NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|568953835|ref|XP_006509058|]
View 

ankyrin-1 isoform X7 [Mus musculus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 1287-1416 5.92e-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: 221.96  E-value: 5.92e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  1287 VPYMAKFVIFAKMNDAREGRLRCYCMTDDKVDKTLEQHENFVEVARSRDIEVLEGMPLFAELSGNLVPVKKAAQQRSFHF 1366
Cdd:pfam17809    1 VPYLAKFVVFAKRYDPGEARLRCACMTDDGEDKTLEFHEGFTEVARSRDVEVLEGSPVSIELSGNLVPIKKKSQSRQMDF 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 568953835  1367 QSFRENRLAIPVKVRDSSREPGGFLSFLRKTMKYEDTQH-ILCHLNITMPP 1416
Cdd:pfam17809   81 KAFRENRLDGSVRVKDPSDPPKGLLSFMRDAKVDGGTVSqPLCTLNIVLPQ 131
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
227-479 6.75e-58

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 202.49  E-value: 6.75e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  227 ALHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMV 306
Cdd:COG0666    24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIV 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  307 RLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQYNAEIDDIT 386
Cdd:COG0666   104 KLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  387 LDHLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMG 466
Cdd:COG0666   184 NDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAG 263

                         250
                  ....*....|...
gi 568953835  467 HLPIVKNLLQRGA 479
Cdd:COG0666   264 AALIVKLLLLALL 276
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
570-838 7.09e-58

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 202.49  E-value: 7.09e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  570 ALALLEKEASQACMTKKGFTPLHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSP 649
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  650 AWNGYTPLHIAAKQNQIEVARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQE 729
Cdd:COG0666    84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  730 GHVPVADVLIKHGVTVDATTRMGYTPLHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGA 809
Cdd:COG0666   164 GNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243

                         250       260
                  ....*....|....*....|....*....
gi 568953835  810 SPNEVSSNGTTPLAIAKRLGYISVTDVLK 838
Cdd:COG0666   244 DLNAKDKDGLTALLLAAAAGAALIVKLLL 272
Death_ank1 cd08805
Death domain of Ankyrin-1; Death Domain (DD) of the human protein ankyrin-1 (ANK-1) and ...
 1452-1535 3.13e-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: 175.16  E-value: 3.13e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835 1452 DRVEMRMAVIREHLGLSWAELARELQFSVEDINRIRVENPNSLLDQSTALLTLWVDREGENAKMENLYTALRNIDRSEIV 1531
Cdd:cd08805     1 ERVEMKMAVIREHLGLSWAELARELQFSVEDINRIRVENPNSLLEQSTALLNLWVDREGENAKMEPLYPALYSIDRLTIV 80


                  ....
gi 568953835 1532 NMLE 1535
Cdd:cd08805    81 NILE 84
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
 962-1066 3.53e-49

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


:

Pssm-ID: 128514  Cd Length: 104  Bit Score: 170.22  E-value: 3.53e-49
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835    962 TGFLVSFMVDARGGSMRGSRhNGLRVVIPPRTCAAPTRITCRLVKPQKLNTPPPLAEEEGLASRIIALGPTGAQFLSPVI 1041
Cdd:smart00218    1 PSFLVSGTFDARGGRLRGPR-TGVRLIIPPGAIPQGTRYTCYLVVHKTLSTPPPLEEGETLLSPVVECGPHGALFLRPVI 79

                            90       100
                    ....*....|....*....|....*
gi 568953835   1042 VEIPHFASHGRGDRELVVLRSENGS 1066
Cdd:smart00218   80 LEVPHCASLRPRDWEIVLLRSENGG 104
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
60-327 3.58e-49

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 177.45  E-value: 3.58e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   60 KADAATSFLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALA 139
Cdd:COG0666    51 DALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYN 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  140 GQDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLINYGt 219
Cdd:COG0666   131 GNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAG- 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  220 kgkvrlpalhiaarnddtrtaavllqndPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASR 299
Cdd:COG0666   210 ----------------------------ADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAA 261

                         250       260
                  ....*....|....*....|....*...
gi 568953835  300 RGNVIMVRLLLDRGAQIETRTKDELTPL 327
Cdd:COG0666   262 AGAALIVKLLLLALLLLAAALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
459-549 7.13e-23

Ankyrin repeats (3 copies);


:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 94.41  E-value: 7.13e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   459 LHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQnkAKANAKAKDDQTPLHCAARIGHTGMVK 538
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE--HADVNLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|.
gi 568953835   539 LLLENGASPNL 549
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 ...
 1287-1416 5.92e-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: 221.96  E-value: 5.92e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  1287 VPYMAKFVIFAKMNDAREGRLRCYCMTDDKVDKTLEQHENFVEVARSRDIEVLEGMPLFAELSGNLVPVKKAAQQRSFHF 1366
Cdd:pfam17809    1 VPYLAKFVVFAKRYDPGEARLRCACMTDDGEDKTLEFHEGFTEVARSRDVEVLEGSPVSIELSGNLVPIKKKSQSRQMDF 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 568953835  1367 QSFRENRLAIPVKVRDSSREPGGFLSFLRKTMKYEDTQH-ILCHLNITMPP 1416
Cdd:pfam17809   81 KAFRENRLDGSVRVKDPSDPPKGLLSFMRDAKVDGGTVSqPLCTLNIVLPQ 131
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
227-479 6.75e-58

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 202.49  E-value: 6.75e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  227 ALHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMV 306
Cdd:COG0666    24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIV 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  307 RLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQYNAEIDDIT 386
Cdd:COG0666   104 KLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  387 LDHLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMG 466
Cdd:COG0666   184 NDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAG 263

                         250
                  ....*....|...
gi 568953835  467 HLPIVKNLLQRGA 479
Cdd:COG0666   264 AALIVKLLLLALL 276
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
570-838 7.09e-58

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 202.49  E-value: 7.09e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  570 ALALLEKEASQACMTKKGFTPLHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSP 649
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  650 AWNGYTPLHIAAKQNQIEVARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQE 729
Cdd:COG0666    84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  730 GHVPVADVLIKHGVTVDATTRMGYTPLHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGA 809
Cdd:COG0666   164 GNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243

                         250       260
                  ....*....|....*....|....*....
gi 568953835  810 SPNEVSSNGTTPLAIAKRLGYISVTDVLK 838
Cdd:COG0666   244 DLNAKDKDGLTALLLAAAAGAALIVKLLL 272
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
372-643 1.58e-53

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 189.78  E-value: 1.58e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  372 VRLLLQYNAEIDDITLDHLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAV 451
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  452 TESGLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKAKANAKAKDDQTPLHCAARI 531
Cdd:COG0666    84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  532 GHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALLEKEASQACMTKKGFTPLHVAAKYGKVRLAELLLEHDA 611
Cdd:COG0666   164 GNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243

                         250       260       270
                  ....*....|....*....|....*....|..
gi 568953835  612 HPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRG 643
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 ...
 1452-1535 3.13e-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: 175.16  E-value: 3.13e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835 1452 DRVEMRMAVIREHLGLSWAELARELQFSVEDINRIRVENPNSLLDQSTALLTLWVDREGENAKMENLYTALRNIDRSEIV 1531
Cdd:cd08805     1 ERVEMKMAVIREHLGLSWAELARELQFSVEDINRIRVENPNSLLEQSTALLNLWVDREGENAKMEPLYPALYSIDRLTIV 80


                  ....
gi 568953835 1532 NMLE 1535
Cdd:cd08805    81 NILE 84
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
 962-1066 3.53e-49

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


Pssm-ID: 128514  Cd Length: 104  Bit Score: 170.22  E-value: 3.53e-49
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835    962 TGFLVSFMVDARGGSMRGSRhNGLRVVIPPRTCAAPTRITCRLVKPQKLNTPPPLAEEEGLASRIIALGPTGAQFLSPVI 1041
Cdd:smart00218    1 PSFLVSGTFDARGGRLRGPR-TGVRLIIPPGAIPQGTRYTCYLVVHKTLSTPPPLEEGETLLSPVVECGPHGALFLRPVI 79

                            90       100
                    ....*....|....*....|....*
gi 568953835   1042 VEIPHFASHGRGDRELVVLRSENGS 1066
Cdd:smart00218   80 LEVPHCASLRPRDWEIVLLRSENGG 104
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
60-327 3.58e-49

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 177.45  E-value: 3.58e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   60 KADAATSFLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALA 139
Cdd:COG0666    51 DALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYN 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  140 GQDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLINYGt 219
Cdd:COG0666   131 GNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAG- 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  220 kgkvrlpalhiaarnddtrtaavllqndPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASR 299
Cdd:COG0666   210 ----------------------------ADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAA 261

                         250       260
                  ....*....|....*....|....*...
gi 568953835  300 RGNVIMVRLLLDRGAQIETRTKDELTPL 327
Cdd:COG0666   262 AGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 597-810 1.98e-39

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 153.28  E-value: 1.98e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  597 YGKVRLAELLLEHDAHPNAAG-----KNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQI----- 666
Cdd:PHA03100    7 LTKSRIIKVKNIKYIIMEDDLndysyKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvk 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  667 EVARSLLQYGGSANAESVQGVTPLHLAAQE--GHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHV--PVADVLIKHG 742
Cdd:PHA03100   87 EIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKG 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  743 VTVDATTR----------------MGYTPLHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLK 806
Cdd:PHA03100  167 VDINAKNRvnyllsygvpinikdvYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLN 246


                  ....
gi 568953835  807 NGAS 810
Cdd:PHA03100  247 NGPS 250
ZU5 pfam00791
ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.
 966-1063 3.41e-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: 135.73  E-value: 3.41e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   966 VSFMVDARGGSMRGSrHNGLRVVIPPRTCAAPTRITCRLVKPQKLNTPPPLAEEEGLASRIIALGPTGAQFLSPVIVEIP 1045
Cdd:pfam00791    1 VSGLVDSRGGRLVLP-NSGVSLLIPPGAIPEGTRIECYLAVNRDESSRPPLEEGETLLSPVVECGPPGLKFLKPVILEVP 79

                           90
                   ....*....|....*...
gi 568953835  1046 HFASHGRGDRELVVLRSE 1063
Cdd:pfam00791   80 HCASLRPEEWEIVLKRSD 97
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 141-486 9.66e-37

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 149.83  E-value: 9.66e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  141 QDE--VVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLI-NY 217
Cdd:PHA02876  155 QDEllIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIdNR 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  218 GTKGKVRLPALHiAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLN-VAQLLLNRGASVNFTPQNGITPLHI 296
Cdd:PHA02876  235 SNINKNDLSLLK-AIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYL 313

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  297 ASRRG-NVIMVRLLLDRGAQIETRTKDELTPLHCAA---RNGHVRISeiLLDHGAPIQAKTKNGLSPIHMAAQGDHLDCV 372
Cdd:PHA02876  314 MAKNGyDTENIRTLIMLGADVNAADRLYITPLHQAStldRNKDIVIT--LLELGANVNARDYCDKTPIHYAAVRNNVVII 391

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  373 RLLLQYNAEIDDITLDHLTPLHVAAhCGH--HRVAKVLLDKGAKPNSRALNGFTPLHIACKKN-HIRVMELLLKTGASID 449
Cdd:PHA02876  392 NTLLDYGADIEALSQKIGTALHFAL-CGTnpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVN 470

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 568953835  450 AVTESGLTPLHVAsfMGHLPIVKNLLQRGASPNVSNV 486
Cdd:PHA02876  471 AINIQNQYPLLIA--LEYHGIVNILLHYGAELRDSRV 505
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 100-318 2.88e-29

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 122.85  E-value: 2.88e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  100 LHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQD-----EVVRELVNYGANVNAQSQKGFTPLYMAAQE-- 172
Cdd:PHA03100   39 LYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKks 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  173 NHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHE--NVVAHLINYGT----KGKVRLpalhiaarnddtrtaavLLQN 246
Cdd:PHA03100  119 NSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVdinaKNRVNY-----------------LLSY 181

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568953835  247 DPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLDRGAQIET 318
Cdd:PHA03100  182 GVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 433-643 8.93e-24

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 106.23  E-value: 8.93e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  433 NHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKA 512
Cdd:PHA02875   13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  513 -KANAKAKDDQTPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALLEKEASQACMTKKGFTPL 591
Cdd:PHA02875   93 fADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPL 172

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568953835  592 HVAAKYGKVRLAELLLEHDAHPNAAGKNG-LTPLHVAVHHNNLDIVKLLLPRG 643
Cdd:PHA02875  173 IIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRG 225
Ank_2 pfam12796
Ankyrin repeats (3 copies);
459-549 7.13e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 94.41  E-value: 7.13e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   459 LHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQnkAKANAKAKDDQTPLHCAARIGHTGMVK 538
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE--HADVNLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|.
gi 568953835   539 LLLENGASPNL 549
Cdd:pfam12796   79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
100-190 1.44e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 93.64  E-value: 1.44e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   100 LHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQDEVVRELVNYgANVNAQSQkGFTPLYMAAQENHLEVVK 179
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                           90
                   ....*....|.
gi 568953835   180 FLLENGANQNV 190
Cdd:pfam12796   79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
525-615 2.31e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.87  E-value: 2.31e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   525 LHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALLEKEASQacMTKKGFTPLHVAAKYGKVRLAE 604
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN--LKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|.
gi 568953835   605 LLLEHDAHPNA 615
Cdd:pfam12796   79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
393-485 3.48e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.49  E-value: 3.48e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   393 LHVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASidAVTESGLTPLHVASFMGHLPIVK 472
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 568953835   473 NLLQRGASPNVSN 485
Cdd:pfam12796   79 LLLEKGADINVKD 91
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
 1451-1537 2.84e-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: 89.78  E-value: 2.84e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   1451 TDRVEMRMAVIREH-LGLSWAELARELQFSVEDINRIRVENPNSLLDQSTALLTLWVDREGENAKMENLYTALRNIDRSE 1529
Cdd:smart00005    1 PELTRQKLAKLLDHpLGLDWRELARKLGLSEADIDQIRTEAPRDLAEQSVQLLRLWEQREGKNATLGTLLEALRKMGRDD 80


                    ....*...
gi 568953835   1530 IVNMLEGS 1537
Cdd:smart00005   81 AVELLRSE 88
Death pfam00531
Death domain;
1455-1535 1.29e-19

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 85.11  E-value: 1.29e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  1455 EMRMAVIREH---LGLSWAELARELQFSVEDINRIRVENPNsLLDQSTALLTLWVDREGENAKMENLYTALRNIDRSEIV 1531
Cdd:pfam00531    1 RKQLDRLLDPpppLGKDWRELARKLGLSENEIDEIESENPR-LRSQTYELLRLWEQREGKNATVGTLLEALRKLGRRDAA 79


                   ....
gi 568953835  1532 NMLE 1535
Cdd:pfam00531   80 EKIQ 83
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 556-732 3.18e-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: 3.18e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  556 TPLHTAAREGHVDTALALLEKEASQACMTKK-GFTPLHVAAKYGKVRLAELLLEhdAHPNAAGK-------NGLTPLHVA 627
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGAlGETALHVAALYDNLEAAVVLME--AAPELVNEpmtsdlyQGETALHIA 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  628 VHHNNLDIVKLLLPRGG--------------SPHSPAWNGYTPLHIAAKQNQIEVARSLLQYGGSANAESVQGVTPLH-L 692
Cdd:cd22192    97 VVNQNLNLVRELIARGAdvvspratgtffrpGPKNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHiL 176

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 568953835  693 AAQEGHT---EMVALLLSKQANGNLG------NKSGLTPLHLVSQEGHV 732
Cdd:cd22192   177 VLQPNKTfacQMYDLILSYDKEDDLQpldlvpNNQGLTPFKLAAKEGNI 225
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 228-397 8.58e-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: 8.58e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  228 LHIAARNDDTRTAAVLLQNdPNPDVLSK--TGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQN-----GITPLHIASRR 300
Cdd:cd22192    21 LLLAAKENDVQAIKKLLKC-PSCDLFQRgaLGETALHVAALYDNLEAAVVLMEAAPELVNEPMTsdlyqGETALHIAVVN 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  301 GNVIMVRLLLDRGAQIET---------RTKDELT-----PLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAA-- 364
Cdd:cd22192   100 QNLNLVRELIARGADVVSpratgtffrPGPKNLIyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVlq 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 568953835  365 QGDHLDC--VRLLLQYNAEIDDITLDH------LTPLHVAA 397
Cdd:cd22192   180 PNKTFACqmYDLILSYDKEDDLQPLDLvpnnqgLTPFKLAA 220
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 128-279 8.72e-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: 8.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  128 KGNTALHIAALAGQDEVVRELVNYGANVNAQSQKGF--------------TPLYMAAQENHLEVVKFLLENGANqNVATE 193
Cdd:cd22194   140 EGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVFfnpkykhegfyfgeTPLALAACTNQPEIVQLLMEKEST-DITSQ 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  194 DGFTplavalqqgheNVVAHlinygtkgkvrlpALHIAARNDDTRTAAV------LLQNDPNPD---VLSKTGFTPLHIA 264
Cdd:cd22194   219 DSRG-----------NTVLH-------------ALVTVAEDSKTQNDFVkrmydmILLKSENKNletIRNNEGLTPLQLA 274

                         170
                  ....*....|....*
gi 568953835  265 AHYENLNVAQLLLNR 279
Cdd:cd22194   275 AKMGKAEILKYILSR 289
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 424-607 2.91e-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: 2.91e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  424 TPLHIACKKNHIRVMELLLKTgASIDAVTESGL--TPLHVASFMGHLPIVKNLLQrgASPNVSNVKV-------ETPLHM 494
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKC-PSCDLFQRGALgeTALHVAALYDNLEAAVVLME--AAPELVNEPMtsdlyqgETALHI 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  495 AARAGHTEVAKYLLQNKAkanakakDDQTP---------------------LHCAARIGHTGMVKLLLENGASPNLATTA 553
Cdd:cd22192    96 AVVNQNLNLVRELIARGA-------DVVSPratgtffrpgpknliyygehpLSFAACVGNEEIVRLLIEHGADIRAQDSL 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568953835  554 GHTPLH------TAAREGHVDTALALLEKEASQACM----TKKGFTPLHVAAKYGKVRLAELLL 607
Cdd:cd22192   169 GNTVLHilvlqpNKTFACQMYDLILSYDKEDDLQPLdlvpNNQGLTPFKLAAKEGNIVMFQHLV 232
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 157-377 1.34e-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: 1.34e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   157 AQSQKGFTPlymAAQENHLEVVKFLLENGA--NQNVATEDGFTPLAVALQQG-HENVVAHLINYGTKGKVRLPALHIAAR 233
Cdd:TIGR00870   15 SDEEKAFLP---AAERGDLASVYRDLEEPKklNINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAVGDTLLHAISL 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   234 ND--------------DTRTAAVLLQNDPNPDVLSKtGFTPLHIAAHYENLNVAQLLLNRGASVN-------FTPQNGIT 292
Cdd:TIGR00870   92 EYvdaveaillhllaaFRKSGPLELANDQYTSEFTP-GITALHLAAHRQNYEIVKLLLERGASVParacgdfFVKSQGVD 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   293 -------PLHIASRRGNVIMVRLLLDRGAQIETRtkDEL--TPLHCA-------ARNGHVRIS--EILLDHGAPIQAKTK 354
Cdd:TIGR00870  171 sfyhgesPLNAAACLGSPSIVALLSEDPADILTA--DSLgnTLLHLLvmenefkAEYEELSCQmyNFALSLLDKLRDSKE 248

                          250       260       270
                   ....*....|....*....|....*....|
gi 568953835   355 -------NGLSPIHMAAQGDHLDCVRLLLQ 377
Cdd:TIGR00870  249 levilnhQGLTPLKLAAKEGRIVLFRLKLA 278
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 664-826 4.08e-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: 4.08e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   664 NQIEVARSLLQYGGSANAESVQ-------GVTPLHLAAQEG-HTEMVALLLSKQANGNLGNksglTPLHLVSQEGHVPVA 735
Cdd:TIGR00870   23 PAAERGDLASVYRDLEEPKKLNincpdrlGRSALFVAAIENeNLELTELLLNLSCRGAVGD----TLLHAISLEYVDAVE 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   736 DVLI-------KHGVTVDATTRM------GYTPLHVASHYGNIKLVKFLLQHQADVNAKTK--------------LGYSP 788
Cdd:TIGR00870   99 AILLhllaafrKSGPLELANDQYtseftpGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESP 178

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 568953835   789 LHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIAK 826
Cdd:TIGR00870  179 LNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLV 216
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 438-591 6.54e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 61.04  E-value: 6.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  438 MELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKAKANAK 517
Cdd:PLN03192  541 LEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPH 620

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568953835  518 AKDDqtpLHC-AARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALLEKEASQACM-TKKGFTPL 591
Cdd:PLN03192  621 AAGD---LLCtAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAnTDDDFSPT 693
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 67-344 6.61e-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: 54.32  E-value: 6.61e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835    67 FLRAARSGNLDKALDHLRNG--VDINTCNQNGLNGLHLASKEGHVKMVVELLHKeiiLETTTKKGNTALHIAALAGQDeV 144
Cdd:TIGR00870   21 FLPAAERGDLASVYRDLEEPkkLNINCPDRLGRSALFVAAIENENLELTELLLN---LSCRGAVGDTLLHAISLEYVD-A 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   145 VRELVNYGAN----------VNAQS----QKGFTPLYMAAQENHLEVVKFLLENGANQNV-ATEDGFTplavaLQQGHEn 209
Cdd:TIGR00870   97 VEAILLHLLAafrksgplelANDQYtsefTPGITALHLAAHRQNYEIVKLLLERGASVPArACGDFFV-----KSQGVD- 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   210 vvahLINYGtkgkvRLPaLHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIA-------AHYENL-----NVAQLLL 277
Cdd:TIGR00870  171 ----SFYHG-----ESP-LNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLvmenefkAEYEELscqmyNFALSLL 240

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568953835   278 NRGAS-------VNFtpqNGITPLHIASRRGNVIMVRLLLdrgaQIETRTKDeltplHCAARNGHVRISEILLD 344
Cdd:TIGR00870  241 DKLRDskeleviLNH---QGLTPLKLAAKEGRIVLFRLKL----AIKYKQKK-----FVAWPNGQQLLSLYWLE 302
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 421-450 8.41e-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: 8.41e-07
                            10        20        30
                    ....*....|....*....|....*....|
gi 568953835    421 NGFTPLHIACKKNHIRVMELLLKTGASIDA 450
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 751-780 1.53e-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: 1.53e-06
                            10        20        30
                    ....*....|....*....|....*....|
gi 568953835    751 MGYTPLHVASHYGNIKLVKFLLQHQADVNA 780
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 161-190 2.38e-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: 2.38e-06
                            10        20        30
                    ....*....|....*....|....*....|
gi 568953835    161 KGFTPLYMAAQENHLEVVKFLLENGANQNV 190
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 520-549 2.20e-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: 2.20e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 568953835    520 DDQTPLHCAARIGHTGMVKLLLENGASPNL 549
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 485-608 1.10e-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: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  485 NVKVETPLHMAARAGHTEVAKYLLQNKAKANAKAKDD--------------QTPLHCAARIGHTGMVKLLLENGASP-NL 549
Cdd:cd22194   138 AYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVffnpkykhegfyfgETPLALAACTNQPEIVQLLMEKESTDiTS 217

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568953835  550 ATTAGHTPLH---TAAR--EGHV-------DTALALLEKEASQACMTKKGFTPLHVAAKYGKVRLAELLLE 608
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 ...
 1287-1416 5.92e-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: 221.96  E-value: 5.92e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  1287 VPYMAKFVIFAKMNDAREGRLRCYCMTDDKVDKTLEQHENFVEVARSRDIEVLEGMPLFAELSGNLVPVKKAAQQRSFHF 1366
Cdd:pfam17809    1 VPYLAKFVVFAKRYDPGEARLRCACMTDDGEDKTLEFHEGFTEVARSRDVEVLEGSPVSIELSGNLVPIKKKSQSRQMDF 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 568953835  1367 QSFRENRLAIPVKVRDSSREPGGFLSFLRKTMKYEDTQH-ILCHLNITMPP 1416
Cdd:pfam17809   81 KAFRENRLDGSVRVKDPSDPPKGLLSFMRDAKVDGGTVSqPLCTLNIVLPQ 131
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
227-479 6.75e-58

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 202.49  E-value: 6.75e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  227 ALHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMV 306
Cdd:COG0666    24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIV 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  307 RLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQYNAEIDDIT 386
Cdd:COG0666   104 KLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  387 LDHLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMG 466
Cdd:COG0666   184 NDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAG 263

                         250
                  ....*....|...
gi 568953835  467 HLPIVKNLLQRGA 479
Cdd:COG0666   264 AALIVKLLLLALL 276
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
570-838 7.09e-58

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 202.49  E-value: 7.09e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  570 ALALLEKEASQACMTKKGFTPLHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSP 649
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  650 AWNGYTPLHIAAKQNQIEVARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQE 729
Cdd:COG0666    84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  730 GHVPVADVLIKHGVTVDATTRMGYTPLHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGA 809
Cdd:COG0666   164 GNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243

                         250       260
                  ....*....|....*....|....*....
gi 568953835  810 SPNEVSSNGTTPLAIAKRLGYISVTDVLK 838
Cdd:COG0666   244 DLNAKDKDGLTALLLAAAAGAALIVKLLL 272
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
240-525 3.21e-57

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 200.57  E-value: 3.21e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  240 AAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLDRGAQIETR 319
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  320 TKDELTPLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQYNAEIDDITLDHLTPLHVAAHC 399
Cdd:COG0666    84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  400 GHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGA 479
Cdd:COG0666   164 GNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 568953835  480 SPNVSNVKVETPLHMAARAGHTEVAKYLLQNKAKANAKAKDDQTPL 525
Cdd:COG0666   244 DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
270-558 4.67e-57

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 200.18  E-value: 4.67e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  270 LNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILLDHGAPI 349
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  350 QAKTKNGLSPIHMAAQGDHLDCVRLLLQYNAEIDDITLDHLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIA 429
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  430 CKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQ 509
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 568953835  510 NKAKANAKAKDDQTPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPL 558
Cdd:COG0666   241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
435-723 1.15e-56

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 199.02  E-value: 1.15e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  435 IRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKAKA 514
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  515 NAKAKDDQTPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALLEKEASQACMTKKGFTPLHVA 594
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  595 AKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQIEVARSLLQ 674
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 568953835  675 YGGSANAESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPL 723
Cdd:COG0666   241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
172-459 2.08e-56

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 198.25  E-value: 2.08e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  172 ENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLINYGTKGKVRLPALHIAARNDDTRTAAVLLQNDPNPD 251
Cdd:COG0666     2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  252 VLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLDRGAQIETRTKDELTPLHCAA 331
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  332 RNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQYNAEIDDITLDHLTPLHVAAHCGHHRVAKVLLDK 411
Cdd:COG0666   162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 568953835  412 GAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPL 459
Cdd:COG0666   242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
536-822 9.96e-56

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 196.33  E-value: 9.96e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  536 MVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALLEKEASQACMTKKGFTPLHVAAKYGKVRLAELLLEHDAHPNA 615
Cdd:COG0666     3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  616 AGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQIEVARSLLQYGGSANAESVQGVTPLHLAAQ 695
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  696 EGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADVLIKHGVTVDATTRMGYTPLHVASHYGNIKLVKFLLQHQ 775
Cdd:COG0666   163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 568953835  776 ADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPL 822
Cdd:COG0666   243 ADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
76-393 1.86e-55

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 195.56  E-value: 1.86e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   76 LDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQDEVVRELVNYGANV 155
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  156 NAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPlavalqqghenvvahlinygtkgkvrlpaLHIAARND 235
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETP-----------------------------LHLAAYNG 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  236 DTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLDRGAQ 315
Cdd:COG0666   132 NLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGAD 211

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568953835  316 IETRTKDELTPLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQYNAEIDDITLDHLTPL 393
Cdd:COG0666   212 VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
338-624 2.03e-55

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 195.56  E-value: 2.03e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  338 ISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQYNAEIDDITLDHLTPLHVAAHCGHHRVAKVLLDKGAKPNS 417
Cdd:COG0666     3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  418 RALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAAR 497
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  498 AGHTEVAKYLLQNKAKANAKAKDDQTPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALLEKE 577
Cdd:COG0666   163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 568953835  578 ASQACMTKKGFTPLHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPL 624
Cdd:COG0666   243 ADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
54-357 1.06e-54

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 193.25  E-value: 1.06e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   54 NKMGFCKADAATSFLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTAL 133
Cdd:COG0666    12 LAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  134 HIAALAGQDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPlavalqqghenvvah 213
Cdd:COG0666    92 HAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTP--------------- 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  214 linygtkgkvrlpaLHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITP 293
Cdd:COG0666   157 --------------LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTA 222

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568953835  294 LHIASRRGNVIMVRLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILLDHGAPIQAKTKNGL 357
Cdd:COG0666   223 LDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLL 286
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
468-742 5.89e-54

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 191.32  E-value: 5.89e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  468 LPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKAKANAKAKDDQTPLHCAARIGHTGMVKLLLENGASP 547
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  548 NLATTAGHTPLHTAAREGHVDTALALLEKEASQACMTKKGFTPLHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVA 627
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  628 VHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQIEVARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVALLLS 707
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 568953835  708 KQANGNLGNKSGLTPLHLVSQEGHVPVADVLIKHG 742
Cdd:COG0666   241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLAL 275
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
502-785 1.54e-53

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 189.78  E-value: 1.54e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  502 EVAKYLLQNKAKANAKAKDDQTPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALLEKEASQA 581
Cdd:COG0666     2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  582 CMTKKGFTPLHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAA 661
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  662 KQNQIEVARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADVLIKH 741
Cdd:COG0666   162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 568953835  742 GVTVDATTRMGYTPLHVASHYGNIKLVKFLLQHQADVNAKTKLG 785
Cdd:COG0666   242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
372-643 1.58e-53

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 189.78  E-value: 1.58e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  372 VRLLLQYNAEIDDITLDHLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAV 451
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  452 TESGLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKAKANAKAKDDQTPLHCAARI 531
Cdd:COG0666    84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  532 GHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALLEKEASQACMTKKGFTPLHVAAKYGKVRLAELLLEHDA 611
Cdd:COG0666   164 GNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243

                         250       260       270
                  ....*....|....*....|....*....|..
gi 568953835  612 HPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRG 643
Cdd:COG0666   244 DLNAKDKDGLTALLLAAAAGAALIVKLLLLAL 275
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
402-690 2.59e-53

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 189.39  E-value: 2.59e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  402 HRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASP 481
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  482 NVSNVKVETPLHMAARAGHTEVAKYLLQNKAKANAKAKDDQTPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTA 561
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  562 AREGHVDTALALLEKEASQACMTKKGFTPLHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLP 641
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 568953835  642 RGGSPHSPAWNGYTPLHIAAKQNQIEVARSLLQYGGSANAESVQGVTPL 690
Cdd:COG0666   241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
602-838 7.90e-53

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 187.85  E-value: 7.90e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  602 LAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQIEVARSLLQYGGSANA 681
Cdd:COG0666     3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  682 ESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADVLIKHGVTVDATTRMGYTPLHVASH 761
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568953835  762 YGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIAKRLGYISVTDVLK 838
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 ...
 1452-1535 3.13e-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: 175.16  E-value: 3.13e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835 1452 DRVEMRMAVIREHLGLSWAELARELQFSVEDINRIRVENPNSLLDQSTALLTLWVDREGENAKMENLYTALRNIDRSEIV 1531
Cdd:cd08805     1 ERVEMKMAVIREHLGLSWAELARELQFSVEDINRIRVENPNSLLEQSTALLNLWVDREGENAKMEPLYPALYSIDRLTIV 80


                  ....
gi 568953835 1532 NMLE 1535
Cdd:cd08805    81 NILE 84
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
 962-1066 3.53e-49

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


Pssm-ID: 128514  Cd Length: 104  Bit Score: 170.22  E-value: 3.53e-49
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835    962 TGFLVSFMVDARGGSMRGSRhNGLRVVIPPRTCAAPTRITCRLVKPQKLNTPPPLAEEEGLASRIIALGPTGAQFLSPVI 1041
Cdd:smart00218    1 PSFLVSGTFDARGGRLRGPR-TGVRLIIPPGAIPQGTRYTCYLVVHKTLSTPPPLEEGETLLSPVVECGPHGALFLRPVI 79

                            90       100
                    ....*....|....*....|....*
gi 568953835   1042 VEIPHFASHGRGDRELVVLRSENGS 1066
Cdd:smart00218   80 LEVPHCASLRPRDWEIVLLRSENGG 104
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
60-327 3.58e-49

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 177.45  E-value: 3.58e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   60 KADAATSFLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALA 139
Cdd:COG0666    51 DALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYN 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  140 GQDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLINYGt 219
Cdd:COG0666   131 GNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAG- 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  220 kgkvrlpalhiaarnddtrtaavllqndPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASR 299
Cdd:COG0666   210 ----------------------------ADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAA 261

                         250       260
                  ....*....|....*....|....*...
gi 568953835  300 RGNVIMVRLLLDRGAQIETRTKDELTPL 327
Cdd:COG0666   262 AGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
633-837 5.11e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 153.96  E-value: 5.11e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  633 LDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQIEVARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVALLLSKQANG 712
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  713 NLGNKSGLTPLHLVSQEGHVPVADVLIKHGVTVDATTRMGYTPLHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQA 792
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 568953835  793 AQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIAKRLGYISVTDVL 837
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 597-810 1.98e-39

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 153.28  E-value: 1.98e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  597 YGKVRLAELLLEHDAHPNAAG-----KNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQI----- 666
Cdd:PHA03100    7 LTKSRIIKVKNIKYIIMEDDLndysyKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvk 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  667 EVARSLLQYGGSANAESVQGVTPLHLAAQE--GHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHV--PVADVLIKHG 742
Cdd:PHA03100   87 EIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKG 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  743 VTVDATTR----------------MGYTPLHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLK 806
Cdd:PHA03100  167 VDINAKNRvnyllsygvpinikdvYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLN 246


                  ....
gi 568953835  807 NGAS 810
Cdd:PHA03100  247 NGPS 250
ZU5 pfam00791
ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.
 966-1063 3.41e-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: 135.73  E-value: 3.41e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   966 VSFMVDARGGSMRGSrHNGLRVVIPPRTCAAPTRITCRLVKPQKLNTPPPLAEEEGLASRIIALGPTGAQFLSPVIVEIP 1045
Cdd:pfam00791    1 VSGLVDSRGGRLVLP-NSGVSLLIPPGAIPEGTRIECYLAVNRDESSRPPLEEGETLLSPVVECGPPGLKFLKPVILEVP 79

                           90
                   ....*....|....*...
gi 568953835  1046 HFASHGRGDRELVVLRSE 1063
Cdd:pfam00791   80 HCASLRPEEWEIVLKRSD 97
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 141-486 9.66e-37

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 149.83  E-value: 9.66e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  141 QDE--VVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLI-NY 217
Cdd:PHA02876  155 QDEllIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIdNR 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  218 GTKGKVRLPALHiAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLN-VAQLLLNRGASVNFTPQNGITPLHI 296
Cdd:PHA02876  235 SNINKNDLSLLK-AIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYL 313

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  297 ASRRG-NVIMVRLLLDRGAQIETRTKDELTPLHCAA---RNGHVRISeiLLDHGAPIQAKTKNGLSPIHMAAQGDHLDCV 372
Cdd:PHA02876  314 MAKNGyDTENIRTLIMLGADVNAADRLYITPLHQAStldRNKDIVIT--LLELGANVNARDYCDKTPIHYAAVRNNVVII 391

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  373 RLLLQYNAEIDDITLDHLTPLHVAAhCGH--HRVAKVLLDKGAKPNSRALNGFTPLHIACKKN-HIRVMELLLKTGASID 449
Cdd:PHA02876  392 NTLLDYGADIEALSQKIGTALHFAL-CGTnpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVN 470

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 568953835  450 AVTESGLTPLHVAsfMGHLPIVKNLLQRGASPNVSNV 486
Cdd:PHA02876  471 AINIQNQYPLLIA--LEYHGIVNILLHYGAELRDSRV 505
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 243-480 6.46e-34

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 136.72  E-value: 6.46e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  243 LLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVI-----MVRLLLDRGAQIE 317
Cdd:PHA03100   21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLtdvkeIVKLLLEYGANVN 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  318 TRTKDELTPLHCAARN--GHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDH--LDCVRLLLQYNAEIDDITldhltpl 393
Cdd:PHA03100  101 APDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKN------- 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  394 hvaahcghhRVaKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKN 473
Cdd:PHA03100  174 ---------RV-NYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKL 243


                  ....*..
gi 568953835  474 LLQRGAS 480
Cdd:PHA03100  244 LLNNGPS 250
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 291-509 3.77e-33

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 134.41  E-value: 3.77e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  291 ITPLHIASRRGNVIMVRLLLDRGAQIETRTKDELTPLHCAARNGHV-----RISEILLDHGAPIQAKTKNGLSPIHMAAQ 365
Cdd:PHA03100   36 VLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAIS 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  366 G--DHLDCVRLLLQYNAEIDDITLDHLTPLHVAAHCGHH--RVAKVLLDKGAKPNsralngftplhiacKKNHIrvmELL 441
Cdd:PHA03100  116 KksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDIN--------------AKNRV---NYL 178

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568953835  442 LKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQ 509
Cdd:PHA03100  179 LSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLN 246
PHA03095 PHA03095
ankyrin-like protein; Provisional
 167-465 8.94e-33

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 134.38  E-value: 8.94e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  167 YMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVvahlinygtKGKVRLpalhiaarnddtrtaavLLQN 246
Cdd:PHA03095   19 LLNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKV---------KDIVRL-----------------LLEA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  247 DPNPDVLSKTGFTPLHIAAHYEN-LNVAQLLLNRGASVNFTPQNGITPLHI--ASRRGNVIMVRLLLDRGAQIETRTKDE 323
Cdd:PHA03095   73 GADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYG 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  324 LTPLHCAARNGHVRIS--EILLDHGAPIQAKTKNGLSPIHMAAQG--DHLDCVRLLLQYNAEIDDITLDHLTPLHVAAHC 399
Cdd:PHA03095  153 MTPLAVLLKSRNANVEllRLLIDAGADVYAVDDRFRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSMATG 232

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568953835  400 GHHRVAKV--LLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLhvaSFM 465
Cdd:PHA03095  233 SSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL---SLM 297
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 243-451 1.17e-32

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 133.25  E-value: 1.17e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  243 LLQNDPNPDVLSKTGFTPLHIAAHY-----ENLNVAQLLLNRGASVNFTPQNGITPLHIAS--RRGNVIMVRLLLDRGAQ 315
Cdd:PHA03100   54 LLDNGADINSSTKNNSTPLHYLSNIkynltDVKEIVKLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGAN 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  316 IETRTKDELTPLHCAARNGHV--RISEILLDHGAPIQAKTKnglspihmaaqgdhldcVRLLLQYNAEIDDITLDHLTPL 393
Cdd:PHA03100  134 VNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKDVYGFTPL 196

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568953835  394 HVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAV 451
Cdd:PHA03100  197 HYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTI 254
PHA03095 PHA03095
ankyrin-like protein; Provisional
 270-576 8.82e-32

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 131.30  E-value: 8.82e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  270 LNVAQLLLNRGASVNFTPQNGITPLHIASRRGN---VIMVRLLLDRGAQIETRTKDELTPLHCAARNGHV-RISEILLDH 345
Cdd:PHA03095   27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKA 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  346 GAPIQAKTKNGLSPIHMAAQGD--HLDCVRLLLQYNAEIDDITLDHLTPLHVaaHCGHHRVA----KVLLDKGAKPNSRA 419
Cdd:PHA03095  107 GADVNAKDKVGRTPLHVYLSGFniNPKVIRLLLRKGADVNALDLYGMTPLAV--LLKSRNANvellRLLIDAGADVYAVD 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  420 LNGFTPLHIACKKNHIR--VMELLLKTGASIDAVTESGLTPLHVASFMGHL--PIVKNLLQRGASPNVSNVKVETPLHMA 495
Cdd:PHA03095  185 DRFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATGSSCkrSLVLPLLIAGISINARNRYGQTPLHYA 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  496 ARAGHTEVAKYLLQNkakanakakddqtplhcaarightgmvklllenGASPNLATTAGHTPLHTAAREGHVDTALALLE 575
Cdd:PHA03095  265 AVFNNPRACRRLIAL---------------------------------GADINAVSSDGNTPLSLMVRNNNGRAVRAALA 311


                  .
gi 568953835  576 K 576
Cdd:PHA03095  312 K 312
Death_ank cd08317
Death domain associated with Ankyrins; Death Domain (DD) associated with Ankyrins. Ankyrins ...
 1452-1535 2.13e-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: 118.52  E-value: 2.13e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835 1452 DRVEMRMAVIREHLGLSWAELARELQFSVEDINRIRVENPNSLLDQSTALLTLWVDREGENAKMENLYTALRNIDRSEIV 1531
Cdd:cd08317     1 HRADLRLSDIANLLGSDWPELARELGVSEEDIDLIRSENPNSLAQQAMAMLRLWLEREGEKATGNALESALKKIGRDDIV 80


                  ....
gi 568953835 1532 NMLE 1535
Cdd:cd08317    81 EKCE 84
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 264-483 2.37e-31

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 128.96  E-value: 2.37e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  264 AAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILL 343
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  344 DHGAPIQ-AKTKNGLSPIHMAAQGDHLDCVRLLLQYNAEIDDITLDHLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNG 422
Cdd:PHA02875   89 DLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCG 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568953835  423 FTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLP-IVKNLLQRGASPNV 483
Cdd:PHA02875  169 CTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIdIVRLFIKRGADCNI 230
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 503-837 1.25e-29

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 127.49  E-value: 1.25e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  503 VAKYLLQNKAKANAKAKDDQTPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALLEKEASqac 582
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSN--- 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  583 MTKKGFTPLHvAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLD-IVKLLLPRGGSPHSPAWNGYTPLHIAA 661
Cdd:PHA02876  237 INKNDLSLLK-AIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMA 315

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  662 KQN-QIEVARSLLQYGGSANAESVQGVTPLHLAAQ-EGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADVLI 739
Cdd:PHA02876  316 KNGyDTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLL 395

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  740 KHGVTVDATTRMGYTPLHVASHYGNIKL-VKFLLQHQADVNAKTKLGYSPLHQAAQQG-HTDIVTLLLKNGASPNEVSSN 817
Cdd:PHA02876  396 DYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQ 475

                         330       340
                  ....*....|....*....|
gi 568953835  818 GTTPLAIAkrLGYISVTDVL 837
Cdd:PHA02876  476 NQYPLLIA--LEYHGIVNIL 493
PHA03095 PHA03095
ankyrin-like protein; Provisional
 537-863 1.32e-29

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 124.75  E-value: 1.32e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  537 VKLLLENGASPNLATTAGHTPLHTAAREGH---VDTALALLEKEASQACMTKKGFTPLHVAAKYGKV-RLAELLLEHDAH 612
Cdd:PHA03095   30 VRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGAD 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  613 PNAAGKNGLTPLHV--AVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQIEVA--RSLLQYGGSANAESVQGVT 688
Cdd:PHA03095  110 VNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVEllRLLIDAGADVYAVDDRFRS 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  689 PLHLAAQEGHT--EMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADV--LIKHGVTVDATTRMGYTPLHVASHYGN 764
Cdd:PHA03095  190 LLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNN 269

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  765 IKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSNgttpLAIAKRLGYISVTD-----VLKV 839
Cdd:PHA03095  270 PRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAAT----LNTASVAGGDIPSDatrlcVAKV 345

                         330       340
                  ....*....|....*....|....
gi 568953835  840 VTDETSVVLvSDKHRMSYPETVDE 863
Cdd:PHA03095  346 VLRGAFSLL-PEPIRAYHADFIRE 368
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 251-530 2.21e-29

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 124.22  E-value: 2.21e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  251 DVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLdrGAQIETRTKDELTPLHCA 330
Cdd:PHA02878   31 TSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMI--RSINKCSVFYTLVAIKDA 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  331 ARNGHVRISE-ILLDHGAPIQAKTkngLSPIHMAAQGDHLDC--VRLLLQYNAEIDDITLDHL-TPLHVAAHCGHHRVAK 406
Cdd:PHA02878  109 FNNRNVEIFKiILTNRYKNIQTID---LVYIDKKSKDDIIEAeiTKLLLSYGADINMKDRHKGnTALHYATENKDQRLTE 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  407 VLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVA-SFMGHLPIVKNLLQRGASPNV-S 484
Cdd:PHA02878  186 LLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAkS 265

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 568953835  485 NVKVETPLHMAARAghTEVAKYLLQNKAKANAKAKDDQTPLHCAAR 530
Cdd:PHA02878  266 YILGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAVK 309
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 100-318 2.88e-29

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 122.85  E-value: 2.88e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  100 LHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQD-----EVVRELVNYGANVNAQSQKGFTPLYMAAQE-- 172
Cdd:PHA03100   39 LYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKks 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  173 NHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHE--NVVAHLINYGT----KGKVRLpalhiaarnddtrtaavLLQN 246
Cdd:PHA03100  119 NSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVdinaKNRVNY-----------------LLSY 181

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568953835  247 DPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLDRGAQIET 318
Cdd:PHA03100  182 GVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 233-545 9.01e-29

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 124.79  E-value: 9.01e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  233 RNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVR----- 307
Cdd:PHA02876  154 QQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKaiidn 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  308 ------------------------LLLDRGAQIETRTKDELTPLHCAARNGHV-RISEILLDHGAPIQAKTKNGLSPIH- 361
Cdd:PHA02876  234 rsninkndlsllkairnedletslLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYl 313

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  362 MAAQGDHLDCVRLLLQYNAEIDDITLDHLTPLHVAAHCGHHR-VAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMEL 440
Cdd:PHA02876  314 MAKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKdIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINT 393

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  441 LLKTGASIDAVTESGLTPLHVAsFMGHLPI--VKNLLQRGASPNVSNVKVETPLHMAARAG-HTEVAKYLLQNKAKANAK 517
Cdd:PHA02876  394 LLDYGADIEALSQKIGTALHFA-LCGTNPYmsVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAI 472

                         330       340
                  ....*....|....*....|....*...
gi 568953835  518 AKDDQTPLHCAarIGHTGMVKLLLENGA 545
Cdd:PHA02876  473 NIQNQYPLLIA--LEYHGIVNILLHYGA 498
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 307-597 9.24e-29

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 121.61  E-value: 9.24e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  307 RLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLlqynaeIDDIT 386
Cdd:PHA02874   19 KIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLL------IDNGV 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  387 LDHLTPLHvaahCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMG 466
Cdd:PHA02874   93 DTSILPIP----CIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHN 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  467 HLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKAKANAKAKDDQTPLHCAarIGHTGMVKLLLENGAS 546
Cdd:PHA02874  169 FFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA--IIHNRSAIELLINNAS 246

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568953835  547 PNLATTAGHTPLHTAAR-EGHVDTALALLEKEASQACMTKKGFTPLHVAAKY 597
Cdd:PHA02874  247 INDQDIDGSTPLHHAINpPCDIDIIDILLYHKADISIKDNKGENPIDTAFKY 298
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 268-611 5.87e-28

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 122.48  E-value: 5.87e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  268 ENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILLDHGA 347
Cdd:PHA02876  156 DELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRS 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  348 PIQaktKNGLSPIHmAAQGDHLDCVRLLLQYNAEIDDITLDHLTPLHVAAHCGH-HRVAKVLLDKGAKPNSRALNGFTPL 426
Cdd:PHA02876  236 NIN---KNDLSLLK-AIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPL 311

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  427 HIACKKNH-IRVMELLLKTGASIDAVTESGLTPLHVASFMG-HLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVA 504
Cdd:PHA02876  312 YLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVII 391

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  505 KYLLQNKAKANAKAKDDQTPLHCAARIGHTGM-VKLLLENGASPNLATTAGHTPLHTAAREG-HVDTALALLEKEASQAC 582
Cdd:PHA02876  392 NTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNA 471

                         330       340
                  ....*....|....*....|....*....
gi 568953835  583 MTKKGFTPLHVAAKYGKVrlAELLLEHDA 611
Cdd:PHA02876  472 INIQNQYPLLIALEYHGI--VNILLHYGA 498
PHA03095 PHA03095
ankyrin-like protein; Provisional
 83-380 9.06e-28

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 119.36  E-value: 9.06e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   83 LRNGVDINTCNQNGLNGLH--LASKEGHVKMVVE-LLHKEIILETTTKKGNTALHIAALAGQDE-VVRELVNYGANVNAQ 158
Cdd:PHA03095   34 LAAGADVNFRGEYGKTPLHlyLHYSSEKVKDIVRlLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAGADVNAK 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  159 SQKGFTPL--YMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENV--VAHLINYG----TKGKVRLPALHI 230
Cdd:PHA03095  114 DKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGadvyAVDDRFRSLLHH 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  231 AARNDDTRTAAV--LLQNDPNPDVLSKTGFTPLHIAAHY---ENLNVAQLLLNrGASVNFTPQNGITPLHIASRRGNVIM 305
Cdd:PHA03095  194 HLQSFKPRARIVreLIRAGCDPAATDMLGNTPLHSMATGsscKRSLVLPLLIA-GISINARNRYGQTPLHYAAVFNNPRA 272

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568953835  306 VRLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILLDHGAPIQ--AKTKNGLSPihmAAQGDHLDCVRLLLQYNA 380
Cdd:PHA03095  273 CRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAEtvAATLNTASV---AGGDIPSDATRLCVAKVV 346
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 163-462 2.86e-27

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 118.06  E-value: 2.86e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  163 FTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLINYGTKGKVRlpalhiaarnddtrtaav 242
Cdd:PHA02878   38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVF------------------ 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  243 llqndpNPDVLSKTGFtplhiaaHYENLNVAQLLLNRGASVNFTpqngITPLHIASRRGNVI----MVRLLLDRGAQIET 318
Cdd:PHA02878  100 ------YTLVAIKDAF-------NNRNVEIFKIILTNRYKNIQT----IDLVYIDKKSKDDIieaeITKLLLSYGADINM 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  319 RTKDEL-TPLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQYNAEIDDITLDHLTPLHVA- 396
Cdd:PHA02878  163 KDRHKGnTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISv 242

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568953835  397 AHCGHHRVAKVLLDKGAKPNSRA-LNGFTPLHIACKKNhiRVMELLLKTGASIDAVTESGLTPLHVA 462
Cdd:PHA02878  243 GYCKDYDILKLLLEHGVDVNAKSyILGLTALHSSIKSE--RKLKLLLEYGADINSLNSYKLTPLSSA 307
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 557-830 5.32e-27

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 117.29  E-value: 5.32e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  557 PLHTAAREGHVDTALALLEKEASQACMTKKGFTPLHVAAKY-GKVRLAELLLEHDahpNAAGKNGLTPLHVAVHHNNLDI 635
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEpNKLGMKEMIRSIN---KCSVFYTLVAIKDAFNNRNVEI 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  636 VKLLLPRGGSphspawNGYT----PLHIAAKQNQIE--VARSLLQYGGSANAESV-QGVTPLHLAAQEGHTEMVALLLSK 708
Cdd:PHA02878  117 FKIILTNRYK------NIQTidlvYIDKKSKDDIIEaeITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSY 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  709 QANGNLGNKSGLTPLHLVSQEGHVPVADVLIKHGVTVDATTRMGYTPLHVASHY-GNIKLVKFLLQHQADVNAK-TKLGY 786
Cdd:PHA02878  191 GANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKsYILGL 270

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 568953835  787 SPLHQAAQQghTDIVTLLLKNGASPNEVSSNGTTPLAIA--KRLGY 830
Cdd:PHA02878  271 TALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAvkQYLCI 314
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 627-818 9.18e-27

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 115.47  E-value: 9.18e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  627 AVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQIEVARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVALLL 706
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  707 --SKQANgNLGNKSGLTPLHLVSQEGHVPVADVLIKHGVTVDATTRMGYTPLHVASHYGNIKLVKFLLQHQADVNAKTKL 784
Cdd:PHA02875   89 dlGKFAD-DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCC 167

                         170       180       190
                  ....*....|....*....|....*....|....
gi 568953835  785 GYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSNG 818
Cdd:PHA02875  168 GCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNG 201
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 589-838 2.24e-26

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 114.68  E-value: 2.24e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  589 TPLHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHS---PAWNG------------ 653
Cdd:PHA02874   37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSIlpiPCIEKdmiktildcgid 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  654 --------YTPLHIAAKQNQIEVARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHL 725
Cdd:PHA02874  117 vnikdaelKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  726 VSQEGHVPVADVLIKHGVTVDATTRMGYTPLHVASHYgNIKLVKFLLqHQADVNAKTKLGYSPLHQAAQQG-HTDIVTLL 804
Cdd:PHA02874  197 AAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIH-NRSAIELLI-NNASINDQDIDGSTPLHHAINPPcDIDIIDIL 274

                         250       260       270
                  ....*....|....*....|....*....|....
gi 568953835  805 LKNGASPNEVSSNGTTPLAIAKRlgYISVTDVLK 838
Cdd:PHA02874  275 LYHKADISIKDNKGENPIDTAFK--YINKDPVIK 306
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 594-812 3.25e-26

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 113.55  E-value: 3.25e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  594 AAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQIEVARSLL 673
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  674 QYGGSANAESVQ-GVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADVLIKHGVTVDATTRMG 752
Cdd:PHA02875   89 DLGKFADDVFYKdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCG 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568953835  753 YTPLHVASHYGNIKLVKFLLQHQADVNAKTKLG-YSPLHQAAQQGHTDIVTLLLKNGASPN 812
Cdd:PHA02875  169 CTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCN 229
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 298-546 3.79e-26

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 113.61  E-value: 3.79e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  298 SRRGNVIMVRLLLDRGAQIETRTKDELTPLHCAARngHVRIS--EILLDHGAPIQAKTKNGLSPIH-----MAAQGDHLD 370
Cdd:PHA03100   10 SRIIKVKNIKYIIMEDDLNDYSYKKPVLPLYLAKE--ARNIDvvKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  371 CVRLLLQYNAEIDDITLDHLTPLHVAA--HCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHI--RVMELLLKTGA 446
Cdd:PHA03100   88 IVKLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGV 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  447 SIDAVTEsgltplhvasfmghlpiVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKAKANAKAKDDQTPLH 526
Cdd:PHA03100  168 DINAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLH 230

                         250       260
                  ....*....|....*....|
gi 568953835  527 CAARIGHTGMVKLLLENGAS 546
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 ...
 1452-1535 2.83e-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: 101.29  E-value: 2.83e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835 1452 DRVEMRMAVIREHLGLSWAELARELQFSVEDINRIRVENPNSLLDQSTALLTLWVDREGENAKMENLYTALRNIDRSEIV 1531
Cdd:cd08803     1 ERTDIRMAIVADHLGLSWTELARELNFSVDEINQIRVENPNSLIAQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIV 80


                  ....
gi 568953835 1532 NMLE 1535
Cdd:cd08803    81 TLLE 84
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 499-714 5.27e-25

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 110.08  E-value: 5.27e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  499 GHTEVAKYLLQNKAKANAKAKDDQTPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALLEKEA 578
Cdd:PHA02875   13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  579 -SQACMTKKGFTPLHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPL 657
Cdd:PHA02875   93 fADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPL 172

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568953835  658 HIAAKQNQIEVARSLLQYGGSANAESVQG-VTPLHLAAQEGHTEMVALLLSKQANGNL 714
Cdd:PHA02875  173 IIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNI 230
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 139-473 7.12e-25

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 110.05  E-value: 7.12e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  139 AGQDEVVRELV-NYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLINY 217
Cdd:PHA02874   11 SGDIEAIEKIIkNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDN 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  218 GTKGKVrLPALHIaaRNDDTRTaavLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIA 297
Cdd:PHA02874   91 GVDTSI-LPIPCI--EKDMIKT---ILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIA 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  298 SRRGNVIMVRLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQgdHLDCVRLLLQ 377
Cdd:PHA02874  165 IKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLI 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  378 YNAEIDDITLDHLTPLHVAAH--CGHHrVAKVLLDKGAKPNSRALNGFTPLHIACKknHIRVMELLLKTGAsiDAVTESG 455
Cdd:PHA02874  243 NNASINDQDIDGSTPLHHAINppCDID-IIDILLYHKADISIKDNKGENPIDTAFK--YINKDPVIKDIIA--NAVLIKE 317

                         330
                  ....*....|....*...
gi 568953835  456 LTPLHVASFMGHLPIVKN 473
Cdd:PHA02874  318 ADKLKDSDFLEHIEIKDN 335
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 173-387 5.20e-24

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 107.00  E-value: 5.20e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  173 NHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLINYGTKGKVRLPA----LHIAARNDDTRTAAVLLQ-ND 247
Cdd:PHA02875   13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDieseLHDAVEEGDVKAVEELLDlGK 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  248 PNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLDRGAQIETRTKDELTPL 327
Cdd:PHA02875   93 FADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPL 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568953835  328 HCAARNGHVRISEILLDHGAPIQAKTKNG-LSPIHMAAQGDHLDCVRLLLQYNAEIDDITL 387
Cdd:PHA02875  173 IIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNIMFM 233
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 433-643 8.93e-24

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 106.23  E-value: 8.93e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  433 NHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKA 512
Cdd:PHA02875   13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  513 -KANAKAKDDQTPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALLEKEASQACMTKKGFTPL 591
Cdd:PHA02875   93 fADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPL 172

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568953835  592 HVAAKYGKVRLAELLLEHDAHPNAAGKNG-LTPLHVAVHHNNLDIVKLLLPRG 643
Cdd:PHA02875  173 IIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRG 225
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 404-693 2.27e-23

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 105.43  E-value: 2.27e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  404 VAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNV 483
Cdd:PHA02874   17 IEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSI 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  484 SNVKvetplhmaarAGHTEVAKYLLQNKAKANAKAKDDQTPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAR 563
Cdd:PHA02874   97 LPIP----------CIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIK 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  564 EGHVDTALALLEKEASQACMTKKGFTPLHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNlDIVKLLLpRG 643
Cdd:PHA02874  167 HNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLI-NN 244

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568953835  644 GSPHSPAWNGYTPLHIAAKQN-QIEVARSLLQYGGSANAESVQGVTPLHLA 693
Cdd:PHA02874  245 ASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTA 295
Death_ank2 cd08804
Death domain of Ankyrin-2; Death Domain (DD) of Ankyrin-2 (ANK-2) and related proteins. ...
 1452-1535 2.58e-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: 95.54  E-value: 2.58e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835 1452 DRVEMRMAVIREHLGLSWAELARELQFSVEDINRIRVENPNSLLDQSTALLTLWVDREGENAKMENLYTALRNIDRSEIV 1531
Cdd:cd08804     1 ERTEERLAHIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLTQCLTKINRMDIV 80


                  ....
gi 568953835 1532 NMLE 1535
Cdd:cd08804    81 HLME 84
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 423-726 7.13e-23

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 104.58  E-value: 7.13e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  423 FTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNVSN--VKVETPLHMAaragH 500
Cdd:PHA02878   38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFYtlVAIKDAFNNR----N 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  501 TEVAKYLLQNKAKANAKAKDDQTPLHCAARIGHTGMVKLLLENGASPNLATTaghtplhtaareghvdtalallekeasq 580
Cdd:PHA02878  114 VEIFKIILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDR---------------------------- 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  581 acmtKKGFTPLHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIA 660
Cdd:PHA02878  166 ----HKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIS 241

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568953835  661 AKQ-NQIEVARSLLQYGGSANAES-VQGVTPLHLAAQEghTEMVALLLSKQANGNLGNKSGLTPLHLV 726
Cdd:PHA02878  242 VGYcKDYDILKLLLEHGVDVNAKSyILGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSA 307
Ank_2 pfam12796
Ankyrin repeats (3 copies);
459-549 7.13e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 94.41  E-value: 7.13e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   459 LHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQnkAKANAKAKDDQTPLHCAARIGHTGMVK 538
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE--HADVNLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|.
gi 568953835   539 LLLENGASPNL 549
Cdd:pfam12796   79 LLLEKGADINV 89
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 523-747 7.50e-23

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 103.59  E-value: 7.50e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  523 TPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHV-----DTALALLEKEASQACMTKKGFTPLHVAA-- 595
Cdd:PHA03100   37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAIsk 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  596 KYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVH--HNNLDIVKLLLPRGgsphspawngytplhiaAKQNQIEVARSLL 673
Cdd:PHA03100  117 KSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLEsnKIDLKILKLLIDKG-----------------VDINAKNRVNYLL 179

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568953835  674 QYGGSANAESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADVLIKHGVTVDA 747
Cdd:PHA03100  180 SYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
Ank_2 pfam12796
Ankyrin repeats (3 copies);
100-190 1.44e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 93.64  E-value: 1.44e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   100 LHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQDEVVRELVNYgANVNAQSQkGFTPLYMAAQENHLEVVK 179
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                           90
                   ....*....|.
gi 568953835   180 FLLENGANQNV 190
Cdd:pfam12796   79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
525-615 2.31e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.87  E-value: 2.31e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   525 LHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALLEKEASQacMTKKGFTPLHVAAKYGKVRLAE 604
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN--LKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|.
gi 568953835   605 LLLEHDAHPNA 615
Cdd:pfam12796   79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
393-485 3.48e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.49  E-value: 3.48e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   393 LHVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASidAVTESGLTPLHVASFMGHLPIVK 472
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 568953835   473 NLLQRGASPNVSN 485
Cdd:pfam12796   79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
360-450 4.71e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.10  E-value: 4.71e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   360 IHMAAQGDHLDCVRLLLQYNAEIDDITLDHLTPLHVAAHCGHHRVAKVLLDKgAKPNSRaLNGFTPLHIACKKNHIRVME 439
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLK-DNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|.
gi 568953835   440 LLLKTGASIDA 450
Cdd:pfam12796   79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
327-418 7.01e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 91.72  E-value: 7.01e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   327 LHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQYNAEidDITLDHLTPLHVAAHCGHHRVAK 406
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 568953835   407 VLLDKGAKPNSR 418
Cdd:pfam12796   79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
723-812 8.95e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 91.33  E-value: 8.95e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   723 LHLVSQEGHVPVADVLIKHGVTVDATTRMGYTPLHVASHYGNIKLVKFLLQHqADVNAKTKlGYSPLHQAAQQGHTDIVT 802
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                           90
                   ....*....|
gi 568953835   803 LLLKNGASPN 812
Cdd:pfam12796   79 LLLEKGADIN 88
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 62-332 9.39e-22

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 100.42  E-value: 9.39e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   62 DAATSFLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMV--------------VELLHKEII------ 121
Cdd:PHA02874   34 ETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIkllidngvdtsilpIPCIEKDMIktildc 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  122 ---LETTTKKGNTALHIAALAGQDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTP 198
Cdd:PHA02874  114 gidVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESP 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  199 lavalqqghenvvahlinygtkgkvrlpaLHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYeNLNVAQLLLN 278
Cdd:PHA02874  194 -----------------------------LHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIH-NRSAIELLIN 243

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568953835  279 rGASVNFTPQNGITPLHIASRRG-NVIMVRLLLDRGAQIETRTKDELTPLHCAAR 332
Cdd:PHA02874  244 -NASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAFK 297
Ank_2 pfam12796
Ankyrin repeats (3 copies);
690-781 1.06e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 91.33  E-value: 1.06e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   690 LHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADVLIKHgVTVDATTRmGYTPLHVASHYGNIKLVK 769
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 568953835   770 FLLQHQADVNAK 781
Cdd:pfam12796   79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
591-681 1.31e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.95  E-value: 1.31e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   591 LHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSphSPAWNGYTPLHIAAKQNQIEVAR 670
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|.
gi 568953835   671 SLLQYGGSANA 681
Cdd:pfam12796   79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
261-352 1.50e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.56  E-value: 1.50e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   261 LHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLDRGAQieTRTKDELTPLHCAARNGHVRISE 340
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 568953835   341 ILLDHGAPIQAK 352
Cdd:pfam12796   79 LLLEKGADINVK 90
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
 1451-1537 2.84e-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: 89.78  E-value: 2.84e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   1451 TDRVEMRMAVIREH-LGLSWAELARELQFSVEDINRIRVENPNSLLDQSTALLTLWVDREGENAKMENLYTALRNIDRSE 1529
Cdd:smart00005    1 PELTRQKLAKLLDHpLGLDWRELARKLGLSEADIDQIRTEAPRDLAEQSVQLLRLWEQREGKNATLGTLLEALRKMGRDD 80


                    ....*...
gi 568953835   1530 IVNMLEGS 1537
Cdd:smart00005   81 AVELLRSE 88
Ank_2 pfam12796
Ankyrin repeats (3 copies);
133-220 4.00e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.40  E-value: 4.00e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   133 LHIAALAGQDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENgANQNVaTEDGFTPLAVALQQGHENVVA 212
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNL-KDNGRTALHYAARSGHLEIVK 78


                   ....*...
gi 568953835   213 HLINYGTK 220
Cdd:pfam12796   79 LLLEKGAD 86
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 521-828 4.78e-21

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 98.14  E-value: 4.78e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  521 DQTPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDtALALLEKEASQACMTKKGF-TPLHVAAKYGK 599
Cdd:PHA02875    2 DQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSE-AIKLLMKHGAIPDVKYPDIeSELHDAVEEGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  600 VRLAELLLEHDAHPN-AAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQIEVARSLLQYGGS 678
Cdd:PHA02875   81 VKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKAC 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  679 ANAESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSG-LTPLHLVSQEGHVPVADVLIKHGVTVD-ATTRMG--YT 754
Cdd:PHA02875  161 LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNiMFMIEGeeCT 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568953835  755 PLHVASHYgniklvkfllqhqaDVNAKTklgysplhQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIAKRL 828
Cdd:PHA02875  241 ILDMICNM--------------CTNLES--------EAIDALIADIAIRIHKKTIRRDEGFKNNMSTIEDKEEF 292
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 133-458 8.01e-21

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 98.03  E-value: 8.01e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  133 LHIAALAGQDEVVRELVNYGANVNAQSQKGFTPLYMAAQE-------------------------------NHLEVVKFL 181
Cdd:PHA02878   41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEpnklgmkemirsinkcsvfytlvaikdafnnRNVEIFKII 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  182 LENGANQNVATEDGFTPLAVALQQGHENVVAHLINYGTKGKVRL-----PALHIAARNDDTRTAAVLLQNDPNPDVLSKT 256
Cdd:PHA02878  121 LTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDrhkgnTALHYATENKDQRLTELLLSYGANVNIPDKT 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  257 GFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRgnvimvrlLLDrgaqietrtkdeltplhcaarnghV 336
Cdd:PHA02878  201 NNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGY--------CKD------------------------Y 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  337 RISEILLDHGAPIQAK-TKNGLSPIHMAAQGDhlDCVRLLLQYNAEIDDITLDHLTPLHVAA------HCGHHRVAKVLL 409
Cdd:PHA02878  249 DILKLLLEHGVDVNAKsYILGLTALHSSIKSE--RKLKLLLEYGADINSLNSYKLTPLSSAVkqylciNIGRILISNICL 326

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 568953835  410 DKGAKPNSRALNGFTpLHIACKKNHIRVMELLLKTGASIDAVTESGLTP 458
Cdd:PHA02878  327 LKRIKPDIKNSEGFI-DNMDCITSNKRLNQIKDKCEDELNRLASIKITN 374
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 462-680 1.56e-20

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 96.60  E-value: 1.56e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  462 ASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKAKANAKAKDDQTPLHCAARIGHTGMVKLLL 541
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  542 ENGASPN-LATTAGHTPLHTAAREGHVDTALALLEKEASQACMTKKGFTPLHVAAKYGKVRLAELLLEHDAHPNAAGKNG 620
Cdd:PHA02875   89 DLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCG 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568953835  621 LTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNG-YTPLHIAAKQNQIEVARSLLQYGGSAN 680
Cdd:PHA02875  169 CTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCN 229
Ank_2 pfam12796
Ankyrin repeats (3 copies);
492-579 2.69e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.09  E-value: 2.69e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   492 LHMAARAGHTEVAKYLLQNKAKANAKAKDDQTPLHCAARIGHTGMVKLLLENGASPNlaTTAGHTPLHTAAREGHVDTAL 571
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78


                   ....*...
gi 568953835   572 ALLEKEAS 579
Cdd:pfam12796   79 LLLEKGAD 86
Ank_2 pfam12796
Ankyrin repeats (3 copies);
657-748 3.97e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.71  E-value: 3.97e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   657 LHIAAKQNQIEVARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVALLLSKqANGNLGNKsGLTPLHLVSQEGHVPVAD 736
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 568953835   737 VLIKHGVTVDAT 748
Cdd:pfam12796   79 LLLEKGADINVK 90
Death cd01670
Death Domain: a protein-protein interaction domain; Death Domains (DDs) are protein-protein ...
 1460-1535 4.74e-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: 86.18  E-value: 4.74e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568953835 1460 VIREHLGLSWAELARELQFSVEDINRIRVENPNSLLDQSTALLTLWVDREGENAKMENLYTALRNIDRSEIVNMLE 1535
Cdd:cd01670     4 LVAEELGRDWKKLARKLGLSEGDIDQIEEDNRDDLKEQAYQMLERWREREGDEATLGRLIQALREIGRRDLAEKLE 79
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 359-628 7.89e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 94.95  E-value: 7.89e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  359 PIHMAAQGDHLDCVRLLLQYNAEIDDITLDHLTPLHVAAHCGHHRVAKVLLdkgAKPNSRAL-NGFTPLHIACKKNHIRV 437
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMI---RSINKCSVfYTLVAIKDAFNNRNVEI 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  438 MELLLKTgaSIDAVTESGLTPLHVASFMGHL--PIVKNLLQRGASPN-VSNVKVETPLHMAARAGHTEVAKYLLQNKAKA 514
Cdd:PHA02878  117 FKIILTN--RYKNIQTIDLVYIDKKSKDDIIeaEITKLLLSYGADINmKDRHKGNTALHYATENKDQRLTELLLSYGANV 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  515 NAKAKDDQTPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTA-AREGHVDTALALLEKEAS-QACMTKKGFTPLH 592
Cdd:PHA02878  195 NIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDvNAKSYILGLTALH 274

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 568953835  593 VAAKygKVRLAELLLEHDAHPNAAGKNGLTPLHVAV 628
Cdd:PHA02878  275 SSIK--SERKLKLLLEYGADINSLNSYKLTPLSSAV 308
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 599-825 1.04e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 95.90  E-value: 1.04e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  599 KVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQIEVAR-------- 670
Cdd:PHA02876  157 ELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKaiidnrsn 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  671 -------------------SLLQY--GGSANAESVQGVTPLHLAAQEGH-TEMVALLLSKQANGNLGNKSGLTPLHLVSQ 728
Cdd:PHA02876  237 inkndlsllkairnedletSLLLYdaGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAK 316

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  729 EGH-VPVADVLIKHGVTVDATTRMGYTPLHVASHYGNIK-LVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLK 806
Cdd:PHA02876  317 NGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKdIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLD 396

                         250
                  ....*....|....*....
gi 568953835  807 NGASPNEVSSNGTTPLAIA 825
Cdd:PHA02876  397 YGADIEALSQKIGTALHFA 415
Ank_2 pfam12796
Ankyrin repeats (3 copies);
228-319 1.29e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.17  E-value: 1.29e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   228 LHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTpqNGITPLHIASRRGNVIMVR 307
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD--NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 568953835   308 LLLDRGAQIETR 319
Cdd:pfam12796   79 LLLEKGADINVK 90
Death pfam00531
Death domain;
1455-1535 1.29e-19

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 85.11  E-value: 1.29e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  1455 EMRMAVIREH---LGLSWAELARELQFSVEDINRIRVENPNsLLDQSTALLTLWVDREGENAKMENLYTALRNIDRSEIV 1531
Cdd:pfam00531    1 RKQLDRLLDPpppLGKDWRELARKLGLSENEIDEIESENPR-LRSQTYELLRLWEQREGKNATVGTLLEALRKLGRRDAA 79


                   ....
gi 568953835  1532 NMLE 1535
Cdd:pfam00531   80 EKIQ 83
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 621-840 5.12e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 92.64  E-value: 5.12e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  621 LTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQ-NQI---EVARSLLQYGGSANAESVQGvtplhlAAQE 696
Cdd:PHA02878   38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEpNKLgmkEMIRSINKCSVFYTLVAIKD------AFNN 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  697 GHTEMVALLLSKQANGNlgNKSGLTPLHLVSQEGHV--PVADVLIKHGVTVDATTR-MGYTPLHVASHYGNIKLVKFLLQ 773
Cdd:PHA02878  112 RNVEIFKIILTNRYKNI--QTIDLVYIDKKSKDDIIeaEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLS 189

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568953835  774 HQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIAkrLGYISVTDVLKVV 840
Cdd:PHA02878  190 YGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIS--VGYCKDYDILKLL 254
Ank_2 pfam12796
Ankyrin repeats (3 copies);
426-509 7.73e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.86  E-value: 7.73e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   426 LHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRgASPNVSNVKvETPLHMAARAGHTEVAK 505
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG-RTALHYAARSGHLEIVK 78


                   ....
gi 568953835   506 YLLQ 509
Cdd:pfam12796   79 LLLE 82
PHA03095 PHA03095
ankyrin-like protein; Provisional
 700-824 3.20e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 90.08  E-value: 3.20e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  700 EMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADV---LIKHGVTVDATTRMGYTPLHVASHYGN-IKLVKFLLQHQ 775
Cdd:PHA03095   28 EEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAG 107

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568953835  776 ADVNAKTKLGYSPLHQ--AAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAI 824
Cdd:PHA03095  108 ADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAV 158
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 70-314 3.78e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 89.28  E-value: 3.78e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   70 AARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQDEVVRELV 149
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  150 NYGANVN-AQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPlavalqqghenvvahlinygtkgkvrlpaL 228
Cdd:PHA02875   89 DLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSP-----------------------------L 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  229 HIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNG-ITPLHIASRRGNVIMVR 307
Cdd:PHA02875  140 HLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVR 219


                  ....*..
gi 568953835  308 LLLDRGA 314
Cdd:PHA02875  220 LFIKRGA 226
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 369-584 7.25e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 88.51  E-value: 7.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  369 LDCVRLLLQYNAEIDDITLDHLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASI 448
Cdd:PHA02875   15 LDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  449 DAVT-ESGLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKAKANAKAKDDQTPLHC 527
Cdd:PHA02875   95 DDVFyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLII 174

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568953835  528 AARIGHTGMVKLLLENGASPNLATTAGH-TPLHTAAREGHVDTALALLEKEASQACMT 584
Cdd:PHA02875  175 AMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADCNIMF 232
Ank_2 pfam12796
Ankyrin repeats (3 copies);
67-158 8.56e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.16  E-value: 8.56e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835    67 FLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMvVELLHKEIILETTTkKGNTALHIAALAGQDEVVR 146
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEI-VKLLLEHADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 568953835   147 ELVNYGANVNAQ 158
Cdd:pfam12796   79 LLLEKGADINVK 90
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 556-732 3.18e-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: 3.18e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  556 TPLHTAAREGHVDTALALLEKEASQACMTKK-GFTPLHVAAKYGKVRLAELLLEhdAHPNAAGK-------NGLTPLHVA 627
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGAlGETALHVAALYDNLEAAVVLME--AAPELVNEpmtsdlyQGETALHIA 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  628 VHHNNLDIVKLLLPRGG--------------SPHSPAWNGYTPLHIAAKQNQIEVARSLLQYGGSANAESVQGVTPLH-L 692
Cdd:cd22192    97 VVNQNLNLVRELIARGAdvvspratgtffrpGPKNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHiL 176

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 568953835  693 AAQEGHT---EMVALLLSKQANGNLG------NKSGLTPLHLVSQEGHV 732
Cdd:cd22192   177 VLQPNKTfacQMYDLILSYDKEDDLQpldlvpNNQGLTPFKLAAKEGNI 225
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 664-837 3.32e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 86.20  E-value: 3.32e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  664 NQIEVARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADVLIKHGV 743
Cdd:PHA02875   13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  744 TV-DATTRMGYTPLHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPL 822
Cdd:PHA02875   93 FAdDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPL 172

                         170
                  ....*....|....*
gi 568953835  823 AIAKRLGYISVTDVL 837
Cdd:PHA02875  173 IIAMAKGDIAICKML 187
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 523-709 5.20e-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: 5.20e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  523 TPLHCAARIGHTGMVKLLLENGASPNLATTA-GHTPLHTAAREGHVDTALALLE--KEASQACMTK---KGFTPLHVAAK 596
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGAlGETALHVAALYDNLEAAVVLMEaaPELVNEPMTSdlyQGETALHIAVV 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  597 YGKVRLAELLLEHDA---HPNAAG-------KN----GLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAK 662
Cdd:cd22192    99 NQNLNLVRELIARGAdvvSPRATGtffrpgpKNliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVL 178

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568953835  663 QNQIEVARS----LLQYGGSANAESV------QGVTPLHLAAQEGHTEMVALLLSKQ 709
Cdd:cd22192   179 QPNKTFACQmydlILSYDKEDDLQPLdlvpnnQGLTPFKLAAKEGNIVMFQHLVQKR 235
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 228-397 8.58e-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: 8.58e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  228 LHIAARNDDTRTAAVLLQNdPNPDVLSK--TGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQN-----GITPLHIASRR 300
Cdd:cd22192    21 LLLAAKENDVQAIKKLLKC-PSCDLFQRgaLGETALHVAALYDNLEAAVVLMEAAPELVNEPMTsdlyqGETALHIAVVN 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  301 GNVIMVRLLLDRGAQIET---------RTKDELT-----PLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAA-- 364
Cdd:cd22192   100 QNLNLVRELIARGADVVSpratgtffrPGPKNLIyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVlq 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 568953835  365 QGDHLDC--VRLLLQYNAEIDDITLDH------LTPLHVAA 397
Cdd:cd22192   180 PNKTFACqmYDLILSYDKEDDLQPLDLvpnnqgLTPFKLAA 220
Ank_2 pfam12796
Ankyrin repeats (3 copies);
756-837 9.11e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.08  E-value: 9.11e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   756 LHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASpnEVSSNGTTPLAIAKRLGYISVTD 835
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78


                   ..
gi 568953835   836 VL 837
Cdd:pfam12796   79 LL 80
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 662-828 2.53e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 78.57  E-value: 2.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  662 KQNQIEVARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADVLIKH 741
Cdd:PHA02876  154 QQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDN 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  742 -----------------------------GVTVDATTRMGYTPLHVASHYGNI-KLVKFLLQHQADVNAKTKLGYSPLHQ 791
Cdd:PHA02876  234 rsninkndlsllkairnedletslllydaGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYL 313

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 568953835  792 AAQQGH-TDIVTLLLKNGASPNEVSSNGTTPLAIAKRL 828
Cdd:PHA02876  314 MAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTL 351
Death_FADD cd08306
Fas-associated Death Domain protein-protein interaction domain; Death domain (DD) found in ...
 1460-1523 8.12e-13

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: 65.78  E-value: 8.12e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568953835 1460 VIREHLGLSWAELARELQFSVEDINRIRVENPNSLLDQSTALLTLWVDREGENAKMENLYTALR 1523
Cdd:cd08306     7 VICENLGRDWRQLARKLGLSETKIESISEAHPRNLREQVRQSLREWKKIKKAEATVADLIKALR 70
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 128-279 8.72e-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: 8.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  128 KGNTALHIAALAGQDEVVRELVNYGANVNAQSQKGF--------------TPLYMAAQENHLEVVKFLLENGANqNVATE 193
Cdd:cd22194   140 EGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVFfnpkykhegfyfgeTPLALAACTNQPEIVQLLMEKEST-DITSQ 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  194 DGFTplavalqqgheNVVAHlinygtkgkvrlpALHIAARNDDTRTAAV------LLQNDPNPD---VLSKTGFTPLHIA 264
Cdd:cd22194   219 DSRG-----------NTVLH-------------ALVTVAEDSKTQNDFVkrmydmILLKSENKNletIRNNEGLTPLQLA 274

                         170
                  ....*....|....*
gi 568953835  265 AHYENLNVAQLLLNR 279
Cdd:cd22194   275 AKMGKAEILKYILSR 289
Ank_4 pfam13637
Ankyrin repeats (many copies);
589-640 2.12e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 63.45  E-value: 2.12e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568953835   589 TPLHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLL 640
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
752-805 4.33e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 62.68  E-value: 4.33e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 568953835   752 GYTPLHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLL 805
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02946 PHA02946
ankyin-like protein; Provisional
 601-843 9.68e-12

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 69.31  E-value: 9.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  601 RLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQ--IEVARSLLQYGGS 678
Cdd:PHA02946   53 RFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAK 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  679 A-NAESVQGVTPLhLAAQEGHTEMVALLLSKQANGNLGNKSGLTPL--HLVSQEGHVPVADVLIKHGVTVDATTRMGYTP 755
Cdd:PHA02946  133 InNSVDEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFGKNHIhrHLMSDNPKASTISWMMKLGISPSKPDHDGNTP 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  756 LHV--ASHYGNIKLVKFLLQhQADVNAKTKLGYSPLhqaaqqghtdivTLLLKNGASPNEVSSNGTTPLAIAKRLGYISV 833
Cdd:PHA02946  212 LHIvcSKTVKNVDIINLLLP-STDVNKQNKFGDSPL------------TLLIKTLSPAHLINKLLSTSNVITDQTVNICI 278

                         250
                  ....*....|....
gi 568953835  834 ----TDVLKVVTDE 843
Cdd:PHA02946  279 fydrDDVLEIINDK 292
Ank_4 pfam13637
Ankyrin repeats (many copies);
455-508 1.11e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 61.52  E-value: 1.11e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 568953835   455 GLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLL 508
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
129-182 1.59e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 60.75  E-value: 1.59e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 568953835   129 GNTALHIAALAGQDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLL 182
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 688-824 2.39e-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: 2.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  688 TPLHLAAQEGHTEMVA-LLLSKQAN----GNLGNksglTPLHLVSQEGHVPVADVLIKHG---VTVDATTRM--GYTPLH 757
Cdd:cd22192    19 SPLLLAAKENDVQAIKkLLKCPSCDlfqrGALGE----TALHVAALYDNLEAAVVLMEAApelVNEPMTSDLyqGETALH 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  758 VASHYGNIKLVKFLLQHQADV------------NAKTKLGYS--PLHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLA 823
Cdd:cd22192    95 IAVVNQNLNLVRELIARGADVvspratgtffrpGPKNLIYYGehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174


                  .
gi 568953835  824 I 824
Cdd:cd22192   175 I 175
Ank_4 pfam13637
Ankyrin repeats (many copies);
424-475 2.51e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 60.37  E-value: 2.51e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568953835   424 TPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLL 475
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 528-711 2.97e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 68.74  E-value: 2.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  528 AARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALLEkeasQACmtkkgftPLHVaakygkvrlaelll 607
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLK----HAC-------NVHI-------------- 586

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  608 eHDAHPNAAGKNGLTplhvAVHHNNLDIVkLLLPRGGSPHSpawnGYTPLHIAAKQNQIEVARSLLQYGGSANAESVQGV 687
Cdd:PLN03192  587 -RDANGNTALWNAIS----AKHHKIFRIL-YHFASISDPHA----AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGA 656

                         170       180
                  ....*....|....*....|....
gi 568953835  688 TPLHLAAQEGHTEMVALLLSKQAN 711
Cdd:PLN03192  657 TALQVAMAEDHVDMVRLLIMNGAD 680
Ank_4 pfam13637
Ankyrin repeats (many copies);
389-442 5.28e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.60  E-value: 5.28e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 568953835   389 HLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLL 442
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 271-542 5.42e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 67.46  E-value: 5.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  271 NVAQLLLNRGASVNFTPQ-NGITPLHIASRRGNVIMVRLLLDRGAQIETRTKDElTPLHCAARNGHV------RISEILL 343
Cdd:PHA02989   17 NALEFLLRTGFDVNEEYRgNSILLLYLKRKDVKIKIVKLLIDNGADVNYKGYIE-TPLCAVLRNREItsnkikKIVKLLL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  344 DHGAPIQAKTKNGLSPIHMAAQGDH---LDCVRLLLQYNAEIDDI-TLDHLTPLHVAAHCGHHR--VAKVLLDKGAKP-N 416
Cdd:PHA02989   96 KFGADINLKTFNGVSPIVCFIYNSNinnCDMLRFLLSKGINVNDVkNSRGYNLLHMYLESFSVKkdVIKILLSFGVNLfE 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  417 SRALNGFTPLHIACKKN----HIRVMELLLKTGASI---DAVTESGLTplhvaSFMGHLPI-------VKNLLQRGASPN 482
Cdd:PHA02989  176 KTSLYGLTPMNIYLRNDidviSIKVIKYLIKKGVNIetnNNGSESVLE-----SFLDNNKIlskkefkVLNFILKYIKIN 250

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  483 VSNVKVETPLHMAARAGHTEVAKYLLQNKAKANAKAKDDQTPLHCAARIGHTGMVKLLLE 542
Cdd:PHA02989  251 KKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNRILQ 310
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 61-204 5.60e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 66.91  E-value: 5.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   61 ADAATSFLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAG 140
Cdd:PHA02874  122 AELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYG 201

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568953835  141 QDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHlEVVKFLLENgANQNVATEDGFTPLAVALQ 204
Cdd:PHA02874  202 DYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLINN-ASINDQDIDGSTPLHHAIN 263
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 625-815 6.76e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 67.59  E-value: 6.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  625 HVAVHhnNLDIVKLLLPRGGSpHSPAWNGYTPLHIAAKQNQiEVARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVAL 704
Cdd:PLN03192  501 HKELH--DLNVGDLLGDNGGE-HDDPNMASNLLTVASTGNA-ALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLV 576

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  705 LLSKQANGNLGNKSGLTPLHLVSQEGHVPVADVLIKHGVTVDATTrmGYTPLHVASHYGNIKLVKFLLQHQADVNAKTKL 784
Cdd:PLN03192  577 LLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHA--AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQ 654

                         170       180       190
                  ....*....|....*....|....*....|.
gi 568953835  785 GYSPLHQAAQQGHTDIVTLLLKNGASPNEVS 815
Cdd:PLN03192  655 GATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
Ank_4 pfam13637
Ankyrin repeats (many copies);
259-310 1.01e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.83  E-value: 1.01e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568953835   259 TPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLL 310
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
323-376 1.50e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.05  E-value: 1.50e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 568953835   323 ELTPLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLL 376
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 75-220 1.55e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 66.24  E-value: 1.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   75 NLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIaALAGQDEV--VRELVNYG 152
Cdd:PHA02876  354 NKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHF-ALCGTNPYmsVKTLIDRG 432

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568953835  153 ANVNAQSQKGFTPLYMAAQEN-HLEVVKFLLENGANQNVATEDGFTPLAVALqqGHENVVAHLINYGTK 220
Cdd:PHA02876  433 ANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGAE 499
Ank_4 pfam13637
Ankyrin repeats (many copies);
356-409 1.66e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.05  E-value: 1.66e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 568953835   356 GLSPIHMAAQGDHLDCVRLLLQYNAEIDDITLDHLTPLHVAAHCGHHRVAKVLL 409
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 424-607 2.91e-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: 2.91e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  424 TPLHIACKKNHIRVMELLLKTgASIDAVTESGL--TPLHVASFMGHLPIVKNLLQrgASPNVSNVKV-------ETPLHM 494
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKC-PSCDLFQRGALgeTALHVAALYDNLEAAVVLME--AAPELVNEPMtsdlyqgETALHI 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  495 AARAGHTEVAKYLLQNKAkanakakDDQTP---------------------LHCAARIGHTGMVKLLLENGASPNLATTA 553
Cdd:cd22192    96 AVVNQNLNLVRELIARGA-------DVVSPratgtffrpgpknliyygehpLSFAACVGNEEIVRLLIEHGADIRAQDSL 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568953835  554 GHTPLH------TAAREGHVDTALALLEKEASQACM----TKKGFTPLHVAAKYGKVRLAELLL 607
Cdd:cd22192   169 GNTVLHilvlqpNKTFACQMYDLILSYDKEDDLQPLdlvpNNQGLTPFKLAAKEGNIVMFQHLV 232
Ank_4 pfam13637
Ankyrin repeats (many copies);
490-541 3.19e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 57.28  E-value: 3.19e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568953835   490 TPLHMAARAGHTEVAKYLLQNKAKANAKAKDDQTPLHCAARIGHTGMVKLLL 541
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 100-312 3.51e-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: 3.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  100 LHLASKEGHVKMVVELL-HKEIILETTTKKGNTALHIAALAGQDEV-------VRELVNygANVNAQSQKGFTPLYMAAQ 171
Cdd:cd22192    21 LLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAavvlmeaAPELVN--EPMTSDLYQGETALHIAVV 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  172 ENHLEVVKFLLENGANQNVATEDG--FT------------PLAVALQQGHENVVAHLINYGTkgkvrlpalhiAARNDDT 237
Cdd:cd22192    99 NQNLNLVRELIARGADVVSPRATGtfFRpgpknliyygehPLSFAACVGNEEIVRLLIEHGA-----------DIRAQDS 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  238 RtaavllqndpnpdvlsktGFTPLHIAAHYENLNVA----QLLLNRGASVNFTP------QNGITPLHIASRRGNVIMVR 307
Cdd:cd22192   168 L------------------GNTVLHILVLQPNKTFAcqmyDLILSYDKEDDLQPldlvpnNQGLTPFKLAAKEGNIVMFQ 229


                  ....*
gi 568953835  308 LLLDR 312
Cdd:cd22192   230 HLVQK 234
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 64-218 4.33e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 64.89  E-value: 4.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   64 ATSFLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQDE 143
Cdd:PLN03192  526 ASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHK 605

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568953835  144 VVRELVNYGANVNAQSqkGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLINYG 218
Cdd:PLN03192  606 IFRILYHFASISDPHA--AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNG 678
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 330-485 4.56e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 64.89  E-value: 4.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  330 AARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQY--NAEIDDITLDhlTPLHVAAHCGHHRVAKV 407
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHacNVHIRDANGN--TALWNAISAKHHKIFRI 609

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568953835  408 LLDKGAKPNSRAlnGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNVSN 485
Cdd:PLN03192  610 LYHFASISDPHA--AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
PHA02798 PHA02798
ankyrin-like protein; Provisional
 249-495 7.64e-10

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 63.70  E-value: 7.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  249 NPDVLSKTgFTPLHIAAHYEN--LNVAQLLLNRGASVNFTPQNGITPL-----HIASRRGNVIMVRLLLDRGAQIETRTK 321
Cdd:PHA02798   29 NPNEIVNE-YSIFQKYLQRDSpsTDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNS 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  322 DELTPLHCAARNGHVRISEILL---DHGAPIQAKTKNGLSPIHMAAQGDH---LDCVRLLLQYNAEIDDIT-LDHLTPLH 394
Cdd:PHA02798  108 DGETPLYCLLSNGYINNLEILLfmiENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINTHNnKEKYDTLH 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  395 VAAHCGHHR----VAKVLLDKG---AKPN----SRALNGFTPLHIACKKNHIRVMELLLKTgASIDAVTESGLTPLHVAS 463
Cdd:PHA02798  188 CYFKYNIDRidadILKLFVDNGfiiNKENkshkKKFMEYLNSLLYDNKRFKKNILDFIFSY-IDINQVDELGFNPLYYSV 266

                         250       260       270
                  ....*....|....*....|....*....|..
gi 568953835  464 FMGHLPIVKNLLQRGASPNVSNVKVETPLHMA 495
Cdd:PHA02798  267 SHNNRKIFEYLLQLGGDINIITELGNTCLFTA 298
Ank_4 pfam13637
Ankyrin repeats (many copies);
653-706 1.06e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.74  E-value: 1.06e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 568953835   653 GYTPLHIAAKQNQIEVARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVALLL 706
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 143-486 1.11e-09

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 63.39  E-value: 1.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  143 EVVRELVNYGANVNAQSQKGFTPL--YMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGhENVVAHLINY--- 217
Cdd:PHA02716  193 DILEWLCNNGVNVNLQNNHLITPLhtYLITGNVCASVIKKIIELGGDMDMKCVNGMSPIMTYIINI-DNINPEITNIyie 271

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  218 ---GTKGKVRLPALHI---AARNDDTRTAAVLLQNDPNPDVLSKTGFTPLH--IAAHYENLNVAQLLLNRGASVNFTPQN 289
Cdd:PHA02716  272 sldGNKVKNIPMILHSyitLARNIDISVVYSFLQPGVKLHYKDSAGRTCLHqyILRHNISTDIIKLLHEYGNDLNEPDNI 351

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  290 GITPLHIASRRGNVI--------------MVRLLLDRGAQIETRTKDELTPLH---CAARN-GHVRISEILldhgapIQA 351
Cdd:PHA02716  352 GNTVLHTYLSMLSVVnildpetdndirldVIQCLISLGADITAVNCLGYTPLTsyiCTAQNyMYYDIIDCL------ISD 425

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  352 KTKNGLSpiHMAAQG-----DHLDCV--RLLLQYNAEIDDITLDH----LTPLHVAAHCGhhrvakvlLDKGAKPNSRAL 420
Cdd:PHA02716  426 KVLNMVK--HRILQDllirvDDTPCIihHIIAKYNIPTDLYTDEYepydSTKIHDVYHCA--------IIERYNNAVCET 495

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568953835  421 NGFTPLHIA--CKKNHIRVME---LLLKTGASIDAVTESGLTPLHVA----SFMGHLP-IVKNLLQRgaSPNVSNV 486
Cdd:PHA02716  496 SGMTPLHVSiiSHTNANIVMDsfvYLLSIQYNINIPTKNGVTPLMLTmrnnRLSGHQWyIVKNILDK--RPNVDIV 569
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 157-377 1.34e-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: 1.34e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   157 AQSQKGFTPlymAAQENHLEVVKFLLENGA--NQNVATEDGFTPLAVALQQG-HENVVAHLINYGTKGKVRLPALHIAAR 233
Cdd:TIGR00870   15 SDEEKAFLP---AAERGDLASVYRDLEEPKklNINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAVGDTLLHAISL 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   234 ND--------------DTRTAAVLLQNDPNPDVLSKtGFTPLHIAAHYENLNVAQLLLNRGASVN-------FTPQNGIT 292
Cdd:TIGR00870   92 EYvdaveaillhllaaFRKSGPLELANDQYTSEFTP-GITALHLAAHRQNYEIVKLLLERGASVParacgdfFVKSQGVD 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   293 -------PLHIASRRGNVIMVRLLLDRGAQIETRtkDEL--TPLHCA-------ARNGHVRIS--EILLDHGAPIQAKTK 354
Cdd:TIGR00870  171 sfyhgesPLNAAACLGSPSIVALLSEDPADILTA--DSLgnTLLHLLvmenefkAEYEELSCQmyNFALSLLDKLRDSKE 248

                          250       260       270
                   ....*....|....*....|....*....|
gi 568953835   355 -------NGLSPIHMAAQGDHLDCVRLLLQ 377
Cdd:TIGR00870  249 levilnhQGLTPLKLAAKEGRIVLFRLKLA 278
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 284-381 1.57e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 62.99  E-value: 1.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  284 NFTPQNGITP--LHIAS-------RRGNVIMVRLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILLDHGAPIQAKTK 354
Cdd:PTZ00322   67 NLTTEEVIDPvvAHMLTvelcqlaASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDK 146

                          90       100
                  ....*....|....*....|....*..
gi 568953835  355 NGLSPIHMAAQGDHLDCVRLLLQYNAE 381
Cdd:PTZ00322  147 DGKTPLELAEENGFREVVQLLSRHSQC 173
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 589-825 1.94e-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: 1.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  589 TPLHVAAKYGKVR-LAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLprggsphspawngytplhiaakqnqiE 667
Cdd:cd22192    19 SPLLLAAKENDVQaIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLM--------------------------E 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  668 VARSLLQYggSANAESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTplhlvsqegHVPVADVLIKHGvtvda 747
Cdd:cd22192    73 AAPELVNE--PMTSDLYQGETALHIAVVNQNLNLVRELIARGADVVSPRATGTF---------FRPGPKNLIYYG----- 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  748 ttrmgYTPLHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVT----LLL-----KNGASPNEVSSN- 817
Cdd:cd22192   137 -----EHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFACqmydLILsydkeDDLQPLDLVPNNq 211


                  ....*...
gi 568953835  818 GTTPLAIA 825
Cdd:cd22192   212 GLTPFKLA 219
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 68-279 2.15e-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: 2.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   68 LRAARSGNLDkALDHLRNGVDINTCnQNGLNG---LHLASKEGHVKMVVELLH--KEIILETTTK---KGNTALHIAALA 139
Cdd:cd22192    22 LLAAKENDVQ-AIKKLLKCPSCDLF-QRGALGetaLHVAALYDNLEAAVVLMEaaPELVNEPMTSdlyQGETALHIAVVN 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  140 GQDEVVRELVNYGANVNAQSQKG--FT------------PLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQ 205
Cdd:cd22192   100 QNLNLVRELIARGADVVSPRATGtfFRpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQ 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  206 GHENVVAHLINygtkgkvrlpalhiaarnddtrtaaVLLQNDPNPD------VLSKTGFTPLHIAAHYENLNVAQLLLNR 279
Cdd:cd22192   180 PNKTFACQMYD-------------------------LILSYDKEDDlqpldlVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
Ank_4 pfam13637
Ankyrin repeats (many copies);
292-343 2.69e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.59  E-value: 2.69e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568953835   292 TPLHIASRRGNVIMVRLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILL 343
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 554-712 3.60e-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: 3.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  554 GHTPLHTAA---REGHVDTALALLE--------KEASQACMTK---KGFTPLHVAAKYGKVRLAELLLEH--DAHPNAAG 617
Cdd:cd21882    26 GKTCLHKAAlnlNDGVNEAIMLLLEaapdsgnpKELVNAPCTDefyQGQTALHIAIENRNLNLVRLLVENgaDVSARATG 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  618 KN-----------GLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWN---GYTPLHIAAKQNQIEVARS---------LLQ 674
Cdd:cd21882   106 RFfrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPAALEAQdslGNTVLHALVLQADNTPENSafvcqmynlLLS 185

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 568953835  675 YGGSANA----ESV---QGVTPLHLAAQEGHTEMVALLLSKQANG 712
Cdd:cd21882   186 YGAHLDPtqqlEEIpnhQGLTPLKLAAVEGKIVMFQHILQREFSG 230
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 664-826 4.08e-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: 4.08e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   664 NQIEVARSLLQYGGSANAESVQ-------GVTPLHLAAQEG-HTEMVALLLSKQANGNLGNksglTPLHLVSQEGHVPVA 735
Cdd:TIGR00870   23 PAAERGDLASVYRDLEEPKKLNincpdrlGRSALFVAAIENeNLELTELLLNLSCRGAVGD----TLLHAISLEYVDAVE 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   736 DVLI-------KHGVTVDATTRM------GYTPLHVASHYGNIKLVKFLLQHQADVNAKTK--------------LGYSP 788
Cdd:TIGR00870   99 AILLhllaafrKSGPLELANDQYtseftpGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESP 178

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 568953835   789 LHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIAK 826
Cdd:TIGR00870  179 LNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLV 216
Ank_5 pfam13857
Ankyrin repeats (many copies);
408-462 5.00e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 53.89  E-value: 5.00e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 568953835   408 LLDKG-AKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVA 462
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 224-345 5.54e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 61.07  E-value: 5.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  224 RLPALHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNvAQLLLNRGASVNFTPQNGITPLHIASRRGNV 303
Cdd:PTZ00322   50 HLEALEATENKDATPDHNLTTEEVIDPVVAHMLTVELCQLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHV 128

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 568953835  304 IMVRLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILLDH 345
Cdd:PTZ00322  129 QVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 587-790 5.62e-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: 5.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  587 GFTPLHVAAKY---GKVRLAELLLEHDAHPNAAGK-----------NGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPA-- 650
Cdd:cd21882    26 GKTCLHKAALNlndGVNEAIMLLLEAAPDSGNPKElvnapctdefyQGQTALHIAIENRNLNLVRLLVENGADVSARAtg 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  651 -----------WNGYTPLHIAAKQNQIEVARSLLQYGGSANAESVQ---GVTPLH-LAAQEGHTEMVALLLSKQANGNLG 715
Cdd:cd21882   106 rffrkspgnlfYFGELPLSLAACTNQEEIVRLLLENGAQPAALEAQdslGNTVLHaLVLQADNTPENSAFVCQMYNLLLS 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  716 NKSGLTPLhlvsqeghVPVADVlikhgvtvdaTTRMGYTPLHVASHYGNIKLVKFLLQHQADVNAK------TKLGYSPL 789
Cdd:cd21882   186 YGAHLDPT--------QQLEEI----------PNHQGLTPLKLAAVEGKIVMFQHILQREFSGPYQplsrkfTEWTYGPV 247


                  .
gi 568953835  790 H 790
Cdd:cd21882   248 T 248
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 438-591 6.54e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 61.04  E-value: 6.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  438 MELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKAKANAK 517
Cdd:PLN03192  541 LEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPH 620

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568953835  518 AKDDqtpLHC-AARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALLEKEASQACM-TKKGFTPL 591
Cdd:PLN03192  621 AAGD---LLCtAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAnTDDDFSPT 693
PHA02798 PHA02798
ankyrin-like protein; Provisional
 143-386 7.40e-09

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 60.62  E-value: 7.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  143 EVVRELVNYGANVNAQSQKGFTPL-----YMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLIny 217
Cdd:PHA02798   52 DIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILL-- 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  218 gtkgkvrlpalhiaarnddtrtaaVLLQNDPNPDVLSKTGFTPLHI---AAHYENLNVAQLLLNRGASVN-FTPQNGITP 293
Cdd:PHA02798  130 ------------------------FMIENGADTTLLDKDGFTMLQVylqSNHHIDIEIIKLLLEKGVDINtHNNKEKYDT 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  294 LHIASR----RGNVIMVRLLLDRGAQIETRTK-------DELTPLHCAARNGHVRISEILLDHgAPIQAKTKNGLSPIHM 362
Cdd:PHA02798  186 LHCYFKynidRIDADILKLFVDNGFIINKENKshkkkfmEYLNSLLYDNKRFKKNILDFIFSY-IDINQVDELGFNPLYY 264

                         250       260
                  ....*....|....*....|....
gi 568953835  363 AAQGDHLDCVRLLLQYNAEIDDIT 386
Cdd:PHA02798  265 SVSHNNRKIFEYLLQLGGDINIIT 288
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 405-475 8.27e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 60.68  E-value: 8.27e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568953835  405 AKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLL 475
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 243-388 8.73e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 60.65  E-value: 8.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  243 LLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLDRGAQIETRTKD 322
Cdd:PLN03192  544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAG 623

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568953835  323 ELtpLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQYNAEIDDITLD 388
Cdd:PLN03192  624 DL--LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTD 687
Ank_4 pfam13637
Ankyrin repeats (many copies);
686-739 9.34e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.05  E-value: 9.34e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 568953835   686 GVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADVLI 739
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 532-620 9.98e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 60.30  E-value: 9.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  532 GHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALLEKEASQACMTKKGFTPLHVAAKYGKVRLAELLLEHDA 611
Cdd:PTZ00322   93 GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQ 172


                  ....*....
gi 568953835  612 HPNAAGKNG 620
Cdd:PTZ00322  173 CHFELGANA 181
Ank_4 pfam13637
Ankyrin repeats (many copies);
719-772 1.05e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.05  E-value: 1.05e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 568953835   719 GLTPLHLVSQEGHVPVADVLIKHGVTVDATTRMGYTPLHVASHYGNIKLVKFLL 772
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Death_NMPP84 cd08318
Death domain of Nuclear Matrix Protein P84; Death domain (DD) found in the Nuclear Matrix ...
 1457-1534 1.18e-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: 54.06  E-value: 1.18e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568953835 1457 RMAVIREHLGLSWAELARELQFSVEDINRIRvENPNSLLDQSTALLTLWVDREGENAKMENLYTALRNIDRSEIVNML 1534
Cdd:cd08318     9 QIDVLANKLGEQWKTLAPYLEMKDKDIRQIE-SDSEDMKMRAKQLLVTWQDREGAQATPEILMTALNAAGLNEIAENL 85
PHA02946 PHA02946
ankyin-like protein; Provisional
 110-294 1.30e-08

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 59.68  E-value: 1.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  110 KMVVELLHKEIILETTTKKGNTALHIAALAGQDEVVRELVNYGANVNAQSQKGFTPLYM--AAQENHLEVVKFLLENGAN 187
Cdd:PHA02946   53 RFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYlsGTDDEVIERINLLVQYGAK 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  188 -QNVATEDGFTPLaVALQQGHENVVAHLINYGTKGKV------RLPALHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTP 260
Cdd:PHA02946  133 iNNSVDEEGCGPL-LACTDPSERVFKKIMSIGFEARIvdkfgkNHIHRHLMSDNPKASTISWMMKLGISPSKPDHDGNTP 211

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 568953835  261 LHI--AAHYENLNVAQLLLnrgASVNFTPQN--GITPL 294
Cdd:PHA02946  212 LHIvcSKTVKNVDIINLLL---PSTDVNKQNkfGDSPL 246
Ank_5 pfam13857
Ankyrin repeats (many copies);
771-825 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 568953835   771 LLQH-QADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIA 825
Cdd:pfam13857    1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
164-215 1.41e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.66  E-value: 1.41e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568953835   164 TPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLI 215
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
523-574 2.08e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 2.08e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568953835   523 TPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALL 574
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
224-277 2.39e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.89  E-value: 2.39e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 568953835   224 RLPALHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLL 277
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 86-205 2.90e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 58.35  E-value: 2.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   86 GVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQD-EVVRELVNYGANVNAQSQ-KGF 163
Cdd:PHA02878  191 GANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDyDILKLLLEHGVDVNAKSYiLGL 270

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 568953835  164 TPLYMAAQENhlEVVKFLLENGANQNVATEDGFTPLAVALQQ 205
Cdd:PHA02878  271 TALHSSIKSE--RKLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 62-192 2.97e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.08  E-value: 2.97e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   62 DAATSFLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQ 141
Cdd:PHA02875  101 DGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGD 180

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568953835  142 DEVVRELVNYGANVNAQSQKG-FTPLYMAAQENHLEVVKFLLENGANQNVAT 192
Cdd:PHA02875  181 IAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNIMF 232
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 136-283 4.23e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 58.34  E-value: 4.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  136 AALAGQDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENV----- 210
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIfrily 611

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568953835  211 -VAHLINYGTKGKVrlpaLHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASV 283
Cdd:PLN03192  612 hFASISDPHAAGDL----LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 528-696 4.37e-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: 4.37e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   528 AARIGHTGMVKLLLENGAS--PNLATTAGHTPLHTAAREGHVDTALALLEKEASQACMtkkGFTPLHVAAKyGKVRLAEL 605
Cdd:TIGR00870   24 AAERGDLASVYRDLEEPKKlnINCPDRLGRSALFVAAIENENLELTELLLNLSCRGAV---GDTLLHAISL-EYVDAVEA 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   606 LLEH--DAHP--------NAAGKN----GLTPLHVAVHHNNLDIVKLLLPRGG-------------SPHSP-AWNGYTPL 657
Cdd:TIGR00870  100 ILLHllAAFRksgplelaNDQYTSeftpGITALHLAAHRQNYEIVKLLLERGAsvparacgdffvkSQGVDsFYHGESPL 179

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 568953835   658 HIAAKQNQIEVARSLLQYGGSANAESVQGVTPLHLAAQE 696
Cdd:TIGR00870  180 NAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVME 218
Ank_5 pfam13857
Ankyrin repeats (many copies);
148-202 6.20e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.81  E-value: 6.20e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 568953835   148 LVNYG-ANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVA 202
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
738-792 7.84e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.42  E-value: 7.84e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 568953835   738 LIKHG-VTVDATTRMGYTPLHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQA 792
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02798 PHA02798
ankyrin-like protein; Provisional
 143-385 8.32e-08

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 57.15  E-value: 8.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  143 EVVRELVNYGANVNAQSQKGFTPLYMAAQE---NHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHenvvahlinygt 219
Cdd:PHA02798   90 DIVKILIENGADINKKNSDGETPLYCLLSNgyiNNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNH------------ 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  220 kgkvrlpalHIaarndDTRTAAVLLQNDPNPDVLS-KTGFTPLHIAAHYE----NLNVAQLLLNRGASVN----FTPQNG 290
Cdd:PHA02798  158 ---------HI-----DIEIIKLLLEKGVDINTHNnKEKYDTLHCYFKYNidriDADILKLFVDNGFIINkenkSHKKKF 223

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  291 I---TPLHIASRRGNVIMVRLLLdrgAQIETRTKDEL--TPLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQ 365
Cdd:PHA02798  224 MeylNSLLYDNKRFKKNILDFIF---SYIDINQVDELgfNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFE 300

                         250       260
                  ....*....|....*....|
gi 568953835  366 GDHLDCVRLLLQYNAEIDDI 385
Cdd:PHA02798  301 NESKFIFNSILNKKPNKNTI 320
Ank_5 pfam13857
Ankyrin repeats (many copies);
275-330 8.56e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.42  E-value: 8.56e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 568953835   275 LLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLDRGAQIETRTKDELTPLHCA 330
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 440-508 8.90e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.22  E-value: 8.90e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568953835  440 LLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLL 508
Cdd:PTZ00322  100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 636-707 1.13e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.83  E-value: 1.13e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568953835  636 VKLLLPRGGSPHSPAWNGYTPLHIAAKQNQIEVARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVALLLS 707
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
Ank_4 pfam13637
Ankyrin repeats (many copies);
554-607 1.14e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.97  E-value: 1.14e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 568953835   554 GHTPLHTAAREGHVDTALALLEKEASQACMTKKGFTPLHVAAKYGKVRLAELLL 607
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
585-627 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 568953835   585 KKGFTPLHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVA 627
Cdd:pfam13857   14 GEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 693-869 1.16e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 57.19  E-value: 1.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  693 AAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADVLIKHGVTVDATTRMGYTPLHVASHYGNIKLVKFLL 772
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY 611

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  773 QHQADVNAKTklGYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIAKRLGYISVTDVLkvVTDETSVVLVSDK 852
Cdd:PLN03192  612 HFASISDPHA--AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLL--IMNGADVDKANTD 687

                         170
                  ....*....|....*..
gi 568953835  853 HRMSyPETVDEILDVSE 869
Cdd:PLN03192  688 DDFS-PTELRELLQKRE 703
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 361-443 1.19e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.83  E-value: 1.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  361 HMAAQGDHLDcVRLLLQYNAEIDDITLDHLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMEL 440
Cdd:PTZ00322   88 QLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                  ...
gi 568953835  441 LLK 443
Cdd:PTZ00322  167 LSR 169
Ank_4 pfam13637
Ankyrin repeats (many copies);
620-673 1.71e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.58  E-value: 1.71e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 568953835   620 GLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQIEVARSLL 673
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 556-653 2.10e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.06  E-value: 2.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  556 TPLHTAAREGHVDTALA---------------------LLEKEASQACMTKKGFTPLHVAAKYGKVRLAELLLEHDAHPN 614
Cdd:PTZ00322   63 TPDHNLTTEEVIDPVVAhmltvelcqlaasgdavgariLLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPT 142

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 568953835  615 AAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNG 653
Cdd:PTZ00322  143 LLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGANA 181
Ank_5 pfam13857
Ankyrin repeats (many copies);
606-660 2.28e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 49.27  E-value: 2.28e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 568953835   606 LLEHD-AHPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIA 660
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 175-359 2.30e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 56.03  E-value: 2.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  175 LEVVKFLLENGAnQNVATEDGFTPLAVAlQQGHENVVAHLINYG-------TKGKVrlpALHIAARNDDTRTAAVLLQND 247
Cdd:PLN03192  507 LNVGDLLGDNGG-EHDDPNMASNLLTVA-STGNAALLEELLKAKldpdigdSKGRT---PLHIAASKGYEDCVLVLLKHA 581

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  248 PNPDVLSKTGFTPLH---IAAHYENLNVaqllLNRGASVNfTPQNGITPLHIASRRGNVIMVRLLLDRGAQIETRTKDEL 324
Cdd:PLN03192  582 CNVHIRDANGNTALWnaiSAKHHKIFRI----LYHFASIS-DPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGA 656

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 568953835  325 TPLHCAARNGHVRISEILLDHGAPI-QAKTKNGLSP 359
Cdd:PLN03192  657 TALQVAMAEDHVDMVRLLIMNGADVdKANTDDDFSP 692
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 534-835 2.37e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 55.52  E-value: 2.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  534 TGMVKLLLENGASPNlattaghtplhtaaREGHVDTAL-ALLEKEASQACMTKKgftplhvaakygkvrLAELLLEHDAH 612
Cdd:PHA02989   50 IKIVKLLIDNGADVN--------------YKGYIETPLcAVLRNREITSNKIKK---------------IVKLLLKFGAD 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  613 PNAAGKNGLTPLHVAVHH---NNLDIVKLLLPRGGSPHS-PAWNGYTPLHIAAKQNQI--EVARSLLQYGgsanaesvqg 686
Cdd:PHA02989  101 INLKTFNGVSPIVCFIYNsniNNCDMLRFLLSKGINVNDvKNSRGYNLLHMYLESFSVkkDVIKILLSFG---------- 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  687 VTPLHLAAQEGHTEMvalllskqaNGNLGNKsgltpLHLVSqeghVPVADVLIKHGVTVDATTRMGYTPL------HVAS 760
Cdd:PHA02989  171 VNLFEKTSLYGLTPM---------NIYLRND-----IDVIS----IKVIKYLIKKGVNIETNNNGSESVLesfldnNKIL 232

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568953835  761 HYGNIKLVKFLLQHqADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIAKRLGYISVTD 835
Cdd:PHA02989  233 SKKEFKVLNFILKY-IKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLN 306
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 343-614 3.91e-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: 3.91e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   343 LDHGAPIQAKTKN--GLSPIHMAA-QGDHLDCVRLLLQYNAEIDdiTLDHLtpLHVAAHCGHHRVAKVLLDKGAKP---- 415
Cdd:TIGR00870   37 LEEPKKLNINCPDrlGRSALFVAAiENENLELTELLLNLSCRGA--VGDTL--LHAISLEYVDAVEAILLHLLAAFrksg 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   416 -----NSRALNGFTPlhiackknhirvmelllktgasidavtesGLTPLHVASFMGHLPIVKNLLQRGASPNVS---NVK 487
Cdd:TIGR00870  113 plelaNDQYTSEFTP-----------------------------GITALHLAAHRQNYEIVKLLLERGASVPARacgDFF 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   488 VETPLHMAARAGhtevakyllqnkakanakakddQTPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHV 567
Cdd:TIGR00870  164 VKSQGVDSFYHG----------------------ESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVMENEF 221

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   568 ------------DTALALLEKEAS----QACMTKKGFTPLHVAAKYGKVRLAELLL-------EHDAHPN 614
Cdd:TIGR00870  222 kaeyeelscqmyNFALSLLDKLRDskelEVILNHQGLTPLKLAAKEGRIVLFRLKLaikykqkKFVAWPN 291
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 691-774 4.80e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.90  E-value: 4.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  691 HLAAQeGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADVLIKHGVTVDATTRMGYTPLHVASHYGNIKLVKF 770
Cdd:PTZ00322   88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                  ....
gi 568953835  771 LLQH 774
Cdd:PTZ00322  167 LSRH 170
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 754-853 5.17e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 52.51  E-value: 5.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  754 TPLH--VASHYGNIKLVKFLLQHQADVNAKTK-LGYSPLH---QAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIakR 827
Cdd:PHA02859   53 TPIFscLEKDKVNVEILKFLIENGADVNFKTRdNNLSALHhylSFNKNVEPEILKILIDSGSSITEEDEDGKNLLHM--Y 130

                          90       100
                  ....*....|....*....|....*..
gi 568953835  828 LGYISV-TDVLKVVTDETSVVLVSDKH 853
Cdd:PHA02859  131 MCNFNVrINVIKLLIDSGVSFLNKDFD 157
Ank_5 pfam13857
Ankyrin repeats (many copies);
243-297 5.25e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.11  E-value: 5.25e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 568953835   243 LLQNDP-NPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIA 297
Cdd:pfam13857    1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 354-449 6.40e-07

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 51.03  E-value: 6.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  354 KNGLSPIHMAAQGDHLDC---VRLLLQYNAEID-DITLDHLTPLHVAAHCGHHRVAKVLLDKgAKPNSRALNGF--TPLH 427
Cdd:PHA02736   53 RHGKQCVHIVSNPDKADPqekLKLLMEWGADINgKERVFGNTPLHIAVYTQNYELATWLCNQ-PGVNMEILNYAfkTPYY 131

                          90       100
                  ....*....|....*....|..
gi 568953835  428 IACKKNHIRVMELLLKTGASID 449
Cdd:PHA02736  132 VACERHDAKMMNILRAKGAQCK 153
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 67-344 6.61e-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: 54.32  E-value: 6.61e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835    67 FLRAARSGNLDKALDHLRNG--VDINTCNQNGLNGLHLASKEGHVKMVVELLHKeiiLETTTKKGNTALHIAALAGQDeV 144
Cdd:TIGR00870   21 FLPAAERGDLASVYRDLEEPkkLNINCPDRLGRSALFVAAIENENLELTELLLN---LSCRGAVGDTLLHAISLEYVD-A 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   145 VRELVNYGAN----------VNAQS----QKGFTPLYMAAQENHLEVVKFLLENGANQNV-ATEDGFTplavaLQQGHEn 209
Cdd:TIGR00870   97 VEAILLHLLAafrksgplelANDQYtsefTPGITALHLAAHRQNYEIVKLLLERGASVPArACGDFFV-----KSQGVD- 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   210 vvahLINYGtkgkvRLPaLHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIA-------AHYENL-----NVAQLLL 277
Cdd:TIGR00870  171 ----SFYHG-----ESP-LNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLvmenefkAEYEELscqmyNFALSLL 240

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568953835   278 NRGAS-------VNFtpqNGITPLHIASRRGNVIMVRLLLdrgaQIETRTKDeltplHCAARNGHVRISEILLD 344
Cdd:TIGR00870  241 DKLRDskeleviLNH---QGLTPLKLAAKEGRIVLFRLKL----AIKYKQKK-----FVAWPNGQQLLSLYWLE 302
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 118-287 7.06e-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: 7.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  118 KEIILETTTK---KGNTALHIAALAGQDEVVRELVNYGANVNAQSQKGF-------------TPLYMAAQENHLEVVKFL 181
Cdd:cd21882    59 KELVNAPCTDefyQGQTALHIAIENRNLNLVRLLVENGADVSARATGRFfrkspgnlfyfgeLPLSLAACTNQEEIVRLL 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  182 LENGANqnvatedgftPLAVALQQGHENVVAHLINYGTKGKVRLPALHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPL 261
Cdd:cd21882   139 LENGAQ----------PAALEAQDSLGNTVLHALVLQADNTPENSAFVCQMYNLLLSYGAHLDPTQQLEEIPNHQGLTPL 208

                         170       180
                  ....*....|....*....|....*.
gi 568953835  262 HIAAHYENLNVAQLLLNRGASVNFTP 287
Cdd:cd21882   209 KLAAVEGKIVMFQHILQREFSGPYQP 234
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 752-783 7.49e-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: 47.28  E-value: 7.49e-07
                           10        20        30
                   ....*....|....*....|....*....|...
gi 568953835   752 GYTPLHVAS-HYGNIKLVKFLLQHQADVNAKTK 783
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 421-450 8.41e-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: 8.41e-07
                            10        20        30
                    ....*....|....*....|....*....|
gi 568953835    421 NGFTPLHIACKKNHIRVMELLLKTGASIDA 450
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02798 PHA02798
ankyrin-like protein; Provisional
 599-825 9.25e-07

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 53.69  E-value: 9.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  599 KVRLAELLLEHDAHPNAAGKNGLTPL-----HVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQ---NQIEVAR 670
Cdd:PHA02798   50 STDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNgyiNNLEILL 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  671 SLLQYGGSANAESVQGVTPLHLAAQEGHT---EMVALLLSKQANGNL-GNKSGLTPLHLVSQEG----HVPVADVLIKHG 742
Cdd:PHA02798  130 FMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDINThNNKEKYDTLHCYFKYNidriDADILKLFVDNG 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  743 VTV---DATTRMGYTPLHVASHYGNIK----LVKFLLQHqADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNEVS 815
Cdd:PHA02798  210 FIInkeNKSHKKKFMEYLNSLLYDNKRfkknILDFIFSY-IDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIIT 288

                         250
                  ....*....|
gi 568953835  816 SNGTTPLAIA 825
Cdd:PHA02798  289 ELGNTCLFTA 298
Ank_4 pfam13637
Ankyrin repeats (many copies);
785-837 1.00e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.27  E-value: 1.00e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568953835   785 GYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIAKRLGYISVTDVL 837
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
Death_RAIDD cd08319
Death domain of RIP-associated ICH-1 homologous protein with a death domain; Death domain (DD) ...
 1451-1526 1.13e-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: 48.09  E-value: 1.13e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568953835 1451 TDRVEMRMAvirEHLGLSWAELARELQFSVEDINRIRVENPNSLLDQSTALLTLWVDREGENAKMENLYTALRNID 1526
Cdd:cd08319     1 TDRQLNKLA---QRLGPEWEQVLLDLGLSKADIYRCKADHPYNVQSQIVEALVKWKQRQGKKATVQSLIQSLKAVE 73
Ank_5 pfam13857
Ankyrin repeats (many copies);
672-726 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 568953835   672 LLQYGG-SANAESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLV 726
Cdd:pfam13857    1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 650-772 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 568953835  650 AWNGYTPLHIAAKQNQIEVARSLLQYGGSANAESvQGV---------------TPLHLAAQEGHTEMVALLLSK-QANGN 713
Cdd:cd22194   138 AYEGQTALNIAIERRQGDIVKLLIAKGADVNAHA-KGVffnpkykhegfyfgeTPLALAACTNQPEIVQLLMEKeSTDIT 216

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568953835  714 LGNKSGLTPLHLVsqeghVPVAD---------------VLIKHGVTVDATTR--MGYTPLHVASHYGNIKLVKFLL 772
Cdd:cd22194   217 SQDSRGNTVLHAL-----VTVAEdsktqndfvkrmydmILLKSENKNLETIRnnEGLTPLQLAAKMGKAEILKYIL 287
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 752-780 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 568953835   752 GYTPLHVASHYGNIKLVKFLLQHQADVNA 780
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 751-780 1.53e-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: 1.53e-06
                            10        20        30
                    ....*....|....*....|....*....|
gi 568953835    751 MGYTPLHVASHYGNIKLVKFLLQHQADVNA 780
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 76-279 1.56e-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: 1.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   76 LDKALDHLRNGVdintcNQNGLNGLHLASKEGHVKMVVELLHKEiiletTTKKGNTALHIAALAGQDEVVRELVNYGANV 155
Cdd:cd22196    51 LLKAMLNLHNGQ-----NDTISLLLDIAEKTGNLKEFVNAAYTD-----SYYKGQTALHIAIERRNMHLVELLVQNGADV 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  156 NA----------QSQKGF----TPLYMAAQENHLEVVKFLLENGANQ-NVATEDGFTplavalqqgheNVVAHlinygtk 220
Cdd:cd22196   121 HArasgeffkkkKGGPGFyfgeLPLSLAACTNQLDIVKFLLENPHSPaDISARDSMG-----------NTVLH------- 182

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568953835  221 gkvrlpALHIAARNDDTRTAAV--------LLQNDPNP-----DVLSKTGFTPLHIAAHYENLNVAQLLLNR 279
Cdd:cd22196   183 ------ALVEVADNTPENTKFVtkmyneilILGAKIRPllkleEITNKKGLTPLKLAAKTGKIGIFAYILGR 248
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 134-217 1.58e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.36  E-value: 1.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  134 HIAAlAGQDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAH 213
Cdd:PTZ00322   88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                  ....
gi 568953835  214 LINY 217
Cdd:PTZ00322  167 LSRH 170
PHA02946 PHA02946
ankyin-like protein; Provisional
 276-459 1.61e-06

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 52.75  E-value: 1.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  276 LLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLDRGAQIETRTKDELTPLHCAARNGHVRISEI--LLDHGAPIQAKT 353
Cdd:PHA02946   58 LLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIERInlLVQYGAKINNSV 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  354 -KNGLSPIHMAAQGDHLDCVRLL-LQYNAEIDDITLDHLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACK 431
Cdd:PHA02946  138 dEEGCGPLLACTDPSERVFKKIMsIGFEARIVDKFGKNHIHRHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCS 217

                         170       180       190
                  ....*....|....*....|....*....|
gi 568953835  432 KN--HIRVMELLLKTgASIDAVTESGLTPL 459
Cdd:PHA02946  218 KTvkNVDIINLLLPS-TDVNKQNKFGDSPL 246
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 493-574 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 568953835  493 HMAArAGHTEVAKYLLQNKAKANAKAKDDQTPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALA 572
Cdd:PTZ00322   88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                  ..
gi 568953835  573 LL 574
Cdd:PTZ00322  167 LS 168
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 129-312 2.27e-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: 2.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  129 GNTALHIAALAGQD----------EVVRELVNYGANVNAQSQ----KGFTPLYMAAQENHLEVVKFLLENGAN-QNVATE 193
Cdd:cd21882    26 GKTCLHKAALNLNDgvneaimlllEAAPDSGNPKELVNAPCTdefyQGQTALHIAIENRNLNLVRLLVENGADvSARATG 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  194 DGFT------------PLAVALQQGHENVVAHLINYGTKgkvrlPAlHIAARND--DTRTAAVLLQNDPNPDvlsKTGFt 259
Cdd:cd21882   106 RFFRkspgnlfyfgelPLSLAACTNQEEIVRLLLENGAQ-----PA-ALEAQDSlgNTVLHALVLQADNTPE---NSAF- 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  260 plhiAAHYENlnvaqLLLNRGASVNFTPQ-------NGITPLHIASRRGNVIMVRLLLDR 312
Cdd:cd21882   176 ----VCQMYN-----LLLSYGAHLDPTQQleeipnhQGLTPLKLAAVEGKIVMFQHILQR 226
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 161-190 2.38e-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: 2.38e-06
                            10        20        30
                    ....*....|....*....|....*....|
gi 568953835    161 KGFTPLYMAAQENHLEVVKFLLENGANQNV 190
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 143-312 2.62e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 52.05  E-value: 2.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  143 EVVRELVNYGANVNA-QSQKGFTPLYMAAQENHL--EVVKFLLENGANQNVATE-DGFTPLAVALQQGHENVVAHLINYG 218
Cdd:PHA02989  125 DMLRFLLSKGINVNDvKNSRGYNLLHMYLESFSVkkDVIKILLSFGVNLFEKTSlYGLTPMNIYLRNDIDVISIKVIKYL 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  219 TKGKVRLP---ALHIAARNDDTRTAAVLLQND----------PNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNF 285
Cdd:PHA02989  205 IKKGVNIEtnnNGSESVLESFLDNNKILSKKEfkvlnfilkyIKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYN 284

                         170       180
                  ....*....|....*....|....*..
gi 568953835  286 TPQNGITPLHIASRRGNVIMVRLLLDR 312
Cdd:PHA02989  285 VSKDGDTVLTYAIKHGNIDMLNRILQL 311
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 435-616 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 568953835  435 IRVMELLLK-TGASIDAVTESGLtpLHVASfMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKAK 513
Cdd:PLN03192  507 LNVGDLLGDnGGEHDDPNMASNL--LTVAS-TGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACN 583

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  514 ANAKAKDDQTPLHCAARIGHTGMVKLLLENGASPNlaTTAGHTPLHTAAREGHVDTALALLEKEASQACMTKKGFTPLHV 593
Cdd:PLN03192  584 VHIRDANGNTALWNAISAKHHKIFRILYHFASISD--PHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQV 661

                         170       180
                  ....*....|....*....|...
gi 568953835  594 AAKYGKVRLAELLLEHDAHPNAA 616
Cdd:PLN03192  662 AMAEDHVDMVRLLIMNGADVDKA 684
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 520-551 4.46e-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. 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: 4.46e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 568953835   520 DDQTPLHCAA-RIGHTGMVKLLLENGASPNLAT 551
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
Ank_5 pfam13857
Ankyrin repeats (many copies);
440-495 4.68e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.42  E-value: 4.68e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 568953835   440 LLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMA 495
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 259-356 4.83e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 49.43  E-value: 4.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  259 TPLH--IAAHYENLNVAQLLLNRGASVNF-TPQNGITPLH---IASRRGNVIMVRLLLDRGAQIETRTKDELTPLHCAAR 332
Cdd:PHA02859   53 TPIFscLEKDKVNVEILKFLIENGADVNFkTRDNNLSALHhylSFNKNVEPEILKILIDSGSSITEEDEDGKNLLHMYMC 132

                          90       100
                  ....*....|....*....|....*.
gi 568953835  333 NGHVRIS--EILLDHGAPIQAKTKNG 356
Cdd:PHA02859  133 NFNVRINviKLLIDSGVSFLNKDFDN 158
Ank_5 pfam13857
Ankyrin repeats (many copies);
653-693 5.21e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.42  E-value: 5.21e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 568953835   653 GYTPLHIAAKQNQIEVARSLLQYGGSANAESVQGVTPLHLA 693
Cdd:pfam13857   16 GYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 252-591 5.23e-06

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 51.45  E-value: 5.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  252 VLSKTGFTPLH--IAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVI--MVRLLLDRGAQIETRTKDELTPL 327
Cdd:PHA02716  172 VCKKTGYGILHayLGNMYVDIDILEWLCNNGVNVNLQNNHLITPLHTYLITGNVCasVIKKIIELGGDMDMKCVNGMSPI 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  328 HCAARNGHVRISEILLDHGAPIQA-KTKNGLSPIHM---AAQGDHLDCVRLLLQYNAEIDDITLDHLTPLH--VAAHCGH 401
Cdd:PHA02716  252 MTYIINIDNINPEITNIYIESLDGnKVKNIPMILHSyitLARNIDISVVYSFLQPGVKLHYKDSAGRTCLHqyILRHNIS 331

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  402 HRVAKVLLDKGAKPNSRALNGFTPLHIACKK------------NHIR--VMELLLKTGASIDAVTESGLTPL-----HVA 462
Cdd:PHA02716  332 TDIIKLLHEYGNDLNEPDNIGNTVLHTYLSMlsvvnildpetdNDIRldVIQCLISLGADITAVNCLGYTPLtsyicTAQ 411

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  463 SFMGHLPI-------VKNLLQRGASPNVSNVKVETPlhmaaRAGHTEVAKYLLQNKAKANAKAKDDQTPLHCAArigHTG 535
Cdd:PHA02716  412 NYMYYDIIdclisdkVLNMVKHRILQDLLIRVDDTP-----CIIHHIIAKYNIPTDLYTDEYEPYDSTKIHDVY---HCA 483

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568953835  536 MVKLLlengaSPNLATTAGHTPLHTAAREGH-----VDTALALLEKEASQACMTKKGFTPL 591
Cdd:PHA02716  484 IIERY-----NNAVCETSGMTPLHVSIISHTnanivMDSFVYLLSIQYNINIPTKNGVTPL 539
PHA02798 PHA02798
ankyrin-like protein; Provisional
 167-462 5.86e-06

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 50.99  E-value: 5.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  167 YMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALqqghenvvAHLINYGTKGKVRLpalhiaarnddtrtaaVLLQN 246
Cdd:PHA02798   43 YLQRDSPSTDIVKLFINLGANVNGLDNEYSTPLCTIL--------SNIKDYKHMLDIVK----------------ILIEN 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  247 DPNPDVLSKTGFTPLHIAAHYENLNVAQLLL---NRGASVNFTPQNGITPLHIASRRGNVI---MVRLLLDRGAQIETRT 320
Cdd:PHA02798   99 GADINKKNSDGETPLYCLLSNGYINNLEILLfmiENGADTTLLDKDGFTMLQVYLQSNHHIdieIIKLLLEKGVDINTHN 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  321 KDE-LTPLHCAARNGHVRIS----EILLDHGAPIQAKTKNGLSPIhmaaqgdhLDCVRLLLQYNAEIDDITLDhltplhv 395
Cdd:PHA02798  179 NKEkYDTLHCYFKYNIDRIDadilKLFVDNGFIINKENKSHKKKF--------MEYLNSLLYDNKRFKKNILD------- 243

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568953835  396 aahcghhrvakvLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVA 462
Cdd:PHA02798  244 ------------FIFSYIDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTA 298
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 421-453 6.79e-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: 44.59  E-value: 6.79e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 568953835   421 NGFTPLHIACKK-NHIRVMELLLKTGASIDAVTE 453
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 586-709 7.54e-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: 7.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  586 KGFTPLHVAAKYGKVRLAELLLEHDAHPNAAGKN--------------GLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAW 651
Cdd:cd22194   140 EGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEIVQLLMEKESTDITSQD 219

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568953835  652 N-GYTPLH---IAAKQNQ------IEVARSLLQYGGSANAESV---QGVTPLHLAAQEGHTEMVALLLSKQ 709
Cdd:cd22194   220 SrGNTVLHalvTVAEDSKtqndfvKRMYDMILLKSENKNLETIrnnEGLTPLQLAAKMGKAEILKYILSRE 290
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 128-158 7.72e-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: 7.72e-06
                           10        20        30
                   ....*....|....*....|....*....|..
gi 568953835   128 KGNTALHIAAL-AGQDEVVRELVNYGANVNAQ 158
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNAR 32
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 128-157 8.92e-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: 8.92e-06
                            10        20        30
                    ....*....|....*....|....*....|
gi 568953835    128 KGNTALHIAALAGQDEVVRELVNYGANVNA 157
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 682-830 9.11e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 50.83  E-value: 9.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  682 ESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADVLIKHGVTVDATTRMGYTPLHVASH 761
Cdd:PHA02876  141 ESIEYMKLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVD 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  762 YGNIKLVKFLLQHQADVNA--------------KTKL-----GYS----------PLHQAAQQGH-TDIVTLLLKNGASP 811
Cdd:PHA02876  221 SKNIDTIKAIIDNRSNINKndlsllkairnedlETSLllydaGFSvnsiddckntPLHHASQAPSlSRLVPKLLERGADV 300

                         170
                  ....*....|....*....
gi 568953835  812 NEVSSNGTTPLAIAKRLGY 830
Cdd:PHA02876  301 NAKNIKGETPLYLMAKNGY 319
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 128-279 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 568953835  128 KGNTALHIAALAGQDEVVRELVNYGANVNAQSQKGF--------------TPLYMAAQENHLEVVKFLLENganqnvate 193
Cdd:cd22193    75 EGQTALHIAIERRQGDIVALLVENGADVHAHAKGRFfqpkyqgegfyfgeLPLSLAACTNQPDIVQYLLEN--------- 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  194 dGFTPLAVALQQGHENVVAHlinygtkgkvrlpALHIAARNDDTRTAAV------LLQNDPN--PDV-----LSKTGFTP 260
Cdd:cd22193   146 -EHQPADIEAQDSRGNTVLH-------------ALVTVADNTKENTKFVtrmydmILIRGAKlcPTVeleeiRNNDGLTP 211

                         170
                  ....*....|....*....
gi 568953835  261 LHIAAHYENLNVAQLLLNR 279
Cdd:cd22193   212 LQLAAKMGKIEILKYILQR 230
Ank_5 pfam13857
Ankyrin repeats (many copies);
309-363 1.10e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.64  E-value: 1.10e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 568953835   309 LLDRG-AQIETRTKDELTPLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMA 363
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 564-709 1.40e-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: 1.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  564 EGHVDTALALLE--------KEASQACMTK---KGFTPLHVAAKYGKVRLAELLLEHDAHPNAA----------GKNGL- 621
Cdd:cd22196    60 NGQNDTISLLLDiaektgnlKEFVNAAYTDsyyKGQTALHIAIERRNMHLVELLVQNGADVHARasgeffkkkkGGPGFy 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  622 ---TPLHVAVHHNNLDIVKLLLPrggSPHSPA------WNGYTPLH--IAAKQNQIEVAR-------SLLQYGG----SA 679
Cdd:cd22196   140 fgeLPLSLAACTNQLDIVKFLLE---NPHSPAdisardSMGNTVLHalVEVADNTPENTKfvtkmynEILILGAkirpLL 216

                         170       180       190
                  ....*....|....*....|....*....|...
gi 568953835  680 NAESV---QGVTPLHLAAQEGHTEMVALLLSKQ 709
Cdd:cd22196   217 KLEEItnkKGLTPLKLAAKTGKIGIFAYILGRE 249
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 619-647 1.41e-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: 1.41e-05
                            10        20
                    ....*....|....*....|....*....
gi 568953835    619 NGLTPLHVAVHHNNLDIVKLLLPRGGSPH 647
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 658-741 1.46e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.90  E-value: 1.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  658 HIAAKQNQIEvARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADV 737
Cdd:PTZ00322   88 QLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                  ....
gi 568953835  738 LIKH 741
Cdd:PTZ00322  167 LSRH 170
Ank_4 pfam13637
Ankyrin repeats (many copies);
100-149 1.56e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.80  E-value: 1.56e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 568953835   100 LHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQDEVVRELV 149
Cdd:pfam13637    5 LHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 455-485 1.60e-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: 1.60e-05
                           10        20        30
                   ....*....|....*....|....*....|..
gi 568953835   455 GLTPLHVASFM-GHLPIVKNLLQRGASPNVSN 485
Cdd:pfam00023    2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 219-480 1.63e-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: 1.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  219 TKGKVRLPALHIAARNDDTR---TAAVLLQNDPNPDVLSKTGFTPLhIAAHYEnlnvaqlllnrgasvnftpqnGITPLH 295
Cdd:cd21882    21 QRGATGKTCLHKAALNLNDGvneAIMLLLEAAPDSGNPKELVNAPC-TDEFYQ---------------------GQTALH 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  296 IASRRGNVIMVRLLLDRGAQIETRTKdeltplhcaarnghvriseilldhGAPIQAKTKNGL----SPIHMAAQGDHLDC 371
Cdd:cd21882    79 IAIENRNLNLVRLLVENGADVSARAT------------------------GRFFRKSPGNLFyfgeLPLSLAACTNQEEI 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  372 VRLLLQYNAEIDDITL-DHL--TPLHvaahcghhrvAKVLLDKGAKPNSRalngftplhIACKknhirVMELLLKTGA-- 446
Cdd:cd21882   135 VRLLLENGAQPAALEAqDSLgnTVLH----------ALVLQADNTPENSA---------FVCQ-----MYNLLLSYGAhl 190

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 568953835  447 ----SIDAVT-ESGLTPLHVASFMGHLPIVKNLLQRGAS 480
Cdd:cd21882   191 dptqQLEEIPnHQGLTPLKLAAVEGKIVMFQHILQREFS 229
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 83-157 1.74e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 49.28  E-value: 1.74e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568953835   83 LRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQDEVVRELVNYGANVNA 157
Cdd:PHA03100  179 LSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 768-837 1.85e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.90  E-value: 1.85e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  768 VKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIAKRLGYISVTDVL 837
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
Ank_5 pfam13857
Ankyrin repeats (many copies);
115-169 2.10e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.49  E-value: 2.10e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 568953835   115 LLHKEIILETTTKKGNTALHIAALAGQDEVVRELVNYGANVNAQSQKGFTPLYMA 169
Cdd:pfam13857    2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 520-549 2.20e-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: 2.20e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 568953835    520 DDQTPLHCAARIGHTGMVKLLLENGASPNL 549
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 632-855 2.51e-05

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 49.53  E-value: 2.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  632 NLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQI--EVARSLLQYGGSANAESVQGVTPL--HLAAQEGHTEMVALLLS 707
Cdd:PHA02716  191 DIDILEWLCNNGVNVNLQNNHLITPLHTYLITGNVcaSVIKKIIELGGDMDMKCVNGMSPImtYIINIDNINPEITNIYI 270

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  708 KQANGNlgnKSGLTP--LHL---VSQEGHVPVADVLIKHGVTVDATTRMGYTPLH--VASHYGNIKLVKFLLQHQADVNA 780
Cdd:PHA02716  271 ESLDGN---KVKNIPmiLHSyitLARNIDISVVYSFLQPGVKLHYKDSAGRTCLHqyILRHNISTDIIKLLHEYGNDLNE 347

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  781 KTKLGYSPLH--------------QAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLA----IAKRLGYISVTDVLkvVTD 842
Cdd:PHA02716  348 PDNIGNTVLHtylsmlsvvnildpETDNDIRLDVIQCLISLGADITAVNCLGYTPLTsyicTAQNYMYYDIIDCL--ISD 425

                         250
                  ....*....|...
gi 568953835  843 EtsvVLVSDKHRM 855
Cdd:PHA02716  426 K---VLNMVKHRI 435
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 752-822 2.74e-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: 2.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  752 GYTPLHVASHYGNIKLVKFLLQHQADVNA--------KTK------LGYSPLHQAAQQGHTDIVTLLLKNGASPNEVS-- 815
Cdd:cd22196    94 GQTALHIAIERRNMHLVELLVQNGADVHArasgeffkKKKggpgfyFGELPLSLAACTNQLDIVKFLLENPHSPADISar 173


                  ....*...
gi 568953835  816 -SNGTTPL 822
Cdd:cd22196   174 dSMGNTVL 181
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 257-284 2.75e-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: 2.75e-05
                            10        20
                    ....*....|....*....|....*...
gi 568953835    257 GFTPLHIAAHYENLNVAQLLLNRGASVN 284
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank_5 pfam13857
Ankyrin repeats (many copies);
342-396 2.85e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.49  E-value: 2.85e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 568953835   342 LLDHG-APIQAKTKNGLSPIHMAAQGDHLDCVRLLLQYNAEIDDITLDHLTPLHVA 396
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 620-738 3.22e-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: 3.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  620 GLTPLHVAVHHNNLDIVKLLLPRGGSPHSPA--------------WNGYTPLHIAAKQNQIEVARSLLQYGGSA---NAE 682
Cdd:cd22196    94 GQTALHIAIERRNMHLVELLVQNGADVHARAsgeffkkkkggpgfYFGELPLSLAACTNQLDIVKFLLENPHSPadiSAR 173

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568953835  683 SVQGVTPLH-LAAQEGHTEMVALLLSKQANG---------------NLGNKSGLTPLHLVSQEGHVPV-ADVL 738
Cdd:cd22196   174 DSMGNTVLHaLVEVADNTPENTKFVTKMYNEililgakirpllkleEITNKKGLTPLKLAAKTGKIGIfAYIL 246
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 289-321 3.23e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 42.66  E-value: 3.23e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 568953835   289 NGITPLHIAS-RRGNVIMVRLLLDRGAQIETRTK 321
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
522-561 3.30e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.10  E-value: 3.30e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 568953835   522 QTPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTA 561
Cdd:pfam13857   17 YTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 128-157 3.39e-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: 3.39e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 568953835   128 KGNTALHIAALAGQDEVVRELVNYGANVNA 157
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Death_p75NR cd08311
Death domain of p75 Neurotrophin Receptor; Death Domain (DD) found in p75 neurotrophin ...
 1468-1535 3.48e-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: 43.81  E-value: 3.48e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568953835 1468 SWAELARELQFSVEDINRI-RVENPnslldqSTALLTLWVDREGenAKMENLYTALRNIDRSEIVNMLE 1535
Cdd:cd08311    20 DWRALAGELGYSAEEIDSFaREADP------CRALLTDWSAQDG--ATLGVLLTALRKIGRDDIVEILQ 80
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 289-317 3.70e-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: 3.70e-05
                            10        20
                    ....*....|....*....|....*....
gi 568953835    289 NGITPLHIASRRGNVIMVRLLLDRGAQIE 317
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 735-818 3.77e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.74  E-value: 3.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  735 ADVLIKHGVTVDATTRMGYTPLHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNEV 814
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFEL 177


                  ....
gi 568953835  815 SSNG 818
Cdd:PTZ00322  178 GANA 181
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 421-450 3.77e-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: 3.77e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 568953835   421 NGFTPLHIACKKNHIRVMELLLKTGASIDA 450
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 161-193 4.47e-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: 4.47e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 568953835   161 KGFTPLYMAA-QENHLEVVKFLLENGANQNVATE 193
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
704-759 4.48e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.72  E-value: 4.48e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 568953835   704 LLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADVLIKHGVTVDATTRMGYTPLHVA 759
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 355-384 5.16e-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: 5.16e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 568953835    355 NGLSPIHMAAQGDHLDCVRLLLQYNAEIDD 384
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 520-548 5.53e-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: 5.53e-05
                           10        20
                   ....*....|....*....|....*....
gi 568953835   520 DDQTPLHCAARIGHTGMVKLLLENGASPN 548
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 372-508 6.26e-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: 6.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  372 VRLLLQY-----------NAEIDDITLDHLTPLHVAAHCGHHRVAKVLLDKGAKPNSRA----------LNGF----TPL 426
Cdd:cd22194   113 VRILLAFaeengildrfiNAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAkgvffnpkykHEGFyfgeTPL 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  427 HIACKKNHIRVMELLLKTGASIDAVTES-GLTPLH----VA-SFMGHLPIVKNL----LQRGASPN---VSNVKVETPLH 493
Cdd:cd22194   193 ALAACTNQPEIVQLLMEKESTDITSQDSrGNTVLHalvtVAeDSKTQNDFVKRMydmiLLKSENKNletIRNNEGLTPLQ 272

                         170
                  ....*....|....*
gi 568953835  494 MAARAGHTEVAKYLL 508
Cdd:cd22194   273 LAAKMGKAEILKYIL 287
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 236-332 6.45e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 46.90  E-value: 6.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  236 DTRTAAVLLQNDPN-PDVLSKTGFT-PLHIAAHYENLNVAQLLLNRGASVN-FTPQNGITPLHIASRRGNVIMVRLLLDR 312
Cdd:PHA02884   47 DIIDAILKLGADPEaPFPLSENSKTnPLIYAIDCDNDDAAKLLIRYGADVNrYAEEAKITPLYISVLHGCLKCLEILLSY 126

                          90       100
                  ....*....|....*....|
gi 568953835  313 GAQIETRTKDELTPLHCAAR 332
Cdd:PHA02884  127 GADINIQTNDMVTPIELALM 146
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 342-509 6.61e-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: 6.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  342 LLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQY-----------NAEIDDITLDHLTPLHVAAHCGHHRVAKVLLD 410
Cdd:cd22193    18 LTDSEFTESSTGKTCLMKALLNLNPGTNDTIRILLDIaektdnlkrfiNAEYTDEYYEGQTALHIAIERRQGDIVALLVE 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  411 KGAKPNSRALNGF--------------TPLHIACKKNHIRVMELLLK---TGASIDAVTESGLTPLH----VA-SFMGHL 468
Cdd:cd22193    98 NGADVHAHAKGRFfqpkyqgegfyfgeLPLSLAACTNQPDIVQYLLEnehQPADIEAQDSRGNTVLHalvtVAdNTKENT 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568953835  469 PIVKN----LLQRGAS-------PNVSNVKVETPLHMAARAGHTEVAKYLLQ 509
Cdd:cd22193   178 KFVTRmydmILIRGAKlcptvelEEIRNNDGLTPLQLAAKMGKIEILKYILQ 229
Ank_5 pfam13857
Ankyrin repeats (many copies);
374-429 6.63e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 6.63e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 568953835   374 LLLQYNAEIDDITLDHLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIA 429
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Death_PIDD cd08779
Death Domain of p53-induced protein with a death domain; Death domain (DD) found in PIDD ...
 1461-1535 6.74e-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: 6.74e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568953835 1461 IREHLGLSWAELARELQFSVEDINRIRVENPNSLLDQSTALLTLWVDREGENA-KMENLYTALRNIDRSEIVNMLE 1535
Cdd:cd08779     8 LAKELGEDWQKLALHLGVSYSRIQRIKRKNRDDLDEQILDMLFSWAKTLPTSPdKVGLLVTALSKSGRSDLAEELR 83
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 388-418 6.82e-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: 6.82e-05
                           10        20        30
                   ....*....|....*....|....*....|..
gi 568953835   388 DHLTPLHVAA-HCGHHRVAKVLLDKGAKPNSR 418
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNAR 32
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 257-284 7.23e-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: 7.23e-05
                           10        20
                   ....*....|....*....|....*....
gi 568953835   257 GFTPLHIAA-HYENLNVAQLLLNRGASVN 284
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVN 30
Death_DRs cd08784
Death Domain of Death Receptors; Death domain (DD) found in death receptor proteins. Death ...
 1467-1526 7.49e-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: 42.95  E-value: 7.49e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835 1467 LSWAELARELQFSVEDINRIRVENPNSLLDQSTALLTLWVDREGENAKMENLYTALRNID 1526
Cdd:cd08784    12 SQWKGFVRKLGLNEAEIDEIKNDNVQDTAEAKYQMLRNWHQLTGRKAAYDTLIKDLKKMN 71
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 294-509 8.93e-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: 8.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   294 LHIASRRGNVIMVRLLLDRGAQIETrtkdELTPLHcAARNGHVRISEILLDHGAPIQAKTKNglspihmaaqgdhldcvr 373
Cdd:TIGR00870   57 FVAAIENENLELTELLLNLSCRGAV----GDTLLH-AISLEYVDAVEAILLHLLAAFRKSGP------------------ 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   374 LLLQYNAEIDDITLDHlTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNGF--------------TPLHIACKKNHIRVME 439
Cdd:TIGR00870  114 LELANDQYTSEFTPGI-TALHLAAHRQNYEIVKLLLERGASVPARACGDFfvksqgvdsfyhgeSPLNAAACLGSPSIVA 192

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   440 LLLKTGASIDAVTESGLTPLH----VASF--------MGHLPIVKNLLQRGASPN----VSNVKVETPLHMAARAGHTEV 503
Cdd:TIGR00870  193 LLSEDPADILTADSLGNTLLHllvmENEFkaeyeelsCQMYNFALSLLDKLRDSKelevILNHQGLTPLKLAAKEGRIVL 272


                   ....*.
gi 568953835   504 AKYLLQ 509
Cdd:TIGR00870  273 FRLKLA 278
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 785-812 1.02e-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: 1.02e-04
                           10        20
                   ....*....|....*....|....*....
gi 568953835   785 GYSPLHQAAQQ-GHTDIVTLLLKNGASPN 812
Cdd:pfam00023    2 GNTPLHLAAGRrGNLEIVKLLLSKGADVN 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 388-416 1.10e-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: 1.10e-04
                            10        20
                    ....*....|....*....|....*....
gi 568953835    388 DHLTPLHVAAHCGHHRVAKVLLDKGAKPN 416
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 289-318 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: 41.09  E-value: 1.10e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 568953835   289 NGITPLHIASRRGNVIMVRLLLDRGAQIET 318
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 455-483 1.21e-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: 1.21e-04
                            10        20
                    ....*....|....*....|....*....
gi 568953835    455 GLTPLHVASFMGHLPIVKNLLQRGASPNV 483
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 678-824 1.35e-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: 1.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  678 SANAESVQGVTPLHLAA---QEGHTEMVALLLskQANGNLGNksgltPLHLVSQeghvPVADVLIKhgvtvdattrmGYT 754
Cdd:cd21882    18 SAYQRGATGKTCLHKAAlnlNDGVNEAIMLLL--EAAPDSGN-----PKELVNA----PCTDEFYQ-----------GQT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  755 PLHVASHYGNIKLVKFLLQHQADVNAKTK-------------LGYSPLHQAAQQGHTDIVTLLLKNGASPNEVS---SNG 818
Cdd:cd21882    76 ALHIAIENRNLNLVRLLVENGADVSARATgrffrkspgnlfyFGELPLSLAACTNQEEIVRLLLENGAQPAALEaqdSLG 155


                  ....*.
gi 568953835  819 TTPLAI 824
Cdd:cd21882   156 NTVLHA 161
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 586-618 1.53e-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: 40.74  E-value: 1.53e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 568953835   586 KGFTPLHVAA-KYGKVRLAELLLEHDAHPNAAGK 618
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 652-681 1.58e-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: 1.58e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 568953835    652 NGYTPLHIAAKQNQIEVARSLLQYGGSANA 681
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 614-775 1.67e-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: 46.77  E-value: 1.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  614 NAAGKN----GLTPLHVAVHHNNLDIVKLLLPRGGSPHSPA-------------WNGYTPLHIAAKQNQIEVARSLLQyg 676
Cdd:cd22197    84 NAQCTDeyyrGHSALHIAIEKRSLQCVKLLVENGADVHARAcgrffqkkqgtcfYFGELPLSLAACTKQWDVVNYLLE-- 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  677 gsanaesvQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHlvsqeghvpvaDVLIKHGVTVDATTRM----- 751
Cdd:cd22197   162 --------NPHQPASLQAQDSLGNTVLHALVMIADNSPENSALVIKMY-----------DGLLQAGARLCPTVQLeeisn 222

                         170       180
                  ....*....|....*....|....*.
gi 568953835  752 --GYTPLHVASHYGNIKLVKFLLQHQ 775
Cdd:cd22197   223 heGLTPLKLAAKEGKIEIFRHILQRE 248
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 471-541 1.67e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.43  E-value: 1.67e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568953835  471 VKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKAKANAKAKDDQTPLHCAARIGHTGMVKLLL 541
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 322-354 1.75e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 40.35  E-value: 1.75e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 568953835   322 DELTPLHCAA-RNGHVRISEILLDHGAPIQAKTK 354
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 356-477 1.82e-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: 1.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  356 GLSPIHMAAQGDHLDCVRLLLQYNAEIDDITLDHL-------------TPLHVAAHCGHHRVAKVLLDKGAKPNS---RA 419
Cdd:cd22197    94 GHSALHIAIEKRSLQCVKLLVENGADVHARACGRFfqkkqgtcfyfgeLPLSLAACTKQWDVVNYLLENPHQPASlqaQD 173

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568953835  420 LNGFTPLH----IA--CKKNH---IRVMELLLKTGASIDA-------VTESGLTPLHVASFMGHLPIVKNLLQR 477
Cdd:cd22197   174 SLGNTVLHalvmIAdnSPENSalvIKMYDGLLQAGARLCPtvqleeiSNHEGLTPLKLAAKEGKIEIFRHILQR 247
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 678-809 1.83e-04

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 43.71  E-value: 1.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  678 SANAESVQGVTPLHLAAQEGhtEMVALLLSKQA----NGNLG---NKSGLTPLHLVSQEGHV-PVADV--LIKHGVTVDA 747
Cdd:PHA02736    9 FASEPDIEGENILHYLCRNG--GVTDLLAFKNAisdeNRYLVleyNRHGKQCVHIVSNPDKAdPQEKLklLMEWGADING 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568953835  748 TTRM-GYTPLHVASHYGNIKLVKFLLQH-QADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGA 809
Cdd:PHA02736   87 KERVfGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGA 150
PHA02795 PHA02795
ankyrin-like protein; Provisional
 143-206 1.95e-04

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 46.14  E-value: 1.95e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568953835  143 EVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQG 206
Cdd:PHA02795  202 EIYKLCIPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRG 265
PHA02946 PHA02946
ankyin-like protein; Provisional
 397-484 2.03e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 46.20  E-value: 2.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  397 AHCG----HHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPI-- 470
Cdd:PHA02946   43 AYCGikglDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIer 122

                          90
                  ....*....|....
gi 568953835  471 VKNLLQRGASPNVS 484
Cdd:PHA02946  123 INLLVQYGAKINNS 136
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 624-728 2.13e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 45.36  E-value: 2.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  624 LHVAVHHNNLDIVKLLLPRGGSPHSP---AWNGYT-PLHIAAKQNQIEVARSLLQYGGSANAESVQGV-TPLHLAAQEGH 698
Cdd:PHA02884   37 LYSSIKFHYTDIIDAILKLGADPEAPfplSENSKTnPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLHGC 116

                          90       100       110
                  ....*....|....*....|....*....|
gi 568953835  699 TEMVALLLSKQANGNLGNKSGLTPLHLVSQ 728
Cdd:PHA02884  117 LKCLEILLSYGADINIQTNDMVTPIELALM 146
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 129-182 2.17e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.04  E-value: 2.17e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568953835  129 GNTALHIAALAGQDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLL 182
Cdd:PTZ00322  115 GRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 785-813 2.23e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.88  E-value: 2.23e-04
                            10        20
                    ....*....|....*....|....*....
gi 568953835    785 GYSPLHQAAQQGHTDIVTLLLKNGASPNE 813
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 619-647 2.24e-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: 2.24e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 568953835   619 NGLTPLHVAV-HHNNLDIVKLLLPRGGSPH 647
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVN 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 685-717 2.30e-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: 2.30e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 568953835   685 QGVTPLHLAA-QEGHTEMVALLLSKQANGNLGNK 717
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 586-615 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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.93  E-value: 2.34e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 568953835   586 KGFTPLHVAAKYGKVRLAELLLEHDAHPNA 615
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA03095 PHA03095
ankyrin-like protein; Provisional
 765-822 2.71e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.79  E-value: 2.71e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568953835  765 IKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGH---TDIVTLLLKNGASPNEVSSNGTTPL 822
Cdd:PHA03095   27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPL 87
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 422-630 2.92e-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: 2.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  422 GFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLH--VASFMGHLpivknllqrgaspnvsnvkvetPLHMAARAG 499
Cdd:cd22197    94 GHSALHIAIEKRSLQCVKLLVENGADVHARACGRFFQKKqgTCFYFGEL----------------------PLSLAACTK 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  500 HTEVAKYLLQNKAKANAKAKDD---QTPLHCAARIGH---------TGMVKLLLENGA--SPNL-----ATTAGHTPLHT 560
Cdd:cd22197   152 QWDVVNYLLENPHQPASLQAQDslgNTVLHALVMIADnspensalvIKMYDGLLQAGArlCPTVqleeiSNHEGLTPLKL 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  561 AAREGHVDTALALLEKEASQAC--MTKKgFT-----PLHVAA-------KYGKVRLAELLLEHDAHPNAAGKNGLTPLHV 626
Cdd:cd22197   232 AAKEGKIEIFRHILQREFSGPYqhLSRK-FTewcygPVRVSLydlssvdSWEKNSVLEIIAFHSKSPNRHRMVVLEPLNK 310


                  ....
gi 568953835  627 AVHH 630
Cdd:cd22197   311 LLQE 314
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 619-647 3.24e-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: 3.24e-04
                           10        20
                   ....*....|....*....|....*....
gi 568953835   619 NGLTPLHVAVHHNNLDIVKLLLPRGGSPH 647
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 521-674 3.44e-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: 3.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   521 DQTPLHCAARIGHTGMVKLLLENGASPNLATTAGhtplhtaareghvdtalallekeasqACMTKKGFT-------PLHV 593
Cdd:TIGR00870  128 GITALHLAAHRQNYEIVKLLLERGASVPARACGD--------------------------FFVKSQGVDsfyhgesPLNA 181

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   594 AAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNL------------DIVKLLLPRGGSP----HSPAWNGYTPL 657
Cdd:TIGR00870  182 AACLGSPSIVALLSEDPADILTADSLGNTLLHLLVMENEFkaeyeelscqmyNFALSLLDKLRDSkeleVILNHQGLTPL 261

                          170
                   ....*....|....*..
gi 568953835   658 HIAAKQNQIEVARSLLQ 674
Cdd:TIGR00870  262 KLAAKEGRIVLFRLKLA 278
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 586-709 3.63e-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: 3.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  586 KGFTPLHVAAKYGKVRLAELLLEHDAHPNAAGKN--------------GLTPLHVAVHHNNLDIVKLLLPrggSPHSPA- 650
Cdd:cd22193    75 EGQTALHIAIERRQGDIVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLSLAACTNQPDIVQYLLE---NEHQPAd 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  651 -----WNGYTPLH----IA--AKQNQIEVAR---SLLQYGG----SANAESV---QGVTPLHLAAQEGHTEMVALLLSKQ 709
Cdd:cd22193   152 ieaqdSRGNTVLHalvtVAdnTKENTKFVTRmydMILIRGAklcpTVELEEIrnnDGLTPLQLAAKMGKIEILKYILQRE 231
PHA02946 PHA02946
ankyin-like protein; Provisional
 137-310 3.68e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 45.04  E-value: 3.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  137 ALAGQDE-VVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENV--VAH 213
Cdd:PHA02946   46 GIKGLDErFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIerINL 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  214 LINYGTKgkvrlpalhIAARNDDTRTAAVLLQNDPNPDVLSKT-----------GFTPLHIAAHYENLN----VAQLLLN 278
Cdd:PHA02946  126 LVQYGAK---------INNSVDEEGCGPLLACTDPSERVFKKImsigfearivdKFGKNHIHRHLMSDNpkasTISWMMK 196

                         170       180       190
                  ....*....|....*....|....*....|....
gi 568953835  279 RGASVNFTPQNGITPLHIASRR--GNVIMVRLLL 310
Cdd:PHA02946  197 LGISPSKPDHDGNTPLHIVCSKtvKNVDIINLLL 230
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 161-190 3.86e-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: 3.86e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 568953835   161 KGFTPLYMAAQENHLEVVKFLLENGANQNV 190
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 257-284 3.86e-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: 3.86e-04
                           10        20
                   ....*....|....*....|....*...
gi 568953835   257 GFTPLHIAAHYENLNVAQLLLNRGASVN 284
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADIN 29
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 586-615 4.01e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.49  E-value: 4.01e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 568953835    586 KGFTPLHVAAKYGKVRLAELLLEHDAHPNA 615
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 685-711 4.47e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.11  E-value: 4.47e-04
                            10        20
                    ....*....|....*....|....*..
gi 568953835    685 QGVTPLHLAAQEGHTEMVALLLSKQAN 711
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 785-813 4.52e-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: 4.52e-04
                           10        20
                   ....*....|....*....|....*....
gi 568953835   785 GYSPLHQAAQQGHTDIVTLLLKNGASPNE 813
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
65-116 4.83e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.95  E-value: 4.83e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568953835    65 TSFLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELL 116
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 586-712 4.96e-04

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


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 45.23  E-value: 4.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  586 KGFTPLHVAAKYGKVRLAELLLEH--DAHPNAAG----KN-------GLTPLHVAVHHNNLDIVKLLLPRggsPHSPAW- 651
Cdd:cd22197    93 RGHSALHIAIEKRSLQCVKLLVENgaDVHARACGrffqKKqgtcfyfGELPLSLAACTKQWDVVNYLLEN---PHQPASl 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  652 -----NGYTPLH----IA--AKQNQIEVAR---SLLQYGGSANAE-------SVQGVTPLHLAAQEGHTEMVALLLSKQA 710
Cdd:cd22197   170 qaqdsLGNTVLHalvmIAdnSPENSALVIKmydGLLQAGARLCPTvqleeisNHEGLTPLKLAAKEGKIEIFRHILQREF 249


                  ..
gi 568953835  711 NG 712
Cdd:cd22197   250 SG 251
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 142-204 5.01e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 44.20  E-value: 5.01e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568953835  142 DEVVRELVNYGANVNAQSQKG-FTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQ 204
Cdd:PHA02884   83 DDAAKLLIRYGADVNRYAEEAkITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELALM 146
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 652-681 5.50e-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: 5.50e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 568953835   652 NGYTPLHIAAKQNQIEVARSLLQYGGSANA 681
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 355-386 5.75e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.81  E-value: 5.75e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 568953835   355 NGLSPIHMAA-QGDHLDCVRLLLQYNAEIDDIT 386
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 455-483 6.13e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.78  E-value: 6.13e-04
                           10        20
                   ....*....|....*....|....*....
gi 568953835   455 GLTPLHVASFMGHLPIVKNLLQRGASPNV 483
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 620-734 6.37e-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: 6.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  620 GLTPLHVAVHHNNLDIVKLLLPRGGSPHSPA--------------WNGYTPLHIAAKQNQIEVARSLLQYG---GSANAE 682
Cdd:cd22193    76 GQTALHIAIERRQGDIVALLVENGADVHAHAkgrffqpkyqgegfYFGELPLSLAACTNQPDIVQYLLENEhqpADIEAQ 155

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568953835  683 SVQGVTPLHLAAQEGH---------TEMVALLLSKQAN-------GNLGNKSGLTPLHLVSQEGHVPV 734
Cdd:cd22193   156 DSRGNTVLHALVTVADntkentkfvTRMYDMILIRGAKlcptvelEEIRNNDGLTPLQLAAKMGKIEI 223
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 214-315 6.40e-04

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 42.17  E-value: 6.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  214 LINYGTKGKvrlPALHIAARND--DTRTAAVLLQN---DPNPDVlSKTGFTPLHIAAHYENLNVAQLLLNRGA----SVN 284
Cdd:PHA02736   48 VLEYNRHGK---QCVHIVSNPDkaDPQEKLKLLMEwgaDINGKE-RVFGNTPLHIAVYTQNYELATWLCNQPGvnmeILN 123

                          90       100       110
                  ....*....|....*....|....*....|.
gi 568953835  285 FTPQngiTPLHIASRRGNVIMVRLLLDRGAQ 315
Cdd:PHA02736  124 YAFK---TPYYVACERHDAKMMNILRAKGAQ 151
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 388-416 6.57e-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: 6.57e-04
                           10        20
                   ....*....|....*....|....*....
gi 568953835   388 DHLTPLHVAAHCGHHRVAKVLLDKGAKPN 416
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 369-624 9.55e-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: 9.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  369 LDCVRLLLQYNAEIDDITLDhlTPLHVAA---HCGHHRVAKVLLDKGAKPNSRA-----------LNGFTPLHIACKKNH 434
Cdd:cd21882     8 LECLRWYLTDSAYQRGATGK--TCLHKAAlnlNDGVNEAIMLLLEAAPDSGNPKelvnapctdefYQGQTALHIAIENRN 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  435 IRVMELLLKTGASIDAVTESgltplhvASFMGHlpiVKNLLQRGaspnvsnvkvETPLHMAARAGHTEVAKYLLQNKAKA 514
Cdd:cd21882    86 LNLVRLLVENGADVSARATG-------RFFRKS---PGNLFYFG----------ELPLSLAACTNQEEIVRLLLENGAQP 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  515 NAKAKDD---QTPLHCAARIGH---------TGMVKLLLENGASPN-------LATTAGHTPLHTAAREGHVDTALALLE 575
Cdd:cd21882   146 AALEAQDslgNTVLHALVLQADntpensafvCQMYNLLLSYGAHLDptqqleeIPNHQGLTPLKLAAVEGKIVMFQHILQ 225

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568953835  576 KEASQACM------TKKGFTPLHVAA-------KYGKVRLAELLLEHDAHPNAAGKNGLTPL 624
Cdd:cd21882   226 REFSGPYQplsrkfTEWTYGPVTSSLydlseidSWEKNSVLELIAFSKKREARHQMLVQEPL 287
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 322-349 9.62e-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: 38.34  E-value: 9.62e-04
                            10        20
                    ....*....|....*....|....*...
gi 568953835    322 DELTPLHCAARNGHVRISEILLDHGAPI 349
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
PHA02798 PHA02798
ankyrin-like protein; Provisional
 76-318 1.05e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 43.67  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   76 LDKALDHLRNGVDINTCNQNGLNGLHLaskeghvkmvveLLHKEIIletttkkgntalhiaalaGQDEVVRELVNYGANV 155
Cdd:PHA02798   89 LDIVKILIENGADINKKNSDGETPLYC------------LLSNGYI------------------NNLEILLFMIENGADT 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  156 NAQSQKGFTPLYMAAQENH---LEVVKFLLENGANQNV-ATEDGFTPLAVALQQGHE----NVVAHLINYG--------- 218
Cdd:PHA02798  139 TLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINThNNKEKYDTLHCYFKYNIDridaDILKLFVDNGfiinkenks 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  219 TKGKVR--LPALHIAARNDDTRTAAVLLQ--NDPNPDVLsktGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPL 294
Cdd:PHA02798  219 HKKKFMeyLNSLLYDNKRFKKNILDFIFSyiDINQVDEL---GFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCL 295

                         250       260
                  ....*....|....*....|....
gi 568953835  295 HIASRRGNVIMVRLLLDRGAQIET 318
Cdd:PHA02798  296 FTAFENESKFIFNSILNKKPNKNT 319
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 485-608 1.10e-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: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  485 NVKVETPLHMAARAGHTEVAKYLLQNKAKANAKAKDD--------------QTPLHCAARIGHTGMVKLLLENGASP-NL 549
Cdd:cd22194   138 AYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVffnpkykhegfyfgETPLALAACTNQPEIVQLLMEKESTDiTS 217

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568953835  550 ATTAGHTPLH---TAAR--EGHV-------DTALALLEKEASQACMTKKGFTPLHVAAKYGKVRLAELLLE 608
Cdd:cd22194   218 QDSRGNTVLHalvTVAEdsKTQNdfvkrmyDMILLKSENKNLETIRNNEGLTPLQLAAKMGKAEILKYILS 288
Ank_5 pfam13857
Ankyrin repeats (many copies);
83-136 1.29e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.48  E-value: 1.29e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 568953835    83 LRNG-VDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIA 136
Cdd:pfam13857    2 LEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 652-681 1.46e-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: 1.46e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 568953835   652 NGYTPLHIAAKQ-NQIEVARSLLQYGGSANA 681
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNA 31
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 522-674 2.12e-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: 2.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  522 QTPLHCAARIGHTGMVKLLLENGASPNLATTA-------------GHTPLHTAAREGHVDTALALLEKEASQACMTKK-- 586
Cdd:cd22197    95 HSALHIAIEKRSLQCVKLLVENGADVHARACGrffqkkqgtcfyfGELPLSLAACTKQWDVVNYLLENPHQPASLQAQds 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  587 -GFTPLHvaakygkvrlAELLLEHDAHPNAAgkngltpLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQ 665
Cdd:cd22197   175 lGNTVLH----------ALVMIADNSPENSA-------LVIKMYDGLLQAGARLCPTVQLEEISNHEGLTPLKLAAKEGK 237


                  ....*....
gi 568953835  666 IEVARSLLQ 674
Cdd:cd22197   238 IEIFRHILQ 246
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 719-750 2.19e-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: 2.19e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 568953835   719 GLTPLHL-VSQEGHVPVADVLIKHGVTVDATTR 750
Cdd:pfam00023    2 GNTPLHLaAGRRGNLEIVKLLLSKGADVNARDK 34
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 257-395 2.43e-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: 2.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  257 GFTPLHIAAHYENLNVAQLLLNRGASVN-------FTPQN-------GITPLHIASRRGNVIMVRLLLDRGAQIETrTKD 322
Cdd:cd22194   141 GQTALNIAIERRQGDIVKLLIAKGADVNahakgvfFNPKYkhegfyfGETPLALAACTNQPEIVQLLMEKESTDIT-SQD 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  323 EL--TPLHC---AARNGHVRIS-------EILLDHGAPIQAKTKN--GLSPIHMAAQGDHLDCVRLLLqyNAEIDDITLD 388
Cdd:cd22194   220 SRgnTVLHAlvtVAEDSKTQNDfvkrmydMILLKSENKNLETIRNneGLTPLQLAAKMGKAEILKYIL--SREIKEKPNR 297


                  ....*..
gi 568953835  389 HLTPLHV 395
Cdd:cd22194   298 SLSRKFT 304
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 89-223 2.43e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 40.63  E-value: 2.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   89 INTCNQN--GLNGLHLASKEGHVkmvVELL-HKEIILETT-------TKKGNTALHIAALAGQ---DEVVRELVNYGANV 155
Cdd:PHA02736    8 IFASEPDieGENILHYLCRNGGV---TDLLaFKNAISDENrylvleyNRHGKQCVHIVSNPDKadpQEKLKLLMEWGADI 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  156 NAQSQK-GFTPLYMAAQENHLEVVKFLLEN-GANQNVATEDGFTPLAVALQQGHENVVAHLINYGTKGKV 223
Cdd:PHA02736   85 NGKERVfGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGAQCKV 154
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 763-866 2.49e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 42.64  E-value: 2.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  763 GNIKLVKFLLQHQAD-VNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIAKRLGyisVTDVLKVVT 841
Cdd:PHA02874   12 GDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIG---AHDIIKLLI 88

                          90       100
                  ....*....|....*....|....*...
gi 568953835  842 D---ETSVVLVSDKHRmsypETVDEILD 866
Cdd:PHA02874   89 DngvDTSILPIPCIEK----DMIKTILD 112
PHA02791 PHA02791
ankyrin-like protein; Provisional
 550-745 3.48e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 41.57  E-value: 3.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  550 ATTAGHTPLHTAAREGHVDTALALLEKEASQACMTKKgfTPLHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVH 629
Cdd:PHA02791   26 ADVHGHSALYYAIADNNVRLVCTLLNAGALKNLLENE--FPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVD 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  630 HNNLDIVKLLLPRGGSPHSPAWNGY-TPLHIAAKQNQIEVARSLLQYGGSANAESVQgVTPLHLAAQEGHTEMVALLLSK 708
Cdd:PHA02791  104 SGNMQTVKLFVKKNWRLMFYGKTGWkTSFYHAVMLNDVSIVSYFLSEIPSTFDLAIL-LSCIHITIKNGHVDMMILLLDY 182

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 568953835  709 QANGNLGNKSGLTP-LHLVSQEGHVPVADVLIKHGVTV 745
Cdd:PHA02791  183 MTSTNTNNSLLFIPdIKLAIDNKDLEMLQALFKYDINI 220
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 490-509 3.88e-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: 3.88e-03
                            10        20
                    ....*....|....*....|
gi 568953835    490 TPLHMAARAGHTEVAKYLLQ 509
Cdd:smart00248    4 TPLHLAAENGNLEVVKLLLD 23
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 143-218 4.31e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 40.57  E-value: 4.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  143 EVVRELVNYGANVNAQSQ-KGFTPL--YMAAQEN-HLEVVKFLLENGANQNVATEDGFTPLAVALQQGHEN--VVAHLIN 216
Cdd:PHA02859   67 EILKFLIENGADVNFKTRdNNLSALhhYLSFNKNvEPEILKILIDSGSSITEEDEDGKNLLHMYMCNFNVRinVIKLLID 146


                  ..
gi 568953835  217 YG 218
Cdd:PHA02859  147 SG 148
PHA02791 PHA02791
ankyrin-like protein; Provisional
 652-816 4.82e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 41.18  E-value: 4.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  652 NGYTPLHIAAKQNQIEVARSLLQYGGSANAesVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGH 731
Cdd:PHA02791   29 HGHSALYYAIADNNVRLVCTLLNAGALKNL--LENEFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGN 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  732 VPVADVLIKHGVTVDATTRMGY-TPLHVASHYGNIKLVKFLLqhqADVNAKTKLG--YSPLHQAAQQGHTDIVTLLLKNG 808
Cdd:PHA02791  107 MQTVKLFVKKNWRLMFYGKTGWkTSFYHAVMLNDVSIVSYFL---SEIPSTFDLAilLSCIHITIKNGHVDMMILLLDYM 183


                  ....*...
gi 568953835  809 ASPNEVSS 816
Cdd:PHA02791  184 TSTNTNNS 191
PHA02795 PHA02795
ankyrin-like protein; Provisional
 737-831 5.07e-03

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 41.52  E-value: 5.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  737 VLIKHGVTVDATTRMGYTPLHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNEVSS 816
Cdd:PHA02795  173 IPDENDVKLDLYKIIQYTRGFLVDEPTVLEIYKLCIPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMS 252

                          90
                  ....*....|....*
gi 568953835  817 NGTTPLAIAKRLGYI 831
Cdd:PHA02795  253 NGYTCLDVAVDRGSV 267
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 734-825 5.18e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.78  E-value: 5.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  734 VADVLIKHGVTvDATTRMGYTPLHVAShYGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNE 813
Cdd:PLN03192  509 VGDLLGDNGGE-HDDPNMASNLLTVAS-TGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHI 586

                          90
                  ....*....|....
gi 568953835  814 VSSNGTTPL--AIA 825
Cdd:PLN03192  587 RDANGNTALwnAIS 600
PHA02741 PHA02741
hypothetical protein; Provisional
 93-210 6.44e-03

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 39.64  E-value: 6.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835   93 NQNGLNGLHLASKEGHVKMVVELL------HKEIILETTTKKGNTALHIAALAGQD----EVVRELVNYGANVNAQ-SQK 161
Cdd:PHA02741   18 NSEGENFFHEAARCGCFDIIARFTpfirgdCHAAALNATDDAGQMCIHIAAEKHEAqlaaEIIDHLIELGADINAQeMLE 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 568953835  162 GFTPLYMAAQENHLEVVKFLL-ENGANQNVATEDGFTPLAVAlqQGHENV 210
Cdd:PHA02741   98 GDTALHLAAHRRDHDLAEWLCcQPGIDLHFCNADNKSPFELA--IDNEDV 145
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 389-463 6.82e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 40.74  E-value: 6.82e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568953835  389 HLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNG-FTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVAS 463
Cdd:PHA02884   70 KTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAkITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELAL 145
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 124-312 7.65e-03

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


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 40.99  E-value: 7.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  124 TTTKKGNTALHIAALAGQD----------EVVRELVNYGANVNAQSQ----KGFTPLYMAAQENHLEVVKFLLENGANQN 189
Cdd:cd22197    42 TEGSTGKTCLMKAVLNLQDgvnacimpllEIDKDSGNPKPLVNAQCTdeyyRGHSALHIAIEKRSLQCVKLLVENGADVH 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  190 VATEDGFTplavalqQGHENVVAHlinYGtkgkvRLPaLHIAARNDDTRTAAVLLQNDPNPDVLSKT---GFTPLH---- 262
Cdd:cd22197   122 ARACGRFF-------QKKQGTCFY---FG-----ELP-LSLAACTKQWDVVNYLLENPHQPASLQAQdslGNTVLHalvm 185

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568953835  263 IAAHYENlNVAQL------LLNRGASVNFTPQ-------NGITPLHIASRRGNVIMVRLLLDR 312
Cdd:cd22197   186 IADNSPE-NSALVikmydgLLQAGARLCPTVQleeisnhEGLTPLKLAAKEGKIEIFRHILQR 247
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 355-383 8.30e-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: 8.30e-03
                           10        20
                   ....*....|....*....|....*....
gi 568953835   355 NGLSPIHMAAQGDHLDCVRLLLQYNAEID 383
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 404-481 8.95e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 39.80  E-value: 8.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  404 VAKVLLDKGAKPNSRAL-NGFTPLH--IACKKN-HIRVMELLLKTGASIDAVTESGLTPLHV--ASFMGHLPIVKNLLQR 477
Cdd:PHA02859   68 ILKFLIENGADVNFKTRdNNLSALHhyLSFNKNvEPEILKILIDSGSSITEEDEDGKNLLHMymCNFNVRINVIKLLIDS 147


                  ....
gi 568953835  478 GASP 481
Cdd:PHA02859  148 GVSF 151
PHA02946 PHA02946
ankyin-like protein; Provisional
 328-494 9.61e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 40.81  E-value: 9.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  328 HCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQYNAEIDDITLDHLTPLHVAAHCGHHRVAKV 407
Cdd:PHA02946   44 YCGIKGLDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIERI 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953835  408 --LLDKGAK-PNSRALNGFTPLhIACKKNHIRVMELLLKTGASIDAVTESGLTPLHvASFMGHLP---IVKNLLQRGASP 481
Cdd:PHA02946  124 nlLVQYGAKiNNSVDEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFGKNHIH-RHLMSDNPkasTISWMMKLGISP 201

                         170
                  ....*....|...
gi 568953835  482 NVSNVKVETPLHM 494
Cdd:PHA02946  202 SKPDHDGNTPLHI 214
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH