NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|160707911|ref|NP_112435|]
View 

ankyrin-1 isoform 2 [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 ...
 1248-1377 4.06e-67

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


:

Pssm-ID: 375346  Cd Length: 131  Bit Score: 222.35  E-value: 4.06e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  1248 VPYMAKFVIFAKMNDAREGRLRCYCMTDDKVDKTLEQHENFVEVARSRDIEVLEGMPLFAELSGNLVPVKKAAQQRSFHF 1327
Cdd:pfam17809    1 VPYLAKFVVFAKRYDPGEARLRCACMTDDGEDKTLEFHEGFTEVARSRDVEVLEGSPVSIELSGNLVPIKKKSQSRQMDF 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 160707911  1328 QSFRENRLAIPVKVRDSSREPGGFLSFLRKTMKYEDTQH-ILCHLNITMPP 1377
Cdd:pfam17809   81 KAFRENRLDGSVRVKDPSDPPKGLLSFMRDAKVDGGTVSqPLCTLNIVLPQ 131
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
180-445 5.08e-57

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 199.80  E-value: 5.08e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  180 ALHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMV 259
Cdd:COG0666    24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIV 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  260 RLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQYNAEIDDIT 339
Cdd:COG0666   104 KLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  340 LDHLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMG 419
Cdd:COG0666   184 NDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAG 263

                         250       260
                  ....*....|....*....|....*.
gi 160707911  420 HLPIVKNLLQRGASPNVSNVKVETPL 445
Cdd:COG0666   264 AALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
523-791 5.33e-57

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 199.80  E-value: 5.33e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  523 ALALLEKEASQACMTKKGFTPLHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSP 602
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  603 AWNGYTPLHIAAKQNQIEVARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQE 682
Cdd:COG0666    84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  683 GHVPVADVLIKHGVTVDATTRMGYTPLHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGA 762
Cdd:COG0666   164 GNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243

                         250       260
                  ....*....|....*....|....*....
gi 160707911  763 SPNEVSSNGTTPLAIAKRLGYISVTDVLK 791
Cdd:COG0666   244 DLNAKDKDGLTALLLAAAAGAALIVKLLL 272
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
11-310 1.00e-53

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 190.55  E-value: 1.00e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   11 DPAADAATSFLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAA 90
Cdd:COG0666    16 LLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   91 LAGQDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPlavalqqghenvvahliny 170
Cdd:COG0666    96 RNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTP------------------- 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  171 gtkgkvrlpaLHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIA 250
Cdd:COG0666   157 ----------LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLA 226

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  251 SRRGNVIMVRLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILLDHGAPIQAKTKNGL 310
Cdd:COG0666   227 AENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLL 286
Death_ank1 cd08805
Death domain of Ankyrin-1; Death Domain (DD) of the human protein ankyrin-1 (ANK-1) and ...
 1413-1496 5.18e-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: 174.39  E-value: 5.18e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911 1413 DRVEMRMAVIREHLGLSWAELARELQFSVEDINRIRVENPNSLLDQSTALLTLWVDREGENAKMENLYTALRNIDRSEIV 1492
Cdd:cd08805     1 ERVEMKMAVIREHLGLSWAELARELQFSVEDINRIRVENPNSLLEQSTALLNLWVDREGENAKMEPLYPALYSIDRLTIV 80


                  ....
gi 160707911 1493 NMLE 1496
Cdd:cd08805    81 NILE 84
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
 923-1027 3.00e-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: 3.00e-49
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911    923 TGFLVSFMVDARGGSMRGSRhNGLRVVIPPRTCAAPTRITCRLVKPQKLNTPPPLAEEEGLASRIIALGPTGAQFLSPVI 1002
Cdd:smart00218    1 PSFLVSGTFDARGGRLRGPR-TGVRLIIPPGAIPQGTRYTCYLVVHKTLSTPPPLEEGETLLSPVVECGPHGALFLRPVI 79

                            90       100
                    ....*....|....*....|....*
gi 160707911   1003 VEIPHFASHGRGDRELVVLRSENGS 1027
Cdd:smart00218   80 LEVPHCASLRPRDWEIVLLRSENGG 104
Ank_2 pfam12796
Ankyrin repeats (3 copies);
412-502 1.03e-22

Ankyrin repeats (3 copies);


:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 94.03  E-value: 1.03e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   412 LHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQnkAKANAKAKDDQTPLHCAARIGHTGMVK 491
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE--HADVNLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|.
gi 160707911   492 LLLENGASPNL 502
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 ...
 1248-1377 4.06e-67

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


Pssm-ID: 375346  Cd Length: 131  Bit Score: 222.35  E-value: 4.06e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  1248 VPYMAKFVIFAKMNDAREGRLRCYCMTDDKVDKTLEQHENFVEVARSRDIEVLEGMPLFAELSGNLVPVKKAAQQRSFHF 1327
Cdd:pfam17809    1 VPYLAKFVVFAKRYDPGEARLRCACMTDDGEDKTLEFHEGFTEVARSRDVEVLEGSPVSIELSGNLVPIKKKSQSRQMDF 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 160707911  1328 QSFRENRLAIPVKVRDSSREPGGFLSFLRKTMKYEDTQH-ILCHLNITMPP 1377
Cdd:pfam17809   81 KAFRENRLDGSVRVKDPSDPPKGLLSFMRDAKVDGGTVSqPLCTLNIVLPQ 131
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
180-445 5.08e-57

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 199.80  E-value: 5.08e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  180 ALHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMV 259
Cdd:COG0666    24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIV 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  260 RLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQYNAEIDDIT 339
Cdd:COG0666   104 KLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  340 LDHLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMG 419
Cdd:COG0666   184 NDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAG 263

                         250       260
                  ....*....|....*....|....*.
gi 160707911  420 HLPIVKNLLQRGASPNVSNVKVETPL 445
Cdd:COG0666   264 AALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
523-791 5.33e-57

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 199.80  E-value: 5.33e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  523 ALALLEKEASQACMTKKGFTPLHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSP 602
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  603 AWNGYTPLHIAAKQNQIEVARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQE 682
Cdd:COG0666    84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  683 GHVPVADVLIKHGVTVDATTRMGYTPLHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGA 762
Cdd:COG0666   164 GNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243

                         250       260
                  ....*....|....*....|....*....
gi 160707911  763 SPNEVSSNGTTPLAIAKRLGYISVTDVLK 791
Cdd:COG0666   244 DLNAKDKDGLTALLLAAAAGAALIVKLLL 272
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
11-310 1.00e-53

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 190.55  E-value: 1.00e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   11 DPAADAATSFLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAA 90
Cdd:COG0666    16 LLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   91 LAGQDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPlavalqqghenvvahliny 170
Cdd:COG0666    96 RNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTP------------------- 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  171 gtkgkvrlpaLHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIA 250
Cdd:COG0666   157 ----------LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLA 226

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  251 SRRGNVIMVRLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILLDHGAPIQAKTKNGL 310
Cdd:COG0666   227 AENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLL 286
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
325-596 1.07e-52

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 187.47  E-value: 1.07e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  325 VRLLLQYNAEIDDITLDHLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAV 404
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  405 TESGLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKAKANAKAKDDQTPLHCAARI 484
Cdd:COG0666    84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  485 GHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALLEKEASQACMTKKGFTPLHVAAKYGKVRLAELLLEHDA 564
Cdd:COG0666   164 GNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243

                         250       260       270
                  ....*....|....*....|....*....|..
gi 160707911  565 HPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRG 596
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 ...
 1413-1496 5.18e-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: 174.39  E-value: 5.18e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911 1413 DRVEMRMAVIREHLGLSWAELARELQFSVEDINRIRVENPNSLLDQSTALLTLWVDREGENAKMENLYTALRNIDRSEIV 1492
Cdd:cd08805     1 ERVEMKMAVIREHLGLSWAELARELQFSVEDINRIRVENPNSLLEQSTALLNLWVDREGENAKMEPLYPALYSIDRLTIV 80


                  ....
gi 160707911 1493 NMLE 1496
Cdd:cd08805    81 NILE 84
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
 923-1027 3.00e-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: 3.00e-49
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911    923 TGFLVSFMVDARGGSMRGSRhNGLRVVIPPRTCAAPTRITCRLVKPQKLNTPPPLAEEEGLASRIIALGPTGAQFLSPVI 1002
Cdd:smart00218    1 PSFLVSGTFDARGGRLRGPR-TGVRLIIPPGAIPQGTRYTCYLVVHKTLSTPPPLEEGETLLSPVVECGPHGALFLRPVI 79

                            90       100
                    ....*....|....*....|....*
gi 160707911   1003 VEIPHFASHGRGDRELVVLRSENGS 1027
Cdd:smart00218   80 LEVPHCASLRPRDWEIVLLRSENGG 104
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 550-763 1.89e-39

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 153.28  E-value: 1.89e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  550 YGKVRLAELLLEHDAHPNAAG-----KNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQI----- 619
Cdd:PHA03100    7 LTKSRIIKVKNIKYIIMEDDLndysyKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvk 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  620 EVARSLLQYGGSANAESVQGVTPLHLAAQE--GHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHV--PVADVLIKHG 695
Cdd:PHA03100   87 EIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKG 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  696 VTVDATTR----------------MGYTPLHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLK 759
Cdd:PHA03100  167 VDINAKNRvnyllsygvpinikdvYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLN 246


                  ....
gi 160707911  760 NGAS 763
Cdd:PHA03100  247 NGPS 250
ZU5 pfam00791
ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.
 927-1024 2.76e-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: 2.76e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   927 VSFMVDARGGSMRGSrHNGLRVVIPPRTCAAPTRITCRLVKPQKLNTPPPLAEEEGLASRIIALGPTGAQFLSPVIVEIP 1006
Cdd:pfam00791    1 VSGLVDSRGGRLVLP-NSGVSLLIPPGAIPEGTRIECYLAVNRDESSRPPLEEGETLLSPVVECGPPGLKFLKPVILEVP 79

                           90
                   ....*....|....*...
gi 160707911  1007 HFASHGRGDRELVVLRSE 1024
Cdd:pfam00791   80 HCASLRPEEWEIVLKRSD 97
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 94-439 9.17e-37

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 149.83  E-value: 9.17e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   94 QDE--VVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLI-NY 170
Cdd:PHA02876  155 QDEllIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIdNR 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  171 GTKGKVRLPALHiAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLN-VAQLLLNRGASVNFTPQNGITPLHI 249
Cdd:PHA02876  235 SNINKNDLSLLK-AIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYL 313

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  250 ASRRG-NVIMVRLLLDRGAQIETRTKDELTPLHCAA---RNGHVRISeiLLDHGAPIQAKTKNGLSPIHMAAQGDHLDCV 325
Cdd:PHA02876  314 MAKNGyDTENIRTLIMLGADVNAADRLYITPLHQAStldRNKDIVIT--LLELGANVNARDYCDKTPIHYAAVRNNVVII 391

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  326 RLLLQYNAEIDDITLDHLTPLHVAAhCGH--HRVAKVLLDKGAKPNSRALNGFTPLHIACKKN-HIRVMELLLKTGASID 402
Cdd:PHA02876  392 NTLLDYGADIEALSQKIGTALHFAL-CGTnpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVN 470

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 160707911  403 AVTESGLTPLHVAsfMGHLPIVKNLLQRGASPNVSNV 439
Cdd:PHA02876  471 AINIQNQYPLLIA--LEYHGIVNILLHYGAELRDSRV 505
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 53-271 2.76e-29

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 122.85  E-value: 2.76e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   53 LHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQD-----EVVRELVNYGANVNAQSQKGFTPLYMAAQE-- 125
Cdd:PHA03100   39 LYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKks 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  126 NHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHE--NVVAHLINYGT----KGKVRLpalhiaarnddtrtaavLLQN 199
Cdd:PHA03100  119 NSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVdinaKNRVNY-----------------LLSY 181

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 160707911  200 DPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLDRGAQIET 271
Cdd:PHA03100  182 GVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 386-596 8.55e-24

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 106.23  E-value: 8.55e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  386 NHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKA 465
Cdd:PHA02875   13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  466 -KANAKAKDDQTPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALLEKEASQACMTKKGFTPL 544
Cdd:PHA02875   93 fADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPL 172

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 160707911  545 HVAAKYGKVRLAELLLEHDAHPNAAGKNG-LTPLHVAVHHNNLDIVKLLLPRG 596
Cdd:PHA02875  173 IIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRG 225
Ank_2 pfam12796
Ankyrin repeats (3 copies);
412-502 1.03e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 94.03  E-value: 1.03e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   412 LHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQnkAKANAKAKDDQTPLHCAARIGHTGMVK 491
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE--HADVNLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|.
gi 160707911   492 LLLENGASPNL 502
Cdd:pfam12796   79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
53-143 2.08e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 93.26  E-value: 2.08e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911    53 LHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQDEVVRELVNYgANVNAQSQkGFTPLYMAAQENHLEVVK 132
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                           90
                   ....*....|.
gi 160707911   133 FLLENGANQNV 143
Cdd:pfam12796   79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
478-568 3.26e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.49  E-value: 3.26e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   478 LHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALLEKEASQacMTKKGFTPLHVAAKYGKVRLAE 557
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN--LKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|.
gi 160707911   558 LLLEHDAHPNA 568
Cdd:pfam12796   79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
346-438 4.90e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.10  E-value: 4.90e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   346 LHVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASidAVTESGLTPLHVASFMGHLPIVK 425
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 160707911   426 NLLQRGASPNVSN 438
Cdd:pfam12796   79 LLLEKGADINVKD 91
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
 1412-1498 3.96e-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: 89.39  E-value: 3.96e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   1412 TDRVEMRMAVIREH-LGLSWAELARELQFSVEDINRIRVENPNSLLDQSTALLTLWVDREGENAKMENLYTALRNIDRSE 1490
Cdd:smart00005    1 PELTRQKLAKLLDHpLGLDWRELARKLGLSEADIDQIRTEAPRDLAEQSVQLLRLWEQREGKNATLGTLLEALRKMGRDD 80


                    ....*...
gi 160707911   1491 IVNMLEGS 1498
Cdd:smart00005   81 AVELLRSE 88
Death pfam00531
Death domain;
1416-1496 1.57e-19

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 84.72  E-value: 1.57e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  1416 EMRMAVIREH---LGLSWAELARELQFSVEDINRIRVENPNsLLDQSTALLTLWVDREGENAKMENLYTALRNIDRSEIV 1492
Cdd:pfam00531    1 RKQLDRLLDPpppLGKDWRELARKLGLSENEIDEIESENPR-LRSQTYELLRLWEQREGKNATVGTLLEALRKLGRRDAA 79


                   ....
gi 160707911  1493 NMLE 1496
Cdd:pfam00531   80 EKIQ 83
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 509-685 3.04e-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: 3.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  509 TPLHTAAREGHVDTALALLEKEASQACMTKK-GFTPLHVAAKYGKVRLAELLLEhdAHPNAAGK-------NGLTPLHVA 580
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGAlGETALHVAALYDNLEAAVVLME--AAPELVNEpmtsdlyQGETALHIA 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  581 VHHNNLDIVKLLLPRGG--------------SPHSPAWNGYTPLHIAAKQNQIEVARSLLQYGGSANAESVQGVTPLH-L 645
Cdd:cd22192    97 VVNQNLNLVRELIARGAdvvspratgtffrpGPKNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHiL 176

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 160707911  646 AAQEGHT---EMVALLLSKQANGNLG------NKSGLTPLHLVSQEGHV 685
Cdd:cd22192   177 VLQPNKTfacQMYDLILSYDKEDDLQpldlvpNNQGLTPFKLAAKEGNI 225
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 181-350 8.20e-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: 86.22  E-value: 8.20e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  181 LHIAARNDDTRTAAVLLQNdPNPDVLSK--TGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQN-----GITPLHIASRR 253
Cdd:cd22192    21 LLLAAKENDVQAIKKLLKC-PSCDLFQRgaLGETALHVAALYDNLEAAVVLMEAAPELVNEPMTsdlyqGETALHIAVVN 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  254 GNVIMVRLLLDRGAQIET---------RTKDELT-----PLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAA-- 317
Cdd:cd22192   100 QNLNLVRELIARGADVVSpratgtffrPGPKNLIyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVlq 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 160707911  318 QGDHLDC--VRLLLQYNAEIDDITLDH------LTPLHVAA 350
Cdd:cd22192   180 PNKTFACqmYDLILSYDKEDDLQPLDLvpnnqgLTPFKLAA 220
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 81-232 8.34e-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: 8.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   81 KGNTALHIAALAGQDEVVRELVNYGANVNAQSQKGF--------------TPLYMAAQENHLEVVKFLLENGANqNVATE 146
Cdd:cd22194   140 EGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVFfnpkykhegfyfgeTPLALAACTNQPEIVQLLMEKEST-DITSQ 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  147 DGFTplavalqqgheNVVAHlinygtkgkvrlpALHIAARNDDTRTAAV------LLQNDPNPD---VLSKTGFTPLHIA 217
Cdd:cd22194   219 DSRG-----------NTVLH-------------ALVTVAEDSKTQNDFVkrmydmILLKSENKNletIRNNEGLTPLQLA 274

                         170
                  ....*....|....*
gi 160707911  218 AHYENLNVAQLLLNR 232
Cdd:cd22194   275 AKMGKAEILKYILSR 289
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 377-560 2.76e-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: 2.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  377 TPLHIACKKNHIRVMELLLKTgASIDAVTESGL--TPLHVASFMGHLPIVKNLLQrgASPNVSNVKV-------ETPLHM 447
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKC-PSCDLFQRGALgeTALHVAALYDNLEAAVVLME--AAPELVNEPMtsdlyqgETALHI 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  448 AARAGHTEVAKYLLQNKAkanakakDDQTP---------------------LHCAARIGHTGMVKLLLENGASPNLATTA 506
Cdd:cd22192    96 AVVNQNLNLVRELIARGA-------DVVSPratgtffrpgpknliyygehpLSFAACVGNEEIVRLLIEHGADIRAQDSL 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 160707911  507 GHTPLH------TAAREGHVDTALALLEKEASQACM----TKKGFTPLHVAAKYGKVRLAELLL 560
Cdd:cd22192   169 GNTVLHilvlqpNKTFACQMYDLILSYDKEDDLQPLdlvpNNQGLTPFKLAAKEGNIVMFQHLV 232
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 110-330 1.28e-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: 1.28e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   110 AQSQKGFTPlymAAQENHLEVVKFLLENGA--NQNVATEDGFTPLAVALQQG-HENVVAHLINYGTKGKVRLPALHIAAR 186
Cdd:TIGR00870   15 SDEEKAFLP---AAERGDLASVYRDLEEPKklNINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAVGDTLLHAISL 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   187 ND--------------DTRTAAVLLQNDPNPDVLSKtGFTPLHIAAHYENLNVAQLLLNRGASVN-------FTPQNGIT 245
Cdd:TIGR00870   92 EYvdaveaillhllaaFRKSGPLELANDQYTSEFTP-GITALHLAAHRQNYEIVKLLLERGASVParacgdfFVKSQGVD 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   246 -------PLHIASRRGNVIMVRLLLDRGAQIETRtkDEL--TPLHCA-------ARNGHVRIS--EILLDHGAPIQAKTK 307
Cdd:TIGR00870  171 sfyhgesPLNAAACLGSPSIVALLSEDPADILTA--DSLgnTLLHLLvmenefkAEYEELSCQmyNFALSLLDKLRDSKE 248

                          250       260       270
                   ....*....|....*....|....*....|
gi 160707911   308 -------NGLSPIHMAAQGDHLDCVRLLLQ 330
Cdd:TIGR00870  249 levilnhQGLTPLKLAAKEGRIVLFRLKLA 278
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 617-779 3.91e-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: 3.91e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   617 NQIEVARSLLQYGGSANAESVQ-------GVTPLHLAAQEG-HTEMVALLLSKQANGNLGNksglTPLHLVSQEGHVPVA 688
Cdd:TIGR00870   23 PAAERGDLASVYRDLEEPKKLNincpdrlGRSALFVAAIENeNLELTELLLNLSCRGAVGD----TLLHAISLEYVDAVE 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   689 DVLI-------KHGVTVDATTRM------GYTPLHVASHYGNIKLVKFLLQHQADVNAKTK--------------LGYSP 741
Cdd:TIGR00870   99 AILLhllaafrKSGPLELANDQYtseftpGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESP 178

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 160707911   742 LHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIAK 779
Cdd:TIGR00870  179 LNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLV 216
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 391-544 6.49e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 61.04  E-value: 6.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  391 MELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKAKANAK 470
Cdd:PLN03192  541 LEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPH 620

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160707911  471 AKDDqtpLHC-AARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALLEKEASQACM-TKKGFTPL 544
Cdd:PLN03192  621 AAGD---LLCtAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAnTDDDFSPT 693
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 20-297 6.34e-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: 6.34e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911    20 FLRAARSGNLDKALDHLRNG--VDINTCNQNGLNGLHLASKEGHVKMVVELLHKeiiLETTTKKGNTALHIAALAGQDeV 97
Cdd:TIGR00870   21 FLPAAERGDLASVYRDLEEPkkLNINCPDRLGRSALFVAAIENENLELTELLLN---LSCRGAVGDTLLHAISLEYVD-A 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911    98 VRELVNYGAN----------VNAQS----QKGFTPLYMAAQENHLEVVKFLLENGANQNV-ATEDGFTplavaLQQGHEn 162
Cdd:TIGR00870   97 VEAILLHLLAafrksgplelANDQYtsefTPGITALHLAAHRQNYEIVKLLLERGASVPArACGDFFV-----KSQGVD- 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   163 vvahLINYGtkgkvRLPaLHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIA-------AHYENL-----NVAQLLL 230
Cdd:TIGR00870  171 ----SFYHG-----ESP-LNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLvmenefkAEYEELscqmyNFALSLL 240

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 160707911   231 NRGAS-------VNFtpqNGITPLHIASRRGNVIMVRLLLdrgaQIETRTKDeltplHCAARNGHVRISEILLD 297
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 ...
 374-403 9.48e-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: 9.48e-07
                            10        20        30
                    ....*....|....*....|....*....|
gi 160707911    374 NGFTPLHIACKKNHIRVMELLLKTGASIDA 403
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 704-733 1.74e-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: 1.74e-06
                            10        20        30
                    ....*....|....*....|....*....|
gi 160707911    704 MGYTPLHVASHYGNIKLVKFLLQHQADVNA 733
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 114-143 2.65e-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: 45.27  E-value: 2.65e-06
                            10        20        30
                    ....*....|....*....|....*....|
gi 160707911    114 KGFTPLYMAAQENHLEVVKFLLENGANQNV 143
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 473-502 2.41e-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: 42.57  E-value: 2.41e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 160707911    473 DDQTPLHCAARIGHTGMVKLLLENGASPNL 502
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 438-561 1.06e-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: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  438 NVKVETPLHMAARAGHTEVAKYLLQNKAKANAKAKDD--------------QTPLHCAARIGHTGMVKLLLENGASP-NL 502
Cdd:cd22194   138 AYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVffnpkykhegfyfgETPLALAACTNQPEIVQLLMEKESTDiTS 217

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 160707911  503 ATTAGHTPLH---TAAR--EGHV-------DTALALLEKEASQACMTKKGFTPLHVAAKYGKVRLAELLLE 561
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 ...
 1248-1377 4.06e-67

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


Pssm-ID: 375346  Cd Length: 131  Bit Score: 222.35  E-value: 4.06e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  1248 VPYMAKFVIFAKMNDAREGRLRCYCMTDDKVDKTLEQHENFVEVARSRDIEVLEGMPLFAELSGNLVPVKKAAQQRSFHF 1327
Cdd:pfam17809    1 VPYLAKFVVFAKRYDPGEARLRCACMTDDGEDKTLEFHEGFTEVARSRDVEVLEGSPVSIELSGNLVPIKKKSQSRQMDF 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 160707911  1328 QSFRENRLAIPVKVRDSSREPGGFLSFLRKTMKYEDTQH-ILCHLNITMPP 1377
Cdd:pfam17809   81 KAFRENRLDGSVRVKDPSDPPKGLLSFMRDAKVDGGTVSqPLCTLNIVLPQ 131
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
180-445 5.08e-57

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 199.80  E-value: 5.08e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  180 ALHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMV 259
Cdd:COG0666    24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIV 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  260 RLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQYNAEIDDIT 339
Cdd:COG0666   104 KLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  340 LDHLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMG 419
Cdd:COG0666   184 NDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAG 263

                         250       260
                  ....*....|....*....|....*.
gi 160707911  420 HLPIVKNLLQRGASPNVSNVKVETPL 445
Cdd:COG0666   264 AALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
523-791 5.33e-57

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 199.80  E-value: 5.33e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  523 ALALLEKEASQACMTKKGFTPLHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSP 602
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  603 AWNGYTPLHIAAKQNQIEVARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQE 682
Cdd:COG0666    84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  683 GHVPVADVLIKHGVTVDATTRMGYTPLHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGA 762
Cdd:COG0666   164 GNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243

                         250       260
                  ....*....|....*....|....*....
gi 160707911  763 SPNEVSSNGTTPLAIAKRLGYISVTDVLK 791
Cdd:COG0666   244 DLNAKDKDGLTALLLAAAAGAALIVKLLL 272
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
193-478 2.07e-56

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 198.25  E-value: 2.07e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  193 AAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLDRGAQIETR 272
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  273 TKDELTPLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQYNAEIDDITLDHLTPLHVAAHC 352
Cdd:COG0666    84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  353 GHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGA 432
Cdd:COG0666   164 GNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 160707911  433 SPNVSNVKVETPLHMAARAGHTEVAKYLLQNKAKANAKAKDDQTPL 478
Cdd:COG0666   244 DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
223-511 3.41e-56

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 197.48  E-value: 3.41e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  223 LNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILLDHGAPI 302
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  303 QAKTKNGLSPIHMAAQGDHLDCVRLLLQYNAEIDDITLDHLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIA 382
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  383 CKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQ 462
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 160707911  463 NKAKANAKAKDDQTPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPL 511
Cdd:COG0666   241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
388-676 8.27e-56

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 196.33  E-value: 8.27e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  388 IRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKAKA 467
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  468 NAKAKDDQTPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALLEKEASQACMTKKGFTPLHVA 547
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  548 AKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQIEVARSLLQ 627
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 160707911  628 YGGSANAESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPL 676
Cdd:COG0666   241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
125-412 1.80e-55

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 195.56  E-value: 1.80e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  125 ENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLINYGTKGKVRLPALHIAARNDDTRTAAVLLQNDPNPD 204
Cdd:COG0666     2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  205 VLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLDRGAQIETRTKDELTPLHCAA 284
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  285 RNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQYNAEIDDITLDHLTPLHVAAHCGHHRVAKVLLDK 364
Cdd:COG0666   162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 160707911  365 GAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPL 412
Cdd:COG0666   242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
489-775 6.48e-55

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 194.02  E-value: 6.48e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  489 MVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALLEKEASQACMTKKGFTPLHVAAKYGKVRLAELLLEHDAHPNA 568
Cdd:COG0666     3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  569 AGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQIEVARSLLQYGGSANAESVQGVTPLHLAAQ 648
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  649 EGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADVLIKHGVTVDATTRMGYTPLHVASHYGNIKLVKFLLQHQ 728
Cdd:COG0666   163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 160707911  729 ADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPL 775
Cdd:COG0666   243 ADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
291-577 1.41e-54

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 192.86  E-value: 1.41e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  291 ISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQYNAEIDDITLDHLTPLHVAAHCGHHRVAKVLLDKGAKPNS 370
Cdd:COG0666     3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  371 RALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAAR 450
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  451 AGHTEVAKYLLQNKAKANAKAKDDQTPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALLEKE 530
Cdd:COG0666   163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 160707911  531 ASQACMTKKGFTPLHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPL 577
Cdd:COG0666   243 ADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
29-346 1.51e-54

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 192.86  E-value: 1.51e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   29 LDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQDEVVRELVNYGANV 108
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  109 NAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPlavalqqghenvvahlinygtkgkvrlpaLHIAARND 188
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETP-----------------------------LHLAAYNG 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  189 DTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLDRGAQ 268
Cdd:COG0666   132 NLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGAD 211

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 160707911  269 IETRTKDELTPLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQYNAEIDDITLDHLTPL 346
Cdd:COG0666   212 VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
11-310 1.00e-53

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 190.55  E-value: 1.00e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   11 DPAADAATSFLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAA 90
Cdd:COG0666    16 LLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   91 LAGQDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPlavalqqghenvvahliny 170
Cdd:COG0666    96 RNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTP------------------- 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  171 gtkgkvrlpaLHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIA 250
Cdd:COG0666   157 ----------LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLA 226

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  251 SRRGNVIMVRLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILLDHGAPIQAKTKNGL 310
Cdd:COG0666   227 AENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLL 286
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
256-531 2.36e-53

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 189.39  E-value: 2.36e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  256 VIMVRLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQYNAEI 335
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  336 DDITLDHLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVA 415
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  416 SFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKAKANAKAKDDQTPLHCAARIGHTGMVKLLLE 495
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 160707911  496 NGASPNLATTAGHTPLHTAAREGHVDTALALLEKEA 531
Cdd:COG0666   241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALL 276
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
421-695 3.83e-53

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 188.62  E-value: 3.83e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  421 LPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKAKANAKAKDDQTPLHCAARIGHTGMVKLLLENGASP 500
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  501 NLATTAGHTPLHTAAREGHVDTALALLEKEASQACMTKKGFTPLHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVA 580
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  581 VHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQIEVARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVALLLS 660
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 160707911  661 KQANGNLGNKSGLTPLHLVSQEGHVPVADVLIKHG 695
Cdd:COG0666   241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLAL 275
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
455-738 9.81e-53

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 187.47  E-value: 9.81e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  455 EVAKYLLQNKAKANAKAKDDQTPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALLEKEASQA 534
Cdd:COG0666     2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  535 CMTKKGFTPLHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAA 614
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  615 KQNQIEVARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADVLIKH 694
Cdd:COG0666   162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 160707911  695 GVTVDATTRMGYTPLHVASHYGNIKLVKFLLQHQADVNAKTKLG 738
Cdd:COG0666   242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
325-596 1.07e-52

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 187.47  E-value: 1.07e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  325 VRLLLQYNAEIDDITLDHLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAV 404
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  405 TESGLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKAKANAKAKDDQTPLHCAARI 484
Cdd:COG0666    84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  485 GHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALLEKEASQACMTKKGFTPLHVAAKYGKVRLAELLLEHDA 564
Cdd:COG0666   164 GNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243

                         250       260       270
                  ....*....|....*....|....*....|..
gi 160707911  565 HPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRG 596
Cdd:COG0666   244 DLNAKDKDGLTALLLAAAAGAALIVKLLLLAL 275
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
355-643 1.71e-52

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 186.70  E-value: 1.71e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  355 HRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASP 434
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  435 NVSNVKVETPLHMAARAGHTEVAKYLLQNKAKANAKAKDDQTPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTA 514
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  515 AREGHVDTALALLEKEASQACMTKKGFTPLHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLP 594
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 160707911  595 RGGSPHSPAWNGYTPLHIAAKQNQIEVARSLLQYGGSANAESVQGVTPL 643
Cdd:COG0666   241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
555-791 5.03e-52

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 185.54  E-value: 5.03e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  555 LAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQIEVARSLLQYGGSANA 634
Cdd:COG0666     3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  635 ESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADVLIKHGVTVDATTRMGYTPLHVASH 714
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 160707911  715 YGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIAKRLGYISVTDVLK 791
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 ...
 1413-1496 5.18e-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: 174.39  E-value: 5.18e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911 1413 DRVEMRMAVIREHLGLSWAELARELQFSVEDINRIRVENPNSLLDQSTALLTLWVDREGENAKMENLYTALRNIDRSEIV 1492
Cdd:cd08805     1 ERVEMKMAVIREHLGLSWAELARELQFSVEDINRIRVENPNSLLEQSTALLNLWVDREGENAKMEPLYPALYSIDRLTIV 80


                  ....
gi 160707911 1493 NMLE 1496
Cdd:cd08805    81 NILE 84
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
 923-1027 3.00e-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: 3.00e-49
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911    923 TGFLVSFMVDARGGSMRGSRhNGLRVVIPPRTCAAPTRITCRLVKPQKLNTPPPLAEEEGLASRIIALGPTGAQFLSPVI 1002
Cdd:smart00218    1 PSFLVSGTFDARGGRLRGPR-TGVRLIIPPGAIPQGTRYTCYLVVHKTLSTPPPLEEGETLLSPVVECGPHGALFLRPVI 79

                            90       100
                    ....*....|....*....|....*
gi 160707911   1003 VEIPHFASHGRGDRELVVLRSENGS 1027
Cdd:smart00218   80 LEVPHCASLRPRDWEIVLLRSENGG 104
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
13-280 3.04e-48

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 174.76  E-value: 3.04e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   13 AADAATSFLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALA 92
Cdd:COG0666    51 DALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYN 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   93 GQDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLINYGt 172
Cdd:COG0666   131 GNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAG- 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  173 kgkvrlpalhiaarnddtrtaavllqndPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASR 252
Cdd:COG0666   210 ----------------------------ADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAA 261

                         250       260
                  ....*....|....*....|....*...
gi 160707911  253 RGNVIMVRLLLDRGAQIETRTKDELTPL 280
Cdd:COG0666   262 AGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
586-790 2.23e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 152.03  E-value: 2.23e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  586 LDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQIEVARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVALLLSKQANG 665
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  666 NLGNKSGLTPLHLVSQEGHVPVADVLIKHGVTVDATTRMGYTPLHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQA 745
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 160707911  746 AQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIAKRLGYISVTDVL 790
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 550-763 1.89e-39

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 153.28  E-value: 1.89e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  550 YGKVRLAELLLEHDAHPNAAG-----KNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQI----- 619
Cdd:PHA03100    7 LTKSRIIKVKNIKYIIMEDDLndysyKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvk 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  620 EVARSLLQYGGSANAESVQGVTPLHLAAQE--GHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHV--PVADVLIKHG 695
Cdd:PHA03100   87 EIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKG 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  696 VTVDATTR----------------MGYTPLHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLK 759
Cdd:PHA03100  167 VDINAKNRvnyllsygvpinikdvYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLN 246


                  ....
gi 160707911  760 NGAS 763
Cdd:PHA03100  247 NGPS 250
ZU5 pfam00791
ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.
 927-1024 2.76e-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: 2.76e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   927 VSFMVDARGGSMRGSrHNGLRVVIPPRTCAAPTRITCRLVKPQKLNTPPPLAEEEGLASRIIALGPTGAQFLSPVIVEIP 1006
Cdd:pfam00791    1 VSGLVDSRGGRLVLP-NSGVSLLIPPGAIPEGTRIECYLAVNRDESSRPPLEEGETLLSPVVECGPPGLKFLKPVILEVP 79

                           90
                   ....*....|....*...
gi 160707911  1007 HFASHGRGDRELVVLRSE 1024
Cdd:pfam00791   80 HCASLRPEEWEIVLKRSD 97
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 94-439 9.17e-37

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 149.83  E-value: 9.17e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   94 QDE--VVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLI-NY 170
Cdd:PHA02876  155 QDEllIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIdNR 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  171 GTKGKVRLPALHiAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLN-VAQLLLNRGASVNFTPQNGITPLHI 249
Cdd:PHA02876  235 SNINKNDLSLLK-AIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYL 313

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  250 ASRRG-NVIMVRLLLDRGAQIETRTKDELTPLHCAA---RNGHVRISeiLLDHGAPIQAKTKNGLSPIHMAAQGDHLDCV 325
Cdd:PHA02876  314 MAKNGyDTENIRTLIMLGADVNAADRLYITPLHQAStldRNKDIVIT--LLELGANVNARDYCDKTPIHYAAVRNNVVII 391

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  326 RLLLQYNAEIDDITLDHLTPLHVAAhCGH--HRVAKVLLDKGAKPNSRALNGFTPLHIACKKN-HIRVMELLLKTGASID 402
Cdd:PHA02876  392 NTLLDYGADIEALSQKIGTALHFAL-CGTnpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVN 470

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 160707911  403 AVTESGLTPLHVAsfMGHLPIVKNLLQRGASPNVSNV 439
Cdd:PHA02876  471 AINIQNQYPLLIA--LEYHGIVNILLHYGAELRDSRV 505
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 196-433 6.18e-34

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 136.72  E-value: 6.18e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  196 LLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVI-----MVRLLLDRGAQIE 270
Cdd:PHA03100   21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLtdvkeIVKLLLEYGANVN 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  271 TRTKDELTPLHCAARN--GHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDH--LDCVRLLLQYNAEIDDITldhltpl 346
Cdd:PHA03100  101 APDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKN------- 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  347 hvaahcghhRVaKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKN 426
Cdd:PHA03100  174 ---------RV-NYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKL 243


                  ....*..
gi 160707911  427 LLQRGAS 433
Cdd:PHA03100  244 LLNNGPS 250
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 244-462 3.61e-33

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 134.41  E-value: 3.61e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  244 ITPLHIASRRGNVIMVRLLLDRGAQIETRTKDELTPLHCAARNGHV-----RISEILLDHGAPIQAKTKNGLSPIHMAAQ 318
Cdd:PHA03100   36 VLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAIS 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  319 G--DHLDCVRLLLQYNAEIDDITLDHLTPLHVAAHCGHH--RVAKVLLDKGAKPNsralngftplhiacKKNHIrvmELL 394
Cdd:PHA03100  116 KksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDIN--------------AKNRV---NYL 178

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 160707911  395 LKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQ 462
Cdd:PHA03100  179 LSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLN 246
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 196-404 1.12e-32

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 133.25  E-value: 1.12e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  196 LLQNDPNPDVLSKTGFTPLHIAAHY-----ENLNVAQLLLNRGASVNFTPQNGITPLHIAS--RRGNVIMVRLLLDRGAQ 268
Cdd:PHA03100   54 LLDNGADINSSTKNNSTPLHYLSNIkynltDVKEIVKLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGAN 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  269 IETRTKDELTPLHCAARNGHV--RISEILLDHGAPIQAKTKnglspihmaaqgdhldcVRLLLQYNAEIDDITLDHLTPL 346
Cdd:PHA03100  134 VNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKDVYGFTPL 196

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 160707911  347 HVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAV 404
Cdd:PHA03100  197 HYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTI 254
PHA03095 PHA03095
ankyrin-like protein; Provisional
 120-418 1.13e-32

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 134.00  E-value: 1.13e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  120 YMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVvahlinygtKGKVRLpalhiaarnddtrtaavLLQN 199
Cdd:PHA03095   19 LLNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKV---------KDIVRL-----------------LLEA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  200 DPNPDVLSKTGFTPLHIAAHYEN-LNVAQLLLNRGASVNFTPQNGITPLHI--ASRRGNVIMVRLLLDRGAQIETRTKDE 276
Cdd:PHA03095   73 GADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYG 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  277 LTPLHCAARNGHVRIS--EILLDHGAPIQAKTKNGLSPIHMAAQG--DHLDCVRLLLQYNAEIDDITLDHLTPLHVAAHC 352
Cdd:PHA03095  153 MTPLAVLLKSRNANVEllRLLIDAGADVYAVDDRFRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSMATG 232

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 160707911  353 GHHRVAKV--LLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLhvaSFM 418
Cdd:PHA03095  233 SSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL---SLM 297
PHA03095 PHA03095
ankyrin-like protein; Provisional
 223-529 1.05e-31

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 131.30  E-value: 1.05e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  223 LNVAQLLLNRGASVNFTPQNGITPLHIASRRGN---VIMVRLLLDRGAQIETRTKDELTPLHCAARNGHV-RISEILLDH 298
Cdd:PHA03095   27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKA 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  299 GAPIQAKTKNGLSPIHMAAQGD--HLDCVRLLLQYNAEIDDITLDHLTPLHVaaHCGHHRVA----KVLLDKGAKPNSRA 372
Cdd:PHA03095  107 GADVNAKDKVGRTPLHVYLSGFniNPKVIRLLLRKGADVNALDLYGMTPLAV--LLKSRNANvellRLLIDAGADVYAVD 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  373 LNGFTPLHIACKKNHIR--VMELLLKTGASIDAVTESGLTPLHVASFMGHL--PIVKNLLQRGASPNVSNVKVETPLHMA 448
Cdd:PHA03095  185 DRFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATGSSCkrSLVLPLLIAGISINARNRYGQTPLHYA 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  449 ARAGHTEVAKYLLQNkakanakakddqtplhcaarightgmvklllenGASPNLATTAGHTPLHTAAREGHVDTALALLE 528
Cdd:PHA03095  265 AVFNNPRACRRLIAL---------------------------------GADINAVSSDGNTPLSLMVRNNNGRAVRAALA 311


                  .
gi 160707911  529 K 529
Cdd:PHA03095  312 K 312
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 217-436 2.26e-31

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 128.96  E-value: 2.26e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  217 AAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILL 296
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  297 DHGAPIQ-AKTKNGLSPIHMAAQGDHLDCVRLLLQYNAEIDDITLDHLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNG 375
Cdd:PHA02875   89 DLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCG 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 160707911  376 FTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLP-IVKNLLQRGASPNV 436
Cdd:PHA02875  169 CTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIdIVRLFIKRGADCNI 230
Death_ank cd08317
Death domain associated with Ankyrins; Death Domain (DD) associated with Ankyrins. Ankyrins ...
 1413-1496 3.09e-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: 118.14  E-value: 3.09e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911 1413 DRVEMRMAVIREHLGLSWAELARELQFSVEDINRIRVENPNSLLDQSTALLTLWVDREGENAKMENLYTALRNIDRSEIV 1492
Cdd:cd08317     1 HRADLRLSDIANLLGSDWPELARELGVSEEDIDLIRSENPNSLAQQAMAMLRLWLEREGEKATGNALESALKKIGRDDIV 80


                  ....
gi 160707911 1493 NMLE 1496
Cdd:cd08317    81 EKCE 84
PHA03095 PHA03095
ankyrin-like protein; Provisional
 490-816 1.54e-29

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 124.75  E-value: 1.54e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  490 VKLLLENGASPNLATTAGHTPLHTAAREGH---VDTALALLEKEASQACMTKKGFTPLHVAAKYGKV-RLAELLLEHDAH 565
Cdd:PHA03095   30 VRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGAD 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  566 PNAAGKNGLTPLHV--AVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQIEVA--RSLLQYGGSANAESVQGVT 641
Cdd:PHA03095  110 VNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVEllRLLIDAGADVYAVDDRFRS 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  642 PLHLAAQEGHT--EMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADV--LIKHGVTVDATTRMGYTPLHVASHYGN 717
Cdd:PHA03095  190 LLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNN 269

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  718 IKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSNgttpLAIAKRLGYISVTD-----VLKV 792
Cdd:PHA03095  270 PRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAAT----LNTASVAGGDIPSDatrlcVAKV 345

                         330       340
                  ....*....|....*....|....
gi 160707911  793 VTDETSVVLvSDKHRMSYPETVDE 816
Cdd:PHA03095  346 VLRGAFSLL-PEPIRAYHADFIRE 368
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 204-483 2.13e-29

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 124.22  E-value: 2.13e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  204 DVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLdrGAQIETRTKDELTPLHCA 283
Cdd:PHA02878   31 TSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMI--RSINKCSVFYTLVAIKDA 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  284 ARNGHVRISE-ILLDHGAPIQAKTkngLSPIHMAAQGDHLDC--VRLLLQYNAEIDDITLDHL-TPLHVAAHCGHHRVAK 359
Cdd:PHA02878  109 FNNRNVEIFKiILTNRYKNIQTID---LVYIDKKSKDDIIEAeiTKLLLSYGADINMKDRHKGnTALHYATENKDQRLTE 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  360 VLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVA-SFMGHLPIVKNLLQRGASPNV-S 437
Cdd:PHA02878  186 LLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAkS 265

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 160707911  438 NVKVETPLHMAARAghTEVAKYLLQNKAKANAKAKDDQTPLHCAAR 483
Cdd:PHA02878  266 YILGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAVK 309
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 53-271 2.76e-29

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 122.85  E-value: 2.76e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   53 LHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQD-----EVVRELVNYGANVNAQSQKGFTPLYMAAQE-- 125
Cdd:PHA03100   39 LYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKks 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  126 NHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHE--NVVAHLINYGT----KGKVRLpalhiaarnddtrtaavLLQN 199
Cdd:PHA03100  119 NSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVdinaKNRVNY-----------------LLSY 181

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 160707911  200 DPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLDRGAQIET 271
Cdd:PHA03100  182 GVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 186-498 8.57e-29

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 124.79  E-value: 8.57e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  186 RNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVR----- 260
Cdd:PHA02876  154 QQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKaiidn 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  261 ------------------------LLLDRGAQIETRTKDELTPLHCAARNGHV-RISEILLDHGAPIQAKTKNGLSPIH- 314
Cdd:PHA02876  234 rsninkndlsllkairnedletslLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYl 313

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  315 MAAQGDHLDCVRLLLQYNAEIDDITLDHLTPLHVAAHCGHHR-VAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMEL 393
Cdd:PHA02876  314 MAKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKdIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINT 393

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  394 LLKTGASIDAVTESGLTPLHVAsFMGHLPI--VKNLLQRGASPNVSNVKVETPLHMAARAG-HTEVAKYLLQNKAKANAK 470
Cdd:PHA02876  394 LLDYGADIEALSQKIGTALHFA-LCGTNPYmsVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAI 472

                         330       340
                  ....*....|....*....|....*...
gi 160707911  471 AKDDQTPLHCAarIGHTGMVKLLLENGA 498
Cdd:PHA02876  473 NIQNQYPLLIA--LEYHGIVNILLHYGA 498
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 260-550 8.75e-29

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 121.61  E-value: 8.75e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  260 RLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLlqynaeIDDIT 339
Cdd:PHA02874   19 KIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLL------IDNGV 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  340 LDHLTPLHvaahCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMG 419
Cdd:PHA02874   93 DTSILPIP----CIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHN 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  420 HLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKAKANAKAKDDQTPLHCAarIGHTGMVKLLLENGAS 499
Cdd:PHA02874  169 FFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA--IIHNRSAIELLINNAS 246

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 160707911  500 PNLATTAGHTPLHTAAR-EGHVDTALALLEKEASQACMTKKGFTPLHVAAKY 550
Cdd:PHA02874  247 INDQDIDGSTPLHHAINpPCDIDIIDILLYHKADISIKDNKGENPIDTAFKY 298
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 221-564 5.68e-28

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 122.48  E-value: 5.68e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  221 ENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILLDHGA 300
Cdd:PHA02876  156 DELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRS 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  301 PIQaktKNGLSPIHmAAQGDHLDCVRLLLQYNAEIDDITLDHLTPLHVAAHCGH-HRVAKVLLDKGAKPNSRALNGFTPL 379
Cdd:PHA02876  236 NIN---KNDLSLLK-AIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPL 311

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  380 HIACKKNH-IRVMELLLKTGASIDAVTESGLTPLHVASFMG-HLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVA 457
Cdd:PHA02876  312 YLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVII 391

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  458 KYLLQNKAKANAKAKDDQTPLHCAARIGHTGM-VKLLLENGASPNLATTAGHTPLHTAAREG-HVDTALALLEKEASQAC 535
Cdd:PHA02876  392 NTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNA 471

                         330       340
                  ....*....|....*....|....*....
gi 160707911  536 MTKKGFTPLHVAAKYGKVrlAELLLEHDA 564
Cdd:PHA02876  472 INIQNQYPLLIALEYHGI--VNILLHYGA 498
PHA03095 PHA03095
ankyrin-like protein; Provisional
 36-333 1.09e-27

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 118.97  E-value: 1.09e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   36 LRNGVDINTCNQNGLNGLH--LASKEGHVKMVVE-LLHKEIILETTTKKGNTALHIAALAGQDE-VVRELVNYGANVNAQ 111
Cdd:PHA03095   34 LAAGADVNFRGEYGKTPLHlyLHYSSEKVKDIVRlLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAGADVNAK 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  112 SQKGFTPL--YMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENV--VAHLINYG----TKGKVRLPALHI 183
Cdd:PHA03095  114 DKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGadvyAVDDRFRSLLHH 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  184 AARNDDTRTAAV--LLQNDPNPDVLSKTGFTPLHIAAHY---ENLNVAQLLLNrGASVNFTPQNGITPLHIASRRGNVIM 258
Cdd:PHA03095  194 HLQSFKPRARIVreLIRAGCDPAATDMLGNTPLHSMATGsscKRSLVLPLLIA-GISINARNRYGQTPLHYAAVFNNPRA 272

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 160707911  259 VRLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILLDHGAPIQ--AKTKNGLSPihmAAQGDHLDCVRLLLQYNA 333
Cdd:PHA03095  273 CRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAEtvAATLNTASV---AGGDIPSDATRLCVAKVV 346
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 116-415 2.73e-27

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 118.06  E-value: 2.73e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  116 FTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLINYGTKGKVRlpalhiaarnddtrtaav 195
Cdd:PHA02878   38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVF------------------ 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  196 llqndpNPDVLSKTGFtplhiaaHYENLNVAQLLLNRGASVNFTpqngITPLHIASRRGNVI----MVRLLLDRGAQIET 271
Cdd:PHA02878  100 ------YTLVAIKDAF-------NNRNVEIFKIILTNRYKNIQT----IDLVYIDKKSKDDIieaeITKLLLSYGADINM 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  272 RTKDEL-TPLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQYNAEIDDITLDHLTPLHVA- 349
Cdd:PHA02878  163 KDRHKGnTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISv 242

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 160707911  350 AHCGHHRVAKVLLDKGAKPNSRA-LNGFTPLHIACKKNhiRVMELLLKTGASIDAVTESGLTPLHVA 415
Cdd:PHA02878  243 GYCKDYDILKLLLEHGVDVNAKSyILGLTALHSSIKSE--RKLKLLLEYGADINSLNSYKLTPLSSA 307
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 510-783 5.08e-27

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 117.29  E-value: 5.08e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  510 PLHTAAREGHVDTALALLEKEASQACMTKKGFTPLHVAAKY-GKVRLAELLLEHDahpNAAGKNGLTPLHVAVHHNNLDI 588
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEpNKLGMKEMIRSIN---KCSVFYTLVAIKDAFNNRNVEI 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  589 VKLLLPRGGSphspawNGYT----PLHIAAKQNQIE--VARSLLQYGGSANAESV-QGVTPLHLAAQEGHTEMVALLLSK 661
Cdd:PHA02878  117 FKIILTNRYK------NIQTidlvYIDKKSKDDIIEaeITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSY 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  662 QANGNLGNKSGLTPLHLVSQEGHVPVADVLIKHGVTVDATTRMGYTPLHVASHY-GNIKLVKFLLQHQADVNAK-TKLGY 739
Cdd:PHA02878  191 GANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKsYILGL 270

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 160707911  740 SPLHQAAQQghTDIVTLLLKNGASPNEVSSNGTTPLAIA--KRLGY 783
Cdd:PHA02878  271 TALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAvkQYLCI 314
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 580-771 8.78e-27

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 115.47  E-value: 8.78e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  580 AVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQIEVARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVALLL 659
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  660 --SKQANgNLGNKSGLTPLHLVSQEGHVPVADVLIKHGVTVDATTRMGYTPLHVASHYGNIKLVKFLLQHQADVNAKTKL 737
Cdd:PHA02875   89 dlGKFAD-DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCC 167

                         170       180       190
                  ....*....|....*....|....*....|....
gi 160707911  738 GYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSNG 771
Cdd:PHA02875  168 GCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNG 201
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 542-791 2.14e-26

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 114.68  E-value: 2.14e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  542 TPLHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHS---PAWNG------------ 606
Cdd:PHA02874   37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSIlpiPCIEKdmiktildcgid 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  607 --------YTPLHIAAKQNQIEVARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHL 678
Cdd:PHA02874  117 vnikdaelKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  679 VSQEGHVPVADVLIKHGVTVDATTRMGYTPLHVASHYgNIKLVKFLLqHQADVNAKTKLGYSPLHQAAQQG-HTDIVTLL 757
Cdd:PHA02874  197 AAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIH-NRSAIELLI-NNASINDQDIDGSTPLHHAINPPcDIDIIDIL 274

                         250       260       270
                  ....*....|....*....|....*....|....
gi 160707911  758 LKNGASPNEVSSNGTTPLAIAKRlgYISVTDVLK 791
Cdd:PHA02874  275 LYHKADISIKDNKGENPIDTAFK--YINKDPVIK 306
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 547-765 3.11e-26

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 113.55  E-value: 3.11e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  547 AAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQIEVARSLL 626
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  627 QYGGSANAESVQ-GVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADVLIKHGVTVDATTRMG 705
Cdd:PHA02875   89 DLGKFADDVFYKdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCG 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 160707911  706 YTPLHVASHYGNIKLVKFLLQHQADVNAKTKLG-YSPLHQAAQQGHTDIVTLLLKNGASPN 765
Cdd:PHA02875  169 CTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCN 229
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 251-499 3.73e-26

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 113.61  E-value: 3.73e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  251 SRRGNVIMVRLLLDRGAQIETRTKDELTPLHCAARngHVRIS--EILLDHGAPIQAKTKNGLSPIH-----MAAQGDHLD 323
Cdd:PHA03100   10 SRIIKVKNIKYIIMEDDLNDYSYKKPVLPLYLAKE--ARNIDvvKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  324 CVRLLLQYNAEIDDITLDHLTPLHVAA--HCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHI--RVMELLLKTGA 399
Cdd:PHA03100   88 IVKLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGV 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  400 SIDAVTEsgltplhvasfmghlpiVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKAKANAKAKDDQTPLH 479
Cdd:PHA03100  168 DINAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLH 230

                         250       260
                  ....*....|....*....|
gi 160707911  480 CAARIGHTGMVKLLLENGAS 499
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 ...
 1413-1496 3.51e-25

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


Pssm-ID: 176781  Cd Length: 84  Bit Score: 100.90  E-value: 3.51e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911 1413 DRVEMRMAVIREHLGLSWAELARELQFSVEDINRIRVENPNSLLDQSTALLTLWVDREGENAKMENLYTALRNIDRSEIV 1492
Cdd:cd08803     1 ERTDIRMAIVADHLGLSWTELARELNFSVDEINQIRVENPNSLIAQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIV 80


                  ....
gi 160707911 1493 NMLE 1496
Cdd:cd08803    81 TLLE 84
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 452-667 5.08e-25

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 110.08  E-value: 5.08e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  452 GHTEVAKYLLQNKAKANAKAKDDQTPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALLEKEA 531
Cdd:PHA02875   13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  532 -SQACMTKKGFTPLHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPL 610
Cdd:PHA02875   93 fADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPL 172

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 160707911  611 HIAAKQNQIEVARSLLQYGGSANAESVQG-VTPLHLAAQEGHTEMVALLLSKQANGNL 667
Cdd:PHA02875  173 IIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNI 230
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 92-426 6.81e-25

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 110.05  E-value: 6.81e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   92 AGQDEVVRELV-NYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLINY 170
Cdd:PHA02874   11 SGDIEAIEKIIkNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDN 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  171 GTKGKVrLPALHIaaRNDDTRTaavLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIA 250
Cdd:PHA02874   91 GVDTSI-LPIPCI--EKDMIKT---ILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIA 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  251 SRRGNVIMVRLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQgdHLDCVRLLLQ 330
Cdd:PHA02874  165 IKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLI 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  331 YNAEIDDITLDHLTPLHVAAH--CGHHrVAKVLLDKGAKPNSRALNGFTPLHIACKknHIRVMELLLKTGAsiDAVTESG 408
Cdd:PHA02874  243 NNASINDQDIDGSTPLHHAINppCDID-IIDILLYHKADISIKDNKGENPIDTAFK--YINKDPVIKDIIA--NAVLIKE 317

                         330
                  ....*....|....*...
gi 160707911  409 LTPLHVASFMGHLPIVKN 426
Cdd:PHA02874  318 ADKLKDSDFLEHIEIKDN 335
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 523-790 2.92e-24

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 110.54  E-value: 2.92e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  523 ALALLEKEASQACMTKKGFTPLHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVK------------ 590
Cdd:PHA02876  161 AEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKaiidnrsninkn 240

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  591 -----------------LLLPRGGSPHSPAWNGYTPLHIAAKQNQI-EVARSLLQYGGSANAESVQGVTPLHLAAQEGH- 651
Cdd:PHA02876  241 dlsllkairnedletslLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAKNGYd 320

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  652 TEMVALLLSKQANGNLGNKSGLTPLHLVSQ-EGHVPVADVLIKHGVTVDATTRMGYTPLHVASHYGNIKLVKFLLQHQAD 730
Cdd:PHA02876  321 TENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGAD 400

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  731 ----------------------------------VNAKTKLGYSPLHQAAQQG-HTDIVTLLLKNGASPNEVSSNGTTPL 775
Cdd:PHA02876  401 iealsqkigtalhfalcgtnpymsvktlidrganVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPL 480

                         330
                  ....*....|....*
gi 160707911  776 AIAkrLGYISVTDVL 790
Cdd:PHA02876  481 LIA--LEYHGIVNIL 493
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 126-340 4.97e-24

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 107.00  E-value: 4.97e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  126 NHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLINYGTKGKVRLPA----LHIAARNDDTRTAAVLLQ-ND 200
Cdd:PHA02875   13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDieseLHDAVEEGDVKAVEELLDlGK 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  201 PNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLDRGAQIETRTKDELTPL 280
Cdd:PHA02875   93 FADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPL 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 160707911  281 HCAARNGHVRISEILLDHGAPIQAKTKNG-LSPIHMAAQGDHLDCVRLLLQYNAEIDDITL 340
Cdd:PHA02875  173 IIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNIMFM 233
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 386-596 8.55e-24

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 106.23  E-value: 8.55e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  386 NHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKA 465
Cdd:PHA02875   13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  466 -KANAKAKDDQTPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALLEKEASQACMTKKGFTPL 544
Cdd:PHA02875   93 fADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPL 172

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 160707911  545 HVAAKYGKVRLAELLLEHDAHPNAAGKNG-LTPLHVAVHHNNLDIVKLLLPRG 596
Cdd:PHA02875  173 IIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRG 225
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 357-646 2.21e-23

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 105.43  E-value: 2.21e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  357 VAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNV 436
Cdd:PHA02874   17 IEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSI 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  437 SNVKvetplhmaarAGHTEVAKYLLQNKAKANAKAKDDQTPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAR 516
Cdd:PHA02874   97 LPIP----------CIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIK 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  517 EGHVDTALALLEKEASQACMTKKGFTPLHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNlDIVKLLLpRG 596
Cdd:PHA02874  167 HNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLI-NN 244

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 160707911  597 GSPHSPAWNGYTPLHIAAKQN-QIEVARSLLQYGGSANAESVQGVTPLHLA 646
Cdd:PHA02874  245 ASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTA 295
Death_ank2 cd08804
Death domain of Ankyrin-2; Death Domain (DD) of Ankyrin-2 (ANK-2) and related proteins. ...
 1413-1496 2.64e-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: 2.64e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911 1413 DRVEMRMAVIREHLGLSWAELARELQFSVEDINRIRVENPNSLLDQSTALLTLWVDREGENAKMENLYTALRNIDRSEIV 1492
Cdd:cd08804     1 ERTEERLAHIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLTQCLTKINRMDIV 80


                  ....
gi 160707911 1493 NMLE 1496
Cdd:cd08804    81 HLME 84
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 376-679 6.81e-23

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 104.58  E-value: 6.81e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  376 FTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNVSN--VKVETPLHMAaragH 453
Cdd:PHA02878   38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFYtlVAIKDAFNNR----N 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  454 TEVAKYLLQNKAKANAKAKDDQTPLHCAARIGHTGMVKLLLENGASPNLATTaghtplhtaareghvdtalallekeasq 533
Cdd:PHA02878  114 VEIFKIILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDR---------------------------- 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  534 acmtKKGFTPLHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIA 613
Cdd:PHA02878  166 ----HKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIS 241

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 160707911  614 AKQ-NQIEVARSLLQYGGSANAES-VQGVTPLHLAAQEghTEMVALLLSKQANGNLGNKSGLTPLHLV 679
Cdd:PHA02878  242 VGYcKDYDILKLLLEHGVDVNAKSyILGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSA 307
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 476-700 7.17e-23

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 103.59  E-value: 7.17e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  476 TPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHV-----DTALALLEKEASQACMTKKGFTPLHVAA-- 548
Cdd:PHA03100   37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAIsk 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  549 KYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVH--HNNLDIVKLLLPRGgsphspawngytplhiaAKQNQIEVARSLL 626
Cdd:PHA03100  117 KSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLEsnKIDLKILKLLIDKG-----------------VDINAKNRVNYLL 179

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 160707911  627 QYGGSANAESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADVLIKHGVTVDA 700
Cdd:PHA03100  180 SYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
Ank_2 pfam12796
Ankyrin repeats (3 copies);
412-502 1.03e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 94.03  E-value: 1.03e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   412 LHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQnkAKANAKAKDDQTPLHCAARIGHTGMVK 491
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE--HADVNLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|.
gi 160707911   492 LLLENGASPNL 502
Cdd:pfam12796   79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
53-143 2.08e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 93.26  E-value: 2.08e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911    53 LHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQDEVVRELVNYgANVNAQSQkGFTPLYMAAQENHLEVVK 132
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                           90
                   ....*....|.
gi 160707911   133 FLLENGANQNV 143
Cdd:pfam12796   79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
478-568 3.26e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.49  E-value: 3.26e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   478 LHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALLEKEASQacMTKKGFTPLHVAAKYGKVRLAE 557
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN--LKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|.
gi 160707911   558 LLLEHDAHPNA 568
Cdd:pfam12796   79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
346-438 4.90e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.10  E-value: 4.90e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   346 LHVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASidAVTESGLTPLHVASFMGHLPIVK 425
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 160707911   426 NLLQRGASPNVSN 438
Cdd:pfam12796   79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
313-403 6.75e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 91.72  E-value: 6.75e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   313 IHMAAQGDHLDCVRLLLQYNAEIDDITLDHLTPLHVAAHCGHHRVAKVLLDKGAKpnSRALNGFTPLHIACKKNHIRVME 392
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|.
gi 160707911   393 LLLKTGASIDA 403
Cdd:pfam12796   79 LLLEKGADINV 89
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 15-285 8.98e-22

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 100.42  E-value: 8.98e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   15 DAATSFLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMV--------------VELLHKEII------ 74
Cdd:PHA02874   34 ETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIkllidngvdtsilpIPCIEKDMIktildc 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   75 ---LETTTKKGNTALHIAALAGQDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTP 151
Cdd:PHA02874  114 gidVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESP 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  152 lavalqqghenvvahlinygtkgkvrlpaLHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYeNLNVAQLLLN 231
Cdd:PHA02874  194 -----------------------------LHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIH-NRSAIELLIN 243

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 160707911  232 rGASVNFTPQNGITPLHIASRRG-NVIMVRLLLDRGAQIETRTKDELTPLHCAAR 285
Cdd:PHA02874  244 -NASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAFK 297
Ank_2 pfam12796
Ankyrin repeats (3 copies);
280-371 1.01e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 91.33  E-value: 1.01e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   280 LHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQYNAEidDITLDHLTPLHVAAHCGHHRVAK 359
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 160707911   360 VLLDKGAKPNSR 371
Cdd:pfam12796   79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
676-765 1.30e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.95  E-value: 1.30e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   676 LHLVSQEGHVPVADVLIKHGVTVDATTRMGYTPLHVASHYGNIKLVKFLLQHqADVNAKTKlGYSPLHQAAQQGHTDIVT 755
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                           90
                   ....*....|
gi 160707911   756 LLLKNGASPN 765
Cdd:pfam12796   79 LLLEKGADIN 88
Ank_2 pfam12796
Ankyrin repeats (3 copies);
643-734 1.51e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.56  E-value: 1.51e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   643 LHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADVLIKHgVTVDATTRmGYTPLHVASHYGNIKLVK 722
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 160707911   723 FLLQHQADVNAK 734
Cdd:pfam12796   79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
544-634 1.75e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.56  E-value: 1.75e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   544 LHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSphSPAWNGYTPLHIAAKQNQIEVAR 623
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|.
gi 160707911   624 SLLQYGGSANA 634
Cdd:pfam12796   79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
214-305 2.07e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.18  E-value: 2.07e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   214 LHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLDRGAQieTRTKDELTPLHCAARNGHVRISE 293
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 160707911   294 ILLDHGAPIQAK 305
Cdd:pfam12796   79 LLLEKGADINVK 90
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
 1412-1498 3.96e-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: 89.39  E-value: 3.96e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   1412 TDRVEMRMAVIREH-LGLSWAELARELQFSVEDINRIRVENPNSLLDQSTALLTLWVDREGENAKMENLYTALRNIDRSE 1490
Cdd:smart00005    1 PELTRQKLAKLLDHpLGLDWRELARKLGLSEADIDQIRTEAPRDLAEQSVQLLRLWEQREGKNATLGTLLEALRKMGRDD 80


                    ....*...
gi 160707911   1491 IVNMLEGS 1498
Cdd:smart00005   81 AVELLRSE 88
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 474-781 4.57e-21

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 98.14  E-value: 4.57e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  474 DQTPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDtALALLEKEASQACMTKKGF-TPLHVAAKYGK 552
Cdd:PHA02875    2 DQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSE-AIKLLMKHGAIPDVKYPDIeSELHDAVEEGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  553 VRLAELLLEHDAHPN-AAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQIEVARSLLQYGGS 631
Cdd:PHA02875   81 VKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKAC 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  632 ANAESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSG-LTPLHLVSQEGHVPVADVLIKHGVTVD-ATTRMG--YT 707
Cdd:PHA02875  161 LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNiMFMIEGeeCT 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 160707911  708 PLHVASHYgniklvkfllqhqaDVNAKTklgysplhQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIAKRL 781
Cdd:PHA02875  241 ILDMICNM--------------CTNLES--------EAIDALIADIAIRIHKKTIRRDEGFKNNMSTIEDKEEF 292
Ank_2 pfam12796
Ankyrin repeats (3 copies);
86-173 5.68e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.02  E-value: 5.68e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911    86 LHIAALAGQDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENgANQNVaTEDGFTPLAVALQQGHENVVA 165
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNL-KDNGRTALHYAARSGHLEIVK 78


                   ....*...
gi 160707911   166 HLINYGTK 173
Cdd:pfam12796   79 LLLEKGAD 86
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 86-411 7.65e-21

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 98.03  E-value: 7.65e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   86 LHIAALAGQDEVVRELVNYGANVNAQSQKGFTPLYMAAQE-------------------------------NHLEVVKFL 134
Cdd:PHA02878   41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEpnklgmkemirsinkcsvfytlvaikdafnnRNVEIFKII 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  135 LENGANQNVATEDGFTPLAVALQQGHENVVAHLINYGTKGKVRL-----PALHIAARNDDTRTAAVLLQNDPNPDVLSKT 209
Cdd:PHA02878  121 LTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDrhkgnTALHYATENKDQRLTELLLSYGANVNIPDKT 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  210 GFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRgnvimvrlLLDrgaqietrtkdeltplhcaarnghV 289
Cdd:PHA02878  201 NNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGY--------CKD------------------------Y 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  290 RISEILLDHGAPIQAK-TKNGLSPIHMAAQGDhlDCVRLLLQYNAEIDDITLDHLTPLHVAA------HCGHHRVAKVLL 362
Cdd:PHA02878  249 DILKLLLEHGVDVNAKsYILGLTALHSSIKSE--RKLKLLLEYGADINSLNSYKLTPLSSAVkqylciNIGRILISNICL 326

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 160707911  363 DKGAKPNSRALNGFTpLHIACKKNHIRVMELLLKTGASIDAVTESGLTP 411
Cdd:PHA02878  327 LKRIKPDIKNSEGFI-DNMDCITSNKRLNQIKDKCEDELNRLASIKITN 374
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 415-633 1.51e-20

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 96.60  E-value: 1.51e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  415 ASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKAKANAKAKDDQTPLHCAARIGHTGMVKLLL 494
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  495 ENGASPN-LATTAGHTPLHTAAREGHVDTALALLEKEASQACMTKKGFTPLHVAAKYGKVRLAELLLEHDAHPNAAGKNG 573
Cdd:PHA02875   89 DLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCG 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 160707911  574 LTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNG-YTPLHIAAKQNQIEVARSLLQYGGSAN 633
Cdd:PHA02875  169 CTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCN 229
Ank_2 pfam12796
Ankyrin repeats (3 copies);
445-532 3.86e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.71  E-value: 3.86e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   445 LHMAARAGHTEVAKYLLQNKAKANAKAKDDQTPLHCAARIGHTGMVKLLLENGASPNlaTTAGHTPLHTAAREGHVDTAL 524
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78


                   ....*...
gi 160707911   525 ALLEKEAS 532
Cdd:pfam12796   79 LLLEKGAD 86
Ank_2 pfam12796
Ankyrin repeats (3 copies);
610-701 5.59e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.32  E-value: 5.59e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   610 LHIAAKQNQIEVARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVALLLSKqANGNLGNKsGLTPLHLVSQEGHVPVAD 689
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 160707911   690 VLIKHGVTVDAT 701
Cdd:pfam12796   79 LLLEKGADINVK 90
Death cd01670
Death Domain: a protein-protein interaction domain; Death Domains (DDs) are protein-protein ...
 1421-1496 6.54e-20

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


Pssm-ID: 260017 [Multi-domain]  Cd Length: 79  Bit Score: 85.41  E-value: 6.54e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160707911 1421 VIREHLGLSWAELARELQFSVEDINRIRVENPNSLLDQSTALLTLWVDREGENAKMENLYTALRNIDRSEIVNMLE 1496
Cdd:cd01670     4 LVAEELGRDWKKLARKLGLSEGDIDQIEEDNRDDLKEQAYQMLERWREREGDEATLGRLIQALREIGRRDLAEKLE 79
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 312-581 7.54e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 94.95  E-value: 7.54e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  312 PIHMAAQGDHLDCVRLLLQYNAEIDDITLDHLTPLHVAAHCGHHRVAKVLLdkgAKPNSRAL-NGFTPLHIACKKNHIRV 390
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMI---RSINKCSVfYTLVAIKDAFNNRNVEI 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  391 MELLLKTgaSIDAVTESGLTPLHVASFMGHL--PIVKNLLQRGASPN-VSNVKVETPLHMAARAGHTEVAKYLLQNKAKA 467
Cdd:PHA02878  117 FKIILTN--RYKNIQTIDLVYIDKKSKDDIIeaEITKLLLSYGADINmKDRHKGNTALHYATENKDQRLTELLLSYGANV 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  468 NAKAKDDQTPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTA-AREGHVDTALALLEKEAS-QACMTKKGFTPLH 545
Cdd:PHA02878  195 NIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDvNAKSYILGLTALH 274

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 160707911  546 VAAKygKVRLAELLLEHDAHPNAAGKNGLTPLHVAV 581
Cdd:PHA02878  275 SSIK--SERKLKLLLEYGADINSLNSYKLTPLSSAV 308
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 552-778 9.94e-20

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 95.90  E-value: 9.94e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  552 KVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQIEVAR-------- 623
Cdd:PHA02876  157 ELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKaiidnrsn 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  624 -------------------SLLQY--GGSANAESVQGVTPLHLAAQEGH-TEMVALLLSKQANGNLGNKSGLTPLHLVSQ 681
Cdd:PHA02876  237 inkndlsllkairnedletSLLLYdaGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAK 316

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  682 EGH-VPVADVLIKHGVTVDATTRMGYTPLHVASHYGNIK-LVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLK 759
Cdd:PHA02876  317 NGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKdIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLD 396

                         250
                  ....*....|....*....
gi 160707911  760 NGASPNEVSSNGTTPLAIA 778
Cdd:PHA02876  397 YGADIEALSQKIGTALHFA 415
Death pfam00531
Death domain;
1416-1496 1.57e-19

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 84.72  E-value: 1.57e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  1416 EMRMAVIREH---LGLSWAELARELQFSVEDINRIRVENPNsLLDQSTALLTLWVDREGENAKMENLYTALRNIDRSEIV 1492
Cdd:pfam00531    1 RKQLDRLLDPpppLGKDWRELARKLGLSENEIDEIESENPR-LRSQTYELLRLWEQREGKNATVGTLLEALRKLGRRDAA 79


                   ....
gi 160707911  1493 NMLE 1496
Cdd:pfam00531   80 EKIQ 83
Ank_2 pfam12796
Ankyrin repeats (3 copies);
181-272 1.76e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.78  E-value: 1.76e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   181 LHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTpqNGITPLHIASRRGNVIMVR 260
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD--NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 160707911   261 LLLDRGAQIETR 272
Cdd:pfam12796   79 LLLEKGADINVK 90
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 574-793 4.89e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 92.64  E-value: 4.89e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  574 LTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQ-NQI---EVARSLLQYGGSANAESVQGvtplhlAAQE 649
Cdd:PHA02878   38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEpNKLgmkEMIRSINKCSVFYTLVAIKD------AFNN 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  650 GHTEMVALLLSKQANGNlgNKSGLTPLHLVSQEGHV--PVADVLIKHGVTVDATTR-MGYTPLHVASHYGNIKLVKFLLQ 726
Cdd:PHA02878  112 RNVEIFKIILTNRYKNI--QTIDLVYIDKKSKDDIIeaEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLS 189

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 160707911  727 HQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIAkrLGYISVTDVLKVV 793
Cdd:PHA02878  190 YGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIS--VGYCKDYDILKLL 254
Ank_2 pfam12796
Ankyrin repeats (3 copies);
379-462 1.08e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.47  E-value: 1.08e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   379 LHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRgASPNVSNVKvETPLHMAARAGHTEVAK 458
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG-RTALHYAARSGHLEIVK 78


                   ....
gi 160707911   459 YLLQ 462
Cdd:pfam12796   79 LLLE 82
PHA03095 PHA03095
ankyrin-like protein; Provisional
 653-777 3.52e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 89.70  E-value: 3.52e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  653 EMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADV---LIKHGVTVDATTRMGYTPLHVASHYGN-IKLVKFLLQHQ 728
Cdd:PHA03095   28 EEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAG 107

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 160707911  729 ADVNAKTKLGYSPLHQ--AAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAI 777
Cdd:PHA03095  108 ADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAV 158
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 23-267 3.62e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 89.28  E-value: 3.62e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   23 AARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQDEVVRELV 102
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  103 NYGANVN-AQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPlavalqqghenvvahlinygtkgkvrlpaL 181
Cdd:PHA02875   89 DLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSP-----------------------------L 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  182 HIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNG-ITPLHIASRRGNVIMVR 260
Cdd:PHA02875  140 HLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVR 219


                  ....*..
gi 160707911  261 LLLDRGA 267
Cdd:PHA02875  220 LFIKRGA 226
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 322-537 7.00e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 88.12  E-value: 7.00e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  322 LDCVRLLLQYNAEIDDITLDHLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASI 401
Cdd:PHA02875   15 LDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  402 DAVT-ESGLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKAKANAKAKDDQTPLHC 480
Cdd:PHA02875   95 DDVFyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLII 174

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 160707911  481 AARIGHTGMVKLLLENGASPNLATTAGH-TPLHTAAREGHVDTALALLEKEASQACMT 537
Cdd:PHA02875  175 AMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADCNIMF 232
Ank_2 pfam12796
Ankyrin repeats (3 copies);
20-111 1.19e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.39  E-value: 1.19e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911    20 FLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMvVELLHKEIILETTTkKGNTALHIAALAGQDEVVR 99
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEI-VKLLLEHADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 160707911   100 ELVNYGANVNAQ 111
Cdd:pfam12796   79 LLLEKGADINVK 90
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 509-685 3.04e-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: 3.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  509 TPLHTAAREGHVDTALALLEKEASQACMTKK-GFTPLHVAAKYGKVRLAELLLEhdAHPNAAGK-------NGLTPLHVA 580
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGAlGETALHVAALYDNLEAAVVLME--AAPELVNEpmtsdlyQGETALHIA 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  581 VHHNNLDIVKLLLPRGG--------------SPHSPAWNGYTPLHIAAKQNQIEVARSLLQYGGSANAESVQGVTPLH-L 645
Cdd:cd22192    97 VVNQNLNLVRELIARGAdvvspratgtffrpGPKNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHiL 176

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 160707911  646 AAQEGHT---EMVALLLSKQANGNLG------NKSGLTPLHLVSQEGHV 685
Cdd:cd22192   177 VLQPNKTfacQMYDLILSYDKEDDLQpldlvpNNQGLTPFKLAAKEGNI 225
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 617-790 3.18e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 86.20  E-value: 3.18e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  617 NQIEVARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADVLIKHGV 696
Cdd:PHA02875   13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  697 TV-DATTRMGYTPLHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPL 775
Cdd:PHA02875   93 FAdDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPL 172

                         170
                  ....*....|....*
gi 160707911  776 AIAKRLGYISVTDVL 790
Cdd:PHA02875  173 IIAMAKGDIAICKML 187
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 476-662 4.97e-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: 4.97e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  476 TPLHCAARIGHTGMVKLLLENGASPNLATTA-GHTPLHTAAREGHVDTALALLE--KEASQACMTK---KGFTPLHVAAK 549
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGAlGETALHVAALYDNLEAAVVLMEaaPELVNEPMTSdlyQGETALHIAVV 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  550 YGKVRLAELLLEHDA---HPNAAG-------KN----GLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAK 615
Cdd:cd22192    99 NQNLNLVRELIARGAdvvSPRATGtffrpgpKNliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVL 178

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 160707911  616 QNQIEVARS----LLQYGGSANAESV------QGVTPLHLAAQEGHTEMVALLLSKQ 662
Cdd:cd22192   179 QPNKTFACQmydlILSYDKEDDLQPLdlvpnnQGLTPFKLAAKEGNIVMFQHLVQKR 235
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 181-350 8.20e-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: 86.22  E-value: 8.20e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  181 LHIAARNDDTRTAAVLLQNdPNPDVLSK--TGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQN-----GITPLHIASRR 253
Cdd:cd22192    21 LLLAAKENDVQAIKKLLKC-PSCDLFQRgaLGETALHVAALYDNLEAAVVLMEAAPELVNEPMTsdlyqGETALHIAVVN 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  254 GNVIMVRLLLDRGAQIET---------RTKDELT-----PLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAA-- 317
Cdd:cd22192   100 QNLNLVRELIARGADVVSpratgtffrPGPKNLIyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVlq 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 160707911  318 QGDHLDC--VRLLLQYNAEIDDITLDH------LTPLHVAA 350
Cdd:cd22192   180 PNKTFACqmYDLILSYDKEDDLQPLDLvpnnqgLTPFKLAA 220
Ank_2 pfam12796
Ankyrin repeats (3 copies);
709-790 1.16e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.69  E-value: 1.16e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   709 LHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASpnEVSSNGTTPLAIAKRLGYISVTD 788
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78


                   ..
gi 160707911   789 VL 790
Cdd:pfam12796   79 LL 80
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 615-781 2.42e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 78.57  E-value: 2.42e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  615 KQNQIEVARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADVLIKH 694
Cdd:PHA02876  154 QQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDN 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  695 -----------------------------GVTVDATTRMGYTPLHVASHYGNI-KLVKFLLQHQADVNAKTKLGYSPLHQ 744
Cdd:PHA02876  234 rsninkndlsllkairnedletslllydaGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYL 313

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 160707911  745 AAQQGH-TDIVTLLLKNGASPNEVSSNGTTPLAIAKRL 781
Cdd:PHA02876  314 MAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTL 351
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 81-232 8.34e-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: 8.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   81 KGNTALHIAALAGQDEVVRELVNYGANVNAQSQKGF--------------TPLYMAAQENHLEVVKFLLENGANqNVATE 146
Cdd:cd22194   140 EGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVFfnpkykhegfyfgeTPLALAACTNQPEIVQLLMEKEST-DITSQ 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  147 DGFTplavalqqgheNVVAHlinygtkgkvrlpALHIAARNDDTRTAAV------LLQNDPNPD---VLSKTGFTPLHIA 217
Cdd:cd22194   219 DSRG-----------NTVLH-------------ALVTVAEDSKTQNDFVkrmydmILLKSENKNletIRNNEGLTPLQLA 274

                         170
                  ....*....|....*
gi 160707911  218 AHYENLNVAQLLLNR 232
Cdd:cd22194   275 AKMGKAEILKYILSR 289
Death_FADD cd08306
Fas-associated Death Domain protein-protein interaction domain; Death domain (DD) found in ...
 1421-1484 9.14e-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: 65.39  E-value: 9.14e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 160707911 1421 VIREHLGLSWAELARELQFSVEDINRIRVENPNSLLDQSTALLTLWVDREGENAKMENLYTALR 1484
Cdd:cd08306     7 VICENLGRDWRQLARKLGLSETKIESISEAHPRNLREQVRQSLREWKKIKKAEATVADLIKALR 70
Ank_4 pfam13637
Ankyrin repeats (many copies);
542-593 2.61e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 63.06  E-value: 2.61e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 160707911   542 TPLHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLL 593
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
705-758 5.59e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 62.29  E-value: 5.59e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 160707911   705 GYTPLHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLL 758
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02946 PHA02946
ankyin-like protein; Provisional
 554-796 8.35e-12

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 69.70  E-value: 8.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  554 RLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQ--IEVARSLLQYGGS 631
Cdd:PHA02946   53 RFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAK 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  632 A-NAESVQGVTPLhLAAQEGHTEMVALLLSKQANGNLGNKSGLTPL--HLVSQEGHVPVADVLIKHGVTVDATTRMGYTP 708
Cdd:PHA02946  133 InNSVDEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFGKNHIhrHLMSDNPKASTISWMMKLGISPSKPDHDGNTP 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  709 LHV--ASHYGNIKLVKFLLQhQADVNAKTKLGYSPLhqaaqqghtdivTLLLKNGASPNEVSSNGTTPLAIAKRLGYISV 786
Cdd:PHA02946  212 LHIvcSKTVKNVDIINLLLP-STDVNKQNKFGDSPL------------TLLIKTLSPAHLINKLLSTSNVITDQTVNICI 278

                         250
                  ....*....|....
gi 160707911  787 ----TDVLKVVTDE 796
Cdd:PHA02946  279 fydrDDVLEIINDK 292
Ank_4 pfam13637
Ankyrin repeats (many copies);
408-461 1.36e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 61.14  E-value: 1.36e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 160707911   408 GLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLL 461
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
82-135 1.95e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 60.75  E-value: 1.95e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 160707911    82 GNTALHIAALAGQDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLL 135
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 641-777 2.29e-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: 2.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  641 TPLHLAAQEGHTEMVA-LLLSKQAN----GNLGNksglTPLHLVSQEGHVPVADVLIKHG---VTVDATTRM--GYTPLH 710
Cdd:cd22192    19 SPLLLAAKENDVQAIKkLLKCPSCDlfqrGALGE----TALHVAALYDNLEAAVVLMEAApelVNEPMTSDLyqGETALH 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  711 VASHYGNIKLVKFLLQHQADV------------NAKTKLGYS--PLHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLA 776
Cdd:cd22192    95 IAVVNQNLNLVRELIARGADVvspratgtffrpGPKNLIYYGehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174


                  .
gi 160707911  777 I 777
Cdd:cd22192   175 I 175
Ank_4 pfam13637
Ankyrin repeats (many copies);
377-428 3.03e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.98  E-value: 3.03e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 160707911   377 TPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLL 428
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 481-664 3.06e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 68.74  E-value: 3.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  481 AARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALLEkeasQACmtkkgftPLHVaakygkvrlaelll 560
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLK----HAC-------NVHI-------------- 586

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  561 eHDAHPNAAGKNGLTplhvAVHHNNLDIVkLLLPRGGSPHSpawnGYTPLHIAAKQNQIEVARSLLQYGGSANAESVQGV 640
Cdd:PLN03192  587 -RDANGNTALWNAIS----AKHHKIFRIL-YHFASISDPHA----AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGA 656

                         170       180
                  ....*....|....*....|....
gi 160707911  641 TPLHLAAQEGHTEMVALLLSKQAN 664
Cdd:PLN03192  657 TALQVAMAEDHVDMVRLLIMNGAD 680
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 224-495 5.19e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 67.46  E-value: 5.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  224 NVAQLLLNRGASVNFTPQ-NGITPLHIASRRGNVIMVRLLLDRGAQIETRTKDElTPLHCAARNGHV------RISEILL 296
Cdd:PHA02989   17 NALEFLLRTGFDVNEEYRgNSILLLYLKRKDVKIKIVKLLIDNGADVNYKGYIE-TPLCAVLRNREItsnkikKIVKLLL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  297 DHGAPIQAKTKNGLSPIHMAAQGDH---LDCVRLLLQYNAEIDDI-TLDHLTPLHVAAHCGHHR--VAKVLLDKGAKP-N 369
Cdd:PHA02989   96 KFGADINLKTFNGVSPIVCFIYNSNinnCDMLRFLLSKGINVNDVkNSRGYNLLHMYLESFSVKkdVIKILLSFGVNLfE 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  370 SRALNGFTPLHIACKKN----HIRVMELLLKTGASI---DAVTESGLTplhvaSFMGHLPI-------VKNLLQRGASPN 435
Cdd:PHA02989  176 KTSLYGLTPMNIYLRNDidviSIKVIKYLIKKGVNIetnNNGSESVLE-----SFLDNNKIlskkefkVLNFILKYIKIN 250

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  436 VSNVKVETPLHMAARAGHTEVAKYLLQNKAKANAKAKDDQTPLHCAARIGHTGMVKLLLE 495
Cdd:PHA02989  251 KKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNRILQ 310
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 14-157 5.36e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 66.91  E-value: 5.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   14 ADAATSFLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAG 93
Cdd:PHA02874  122 AELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYG 201

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 160707911   94 QDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHlEVVKFLLENgANQNVATEDGFTPLAVALQ 157
Cdd:PHA02874  202 DYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLINN-ASINDQDIDGSTPLHHAIN 263
Ank_4 pfam13637
Ankyrin repeats (many copies);
342-395 6.07e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.21  E-value: 6.07e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 160707911   342 HLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLL 395
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 578-768 7.35e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 67.59  E-value: 7.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  578 HVAVHhnNLDIVKLLLPRGGSpHSPAWNGYTPLHIAAKQNQiEVARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVAL 657
Cdd:PLN03192  501 HKELH--DLNVGDLLGDNGGE-HDDPNMASNLLTVASTGNA-ALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLV 576

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  658 LLSKQANGNLGNKSGLTPLHLVSQEGHVPVADVLIKHGVTVDATTrmGYTPLHVASHYGNIKLVKFLLQHQADVNAKTKL 737
Cdd:PLN03192  577 LLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHA--AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQ 654

                         170       180       190
                  ....*....|....*....|....*....|.
gi 160707911  738 GYSPLHQAAQQGHTDIVTLLLKNGASPNEVS 768
Cdd:PLN03192  655 GATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
Ank_4 pfam13637
Ankyrin repeats (many copies);
212-263 1.20e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.44  E-value: 1.20e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 160707911   212 TPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLL 263
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 28-173 1.49e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 66.24  E-value: 1.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   28 NLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIaALAGQDEV--VRELVNYG 105
Cdd:PHA02876  354 NKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHF-ALCGTNPYmsVKTLIDRG 432

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 160707911  106 ANVNAQSQKGFTPLYMAAQEN-HLEVVKFLLENGANQNVATEDGFTPLAVALqqGHENVVAHLINYGTK 173
Cdd:PHA02876  433 ANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGAE 499
Ank_4 pfam13637
Ankyrin repeats (many copies);
276-329 1.81e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.05  E-value: 1.81e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 160707911   276 ELTPLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLL 329
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
309-362 1.98e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 57.67  E-value: 1.98e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 160707911   309 GLSPIHMAAQGDHLDCVRLLLQYNAEIDDITLDHLTPLHVAAHCGHHRVAKVLL 362
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 9-171 2.14e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 66.04  E-value: 2.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911    9 GSDPAADAATSFLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHI 88
Cdd:PLN03192  518 GEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWN 597

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   89 AALAGQDEVVRELVNYGANVNAQSqkGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLI 168
Cdd:PLN03192  598 AISAKHHKIFRILYHFASISDPHA--AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLI 675


                  ...
gi 160707911  169 NYG 171
Cdd:PLN03192  676 MNG 678
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 377-560 2.76e-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: 2.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  377 TPLHIACKKNHIRVMELLLKTgASIDAVTESGL--TPLHVASFMGHLPIVKNLLQrgASPNVSNVKV-------ETPLHM 447
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKC-PSCDLFQRGALgeTALHVAALYDNLEAAVVLME--AAPELVNEPMtsdlyqgETALHI 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  448 AARAGHTEVAKYLLQNKAkanakakDDQTP---------------------LHCAARIGHTGMVKLLLENGASPNLATTA 506
Cdd:cd22192    96 AVVNQNLNLVRELIARGA-------DVVSPratgtffrpgpknliyygehpLSFAACVGNEEIVRLLIEHGADIRAQDSL 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 160707911  507 GHTPLH------TAAREGHVDTALALLEKEASQACM----TKKGFTPLHVAAKYGKVRLAELLL 560
Cdd:cd22192   169 GNTVLHilvlqpNKTFACQMYDLILSYDKEDDLQPLdlvpNNQGLTPFKLAAKEGNIVMFQHLV 232
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 53-265 3.36e-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: 3.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   53 LHLASKEGHVKMVVELL-HKEIILETTTKKGNTALHIAALAGQDEV-------VRELVNygANVNAQSQKGFTPLYMAAQ 124
Cdd:cd22192    21 LLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAavvlmeaAPELVN--EPMTSDLYQGETALHIAVV 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  125 ENHLEVVKFLLENGANQNVATEDG--FT------------PLAVALQQGHENVVAHLINYGTkgkvrlpalhiAARNDDT 190
Cdd:cd22192    99 NQNLNLVRELIARGADVVSPRATGtfFRpgpknliyygehPLSFAACVGNEEIVRLLIEHGA-----------DIRAQDS 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  191 RtaavllqndpnpdvlsktGFTPLHIAAHYENLNVA----QLLLNRGASVNFTP------QNGITPLHIASRRGNVIMVR 260
Cdd:cd22192   168 L------------------GNTVLHILVLQPNKTFAcqmyDLILSYDKEDDLQPldlvpnNQGLTPFKLAAKEGNIVMFQ 229


                  ....*
gi 160707911  261 LLLDR 265
Cdd:cd22192   230 HLVQK 234
Ank_4 pfam13637
Ankyrin repeats (many copies);
443-494 3.93e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.90  E-value: 3.93e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 160707911   443 TPLHMAARAGHTEVAKYLLQNKAKANAKAKDDQTPLHCAARIGHTGMVKLLL 494
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 283-438 5.09e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 64.50  E-value: 5.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  283 AARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQY--NAEIDDITLDhlTPLHVAAHCGHHRVAKV 360
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHacNVHIRDANGN--TALWNAISAKHHKIFRI 609

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 160707911  361 LLDKGAKPNSRAlnGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNVSN 438
Cdd:PLN03192  610 LYHFASISDPHA--AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
PHA02798 PHA02798
ankyrin-like protein; Provisional
 202-448 7.32e-10

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 63.70  E-value: 7.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  202 NPDVLSKTgFTPLHIAAHYEN--LNVAQLLLNRGASVNFTPQNGITPL-----HIASRRGNVIMVRLLLDRGAQIETRTK 274
Cdd:PHA02798   29 NPNEIVNE-YSIFQKYLQRDSpsTDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNS 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  275 DELTPLHCAARNGHVRISEILL---DHGAPIQAKTKNGLSPIHMAAQGDH---LDCVRLLLQYNAEIDDIT-LDHLTPLH 347
Cdd:PHA02798  108 DGETPLYCLLSNGYINNLEILLfmiENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINTHNnKEKYDTLH 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  348 VAAHCGHHR----VAKVLLDKG---AKPN----SRALNGFTPLHIACKKNHIRVMELLLKTgASIDAVTESGLTPLHVAS 416
Cdd:PHA02798  188 CYFKYNIDRidadILKLFVDNGfiiNKENkshkKKFMEYLNSLLYDNKRFKKNILDFIFSY-IDINQVDELGFNPLYYSV 266

                         250       260       270
                  ....*....|....*....|....*....|..
gi 160707911  417 FMGHLPIVKNLLQRGASPNVSNVKVETPLHMA 448
Cdd:PHA02798  267 SHNNRKIFEYLLQLGGDINIITELGNTCLFTA 298
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 96-439 1.07e-09

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 63.39  E-value: 1.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   96 EVVRELVNYGANVNAQSQKGFTPL--YMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGhENVVAHLINY--- 170
Cdd:PHA02716  193 DILEWLCNNGVNVNLQNNHLITPLhtYLITGNVCASVIKKIIELGGDMDMKCVNGMSPIMTYIINI-DNINPEITNIyie 271

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  171 ---GTKGKVRLPALHI---AARNDDTRTAAVLLQNDPNPDVLSKTGFTPLH--IAAHYENLNVAQLLLNRGASVNFTPQN 242
Cdd:PHA02716  272 sldGNKVKNIPMILHSyitLARNIDISVVYSFLQPGVKLHYKDSAGRTCLHqyILRHNISTDIIKLLHEYGNDLNEPDNI 351

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  243 GITPLHIASRRGNVI--------------MVRLLLDRGAQIETRTKDELTPLH---CAARN-GHVRISEILldhgapIQA 304
Cdd:PHA02716  352 GNTVLHTYLSMLSVVnildpetdndirldVIQCLISLGADITAVNCLGYTPLTsyiCTAQNyMYYDIIDCL------ISD 425

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  305 KTKNGLSpiHMAAQG-----DHLDCV--RLLLQYNAEIDDITLDH----LTPLHVAAHCGhhrvakvlLDKGAKPNSRAL 373
Cdd:PHA02716  426 KVLNMVK--HRILQDllirvDDTPCIihHIIAKYNIPTDLYTDEYepydSTKIHDVYHCA--------IIERYNNAVCET 495

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160707911  374 NGFTPLHIA--CKKNHIRVME---LLLKTGASIDAVTESGLTPLHVA----SFMGHLP-IVKNLLQRgaSPNVSNV 439
Cdd:PHA02716  496 SGMTPLHVSiiSHTNANIVMDsfvYLLSIQYNINIPTKNGVTPLMLTmrnnRLSGHQWyIVKNILDK--RPNVDIV 569
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 110-330 1.28e-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: 1.28e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   110 AQSQKGFTPlymAAQENHLEVVKFLLENGA--NQNVATEDGFTPLAVALQQG-HENVVAHLINYGTKGKVRLPALHIAAR 186
Cdd:TIGR00870   15 SDEEKAFLP---AAERGDLASVYRDLEEPKklNINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAVGDTLLHAISL 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   187 ND--------------DTRTAAVLLQNDPNPDVLSKtGFTPLHIAAHYENLNVAQLLLNRGASVN-------FTPQNGIT 245
Cdd:TIGR00870   92 EYvdaveaillhllaaFRKSGPLELANDQYTSEFTP-GITALHLAAHRQNYEIVKLLLERGASVParacgdfFVKSQGVD 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   246 -------PLHIASRRGNVIMVRLLLDRGAQIETRtkDEL--TPLHCA-------ARNGHVRIS--EILLDHGAPIQAKTK 307
Cdd:TIGR00870  171 sfyhgesPLNAAACLGSPSIVALLSEDPADILTA--DSLgnTLLHLLvmenefkAEYEELSCQmyNFALSLLDKLRDSKE 248

                          250       260       270
                   ....*....|....*....|....*....|
gi 160707911   308 -------NGLSPIHMAAQGDHLDCVRLLLQ 330
Cdd:TIGR00870  249 levilnhQGLTPLKLAAKEGRIVLFRLKLA 278
Ank_4 pfam13637
Ankyrin repeats (many copies);
606-659 1.31e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.36  E-value: 1.31e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 160707911   606 GYTPLHIAAKQNQIEVARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVALLL 659
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 237-334 1.60e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 62.99  E-value: 1.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  237 NFTPQNGITP--LHIAS-------RRGNVIMVRLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILLDHGAPIQAKTK 307
Cdd:PTZ00322   67 NLTTEEVIDPvvAHMLTvelcqlaASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDK 146

                          90       100
                  ....*....|....*....|....*..
gi 160707911  308 NGLSPIHMAAQGDHLDCVRLLLQYNAE 334
Cdd:PTZ00322  147 DGKTPLELAEENGFREVVQLLSRHSQC 173
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 542-778 1.86e-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: 1.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  542 TPLHVAAKYGKVR-LAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLprggsphspawngytplhiaakqnqiE 620
Cdd:cd22192    19 SPLLLAAKENDVQaIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLM--------------------------E 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  621 VARSLLQYggSANAESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTplhlvsqegHVPVADVLIKHGvtvda 700
Cdd:cd22192    73 AAPELVNE--PMTSDLYQGETALHIAVVNQNLNLVRELIARGADVVSPRATGTF---------FRPGPKNLIYYG----- 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  701 ttrmgYTPLHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVT----LLL-----KNGASPNEVSSN- 770
Cdd:cd22192   137 -----EHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFACqmydLILsydkeDDLQPLDLVPNNq 211


                  ....*...
gi 160707911  771 GTTPLAIA 778
Cdd:cd22192   212 GLTPFKLA 219
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 21-232 2.06e-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: 2.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   21 LRAARSGNLDkALDHLRNGVDINTCnQNGLNG---LHLASKEGHVKMVVELLH--KEIILETTTK---KGNTALHIAALA 92
Cdd:cd22192    22 LLAAKENDVQ-AIKKLLKCPSCDLF-QRGALGetaLHVAALYDNLEAAVVLMEaaPELVNEPMTSdlyQGETALHIAVVN 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   93 GQDEVVRELVNYGANVNAQSQKG--FT------------PLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQ 158
Cdd:cd22192   100 QNLNLVRELIARGADVVSPRATGtfFRpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQ 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  159 GHENVVAHLINygtkgkvrlpalhiaarnddtrtaaVLLQNDPNPD------VLSKTGFTPLHIAAHYENLNVAQLLLNR 232
Cdd:cd22192   180 PNKTFACQMYD-------------------------LILSYDKEDDlqpldlVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
Ank_4 pfam13637
Ankyrin repeats (many copies);
245-296 3.13e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.20  E-value: 3.13e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 160707911   245 TPLHIASRRGNVIMVRLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILL 296
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 507-665 3.45e-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: 3.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  507 GHTPLHTAA---REGHVDTALALLE--------KEASQACMTK---KGFTPLHVAAKYGKVRLAELLLEH--DAHPNAAG 570
Cdd:cd21882    26 GKTCLHKAAlnlNDGVNEAIMLLLEaapdsgnpKELVNAPCTDefyQGQTALHIAIENRNLNLVRLLVENgaDVSARATG 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  571 KN-----------GLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWN---GYTPLHIAAKQNQIEVARS---------LLQ 627
Cdd:cd21882   106 RFfrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPAALEAQdslGNTVLHALVLQADNTPENSafvcqmynlLLS 185

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 160707911  628 YGGSANA----ESV---QGVTPLHLAAQEGHTEMVALLLSKQANG 665
Cdd:cd21882   186 YGAHLDPtqqlEEIpnhQGLTPLKLAAVEGKIVMFQHILQREFSG 230
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 617-779 3.91e-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: 3.91e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   617 NQIEVARSLLQYGGSANAESVQ-------GVTPLHLAAQEG-HTEMVALLLSKQANGNLGNksglTPLHLVSQEGHVPVA 688
Cdd:TIGR00870   23 PAAERGDLASVYRDLEEPKKLNincpdrlGRSALFVAAIENeNLELTELLLNLSCRGAVGD----TLLHAISLEYVDAVE 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   689 DVLI-------KHGVTVDATTRM------GYTPLHVASHYGNIKLVKFLLQHQADVNAKTK--------------LGYSP 741
Cdd:TIGR00870   99 AILLhllaafrKSGPLELANDQYtseftpGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESP 178

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 160707911   742 LHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIAK 779
Cdd:TIGR00870  179 LNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLV 216
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 540-743 5.38e-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: 5.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  540 GFTPLHVAAKY---GKVRLAELLLEHDAHPNAAGK-----------NGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPA-- 603
Cdd:cd21882    26 GKTCLHKAALNlndGVNEAIMLLLEAAPDSGNPKElvnapctdefyQGQTALHIAIENRNLNLVRLLVENGADVSARAtg 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  604 -----------WNGYTPLHIAAKQNQIEVARSLLQYGGSANAESVQ---GVTPLH-LAAQEGHTEMVALLLSKQANGNLG 668
Cdd:cd21882   106 rffrkspgnlfYFGELPLSLAACTNQEEIVRLLLENGAQPAALEAQdslGNTVLHaLVLQADNTPENSAFVCQMYNLLLS 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  669 NKSGLTPLhlvsqeghVPVADVlikhgvtvdaTTRMGYTPLHVASHYGNIKLVKFLLQHQADVNAK------TKLGYSPL 742
Cdd:cd21882   186 YGAHLDPT--------QQLEEI----------PNHQGLTPLKLAAVEGKIVMFQHILQREFSGPYQplsrkfTEWTYGPV 247


                  .
gi 160707911  743 H 743
Cdd:cd21882   248 T 248
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 177-298 5.68e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 61.07  E-value: 5.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  177 RLPALHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNvAQLLLNRGASVNFTPQNGITPLHIASRRGNV 256
Cdd:PTZ00322   50 HLEALEATENKDATPDHNLTTEEVIDPVVAHMLTVELCQLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHV 128

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 160707911  257 IMVRLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILLDH 298
Cdd:PTZ00322  129 QVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
Ank_5 pfam13857
Ankyrin repeats (many copies);
361-415 6.04e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 53.50  E-value: 6.04e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 160707911   361 LLDKG-AKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVA 415
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 391-544 6.49e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 61.04  E-value: 6.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  391 MELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKAKANAK 470
Cdd:PLN03192  541 LEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPH 620

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160707911  471 AKDDqtpLHC-AARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALLEKEASQACM-TKKGFTPL 544
Cdd:PLN03192  621 AAGD---LLCtAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAnTDDDFSPT 693
PHA02798 PHA02798
ankyrin-like protein; Provisional
 96-339 7.09e-09

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 60.62  E-value: 7.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   96 EVVRELVNYGANVNAQSQKGFTPL-----YMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLIny 170
Cdd:PHA02798   52 DIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILL-- 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  171 gtkgkvrlpalhiaarnddtrtaaVLLQNDPNPDVLSKTGFTPLHI---AAHYENLNVAQLLLNRGASVN-FTPQNGITP 246
Cdd:PHA02798  130 ------------------------FMIENGADTTLLDKDGFTMLQVylqSNHHIDIEIIKLLLEKGVDINtHNNKEKYDT 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  247 LHIASR----RGNVIMVRLLLDRGAQIETRTK-------DELTPLHCAARNGHVRISEILLDHgAPIQAKTKNGLSPIHM 315
Cdd:PHA02798  186 LHCYFKynidRIDADILKLFVDNGFIINKENKshkkkfmEYLNSLLYDNKRFKKNILDFIFSY-IDINQVDELGFNPLYY 264

                         250       260
                  ....*....|....*....|....
gi 160707911  316 AAQGDHLDCVRLLLQYNAEIDDIT 339
Cdd:PHA02798  265 SVSHNNRKIFEYLLQLGGDINIIT 288
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 358-428 8.06e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 60.68  E-value: 8.06e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 160707911  358 AKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLL 428
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 196-341 8.95e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 60.65  E-value: 8.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  196 LLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLDRGAQIETRTKD 275
Cdd:PLN03192  544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAG 623

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160707911  276 ELtpLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQYNAEIDDITLD 341
Cdd:PLN03192  624 DL--LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTD 687
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 485-573 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 160707911  485 GHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALLEKEASQACMTKKGFTPLHVAAKYGKVRLAELLLEHDA 564
Cdd:PTZ00322   93 GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQ 172


                  ....*....
gi 160707911  565 HPNAAGKNG 573
Cdd:PTZ00322  173 CHFELGANA 181
Ank_4 pfam13637
Ankyrin repeats (many copies);
639-692 1.06e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.05  E-value: 1.06e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 160707911   639 GVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADVLI 692
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Death_NMPP84 cd08318
Death domain of Nuclear Matrix Protein P84; Death domain (DD) found in the Nuclear Matrix ...
 1418-1495 1.15e-08

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


Pssm-ID: 260030  Cd Length: 86  Bit Score: 53.68  E-value: 1.15e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 160707911 1418 RMAVIREHLGLSWAELARELQFSVEDINRIRvENPNSLLDQSTALLTLWVDREGENAKMENLYTALRNIDRSEIVNML 1495
Cdd:cd08318     9 QIDVLANKLGEQWKTLAPYLEMKDKDIRQIE-SDSEDMKMRAKQLLVTWQDREGAQATPEILMTALNAAGLNEIAENL 85
PHA02946 PHA02946
ankyin-like protein; Provisional
 63-247 1.16e-08

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 59.68  E-value: 1.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   63 KMVVELLHKEIILETTTKKGNTALHIAALAGQDEVVRELVNYGANVNAQSQKGFTPLYM--AAQENHLEVVKFLLENGAN 140
Cdd:PHA02946   53 RFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYlsGTDDEVIERINLLVQYGAK 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  141 -QNVATEDGFTPLaVALQQGHENVVAHLINYGTKGKV------RLPALHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTP 213
Cdd:PHA02946  133 iNNSVDEEGCGPL-LACTDPSERVFKKIMSIGFEARIvdkfgkNHIHRHLMSDNPKASTISWMMKLGISPSKPDHDGNTP 211

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 160707911  214 LHI--AAHYENLNVAQLLLnrgASVNFTPQN--GITPL 247
Cdd:PHA02946  212 LHIvcSKTVKNVDIINLLL---PSTDVNKQNkfGDSPL 246
Ank_4 pfam13637
Ankyrin repeats (many copies);
672-725 1.26e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.66  E-value: 1.26e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 160707911   672 GLTPLHLVSQEGHVPVADVLIKHGVTVDATTRMGYTPLHVASHYGNIKLVKFLL 725
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
724-778 1.69e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 52.35  E-value: 1.69e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 160707911   724 LLQH-QADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIA 778
Cdd:pfam13857    1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
117-168 1.72e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 1.72e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 160707911   117 TPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLI 168
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
476-527 2.49e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.89  E-value: 2.49e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 160707911   476 TPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALL 527
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
177-230 2.77e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.51  E-value: 2.77e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 160707911   177 RLPALHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLL 230
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 39-158 2.78e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 58.35  E-value: 2.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   39 GVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQD-EVVRELVNYGANVNAQSQ-KGF 116
Cdd:PHA02878  191 GANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDyDILKLLLEHGVDVNAKSYiLGL 270

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 160707911  117 TPLYMAAQENhlEVVKFLLENGANQNVATEDGFTPLAVALQQ 158
Cdd:PHA02878  271 TALHSSIKSE--RKLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 15-145 2.85e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.08  E-value: 2.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   15 DAATSFLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQ 94
Cdd:PHA02875  101 DGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGD 180

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 160707911   95 DEVVRELVNYGANVNAQSQKG-FTPLYMAAQENHLEVVKFLLENGANQNVAT 145
Cdd:PHA02875  181 IAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNIMF 232
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 481-649 4.18e-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: 4.18e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   481 AARIGHTGMVKLLLENGAS--PNLATTAGHTPLHTAAREGHVDTALALLEKEASQACMtkkGFTPLHVAAKyGKVRLAEL 558
Cdd:TIGR00870   24 AAERGDLASVYRDLEEPKKlnINCPDRLGRSALFVAAIENENLELTELLLNLSCRGAV---GDTLLHAISL-EYVDAVEA 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   559 LLEH--DAHP--------NAAGKN----GLTPLHVAVHHNNLDIVKLLLPRGG-------------SPHSP-AWNGYTPL 610
Cdd:TIGR00870  100 ILLHllAAFRksgplelaNDQYTSeftpGITALHLAAHRQNYEIVKLLLERGAsvparacgdffvkSQGVDsFYHGESPL 179

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 160707911   611 HIAAKQNQIEVARSLLQYGGSANAESVQGVTPLHLAAQE 649
Cdd:TIGR00870  180 NAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVME 218
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 89-236 4.41e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 58.34  E-value: 4.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   89 AALAGQDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENV----- 163
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIfrily 611

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 160707911  164 -VAHLINYGTKGKVrlpaLHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASV 236
Cdd:PLN03192  612 hFASISDPHAAGDL----LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
Ank_5 pfam13857
Ankyrin repeats (many copies);
101-155 7.86e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.42  E-value: 7.86e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 160707911   101 LVNYG-ANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVA 155
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02798 PHA02798
ankyrin-like protein; Provisional
 96-338 7.98e-08

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 57.15  E-value: 7.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   96 EVVRELVNYGANVNAQSQKGFTPLYMAAQE---NHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHenvvahlinygt 172
Cdd:PHA02798   90 DIVKILIENGADINKKNSDGETPLYCLLSNgyiNNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNH------------ 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  173 kgkvrlpalHIaarndDTRTAAVLLQNDPNPDVLS-KTGFTPLHIAAHYE----NLNVAQLLLNRGASVN----FTPQNG 243
Cdd:PHA02798  158 ---------HI-----DIEIIKLLLEKGVDINTHNnKEKYDTLHCYFKYNidriDADILKLFVDNGFIINkenkSHKKKF 223

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  244 I---TPLHIASRRGNVIMVRLLLdrgAQIETRTKDEL--TPLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQ 318
Cdd:PHA02798  224 MeylNSLLYDNKRFKKNILDFIF---SYIDINQVDELgfNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFE 300

                         250       260
                  ....*....|....*....|
gi 160707911  319 GDHLDCVRLLLQYNAEIDDI 338
Cdd:PHA02798  301 NESKFIFNSILNKKPNKNTI 320
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 393-461 8.91e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.22  E-value: 8.91e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 160707911  393 LLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLL 461
Cdd:PTZ00322  100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
Ank_5 pfam13857
Ankyrin repeats (many copies);
691-745 9.65e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.42  E-value: 9.65e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 160707911   691 LIKHG-VTVDATTRMGYTPLHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQA 745
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
228-283 1.05e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.04  E-value: 1.05e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 160707911   228 LLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLDRGAQIETRTKDELTPLHCA 283
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 589-660 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 160707911  589 VKLLLPRGGSPHSPAWNGYTPLHIAAKQNQIEVARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVALLLS 660
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 314-396 1.18e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.83  E-value: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  314 HMAAQGDHLDcVRLLLQYNAEIDDITLDHLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMEL 393
Cdd:PTZ00322   88 QLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                  ...
gi 160707911  394 LLK 396
Cdd:PTZ00322  167 LSR 169
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 646-822 1.26e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 56.80  E-value: 1.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  646 AAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADVLIKHGVTVDATTRMGYTPLHVASHYGNIKLVKFLL 725
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY 611

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  726 QHQADVNAKTklGYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIAKRLGYISVTDVLkvVTDETSVVLVSDK 805
Cdd:PLN03192  612 HFASISDPHA--AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLL--IMNGADVDKANTD 687

                         170
                  ....*....|....*..
gi 160707911  806 HRMSyPETVDEILDVSE 822
Cdd:PLN03192  688 DDFS-PTELRELLQKRE 703
Ank_4 pfam13637
Ankyrin repeats (many copies);
507-560 1.32e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.97  E-value: 1.32e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 160707911   507 GHTPLHTAAREGHVDTALALLEKEASQACMTKKGFTPLHVAAKYGKVRLAELLL 560
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
538-580 1.33e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 49.65  E-value: 1.33e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 160707911   538 KKGFTPLHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVA 580
Cdd:pfam13857   14 GEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
573-626 1.95e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.20  E-value: 1.95e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 160707911   573 GLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQIEVARSLL 626
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 509-606 2.12e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.06  E-value: 2.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  509 TPLHTAAREGHVDTALA---------------------LLEKEASQACMTKKGFTPLHVAAKYGKVRLAELLLEHDAHPN 567
Cdd:PTZ00322   63 TPDHNLTTEEVIDPVVAhmltvelcqlaasgdavgariLLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPT 142

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 160707911  568 AAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNG 606
Cdd:PTZ00322  143 LLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGANA 181
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 487-788 2.27e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 55.52  E-value: 2.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  487 TGMVKLLLENGASPNlattaghtplhtaaREGHVDTAL-ALLEKEASQACMTKKgftplhvaakygkvrLAELLLEHDAH 565
Cdd:PHA02989   50 IKIVKLLIDNGADVN--------------YKGYIETPLcAVLRNREITSNKIKK---------------IVKLLLKFGAD 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  566 PNAAGKNGLTPLHVAVHH---NNLDIVKLLLPRGGSPHS-PAWNGYTPLHIAAKQNQI--EVARSLLQYGgsanaesvqg 639
Cdd:PHA02989  101 INLKTFNGVSPIVCFIYNsniNNCDMLRFLLSKGINVNDvKNSRGYNLLHMYLESFSVkkDVIKILLSFG---------- 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  640 VTPLHLAAQEGHTEMvalllskqaNGNLGNKsgltpLHLVSqeghVPVADVLIKHGVTVDATTRMGYTPL------HVAS 713
Cdd:PHA02989  171 VNLFEKTSLYGLTPM---------NIYLRND-----IDVIS----IKVIKYLIKKGVNIETNNNGSESVLesfldnNKIL 232

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 160707911  714 HYGNIKLVKFLLQHqADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIAKRLGYISVTD 788
Cdd:PHA02989  233 SKKEFKVLNFILKY-IKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLN 306
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 128-312 2.51e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 56.03  E-value: 2.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  128 LEVVKFLLENGAnQNVATEDGFTPLAVAlQQGHENVVAHLINYG-------TKGKVrlpALHIAARNDDTRTAAVLLQND 200
Cdd:PLN03192  507 LNVGDLLGDNGG-EHDDPNMASNLLTVA-STGNAALLEELLKAKldpdigdSKGRT---PLHIAASKGYEDCVLVLLKHA 581

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  201 PNPDVLSKTGFTPLH---IAAHYENLNVaqllLNRGASVNfTPQNGITPLHIASRRGNVIMVRLLLDRGAQIETRTKDEL 277
Cdd:PLN03192  582 CNVHIRDANGNTALWnaiSAKHHKIFRI----LYHFASIS-DPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGA 656

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 160707911  278 TPLHCAARNGHVRISEILLDHGAPI-QAKTKNGLSP 312
Cdd:PLN03192  657 TALQVAMAEDHVDMVRLLIMNGADVdKANTDDDFSP 692
Ank_5 pfam13857
Ankyrin repeats (many copies);
559-613 2.75e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.88  E-value: 2.75e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 160707911   559 LLEHD-AHPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIA 613
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 296-567 3.74e-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: 3.74e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   296 LDHGAPIQAKTKN--GLSPIHMAA-QGDHLDCVRLLLQYNAEIDdiTLDHLtpLHVAAHCGHHRVAKVLLDKGAKP---- 368
Cdd:TIGR00870   37 LEEPKKLNINCPDrlGRSALFVAAiENENLELTELLLNLSCRGA--VGDTL--LHAISLEYVDAVEAILLHLLAAFrksg 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   369 -----NSRALNGFTPlhiackknhirvmelllktgasidavtesGLTPLHVASFMGHLPIVKNLLQRGASPNVS---NVK 440
Cdd:TIGR00870  113 plelaNDQYTSEFTP-----------------------------GITALHLAAHRQNYEIVKLLLERGASVPARacgDFF 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   441 VETPLHMAARAGhtevakyllqnkakanakakddQTPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHV 520
Cdd:TIGR00870  164 VKSQGVDSFYHG----------------------ESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVMENEF 221

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   521 ------------DTALALLEKEAS----QACMTKKGFTPLHVAAKYGKVRLAELLL-------EHDAHPN 567
Cdd:TIGR00870  222 kaeyeelscqmyNFALSLLDKLRDskelEVILNHQGLTPLKLAAKEGRIVLFRLKLaikykqkKFVAWPN 291
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 644-727 4.85e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.90  E-value: 4.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  644 HLAAQeGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADVLIKHGVTVDATTRMGYTPLHVASHYGNIKLVKF 723
Cdd:PTZ00322   88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                  ....
gi 160707911  724 LLQH 727
Cdd:PTZ00322  167 LSRH 170
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 707-806 4.97e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 52.51  E-value: 4.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  707 TPLH--VASHYGNIKLVKFLLQHQADVNAKTK-LGYSPLH---QAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIakR 780
Cdd:PHA02859   53 TPIFscLEKDKVNVEILKFLIENGADVNFKTRdNNLSALHhylSFNKNVEPEILKILIDSGSSITEEDEDGKNLLHM--Y 130

                          90       100
                  ....*....|....*....|....*..
gi 160707911  781 LGYISV-TDVLKVVTDETSVVLVSDKH 806
Cdd:PHA02859  131 MCNFNVrINVIKLLIDSGVSFLNKDFD 157
Ank_5 pfam13857
Ankyrin repeats (many copies);
196-250 6.15e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.11  E-value: 6.15e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 160707911   196 LLQNDP-NPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIA 250
Cdd:pfam13857    1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 20-297 6.34e-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: 6.34e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911    20 FLRAARSGNLDKALDHLRNG--VDINTCNQNGLNGLHLASKEGHVKMVVELLHKeiiLETTTKKGNTALHIAALAGQDeV 97
Cdd:TIGR00870   21 FLPAAERGDLASVYRDLEEPkkLNINCPDRLGRSALFVAAIENENLELTELLLN---LSCRGAVGDTLLHAISLEYVD-A 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911    98 VRELVNYGAN----------VNAQS----QKGFTPLYMAAQENHLEVVKFLLENGANQNV-ATEDGFTplavaLQQGHEn 162
Cdd:TIGR00870   97 VEAILLHLLAafrksgplelANDQYtsefTPGITALHLAAHRQNYEIVKLLLERGASVPArACGDFFV-----KSQGVD- 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   163 vvahLINYGtkgkvRLPaLHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIA-------AHYENL-----NVAQLLL 230
Cdd:TIGR00870  171 ----SFYHG-----ESP-LNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLvmenefkAEYEELscqmyNFALSLL 240

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 160707911   231 NRGAS-------VNFtpqNGITPLHIASRRGNVIMVRLLLdrgaQIETRTKDeltplHCAARNGHVRISEILLD 297
Cdd:TIGR00870  241 DKLRDskeleviLNH---QGLTPLKLAAKEGRIVLFRLKL----AIKYKQKK-----FVAWPNGQQLLSLYWLE 302
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 71-240 6.77e-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: 6.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   71 KEIILETTTK---KGNTALHIAALAGQDEVVRELVNYGANVNAQSQKGF-------------TPLYMAAQENHLEVVKFL 134
Cdd:cd21882    59 KELVNAPCTDefyQGQTALHIAIENRNLNLVRLLVENGADVSARATGRFfrkspgnlfyfgeLPLSLAACTNQEEIVRLL 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  135 LENGANqnvatedgftPLAVALQQGHENVVAHLINYGTKGKVRLPALHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPL 214
Cdd:cd21882   139 LENGAQ----------PAALEAQDSLGNTVLHALVLQADNTPENSAFVCQMYNLLLSYGAHLDPTQQLEEIPNHQGLTPL 208

                         170       180
                  ....*....|....*....|....*.
gi 160707911  215 HIAAHYENLNVAQLLLNRGASVNFTP 240
Cdd:cd21882   209 KLAAVEGKIVMFQHILQREFSGPYQP 234
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 307-402 6.78e-07

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 50.65  E-value: 6.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  307 KNGLSPIHMAAQGDHLDC---VRLLLQYNAEIDDI-TLDHLTPLHVAAHCGHHRVAKVLLDKgAKPNSRALNGF--TPLH 380
Cdd:PHA02736   53 RHGKQCVHIVSNPDKADPqekLKLLMEWGADINGKeRVFGNTPLHIAVYTQNYELATWLCNQ-PGVNMEILNYAfkTPYY 131

                          90       100
                  ....*....|....*....|..
gi 160707911  381 IACKKNHIRVMELLLKTGASID 402
Cdd:PHA02736  132 VACERHDAKMMNILRAKGAQCK 153
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 705-736 8.86e-07

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 46.90  E-value: 8.86e-07
                           10        20        30
                   ....*....|....*....|....*....|...
gi 160707911   705 GYTPLHVAS-HYGNIKLVKFLLQHQADVNAKTK 736
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA02798 PHA02798
ankyrin-like protein; Provisional
 552-778 8.87e-07

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 53.69  E-value: 8.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  552 KVRLAELLLEHDAHPNAAGKNGLTPL-----HVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQ---NQIEVAR 623
Cdd:PHA02798   50 STDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNgyiNNLEILL 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  624 SLLQYGGSANAESVQGVTPLHLAAQEGHT---EMVALLLSKQANGNL-GNKSGLTPLHLVSQEG----HVPVADVLIKHG 695
Cdd:PHA02798  130 FMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDINThNNKEKYDTLHCYFKYNidriDADILKLFVDNG 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  696 VTV---DATTRMGYTPLHVASHYGNIK----LVKFLLQHqADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNEVS 768
Cdd:PHA02798  210 FIInkeNKSHKKKFMEYLNSLLYDNKRfkknILDFIFSY-IDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIIT 288

                         250
                  ....*....|
gi 160707911  769 SNGTTPLAIA 778
Cdd:PHA02798  289 ELGNTCLFTA 298
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 374-403 9.48e-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: 9.48e-07
                            10        20        30
                    ....*....|....*....|....*....|
gi 160707911    374 NGFTPLHIACKKNHIRVMELLLKTGASIDA 403
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
738-790 1.11e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.27  E-value: 1.11e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 160707911   738 GYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIAKRLGYISVTDVL 790
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
Death_RAIDD cd08319
Death domain of RIP-associated ICH-1 homologous protein with a death domain; Death domain (DD) ...
 1412-1487 1.16e-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: 1.16e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160707911 1412 TDRVEMRMAvirEHLGLSWAELARELQFSVEDINRIRVENPNSLLDQSTALLTLWVDREGENAKMENLYTALRNID 1487
Cdd:cd08319     1 TDRQLNKLA---QRLGPEWEQVLLDLGLSKADIYRCKADHPYNVQSQIVEALVKWKQRQGKKATVQSLIQSLKAVE 73
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 603-725 1.37e-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: 1.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  603 AWNGYTPLHIAAKQNQIEVARSLLQYGGSANAESvQGV---------------TPLHLAAQEGHTEMVALLLSK-QANGN 666
Cdd:cd22194   138 AYEGQTALNIAIERRQGDIVKLLIAKGADVNAHA-KGVffnpkykhegfyfgeTPLALAACTNQPEIVQLLMEKeSTDIT 216

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160707911  667 LGNKSGLTPLHLVsqeghVPVAD---------------VLIKHGVTVDATTR--MGYTPLHVASHYGNIKLVKFLL 725
Cdd:cd22194   217 SQDSRGNTVLHAL-----VTVAEdsktqndfvkrmydmILLKSENKNLETIRnnEGLTPLQLAAKMGKAEILKYIL 287
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 29-232 1.49e-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: 1.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   29 LDKALDHLRNGVdintcNQNGLNGLHLASKEGHVKMVVELLHKEiiletTTKKGNTALHIAALAGQDEVVRELVNYGANV 108
Cdd:cd22196    51 LLKAMLNLHNGQ-----NDTISLLLDIAEKTGNLKEFVNAAYTD-----SYYKGQTALHIAIERRNMHLVELLVQNGADV 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  109 NA----------QSQKGF----TPLYMAAQENHLEVVKFLLENGANQ-NVATEDGFTplavalqqgheNVVAHlinygtk 173
Cdd:cd22196   121 HArasgeffkkkKGGPGFyfgeLPLSLAACTNQLDIVKFLLENPHSPaDISARDSMG-----------NTVLH------- 182

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 160707911  174 gkvrlpALHIAARNDDTRTAAV--------LLQNDPNP-----DVLSKTGFTPLHIAAHYENLNVAQLLLNR 232
Cdd:cd22196   183 ------ALVEVADNTPENTKFVtkmyneilILGAKIRPllkleEITNKKGLTPLKLAAKTGKIGIFAYILGR 248
PHA02946 PHA02946
ankyin-like protein; Provisional
 229-412 1.50e-06

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 52.75  E-value: 1.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  229 LLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLDRGAQIETRTKDELTPLHCAARNGHVRISEI--LLDHGAPIQAKT 306
Cdd:PHA02946   58 LLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIERInlLVQYGAKINNSV 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  307 -KNGLSPIHMAAQGDHLDCVRLL-LQYNAEIDDITLDHLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACK 384
Cdd:PHA02946  138 dEEGCGPLLACTDPSERVFKKIMsIGFEARIVDKFGKNHIHRHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCS 217

                         170       180       190
                  ....*....|....*....|....*....|
gi 160707911  385 KN--HIRVMELLLKTgASIDAVTESGLTPL 412
Cdd:PHA02946  218 KTvkNVDIINLLLPS-TDVNKQNKFGDSPL 246
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 87-170 1.56e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.98  E-value: 1.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   87 HIAAlAGQDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAH 166
Cdd:PTZ00322   88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                  ....
gi 160707911  167 LINY 170
Cdd:PTZ00322  167 LSRH 170
Ank_5 pfam13857
Ankyrin repeats (many copies);
625-679 1.61e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.96  E-value: 1.61e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 160707911   625 LLQYGG-SANAESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLV 679
Cdd:pfam13857    1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 704-733 1.74e-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: 1.74e-06
                            10        20        30
                    ....*....|....*....|....*....|
gi 160707911    704 MGYTPLHVASHYGNIKLVKFLLQHQADVNA 733
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 705-733 1.79e-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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 46.10  E-value: 1.79e-06
                           10        20
                   ....*....|....*....|....*....
gi 160707911   705 GYTPLHVASHYGNIKLVKFLLQHQADVNA 733
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 446-527 2.06e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.59  E-value: 2.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  446 HMAArAGHTEVAKYLLQNKAKANAKAKDDQTPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALA 525
Cdd:PTZ00322   88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                  ..
gi 160707911  526 LL 527
Cdd:PTZ00322  167 LS 168
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 82-265 2.18e-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: 2.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   82 GNTALHIAALAGQD----------EVVRELVNYGANVNAQSQ----KGFTPLYMAAQENHLEVVKFLLENGAN-QNVATE 146
Cdd:cd21882    26 GKTCLHKAALNLNDgvneaimlllEAAPDSGNPKELVNAPCTdefyQGQTALHIAIENRNLNLVRLLVENGADvSARATG 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  147 DGFT------------PLAVALQQGHENVVAHLINYGTKgkvrlPAlHIAARND--DTRTAAVLLQNDPNPDvlsKTGFt 212
Cdd:cd21882   106 RFFRkspgnlfyfgelPLSLAACTNQEEIVRLLLENGAQ-----PA-ALEAQDSlgNTVLHALVLQADNTPE---NSAF- 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  213 plhiAAHYENlnvaqLLLNRGASVNFTPQ-------NGITPLHIASRRGNVIMVRLLLDR 265
Cdd:cd21882   176 ----VCQMYN-----LLLSYGAHLDPTQQleeipnhQGLTPLKLAAVEGKIVMFQHILQR 226
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 96-265 2.52e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 52.05  E-value: 2.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   96 EVVRELVNYGANVNA-QSQKGFTPLYMAAQENHL--EVVKFLLENGANQNVATE-DGFTPLAVALQQGHENVVAHLINYG 171
Cdd:PHA02989  125 DMLRFLLSKGINVNDvKNSRGYNLLHMYLESFSVkkDVIKILLSFGVNLFEKTSlYGLTPMNIYLRNDIDVISIKVIKYL 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  172 TKGKVRLP---ALHIAARNDDTRTAAVLLQND----------PNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNF 238
Cdd:PHA02989  205 IKKGVNIEtnnNGSESVLESFLDNNKILSKKEfkvlnfilkyIKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYN 284

                         170       180
                  ....*....|....*....|....*..
gi 160707911  239 TPQNGITPLHIASRRGNVIMVRLLLDR 265
Cdd:PHA02989  285 VSKDGDTVLTYAIKHGNIDMLNRILQL 311
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 114-143 2.65e-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: 45.27  E-value: 2.65e-06
                            10        20        30
                    ....*....|....*....|....*....|
gi 160707911    114 KGFTPLYMAAQENHLEVVKFLLENGANQNV 143
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 388-569 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 160707911  388 IRVMELLLK-TGASIDAVTESGLtpLHVASfMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKAK 466
Cdd:PLN03192  507 LNVGDLLGDnGGEHDDPNMASNL--LTVAS-TGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACN 583

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  467 ANAKAKDDQTPLHCAARIGHTGMVKLLLENGASPNlaTTAGHTPLHTAAREGHVDTALALLEKEASQACMTKKGFTPLHV 546
Cdd:PLN03192  584 VHIRDANGNTALWNAISAKHHKIFRILYHFASISD--PHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQV 661

                         170       180
                  ....*....|....*....|...
gi 160707911  547 AAKYGKVRLAELLLEHDAHPNAA 569
Cdd:PLN03192  662 AMAEDHVDMVRLLIMNGADVDKA 684
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 212-309 4.64e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 49.43  E-value: 4.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  212 TPLH--IAAHYENLNVAQLLLNRGASVNF-TPQNGITPLH---IASRRGNVIMVRLLLDRGAQIETRTKDELTPLHCAAR 285
Cdd:PHA02859   53 TPIFscLEKDKVNVEILKFLIENGADVNFkTRDNNLSALHhylSFNKNVEPEILKILIDSGSSITEEDEDGKNLLHMYMC 132

                          90       100
                  ....*....|....*....|....*.
gi 160707911  286 NGHVRIS--EILLDHGAPIQAKTKNG 309
Cdd:PHA02859  133 NFNVRINviKLLIDSGVSFLNKDFDN 158
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 205-544 5.19e-06

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 51.45  E-value: 5.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  205 VLSKTGFTPLH--IAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVI--MVRLLLDRGAQIETRTKDELTPL 280
Cdd:PHA02716  172 VCKKTGYGILHayLGNMYVDIDILEWLCNNGVNVNLQNNHLITPLHTYLITGNVCasVIKKIIELGGDMDMKCVNGMSPI 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  281 HCAARNGHVRISEILLDHGAPIQA-KTKNGLSPIHM---AAQGDHLDCVRLLLQYNAEIDDITLDHLTPLH--VAAHCGH 354
Cdd:PHA02716  252 MTYIINIDNINPEITNIYIESLDGnKVKNIPMILHSyitLARNIDISVVYSFLQPGVKLHYKDSAGRTCLHqyILRHNIS 331

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  355 HRVAKVLLDKGAKPNSRALNGFTPLHIACKK------------NHIR--VMELLLKTGASIDAVTESGLTPL-----HVA 415
Cdd:PHA02716  332 TDIIKLLHEYGNDLNEPDNIGNTVLHTYLSMlsvvnildpetdNDIRldVIQCLISLGADITAVNCLGYTPLtsyicTAQ 411

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  416 SFMGHLPI-------VKNLLQRGASPNVSNVKVETPlhmaaRAGHTEVAKYLLQNKAKANAKAKDDQTPLHCAArigHTG 488
Cdd:PHA02716  412 NYMYYDIIdclisdkVLNMVKHRILQDLLIRVDDTP-----CIIHHIIAKYNIPTDLYTDEYEPYDSTKIHDVY---HCA 483

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 160707911  489 MVKLLlengaSPNLATTAGHTPLHTAAREGH-----VDTALALLEKEASQACMTKKGFTPL 544
Cdd:PHA02716  484 IIERY-----NNAVCETSGMTPLHVSIISHTnanivMDSFVYLLSIQYNINIPTKNGVTPL 539
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 473-504 5.23e-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: 5.23e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 160707911   473 DDQTPLHCAA-RIGHTGMVKLLLENGASPNLAT 504
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
Ank_5 pfam13857
Ankyrin repeats (many copies);
393-448 5.43e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.42  E-value: 5.43e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 160707911   393 LLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMA 448
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02798 PHA02798
ankyrin-like protein; Provisional
 120-415 5.62e-06

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 50.99  E-value: 5.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  120 YMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALqqghenvvAHLINYGTKGKVRLpalhiaarnddtrtaaVLLQN 199
Cdd:PHA02798   43 YLQRDSPSTDIVKLFINLGANVNGLDNEYSTPLCTIL--------SNIKDYKHMLDIVK----------------ILIEN 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  200 DPNPDVLSKTGFTPLHIAAHYENLNVAQLLL---NRGASVNFTPQNGITPLHIASRRGNVI---MVRLLLDRGAQIETRT 273
Cdd:PHA02798   99 GADINKKNSDGETPLYCLLSNGYINNLEILLfmiENGADTTLLDKDGFTMLQVYLQSNHHIdieIIKLLLEKGVDINTHN 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  274 KDE-LTPLHCAARNGHVRIS----EILLDHGAPIQAKTKNGLSPIhmaaqgdhLDCVRLLLQYNAEIDDITLDhltplhv 348
Cdd:PHA02798  179 NKEkYDTLHCYFKYNIDRIDadilKLFVDNGFIINKENKSHKKKF--------MEYLNSLLYDNKRFKKNILD------- 243

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 160707911  349 aahcghhrvakvLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVA 415
Cdd:PHA02798  244 ------------FIFSYIDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTA 298
Ank_5 pfam13857
Ankyrin repeats (many copies);
606-646 6.17e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.03  E-value: 6.17e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 160707911   606 GYTPLHIAAKQNQIEVARSLLQYGGSANAESVQGVTPLHLA 646
Cdd:pfam13857   16 GYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 539-662 7.23e-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: 7.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  539 KGFTPLHVAAKYGKVRLAELLLEHDAHPNAAGKN--------------GLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAW 604
Cdd:cd22194   140 EGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEIVQLLMEKESTDITSQD 219

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 160707911  605 N-GYTPLH---IAAKQNQ------IEVARSLLQYGGSANAESV---QGVTPLHLAAQEGHTEMVALLLSKQ 662
Cdd:cd22194   220 SrGNTVLHalvTVAEDSKtqndfvKRMYDMILLKSENKNLETIrnnEGLTPLQLAAKMGKAEILKYILSRE 290
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 374-406 7.89e-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: 7.89e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 160707911   374 NGFTPLHIACKK-NHIRVMELLLKTGASIDAVTE 406
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 635-783 8.74e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 50.83  E-value: 8.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  635 ESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADVLIKHGVTVDATTRMGYTPLHVASH 714
Cdd:PHA02876  141 ESIEYMKLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVD 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  715 YGNIKLVKFLLQHQADVNA--------------KTKL-----GYS----------PLHQAAQQGH-TDIVTLLLKNGASP 764
Cdd:PHA02876  221 SKNIDTIKAIIDNRSNINKndlsllkairnedlETSLllydaGFSvnsiddckntPLHHASQAPSlSRLVPKLLERGADV 300

                         170
                  ....*....|....*....
gi 160707911  765 NEVSSNGTTPLAIAKRLGY 783
Cdd:PHA02876  301 NAKNIKGETPLYLMAKNGY 319
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 81-111 9.23e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 43.82  E-value: 9.23e-06
                           10        20        30
                   ....*....|....*....|....*....|..
gi 160707911    81 KGNTALHIAAL-AGQDEVVRELVNYGANVNAQ 111
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNAR 32
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 81-110 9.76e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 43.73  E-value: 9.76e-06
                            10        20        30
                    ....*....|....*....|....*....|
gi 160707911     81 KGNTALHIAALAGQDEVVRELVNYGANVNA 110
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 81-232 9.82e-06

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: 9.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   81 KGNTALHIAALAGQDEVVRELVNYGANVNAQSQKGF--------------TPLYMAAQENHLEVVKFLLENganqnvate 146
Cdd:cd22193    75 EGQTALHIAIERRQGDIVALLVENGADVHAHAKGRFfqpkyqgegfyfgeLPLSLAACTNQPDIVQYLLEN--------- 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  147 dGFTPLAVALQQGHENVVAHlinygtkgkvrlpALHIAARNDDTRTAAV------LLQNDPN--PDV-----LSKTGFTP 213
Cdd:cd22193   146 -EHQPADIEAQDSRGNTVLH-------------ALVTVADNTKENTKFVtrmydmILIRGAKlcPTVeleeiRNNDGLTP 211

                         170
                  ....*....|....*....
gi 160707911  214 LHIAAHYENLNVAQLLLNR 232
Cdd:cd22193   212 LQLAAKMGKIEILKYILQR 230
Ank_5 pfam13857
Ankyrin repeats (many copies);
262-316 1.28e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.26  E-value: 1.28e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 160707911   262 LLDRG-AQIETRTKDELTPLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMA 316
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 517-662 1.34e-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: 1.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  517 EGHVDTALALLE--------KEASQACMTK---KGFTPLHVAAKYGKVRLAELLLEHDAHPNAA----------GKNGL- 574
Cdd:cd22196    60 NGQNDTISLLLDiaektgnlKEFVNAAYTDsyyKGQTALHIAIERRNMHLVELLVQNGADVHARasgeffkkkkGGPGFy 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  575 ---TPLHVAVHHNNLDIVKLLLPrggSPHSPA------WNGYTPLH--IAAKQNQIEVAR-------SLLQYGG----SA 632
Cdd:cd22196   140 fgeLPLSLAACTNQLDIVKFLLE---NPHSPAdisardSMGNTVLHalVEVADNTPENTKfvtkmynEILILGAkirpLL 216

                         170       180       190
                  ....*....|....*....|....*....|...
gi 160707911  633 NAESV---QGVTPLHLAAQEGHTEMVALLLSKQ 662
Cdd:cd22196   217 KLEEItnkKGLTPLKLAAKTGKIGIFAYILGRE 249
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 611-694 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 160707911  611 HIAAKQNQIEvARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADV 690
Cdd:PTZ00322   88 QLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                  ....
gi 160707911  691 LIKH 694
Cdd:PTZ00322  167 LSRH 170
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 172-433 1.56e-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: 1.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  172 TKGKVRLPALHIAARNDDTR---TAAVLLQNDPNPDVLSKTGFTPLhIAAHYEnlnvaqlllnrgasvnftpqnGITPLH 248
Cdd:cd21882    21 QRGATGKTCLHKAALNLNDGvneAIMLLLEAAPDSGNPKELVNAPC-TDEFYQ---------------------GQTALH 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  249 IASRRGNVIMVRLLLDRGAQIETRTKdeltplhcaarnghvriseilldhGAPIQAKTKNGL----SPIHMAAQGDHLDC 324
Cdd:cd21882    79 IAIENRNLNLVRLLVENGADVSARAT------------------------GRFFRKSPGNLFyfgeLPLSLAACTNQEEI 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  325 VRLLLQYNAEIDDITL-DHL--TPLHvaahcghhrvAKVLLDKGAKPNSRalngftplhIACKknhirVMELLLKTGA-- 399
Cdd:cd21882   135 VRLLLENGAQPAALEAqDSLgnTVLH----------ALVLQADNTPENSA---------FVCQ-----MYNLLLSYGAhl 190

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 160707911  400 ----SIDAVT-ESGLTPLHVASFMGHLPIVKNLLQRGAS 433
Cdd:cd21882   191 dptqQLEEIPnHQGLTPLKLAAVEGKIVMFQHILQREFS 229
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 572-600 1.61e-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: 1.61e-05
                            10        20
                    ....*....|....*....|....*....
gi 160707911    572 NGLTPLHVAVHHNNLDIVKLLLPRGGSPH 600
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 36-110 1.67e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 49.28  E-value: 1.67e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 160707911   36 LRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQDEVVRELVNYGANVNA 110
Cdd:PHA03100  179 LSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
Ank_4 pfam13637
Ankyrin repeats (many copies);
53-102 1.71e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.80  E-value: 1.71e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 160707911    53 LHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQDEVVRELV 102
Cdd:pfam13637    5 LHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 408-438 1.82e-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: 43.05  E-value: 1.82e-05
                           10        20        30
                   ....*....|....*....|....*....|..
gi 160707911   408 GLTPLHVASFM-GHLPIVKNLLQRGASPNVSN 438
Cdd:pfam00023    2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 721-790 1.87e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.51  E-value: 1.87e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  721 VKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIAKRLGYISVTDVL 790
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 473-502 2.41e-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: 42.57  E-value: 2.41e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 160707911    473 DDQTPLHCAARIGHTGMVKLLLENGASPNL 502
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 585-808 2.41e-05

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 49.53  E-value: 2.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  585 NLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQI--EVARSLLQYGGSANAESVQGVTPL--HLAAQEGHTEMVALLLS 660
Cdd:PHA02716  191 DIDILEWLCNNGVNVNLQNNHLITPLHTYLITGNVcaSVIKKIIELGGDMDMKCVNGMSPImtYIINIDNINPEITNIYI 270

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  661 KQANGNlgnKSGLTP--LHL---VSQEGHVPVADVLIKHGVTVDATTRMGYTPLH--VASHYGNIKLVKFLLQHQADVNA 733
Cdd:PHA02716  271 ESLDGN---KVKNIPmiLHSyitLARNIDISVVYSFLQPGVKLHYKDSAGRTCLHqyILRHNISTDIIKLLHEYGNDLNE 347

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  734 KTKLGYSPLH--------------QAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLA----IAKRLGYISVTDVLkvVTD 795
Cdd:PHA02716  348 PDNIGNTVLHtylsmlsvvnildpETDNDIRLDVIQCLISLGADITAVNCLGYTPLTsyicTAQNYMYYDIIDCL--ISD 425

                         250
                  ....*....|...
gi 160707911  796 EtsvVLVSDKHRM 808
Cdd:PHA02716  426 K---VLNMVKHRI 435
Ank_5 pfam13857
Ankyrin repeats (many copies);
68-122 2.46e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.49  E-value: 2.46e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 160707911    68 LLHKEIILETTTKKGNTALHIAALAGQDEVVRELVNYGANVNAQSQKGFTPLYMA 122
Cdd:pfam13857    2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 705-775 2.63e-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: 2.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  705 GYTPLHVASHYGNIKLVKFLLQHQADVNA--------KTK------LGYSPLHQAAQQGHTDIVTLLLKNGASPNEVS-- 768
Cdd:cd22196    94 GQTALHIAIERRNMHLVELLVQNGADVHArasgeffkKKKggpgfyFGELPLSLAACTNQLDIVKFLLENPHSPADISar 173


                  ....*...
gi 160707911  769 -SNGTTPL 775
Cdd:cd22196   174 dSMGNTVL 181
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 210-237 3.04e-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: 3.04e-05
                            10        20
                    ....*....|....*....|....*...
gi 160707911    210 GFTPLHIAAHYENLNVAQLLLNRGASVN 237
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 573-691 3.09e-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: 3.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  573 GLTPLHVAVHHNNLDIVKLLLPRGGSPHSPA--------------WNGYTPLHIAAKQNQIEVARSLLQYGGSA---NAE 635
Cdd:cd22196    94 GQTALHIAIERRNMHLVELLVQNGADVHARAsgeffkkkkggpgfYFGELPLSLAACTNQLDIVKFLLENPHSPadiSAR 173

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 160707911  636 SVQGVTPLH-LAAQEGHTEMVALLLSKQANG---------------NLGNKSGLTPLHLVSQEGHVPV-ADVL 691
Cdd:cd22196   174 DSMGNTVLHaLVEVADNTPENTKFVTKMYNEililgakirpllkleEITNKKGLTPLKLAAKTGKIGIfAYIL 246
Ank_5 pfam13857
Ankyrin repeats (many copies);
295-349 3.58e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.10  E-value: 3.58e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 160707911   295 LLDHG-APIQAKTKNGLSPIHMAAQGDHLDCVRLLLQYNAEIDDITLDHLTPLHVA 349
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Death_p75NR cd08311
Death domain of p75 Neurotrophin Receptor; Death Domain (DD) found in p75 neurotrophin ...
 1429-1496 3.73e-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: 3.73e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 160707911 1429 SWAELARELQFSVEDINRI-RVENPnslldqSTALLTLWVDREGenAKMENLYTALRNIDRSEIVNMLE 1496
Cdd:cd08311    20 DWRALAGELGYSAEEIDSFaREADP------CRALLTDWSAQDG--ATLGVLLTALRKIGRDDIVEILQ 80
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 242-274 3.75e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 42.28  E-value: 3.75e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 160707911   242 NGITPLHIAS-RRGNVIMVRLLLDRGAQIETRTK 274
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 688-771 3.78e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.74  E-value: 3.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  688 ADVLIKHGVTVDATTRMGYTPLHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNEV 767
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFEL 177


                  ....
gi 160707911  768 SSNG 771
Cdd:PTZ00322  178 GANA 181
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 81-110 3.86e-05

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 42.24  E-value: 3.86e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 160707911    81 KGNTALHIAALAGQDEVVRELVNYGANVNA 110
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
475-514 3.87e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.72  E-value: 3.87e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 160707911   475 QTPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTA 514
Cdd:pfam13857   17 YTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 242-270 4.05e-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: 4.05e-05
                            10        20
                    ....*....|....*....|....*....
gi 160707911    242 NGITPLHIASRRGNVIMVRLLLDRGAQIE 270
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 374-403 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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 41.86  E-value: 4.47e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 160707911   374 NGFTPLHIACKKNHIRVMELLLKTGASIDA 403
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
657-712 4.90e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.72  E-value: 4.90e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 160707911   657 LLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADVLIKHGVTVDATTRMGYTPLHVA 712
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 114-146 5.14e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 41.89  E-value: 5.14e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 160707911   114 KGFTPLYMAA-QENHLEVVKFLLENGANQNVATE 146
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 308-337 5.65e-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: 5.65e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 160707911    308 NGLSPIHMAAQGDHLDCVRLLLQYNAEIDD 337
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 325-461 6.01e-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: 6.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  325 VRLLLQY-----------NAEIDDITLDHLTPLHVAAHCGHHRVAKVLLDKGAKPNSRA----------LNGF----TPL 379
Cdd:cd22194   113 VRILLAFaeengildrfiNAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAkgvffnpkykHEGFyfgeTPL 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  380 HIACKKNHIRVMELLLKTGASIDAVTES-GLTPLH----VA-SFMGHLPIVKNL----LQRGASPN---VSNVKVETPLH 446
Cdd:cd22194   193 ALAACTNQPEIVQLLMEKESTDITSQDSrGNTVLHalvtVAeDSKTQNDFVKRMydmiLLKSENKNletIRNNEGLTPLQ 272

                         170
                  ....*....|....*
gi 160707911  447 MAARAGHTEVAKYLL 461
Cdd:cd22194   273 LAAKMGKAEILKYIL 287
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 189-285 6.19e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 46.90  E-value: 6.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  189 DTRTAAVLLQNDPN-PDVLSKTGFT-PLHIAAHYENLNVAQLLLNRGASVN-FTPQNGITPLHIASRRGNVIMVRLLLDR 265
Cdd:PHA02884   47 DIIDAILKLGADPEaPFPLSENSKTnPLIYAIDCDNDDAAKLLIRYGADVNrYAEEAKITPLYISVLHGCLKCLEILLSY 126

                          90       100
                  ....*....|....*....|
gi 160707911  266 GAQIETRTKDELTPLHCAAR 285
Cdd:PHA02884  127 GADINIQTNDMVTPIELALM 146
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 295-462 6.34e-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: 6.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  295 LLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQY-----------NAEIDDITLDHLTPLHVAAHCGHHRVAKVLLD 363
Cdd:cd22193    18 LTDSEFTESSTGKTCLMKALLNLNPGTNDTIRILLDIaektdnlkrfiNAEYTDEYYEGQTALHIAIERRQGDIVALLVE 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  364 KGAKPNSRALNGF--------------TPLHIACKKNHIRVMELLLK---TGASIDAVTESGLTPLH----VA-SFMGHL 421
Cdd:cd22193    98 NGADVHAHAKGRFfqpkyqgegfyfgeLPLSLAACTNQPDIVQYLLEnehQPADIEAQDSRGNTVLHalvtVAdNTKENT 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 160707911  422 PIVKN----LLQRGAS-------PNVSNVKVETPLHMAARAGHTEVAKYLLQ 462
Cdd:cd22193   178 KFVTRmydmILIRGAKlcptvelEEIRNNDGLTPLQLAAKMGKIEILKYILQ 229
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 473-501 6.68e-05

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 41.47  E-value: 6.68e-05
                           10        20
                   ....*....|....*....|....*....
gi 160707911   473 DDQTPLHCAARIGHTGMVKLLLENGASPN 501
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
Ank_5 pfam13857
Ankyrin repeats (many copies);
327-382 7.33e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 7.33e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 160707911   327 LLLQYNAEIDDITLDHLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIA 382
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Death_PIDD cd08779
Death Domain of p53-induced protein with a death domain; Death domain (DD) found in PIDD ...
 1422-1496 7.59e-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: 7.59e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160707911 1422 IREHLGLSWAELARELQFSVEDINRIRVENPNSLLDQSTALLTLWVDREGENA-KMENLYTALRNIDRSEIVNMLE 1496
Cdd:cd08779     8 LAKELGEDWQKLALHLGVSYSRIQRIKRKNRDDLDEQILDMLFSWAKTLPTSPdKVGLLVTALSKSGRSDLAEELR 83
Death_DRs cd08784
Death Domain of Death Receptors; Death domain (DD) found in death receptor proteins. Death ...
 1428-1487 7.80e-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: 7.80e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911 1428 LSWAELARELQFSVEDINRIRVENPNSLLDQSTALLTLWVDREGENAKMENLYTALRNID 1487
Cdd:cd08784    12 SQWKGFVRKLGLNEAEIDEIKNDNVQDTAEAKYQMLRNWHQLTGRKAAYDTLIKDLKKMN 71
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 341-371 7.84e-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: 7.84e-05
                           10        20        30
                   ....*....|....*....|....*....|..
gi 160707911   341 DHLTPLHVAA-HCGHHRVAKVLLDKGAKPNSR 371
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNAR 32
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 210-237 8.32e-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: 41.12  E-value: 8.32e-05
                           10        20
                   ....*....|....*....|....*....
gi 160707911   210 GFTPLHIAA-HYENLNVAQLLLNRGASVN 237
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVN 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 247-462 8.57e-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: 8.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   247 LHIASRRGNVIMVRLLLDRGAQIETrtkdELTPLHcAARNGHVRISEILLDHGAPIQAKTKNglspihmaaqgdhldcvr 326
Cdd:TIGR00870   57 FVAAIENENLELTELLLNLSCRGAV----GDTLLH-AISLEYVDAVEAILLHLLAAFRKSGP------------------ 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   327 LLLQYNAEIDDITLDHlTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNGF--------------TPLHIACKKNHIRVME 392
Cdd:TIGR00870  114 LELANDQYTSEFTPGI-TALHLAAHRQNYEIVKLLLERGASVPARACGDFfvksqgvdsfyhgeSPLNAAACLGSPSIVA 192

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   393 LLLKTGASIDAVTESGLTPLH----VASF--------MGHLPIVKNLLQRGASPN----VSNVKVETPLHMAARAGHTEV 456
Cdd:TIGR00870  193 LLSEDPADILTADSLGNTLLHllvmENEFkaeyeelsCQMYNFALSLLDKLRDSKelevILNHQGLTPLKLAAKEGRIVL 272


                   ....*.
gi 160707911   457 AKYLLQ 462
Cdd:TIGR00870  273 FRLKLA 278
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 738-765 1.21e-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: 1.21e-04
                           10        20
                   ....*....|....*....|....*....
gi 160707911   738 GYSPLHQAAQQ-GHTDIVTLLLKNGASPN 765
Cdd:pfam00023    2 GNTPLHLAAGRrGNLEIVKLLLSKGADVN 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 341-369 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 160707911    341 DHLTPLHVAAHCGHHRVAKVLLDKGAKPN 369
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 242-271 1.29e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 40.70  E-value: 1.29e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 160707911   242 NGITPLHIASRRGNVIMVRLLLDRGAQIET 271
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 631-777 1.29e-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: 1.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  631 SANAESVQGVTPLHLAA---QEGHTEMVALLLskQANGNLGNksgltPLHLVSQeghvPVADVLIKhgvtvdattrmGYT 707
Cdd:cd21882    18 SAYQRGATGKTCLHKAAlnlNDGVNEAIMLLL--EAAPDSGN-----PKELVNA----PCTDEFYQ-----------GQT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  708 PLHVASHYGNIKLVKFLLQHQADVNAKTK-------------LGYSPLHQAAQQGHTDIVTLLLKNGASPNEVS---SNG 771
Cdd:cd21882    76 ALHIAIENRNLNLVRLLVENGADVSARATgrffrkspgnlfyFGELPLSLAACTNQEEIVRLLLENGAQPAALEaqdSLG 155


                  ....*.
gi 160707911  772 TTPLAI 777
Cdd:cd21882   156 NTVLHA 161
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 408-436 1.35e-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: 1.35e-04
                            10        20
                    ....*....|....*....|....*....
gi 160707911    408 GLTPLHVASFMGHLPIVKNLLQRGASPNV 436
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 605-634 1.71e-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: 1.71e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 160707911    605 NGYTPLHIAAKQNQIEVARSLLQYGGSANA 634
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 424-494 1.73e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.43  E-value: 1.73e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 160707911  424 VKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKAKANAKAKDDQTPLHCAARIGHTGMVKLLL 494
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 567-728 1.74e-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: 1.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  567 NAAGKN----GLTPLHVAVHHNNLDIVKLLLPRGGSPHSPA-------------WNGYTPLHIAAKQNQIEVARSLLQyg 629
Cdd:cd22197    84 NAQCTDeyyrGHSALHIAIEKRSLQCVKLLVENGADVHARAcgrffqkkqgtcfYFGELPLSLAACTKQWDVVNYLLE-- 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  630 gsanaesvQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHlvsqeghvpvaDVLIKHGVTVDATTRM----- 704
Cdd:cd22197   162 --------NPHQPASLQAQDSLGNTVLHALVMIADNSPENSALVIKMY-----------DGLLQAGARLCPTVQLeeisn 222

                         170       180
                  ....*....|....*....|....*.
gi 160707911  705 --GYTPLHVASHYGNIKLVKFLLQHQ 728
Cdd:cd22197   223 heGLTPLKLAAKEGKIEIFRHILQRE 248
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 539-571 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 160707911   539 KGFTPLHVAA-KYGKVRLAELLLEHDAHPNAAGK 571
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 309-430 1.83e-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: 1.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  309 GLSPIHMAAQGDHLDCVRLLLQYNAEIDDITLDHL-------------TPLHVAAHCGHHRVAKVLLDKGAKPNS---RA 372
Cdd:cd22197    94 GHSALHIAIEKRSLQCVKLLVENGADVHARACGRFfqkkqgtcfyfgeLPLSLAACTKQWDVVNYLLENPHQPASlqaQD 173

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 160707911  373 LNGFTPLH----IA--CKKNH---IRVMELLLKTGASIDA-------VTESGLTPLHVASFMGHLPIVKNLLQR 430
Cdd:cd22197   174 SLGNTVLHalvmIAdnSPENSalvIKMYDGLLQAGARLCPtvqleeiSNHEGLTPLKLAAKEGKIEIFRHILQR 247
PHA02795 PHA02795
ankyrin-like protein; Provisional
 96-159 1.84e-04

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 46.14  E-value: 1.84e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 160707911   96 EVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQG 159
Cdd:PHA02795  202 EIYKLCIPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRG 265
PHA02946 PHA02946
ankyin-like protein; Provisional
 350-437 1.95e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 46.20  E-value: 1.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  350 AHCG----HHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPI-- 423
Cdd:PHA02946   43 AYCGikglDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIer 122

                          90
                  ....*....|....
gi 160707911  424 VKNLLQRGASPNVS 437
Cdd:PHA02946  123 INLLVQYGAKINNS 136
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 631-762 1.97e-04

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 43.71  E-value: 1.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  631 SANAESVQGVTPLHLAAQEGhtEMVALLLSKQA----NGNLG---NKSGLTPLHLVSQEGHV-PVADV--LIKHGVTVDA 700
Cdd:PHA02736    9 FASEPDIEGENILHYLCRNG--GVTDLLAFKNAisdeNRYLVleyNRHGKQCVHIVSNPDKAdPQEKLklLMEWGADING 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 160707911  701 TTRM-GYTPLHVASHYGNIKLVKFLL-QHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGA 762
Cdd:PHA02736   87 KERVfGNTPLHIAVYTQNYELATWLCnQPGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGA 150
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 275-307 1.97e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 40.35  E-value: 1.97e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 160707911   275 DELTPLHCAA-RNGHVRISEILLDHGAPIQAKTK 307
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 577-681 2.04e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 45.36  E-value: 2.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  577 LHVAVHHNNLDIVKLLLPRGGSPHSP---AWNGYT-PLHIAAKQNQIEVARSLLQYGGSANAESVQGV-TPLHLAAQEGH 651
Cdd:PHA02884   37 LYSSIKFHYTDIIDAILKLGADPEAPfplSENSKTnPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLHGC 116

                          90       100       110
                  ....*....|....*....|....*....|
gi 160707911  652 TEMVALLLSKQANGNLGNKSGLTPLHLVSQ 681
Cdd:PHA02884  117 LKCLEILLSYGADINIQTNDMVTPIELALM 146
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 82-135 2.16e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.04  E-value: 2.16e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 160707911   82 GNTALHIAALAGQDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLL 135
Cdd:PTZ00322  115 GRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 738-766 2.41e-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: 2.41e-04
                            10        20
                    ....*....|....*....|....*....
gi 160707911    738 GYSPLHQAAQQGHTDIVTLLLKNGASPNE 766
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 572-600 2.52e-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. 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: 2.52e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 160707911   572 NGLTPLHVAV-HHNNLDIVKLLLPRGGSPH 600
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVN 30
PHA03095 PHA03095
ankyrin-like protein; Provisional
 718-775 2.69e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.79  E-value: 2.69e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 160707911  718 IKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGH---TDIVTLLLKNGASPNEVSSNGTTPL 775
Cdd:PHA03095   27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPL 87
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 638-670 2.70e-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: 2.70e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 160707911   638 QGVTPLHLAA-QEGHTEMVALLLSKQANGNLGNK 670
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 539-568 2.72e-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: 2.72e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 160707911   539 KGFTPLHVAAKYGKVRLAELLLEHDAHPNA 568
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 375-583 3.06e-04

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


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 45.62  E-value: 3.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  375 GFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLH--VASFMGHLpivknllqrgaspnvsnvkvetPLHMAARAG 452
Cdd:cd22197    94 GHSALHIAIEKRSLQCVKLLVENGADVHARACGRFFQKKqgTCFYFGEL----------------------PLSLAACTK 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  453 HTEVAKYLLQNKAKANAKAKDD---QTPLHCAARIGH---------TGMVKLLLENGA--SPNL-----ATTAGHTPLHT 513
Cdd:cd22197   152 QWDVVNYLLENPHQPASLQAQDslgNTVLHALVMIADnspensalvIKMYDGLLQAGArlCPTVqleeiSNHEGLTPLKL 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  514 AAREGHVDTALALLEKEASQAC------MTKKGFTPLHVAA-------KYGKVRLAELLLEHDAHPNAAGKNGLTPLHVA 580
Cdd:cd22197   232 AAKEGKIEIFRHILQREFSGPYqhlsrkFTEWCYGPVRVSLydlssvdSWEKNSVLEIIAFHSKSPNRHRMVVLEPLNKL 311


                  ...
gi 160707911  581 VHH 583
Cdd:cd22197   312 LQE 314
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 474-627 3.30e-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: 3.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   474 DQTPLHCAARIGHTGMVKLLLENGASPNLATTAGhtplhtaareghvdtalallekeasqACMTKKGFT-------PLHV 546
Cdd:TIGR00870  128 GITALHLAAHRQNYEIVKLLLERGASVPARACGD--------------------------FFVKSQGVDsfyhgesPLNA 181

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   547 AAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNL------------DIVKLLLPRGGSP----HSPAWNGYTPL 610
Cdd:TIGR00870  182 AACLGSPSIVALLSEDPADILTADSLGNTLLHLLVMENEFkaeyeelscqmyNFALSLLDKLRDSkeleVILNHQGLTPL 261

                          170
                   ....*....|....*..
gi 160707911   611 HIAAKQNQIEVARSLLQ 627
Cdd:TIGR00870  262 KLAAKEGRIVLFRLKLA 278
PHA02946 PHA02946
ankyin-like protein; Provisional
 90-263 3.44e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 45.43  E-value: 3.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   90 ALAGQDE-VVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENV--VAH 166
Cdd:PHA02946   46 GIKGLDErFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIerINL 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  167 LINYGTKgkvrlpalhIAARNDDTRTAAVLLQNDPNPDVLSKT-----------GFTPLHIAAHYENLN----VAQLLLN 231
Cdd:PHA02946  126 LVQYGAK---------INNSVDEEGCGPLLACTDPSERVFKKImsigfearivdKFGKNHIHRHLMSDNpkasTISWMMK 196

                         170       180       190
                  ....*....|....*....|....*....|....
gi 160707911  232 RGASVNFTPQNGITPLHIASRR--GNVIMVRLLL 263
Cdd:PHA02946  197 LGISPSKPDHDGNTPLHIVCSKtvKNVDIINLLL 230
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 539-662 3.48e-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: 3.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  539 KGFTPLHVAAKYGKVRLAELLLEHDAHPNAAGKN--------------GLTPLHVAVHHNNLDIVKLLLPrggSPHSPA- 603
Cdd:cd22193    75 EGQTALHIAIERRQGDIVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLSLAACTNQPDIVQYLLE---NEHQPAd 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  604 -----WNGYTPLH----IA--AKQNQIEVAR---SLLQYGG----SANAESV---QGVTPLHLAAQEGHTEMVALLLSKQ 662
Cdd:cd22193   152 ieaqdSRGNTVLHalvtVAdnTKENTKFVTRmydMILIRGAklcpTVELEEIrnnDGLTPLQLAAKMGKIEILKYILQRE 231
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 572-600 3.91e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.16  E-value: 3.91e-04
                           10        20
                   ....*....|....*....|....*....
gi 160707911   572 NGLTPLHVAVHHNNLDIVKLLLPRGGSPH 600
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 539-568 4.35e-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: 4.35e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 160707911    539 KGFTPLHVAAKYGKVRLAELLLEHDAHPNA 568
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 210-237 4.53e-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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.16  E-value: 4.53e-04
                           10        20
                   ....*....|....*....|....*...
gi 160707911   210 GFTPLHIAAHYENLNVAQLLLNRGASVN 237
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADIN 29
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 114-143 4.53e-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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.16  E-value: 4.53e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 160707911   114 KGFTPLYMAAQENHLEVVKFLLENGANQNV 143
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 95-157 4.81e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 44.20  E-value: 4.81e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 160707911   95 DEVVRELVNYGANVNAQSQKG-FTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQ 157
Cdd:PHA02884   83 DDAAKLLIRYGADVNRYAEEAkITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELALM 146
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 638-664 4.94e-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: 4.94e-04
                            10        20
                    ....*....|....*....|....*..
gi 160707911    638 QGVTPLHLAAQEGHTEMVALLLSKQAN 664
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 738-766 5.15e-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: 5.15e-04
                           10        20
                   ....*....|....*....|....*....
gi 160707911   738 GYSPLHQAAQQGHTDIVTLLLKNGASPNE 766
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 539-665 5.22e-04

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


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 44.85  E-value: 5.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  539 KGFTPLHVAAKYGKVRLAELLLEH--DAHPNAAG----KN-------GLTPLHVAVHHNNLDIVKLLLPRggsPHSPAW- 604
Cdd:cd22197    93 RGHSALHIAIEKRSLQCVKLLVENgaDVHARACGrffqKKqgtcfyfGELPLSLAACTKQWDVVNYLLEN---PHQPASl 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  605 -----NGYTPLH----IA--AKQNQIEVAR---SLLQYGGSANAE-------SVQGVTPLHLAAQEGHTEMVALLLSKQA 663
Cdd:cd22197   170 qaqdsLGNTVLHalvmIAdnSPENSALVIKmydGLLQAGARLCPTvqleeisNHEGLTPLKLAAKEGKIEIFRHILQREF 249


                  ..
gi 160707911  664 NG 665
Cdd:cd22197   250 SG 251
Ank_4 pfam13637
Ankyrin repeats (many copies);
18-69 5.44e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.57  E-value: 5.44e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 160707911    18 TSFLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELL 69
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 573-687 6.11e-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: 6.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  573 GLTPLHVAVHHNNLDIVKLLLPRGGSPHSPA--------------WNGYTPLHIAAKQNQIEVARSLLQYG---GSANAE 635
Cdd:cd22193    76 GQTALHIAIERRQGDIVALLVENGADVHAHAkgrffqpkyqgegfYFGELPLSLAACTNQPDIVQYLLENEhqpADIEAQ 155

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 160707911  636 SVQGVTPLHLAAQEGH---------TEMVALLLSKQAN-------GNLGNKSGLTPLHLVSQEGHVPV 687
Cdd:cd22193   156 DSRGNTVLHALVTVADntkentkfvTRMYDMILIRGAKlcptvelEEIRNNDGLTPLQLAAKMGKIEI 223
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 605-634 6.39e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.78  E-value: 6.39e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 160707911   605 NGYTPLHIAAKQNQIEVARSLLQYGGSANA 634
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 308-339 6.74e-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: 6.74e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 160707911   308 NGLSPIHMAA-QGDHLDCVRLLLQYNAEIDDIT 339
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 167-268 7.17e-04

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 42.17  E-value: 7.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  167 LINYGTKGKvrlPALHIAARND--DTRTAAVLLQN---DPNPDVlSKTGFTPLHIAAHYENLNVAQLLLNRGA----SVN 237
Cdd:PHA02736   48 VLEYNRHGK---QCVHIVSNPDkaDPQEKLKLLMEwgaDINGKE-RVFGNTPLHIAVYTQNYELATWLCNQPGvnmeILN 123

                          90       100       110
                  ....*....|....*....|....*....|.
gi 160707911  238 FTPQngiTPLHIASRRGNVIMVRLLLDRGAQ 268
Cdd:PHA02736  124 YAFK---TPYYVACERHDAKMMNILRAKGAQ 151
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 408-436 7.33e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.39  E-value: 7.33e-04
                           10        20
                   ....*....|....*....|....*....
gi 160707911   408 GLTPLHVASFMGHLPIVKNLLQRGASPNV 436
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 341-369 7.78e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.39  E-value: 7.78e-04
                           10        20
                   ....*....|....*....|....*....
gi 160707911   341 DHLTPLHVAAHCGHHRVAKVLLDKGAKPN 369
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 322-577 9.01e-04

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 44.10  E-value: 9.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  322 LDCVRLLLQYNAEIDDITLDhlTPLHVAA---HCGHHRVAKVLLDKGAKPNSRA-----------LNGFTPLHIACKKNH 387
Cdd:cd21882     8 LECLRWYLTDSAYQRGATGK--TCLHKAAlnlNDGVNEAIMLLLEAAPDSGNPKelvnapctdefYQGQTALHIAIENRN 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  388 IRVMELLLKTGASIDAVTESgltplhvASFMGHlpiVKNLLQRGaspnvsnvkvETPLHMAARAGHTEVAKYLLQNKAKA 467
Cdd:cd21882    86 LNLVRLLVENGADVSARATG-------RFFRKS---PGNLFYFG----------ELPLSLAACTNQEEIVRLLLENGAQP 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  468 NAKAKDD---QTPLHCAARIGH---------TGMVKLLLENGASPN-------LATTAGHTPLHTAAREGHVDTALALLE 528
Cdd:cd21882   146 AALEAQDslgNTVLHALVLQADntpensafvCQMYNLLLSYGAHLDptqqleeIPNHQGLTPLKLAAVEGKIVMFQHILQ 225

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 160707911  529 KEASQACM------TKKGFTPLHVAA-------KYGKVRLAELLLEHDAHPNAAGKNGLTPL 577
Cdd:cd21882   226 REFSGPYQplsrkfTEWTYGPVTSSLydlseidSWEKNSVLELIAFSKKREARHQMLVQEPL 287
PHA02798 PHA02798
ankyrin-like protein; Provisional
 29-271 1.01e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 43.67  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   29 LDKALDHLRNGVDINTCNQNGLNGLHLaskeghvkmvveLLHKEIIletttkkgntalhiaalaGQDEVVRELVNYGANV 108
Cdd:PHA02798   89 LDIVKILIENGADINKKNSDGETPLYC------------LLSNGYI------------------NNLEILLFMIENGADT 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  109 NAQSQKGFTPLYMAAQENH---LEVVKFLLENGANQNV-ATEDGFTPLAVALQQGHE----NVVAHLINYG--------- 171
Cdd:PHA02798  139 TLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINThNNKEKYDTLHCYFKYNIDridaDILKLFVDNGfiinkenks 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  172 TKGKVR--LPALHIAARNDDTRTAAVLLQ--NDPNPDVLsktGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPL 247
Cdd:PHA02798  219 HKKKFMeyLNSLLYDNKRFKKNILDFIFSyiDINQVDEL---GFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCL 295

                         250       260
                  ....*....|....*....|....
gi 160707911  248 HIASRRGNVIMVRLLLDRGAQIET 271
Cdd:PHA02798  296 FTAFENESKFIFNSILNKKPNKNT 319
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 278-302 1.05e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.95  E-value: 1.05e-03
                            10        20
                    ....*....|....*....|....*
gi 160707911    278 TPLHCAARNGHVRISEILLDHGAPI 302
Cdd:smart00248    4 TPLHLAAENGNLEVVKLLLDKGADI 28
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 438-561 1.06e-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: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  438 NVKVETPLHMAARAGHTEVAKYLLQNKAKANAKAKDD--------------QTPLHCAARIGHTGMVKLLLENGASP-NL 502
Cdd:cd22194   138 AYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVffnpkykhegfyfgETPLALAACTNQPEIVQLLMEKESTDiTS 217

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 160707911  503 ATTAGHTPLH---TAAR--EGHV-------DTALALLEKEASQACMTKKGFTPLHVAAKYGKVRLAELLLE 561
Cdd:cd22194   218 QDSRGNTVLHalvTVAEdsKTQNdfvkrmyDMILLKSENKNLETIRNNEGLTPLQLAAKMGKAEILKYILS 288
Ank_5 pfam13857
Ankyrin repeats (many copies);
36-89 1.49e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.48  E-value: 1.49e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 160707911    36 LRNG-VDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIA 89
Cdd:pfam13857    2 LEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 605-634 1.68e-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: 1.68e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 160707911   605 NGYTPLHIAAKQ-NQIEVARSLLQYGGSANA 634
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNA 31
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 475-627 2.11e-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: 2.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  475 QTPLHCAARIGHTGMVKLLLENGASPNLATTA-------------GHTPLHTAAREGHVDTALALLEKEASQACMTKK-- 539
Cdd:cd22197    95 HSALHIAIEKRSLQCVKLLVENGADVHARACGrffqkkqgtcfyfGELPLSLAACTKQWDVVNYLLENPHQPASLQAQds 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  540 -GFTPLHvaakygkvrlAELLLEHDAHPNAAgkngltpLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQ 618
Cdd:cd22197   175 lGNTVLH----------ALVMIADNSPENSA-------LVIKMYDGLLQAGARLCPTVQLEEISNHEGLTPLKLAAKEGK 237


                  ....*....
gi 160707911  619 IEVARSLLQ 627
Cdd:cd22197   238 IEIFRHILQ 246
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 210-348 2.34e-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: 2.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  210 GFTPLHIAAHYENLNVAQLLLNRGASVN-------FTPQN-------GITPLHIASRRGNVIMVRLLLDRGAQIETrTKD 275
Cdd:cd22194   141 GQTALNIAIERRQGDIVKLLIAKGADVNahakgvfFNPKYkhegfyfGETPLALAACTNQPEIVQLLMEKESTDIT-SQD 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  276 EL--TPLHC---AARNGHVRIS-------EILLDHGAPIQAKTKN--GLSPIHMAAQGDHLDCVRLLLqyNAEIDDITLD 341
Cdd:cd22194   220 SRgnTVLHAlvtVAEDSKTQNDfvkrmydMILLKSENKNLETIRNneGLTPLQLAAKMGKAEILKYIL--SREIKEKPNR 297


                  ....*..
gi 160707911  342 HLTPLHV 348
Cdd:cd22194   298 SLSRKFT 304
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 716-819 2.39e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 42.64  E-value: 2.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  716 GNIKLVKFLLQHQAD-VNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIAKRLGyisVTDVLKVVT 794
Cdd:PHA02874   12 GDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIG---AHDIIKLLI 88

                          90       100
                  ....*....|....*....|....*...
gi 160707911  795 D---ETSVVLVSDKHRmsypETVDEILD 819
Cdd:PHA02874   89 DngvDTSILPIPCIEK----DMIKTILD 112
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 672-703 2.47e-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: 2.47e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 160707911   672 GLTPLHL-VSQEGHVPVADVLIKHGVTVDATTR 703
Cdd:pfam00023    2 GNTPLHLaAGRRGNLEIVKLLLSKGADVNARDK 34
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 42-176 2.60e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 40.24  E-value: 2.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   42 INTCNQN--GLNGLHLASKEGHVkmvVELL-HKEIILETT-------TKKGNTALHIAALAGQ---DEVVRELVNYGANV 108
Cdd:PHA02736    8 IFASEPDieGENILHYLCRNGGV---TDLLaFKNAISDENrylvleyNRHGKQCVHIVSNPDKadpQEKLKLLMEWGADI 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  109 NAQSQK-GFTPLYMAAQENHLEVVKFLLEN-GANQNVATEDGFTPLAVALQQGHENVVAHLINYGTKGKV 176
Cdd:PHA02736   85 NGKERVfGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGAQCKV 154
PHA02791 PHA02791
ankyrin-like protein; Provisional
 503-698 3.55e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 41.57  E-value: 3.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  503 ATTAGHTPLHTAAREGHVDTALALLEKEASQACMTKKgfTPLHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVH 582
Cdd:PHA02791   26 ADVHGHSALYYAIADNNVRLVCTLLNAGALKNLLENE--FPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVD 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  583 HNNLDIVKLLLPRGGSPHSPAWNGY-TPLHIAAKQNQIEVARSLLQYGGSANAESVQgVTPLHLAAQEGHTEMVALLLSK 661
Cdd:PHA02791  104 SGNMQTVKLFVKKNWRLMFYGKTGWkTSFYHAVMLNDVSIVSYFLSEIPSTFDLAIL-LSCIHITIKNGHVDMMILLLDY 182

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 160707911  662 QANGNLGNKSGLTP-LHLVSQEGHVPVADVLIKHGVTV 698
Cdd:PHA02791  183 MTSTNTNNSLLFIPdIKLAIDNKDLEMLQALFKYDINI 220
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 96-171 4.15e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 40.57  E-value: 4.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   96 EVVRELVNYGANVNAQSQ-KGFTPL--YMAAQEN-HLEVVKFLLENGANQNVATEDGFTPLAVALQQGHEN--VVAHLIN 169
Cdd:PHA02859   67 EILKFLIENGADVNFKTRdNNLSALhhYLSFNKNvEPEILKILIDSGSSITEEDEDGKNLLHMYMCNFNVRinVIKLLID 146


                  ..
gi 160707911  170 YG 171
Cdd:PHA02859  147 SG 148
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 443-462 4.21e-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: 4.21e-03
                            10        20
                    ....*....|....*....|
gi 160707911    443 TPLHMAARAGHTEVAKYLLQ 462
Cdd:smart00248    4 TPLHLAAENGNLEVVKLLLD 23
PHA02795 PHA02795
ankyrin-like protein; Provisional
 690-784 4.74e-03

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 41.52  E-value: 4.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  690 VLIKHGVTVDATTRMGYTPLHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNEVSS 769
Cdd:PHA02795  173 IPDENDVKLDLYKIIQYTRGFLVDEPTVLEIYKLCIPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMS 252

                          90
                  ....*....|....*
gi 160707911  770 NGTTPLAIAKRLGYI 784
Cdd:PHA02795  253 NGYTCLDVAVDRGSV 267
PHA02791 PHA02791
ankyrin-like protein; Provisional
 605-769 4.97e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 41.18  E-value: 4.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  605 NGYTPLHIAAKQNQIEVARSLLQYGGSANAesVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGH 684
Cdd:PHA02791   29 HGHSALYYAIADNNVRLVCTLLNAGALKNL--LENEFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGN 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  685 VPVADVLIKHGVTVDATTRMGY-TPLHVASHYGNIKLVKFLLqhqADVNAKTKLG--YSPLHQAAQQGHTDIVTLLLKNG 761
Cdd:PHA02791  107 MQTVKLFVKKNWRLMFYGKTGWkTSFYHAVMLNDVSIVSYFL---SEIPSTFDLAilLSCIHITIKNGHVDMMILLLDYM 183


                  ....*...
gi 160707911  762 ASPNEVSS 769
Cdd:PHA02791  184 TSTNTNNS 191
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 687-778 5.42e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.78  E-value: 5.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  687 VADVLIKHGVTvDATTRMGYTPLHVAShYGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNE 766
Cdd:PLN03192  509 VGDLLGDNGGE-HDDPNMASNLLTVAS-TGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHI 586

                          90
                  ....*....|....
gi 160707911  767 VSSNGTTPL--AIA 778
Cdd:PLN03192  587 RDANGNTALwnAIS 600
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 342-416 6.55e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 40.74  E-value: 6.55e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160707911  342 HLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNG-FTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVAS 416
Cdd:PHA02884   70 KTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAkITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELAL 145
PHA02741 PHA02741
hypothetical protein; Provisional
 46-163 6.67e-03

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 39.64  E-value: 6.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   46 NQNGLNGLHLASKEGHVKMVVELL------HKEIILETTTKKGNTALHIAALAGQD----EVVRELVNYGANVNAQ-SQK 114
Cdd:PHA02741   18 NSEGENFFHEAARCGCFDIIARFTpfirgdCHAAALNATDDAGQMCIHIAAEKHEAqlaaEIIDHLIELGADINAQeMLE 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 160707911  115 GFTPLYMAAQENHLEVVKFLL-ENGANQNVATEDGFTPLAVAlqQGHENV 163
Cdd:PHA02741   98 GDTALHLAAHRRDHDLAEWLCcQPGIDLHFCNADNKSPFELA--IDNEDV 145
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 77-265 8.28e-03

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


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 40.99  E-value: 8.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911   77 TTTKKGNTALHIAALAGQD----------EVVRELVNYGANVNAQSQ----KGFTPLYMAAQENHLEVVKFLLENGANQN 142
Cdd:cd22197    42 TEGSTGKTCLMKAVLNLQDgvnacimpllEIDKDSGNPKPLVNAQCTdeyyRGHSALHIAIEKRSLQCVKLLVENGADVH 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  143 VATEDGFTplavalqQGHENVVAHlinYGtkgkvRLPaLHIAARNDDTRTAAVLLQNDPNPDVLSKT---GFTPLH---- 215
Cdd:cd22197   122 ARACGRFF-------QKKQGTCFY---FG-----ELP-LSLAACTKQWDVVNYLLENPHQPASLQAQdslGNTVLHalvm 185

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 160707911  216 IAAHYENlNVAQL------LLNRGASVNFTPQ-------NGITPLHIASRRGNVIMVRLLLDR 265
Cdd:cd22197   186 IADNSPE-NSALVikmydgLLQAGARLCPTVQleeisnhEGLTPLKLAAKEGKIEIFRHILQR 247
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 357-434 8.60e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 39.80  E-value: 8.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  357 VAKVLLDKGAKPNSRAL-NGFTPLH--IACKKN-HIRVMELLLKTGASIDAVTESGLTPLHV--ASFMGHLPIVKNLLQR 430
Cdd:PHA02859   68 ILKFLIENGADVNFKTRdNNLSALHhyLSFNKNvEPEILKILIDSGSSITEEDEDGKNLLHMymCNFNVRINVIKLLIDS 147


                  ....
gi 160707911  431 GASP 434
Cdd:PHA02859  148 GVSF 151
PHA02946 PHA02946
ankyin-like protein; Provisional
 281-447 8.99e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 40.81  E-value: 8.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  281 HCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQYNAEIDDITLDHLTPLHVAAHCGHHRVAKV 360
Cdd:PHA02946   44 YCGIKGLDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIERI 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707911  361 --LLDKGAK-PNSRALNGFTPLhIACKKNHIRVMELLLKTGASIDAVTESGLTPLHvASFMGHLP---IVKNLLQRGASP 434
Cdd:PHA02946  124 nlLVQYGAKiNNSVDEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFGKNHIH-RHLMSDNPkasTISWMMKLGISP 201

                         170
                  ....*....|...
gi 160707911  435 NVSNVKVETPLHM 447
Cdd:PHA02946  202 SKPDHDGNTPLHI 214
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 308-336 9.36e-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: 35.31  E-value: 9.36e-03
                           10        20
                   ....*....|....*....|....*....
gi 160707911   308 NGLSPIHMAAQGDHLDCVRLLLQYNAEID 336
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
 
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