVLVSDK 834
Cdd:PLN03192  612 HFASISDPHA--AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLL--IMNGADVDKANTD 687

                         170
                  ....*....|....*..
gi 160707915  835 HRMSyPETVDEILDVSE 851
Cdd:PLN03192  688 DDFS-PTELRELLQKRE 703
Ank_4 pfam13637
Ankyrin repeats (many copies);
602-655 1.79e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.58  E-value: 1.79e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 160707915   602 GLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQIEVARSLL 655
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 538-635 2.07e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.06  E-value: 2.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  538 TPLHTAAREGHVDTALA---------------------LLEKEASQACMTKKGFTPLHVAAKYGKVRLAELLLEHDAHPN 596
Cdd:PTZ00322   63 TPDHNLTTEEVIDPVVAhmltvelcqlaasgdavgariLLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPT 142

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 160707915  597 AAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNG 635
Cdd:PTZ00322  143 LLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGANA 181
Ank_5 pfam13857
Ankyrin repeats (many copies);
588-642 2.29e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 49.27  E-value: 2.29e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 160707915   588 LLEHD-AHPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIA 642
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 516-817 2.35e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 55.52  E-value: 2.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  516 TGMVKLLLENGASPNlattaghtplhtaaREGHVDTAL-ALLEKEASQACMTKKgftplhvaakygkvrLAELLLEHDAH 594
Cdd:PHA02989   50 IKIVKLLIDNGADVN--------------YKGYIETPLcAVLRNREITSNKIKK---------------IVKLLLKFGAD 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  595 PNAAGKNGLTPLHVAVHH---NNLDIVKLLLPRGGSPHS-PAWNGYTPLHIAAKQNQI--EVARSLLQYGgsanaesvqg 668
Cdd:PHA02989  101 INLKTFNGVSPIVCFIYNsniNNCDMLRFLLSKGINVNDvKNSRGYNLLHMYLESFSVkkDVIKILLSFG---------- 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  669 VTPLHLAAQEGHTEMvalllskqaNGNLGNKsgltpLHLVSqeghVPVADVLIKHGVTVDATTRMGYTPL------HVAS 742
Cdd:PHA02989  171 VNLFEKTSLYGLTPM---------NIYLRND-----IDVIS----IKVIKYLIKKGVNIETNNNGSESVLesfldnNKIL 232

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 160707915  743 HYGNIKLVKFLLQHqADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIAKRLGYISVTD 817
Cdd:PHA02989  233 SKKEFKVLNFILKY-IKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLN 306
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 157-341 2.47e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 56.03  E-value: 2.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  157 LEVVKFLLENGAnQNVATEDGFTPLAVAlQQGHENVVAHLINYG-------TKGKVrlpALHIAARNDDTRTAAVLLQND 229
Cdd:PLN03192  507 LNVGDLLGDNGG-EHDDPNMASNLLTVA-STGNAALLEELLKAKldpdigdSKGRT---PLHIAASKGYEDCVLVLLKHA 581

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  230 PNPDVLSKTGFTPLH---IAAHYENLNVaqllLNRGASVNfTPQNGITPLHIASRRGNVIMVRLLLDRGAQIETRTKDEL 306
Cdd:PLN03192  582 CNVHIRDANGNTALWnaiSAKHHKIFRI----LYHFASIS-DPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGA 656

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 160707915  307 TPLHCAARNGHVRISEILLDHGAPI-QAKTKNGLSP 341
Cdd:PLN03192  657 TALQVAMAEDHVDMVRLLIMNGADVdKANTDDDFSP 692
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 325-596 3.88e-07

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 55.09  E-value: 3.88e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   325 LDHGAPIQAKTKN--GLSPIHMAA-QGDHLDCVRLLLQYNAEIDdiTLDHLtpLHVAAHCGHHRVAKVLLDKGAKP---- 397
Cdd:TIGR00870   37 LEEPKKLNINCPDrlGRSALFVAAiENENLELTELLLNLSCRGA--VGDTL--LHAISLEYVDAVEAILLHLLAAFrksg 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   398 -----NSRALNGFTPlhiackknhirvmelllktgasidavtesGLTPLHVASFMGHLPIVKNLLQRGASPNVS---NVK 469
Cdd:TIGR00870  113 plelaNDQYTSEFTP-----------------------------GITALHLAAHRQNYEIVKLLLERGASVPARacgDFF 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   470 VETPLHMAARAGhtevakyllqnkakanakakddQTPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHV 549
Cdd:TIGR00870  164 VKSQGVDSFYHG----------------------ESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVMENEF 221

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   550 ------------DTALALLEKEAS----QACMTKKGFTPLHVAAKYGKVRLAELLL-------EHDAHPN 596
Cdd:TIGR00870  222 kaeyeelscqmyNFALSLLDKLRDskelEVILNHQGLTPLKLAAKEGRIVLFRLKLaikykqkKFVAWPN 291
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 673-756 4.73e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.90  E-value: 4.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  673 HLAAQeGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADVLIKHGVTVDATTRMGYTPLHVASHYGNIKLVKF 752
Cdd:PTZ00322   88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                  ....
gi 160707915  753 LLQH 756
Cdd:PTZ00322  167 LSRH 170
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 736-835 5.14e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 52.51  E-value: 5.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  736 TPLH--VASHYGNIKLVKFLLQHQADVNAKTK-LGYSPLH---QAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIakR 809
Cdd:PHA02859   53 TPIFscLEKDKVNVEILKFLIENGADVNFKTRdNNLSALHhylSFNKNVEPEILKILIDSGSSITEEDEDGKNLLHM--Y 130

                          90       100
                  ....*....|....*....|....*..
gi 160707915  810 LGYISV-TDVLKVVTDETSVVLVSDKH 835
Cdd:PHA02859  131 MCNFNVrINVIKLLIDSGVSFLNKDFD 157
Ank_5 pfam13857
Ankyrin repeats (many copies);
225-279 5.32e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.11  E-value: 5.32e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 160707915   225 LLQNDP-NPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIA 279
Cdd:pfam13857    1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 100-269 7.01e-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: 54.12  E-value: 7.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  100 KEIILETTTK---KGNTALHIAALAGQDEVVRELVNYGANVNAQSQKGF-------------TPLYMAAQENHLEVVKFL 163
Cdd:cd21882    59 KELVNAPCTDefyQGQTALHIAIENRNLNLVRLLVENGADVSARATGRFfrkspgnlfyfgeLPLSLAACTNQEEIVRLL 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  164 LENGANqnvatedgftPLAVALQQGHENVVAHLINYGTKGKVRLPALHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPL 243
Cdd:cd21882   139 LENGAQ----------PAALEAQDSLGNTVLHALVLQADNTPENSAFVCQMYNLLLSYGAHLDPTQQLEEIPNHQGLTPL 208

                         170       180
                  ....*....|....*....|....*.
gi 160707915  244 HIAAHYENLNVAQLLLNRGASVNFTP 269
Cdd:cd21882   209 KLAAVEGKIVMFQHILQREFSGPYQP 234
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 336-431 7.21e-07

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 50.65  E-value: 7.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  336 KNGLSPIHMAAQGDHLDC---VRLLLQYNAEIDDI-TLDHLTPLHVAAHCGHHRVAKVLLDKgAKPNSRALNGF--TPLH 409
Cdd:PHA02736   53 RHGKQCVHIVSNPDKADPqekLKLLMEWGADINGKeRVFGNTPLHIAVYTQNYELATWLCNQ-PGVNMEILNYAfkTPYY 131

                          90       100
                  ....*....|....*....|..
gi 160707915  410 IACKKNHIRVMELLLKTGASID 431
Cdd:PHA02736  132 VACERHDAKMMNILRAKGAQCK 153
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 734-765 7.97e-07

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: 46.90  E-value: 7.97e-07
                           10        20        30
                   ....*....|....*....|....*....|...
gi 160707915   734 GYTPLHVAS-HYGNIKLVKFLLQHQADVNAKTK 765
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 403-432 8.70e-07

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: 46.81  E-value: 8.70e-07
                            10        20        30
                    ....*....|....*....|....*....|
gi 160707915    403 NGFTPLHIACKKNHIRVMELLLKTGASIDA 432
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02798 PHA02798
ankyrin-like protein; Provisional
 581-807 9.19e-07

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 53.69  E-value: 9.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  581 KVRLAELLLEHDAHPNAAGKNGLTPL-----HVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQ---NQIEVAR 652
Cdd:PHA02798   50 STDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNgyiNNLEILL 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  653 SLLQYGGSANAESVQGVTPLHLAAQEGHT---EMVALLLSKQANGNL-GNKSGLTPLHLVSQEG----HVPVADVLIKHG 724
Cdd:PHA02798  130 FMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDINThNNKEKYDTLHCYFKYNidriDADILKLFVDNG 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  725 VTV---DATTRMGYTPLHVASHYGNIK----LVKFLLQHqADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNEVS 797
Cdd:PHA02798  210 FIInkeNKSHKKKFMEYLNSLLYDNKRfkknILDFIFSY-IDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIIT 288

                         250
                  ....*....|
gi 160707915  798 SNGTTPLAIA 807
Cdd:PHA02798  289 ELGNTCLFTA 298
Ank_4 pfam13637
Ankyrin repeats (many copies);
767-819 1.01e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.27  E-value: 1.01e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 160707915   767 GYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIAKRLGYISVTDVL 819
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank_5 pfam13857
Ankyrin repeats (many copies);
654-708 1.31e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.96  E-value: 1.31e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 160707915   654 LLQYGG-SANAESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLV 708
Cdd:pfam13857    1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 632-754 1.42e-06

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: 53.22  E-value: 1.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  632 AWNGYTPLHIAAKQNQIEVARSLLQYGGSANAESvQGV---------------TPLHLAAQEGHTEMVALLLSK-QANGN 695
Cdd:cd22194   138 AYEGQTALNIAIERRQGDIVKLLIAKGADVNAHA-KGVffnpkykhegfyfgeTPLALAACTNQPEIVQLLMEKeSTDIT 216

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160707915  696 LGNKSGLTPLHLVsqeghVPVAD---------------VLIKHGVTVDATTR--MGYTPLHVASHYGNIKLVKFLL 754
Cdd:cd22194   217 SQDSRGNTVLHAL-----VTVAEdsktqndfvkrmydmILLKSENKNLETIRnnEGLTPLQLAAKMGKAEILKYIL 287
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 734-762 1.46e-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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 46.10  E-value: 1.46e-06
                           10        20
                   ....*....|....*....|....*....
gi 160707915   734 GYTPLHVASHYGNIKLVKFLLQHQADVNA 762
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02946 PHA02946
ankyin-like protein; Provisional
 258-441 1.47e-06

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 52.75  E-value: 1.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  258 LLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLDRGAQIETRTKDELTPLHCAARNGHVRISEI--LLDHGAPIQAKT 335
Cdd:PHA02946   58 LLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIERInlLVQYGAKINNSV 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  336 -KNGLSPIHMAAQGDHLDCVRLL-LQYNAEIDDITLDHLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACK 413
Cdd:PHA02946  138 dEEGCGPLLACTDPSERVFKKIMsIGFEARIVDKFGKNHIHRHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCS 217

                         170       180       190
                  ....*....|....*....|....*....|
gi 160707915  414 KN--HIRVMELLLKTgASIDAVTESGLTPL 441
Cdd:PHA02946  218 KTvkNVDIINLLLPS-TDVNKQNKFGDSPL 246
Death_RAIDD cd08319
Death domain of RIP-associated ICH-1 homologous protein with a death domain; Death domain (DD) ...
 1441-1516 1.53e-06

Death domain of RIP-associated ICH-1 homologous protein with a death domain; Death domain (DD) of RAIDD (RIP-associated ICH-1 homologous protein with a death domain), also known as CRADD (Caspase and RIP adaptor). RAIDD is an adaptor protein that together with the p53-inducible protein PIDD and caspase-2, forms the PIDDosome complex, which is required for caspase-2 activation and plays a role in mediating stress-induced apoptosis. RAIDD contains an N-terminal Caspase Activation and Recruitment Domain (CARD), which interacts with the caspase-2 CARD, and a C-terminal DD, which interacts with the DD of PIDD. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD, DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260031  Cd Length: 83  Bit Score: 47.71  E-value: 1.53e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160707915 1441 TDRVEMRMAvirEHLGLSWAELARELQFSVEDINRIRVENPNSLLDQSTALLTLWVDREGENAKMENLYTALRNID 1516
Cdd:cd08319     1 TDRQLNKLA---QRLGPEWEQVLLDLGLSKADIYRCKADHPYNVQSQIVEALVKWKQRQGKKATVQSLIQSLKAVE 73
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 58-261 1.55e-06

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: 53.27  E-value: 1.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   58 LDKALDHLRNGVdintcNQNGLNGLHLASKEGHVKMVVELLHKEiiletTTKKGNTALHIAALAGQDEVVRELVNYGANV 137
Cdd:cd22196    51 LLKAMLNLHNGQ-----NDTISLLLDIAEKTGNLKEFVNAAYTD-----SYYKGQTALHIAIERRNMHLVELLVQNGADV 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  138 NA----------QSQKGF----TPLYMAAQENHLEVVKFLLENGANQ-NVATEDGFTplavalqqgheNVVAHlinygtk 202
Cdd:cd22196   121 HArasgeffkkkKGGPGFyfgeLPLSLAACTNQLDIVKFLLENPHSPaDISARDSMG-----------NTVLH------- 182

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 160707915  203 gkvrlpALHIAARNDDTRTAAV--------LLQNDPNP-----DVLSKTGFTPLHIAAHYENLNVAQLLLNR 261
Cdd:cd22196   183 ------ALVEVADNTPENTKFVtkmyneilILGAKIRPllkleEITNKKGLTPLKLAAKTGKIGIFAYILGR 248
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 116-199 1.57e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.36  E-value: 1.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  116 HIAAlAGQDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAH 195
Cdd:PTZ00322   88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                  ....
gi 160707915  196 LINY 199
Cdd:PTZ00322  167 LSRH 170
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 733-762 1.58e-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: 46.04  E-value: 1.58e-06
                            10        20        30
                    ....*....|....*....|....*....|
gi 160707915    733 MGYTPLHVASHYGNIKLVKFLLQHQADVNA 762
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 475-556 2.01e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.98  E-value: 2.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  475 HMAArAGHTEVAKYLLQNKAKANAKAKDDQTPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALA 554
Cdd:PTZ00322   88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                  ..
gi 160707915  555 LL 556
Cdd:PTZ00322  167 LS 168
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 111-294 2.26e-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: 52.57  E-value: 2.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  111 GNTALHIAALAGQD----------EVVRELVNYGANVNAQSQ----KGFTPLYMAAQENHLEVVKFLLENGAN-QNVATE 175
Cdd:cd21882    26 GKTCLHKAALNLNDgvneaimlllEAAPDSGNPKELVNAPCTdefyQGQTALHIAIENRNLNLVRLLVENGADvSARATG 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  176 DGFT------------PLAVALQQGHENVVAHLINYGTKgkvrlPAlHIAARND--DTRTAAVLLQNDPNPDvlsKTGFt 241
Cdd:cd21882   106 RFFRkspgnlfyfgelPLSLAACTNQEEIVRLLLENGAQ-----PA-ALEAQDSlgNTVLHALVLQADNTPE---NSAF- 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  242 plhiAAHYENlnvaqLLLNRGASVNFTPQ-------NGITPLHIASRRGNVIMVRLLLDR 294
Cdd:cd21882   176 ----VCQMYN-----LLLSYGAHLDPTQQleeipnhQGLTPLKLAAVEGKIVMFQHILQR 226
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 143-172 2.46e-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: 45.66  E-value: 2.46e-06
                            10        20        30
                    ....*....|....*....|....*....|
gi 160707915    143 KGFTPLYMAAQENHLEVVKFLLENGANQNV 172
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 125-294 2.61e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 52.05  E-value: 2.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  125 EVVRELVNYGANVNA-QSQKGFTPLYMAAQENHL--EVVKFLLENGANQNVATE-DGFTPLAVALQQGHENVVAHLINYG 200
Cdd:PHA02989  125 DMLRFLLSKGINVNDvKNSRGYNLLHMYLESFSVkkDVIKILLSFGVNLFEKTSlYGLTPMNIYLRNDIDVISIKVIKYL 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  201 TKGKVRLP---ALHIAARNDDTRTAAVLLQND----------PNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNF 267
Cdd:PHA02989  205 IKKGVNIEtnnNGSESVLESFLDNNKILSKKEfkvlnfilkyIKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYN 284

                         170       180
                  ....*....|....*....|....*..
gi 160707915  268 TPQNGITPLHIASRRGNVIMVRLLLDR 294
Cdd:PHA02989  285 VSKDGDTVLTYAIKHGNIDMLNRILQL 311
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 417-598 4.15e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 51.79  E-value: 4.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  417 IRVMELLLK-TGASIDAVTESGLtpLHVASfMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKAK 495
Cdd:PLN03192  507 LNVGDLLGDnGGEHDDPNMASNL--LTVAS-TGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACN 583

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  496 ANAKAKDDQTPLHCAARIGHTGMVKLLLENGASPNlaTTAGHTPLHTAAREGHVDTALALLEKEASQACMTKKGFTPLHV 575
Cdd:PLN03192  584 VHIRDANGNTALWNAISAKHHKIFRILYHFASISD--PHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQV 661

                         170       180
                  ....*....|....*....|...
gi 160707915  576 AAKYGKVRLAELLLEHDAHPNAA 598
Cdd:PLN03192  662 AMAEDHVDMVRLLIMNGADVDKA 684
Ank_5 pfam13857
Ankyrin repeats (many copies);
422-477 4.65e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.42  E-value: 4.65e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 160707915   422 LLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMA 477
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 502-533 4.79e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 44.97  E-value: 4.79e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 160707915   502 DDQTPLHCAA-RIGHTGMVKLLLENGASPNLAT 533
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 241-338 4.80e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 49.43  E-value: 4.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  241 TPLH--IAAHYENLNVAQLLLNRGASVNF-TPQNGITPLH---IASRRGNVIMVRLLLDRGAQIETRTKDELTPLHCAAR 314
Cdd:PHA02859   53 TPIFscLEKDKVNVEILKFLIENGADVNFkTRDNNLSALHhylSFNKNVEPEILKILIDSGSSITEEDEDGKNLLHMYMC 132

                          90       100
                  ....*....|....*....|....*.
gi 160707915  315 NGHVRIS--EILLDHGAPIQAKTKNG 338
Cdd:PHA02859  133 NFNVRINviKLLIDSGVSFLNKDFDN 158
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 234-573 5.15e-06

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 51.45  E-value: 5.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  234 VLSKTGFTPLH--IAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVI--MVRLLLDRGAQIETRTKDELTPL 309
Cdd:PHA02716  172 VCKKTGYGILHayLGNMYVDIDILEWLCNNGVNVNLQNNHLITPLHTYLITGNVCasVIKKIIELGGDMDMKCVNGMSPI 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  310 HCAARNGHVRISEILLDHGAPIQA-KTKNGLSPIHM---AAQGDHLDCVRLLLQYNAEIDDITLDHLTPLH--VAAHCGH 383
Cdd:PHA02716  252 MTYIINIDNINPEITNIYIESLDGnKVKNIPMILHSyitLARNIDISVVYSFLQPGVKLHYKDSAGRTCLHqyILRHNIS 331

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  384 HRVAKVLLDKGAKPNSRALNGFTPLHIACKK------------NHIR--VMELLLKTGASIDAVTESGLTPL-----HVA 444
Cdd:PHA02716  332 TDIIKLLHEYGNDLNEPDNIGNTVLHTYLSMlsvvnildpetdNDIRldVIQCLISLGADITAVNCLGYTPLtsyicTAQ 411

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  445 SFMGHLPI-------VKNLLQRGASPNVSNVKVETPlhmaaRAGHTEVAKYLLQNKAKANAKAKDDQTPLHCAArigHTG 517
Cdd:PHA02716  412 NYMYYDIIdclisdkVLNMVKHRILQDLLIRVDDTP-----CIIHHIIAKYNIPTDLYTDEYEPYDSTKIHDVY---HCA 483

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 160707915  518 MVKLLlengaSPNLATTAGHTPLHTAAREGH-----VDTALALLEKEASQACMTKKGFTPL 573
Cdd:PHA02716  484 IIERY-----NNAVCETSGMTPLHVSIISHTnanivMDSFVYLLSIQYNINIPTKNGVTPL 539
Ank_5 pfam13857
Ankyrin repeats (many copies);
635-675 5.23e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.42  E-value: 5.23e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 160707915   635 GYTPLHIAAKQNQIEVARSLLQYGGSANAESVQGVTPLHLA 675
Cdd:pfam13857   16 GYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02798 PHA02798
ankyrin-like protein; Provisional
 149-444 5.82e-06

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 50.99  E-value: 5.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  149 YMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALqqghenvvAHLINYGTKGKVRLpalhiaarnddtrtaaVLLQN 228
Cdd:PHA02798   43 YLQRDSPSTDIVKLFINLGANVNGLDNEYSTPLCTIL--------SNIKDYKHMLDIVK----------------ILIEN 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  229 DPNPDVLSKTGFTPLHIAAHYENLNVAQLLL---NRGASVNFTPQNGITPLHIASRRGNVI---MVRLLLDRGAQIETRT 302
Cdd:PHA02798   99 GADINKKNSDGETPLYCLLSNGYINNLEILLfmiENGADTTLLDKDGFTMLQVYLQSNHHIdieIIKLLLEKGVDINTHN 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  303 KDE-LTPLHCAARNGHVRIS----EILLDHGAPIQAKTKNGLSPIhmaaqgdhLDCVRLLLQYNAEIDDITLDhltplhv 377
Cdd:PHA02798  179 NKEkYDTLHCYFKYNIDRIDadilKLFVDNGFIINKENKSHKKKF--------MEYLNSLLYDNKRFKKNILD------- 243

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 160707915  378 aahcghhrvakvLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVA 444
Cdd:PHA02798  244 ------------FIFSYIDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTA 298
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 403-435 7.03e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 44.20  E-value: 7.03e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 160707915   403 NGFTPLHIACKK-NHIRVMELLLKTGASIDAVTE 435
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 568-691 7.49e-06

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: 50.91  E-value: 7.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  568 KGFTPLHVAAKYGKVRLAELLLEHDAHPNAAGKN--------------GLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAW 633
Cdd:cd22194   140 EGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEIVQLLMEKESTDITSQD 219

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 160707915  634 N-GYTPLH---IAAKQNQ------IEVARSLLQYGGSANAESV---QGVTPLHLAAQEGHTEMVALLLSKQ 691
Cdd:cd22194   220 SrGNTVLHalvTVAEDSKtqndfvKRMYDMILLKSENKNLETIrnnEGLTPLQLAAKMGKAEILKYILSRE 290
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 110-140 8.38e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 44.20  E-value: 8.38e-06
                           10        20        30
                   ....*....|....*....|....*....|..
gi 160707915   110 KGNTALHIAAL-AGQDEVVRELVNYGANVNAQ 140
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNAR 32
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 110-139 9.04e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 44.12  E-value: 9.04e-06
                            10        20        30
                    ....*....|....*....|....*....|
gi 160707915    110 KGNTALHIAALAGQDEVVRELVNYGANVNA 139
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 664-812 9.05e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 50.83  E-value: 9.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  664 ESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADVLIKHGVTVDATTRMGYTPLHVASH 743
Cdd:PHA02876  141 ESIEYMKLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVD 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  744 YGNIKLVKFLLQHQADVNA--------------KTKL-----GYS----------PLHQAAQQGH-TDIVTLLLKNGASP 793
Cdd:PHA02876  221 SKNIDTIKAIIDNRSNINKndlsllkairnedlETSLllydaGFSvnsiddckntPLHHASQAPSlSRLVPKLLERGADV 300

                         170
                  ....*....|....*....
gi 160707915  794 NEVSSNGTTPLAIAKRLGY 812
Cdd:PHA02876  301 NAKNIKGETPLYLMAKNGY 319
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 110-261 1.02e-05

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: 50.56  E-value: 1.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  110 KGNTALHIAALAGQDEVVRELVNYGANVNAQSQKGF--------------TPLYMAAQENHLEVVKFLLENganqnvate 175
Cdd:cd22193    75 EGQTALHIAIERRQGDIVALLVENGADVHAHAKGRFfqpkyqgegfyfgeLPLSLAACTNQPDIVQYLLEN--------- 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  176 dGFTPLAVALQQGHENVVAHlinygtkgkvrlpALHIAARNDDTRTAAV------LLQNDPN--PDV-----LSKTGFTP 242
Cdd:cd22193   146 -EHQPADIEAQDSRGNTVLH-------------ALVTVADNTKENTKFVtrmydmILIRGAKlcPTVeleeiRNNDGLTP 211

                         170
                  ....*....|....*....
gi 160707915  243 LHIAAHYENLNVAQLLLNR 261
Cdd:cd22193   212 LQLAAKMGKIEILKYILQR 230
Ank_5 pfam13857
Ankyrin repeats (many copies);
291-345 1.13e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.26  E-value: 1.13e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 160707915   291 LLDRG-AQIETRTKDELTPLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMA 345
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 546-691 1.39e-05

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 50.19  E-value: 1.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  546 EGHVDTALALLE--------KEASQACMTK---KGFTPLHVAAKYGKVRLAELLLEHDAHPNAA----------GKNGL- 603
Cdd:cd22196    60 NGQNDTISLLLDiaektgnlKEFVNAAYTDsyyKGQTALHIAIERRNMHLVELLVQNGADVHARasgeffkkkkGGPGFy 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  604 ---TPLHVAVHHNNLDIVKLLLPrggSPHSPA------WNGYTPLH--IAAKQNQIEVAR-------SLLQYGG----SA 661
Cdd:cd22196   140 fgeLPLSLAACTNQLDIVKFLLE---NPHSPAdisardSMGNTVLHalVEVADNTPENTKfvtkmynEILILGAkirpLL 216

                         170       180       190
                  ....*....|....*....|....*....|...
gi 160707915  662 NAESV---QGVTPLHLAAQEGHTEMVALLLSKQ 691
Cdd:cd22196   217 KLEEItnkKGLTPLKLAAKTGKIGIFAYILGRE 249
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 640-723 1.45e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.90  E-value: 1.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  640 HIAAKQNQIEvARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADV 719
Cdd:PTZ00322   88 QLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                  ....
gi 160707915  720 LIKH 723
Cdd:PTZ00322  167 LSRH 170
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 601-629 1.46e-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: 43.35  E-value: 1.46e-05
                            10        20
                    ....*....|....*....|....*....
gi 160707915    601 NGLTPLHVAVHHNNLDIVKLLLPRGGSPH 629
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 201-462 1.62e-05

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 49.88  E-value: 1.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  201 TKGKVRLPALHIAARNDDTR---TAAVLLQNDPNPDVLSKTGFTPLhIAAHYEnlnvaqlllnrgasvnftpqnGITPLH 277
Cdd:cd21882    21 QRGATGKTCLHKAALNLNDGvneAIMLLLEAAPDSGNPKELVNAPC-TDEFYQ---------------------GQTALH 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  278 IASRRGNVIMVRLLLDRGAQIETRTKdeltplhcaarnghvriseilldhGAPIQAKTKNGL----SPIHMAAQGDHLDC 353
Cdd:cd21882    79 IAIENRNLNLVRLLVENGADVSARAT------------------------GRFFRKSPGNLFyfgeLPLSLAACTNQEEI 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  354 VRLLLQYNAEIDDITL-DHL--TPLHvaahcghhrvAKVLLDKGAKPNSRalngftplhIACKknhirVMELLLKTGA-- 428
Cdd:cd21882   135 VRLLLENGAQPAALEAqDSLgnTVLH----------ALVLQADNTPENSA---------FVCQ-----MYNLLLSYGAhl 190

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 160707915  429 ----SIDAVT-ESGLTPLHVASFMGHLPIVKNLLQRGAS 462
Cdd:cd21882   191 dptqQLEEIPnHQGLTPLKLAAVEGKIVMFQHILQREFS 229
Ank_4 pfam13637
Ankyrin repeats (many copies);
82-131 1.66e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.80  E-value: 1.66e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 160707915    82 LHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQDEVVRELV 131
Cdd:pfam13637    5 LHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 437-467 1.68e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 43.43  E-value: 1.68e-05
                           10        20        30
                   ....*....|....*....|....*....|..
gi 160707915   437 GLTPLHVASFM-GHLPIVKNLLQRGASPNVSN 467
Cdd:pfam00023    2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 65-139 1.73e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 49.28  E-value: 1.73e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 160707915   65 LRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQDEVVRELVNYGANVNA 139
Cdd:PHA03100  179 LSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 750-819 1.84e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.90  E-value: 1.84e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  750 VKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIAKRLGYISVTDVL 819
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
Ank_5 pfam13857
Ankyrin repeats (many copies);
97-151 2.09e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.49  E-value: 2.09e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 160707915    97 LLHKEIILETTTKKGNTALHIAALAGQDEVVRELVNYGANVNAQSQKGFTPLYMA 151
Cdd:pfam13857    2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 502-531 2.23e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.96  E-value: 2.23e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 160707915    502 DDQTPLHCAARIGHTGMVKLLLENGASPNL 531
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 614-837 2.49e-05

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 49.53  E-value: 2.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  614 NLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQI--EVARSLLQYGGSANAESVQGVTPL--HLAAQEGHTEMVALLLS 689
Cdd:PHA02716  191 DIDILEWLCNNGVNVNLQNNHLITPLHTYLITGNVcaSVIKKIIELGGDMDMKCVNGMSPImtYIINIDNINPEITNIYI 270

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  690 KQANGNlgnKSGLTP--LHL---VSQEGHVPVADVLIKHGVTVDATTRMGYTPLH--VASHYGNIKLVKFLLQHQADVNA 762
Cdd:PHA02716  271 ESLDGN---KVKNIPmiLHSyitLARNIDISVVYSFLQPGVKLHYKDSAGRTCLHqyILRHNISTDIIKLLHEYGNDLNE 347

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  763 KTKLGYSPLH--------------QAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLA----IAKRLGYISVTDVLkvVTD 824
Cdd:PHA02716  348 PDNIGNTVLHtylsmlsvvnildpETDNDIRLDVIQCLISLGADITAVNCLGYTPLTsyicTAQNYMYYDIIDCL--ISD 425

                         250
                  ....*....|...
gi 160707915  825 EtsvVLVSDKHRM 837
Cdd:PHA02716  426 K---VLNMVKHRI 435
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 734-804 2.72e-05

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 49.03  E-value: 2.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  734 GYTPLHVASHYGNIKLVKFLLQHQADVNA--------KTK------LGYSPLHQAAQQGHTDIVTLLLKNGASPNEVS-- 797
Cdd:cd22196    94 GQTALHIAIERRNMHLVELLVQNGADVHArasgeffkKKKggpgfyFGELPLSLAACTNQLDIVKFLLENPHSPADISar 173


                  ....*...
gi 160707915  798 -SNGTTPL 804
Cdd:cd22196   174 dSMGNTVL 181
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 239-266 2.82e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.57  E-value: 2.82e-05
                            10        20
                    ....*....|....*....|....*...
gi 160707915    239 GFTPLHIAAHYENLNVAQLLLNRGASVN 266
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank_5 pfam13857
Ankyrin repeats (many copies);
324-378 2.83e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.49  E-value: 2.83e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 160707915   324 LLDHG-APIQAKTKNGLSPIHMAAQGDHLDCVRLLLQYNAEIDDITLDHLTPLHVA 378
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 602-720 3.20e-05

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 49.03  E-value: 3.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  602 GLTPLHVAVHHNNLDIVKLLLPRGGSPHSPA--------------WNGYTPLHIAAKQNQIEVARSLLQYGGSA---NAE 664
Cdd:cd22196    94 GQTALHIAIERRNMHLVELLVQNGADVHARAsgeffkkkkggpgfYFGELPLSLAACTNQLDIVKFLLENPHSPadiSAR 173

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 160707915  665 SVQGVTPLH-LAAQEGHTEMVALLLSKQANG---------------NLGNKSGLTPLHLVSQEGHVPV-ADVL 720
Cdd:cd22196   174 DSMGNTVLHaLVEVADNTPENTKFVTKMYNEililgakirpllkleEITNKKGLTPLKLAAKTGKIGIfAYIL 246
Ank_5 pfam13857
Ankyrin repeats (many copies);
504-543 3.35e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.10  E-value: 3.35e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 160707915   504 QTPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTA 543
Cdd:pfam13857   17 YTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 110-139 3.37e-05

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 42.24  E-value: 3.37e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 160707915   110 KGNTALHIAALAGQDEVVRELVNYGANVNA 139
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 271-303 3.38e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 42.28  E-value: 3.38e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 160707915   271 NGITPLHIAS-RRGNVIMVRLLLDRGAQIETRTK 303
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 717-800 3.72e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.74  E-value: 3.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  717 ADVLIKHGVTVDATTRMGYTPLHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNEV 796
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFEL 177


                  ....
gi 160707915  797 SSNG 800
Cdd:PTZ00322  178 GANA 181
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 271-299 3.78e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.19  E-value: 3.78e-05
                            10        20
                    ....*....|....*....|....*....
gi 160707915    271 NGITPLHIASRRGNVIMVRLLLDRGAQIE 299
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 403-432 3.79e-05

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 42.24  E-value: 3.79e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 160707915   403 NGFTPLHIACKKNHIRVMELLLKTGASIDA 432
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Death_p75NR cd08311
Death domain of p75 Neurotrophin Receptor; Death Domain (DD) found in p75 neurotrophin ...
 1458-1525 4.29e-05

Death domain of p75 Neurotrophin Receptor; Death Domain (DD) found in p75 neurotrophin receptor (p75NTR, NGFR, TNFRSF16). p75NTR binds members of the neurotrophin (NT) family including nerve growth factor (NGF), brain-derived neurotrophic factor (BDNF), and NT3, among others. It contains an NT-binding extracellular region that bears four cysteine-rich repeats, a transmembrane domain, and an intracellular DD. p75NTR plays roles in the immune, vascular, and nervous systems, and has been shown to promote cell death or survival, and to induce neurite outgrowth or collapse depending on its ligands and co-receptors. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260025  Cd Length: 80  Bit Score: 43.43  E-value: 4.29e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 160707915 1458 SWAELARELQFSVEDINRI-RVENPnslldqSTALLTLWVDREGenAKMENLYTALRNIDRSEIVNMLE 1525
Cdd:cd08311    20 DWRALAGELGYSAEEIDSFaREADP------CRALLTDWSAQDG--ATLGVLLTALRKIGRDDIVEILQ 80
Ank_5 pfam13857
Ankyrin repeats (many copies);
686-741 4.50e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.72  E-value: 4.50e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 160707915   686 LLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADVLIKHGVTVDATTRMGYTPLHVA 741
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 78-261 4.54e-05

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: 48.54  E-value: 4.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915    78 GLNGLHLASKEGHVkmVVE--LLHKEIILETTTK-------------KGNTALHIAALAGQDEVVRELVNYGANVNA--- 139
Cdd:TIGR00870   82 GDTLLHAISLEYVD--AVEaiLLHLLAAFRKSGPlelandqytseftPGITALHLAAHRQNYEIVKLLLERGASVPArac 159

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   140 -------QSQKGF----TPLYMAAQENHLEVVKFLLENGANqnvatedgftPLAvALQQGheNVVAHLINYGTKGKVRLP 208
Cdd:TIGR00870  160 gdffvksQGVDSFyhgeSPLNAAACLGSPSIVALLSEDPAD----------ILT-ADSLG--NTLLHLLVMENEFKAEYE 226

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 160707915   209 ALHIA---------ARNDDTRTAAVLLQNDpnpdvlsktGFTPLHIAAHYENLNVAQLLLNR 261
Cdd:TIGR00870  227 ELSCQmynfalsllDKLRDSKELEVILNHQ---------GLTPLKLAAKEGRIVLFRLKLAI 279
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 143-175 4.76e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 41.89  E-value: 4.76e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 160707915   143 KGFTPLYMAA-QENHLEVVKFLLENGANQNVATE 175
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 337-366 5.34e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.80  E-value: 5.34e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 160707915    337 NGLSPIHMAAQGDHLDCVRLLLQYNAEIDD 366
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 502-530 5.56e-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: 41.86  E-value: 5.56e-05
                           10        20
                   ....*....|....*....|....*....
gi 160707915   502 DDQTPLHCAARIGHTGMVKLLLENGASPN 530
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 354-490 6.22e-05

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 47.83  E-value: 6.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  354 VRLLLQY-----------NAEIDDITLDHLTPLHVAAHCGHHRVAKVLLDKGAKPNSRA----------LNGF----TPL 408
Cdd:cd22194   113 VRILLAFaeengildrfiNAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAkgvffnpkykHEGFyfgeTPL 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  409 HIACKKNHIRVMELLLKTGASIDAVTES-GLTPLH----VA-SFMGHLPIVKNL----LQRGASPN---VSNVKVETPLH 475
Cdd:cd22194   193 ALAACTNQPEIVQLLMEKESTDITSQDSrGNTVLHalvtVAeDSKTQNDFVKRMydmiLLKSENKNletIRNNEGLTPLQ 272

                         170
                  ....*....|....*
gi 160707915  476 MAARAGHTEVAKYLL 490
Cdd:cd22194   273 LAAKMGKAEILKYIL 287
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 218-314 6.41e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 46.90  E-value: 6.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  218 DTRTAAVLLQNDPN-PDVLSKTGFT-PLHIAAHYENLNVAQLLLNRGASVN-FTPQNGITPLHIASRRGNVIMVRLLLDR 294
Cdd:PHA02884   47 DIIDAILKLGADPEaPFPLSENSKTnPLIYAIDCDNDDAAKLLIRYGADVNrYAEEAKITPLYISVLHGCLKCLEILLSY 126

                          90       100
                  ....*....|....*....|
gi 160707915  295 GAQIETRTKDELTPLHCAAR 314
Cdd:PHA02884  127 GADINIQTNDMVTPIELALM 146
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 324-491 6.57e-05

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: 47.87  E-value: 6.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  324 LLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQY-----------NAEIDDITLDHLTPLHVAAHCGHHRVAKVLLD 392
Cdd:cd22193    18 LTDSEFTESSTGKTCLMKALLNLNPGTNDTIRILLDIaektdnlkrfiNAEYTDEYYEGQTALHIAIERRQGDIVALLVE 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  393 KGAKPNSRALNGF--------------TPLHIACKKNHIRVMELLLK---TGASIDAVTESGLTPLH----VA-SFMGHL 450
Cdd:cd22193    98 NGADVHAHAKGRFfqpkyqgegfyfgeLPLSLAACTNQPDIVQYLLEnehQPADIEAQDSRGNTVLHalvtVAdNTKENT 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 160707915  451 PIVKN----LLQRGAS-------PNVSNVKVETPLHMAARAGHTEVAKYLLQ 491
Cdd:cd22193   178 KFVTRmydmILIRGAKlcptvelEEIRNNDGLTPLQLAAKMGKIEILKYILQ 229
Ank_5 pfam13857
Ankyrin repeats (many copies);
356-411 6.66e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 6.66e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 160707915   356 LLLQYNAEIDDITLDHLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIA 411
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 370-400 7.41e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 41.51  E-value: 7.41e-05
                           10        20        30
                   ....*....|....*....|....*....|..
gi 160707915   370 DHLTPLHVAA-HCGHHRVAKVLLDKGAKPNSR 400
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNAR 32
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 239-266 7.78e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 41.51  E-value: 7.78e-05
                           10        20
                   ....*....|....*....|....*....
gi 160707915   239 GFTPLHIAA-HYENLNVAQLLLNRGASVN 266
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVN 30
Death_PIDD cd08779
Death Domain of p53-induced protein with a death domain; Death domain (DD) found in PIDD ...
 1451-1525 8.39e-05

Death Domain of p53-induced protein with a death domain; Death domain (DD) found in PIDD (p53-induced protein with a death domain) and similar proteins. PIDD is a component of the PIDDosome complex, which is an oligomeric caspase-activating complex involved in caspase-2 activation and plays a role in mediating stress-induced apoptosis. The PIDDosome complex is composed of three components, PIDD, RAIDD and caspase-2, which interact through their DDs and DD-like domains. The DD of PIDD interacts with the DD of RAIDD, which also contains a Caspase Activation and Recruitment Domain (CARD) that interacts with the caspase-2 CARD. Autoproteolysis of PIDD determines the downstream signaling event, between pro-survival NF-kB or pro-death caspase-2 activation. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD, DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260049  Cd Length: 86  Bit Score: 43.07  E-value: 8.39e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160707915 1451 IREHLGLSWAELARELQFSVEDINRIRVENPNSLLDQSTALLTLWVDREGENA-KMENLYTALRNIDRSEIVNMLE 1525
Cdd:cd08779     8 LAKELGEDWQKLALHLGVSYSRIQRIKRKNRDDLDEQILDMLFSWAKTLPTSPdKVGLLVTALSKSGRSDLAEELR 83
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 276-491 8.87e-05

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: 47.38  E-value: 8.87e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   276 LHIASRRGNVIMVRLLLDRGAQIETrtkdELTPLHcAARNGHVRISEILLDHGAPIQAKTKNglspihmaaqgdhldcvr 355
Cdd:TIGR00870   57 FVAAIENENLELTELLLNLSCRGAV----GDTLLH-AISLEYVDAVEAILLHLLAAFRKSGP------------------ 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   356 LLLQYNAEIDDITLDHlTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNGF--------------TPLHIACKKNHIRVME 421
Cdd:TIGR00870  114 LELANDQYTSEFTPGI-TALHLAAHRQNYEIVKLLLERGASVPARACGDFfvksqgvdsfyhgeSPLNAAACLGSPSIVA 192

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   422 LLLKTGASIDAVTESGLTPLH----VASF--------MGHLPIVKNLLQRGASPN----VSNVKVETPLHMAARAGHTEV 485
Cdd:TIGR00870  193 LLSEDPADILTADSLGNTLLHllvmENEFkaeyeelsCQMYNFALSLLDKLRDSKelevILNHQGLTPLKLAAKEGRIVL 272


                   ....*.
gi 160707915   486 AKYLLQ 491
Cdd:TIGR00870  273 FRLKLA 278
Death_DRs cd08784
Death Domain of Death Receptors; Death domain (DD) found in death receptor proteins. Death ...
 1457-1516 9.71e-05

Death Domain of Death Receptors; Death domain (DD) found in death receptor proteins. Death receptors are members of the tumor necrosis factor (TNF) receptor superfamily, characterized by having a cytoplasmic DD. Known members of the family are Fas (CD95/APO-1), TNF-receptor 1 (TNFR1/TNFRSF1A/p55/CD120a), TNF-related apoptosis-inducing ligand receptor 1 (TRAIL-R1 /DR4), and receptor 2 (TRAIL-R2/DR5/APO-2/KILLER), as well as Death Receptor 3 (DR3/APO-3/TRAMP/WSL-1/LARD). They are involved in apoptosis signaling pathways. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260054  Cd Length: 80  Bit Score: 42.56  E-value: 9.71e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915 1457 LSWAELARELQFSVEDINRIRVENPNSLLDQSTALLTLWVDREGENAKMENLYTALRNID 1516
Cdd:cd08784    12 SQWKGFVRKLGLNEAEIDEIKNDNVQDTAEAKYQMLRNWHQLTGRKAAYDTLIKDLKKMN 71
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 767-794 1.06e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 41.12  E-value: 1.06e-04
                           10        20
                   ....*....|....*....|....*....
gi 160707915   767 GYSPLHQAAQQ-GHTDIVTLLLKNGASPN 794
Cdd:pfam00023    2 GNTPLHLAAGRrGNLEIVKLLLSKGADVN 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 271-300 1.10e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 40.70  E-value: 1.10e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 160707915   271 NGITPLHIASRRGNVIMVRLLLDRGAQIET 300
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 370-398 1.12e-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: 41.03  E-value: 1.12e-04
                            10        20
                    ....*....|....*....|....*....
gi 160707915    370 DHLTPLHVAAHCGHHRVAKVLLDKGAKPN 398
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 437-465 1.25e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 40.65  E-value: 1.25e-04
                            10        20
                    ....*....|....*....|....*....
gi 160707915    437 GLTPLHVASFMGHLPIVKNLLQRGASPNV 465
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 660-806 1.34e-04

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 46.80  E-value: 1.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  660 SANAESVQGVTPLHLAA---QEGHTEMVALLLskQANGNLGNksgltPLHLVSQeghvPVADVLIKhgvtvdattrmGYT 736
Cdd:cd21882    18 SAYQRGATGKTCLHKAAlnlNDGVNEAIMLLL--EAAPDSGN-----PKELVNA----PCTDEFYQ-----------GQT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  737 PLHVASHYGNIKLVKFLLQHQADVNAKTK-------------LGYSPLHQAAQQGHTDIVTLLLKNGASPNEVS---SNG 800
Cdd:cd21882    76 ALHIAIENRNLNLVRLLVENGADVSARATgrffrkspgnlfyFGELPLSLAACTNQEEIVRLLLENGAQPAALEaqdSLG 155


                  ....*.
gi 160707915  801 TTPLAI 806
Cdd:cd21882   156 NTVLHA 161
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 634-663 1.60e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 40.26  E-value: 1.60e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 160707915    634 NGYTPLHIAAKQNQIEVARSLLQYGGSANA 663
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 568-600 1.62e-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: 40.35  E-value: 1.62e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 160707915   568 KGFTPLHVAA-KYGKVRLAELLLEHDAHPNAAGK 600
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 453-523 1.65e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.43  E-value: 1.65e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 160707915  453 VKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKAKANAKAKDDQTPLHCAARIGHTGMVKLLL 523
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 596-757 1.81e-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: 46.39  E-value: 1.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  596 NAAGKN----GLTPLHVAVHHNNLDIVKLLLPRGGSPHSPA-------------WNGYTPLHIAAKQNQIEVARSLLQyg 658
Cdd:cd22197    84 NAQCTDeyyrGHSALHIAIEKRSLQCVKLLVENGADVHARAcgrffqkkqgtcfYFGELPLSLAACTKQWDVVNYLLE-- 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  659 gsanaesvQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHlvsqeghvpvaDVLIKHGVTVDATTRM----- 733
Cdd:cd22197   162 --------NPHQPASLQAQDSLGNTVLHALVMIADNSPENSALVIKMY-----------DGLLQAGARLCPTVQLeeisn 222

                         170       180
                  ....*....|....*....|....*.
gi 160707915  734 --GYTPLHVASHYGNIKLVKFLLQHQ 757
Cdd:cd22197   223 heGLTPLKLAAKEGKIEIFRHILQRE 248
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 304-336 1.81e-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: 40.35  E-value: 1.81e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 160707915   304 DELTPLHCAA-RNGHVRISEILLDHGAPIQAKTK 336
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 338-459 1.90e-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: 46.39  E-value: 1.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  338 GLSPIHMAAQGDHLDCVRLLLQYNAEIDDITLDHL-------------TPLHVAAHCGHHRVAKVLLDKGAKPNS---RA 401
Cdd:cd22197    94 GHSALHIAIEKRSLQCVKLLVENGADVHARACGRFfqkkqgtcfyfgeLPLSLAACTKQWDVVNYLLENPHQPASlqaQD 173

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 160707915  402 LNGFTPLH----IA--CKKNH---IRVMELLLKTGASIDA-------VTESGLTPLHVASFMGHLPIVKNLLQR 459
Cdd:cd22197   174 SLGNTVLHalvmIAdnSPENSalvIKMYDGLLQAGARLCPtvqleeiSNHEGLTPLKLAAKEGKIEIFRHILQR 247
PHA02795 PHA02795
ankyrin-like protein; Provisional
 125-188 1.91e-04

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 46.14  E-value: 1.91e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 160707915  125 EVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQG 188
Cdd:PHA02795  202 EIYKLCIPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRG 265
PHA02946 PHA02946
ankyin-like protein; Provisional
 379-466 1.92e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 46.20  E-value: 1.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  379 AHCG----HHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPI-- 452
Cdd:PHA02946   43 AYCGikglDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIer 122

                          90
                  ....*....|....
gi 160707915  453 VKNLLQRGASPNVS 466
Cdd:PHA02946  123 INLLVQYGAKINNS 136
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 660-791 2.08e-04

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 43.71  E-value: 2.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  660 SANAESVQGVTPLHLAAQEGhtEMVALLLSKQA----NGNLG---NKSGLTPLHLVSQEGHV-PVADV--LIKHGVTVDA 729
Cdd:PHA02736    9 FASEPDIEGENILHYLCRNG--GVTDLLAFKNAisdeNRYLVleyNRHGKQCVHIVSNPDKAdPQEKLklLMEWGADING 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 160707915  730 TTRM-GYTPLHVASHYGNIKLVKFLL-QHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGA 791
Cdd:PHA02736   87 KERVfGNTPLHIAVYTQNYELATWLCnQPGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGA 150
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 606-710 2.11e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 45.36  E-value: 2.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  606 LHVAVHHNNLDIVKLLLPRGGSPHSP---AWNGYT-PLHIAAKQNQIEVARSLLQYGGSANAESVQGV-TPLHLAAQEGH 680
Cdd:PHA02884   37 LYSSIKFHYTDIIDAILKLGADPEAPfplSENSKTnPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLHGC 116

                          90       100       110
                  ....*....|....*....|....*....|
gi 160707915  681 TEMVALLLSKQANGNLGNKSGLTPLHLVSQ 710
Cdd:PHA02884  117 LKCLEILLSYGADINIQTNDMVTPIELALM 146
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 111-164 2.16e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.04  E-value: 2.16e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 160707915  111 GNTALHIAALAGQDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLL 164
Cdd:PTZ00322  115 GRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 767-795 2.28e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.88  E-value: 2.28e-04
                            10        20
                    ....*....|....*....|....*....
gi 160707915    767 GYSPLHQAAQQGHTDIVTLLLKNGASPNE 795
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 568-597 2.33e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.93  E-value: 2.33e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 160707915   568 KGFTPLHVAAKYGKVRLAELLLEHDAHPNA 597
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 601-629 2.34e-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: 39.97  E-value: 2.34e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 160707915   601 NGLTPLHVAV-HHNNLDIVKLLLPRGGSPH 629
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVN 30
PHA03095 PHA03095
ankyrin-like protein; Provisional
 747-804 2.43e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.79  E-value: 2.43e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 160707915  747 IKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGH---TDIVTLLLKNGASPNEVSSNGTTPL 804
Cdd:PHA03095   27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPL 87
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 667-699 2.45e-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: 39.97  E-value: 2.45e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 160707915   667 QGVTPLHLAA-QEGHTEMVALLLSKQANGNLGNK 699
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 404-612 3.14e-04

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


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 45.62  E-value: 3.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  404 GFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLH--VASFMGHLpivknllqrgaspnvsnvkvetPLHMAARAG 481
Cdd:cd22197    94 GHSALHIAIEKRSLQCVKLLVENGADVHARACGRFFQKKqgTCFYFGEL----------------------PLSLAACTK 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  482 HTEVAKYLLQNKAKANAKAKDD---QTPLHCAARIGH---------TGMVKLLLENGA--SPNL-----ATTAGHTPLHT 542
Cdd:cd22197   152 QWDVVNYLLENPHQPASLQAQDslgNTVLHALVMIADnspensalvIKMYDGLLQAGArlCPTVqleeiSNHEGLTPLKL 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  543 AAREGHVDTALALLEKEASQAC------MTKKGFTPLHVAA-------KYGKVRLAELLLEHDAHPNAAGKNGLTPLHVA 609
Cdd:cd22197   232 AAKEGKIEIFRHILQREFSGPYqhlsrkFTEWCYGPVRVSLydlssvdSWEKNSVLEIIAFHSKSPNRHRMVVLEPLNKL 311


                  ...
gi 160707915  610 VHH 612
Cdd:cd22197   312 LQE 314
PHA02946 PHA02946
ankyin-like protein; Provisional
 119-292 3.19e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 45.43  E-value: 3.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  119 ALAGQDE-VVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENV--VAH 195
Cdd:PHA02946   46 GIKGLDErFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIerINL 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  196 LINYGTKgkvrlpalhIAARNDDTRTAAVLLQNDPNPDVLSKT-----------GFTPLHIAAHYENLN----VAQLLLN 260
Cdd:PHA02946  126 LVQYGAK---------INNSVDEEGCGPLLACTDPSERVFKKImsigfearivdKFGKNHIHRHLMSDNpkasTISWMMK 196

                         170       180       190
                  ....*....|....*....|....*....|....
gi 160707915  261 RGASVNFTPQNGITPLHIASRR--GNVIMVRLLL 292
Cdd:PHA02946  197 LGISPSKPDHDGNTPLHIVCSKtvKNVDIINLLL 230
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 601-629 3.25e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.55  E-value: 3.25e-04
                           10        20
                   ....*....|....*....|....*....
gi 160707915   601 NGLTPLHVAVHHNNLDIVKLLLPRGGSPH 629
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 503-656 3.42e-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: 45.46  E-value: 3.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   503 DQTPLHCAARIGHTGMVKLLLENGASPNLATTAGhtplhtaareghvdtalallekeasqACMTKKGFT-------PLHV 575
Cdd:TIGR00870  128 GITALHLAAHRQNYEIVKLLLERGASVPARACGD--------------------------FFVKSQGVDsfyhgesPLNA 181

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   576 AAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNL------------DIVKLLLPRGGSP----HSPAWNGYTPL 639
Cdd:TIGR00870  182 AACLGSPSIVALLSEDPADILTADSLGNTLLHLLVMENEFkaeyeelscqmyNFALSLLDKLRDSkeleVILNHQGLTPL 261

                          170
                   ....*....|....*..
gi 160707915   640 HIAAKQNQIEVARSLLQ 656
Cdd:TIGR00870  262 KLAAKEGRIVLFRLKLA 278
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 568-691 3.61e-04

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: 45.56  E-value: 3.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  568 KGFTPLHVAAKYGKVRLAELLLEHDAHPNAAGKN--------------GLTPLHVAVHHNNLDIVKLLLPrggSPHSPA- 632
Cdd:cd22193    75 EGQTALHIAIERRQGDIVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLSLAACTNQPDIVQYLLE---NEHQPAd 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  633 -----WNGYTPLH----IA--AKQNQIEVAR---SLLQYGG----SANAESV---QGVTPLHLAAQEGHTEMVALLLSKQ 691
Cdd:cd22193   152 ieaqdSRGNTVLHalvtVAdnTKENTKFVTRmydMILIRGAklcpTVELEEIrnnDGLTPLQLAAKMGKIEILKYILQRE 231
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 239-266 3.84e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.55  E-value: 3.84e-04
                           10        20
                   ....*....|....*....|....*...
gi 160707915   239 GFTPLHIAAHYENLNVAQLLLNRGASVN 266
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADIN 29
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 143-172 3.88e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.16  E-value: 3.88e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 160707915   143 KGFTPLYMAAQENHLEVVKFLLENGANQNV 172
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 568-597 4.11e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.11  E-value: 4.11e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 160707915    568 KGFTPLHVAAKYGKVRLAELLLEHDAHPNA 597
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 767-795 4.45e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.16  E-value: 4.45e-04
                           10        20
                   ....*....|....*....|....*....
gi 160707915   767 GYSPLHQAAQQGHTDIVTLLLKNGASPNE 795
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 667-693 4.62e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.11  E-value: 4.62e-04
                            10        20
                    ....*....|....*....|....*..
gi 160707915    667 QGVTPLHLAAQEGHTEMVALLLSKQAN 693
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 124-186 4.97e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 44.20  E-value: 4.97e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 160707915  124 DEVVRELVNYGANVNAQSQKG-FTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQ 186
Cdd:PHA02884   83 DDAAKLLIRYGADVNRYAEEAkITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELALM 146
Ank_4 pfam13637
Ankyrin repeats (many copies);
47-98 4.99e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.57  E-value: 4.99e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 160707915    47 TSFLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELL 98
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 568-694 5.41e-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: 44.85  E-value: 5.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  568 KGFTPLHVAAKYGKVRLAELLLEH--DAHPNAAG----KN-------GLTPLHVAVHHNNLDIVKLLLPRggsPHSPAW- 633
Cdd:cd22197    93 RGHSALHIAIEKRSLQCVKLLVENgaDVHARACGrffqKKqgtcfyfGELPLSLAACTKQWDVVNYLLEN---PHQPASl 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  634 -----NGYTPLH----IA--AKQNQIEVAR---SLLQYGGSANAE-------SVQGVTPLHLAAQEGHTEMVALLLSKQA 692
Cdd:cd22197   170 qaqdsLGNTVLHalvmIAdnSPENSALVIKmydGLLQAGARLCPTvqleeisNHEGLTPLKLAAKEGKIEIFRHILQREF 249


                  ..
gi 160707915  693 NG 694
Cdd:cd22197   250 SG 251
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 634-663 5.47e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.78  E-value: 5.47e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 160707915   634 NGYTPLHIAAKQNQIEVARSLLQYGGSANA 663
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 337-368 5.94e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.81  E-value: 5.94e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 160707915   337 NGLSPIHMAA-QGDHLDCVRLLLQYNAEIDDIT 368
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 437-465 6.16e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.78  E-value: 6.16e-04
                           10        20
                   ....*....|....*....|....*....
gi 160707915   437 GLTPLHVASFMGHLPIVKNLLQRGASPNV 465
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 602-716 6.33e-04

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: 44.79  E-value: 6.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  602 GLTPLHVAVHHNNLDIVKLLLPRGGSPHSPA--------------WNGYTPLHIAAKQNQIEVARSLLQYG---GSANAE 664
Cdd:cd22193    76 GQTALHIAIERRQGDIVALLVENGADVHAHAkgrffqpkyqgegfYFGELPLSLAACTNQPDIVQYLLENEhqpADIEAQ 155

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 160707915  665 SVQGVTPLHLAAQEGH---------TEMVALLLSKQAN-------GNLGNKSGLTPLHLVSQEGHVPV 716
Cdd:cd22193   156 DSRGNTVLHALVTVADntkentkfvTRMYDMILIRGAKlcptvelEEIRNNDGLTPLQLAAKMGKIEI 223
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 370-398 6.60e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.78  E-value: 6.60e-04
                           10        20
                   ....*....|....*....|....*....
gi 160707915   370 DHLTPLHVAAHCGHHRVAKVLLDKGAKPN 398
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 196-297 7.41e-04

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 42.17  E-value: 7.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  196 LINYGTKGKvrlPALHIAARND--DTRTAAVLLQN---DPNPDVlSKTGFTPLHIAAHYENLNVAQLLLNRGA----SVN 266
Cdd:PHA02736   48 VLEYNRHGK---QCVHIVSNPDkaDPQEKLKLLMEwgaDINGKE-RVFGNTPLHIAVYTQNYELATWLCNQPGvnmeILN 123

                          90       100       110
                  ....*....|....*....|....*....|.
gi 160707915  267 FTPQngiTPLHIASRRGNVIMVRLLLDRGAQ 297
Cdd:PHA02736  124 YAFK---TPYYVACERHDAKMMNILRAKGAQ 151
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 351-606 9.25e-04

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 44.10  E-value: 9.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  351 LDCVRLLLQYNAEIDDITLDhlTPLHVAA---HCGHHRVAKVLLDKGAKPNSRA-----------LNGFTPLHIACKKNH 416
Cdd:cd21882     8 LECLRWYLTDSAYQRGATGK--TCLHKAAlnlNDGVNEAIMLLLEAAPDSGNPKelvnapctdefYQGQTALHIAIENRN 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  417 IRVMELLLKTGASIDAVTESgltplhvASFMGHlpiVKNLLQRGaspnvsnvkvETPLHMAARAGHTEVAKYLLQNKAKA 496
Cdd:cd21882    86 LNLVRLLVENGADVSARATG-------RFFRKS---PGNLFYFG----------ELPLSLAACTNQEEIVRLLLENGAQP 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  497 NAKAKDD---QTPLHCAARIGH---------TGMVKLLLENGASPN-------LATTAGHTPLHTAAREGHVDTALALLE 557
Cdd:cd21882   146 AALEAQDslgNTVLHALVLQADntpensafvCQMYNLLLSYGAHLDptqqleeIPNHQGLTPLKLAAVEGKIVMFQHILQ 225

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 160707915  558 KEASQACM------TKKGFTPLHVAA-------KYGKVRLAELLLEHDAHPNAAGKNGLTPL 606
Cdd:cd21882   226 REFSGPYQplsrkfTEWTYGPVTSSLydlseidSWEKNSVLELIAFSKKREARHQMLVQEPL 287
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 304-331 9.85e-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: 9.85e-04
                            10        20
                    ....*....|....*....|....*...
gi 160707915    304 DELTPLHCAARNGHVRISEILLDHGAPI 331
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
PHA02798 PHA02798
ankyrin-like protein; Provisional
 58-300 1.04e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 43.67  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   58 LDKALDHLRNGVDINTCNQNGLNGLHLaskeghvkmvveLLHKEIIletttkkgntalhiaalaGQDEVVRELVNYGANV 137
Cdd:PHA02798   89 LDIVKILIENGADINKKNSDGETPLYC------------LLSNGYI------------------NNLEILLFMIENGADT 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  138 NAQSQKGFTPLYMAAQENH---LEVVKFLLENGANQNV-ATEDGFTPLAVALQQGHE----NVVAHLINYG--------- 200
Cdd:PHA02798  139 TLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINThNNKEKYDTLHCYFKYNIDridaDILKLFVDNGfiinkenks 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  201 TKGKVR--LPALHIAARNDDTRTAAVLLQ--NDPNPDVLsktGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPL 276
Cdd:PHA02798  219 HKKKFMeyLNSLLYDNKRFKKNILDFIFSyiDINQVDEL---GFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCL 295

                         250       260
                  ....*....|....*....|....
gi 160707915  277 HIASRRGNVIMVRLLLDRGAQIET 300
Cdd:PHA02798  296 FTAFENESKFIFNSILNKKPNKNT 319
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 467-590 1.05e-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: 43.98  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  467 NVKVETPLHMAARAGHTEVAKYLLQNKAKANAKAKDD--------------QTPLHCAARIGHTGMVKLLLENGASP-NL 531
Cdd:cd22194   138 AYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVffnpkykhegfyfgETPLALAACTNQPEIVQLLMEKESTDiTS 217

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 160707915  532 ATTAGHTPLH---TAAR--EGHV-------DTALALLEKEASQACMTKKGFTPLHVAAKYGKVRLAELLLE 590
Cdd:cd22194   218 QDSRGNTVLHalvTVAEdsKTQNdfvkrmyDMILLKSENKNLETIRNNEGLTPLQLAAKMGKAEILKYILS 288
Ank_5 pfam13857
Ankyrin repeats (many copies);
65-118 1.30e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.48  E-value: 1.30e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 160707915    65 LRNG-VDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIA 118
Cdd:pfam13857    2 LEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 634-663 1.59e-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: 1.59e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 160707915   634 NGYTPLHIAAKQ-NQIEVARSLLQYGGSANA 663
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNA 31
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 504-656 2.18e-03

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


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 42.92  E-value: 2.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  504 QTPLHCAARIGHTGMVKLLLENGASPNLATTA-------------GHTPLHTAAREGHVDTALALLEKEASQACMTKK-- 568
Cdd:cd22197    95 HSALHIAIEKRSLQCVKLLVENGADVHARACGrffqkkqgtcfyfGELPLSLAACTKQWDVVNYLLENPHQPASLQAQds 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  569 -GFTPLHvaakygkvrlAELLLEHDAHPNAAgkngltpLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQ 647
Cdd:cd22197   175 lGNTVLH----------ALVMIADNSPENSA-------LVIKMYDGLLQAGARLCPTVQLEEISNHEGLTPLKLAAKEGK 237


                  ....*....
gi 160707915  648 IEVARSLLQ 656
Cdd:cd22197   238 IEIFRHILQ 246
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 701-732 2.29e-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: 2.29e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 160707915   701 GLTPLHL-VSQEGHVPVADVLIKHGVTVDATTR 732
Cdd:pfam00023    2 GNTPLHLaAGRRGNLEIVKLLLSKGADVNARDK 34
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 239-377 2.42e-03

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 42.82  E-value: 2.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  239 GFTPLHIAAHYENLNVAQLLLNRGASVN-------FTPQN-------GITPLHIASRRGNVIMVRLLLDRGAQIETrTKD 304
Cdd:cd22194   141 GQTALNIAIERRQGDIVKLLIAKGADVNahakgvfFNPKYkhegfyfGETPLALAACTNQPEIVQLLMEKESTDIT-SQD 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  305 EL--TPLHC---AARNGHVRIS-------EILLDHGAPIQAKTKN--GLSPIHMAAQGDHLDCVRLLLqyNAEIDDITLD 370
Cdd:cd22194   220 SRgnTVLHAlvtVAEDSKTQNDfvkrmydMILLKSENKNLETIRNneGLTPLQLAAKMGKAEILKYIL--SREIKEKPNR 297


                  ....*..
gi 160707915  371 HLTPLHV 377
Cdd:cd22194   298 SLSRKFT 304
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 745-848 2.47e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 42.64  E-value: 2.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  745 GNIKLVKFLLQHQAD-VNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIAKRLGyisVTDVLKVVT 823
Cdd:PHA02874   12 GDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIG---AHDIIKLLI 88

                          90       100
                  ....*....|....*....|....*...
gi 160707915  824 D---ETSVVLVSDKHRmsypETVDEILD 848
Cdd:PHA02874   89 DngvDTSILPIPCIEK----DMIKTILD 112
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 71-205 2.66e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 40.24  E-value: 2.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   71 INTCNQN--GLNGLHLASKEGHVkmvVELL-HKEIILETT-------TKKGNTALHIAALAGQ---DEVVRELVNYGANV 137
Cdd:PHA02736    8 IFASEPDieGENILHYLCRNGGV---TDLLaFKNAISDENrylvleyNRHGKQCVHIVSNPDKadpQEKLKLLMEWGADI 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  138 NAQSQK-GFTPLYMAAQENHLEVVKFLLEN-GANQNVATEDGFTPLAVALQQGHENVVAHLINYGTKGKV 205
Cdd:PHA02736   85 NGKERVfGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGAQCKV 154
PHA02791 PHA02791
ankyrin-like protein; Provisional
 532-727 3.91e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 41.57  E-value: 3.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  532 ATTAGHTPLHTAAREGHVDTALALLEKEASQACMTKKgfTPLHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVH 611
Cdd:PHA02791   26 ADVHGHSALYYAIADNNVRLVCTLLNAGALKNLLENE--FPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVD 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  612 HNNLDIVKLLLPRGGSPHSPAWNGY-TPLHIAAKQNQIEVARSLLQYGGSANAESVQgVTPLHLAAQEGHTEMVALLLSK 690
Cdd:PHA02791  104 SGNMQTVKLFVKKNWRLMFYGKTGWkTSFYHAVMLNDVSIVSYFLSEIPSTFDLAIL-LSCIHITIKNGHVDMMILLLDY 182

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 160707915  691 QANGNLGNKSGLTP-LHLVSQEGHVPVADVLIKHGVTV 727
Cdd:PHA02791  183 MTSTNTNNSLLFIPdIKLAIDNKDLEMLQALFKYDINI 220
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 472-491 3.98e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.41  E-value: 3.98e-03
                            10        20
                    ....*....|....*....|
gi 160707915    472 TPLHMAARAGHTEVAKYLLQ 491
Cdd:smart00248    4 TPLHLAAENGNLEVVKLLLD 23
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 125-200 4.29e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 40.57  E-value: 4.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  125 EVVRELVNYGANVNAQSQ-KGFTPL--YMAAQEN-HLEVVKFLLENGANQNVATEDGFTPLAVALQQGHEN--VVAHLIN 198
Cdd:PHA02859   67 EILKFLIENGADVNFKTRdNNLSALhhYLSFNKNvEPEILKILIDSGSSITEEDEDGKNLLHMYMCNFNVRinVIKLLID 146


                  ..
gi 160707915  199 YG 200
Cdd:PHA02859  147 SG 148
PHA02795 PHA02795
ankyrin-like protein; Provisional
 719-813 4.91e-03

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 41.52  E-value: 4.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  719 VLIKHGVTVDATTRMGYTPLHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNEVSS 798
Cdd:PHA02795  173 IPDENDVKLDLYKIIQYTRGFLVDEPTVLEIYKLCIPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMS 252

                          90
                  ....*....|....*
gi 160707915  799 NGTTPLAIAKRLGYI 813
Cdd:PHA02795  253 NGYTCLDVAVDRGSV 267
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 716-807 5.42e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.78  E-value: 5.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  716 VADVLIKHGVTvDATTRMGYTPLHVAShYGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNE 795
Cdd:PLN03192  509 VGDLLGDNGGE-HDDPNMASNLLTVAS-TGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHI 586

                          90
                  ....*....|....
gi 160707915  796 VSSNGTTPL--AIA 807
Cdd:PLN03192  587 RDANGNTALwnAIS 600
PHA02791 PHA02791
ankyrin-like protein; Provisional
 634-798 5.47e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 40.80  E-value: 5.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  634 NGYTPLHIAAKQNQIEVARSLLQYGGSANAesVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGH 713
Cdd:PHA02791   29 HGHSALYYAIADNNVRLVCTLLNAGALKNL--LENEFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGN 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  714 VPVADVLIKHGVTVDATTRMGY-TPLHVASHYGNIKLVKFLLqhqADVNAKTKLG--YSPLHQAAQQGHTDIVTLLLKNG 790
Cdd:PHA02791  107 MQTVKLFVKKNWRLMFYGKTGWkTSFYHAVMLNDVSIVSYFL---SEIPSTFDLAilLSCIHITIKNGHVDMMILLLDYM 183


                  ....*...
gi 160707915  791 ASPNEVSS 798
Cdd:PHA02791  184 TSTNTNNS 191
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 371-445 6.77e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 40.74  E-value: 6.77e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160707915  371 HLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNG-FTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVAS 445
Cdd:PHA02884   70 KTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAkITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELAL 145
PHA02741 PHA02741
hypothetical protein; Provisional
 75-192 7.29e-03

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 39.26  E-value: 7.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915   75 NQNGLNGLHLASKEGHVKMVVELL------HKEIILETTTKKGNTALHIAALAGQD----EVVRELVNYGANVNAQ-SQK 143
Cdd:PHA02741   18 NSEGENFFHEAARCGCFDIIARFTpfirgdCHAAALNATDDAGQMCIHIAAEKHEAqlaaEIIDHLIELGADINAQeMLE 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 160707915  144 GFTPLYMAAQENHLEVVKFLL-ENGANQNVATEDGFTPLAVAlqQGHENV 192
Cdd:PHA02741   98 GDTALHLAAHRRDHDLAEWLCcQPGIDLHFCNADNKSPFELA--IDNEDV 145
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 337-365 8.25e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 35.70  E-value: 8.25e-03
                           10        20
                   ....*....|....*....|....*....
gi 160707915   337 NGLSPIHMAAQGDHLDCVRLLLQYNAEID 365
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 106-294 8.57e-03

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


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 40.99  E-value: 8.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  106 TTTKKGNTALHIAALAGQD----------EVVRELVNYGANVNAQSQ----KGFTPLYMAAQENHLEVVKFLLENGANQN 171
Cdd:cd22197    42 TEGSTGKTCLMKAVLNLQDgvnacimpllEIDKDSGNPKPLVNAQCTdeyyRGHSALHIAIEKRSLQCVKLLVENGADVH 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  172 VATEDGFTplavalqQGHENVVAHlinYGtkgkvRLPaLHIAARNDDTRTAAVLLQNDPNPDVLSKT---GFTPLH---- 244
Cdd:cd22197   122 ARACGRFF-------QKKQGTCFY---FG-----ELP-LSLAACTKQWDVVNYLLENPHQPASLQAQdslGNTVLHalvm 185

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 160707915  245 IAAHYENlNVAQL------LLNRGASVNFTPQ-------NGITPLHIASRRGNVIMVRLLLDR 294
Cdd:cd22197   186 IADNSPE-NSALVikmydgLLQAGARLCPTVQleeisnhEGLTPLKLAAKEGKIEIFRHILQR 247
PHA02946 PHA02946
ankyin-like protein; Provisional
 310-476 8.84e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 40.81  E-value: 8.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  310 HCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQYNAEIDDITLDHLTPLHVAAHCGHHRVAKV 389
Cdd:PHA02946   44 YCGIKGLDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIERI 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  390 --LLDKGAK-PNSRALNGFTPLhIACKKNHIRVMELLLKTGASIDAVTESGLTPLHvASFMGHLP---IVKNLLQRGASP 463
Cdd:PHA02946  124 nlLVQYGAKiNNSVDEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFGKNHIH-RHLMSDNPkasTISWMMKLGISP 201

                         170
                  ....*....|...
gi 160707915  464 NVSNVKVETPLHM 476
Cdd:PHA02946  202 SKPDHDGNTPLHI 214
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 386-463 8.90e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 39.80  E-value: 8.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707915  386 VAKVLLDKGAKPNSRAL-NGFTPLH--IACKKN-HIRVMELLLKTGASIDAVTESGLTPLHV--ASFMGHLPIVKNLLQR 459
Cdd:PHA02859   68 ILKFLIENGADVNFKTRdNNLSALHhyLSFNKNvEPEILKILIDSGSSITEEDEDGKNLLHMymCNFNVRINVIKLLIDS 147


                  ....
gi 160707915  460 GASP 463
Cdd:PHA02859  148 GVSF 151
 
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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