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Conserved domains on  [gi|1229385645|ref|NP_001341184|]
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ankyrin-2 isoform 24 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
UPA_2 super family cl39303
UPA domain; The UPA domain is conserved in UNC5, PIDD, and Ankyrins. It has a beta sandwich ...
1303-1432 4.12e-60

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


The actual alignment was detected with superfamily member pfam17809:

Pssm-ID: 375346  Cd Length: 131  Bit Score: 202.32  E-value: 4.12e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645 1303 VPYMAKFVVFAKSHDPIEARLRCFCMTDDKVDKTLEQQENFAEVARSRDVEVLEGKPIYVDCFGNLVPLTKSGQHHIFSF 1382
Cdd:pfam17809    1 VPYLAKFVVFAKRYDPGEARLRCACMTDDGEDKTLEFHEGFTEVARSRDVEVLEGSPVSIELSGNLVPIKKKSQSRQMDF 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1229385645 1383 FAFKENRLPLFVKVRDTTQEPCGRLSFMKEPKSTRGLVHQAICNLNITLP 1432
Cdd:pfam17809   81 KAFRENRLDGSVRVKDPSDPPKGLLSFMRDAKVDGGTVSQPLCTLNIVLP 130
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
528-793 1.43e-59

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 207.11  E-value: 1.43e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  528 LLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHATAKN 607
Cdd:COG0666      7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  608 GYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKV 687
Cdd:COG0666     87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  688 NVADILTKHGADQDAHTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPN 767
Cdd:COG0666    167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246
                          250       260
                   ....*....|....*....|....*.
gi 1229385645  768 ATTANGNTALAIAKRLGYISVVDTLK 793
Cdd:COG0666    247 AKDKDGLTALLLAAAAGAALIVKLLL 272
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
291-579 4.92e-59

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 205.57  E-value: 4.92e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  291 DQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANP 370
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  371 NARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMA 450
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  451 ARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLE 530
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1229385645  531 AGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPL 579
Cdd:COG0666    241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
23-381 2.22e-54

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 192.48  E-value: 2.22e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645   23 LDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGANI 102
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  103 NAQSQNGFTPLYMAAQENHIDVVKYLLENGANqstatedgftplavalqqghnqavaillendtkgkvrlpalhiaarkd 182
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGAD------------------------------------------------ 112
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  183 dtksaalllqndhnadvqskmmVNRTTESGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVK 262
Cdd:COG0666    113 ----------------------VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  263 LLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLLQHKAPVDDVTL 342
Cdd:COG0666    171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250
                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 1229385645  343 DYLTALHVAAHCGHYRVTKLLLDKRANPNARALNGFTPL 381
Cdd:COG0666    251 DGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Death_ank2 cd08804
Death domain of Ankyrin-2; Death Domain (DD) of Ankyrin-2 (ANK-2) and related proteins. ...
1461-1544 1.24e-51

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: 176.43  E-value: 1.24e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645 1461 ERIEERLAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIV 1540
Cdd:cd08804      1 ERTEERLAHIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLTQCLTKINRMDIV 80

                   ....
gi 1229385645 1541 HLME 1544
Cdd:cd08804     81 HLME 84
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
945-1082 2.62e-44

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


:

Pssm-ID: 128514  Cd Length: 104  Bit Score: 155.97  E-value: 2.62e-44
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645   945 SGFLVSFMVDARGGAMRGCRhNGLRIIIPPRKCTAPTRVTCRLVKRHRLATMPPMVEGEGLASRLIEVGPSGAQflgklh 1024
Cdd:smart00218    1 PSFLVSGTFDARGGRLRGPR-TGVRLIIPPGAIPQGTRYTCYLVVHKTLSTPPPLEEGETLLSPVVECGPHGAL------ 73
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1229385645  1025 lptappplnegeslvsrilqlgppgtkFLGPVIVEIPHFAALRGKERELVVLRSENGD 1082
Cdd:smart00218   74 ---------------------------FLRPVILEVPHCASLRPRDWEIVLLRSENGG 104
NESP55 super family cl25759
Neuroendocrine-specific golgi protein P55 (NESP55); This family consists of several mammalian ...
1617-1774 1.70e-08

Neuroendocrine-specific golgi protein P55 (NESP55); This family consists of several mammalian neuroendocrine-specific golgi protein P55 (NESP55) sequences. NESP55 is a novel member of the chromogranin family and is a soluble, acidic, heat-stable secretory protein that is expressed exclusively in endocrine and nervous tissues, although less widely than chromogranins.


The actual alignment was detected with superfamily member pfam06390:

Pssm-ID: 115071 [Multi-domain]  Cd Length: 261  Bit Score: 57.57  E-value: 1.70e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645 1617 TFQDGVPKTEGDSSATALFPQTHKEQVQQDFSGKMQDLPEESSLEYQQEYFVTTPGTET-------SETQKAMIVPSSPS 1689
Cdd:pfam06390   62 SFLNAHHRSAAAAAAAQVFPEPSEPESDHEDEDFEPELARPECLEYDEDDFDTETDSETepesdieSETEFETEPETEPD 141
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645 1690 KTPE-EVSTPAEEEK--------------------LYLQTPTSSERGGSPIIQEPEEPSEHRE------ESSPR--KTSL 1740
Cdd:pfam06390  142 TAPTtEPETEPEDEPgpvvpkgatfhqslterlhaLKLQSADASPRRAPPSTQEPESAREGEEpergplDKDPRdpEEEE 221
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1229385645 1741 VIVESADNQPETCErldEDAAFEKGDDMPEIPPE 1774
Cdd:pfam06390  222 EEKEEEKQQPHRCK---PKKPARRRDPSPESPPK 252
Ank_4 pfam13637
Ankyrin repeats (many copies);
171-232 1.67e-07

Ankyrin repeats (many copies);


:

Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.58  E-value: 1.67e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1229385645  171 RLPALHIAARKDDTKSAALLLQNDHNadvqskmmVNRTTESGFTPLHIAAHYGNVNVATLLL 232
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGAD--------INAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
111-162 2.67e-07

Ankyrin repeats (many copies);


:

Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.81  E-value: 2.67e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1229385645  111 TPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHNQAVAILL 162
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
 
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 ...
1303-1432 4.12e-60

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: 202.32  E-value: 4.12e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645 1303 VPYMAKFVVFAKSHDPIEARLRCFCMTDDKVDKTLEQQENFAEVARSRDVEVLEGKPIYVDCFGNLVPLTKSGQHHIFSF 1382
Cdd:pfam17809    1 VPYLAKFVVFAKRYDPGEARLRCACMTDDGEDKTLEFHEGFTEVARSRDVEVLEGSPVSIELSGNLVPIKKKSQSRQMDF 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1229385645 1383 FAFKENRLPLFVKVRDTTQEPCGRLSFMKEPKSTRGLVHQAICNLNITLP 1432
Cdd:pfam17809   81 KAFRENRLDGSVRVKDPSDPPKGLLSFMRDAKVDGGTVSQPLCTLNIVLP 130
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
528-793 1.43e-59

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 207.11  E-value: 1.43e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  528 LLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHATAKN 607
Cdd:COG0666      7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  608 GYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKV 687
Cdd:COG0666     87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  688 NVADILTKHGADQDAHTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPN 767
Cdd:COG0666    167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246
                          250       260
                   ....*....|....*....|....*.
gi 1229385645  768 ATTANGNTALAIAKRLGYISVVDTLK 793
Cdd:COG0666    247 AKDKDGLTALLLAAAAGAALIVKLLL 272
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
291-579 4.92e-59

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 205.57  E-value: 4.92e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  291 DQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANP 370
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  371 NARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMA 450
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  451 ARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLE 530
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1229385645  531 AGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPL 579
Cdd:COG0666    241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
23-381 2.22e-54

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 192.48  E-value: 2.22e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645   23 LDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGANI 102
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  103 NAQSQNGFTPLYMAAQENHIDVVKYLLENGANqstatedgftplavalqqghnqavaillendtkgkvrlpalhiaarkd 182
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGAD------------------------------------------------ 112
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  183 dtksaalllqndhnadvqskmmVNRTTESGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVK 262
Cdd:COG0666    113 ----------------------VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  263 LLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLLQHKAPVDDVTL 342
Cdd:COG0666    171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250
                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 1229385645  343 DYLTALHVAAHCGHYRVTKLLLDKRANPNARALNGFTPL 381
Cdd:COG0666    251 DGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Death_ank2 cd08804
Death domain of Ankyrin-2; Death Domain (DD) of Ankyrin-2 (ANK-2) and related proteins. ...
1461-1544 1.24e-51

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: 176.43  E-value: 1.24e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645 1461 ERIEERLAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIV 1540
Cdd:cd08804      1 ERTEERLAHIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLTQCLTKINRMDIV 80

                   ....
gi 1229385645 1541 HLME 1544
Cdd:cd08804     81 HLME 84
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
945-1082 2.62e-44

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


Pssm-ID: 128514  Cd Length: 104  Bit Score: 155.97  E-value: 2.62e-44
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645   945 SGFLVSFMVDARGGAMRGCRhNGLRIIIPPRKCTAPTRVTCRLVKRHRLATMPPMVEGEGLASRLIEVGPSGAQflgklh 1024
Cdd:smart00218    1 PSFLVSGTFDARGGRLRGPR-TGVRLIIPPGAIPQGTRYTCYLVVHKTLSTPPPLEEGETLLSPVVECGPHGAL------ 73
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1229385645  1025 lptappplnegeslvsrilqlgppgtkFLGPVIVEIPHFAALRGKERELVVLRSENGD 1082
Cdd:smart00218   74 ---------------------------FLRPVILEVPHCASLRPRDWEIVLLRSENGG 104
PHA03100 PHA03100
ankyrin repeat protein; Provisional
540-764 3.35e-40

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 155.21  E-value: 3.35e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  540 KKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHY-----DNQKVALLLLEKGASPHATAKNGYTPLHI 614
Cdd:PHA03100    33 KKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIkynltDVKEIVKLLLEYGANVNAPDNNGITPLLY 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  615 AA--KKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTD--MVTLLLDKGANIhmstksgltslhlaaqeDKVNVA 690
Cdd:PHA03100   113 AIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDI-----------------NAKNRV 175
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1229385645  691 DILTKHGADQDAHTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGA 764
Cdd:PHA03100   176 NYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
ZU5 pfam00791
ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.
949-1079 1.37e-35

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


Pssm-ID: 459941  Cd Length: 97  Bit Score: 131.11  E-value: 1.37e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  949 VSFMVDARGGAMRGCrHNGLRIIIPPRKCTAPTRVTCRLVKRHRLATMPPMVEGEGLASRLIEvgpsgaqflgklhlpta 1028
Cdd:pfam00791    1 VSGLVDSRGGRLVLP-NSGVSLLIPPGAIPEGTRIECYLAVNRDESSRPPLEEGETLLSPVVE----------------- 62
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1229385645 1029 ppplnegeslvsrilqLGPPGTKFLGPVIVEIPHFAALRGKERELVVLRSE 1079
Cdd:pfam00791   63 ----------------CGPPGLKFLKPVILEVPHCASLRPEEWEIVLKRSD 97
PHA03095 PHA03095
ankyrin-like protein; Provisional
383-668 7.34e-35

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 140.55  E-value: 7.34e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  383 IACKKNRIKVMELLVKYGASIQAITESGLTPIHVaaFMGH-----LNIVLLLLQNGASPDVTNIRGETALHMAARAGQVE 457
Cdd:PHA03095    20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHL--YLHYssekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTL 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  458 -VVRCLLRNGALVDARAREEQTPLHI--ASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASV--LLEAG 532
Cdd:PHA03095    98 dVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVELLrlLIDAG 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  533 AahSLATKK--GFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKN--GLTPLHVAAHYDNQKVALL--LLEKGASPHATAK 606
Cdd:PHA03095   178 A--DVYAVDdrFRSLLHHHLQSFKPRARIVRELIRAGCDPAATDmlGNTPLHSMATGSSCKRSLVlpLLIAGISINARNR 255
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1229385645  607 NGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLDKGANIH 668
Cdd:PHA03095   256 YGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAE 317
PHA03100 PHA03100
ankyrin repeat protein; Provisional
164-406 9.78e-34

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 136.33  E-value: 9.78e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  164 NDTKGKVRLPALHIAARKDDTKSAALLLqnDHNADVQSKMMVNrttesgFTPLHIAAHYG-----NVNVATLLLNRGAAV 238
Cdd:PHA03100    28 NDYSYKKPVLPLYLAKEARNIDVVKILL--DNGADINSSTKNN------STPLHYLSNIKynltdVKEIVKLLLEYGANV 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  239 DFTARNGITPLHVAS--KRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHD--QVVELLLERGAPLLARTKnglsp 314
Cdd:PHA03100   100 NAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKNR----- 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  315 lhmaaqgdhvecVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVME 394
Cdd:PHA03100   175 ------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFK 242
                          250
                   ....*....|..
gi 1229385645  395 LLVKYGASIQAI 406
Cdd:PHA03100   243 LLLNNGPSIKTI 254
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
1460-1545 7.05e-24

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: 97.10  E-value: 7.05e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  1460 QERIEERLAYIADH-LGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMD 1538
Cdd:smart00005    1 PELTRQKLAKLLDHpLGLDWRELARKLGLSEADIDQIRTEAPRDLAEQSVQLLRLWEQREGKNATLGTLLEALRKMGRDD 80

                    ....*..
gi 1229385645  1539 IVHLMET 1545
Cdd:smart00005   81 AVELLRS 87
Ank_2 pfam12796
Ankyrin repeats (3 copies);
47-134 1.52e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 96.34  E-value: 1.52e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645   47 LHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEgANINAQSqNGFTPLYMAAQENHIDVVK 126
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                   ....*...
gi 1229385645  127 YLLENGAN 134
Cdd:pfam12796   79 LLLEKGAD 86
Ank_2 pfam12796
Ankyrin repeats (3 copies);
348-440 2.56e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.87  E-value: 2.56e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  348 LHVAAHCGHYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGAsiQAITESGLTPIHVAAFMGHLNIVL 427
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 1229385645  428 LLLQNGASPDVTN 440
Cdd:pfam12796   79 LLLEKGADINVKD 91
Death pfam00531
Death domain;
1464-1544 2.54e-21

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 89.73  E-value: 2.54e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645 1464 EERLAYIADH---LGFSWTELARELDFTEEQIHQIRIENPNsLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIV 1540
Cdd:pfam00531    1 RKQLDRLLDPpppLGKDWRELARKLGLSENEIDEIESENPR-LRSQTYELLRLWEQREGKNATVGTLLEALRKLGRRDAA 79

                   ....
gi 1229385645 1541 HLME 1544
Cdd:pfam00531   80 EKIQ 83
Ank_2 pfam12796
Ankyrin repeats (3 copies);
678-769 3.57e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.79  E-value: 3.57e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  678 LHLAAQEDKVNVADILTKHGADQDAHTKLGYTPLIVACHYGNVKMVNFLLKQgANVNAKTkNGYTPLHQAAQQGHTHIIN 757
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|..
gi 1229385645  758 VLLQHGAKPNAT 769
Cdd:pfam12796   79 LLLEKGADINVK 90
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
534-728 3.81e-16

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 84.29  E-value: 3.81e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  534 AHSLATKKGF-TPLHVAAKYGSLD-VAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEkgASPH-----ATAK 606
Cdd:cd22192      8 LHLLQQKRISeSPLLLAAKENDVQaIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPElvnepMTSD 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  607 --NGYTPLHIAAKKNQMQIASTLLNYGAEtniVTKQGVT-----------------PLHLASQEGHTDMVTLLLDKGANI 667
Cdd:cd22192     86 lyQGETALHIAVVNQNLNLVRELIARGAD---VVSPRATgtffrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADI 162
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1229385645  668 HMSTKSGLTSLH-LAAQEDKV---NVADILTKHGADQDAHT------KLGYTPLIVACHYGNVKMVNFLLK 728
Cdd:cd22192    163 RAQDSLGNTVLHiLVLQPNKTfacQMYDLILSYDKEDDLQPldlvpnNQGLTPFKLAAKEGNIVMFQHLVQ 233
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
379-565 3.67e-15

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: 81.21  E-value: 3.67e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  379 TPLHIACKKNRIKVMELLVKY-GASIQAITESGLTPIHVAAFMGHLNIVLLLLQngASPDVTNI-------RGETALHMA 450
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNEpmtsdlyQGETALHIA 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  451 ARAGQVEVVRCLLRNGA-LVDARA-----REEQT--------PLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHIS 516
Cdd:cd22192     97 VVNQNLNLVRELIARGAdVVSPRAtgtffRPGPKnliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHIL 176
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1229385645  517 AREGQVDVA----SVLLEA---GAAHSLAT---KKGFTPLHVAAKYGSLDVAKLLLQRR 565
Cdd:cd22192    177 VLQPNKTFAcqmyDLILSYdkeDDLQPLDLvpnNQGLTPFKLAAKEGNIVMFQHLVQKR 235
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
144-334 1.03e-14

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 79.67  E-value: 1.03e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  144 TPLAVALQQGHNQAVAILLENDT-----KGKVRLPALHIAARKDDTKSAALLLQNDH---NADVQSKMMVnrttesGFTP 215
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLLKCPScdlfqRGALGETALHVAALYDNLEAAVVLMEAAPelvNEPMTSDLYQ------GETA 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  216 LHIAAHYGNVNVATLLLNRGAAVdFTARN---------------GITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLT 280
Cdd:cd22192     93 LHIAVVNQNLNLVRELIARGADV-VSPRAtgtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNT 171
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1229385645  281 PLHC----AARSGHDQVVELLL-----ERGAPL-LARTKNGLSPLHMAAQGDHVECVKHLLQHK 334
Cdd:cd22192    172 VLHIlvlqPNKTFACQMYDLILsydkeDDLQPLdLVPNNQGLTPFKLAAKEGNIVMFQHLVQKR 235
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
270-518 1.21e-12

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: 73.19  E-value: 1.21e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  270 QIDAKTRDGLTPLHCAA-RSGHDQVVELLLERGAplLARTknGLSPLHMAAQGdHVECVKHLLQH--KAPVDDVTLDYL- 345
Cdd:TIGR00870   44 NINCPDRLGRSALFVAAiENENLELTELLLNLSC--RGAV--GDTLLHAISLE-YVDAVEAILLHllAAFRKSGPLELAn 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  346 -----------TALHVAAHCGHYRVTKLLLDKRANPNARALNGFtplhiaCKKnriKVMELLVKYGASiqaitesgltPI 414
Cdd:TIGR00870  119 dqytseftpgiTALHLAAHRQNYEIVKLLLERGASVPARACGDF------FVK---SQGVDSFYHGES----------PL 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  415 HVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAA----RAGQVEVVRCLLRNGAL-VDARAREEQ-----------T 478
Cdd:TIGR00870  180 NAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVmeneFKAEYEELSCQMYNFALsLLDKLRDSKelevilnhqglT 259
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1229385645  479 PLHIASRLGKTEIVQLLLQ-------HMAHPdaattngYTPLHISAR 518
Cdd:TIGR00870  260 PLKLAAKEGRIVLFRLKLAikykqkkFVAWP-------NGQQLLSLY 299
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
104-397 4.32e-11

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: 68.18  E-value: 4.32e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  104 AQSQNGFTPlymAAQENHIDVVKYLLENGA--NQSTATEDGFTPLAVALQQGHNQAVAILLEN-DTKGKVRLPALHIAA- 179
Cdd:TIGR00870   15 SDEEKAFLP---AAERGDLASVYRDLEEPKklNINCPDRLGRSALFVAAIENENLELTELLLNlSCRGAVGDTLLHAISl 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  180 RKDDTKSAALLLQNDHNADVQSKMMVNRTTESGF----TPLHIAAHYGNVNVATLLLNRGAAVDFTArNGitplhVASKR 255
Cdd:TIGR00870   92 EYVDAVEAILLHLLAAFRKSGPLELANDQYTSEFtpgiTALHLAAHRQNYEIVKLLLERGASVPARA-CG-----DFFVK 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  256 gnTNMVKLLldrggqidaktRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMAAqgdhvecvkhlLQHKA 335
Cdd:TIGR00870  166 --SQGVDSF-----------YHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLV-----------MENEF 221
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1229385645  336 PVDDVTLD---YLTALHVAAHCGHYRVTKLLLDkranpnaraLNGFTPLHIACKKNRIKVMELLV 397
Cdd:TIGR00870  222 KAEYEELScqmYNFALSLLDKLRDSKELEVILN---------HQGLTPLKLAAKEGRIVLFRLKL 277
NESP55 pfam06390
Neuroendocrine-specific golgi protein P55 (NESP55); This family consists of several mammalian ...
1617-1774 1.70e-08

Neuroendocrine-specific golgi protein P55 (NESP55); This family consists of several mammalian neuroendocrine-specific golgi protein P55 (NESP55) sequences. NESP55 is a novel member of the chromogranin family and is a soluble, acidic, heat-stable secretory protein that is expressed exclusively in endocrine and nervous tissues, although less widely than chromogranins.


Pssm-ID: 115071 [Multi-domain]  Cd Length: 261  Bit Score: 57.57  E-value: 1.70e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645 1617 TFQDGVPKTEGDSSATALFPQTHKEQVQQDFSGKMQDLPEESSLEYQQEYFVTTPGTET-------SETQKAMIVPSSPS 1689
Cdd:pfam06390   62 SFLNAHHRSAAAAAAAQVFPEPSEPESDHEDEDFEPELARPECLEYDEDDFDTETDSETepesdieSETEFETEPETEPD 141
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645 1690 KTPE-EVSTPAEEEK--------------------LYLQTPTSSERGGSPIIQEPEEPSEHRE------ESSPR--KTSL 1740
Cdd:pfam06390  142 TAPTtEPETEPEDEPgpvvpkgatfhqslterlhaLKLQSADASPRRAPPSTQEPESAREGEEpergplDKDPRdpEEEE 221
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1229385645 1741 VIVESADNQPETCErldEDAAFEKGDDMPEIPPE 1774
Cdd:pfam06390  222 EEKEEEKQQPHRCK---PKKPARRRDPSPESPPK 252
Ank_4 pfam13637
Ankyrin repeats (many copies);
171-232 1.67e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.58  E-value: 1.67e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1229385645  171 RLPALHIAARKDDTKSAALLLQNDHNadvqskmmVNRTTESGFTPLHIAAHYGNVNVATLLL 232
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGAD--------INAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
111-162 2.67e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.81  E-value: 2.67e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1229385645  111 TPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHNQAVAILL 162
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
645-781 2.18e-06

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 52.78  E-value: 2.18e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  645 LHLASQEGHTDMVTLLLDKGANIHMstksGLTSLHLAAQEDKVNVADILT---KHGADQDAHTKL----------GYTPL 711
Cdd:TIGR00870   57 FVAAIENENLELTELLLNLSCRGAV----GDTLLHAISLEYVDAVEAILLhllAAFRKSGPLELAndqytseftpGITAL 132
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  712 IVACHYGNVKMVNFLLKQGANVNAKTK--------------NGYTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTAL 777
Cdd:TIGR00870  133 HLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLL 212

                   ....
gi 1229385645  778 AIAK 781
Cdd:TIGR00870  213 HLLV 216
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
108-134 2.53e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 45.66  E-value: 2.53e-06
                            10        20
                    ....*....|....*....|....*..
gi 1229385645   108 NGFTPLYMAAQENHIDVVKYLLENGAN 134
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
376-403 6.48e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 44.50  E-value: 6.48e-06
                            10        20
                    ....*....|....*....|....*...
gi 1229385645   376 NGFTPLHIACKKNRIKVMELLVKYGASI 403
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
739-768 1.21e-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: 43.73  E-value: 1.21e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 1229385645   739 NGYTPLHQAAQQGHTHIINVLLQHGAKPNA 768
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
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 ...
1303-1432 4.12e-60

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: 202.32  E-value: 4.12e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645 1303 VPYMAKFVVFAKSHDPIEARLRCFCMTDDKVDKTLEQQENFAEVARSRDVEVLEGKPIYVDCFGNLVPLTKSGQHHIFSF 1382
Cdd:pfam17809    1 VPYLAKFVVFAKRYDPGEARLRCACMTDDGEDKTLEFHEGFTEVARSRDVEVLEGSPVSIELSGNLVPIKKKSQSRQMDF 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1229385645 1383 FAFKENRLPLFVKVRDTTQEPCGRLSFMKEPKSTRGLVHQAICNLNITLP 1432
Cdd:pfam17809   81 KAFRENRLDGSVRVKDPSDPPKGLLSFMRDAKVDGGTVSQPLCTLNIVLP 130
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
528-793 1.43e-59

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 207.11  E-value: 1.43e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  528 LLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHATAKN 607
Cdd:COG0666      7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  608 GYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKV 687
Cdd:COG0666     87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  688 NVADILTKHGADQDAHTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPN 767
Cdd:COG0666    167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246
                          250       260
                   ....*....|....*....|....*.
gi 1229385645  768 ATTANGNTALAIAKRLGYISVVDTLK 793
Cdd:COG0666    247 AKDKDGLTALLLAAAAGAALIVKLLL 272
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
291-579 4.92e-59

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 205.57  E-value: 4.92e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  291 DQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANP 370
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  371 NARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMA 450
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  451 ARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLE 530
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1229385645  531 AGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPL 579
Cdd:COG0666    241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
225-513 1.70e-58

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 204.03  E-value: 1.70e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  225 VNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAPL 304
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  305 LARTKNGLSPLHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNARALNGFTPLHIA 384
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  385 CKKNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLR 464
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1229385645  465 NGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPL 513
Cdd:COG0666    241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
196-480 4.25e-58

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 202.88  E-value: 4.25e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  196 NADVQSKMMVNRTTESGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKT 275
Cdd:COG0666      5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  276 RDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCG 355
Cdd:COG0666     85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANG 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  356 HYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGAS 435
Cdd:COG0666    165 NLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD 244
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1229385645  436 PDVTNIRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPL 480
Cdd:COG0666    245 LNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
490-777 5.62e-58

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 202.88  E-value: 5.62e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  490 EIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAAD 569
Cdd:COG0666      2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  570 SAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLAS 649
Cdd:COG0666     82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  650 QEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADILTKHGADQDAHTKLGYTPLIVACHYGNVKMVNFLLKQ 729
Cdd:COG0666    162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1229385645  730 GANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTAL 777
Cdd:COG0666    242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
330-612 1.24e-57

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 201.72  E-value: 1.24e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  330 LLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITES 409
Cdd:COG0666      7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  410 GLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKT 489
Cdd:COG0666     87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  490 EIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAAD 569
Cdd:COG0666    167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1229385645  570 SAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHATAKNGYTPL 612
Cdd:COG0666    247 AKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
159-447 1.98e-57

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 200.95  E-value: 1.98e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  159 AILLENDTKGKVRLPALHIAARKDDTKSAALLLQNDHNADVQSKMMVNRTTESGFTPLHIAAHYGNVNVATLLLNRGAAV 238
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  239 DFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMA 318
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  319 AQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVK 398
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1229385645  399 YGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETAL 447
Cdd:COG0666    241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
390-676 5.44e-57

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 199.80  E-value: 5.44e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  390 IKVMELLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNGALV 469
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  470 DARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVA 549
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  550 AKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQMQIASTLLN 629
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1229385645  630 YGAETNIVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLT 676
Cdd:COG0666    241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
462-744 2.99e-56

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 197.87  E-value: 2.99e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  462 LLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKK 541
Cdd:COG0666      7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  542 GFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQM 621
Cdd:COG0666     87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  622 QIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADILTKHGADQD 701
Cdd:COG0666    167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1229385645  702 AHTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPL 744
Cdd:COG0666    247 AKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
259-546 3.62e-56

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 197.48  E-value: 3.62e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  259 NMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLLQHKAPVD 338
Cdd:COG0666      2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  339 DVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAA 418
Cdd:COG0666     82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  419 FMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQH 498
Cdd:COG0666    162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1229385645  499 MAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPL 546
Cdd:COG0666    242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
555-793 3.75e-55

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 194.40  E-value: 3.75e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  555 LDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQMQIASTLLNYGAET 634
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  635 NIVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADILTKHGADQDAHTKLGYTPLIVA 714
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1229385645  715 CHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTALAIAKRLGYISVVDTLK 793
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
362-645 8.18e-55

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 193.63  E-value: 8.18e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  362 LLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNI 441
Cdd:COG0666      6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  442 RGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQ 521
Cdd:COG0666     86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  522 VDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASP 601
Cdd:COG0666    166 LEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADL 245
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1229385645  602 HATAKNGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPL 645
Cdd:COG0666    246 NAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
23-381 2.22e-54

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 192.48  E-value: 2.22e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645   23 LDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGANI 102
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  103 NAQSQNGFTPLYMAAQENHIDVVKYLLENGANqstatedgftplavalqqghnqavaillendtkgkvrlpalhiaarkd 182
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGAD------------------------------------------------ 112
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  183 dtksaalllqndhnadvqskmmVNRTTESGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVK 262
Cdd:COG0666    113 ----------------------VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  263 LLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLLQHKAPVDDVTL 342
Cdd:COG0666    171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250
                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 1229385645  343 DYLTALHVAAHCGHYRVTKLLLDKRANPNARALNGFTPL 381
Cdd:COG0666    251 DGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
5-348 5.18e-54

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 191.32  E-value: 5.18e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645    5 LQKSDSNASFLRAARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIAS 84
Cdd:COG0666     16 LLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAA 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645   85 LAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGANqstatedgftplavalqqghnqavaillen 164
Cdd:COG0666     96 RNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGAD------------------------------ 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  165 dtkgkvrlpalhiaarkddtksaalllqndhnadvqskmmVNRTTESGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARN 244
Cdd:COG0666    146 ----------------------------------------VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDND 185
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  245 GITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGDHV 324
Cdd:COG0666    186 GETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAA 265
                          330       340
                   ....*....|....*....|....
gi 1229385645  325 ECVKHLLQHKAPVDDVTLDYLTAL 348
Cdd:COG0666    266 LIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
423-711 2.49e-53

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 189.39  E-value: 2.49e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  423 LNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHP 502
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  503 DAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVA 582
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  583 AHYDNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLD 662
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1229385645  663 KGANIHMSTKSGLTSLHLAAQEDKVNVADILTKHGADQDAHTKLGYTPL 711
Cdd:COG0666    241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Death_ank2 cd08804
Death domain of Ankyrin-2; Death Domain (DD) of Ankyrin-2 (ANK-2) and related proteins. ...
1461-1544 1.24e-51

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: 176.43  E-value: 1.24e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645 1461 ERIEERLAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIV 1540
Cdd:cd08804      1 ERTEERLAHIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLTQCLTKINRMDIV 80

                   ....
gi 1229385645 1541 HLME 1544
Cdd:cd08804     81 HLME 84
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
3-315 2.52e-50

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 180.54  E-value: 2.52e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645    3 TMLQKSDSNASFLRAARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHI 82
Cdd:COG0666     47 LALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHL 126
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645   83 ASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGANqstatedgftplavalqqghnqavaill 162
Cdd:COG0666    127 AAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGAD---------------------------- 178
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  163 endtkgkvrlpalhiaarkddtksaalllqndhnadvqskmmVNRTTESGFTPLHIAAHYGNVNVATLLLNRGAAVDFTA 242
Cdd:COG0666    179 ------------------------------------------VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKD 216
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1229385645  243 RNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPL 315
Cdd:COG0666    217 NDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
945-1082 2.62e-44

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


Pssm-ID: 128514  Cd Length: 104  Bit Score: 155.97  E-value: 2.62e-44
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645   945 SGFLVSFMVDARGGAMRGCRhNGLRIIIPPRKCTAPTRVTCRLVKRHRLATMPPMVEGEGLASRLIEVGPSGAQflgklh 1024
Cdd:smart00218    1 PSFLVSGTFDARGGRLRGPR-TGVRLIIPPGAIPQGTRYTCYLVVHKTLSTPPPLEEGETLLSPVVECGPHGAL------ 73
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1229385645  1025 lptappplnegeslvsrilqlgppgtkFLGPVIVEIPHFAALRGKERELVVLRSENGD 1082
Cdd:smart00218   74 ---------------------------FLRPVILEVPHCASLRPRDWEIVLLRSENGG 104
PHA03100 PHA03100
ankyrin repeat protein; Provisional
540-764 3.35e-40

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 155.21  E-value: 3.35e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  540 KKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHY-----DNQKVALLLLEKGASPHATAKNGYTPLHI 614
Cdd:PHA03100    33 KKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIkynltDVKEIVKLLLEYGANVNAPDNNGITPLLY 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  615 AA--KKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTD--MVTLLLDKGANIhmstksgltslhlaaqeDKVNVA 690
Cdd:PHA03100   113 AIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDI-----------------NAKNRV 175
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1229385645  691 DILTKHGADQDAHTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGA 764
Cdd:PHA03100   176 NYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
Death_ank cd08317
Death domain associated with Ankyrins; Death Domain (DD) associated with Ankyrins. Ankyrins ...
1461-1544 2.68e-36

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: 132.39  E-value: 2.68e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645 1461 ERIEERLAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIV 1540
Cdd:cd08317      1 HRADLRLSDIANLLGSDWPELARELGVSEEDIDLIRSENPNSLAQQAMAMLRLWLEREGEKATGNALESALKKIGRDDIV 80

                   ....
gi 1229385645 1541 HLME 1544
Cdd:cd08317     81 EKCE 84
ZU5 pfam00791
ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.
949-1079 1.37e-35

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


Pssm-ID: 459941  Cd Length: 97  Bit Score: 131.11  E-value: 1.37e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  949 VSFMVDARGGAMRGCrHNGLRIIIPPRKCTAPTRVTCRLVKRHRLATMPPMVEGEGLASRLIEvgpsgaqflgklhlpta 1028
Cdd:pfam00791    1 VSGLVDSRGGRLVLP-NSGVSLLIPPGAIPEGTRIECYLAVNRDESSRPPLEEGETLLSPVVE----------------- 62
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1229385645 1029 ppplnegeslvsrilqLGPPGTKFLGPVIVEIPHFAALRGKERELVVLRSE 1079
Cdd:pfam00791   63 ----------------CGPPGLKFLKPVILEVPHCASLRPEEWEIVLKRSD 97
PHA03095 PHA03095
ankyrin-like protein; Provisional
383-668 7.34e-35

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 140.55  E-value: 7.34e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  383 IACKKNRIKVMELLVKYGASIQAITESGLTPIHVaaFMGH-----LNIVLLLLQNGASPDVTNIRGETALHMAARAGQVE 457
Cdd:PHA03095    20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHL--YLHYssekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTL 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  458 -VVRCLLRNGALVDARAREEQTPLHI--ASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASV--LLEAG 532
Cdd:PHA03095    98 dVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVELLrlLIDAG 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  533 AahSLATKK--GFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKN--GLTPLHVAAHYDNQKVALL--LLEKGASPHATAK 606
Cdd:PHA03095   178 A--DVYAVDdrFRSLLHHHLQSFKPRARIVRELIRAGCDPAATDmlGNTPLHSMATGSSCKRSLVlpLLIAGISINARNR 255
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1229385645  607 NGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLDKGANIH 668
Cdd:PHA03095   256 YGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAE 317
PHA03100 PHA03100
ankyrin repeat protein; Provisional
577-786 7.74e-34

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 136.33  E-value: 7.74e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  577 TPLHVAAHYDNQKVALLLLEKGASPHATAKNGYTPLHIAA-----KKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQE 651
Cdd:PHA03100    37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISK 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  652 --GHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQ--EDKVNVADILTKHGADQDAHTKlgytplivachygnvkmVNFLL 727
Cdd:PHA03100   117 ksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLEsnKIDLKILKLLIDKGVDINAKNR-----------------VNYLL 179
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1229385645  728 KQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTAL--AIAKRLGYI 786
Cdd:PHA03100   180 SYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLhiAILNNNKEI 240
PHA03100 PHA03100
ankyrin repeat protein; Provisional
164-406 9.78e-34

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 136.33  E-value: 9.78e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  164 NDTKGKVRLPALHIAARKDDTKSAALLLqnDHNADVQSKMMVNrttesgFTPLHIAAHYG-----NVNVATLLLNRGAAV 238
Cdd:PHA03100    28 NDYSYKKPVLPLYLAKEARNIDVVKILL--DNGADINSSTKNN------STPLHYLSNIKynltdVKEIVKLLLEYGANV 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  239 DFTARNGITPLHVAS--KRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHD--QVVELLLERGAPLLARTKnglsp 314
Cdd:PHA03100   100 NAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKNR----- 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  315 lhmaaqgdhvecVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVME 394
Cdd:PHA03100   175 ------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFK 242
                          250
                   ....*....|..
gi 1229385645  395 LLVKYGASIQAI 406
Cdd:PHA03100   243 LLLNNGPSIKTI 254
PHA03100 PHA03100
ankyrin repeat protein; Provisional
190-435 1.99e-32

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 132.48  E-value: 1.99e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  190 LLQNDHNADVQSKMMVnrttesgfTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLH-----VASKRGNTNMVKLL 264
Cdd:PHA03100    21 IIMEDDLNDYSYKKPV--------LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLL 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  265 LDRGGQIDAKTRDGLTPLHCAA--RSGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGDHV--ECVKHLLQHKAPVDDV 340
Cdd:PHA03100    93 LEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAK 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  341 TldyltalhvaahcghyRVtKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAAFM 420
Cdd:PHA03100   173 N----------------RV-NYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILN 235
                          250
                   ....*....|....*
gi 1229385645  421 GHLNIVLLLLQNGAS 435
Cdd:PHA03100   236 NNKEIFKLLLNNGPS 250
PHA03095 PHA03095
ankyrin-like protein; Provisional
324-629 5.73e-32

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 132.07  E-value: 5.73e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  324 VECVKHLLQHKAPVD-DVTLDYlTALHVAAHCGHYRVTK---LLLDKRANPNARALNGFTPLHI-ACKKNRIKVMELLVK 398
Cdd:PHA03095    27 VEEVRRLLAAGADVNfRGEYGK-TPLHLYLHYSSEKVKDivrLLLEAGADVNAPERCGFTPLHLyLYNATTLDVIKLLIK 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  399 YGASIQAITESGLTPIHV--AAFMGHLNIVLLLLQNGASPDVTNIRGETALHmaaragqvevvrCLLRNGAlVDAraree 476
Cdd:PHA03095   106 AGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLA------------VLLKSRN-ANV----- 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  477 qtplhiasrlgktEIVQLLLQHMAHPDAATTNGYTPLHI---SAREGQvDVASVLLEAGAAHSLATKKGFTPLHVAAKYG 553
Cdd:PHA03095   168 -------------ELLRLLIDAGADVYAVDDRFRSLLHHhlqSFKPRA-RIVRELIRAGCDPAATDMLGNTPLHSMATGS 233
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1229385645  554 S---LDVAKLLLqRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQMQIASTLLN 629
Cdd:PHA03095   234 SckrSLVLPLLI-AGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALA 311
PHA02876 PHA02876
ankyrin repeat protein; Provisional
341-733 9.58e-32

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 134.42  E-value: 9.58e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  341 TLDYLTALHVAAHCGHYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAAFM 420
Cdd:PHA02876   142 SIEYMKLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDS 221
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  421 GHLNIVLLLLQNGASPDvtniRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGK-TEIVQLLLQHM 499
Cdd:PHA02876   222 KNIDTIKAIIDNRSNIN----KNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERG 297
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  500 AHPDAATTNGYTPLHISAREGqvdvasvlleagaahslatkkgftplhvaakYGSLDVaKLLLQRRAAADSAGKNGLTPL 579
Cdd:PHA02876   298 ADVNAKNIKGETPLYLMAKNG-------------------------------YDTENI-RTLIMLGADVNAADRLYITPL 345
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  580 HVAAHYD-NQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDM-V 657
Cdd:PHA02876   346 HQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsV 425
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1229385645  658 TLLLDKGANIHMSTKSGLTSLHLAAQED-KVNVADILTKHGADQDAHTKLGYTPLIVACHYGNVkmVNFLLKQGANV 733
Cdd:PHA02876   426 KTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIALEYHGI--VNILLHYGAEL 500
PHA03095 PHA03095
ankyrin-like protein; Provisional
56-403 9.87e-32

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 131.30  E-value: 9.87e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645   56 VGLVQELLGRGSSVDSATKKGNTALHI---ASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQ-ENHIDVVKYLLEN 131
Cdd:PHA03095    27 VEEVRRLLAAGADVNFRGEYGKTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYnATTLDVIKLLIKA 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  132 GANQSTATEDGFTPLAVALQqghNQAVaillendtkgkvrlpalhiaarkdDTKSAALLLqnDHNADVqskmmvNRTTES 211
Cdd:PHA03095   107 GADVNAKDKVGRTPLHVYLS---GFNI------------------------NPKVIRLLL--RKGADV------NALDLY 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  212 GFTPLHIAAHYGNVNVATL--LLNRGA---AVDFtarNGITPLHV--ASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHC 284
Cdd:PHA03095   152 GMTPLAVLLKSRNANVELLrlLIDAGAdvyAVDD---RFRSLLHHhlQSFKPRARIVRELIRAGCDPAATDMLGNTPLHS 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  285 AAR--SGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKL 362
Cdd:PHA03095   229 MATgsSCKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRA 308
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 1229385645  363 LLDKRANPN--ARALNGFTPLH--IACKKNRIKVMELLVKYGASI 403
Cdd:PHA03095   309 ALAKNPSAEtvAATLNTASVAGgdIPSDATRLCVAKVVLRGAFSL 353
PHA02876 PHA02876
ankyrin repeat protein; Provisional
23-434 1.48e-31

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 133.65  E-value: 1.48e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645   23 LDKV-VEYLKGGIDINTCNQNGLN-------ALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKV 94
Cdd:PHA02876   117 LDEAcIHILKEAISGNDIHYDKINesieymkLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNL 196
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645   95 LVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGANqstatedgftplavalqqghnqavaiLLENDTkgkvrlpA 174
Cdd:PHA02876   197 LLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSN--------------------------INKNDL-------S 243
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  175 LHIAARKDDTKSAALLLqndhnadvQSKMMVNRTTESGFTPLHIAAHYGNVN-VATLLLNRGAAVDFTARNGITPLHVAS 253
Cdd:PHA02876   244 LLKAIRNEDLETSLLLY--------DAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMA 315
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  254 KRG-NTNMVKLLLDRGGQIDAKTRDGLTPLHCAAR-SGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLL 331
Cdd:PHA02876   316 KNGyDTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLL 395
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  332 QHKAPVDDVTLDYLTALHVAAhCGH--YRVTKLLLDKRANPNARALNGFTPLHIACKKN-RIKVMELLVKYGASIQAITE 408
Cdd:PHA02876   396 DYGADIEALSQKIGTALHFAL-CGTnpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINI 474
                          410       420
                   ....*....|....*....|....*.
gi 1229385645  409 SGLTPIHVAafMGHLNIVLLLLQNGA 434
Cdd:PHA02876   475 QNQYPLLIA--LEYHGIVNILLHYGA 498
PHA02874 PHA02874
ankyrin repeat protein; Provisional
379-648 1.53e-31

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 130.08  E-value: 1.53e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  379 TPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGAS------PDVTNirgetalhmaar 452
Cdd:PHA02874    37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDtsilpiPCIEK------------ 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  453 agqvEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAG 532
Cdd:PHA02874   105 ----DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKG 180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  533 AAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLleKGASPHATAKNGYTPL 612
Cdd:PHA02874   181 AYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIELLI--NNASINDQDIDGSTPL 258
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1229385645  613 HIAAKKN-QMQIASTLLNYGAETNIVTKQGVTPLHLA 648
Cdd:PHA02874   259 HHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTA 295
PHA03100 PHA03100
ankyrin repeat protein; Provisional
231-471 2.10e-31

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 129.40  E-value: 2.10e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  231 LLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQ-----VVELLLERGAPLL 305
Cdd:PHA03100    21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLtdvkeIVKLLLEYGANVN 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  306 ARTKNGLSPLHMAAQG--DHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHY--RVTKLLLDKRANPNAralngftpl 381
Cdd:PHA03100   101 APDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINA--------- 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  382 hiackKNRIKvmeLLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRC 461
Cdd:PHA03100   172 -----KNRVN---YLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKL 243
                          250
                   ....*....|
gi 1229385645  462 LLRNGALVDA 471
Cdd:PHA03100   244 LLNNGPSIKT 253
PHA02876 PHA02876
ankyrin repeat protein; Provisional
386-765 6.21e-31

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 131.72  E-value: 6.21e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  386 KKNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRcllrn 465
Cdd:PHA02876   154 QQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIK----- 228
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  466 gALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGY--TPLHISAREGQVD-VASVLLEAGAAHSLATKKG 542
Cdd:PHA02876   229 -AIIDNRSNINKNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCknTPLHHASQAPSLSrLVPKLLERGADVNAKNIKG 307
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  543 FTPLHVAAKYG-SLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYD-NQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQ 620
Cdd:PHA02876   308 ETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNN 387
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  621 MQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDM-VTLLLDKGANIHMSTKSGLTSLHLAAQED-KVNVADILTKHGA 698
Cdd:PHA02876   388 VVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGA 467
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1229385645  699 DQDAHTKLGYTPLIVACHYGNvkmvnfllkqganvnaktkngytplhqaaqqghthIINVLLQHGAK 765
Cdd:PHA02876   468 DVNAINIQNQYPLLIALEYHG-----------------------------------IVNILLHYGAE 499
PHA02876 PHA02876
ankyrin repeat protein; Provisional
180-500 4.01e-30

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 129.03  E-value: 4.01e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  180 RKDDTKSAALLLQNdhNADVQSKMMVNRTtesgftPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTN 259
Cdd:PHA02876   154 QQDELLIAEMLLEG--GADVNAKDIYCIT------PIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNID 225
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  260 MVKLLLDRGGQIDAKTRDGL-----------------------------TPLHCAARSGH-DQVVELLLERGAPLLARTK 309
Cdd:PHA02876   226 TIKAIIDNRSNINKNDLSLLkairnedletslllydagfsvnsiddcknTPLHHASQAPSlSRLVPKLLERGADVNAKNI 305
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  310 NGLSPLH-MAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKL-LLDKRANPNARALNGFTPLHIACKK 387
Cdd:PHA02876   306 KGETPLYlMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVItLLELGANVNARDYCDKTPIHYAAVR 385
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  388 NRIKVMELLVKYGASIQAITESGLTPIHVAAF-MGHLNIVLLLLQNGASPDVTNIRGETALHMAARAG-QVEVVRCLLRN 465
Cdd:PHA02876   386 NNVVIINTLLDYGADIEALSQKIGTALHFALCgTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDN 465
                          330       340       350
                   ....*....|....*....|....*....|....*
gi 1229385645  466 GALVDARAREEQTPLHIAsrLGKTEIVQLLLQHMA 500
Cdd:PHA02876   466 GADVNAINIQNQYPLLIA--LEYHGIVNILLHYGA 498
PHA03095 PHA03095
ankyrin-like protein; Provisional
490-793 5.72e-30

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 125.91  E-value: 5.72e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  490 EIVQLLLQHMAHPDAATTNGYTPLHI---SAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGS-LDVAKLLLQRR 565
Cdd:PHA03095    28 EEVRRLLAAGADVNFRGEYGKTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAG 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  566 AAADSAGKNGLTPLHVAAHYDN--QKVALLLLEKGASPHATAKNGYTPLHIAAKKNQ--MQIASTLLNYGAETNIVTKQG 641
Cdd:PHA03095   108 ADVNAKDKVGRTPLHVYLSGFNinPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanVELLRLLIDAGADVYAVDDRF 187
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  642 VTPLH--LASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADI--LTKHGADQDAHTKLGYTPLIVACHY 717
Cdd:PHA03095   188 RSLLHhhLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVF 267
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1229385645  718 GNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQhgAKPNATT-ANgntALAIAKRLGYISVVDTLK 793
Cdd:PHA03095   268 NNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALA--KNPSAETvAA---TLNTASVAGGDIPSDATR 339
PHA02876 PHA02876
ankyrin repeat protein; Provisional
227-633 1.84e-29

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 127.10  E-value: 1.84e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  227 VATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAarsghdqvvelllergaplla 306
Cdd:PHA02876   160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECA--------------------- 218
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  307 rtknglsplhmaaqgdhvecvkhllqhkapVDDVTLDYLTAlhvaahcghyrvtklLLDKRANPNARALNgftpLHIACK 386
Cdd:PHA02876   219 ------------------------------VDSKNIDTIKA---------------IIDNRSNINKNDLS----LLKAIR 249
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  387 KNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGHLN-IVLLLLQNGASPDVTNIRGETALHMAARAG-QVEVVRCLLR 464
Cdd:PHA02876   250 NEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIM 329
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  465 NGALVDARAREEQTPLHIASRLGK-TEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGF 543
Cdd:PHA02876   330 LGADVNAADRLYITPLHQASTLDRnKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIG 409
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  544 TPLHVAAkYGS--LDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQ-KVALLLLEKGASPHATAKNGYTPLHIAAKKNq 620
Cdd:PHA02876   410 TALHFAL-CGTnpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAINIQNQYPLLIALEYH- 487
                          410
                   ....*....|...
gi 1229385645  621 mQIASTLLNYGAE 633
Cdd:PHA02876   488 -GIVNILLHYGAE 499
PHA02876 PHA02876
ankyrin repeat protein; Provisional
455-792 1.92e-29

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 127.10  E-value: 1.92e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  455 QVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAgaa 534
Cdd:PHA02876   157 ELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDN--- 233
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  535 HSLATKKGFTPLHvAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDN-QKVALLLLEKGASPHATAKNGYTPLH 613
Cdd:PHA02876   234 RSNINKNDLSLLK-AIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLY 312
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  614 IAAKKN-QMQIASTLLNYGAETNIVTKQGVTPLHLASQ-EGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVAD 691
Cdd:PHA02876   313 LMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIIN 392
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  692 ILTKHGADQDAHTKLGYTPLIVACHYGNVKM-VNFLLKQGANVNAKTKNGYTPLHQAAQQG-HTHIINVLLQHGAKPNAT 769
Cdd:PHA02876   393 TLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAI 472
                          330       340
                   ....*....|....*....|...
gi 1229385645  770 TANGNTALAIAkrLGYISVVDTL 792
Cdd:PHA02876   473 NIQNQYPLLIA--LEYHGIVNIL 493
PHA03095 PHA03095
ankyrin-like protein; Provisional
114-420 2.46e-29

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 123.98  E-value: 2.46e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  114 YMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHnqavaillendtkgkvrlpalhiaarKDDTKSAALLLqn 193
Cdd:PHA03095    19 LLNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSS--------------------------EKVKDIVRLLL-- 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  194 DHNADVqskmmvNRTTESGFTPLHIAAHYGNV-NVATLLLNRGAAVDFTARNGITPLHV--ASKRGNTNMVKLLLDRGGQ 270
Cdd:PHA03095    71 EAGADV------NAPERCGFTPLHLYLYNATTlDVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGAD 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  271 IDAKTRDGLTPLHCAARSGH--DQVVELLLERGAPLLARTKNGLSPLHMAAQG--DHVECVKHLLQHKAPVDDVTLDYLT 346
Cdd:PHA03095   145 VNALDLYGMTPLAVLLKSRNanVELLRLLIDAGADVYAVDDRFRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNT 224
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1229385645  347 ALHVAAHCGHYRVTKL--LLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIhvaAFM 420
Cdd:PHA03095   225 PLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL---SLM 297
PHA03095 PHA03095
ankyrin-like protein; Provisional
8-335 5.20e-28

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 120.13  E-value: 5.20e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645    8 SDSNASFLRAARAGN--LDKVVEYLKGGIDINTCNQNGLNALHLAAKEGH---VGLVQELLGRGSSVDSATKKGNTALHI 82
Cdd:PHA03095    10 IMEAALYDYLLNASNvtVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHL 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645   83 -ASLAGQAEVVKVLVKEGANINAQSQNGFTPL--YMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQgHNQAVA 159
Cdd:PHA03095    90 yLYNATTLDVIKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKS-RNANVE 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  160 I---LLEND----TKGKVRLPALHIAA---RKDDTKSAALLlqnDHNADVQSKMMvnrtteSGFTPLHIAAHYG---NVN 226
Cdd:PHA03095   169 LlrlLIDAGadvyAVDDRFRSLLHHHLqsfKPRARIVRELI---RAGCDPAATDM------LGNTPLHSMATGSsckRSL 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  227 VATLLLNrGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAP--L 304
Cdd:PHA03095   240 VLPLLIA-GISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSaeT 318
                          330       340       350
                   ....*....|....*....|....*....|..
gi 1229385645  305 LARTKNGLSPLHMAAQGDHV-ECVKHLLQHKA 335
Cdd:PHA03095   319 VAATLNTASVAGGDIPSDATrLCVAKVVLRGA 350
Death_ank3 cd08803
Death domain of Ankyrin-3; Death Domain (DD) of the human protein ankyrin-3 (ANK-3) and ...
1461-1544 5.97e-28

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: 108.61  E-value: 5.97e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645 1461 ERIEERLAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIV 1540
Cdd:cd08803      1 ERTDIRMAIVADHLGLSWTELARELNFSVDEINQIRVENPNSLIAQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIV 80

                   ....
gi 1229385645 1541 HLME 1544
Cdd:cd08803     81 TLLE 84
PHA03100 PHA03100
ankyrin repeat protein; Provisional
456-667 6.56e-28

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 119.00  E-value: 6.56e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  456 VEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQV-----DVASVLLE 530
Cdd:PHA03100    15 VKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLE 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  531 AGAAHSLATKKGFTPLHVAA--KYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHY--DNQKVALLLLEKGAspHATAK 606
Cdd:PHA03100    95 YGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESnkIDLKILKLLIDKGV--DINAK 172
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1229385645  607 N------------------GYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLDKGANI 667
Cdd:PHA03100   173 NrvnyllsygvpinikdvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSI 251
Death_ank1 cd08805
Death domain of Ankyrin-1; Death Domain (DD) of the human protein ankyrin-1 (ANK-1) and ...
1461-1544 8.31e-28

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: 108.14  E-value: 8.31e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645 1461 ERIEERLAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIV 1540
Cdd:cd08805      1 ERVEMKMAVIREHLGLSWAELARELQFSVEDINRIRVENPNSLLEQSTALLNLWVDREGENAKMEPLYPALYSIDRLTIV 80

                   ....
gi 1229385645 1541 HLME 1544
Cdd:cd08805     81 NILE 84
PHA02875 PHA02875
ankyrin repeat protein; Provisional
549-770 1.38e-27

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 117.78  E-value: 1.38e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  549 AAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQMQIASTLL 628
Cdd:PHA02875     9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  629 NYGAETN-IVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADILTKHGADQDAHTKLG 707
Cdd:PHA02875    89 DLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCG 168
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1229385645  708 YTPLIVACHYGNVKMVNFLLKQGANVNAKTKNG-YTPLHQAAQQGHTHIINVLLQHGAKPNATT 770
Cdd:PHA02875   169 CTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNIMF 232
PHA02875 PHA02875
ankyrin repeat protein; Provisional
219-449 2.02e-27

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 117.40  E-value: 2.02e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  219 AAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLL 298
Cdd:PHA02875     9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  299 ERGAPLL-ARTKNGLSPLHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNARALNG 377
Cdd:PHA02875    89 DLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCG 168
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1229385645  378 FTPLHIACKKNRIKVMELLVKYGASIQAITESG-LTPIHVAAFMGHLNIVLLLLQNGASPD-VTNIRGE--TALHM 449
Cdd:PHA02875   169 CTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNiMFMIEGEecTILDM 244
PHA02875 PHA02875
ankyrin repeat protein; Provisional
444-671 4.48e-27

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 116.24  E-value: 4.48e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  444 ETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVD 523
Cdd:PHA02875     3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  524 VASVLLEAGA-AHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASPH 602
Cdd:PHA02875    83 AVEELLDLGKfADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLD 162
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  603 ATAKNGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQG-VTPLHLASQEGHTDMVTLLLDKGANIHMST 671
Cdd:PHA02875   163 IEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNIMF 232
PHA02874 PHA02874
ankyrin repeat protein; Provisional
262-573 4.58e-27

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 116.60  E-value: 4.58e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  262 KLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLLQHKapVDDVT 341
Cdd:PHA02874    19 KIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG--VDTSI 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  342 LdyltalhvAAHCGHYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAAFMG 421
Cdd:PHA02874    97 L--------PIPCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHN 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  422 HLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASrLGKTEIVQLLLQHmAH 501
Cdd:PHA02874   169 FFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI-IHNRSAIELLINN-AS 246
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1229385645  502 PDAATTNGYTPLHISAR-EGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLD-VAKLLLQRRAAADSAGK 573
Cdd:PHA02874   247 INDQDIDGSTPLHHAINpPCDIDIIDILLYHKADISIKDNKGENPIDTAFKYINKDpVIKDIIANAVLIKEADK 320
PHA03100 PHA03100
ankyrin repeat protein; Provisional
322-569 8.79e-27

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 115.53  E-value: 8.79e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  322 DHVECVKHLLQHKAPVDDVTLDYLTALHVAahCGHYRVT-------KLLLDKRANPNARALNGFTPLHIAC-----KKNR 389
Cdd:PHA03100     8 TKSRIIKVKNIKYIIMEDDLNDYSYKKPVL--PLYLAKEarnidvvKILLDNGADINSSTKNNSTPLHYLSnikynLTDV 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  390 IKVMELLVKYGASIQAITESGLTPIHVAAF--MGHLNIVLLLLQNGASPDVTNIRGETALHMAARAGQV--EVVRCLLRN 465
Cdd:PHA03100    86 KEIVKLLLEYGANVNAPDNNGITPLLYAISkkSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDK 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  466 GALVDARAReeqtplhiasrlgkteiVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTP 545
Cdd:PHA03100   166 GVDINAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTP 228
                          250       260
                   ....*....|....*....|....
gi 1229385645  546 LHVAAKYGSLDVAKLLLQRRAAAD 569
Cdd:PHA03100   229 LHIAILNNNKEIFKLLLNNGPSIK 252
PHA02878 PHA02878
ankyrin repeat protein; Provisional
80-428 3.23e-26

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 114.59  E-value: 3.23e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645   80 LHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLenganqSTATEDGFTPLAVALQQG-HNQAV 158
Cdd:PHA02878    41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMI------RSINKCSVFYTLVAIKDAfNNRNV 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  159 AI---LLENDTKGKVRLPALHIAARKDD----TKSAALLLQndHNADVQskmMVNRTTESgfTPLHIAAHYGNVNVATLL 231
Cdd:PHA02878   115 EIfkiILTNRYKNIQTIDLVYIDKKSKDdiieAEITKLLLS--YGADIN---MKDRHKGN--TALHYATENKDQRLTELL 187
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  232 LNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHD-QVVELLLERGAPLLAR-TK 309
Cdd:PHA02878   188 LSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDyDILKLLLEHGVDVNAKsYI 267
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  310 NGLSPLHMAAQGDHVecVKHLLQHKAPVDDVTLDYLTALHVAA------HCGHYRVTKLLLDKRANPNARALNGFTpLHI 383
Cdd:PHA02878   268 LGLTALHSSIKSERK--LKLLLEYGADINSLNSYKLTPLSSAVkqylciNIGRILISNICLLKRIKPDIKNSEGFI-DNM 344
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 1229385645  384 ACKKNRIKVMELLVKYGASIQAITESGLTPIHVAA-FMGHLNIVLL 428
Cdd:PHA02878   345 DCITSNKRLNQIKDKCEDELNRLASIKITNTYSFDdFLKCDNSTLL 390
PHA03100 PHA03100
ankyrin repeat protein; Provisional
16-273 4.25e-26

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 113.22  E-value: 4.25e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645   16 RAARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVglvqelLGRGssvdsatkkgntalhiaslagqAEVVKVL 95
Cdd:PHA03100    41 LAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYN------LTDV----------------------KEIVKLL 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645   96 VKEGANINAQSQNGFTPLYMAAQE--NHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHNqavaillendtkgkvrlp 173
Cdd:PHA03100    93 LEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKI------------------ 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  174 alhiaarkdDTKSAALLLqnDHNADVQSKMMVNR----------TTESGFTPLHIAAHYGNVNVATLLLNRGAAVDFTAR 243
Cdd:PHA03100   155 ---------DLKILKLLI--DKGVDINAKNRVNYllsygvpiniKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNK 223
                          250       260       270
                   ....*....|....*....|....*....|
gi 1229385645  244 NGITPLHVASKRGNTNMVKLLLDRGGQIDA 273
Cdd:PHA03100   224 YGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PHA02878 PHA02878
ankyrin repeat protein; Provisional
213-510 6.50e-26

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 113.82  E-value: 6.50e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  213 FTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLldrggqIDAKTRDGLTPLHCAARSG-HD 291
Cdd:PHA02878    38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEM------IRSINKCSVFYTLVAIKDAfNN 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  292 QVVELLlerGAPLLARTKN----GLSPLHMAAQGDHVEC--VKHLLQHKAPVDDVTLDYL-TALHVAAHCGHYRVTKLLL 364
Cdd:PHA02878   112 RNVEIF---KIILTNRYKNiqtiDLVYIDKKSKDDIIEAeiTKLLLSYGADINMKDRHKGnTALHYATENKDQRLTELLL 188
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  365 DKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVA-AFMGHLNIVLLLLQNGASPDV-TNIR 442
Cdd:PHA02878   189 SYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAkSYIL 268
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1229385645  443 GETALHMAARAGQveVVRCLLRNGALVDARAREEQTPLHIASR------LGKTEIVQLLLQHMAHPDAATTNGY 510
Cdd:PHA02878   269 GLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPLSSAVKqylcinIGRILISNICLLKRIKPDIKNSEGF 340
PHA02875 PHA02875
ankyrin repeat protein; Provisional
582-777 8.53e-25

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 109.31  E-value: 8.53e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  582 AAHYDNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLL 661
Cdd:PHA02875     9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  662 DKGANIH-MSTKSGLTSLHLAAQEDKVNVADILTKHGADQDAHTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNG 740
Cdd:PHA02875    89 DLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCG 168
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1229385645  741 YTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTAL 777
Cdd:PHA02875   169 CTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAA 205
PHA02874 PHA02874
ankyrin repeat protein; Provisional
54-337 3.81e-24

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 107.74  E-value: 3.81e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645   54 GHVGLVQELL-GRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENG 132
Cdd:PHA02874    12 GDIEAIEKIIkNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  133 ANQSTatedgftplaVALQQGHNQAVAILLEN----DTKGKVRLPALHIAARKDDTKSAALLLQndHNADvqskmmVNRT 208
Cdd:PHA02874    92 VDTSI----------LPIPCIEKDMIKTILDCgidvNIKDAELKTFLHYAIKKGDLESIKMLFE--YGAD------VNIE 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  209 TESGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARs 288
Cdd:PHA02874   154 DDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII- 232
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1229385645  289 gHDQVVELLLERGAPLLARTKNGLSPLHMAAQGD-HVECVKHLLQHKAPV 337
Cdd:PHA02874   233 -HNRSAIELLINNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADI 281
PHA02878 PHA02878
ankyrin repeat protein; Provisional
496-785 5.26e-24

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 108.04  E-value: 5.26e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  496 LQHMAH-PDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLqRRAAADSAGkN 574
Cdd:PHA02878    23 IDHTENySTSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMI-RSINKCSVF-Y 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  575 GLTPLHVAAHYDNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQMQIASTLLNYGAETNIVTK-QGVTPLHLASQEGH 653
Cdd:PHA02878   101 TLVAIKDAFNNRNVEIFKIILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDRhKGNTALHYATENKD 180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  654 TDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADILTKHGADQDAHTKLGYTPLIVACHY-GNVKMVNFLLKQGAN 732
Cdd:PHA02878   181 QRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVD 260
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1229385645  733 VNAK-TKNGYTPLHQAAQQghTHIINVLLQHGAKPNATTANGNTALAIA--KRLGY 785
Cdd:PHA02878   261 VNAKsYILGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAvkQYLCI 314
PHA02875 PHA02875
ankyrin repeat protein; Provisional
355-638 6.38e-24

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 106.61  E-value: 6.38e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  355 GHYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGAsiqaitesgltpihvaafmghlnivlllLQNGA 434
Cdd:PHA02875    13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGA----------------------------IPDVK 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  435 SPDVtnirgETALHMAARAGQVEVVRCLLRNGALV-DARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNgytpl 513
Cdd:PHA02875    65 YPDI-----ESELHDAVEEGDVKAVEELLDLGKFAdDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTD----- 134
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  514 hisaregqvdvasvlleagaahslatkkGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALL 593
Cdd:PHA02875   135 ----------------------------KFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKM 186
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1229385645  594 LLEKGASPHATAKNG-YTPLHIAAKKNQMQIASTLLNYGAETNIVT 638
Cdd:PHA02875   187 LLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNIMF 232
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
1460-1545 7.05e-24

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: 97.10  E-value: 7.05e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  1460 QERIEERLAYIADH-LGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMD 1538
Cdd:smart00005    1 PELTRQKLAKLLDHpLGLDWRELARKLGLSEADIDQIRTEAPRDLAEQSVQLLRLWEQREGKNATLGTLLEALRKMGRDD 80

                    ....*..
gi 1229385645  1539 IVHLMET 1545
Cdd:smart00005   81 AVELLRS 87
Ank_2 pfam12796
Ankyrin repeats (3 copies);
47-134 1.52e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 96.34  E-value: 1.52e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645   47 LHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEgANINAQSqNGFTPLYMAAQENHIDVVK 126
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                   ....*...
gi 1229385645  127 YLLENGAN 134
Cdd:pfam12796   79 LLLEKGAD 86
PHA02874 PHA02874
ankyrin repeat protein; Provisional
86-425 1.69e-23

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 105.82  E-value: 1.69e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645   86 AGQAEVVKVLVKEGAN-INAQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHNQAVAILLEN 164
Cdd:PHA02874    11 SGDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDN 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  165 DTKGKVrlpaLHIAARKDDTKSAALllqnDHNADVQSKmmvNRTTEsgfTPLHIAAHYGNVNVATLLLNRGAAVDFTARN 244
Cdd:PHA02874    91 GVDTSI----LPIPCIEKDMIKTIL----DCGIDVNIK---DAELK---TFLHYAIKKGDLESIKMLFEYGADVNIEDDN 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  245 GITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMAAQgdHV 324
Cdd:PHA02874   157 GCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HN 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  325 ECVKHLLQHKAPVDDVTLDYLTALHVAAH--CGhYRVTKLLLDKRANPNARALNGFTPLHIACKK-NRIKVMELLVkygA 401
Cdd:PHA02874   235 RSAIELLINNASINDQDIDGSTPLHHAINppCD-IDIIDILLYHKADISIKDNKGENPIDTAFKYiNKDPVIKDII---A 310
                          330       340
                   ....*....|....*....|....
gi 1229385645  402 SIQAITESGLTPihVAAFMGHLNI 425
Cdd:PHA02874   311 NAVLIKEADKLK--DSDFLEHIEI 332
Ank_2 pfam12796
Ankyrin repeats (3 copies);
216-302 2.34e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 95.95  E-value: 2.34e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  216 LHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRgGQIDAKTrDGLTPLHCAARSGHDQVVE 295
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                   ....*..
gi 1229385645  296 LLLERGA 302
Cdd:pfam12796   79 LLLEKGA 85
Ank_2 pfam12796
Ankyrin repeats (3 copies);
348-440 2.56e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.87  E-value: 2.56e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  348 LHVAAHCGHYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGAsiQAITESGLTPIHVAAFMGHLNIVL 427
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 1229385645  428 LLLQNGASPDVTN 440
Cdd:pfam12796   79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
282-373 6.70e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 91.72  E-value: 6.70e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  282 LHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLLQHKAPvdDVTLDYLTALHVAAHCGHYRVTK 361
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|..
gi 1229385645  362 LLLDKRANPNAR 373
Cdd:pfam12796   79 LLLEKGADINVK 90
PHA02874 PHA02874
ankyrin repeat protein; Provisional
447-792 8.37e-22

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 100.42  E-value: 8.37e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  447 LHMAARAGQVEVVRCLLRN-GALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNgyTPlhisaregqvdva 525
Cdd:PHA02874     5 LRMCIYSGDIEAIEKIIKNkGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTK--IP------------- 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  526 svlleagaahslatkkgfTPLHVAAKYGSLDVAKLLLQrraaadsagkNGLTPLHVAAHYDNQKVALLLLEKGASPHATA 605
Cdd:PHA02874    70 ------------------HPLLTAIKIGAHDIIKLLID----------NGVDTSILPIPCIEKDMIKTILDCGIDVNIKD 121
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  606 KNGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQed 685
Cdd:PHA02874   122 AELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAE-- 199
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  686 kvnvadiltkhgadqdahtklgytplivachYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQqgHTHIINVLLQHGAK 765
Cdd:PHA02874   200 -------------------------------YGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNAS 246
                          330       340       350
                   ....*....|....*....|....*....|
gi 1229385645  766 PNATTANGNTALAIAkrLGY---ISVVDTL 792
Cdd:PHA02874   247 INDQDIDGSTPLHHA--INPpcdIDIIDIL 274
Ank_2 pfam12796
Ankyrin repeats (3 copies);
414-504 8.88e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 91.33  E-value: 8.88e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  414 IHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNgalVDARAREE-QTPLHIASRLGKTEIV 492
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNgRTALHYAARSGHLEIV 77
                           90
                   ....*....|..
gi 1229385645  493 QLLLQHMAHPDA 504
Cdd:pfam12796   78 KLLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
249-335 1.32e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.95  E-value: 1.32e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  249 LHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAplLARTKNGLSPLHMAAQGDHVECVK 328
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78

                   ....*..
gi 1229385645  329 HLLQHKA 335
Cdd:pfam12796   79 LLLEKGA 85
Ank_2 pfam12796
Ankyrin repeats (3 copies);
315-405 1.56e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.56  E-value: 1.56e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  315 LHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKrANPNARaLNGFTPLHIACKKNRIKVME 394
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLK-DNGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|.
gi 1229385645  395 LLVKYGASIQA 405
Cdd:pfam12796   79 LLLEKGADINV 89
Death pfam00531
Death domain;
1464-1544 2.54e-21

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 89.73  E-value: 2.54e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645 1464 EERLAYIADH---LGFSWTELARELDFTEEQIHQIRIENPNsLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIV 1540
Cdd:pfam00531    1 RKQLDRLLDPpppLGKDWRELARKLGLSENEIDEIESENPR-LRSQTYELLRLWEQREGKNATVGTLLEALRKLGRRDAA 79

                   ....
gi 1229385645 1541 HLME 1544
Cdd:pfam00531   80 EKIQ 83
Ank_2 pfam12796
Ankyrin repeats (3 copies);
678-769 3.57e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.79  E-value: 3.57e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  678 LHLAAQEDKVNVADILTKHGADQDAHTKLGYTPLIVACHYGNVKMVNFLLKQgANVNAKTkNGYTPLHQAAQQGHTHIIN 757
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|..
gi 1229385645  758 VLLQHGAKPNAT 769
Cdd:pfam12796   79 LLLEKGADINVK 90
PHA02875 PHA02875
ankyrin repeat protein; Provisional
120-350 4.54e-21

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 98.14  E-value: 4.54e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  120 NHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHNQAVAILLENDTKGKVRLPA----LHIAARKDDTKSAALLLQ-ND 194
Cdd:PHA02875    13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDieseLHDAVEEGDVKAVEELLDlGK 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  195 HNADVQSKmmvnrtteSGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAK 274
Cdd:PHA02875    93 FADDVFYK--------DGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIE 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  275 TRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNG-LSPLHMAAQGDHVECVKHLLQHKAPVDDVTL---DYLTALHV 350
Cdd:PHA02875   165 DCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNIMFMiegEECTILDM 244
PHA02876 PHA02876
ankyrin repeat protein; Provisional
482-780 6.78e-21

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 99.75  E-value: 6.78e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  482 IASRLGKTE--IVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAK 559
Cdd:PHA02876   149 IKERIQQDEllIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIK 228
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  560 LLLQRRAaadSAGKNGLTPLHVAAHYDnQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQM-QIASTLLNYGAETNIVT 638
Cdd:PHA02876   229 AIIDNRS---NINKNDLSLLKAIRNED-LETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKN 304
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  639 KQGVTPLHLASQEGH-TDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKvnvadiltkhgadqdahtklgytplivachy 717
Cdd:PHA02876   305 IKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDR------------------------------- 353
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1229385645  718 gNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTALAIA 780
Cdd:PHA02876   354 -NKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFA 415
PHA02878 PHA02878
ankyrin repeat protein; Provisional
314-582 8.46e-21

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 98.03  E-value: 8.46e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  314 PLHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLdkrANPNARAL-NGFTPLHIACKKNRIKV 392
Cdd:PHA02878    40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMI---RSINKCSVfYTLVAIKDAFNNRNVEI 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  393 ME-LLVKYGASIQAITESGLTPIHVAAFMgHLNIVLLLLQNGASPD-VTNIRGETALHMAARAGQVEVVRCLLRNGALVD 470
Cdd:PHA02878   117 FKiILTNRYKNIQTIDLVYIDKKSKDDII-EAEITKLLLSYGADINmKDRHKGNTALHYATENKDQRLTELLLSYGANVN 195
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  471 ARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHIS-AREGQVDVASVLLEAGAA-HSLATKKGFTPLHV 548
Cdd:PHA02878   196 IPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDvNAKSYILGLTALHS 275
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1229385645  549 AAKygSLDVAKLLLQRRAAADSAGKNGLTPLHVA 582
Cdd:PHA02878   276 SIK--SERKLKLLLEYGADINSLNSYKLTPLSSA 307
Ank_2 pfam12796
Ankyrin repeats (3 copies);
80-167 1.22e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 88.25  E-value: 1.22e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645   80 LHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENgaNQSTATEDGFTPLAVALQQGHNQAVA 159
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH--ADVNLKDNGRTALHYAARSGHLEIVK 78

                   ....*...
gi 1229385645  160 ILLENDTK 167
Cdd:pfam12796   79 LLLEKGAD 86
Ank_2 pfam12796
Ankyrin repeats (3 copies);
480-566 5.77e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.32  E-value: 5.77e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  480 LHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEagAAHSLATKKGFTPLHVAAKYGSLDVAK 559
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE--HADVNLKDNGRTALHYAARSGHLEIVK 78

                   ....*..
gi 1229385645  560 LLLQRRA 566
Cdd:pfam12796   79 LLLEKGA 85
PHA02878 PHA02878
ankyrin repeat protein; Provisional
378-648 5.88e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 95.33  E-value: 5.88e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  378 FTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNirGETALHMAARAGQVE 457
Cdd:PHA02878    38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFY--TLVAIKDAFNNRNVE 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  458 VVRCLLRNG-----ALVDARAREEQTPLHIasrlgKTEIVQLLLQHMAHPDAATTN-GYTPLHISAREGQVDVASVLLEA 531
Cdd:PHA02878   116 IFKIILTNRykniqTIDLVYIDKKSKDDII-----EAEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSY 190
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  532 GAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHY-DNQKVALLLLEKGASPHATAK-NGY 609
Cdd:PHA02878   191 GANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYiLGL 270
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1229385645  610 TPLHIAAKKNqmQIASTLLNYGAETNIVTKQGVTPLHLA 648
Cdd:PHA02878   271 TALHSSIKSE--RKLKLLLEYGADINSLNSYKLTPLSSA 307
PHA02875 PHA02875
ankyrin repeat protein; Provisional
83-302 6.35e-20

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 94.67  E-value: 6.35e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645   83 ASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHNQAVAILL 162
Cdd:PHA02875     9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  163 E-----NDTKGKVRLPALHIAARKDDTKSAALLLQNDHNADVQSKmmvnrtteSGFTPLHIAAHYGNVNVATLLLNRGAA 237
Cdd:PHA02875    89 DlgkfaDDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNT--------DKFSPLHLAVMMGDIKGIELLIDHKAC 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1229385645  238 VDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAA-RSGHDQVVELLLERGA 302
Cdd:PHA02875   161 LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAiENNKIDIVRLFIKRGA 226
PHA02874 PHA02874
ankyrin repeat protein; Provisional
22-254 6.62e-20

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 94.65  E-value: 6.62e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645   22 NLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGAN 101
Cdd:PHA02874   103 EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY 182
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  102 INAQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQqgHNQAVAILLENDTKgkvrlpalhiaark 181
Cdd:PHA02874   183 ANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNAS-------------- 246
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1229385645  182 ddtksaalllqndhnadvqskmmVNRTTESGFTPLHIAAHYG-NVNVATLLLNRGAAVDFTARNGITPLHVASK 254
Cdd:PHA02874   247 -----------------------INDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAFK 297
Ank_2 pfam12796
Ankyrin repeats (3 copies);
546-636 7.36e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.94  E-value: 7.36e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  546 LHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHATakNGYTPLHIAAKKNQMQIAS 625
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD--NGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|.
gi 1229385645  626 TLLNYGAETNI 636
Cdd:pfam12796   79 LLLEKGADINV 89
PHA02874 PHA02874
ankyrin repeat protein; Provisional
17-287 9.17e-20

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 94.26  E-value: 9.17e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645   17 AARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRG---------------------SSVDSATK- 74
Cdd:PHA02874    42 AIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGvdtsilpipciekdmiktildCGIDVNIKd 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645   75 -KGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPlavalqqg 153
Cdd:PHA02874   122 aELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESP-------- 193
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  154 hnqavaillendtkgkvrlpaLHIAARKDDTKSAALLLQNDHNADVQSKmmvnrtteSGFTPLHIAAHYgNVNVATLLLN 233
Cdd:PHA02874   194 ---------------------LHNAAEYGDYACIKLLIDHGNHIMNKCK--------NGFTPLHNAIIH-NRSAIELLIN 243
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1229385645  234 rGAAVDFTARNGITPLHVA-SKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAAR 287
Cdd:PHA02874   244 -NASINDQDIDGSTPLHHAiNPPCDIDIIDILLYHKADISIKDNKGENPIDTAFK 297
PHA02878 PHA02878
ankyrin repeat protein; Provisional
447-741 1.18e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 94.56  E-value: 1.18e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  447 LHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIA----SRLGKTEIVQLLLQhmahpdAATTNGYTPLHISAREGQV 522
Cdd:PHA02878    41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIIckepNKLGMKEMIRSINK------CSVFYTLVAIKDAFNNRNV 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  523 DVASVLLEAgaahslATKKGFTPLHVAAKYGSLD------VAKLLLQRRAAADSAGKNGL-TPLHVAAHYDNQKVALLLL 595
Cdd:PHA02878   115 EIFKIILTN------RYKNIQTIDLVYIDKKSKDdiieaeITKLLLSYGADINMKDRHKGnTALHYATENKDQRLTELLL 188
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  596 EKGASPHATAKNGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQE-GHTDMVTLLLDKGANIHM-STKS 673
Cdd:PHA02878   189 SYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAkSYIL 268
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1229385645  674 GLTSLHLAAQ-EDKVNvadILTKHGADQDAHTKLGYTPLIVAC------HYGNVKMVNFLLKQGANVNAKTKNGY 741
Cdd:PHA02878   269 GLTALHSSIKsERKLK---LLLEYGADINSLNSYKLTPLSSAVkqylciNIGRILISNICLLKRIKPDIKNSEGF 340
Ank_2 pfam12796
Ankyrin repeats (3 copies);
14-105 1.34e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.17  E-value: 1.34e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645   14 FLRAARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSvdSATKKGNTALHIASLAGQAEVVK 93
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|..
gi 1229385645   94 VLVKEGANINAQ 105
Cdd:pfam12796   79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
513-604 3.05e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.01  E-value: 3.05e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  513 LHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAgkNGLTPLHVAAHYDNQKVAL 592
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD--NGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|..
gi 1229385645  593 LLLEKGASPHAT 604
Cdd:pfam12796   79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
381-472 4.63e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 83.63  E-value: 4.63e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  381 LHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNirGETALHMAARAGQVEVVR 460
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN--GRTALHYAARSGHLEIVK 78
                           90
                   ....*....|..
gi 1229385645  461 CLLRNGALVDAR 472
Cdd:pfam12796   79 LLLEKGADINVK 90
Death cd01670
Death Domain: a protein-protein interaction domain; Death Domains (DDs) are protein-protein ...
1467-1544 8.82e-19

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: 82.33  E-value: 8.82e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1229385645 1467 LAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIVHLME 1544
Cdd:cd01670      2 FDLVAEELGRDWKKLARKLGLSEGDIDQIEEDNRDDLKEQAYQMLERWREREGDEATLGRLIQALREIGRRDLAEKLE 79
Ank_2 pfam12796
Ankyrin repeats (3 copies);
612-702 2.03e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 81.70  E-value: 2.03e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  612 LHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLDKgANIHMSTKsGLTSLHLAAQEDKVNVAD 691
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
                           90
                   ....*....|.
gi 1229385645  692 ILTKHGADQDA 702
Cdd:pfam12796   79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
175-274 3.94e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.93  E-value: 3.94e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  175 LHIAARKDDTKSAALLLQNDHNADVQSKmmvnrtteSGFTPLHIAAHYGNVNVATLLLNRGAAVDFTarNGITPLHVASK 254
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDK--------NGRTALHLAAKNGHLEIVKLLLEHADVNLKD--NGRTALHYAAR 70
                           90       100
                   ....*....|....*....|
gi 1229385645  255 RGNTNMVKLLLDRGGQIDAK 274
Cdd:pfam12796   71 SGHLEIVKLLLEKGADINVK 90
PHA02876 PHA02876
ankyrin repeat protein; Provisional
586-792 7.84e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 89.74  E-value: 7.84e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  586 DNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLDKGA 665
Cdd:PHA02876   156 DELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRS 235
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  666 NIHmstKSGLTSLHLAAQEDkVNVADILTKHGADQDAHTKLGYTPLIVACHYGNV-KMVNFLLKQGANVNAKTKNGYTPL 744
Cdd:PHA02876   236 NIN---KNDLSLLKAIRNED-LETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPL 311
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1229385645  745 HQAAQQGH-THIINVLLQHGAKPNATTANGNTALAIAKRLG-YISVVDTL 792
Cdd:PHA02876   312 YLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITL 361
PHA02875 PHA02875
ankyrin repeat protein; Provisional
21-268 3.04e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 86.20  E-value: 3.04e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645   21 GNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGA 100
Cdd:PHA02875    13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  101 NIN-AQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPlavalqqghnqavaillendtkgkvrlpaLHIAA 179
Cdd:PHA02875    93 FADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSP-----------------------------LHLAV 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  180 RKDDTKSAALLLqnDHNAdvqskmMVNRTTESGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNG-ITPLHVASKRGNT 258
Cdd:PHA02875   144 MMGDIKGIELLI--DHKA------CLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKI 215
                          250
                   ....*....|
gi 1229385645  259 NMVKLLLDRG 268
Cdd:PHA02875   216 DIVRLFIKRG 225
Ank_2 pfam12796
Ankyrin repeats (3 copies);
711-792 3.95e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.23  E-value: 3.95e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  711 LIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHgAKPNATTaNGNTALAIAKRLGYISVVD 790
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                   ..
gi 1229385645  791 TL 792
Cdd:pfam12796   79 LL 80
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
534-728 3.81e-16

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 84.29  E-value: 3.81e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  534 AHSLATKKGF-TPLHVAAKYGSLD-VAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEkgASPH-----ATAK 606
Cdd:cd22192      8 LHLLQQKRISeSPLLLAAKENDVQaIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPElvnepMTSD 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  607 --NGYTPLHIAAKKNQMQIASTLLNYGAEtniVTKQGVT-----------------PLHLASQEGHTDMVTLLLDKGANI 667
Cdd:cd22192     86 lyQGETALHIAVVNQNLNLVRELIARGAD---VVSPRATgtffrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADI 162
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1229385645  668 HMSTKSGLTSLH-LAAQEDKV---NVADILTKHGADQDAHT------KLGYTPLIVACHYGNVKMVNFLLK 728
Cdd:cd22192    163 RAQDSLGNTVLHiLVLQPNKTfacQMYDLILSYDKEDDLQPldlvpnNQGLTPFKLAAKEGNIVMFQHLVQ 233
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
474-663 1.45e-15

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: 82.37  E-value: 1.45e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  474 REEQTPLHIASRLGKTEIVQ-LLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAgaAHSLATK-------KGFTP 545
Cdd:cd22192     15 RISESPLLLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEA--APELVNEpmtsdlyQGETA 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  546 LHVAAKYGSLDVAKLLLQRRAAADSA---------GKNGLT-----PLHVAAHYDNQKVALLLLEKGASPHATAKNGYTP 611
Cdd:cd22192     93 LHIAVVNQNLNLVRELIARGADVVSPratgtffrpGPKNLIyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTV 172
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1229385645  612 LHI----AAKKNQMQIASTLLNYGAETNIVT------KQGVTPLHLASQEGHTDMVTLLLDK 663
Cdd:cd22192    173 LHIlvlqPNKTFACQMYDLILSYDKEDDLQPldlvpnNQGLTPFKLAAKEGNIVMFQHLVQK 234
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
379-565 3.67e-15

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: 81.21  E-value: 3.67e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  379 TPLHIACKKNRIKVMELLVKY-GASIQAITESGLTPIHVAAFMGHLNIVLLLLQngASPDVTNI-------RGETALHMA 450
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNEpmtsdlyQGETALHIA 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  451 ARAGQVEVVRCLLRNGA-LVDARA-----REEQT--------PLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHIS 516
Cdd:cd22192     97 VVNQNLNLVRELIARGAdVVSPRAtgtffRPGPKnliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHIL 176
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1229385645  517 AREGQVDVA----SVLLEA---GAAHSLAT---KKGFTPLHVAAKYGSLDVAKLLLQRR 565
Cdd:cd22192    177 VLQPNKTFAcqmyDLILSYdkeDDLQPLDLvpnNQGLTPFKLAAKEGNIVMFQHLVQKR 235
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
144-334 1.03e-14

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 79.67  E-value: 1.03e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  144 TPLAVALQQGHNQAVAILLENDT-----KGKVRLPALHIAARKDDTKSAALLLQNDH---NADVQSKMMVnrttesGFTP 215
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLLKCPScdlfqRGALGETALHVAALYDNLEAAVVLMEAAPelvNEPMTSDLYQ------GETA 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  216 LHIAAHYGNVNVATLLLNRGAAVdFTARN---------------GITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLT 280
Cdd:cd22192     93 LHIAVVNQNLNLVRELIARGADV-VSPRAtgtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNT 171
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1229385645  281 PLHC----AARSGHDQVVELLL-----ERGAPL-LARTKNGLSPLHMAAQGDHVECVKHLLQHK 334
Cdd:cd22192    172 VLHIlvlqPNKTFACQMYDLILsydkeDDLQPLdLVPNNQGLTPFKLAAKEGNIVMFQHLVQKR 235
PHA02875 PHA02875
ankyrin repeat protein; Provisional
619-792 1.80e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 77.72  E-value: 1.80e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  619 NQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADILTKHGA 698
Cdd:PHA02875    13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  699 -DQDAHTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTAL 777
Cdd:PHA02875    93 fADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPL 172
                          170
                   ....*....|....*
gi 1229385645  778 AIAKRLGYISVVDTL 792
Cdd:PHA02875   173 IIAMAKGDIAICKML 187
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
171-398 3.00e-14

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 78.13  E-value: 3.00e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  171 RLPALHIAARKDDTKSaaLLLQNDHNADVQS--KMMVNRTTES------GFTPLHIAAHYGNVNVATLLL-------NRG 235
Cdd:cd22192      4 MLDELHLLQQKRISES--PLLLAAKENDVQAikKLLKCPSCDLfqrgalGETALHVAALYDNLEAAVVLMeaapelvNEP 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  236 AAVDFTArnGITPLHVASKRGNTNMVKLLLDRGGQIDA---------KTRDGLT-----PLHCAARSGHDQVVELLLERG 301
Cdd:cd22192     82 MTSDLYQ--GETALHIAVVNQNLNLVRELIARGADVVSpratgtffrPGPKNLIyygehPLSFAACVGNEEIVRLLIEHG 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  302 APLLARTKNGLSPLHMAAQGDHVECVKH----LLQHKAPVDDVTLDYLtalhvaahcghyrvtkllldkranPNARalnG 377
Cdd:cd22192    160 ADIRAQDSLGNTVLHILVLQPNKTFACQmydlILSYDKEDDLQPLDLV------------------------PNNQ---G 212
                          250       260
                   ....*....|....*....|.
gi 1229385645  378 FTPLHIACKKNRIKVMELLVK 398
Cdd:cd22192    213 LTPFKLAAKEGNIVMFQHLVQ 233
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
627-764 1.24e-13

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 76.45  E-value: 1.24e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  627 LLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADILTKHGADQDAHTkl 706
Cdd:PLN03192   544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHA-- 621
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1229385645  707 GYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGA 764
Cdd:PLN03192   622 AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGA 679
Ank_4 pfam13637
Ankyrin repeats (many copies);
410-463 2.66e-13

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 65.76  E-value: 2.66e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1229385645  410 GLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLL 463
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
543-793 5.23e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 73.76  E-value: 5.23e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  543 FTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDN-QKVALLLLEKGaspHATAKNGYTPLHIAAKKNQM 621
Cdd:PHA02878    38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNkLGMKEMIRSIN---KCSVFYTLVAIKDAFNNRNV 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  622 QIASTLL--NYGAETNIVTKQGVTPLHLASQEghTDMVTLLLDKGANIHMSTK-SGLTSLHLAAqEDKvnvadiltkhga 698
Cdd:PHA02878   115 EIFKIILtnRYKNIQTIDLVYIDKKSKDDIIE--AEITKLLLSYGADINMKDRhKGNTALHYAT-ENK------------ 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  699 dqdahtklgytplivachygNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTALA 778
Cdd:PHA02878   180 --------------------DQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLH 239
                          250
                   ....*....|....*
gi 1229385645  779 IAkrLGYISVVDTLK 793
Cdd:PHA02878   240 IS--VGYCKDYDILK 252
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
270-518 1.21e-12

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: 73.19  E-value: 1.21e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  270 QIDAKTRDGLTPLHCAA-RSGHDQVVELLLERGAplLARTknGLSPLHMAAQGdHVECVKHLLQH--KAPVDDVTLDYL- 345
Cdd:TIGR00870   44 NINCPDRLGRSALFVAAiENENLELTELLLNLSC--RGAV--GDTLLHAISLE-YVDAVEAILLHllAAFRKSGPLELAn 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  346 -----------TALHVAAHCGHYRVTKLLLDKRANPNARALNGFtplhiaCKKnriKVMELLVKYGASiqaitesgltPI 414
Cdd:TIGR00870  119 dqytseftpgiTALHLAAHRQNYEIVKLLLERGASVPARACGDF------FVK---SQGVDSFYHGES----------PL 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  415 HVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAA----RAGQVEVVRCLLRNGAL-VDARAREEQ-----------T 478
Cdd:TIGR00870  180 NAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVmeneFKAEYEELSCQMYNFALsLLDKLRDSKelevilnhqglT 259
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1229385645  479 PLHIASRLGKTEIVQLLLQ-------HMAHPdaattngYTPLHISAR 518
Cdd:TIGR00870  260 PLKLAAKEGRIVLFRLKLAikykqkkFVAWP-------NGQQLLSLY 299
PHA02798 PHA02798
ankyrin-like protein; Provisional
551-770 1.39e-12

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 72.17  E-value: 1.39e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  551 KYGS-LDVAKLLLQRRAAADSAGKNGLTPLHVAAH---YDNQKVALLLLEKGASPHATAKNGYTPLHIAAKKN---QMQI 623
Cdd:PHA02798    84 DYKHmLDIVKILIENGADINKKNSDGETPLYCLLSngyINNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNhhiDIEI 163
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  624 ASTLLNYGAETNIVT-KQGVTPLHLASQEGHT----DMVTLLLDKGANIHMSTKSG-------LTSLHLAAQEDKVNVAD 691
Cdd:PHA02798   164 IKLLLEKGVDINTHNnKEKYDTLHCYFKYNIDridaDILKLFVDNGFIINKENKSHkkkfmeyLNSLLYDNKRFKKNILD 243
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1229385645  692 ILTKHgADQDAHTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHgaKPNATT 770
Cdd:PHA02798   244 FIFSY-IDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNK--KPNKNT 319
PHA02798 PHA02798
ankyrin-like protein; Provisional
554-780 2.19e-12

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 71.79  E-value: 2.19e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  554 SLDVAKLLLQRRAAADSAGKNGLTPL-----HVAAHYDNQKVALLLLEKGASPHATAKNGYTPLHIAAKK---NQMQIAS 625
Cdd:PHA02798    50 STDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNgyiNNLEILL 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  626 TLLNYGAETNIVTKQGVTPLHLASQEGHT---DMVTLLLDKGANIHM-STKSGLTSLHLAAQED----KVNVADILTKHG 697
Cdd:PHA02798   130 FMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDINThNNKEKYDTLHCYFKYNidriDADILKLFVDNG 209
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  698 ---ADQDAHTKLGYTPLIVACHYGNVK----MVNFLLKQgANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATT 770
Cdd:PHA02798   210 fiiNKENKSHKKKFMEYLNSLLYDNKRfkknILDFIFSY-IDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIIT 288
                          250
                   ....*....|
gi 1229385645  771 ANGNTALAIA 780
Cdd:PHA02798   289 ELGNTCLFTA 298
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
304-497 3.06e-12

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: 71.58  E-value: 3.06e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  304 LLARTKNGLSPLHMAAQGDHVECVKHLLQHKApVDDVTLDYL--TALHVAAHCGHYRVTKLLLDkranpNARAL------ 375
Cdd:cd22192     10 LLQQKRISESPLLLAAKENDVQAIKKLLKCPS-CDLFQRGALgeTALHVAALYDNLEAAVVLME-----AAPELvnepmt 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  376 ----NGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLT--------------PIHVAAFMGHLNIVLLLLQNGASPD 437
Cdd:cd22192     84 sdlyQGETALHIAVVNQNLNLVRELIARGADVVSPRATGTFfrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIR 163
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1229385645  438 VTNIRGETALHMAARAGQVEVVrCLLRNGAL-VDARAREEQ----------TPLHIASRLGKTEIVQLLLQ 497
Cdd:cd22192    164 AQDSLGNTVLHILVLQPNKTFA-CQMYDLILsYDKEDDLQPldlvpnnqglTPFKLAAKEGNIVMFQHLVQ 233
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
12-146 3.61e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 71.82  E-value: 3.61e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645   12 ASFLRAARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTAL----------- 80
Cdd:PLN03192   527 SNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnaisakhhki 606
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645   81 -----HIASLA---------------GQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTA-T 139
Cdd:PLN03192   607 frilyHFASISdphaagdllctaakrNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAnT 686

                   ....*..
gi 1229385645  140 EDGFTPL 146
Cdd:PLN03192   687 DDDFSPT 693
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
50-164 7.00e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 70.67  E-value: 7.00e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645   50 AAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLY--------------- 114
Cdd:PLN03192   532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWnaisakhhkifrily 611
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1229385645  115 ----------------MAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHNQAVAILLEN 164
Cdd:PLN03192   612 hfasisdphaagdllcTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMN 677
PHA02876 PHA02876
ankyrin repeat protein; Provisional
22-162 1.13e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 70.09  E-value: 1.13e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645   22 NLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIAsLAGQAEV--VKVLVKEG 99
Cdd:PHA02876   354 NKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFA-LCGTNPYmsVKTLIDRG 432
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1229385645  100 ANINAQSQNGFTPLYMAAQEN-HIDVVKYLLENGANQSTATEDGFTPLAVALqqGHNQAVAILL 162
Cdd:PHA02876   433 ANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILL 494
Ank_4 pfam13637
Ankyrin repeats (many copies);
278-331 2.73e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 60.37  E-value: 2.73e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1229385645  278 GLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLL 331
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
75-234 3.09e-11

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: 68.63  E-value: 3.09e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645   75 KGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGF--------------TPLYMAAQENHIDVVKYLLENGANQSTAte 140
Cdd:cd22194    140 EGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVFfnpkykhegfyfgeTPLALAACTNQPEIVQLLMEKESTDITS-- 217
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  141 dgftplavalqqghnqavailleNDTKGKVRLPALHIAArkDDTKSaalllQNDHNADVQSKMMVNRTTES--------G 212
Cdd:cd22194    218 -----------------------QDSRGNTVLHALVTVA--EDSKT-----QNDFVKRMYDMILLKSENKNletirnneG 267
                          170       180
                   ....*....|....*....|..
gi 1229385645  213 FTPLHIAAHYGNVNVATLLLNR 234
Cdd:cd22194    268 LTPLQLAAKMGKAEILKYILSR 289
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
104-397 4.32e-11

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: 68.18  E-value: 4.32e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  104 AQSQNGFTPlymAAQENHIDVVKYLLENGA--NQSTATEDGFTPLAVALQQGHNQAVAILLEN-DTKGKVRLPALHIAA- 179
Cdd:TIGR00870   15 SDEEKAFLP---AAERGDLASVYRDLEEPKklNINCPDRLGRSALFVAAIENENLELTELLLNlSCRGAVGDTLLHAISl 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  180 RKDDTKSAALLLQNDHNADVQSKMMVNRTTESGF----TPLHIAAHYGNVNVATLLLNRGAAVDFTArNGitplhVASKR 255
Cdd:TIGR00870   92 EYVDAVEAILLHLLAAFRKSGPLELANDQYTSEFtpgiTALHLAAHRQNYEIVKLLLERGASVPARA-CG-----DFFVK 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  256 gnTNMVKLLldrggqidaktRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMAAqgdhvecvkhlLQHKA 335
Cdd:TIGR00870  166 --SQGVDSF-----------YHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLV-----------MENEF 221
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1229385645  336 PVDDVTLD---YLTALHVAAHCGHYRVTKLLLDkranpnaraLNGFTPLHIACKKNRIKVMELLV 397
Cdd:TIGR00870  222 KAEYEELScqmYNFALSLLDKLRDSKELEVILN---------HQGLTPLKLAAKEGRIVLFRLKL 277
Ank_4 pfam13637
Ankyrin repeats (many copies);
247-298 5.40e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.21  E-value: 5.40e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1229385645  247 TPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLL 298
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02798 PHA02798
ankyrin-like protein; Provisional
25-267 5.43e-11

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 67.17  E-value: 5.43e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645   25 KVVEYLKGGIDIN-TCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTAL-----HIASLAGQAEVVKVLVKE 98
Cdd:PHA02798    19 STVKLLIKSCNPNeIVNEYSIFQKYLQRDSPSTDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIEN 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645   99 GANINAQSQNGFTPLYMAAQE---NHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHN---QAVAILLE-----NDTK 167
Cdd:PHA02798    99 GADINKKNSDGETPLYCLLSNgyiNNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEkgvdiNTHN 178
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  168 GKVRLPALHIAARKD----DTKSAALLLQN-----DHNADVQSKMM--------------------------VNRTTESG 212
Cdd:PHA02798   179 NKEKYDTLHCYFKYNidriDADILKLFVDNgfiinKENKSHKKKFMeylnsllydnkrfkknildfifsyidINQVDELG 258
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1229385645  213 FTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDR 267
Cdd:PHA02798   259 FNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNK 313
Ank_4 pfam13637
Ankyrin repeats (many copies);
311-364 7.76e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.83  E-value: 7.76e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1229385645  311 GLSPLHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLL 364
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
17-163 9.80e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 66.17  E-value: 9.80e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645   17 AARAGNLDKVVEYLKGGIDIN-TCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVL 95
Cdd:PHA02875    75 AVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELL 154
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1229385645   96 VKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTATEDG-FTPLAVALQQGHNQAVAILLE 163
Cdd:PHA02875   155 IDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIK 223
Ank_4 pfam13637
Ankyrin repeats (many copies);
379-430 1.07e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.44  E-value: 1.07e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1229385645  379 TPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLL 430
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
76-129 1.27e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.44  E-value: 1.27e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1229385645   76 GNTALHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLL 129
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
707-760 1.34e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.44  E-value: 1.34e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1229385645  707 GYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLL 760
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
344-397 1.51e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.05  E-value: 1.51e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1229385645  344 YLTALHVAAHCGHYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLV 397
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
58-265 1.73e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 65.67  E-value: 1.73e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645   58 LVQELLGRGSSVDSATK-KGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGANQS 136
Cdd:PHA02878   149 ITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTD 228
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  137 TATEDGFTPLAVALQQGHNQAV-AILLEndtkgkvrlpalhiaarkddtksaalllqndHNADVQSKmmvnrTTESGFTP 215
Cdd:PHA02878   229 ARDKCGNTPLHISVGYCKDYDIlKLLLE-------------------------------HGVDVNAK-----SYILGLTA 272
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1229385645  216 LHIAAHygNVNVATLLLNRGAAVDFTARNGITPLHVASK-RGNTNMVKLLL 265
Cdd:PHA02878   273 LHSSIK--SERKLKLLLEYGADINSLNSYKLTPLSSAVKqYLCINIGRILI 321
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
440-564 1.78e-10

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: 65.94  E-value: 1.78e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  440 NIRGETALHMAARAGQVEVVRCLLRNGALVDARA---------REE-----QTPLHIASRLGKTEIVQLLLQHMAHPDAA 505
Cdd:cd22194    138 AYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAkgvffnpkyKHEgfyfgETPLALAACTNQPEIVQLLMEKESTDITS 217
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1229385645  506 T-TNGYTPLH---ISAREGQVDVASV------LLEAGAAHSLAT---KKGFTPLHVAAKYGSLDVAKLLLQR 564
Cdd:cd22194    218 QdSRGNTVLHalvTVAEDSKTQNDFVkrmydmILLKSENKNLETirnNEGLTPLQLAAKMGKAEILKYILSR 289
PHA02878 PHA02878
ankyrin repeat protein; Provisional
33-163 2.07e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 65.29  E-value: 2.07e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645   33 GIDINTCNQNGLN-ALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGFT 111
Cdd:PHA02878   157 GADINMKDRHKGNtALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNT 236
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1229385645  112 PLYMAAQE-NHIDVVKYLLENGAN-QSTATEDGFTPLAVALQQghNQAVAILLE 163
Cdd:PHA02878   237 PLHISVGYcKDYDILKLLLEHGVDvNAKSYILGLTALHSSIKS--ERKLKLLLE 288
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
320-546 2.20e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 66.04  E-value: 2.20e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  320 QGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHcghyrvtkllldkrANPNAralnGFTPLHIACKKNRiKVMELLVKY 399
Cdd:PLN03192   487 QEDNVVILKNFLQHHKELHDLNVGDLLGDNGGEH--------------DDPNM----ASNLLTVASTGNA-ALLEELLKA 547
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  400 GASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQtp 479
Cdd:PLN03192   548 KLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAGDL-- 625
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1229385645  480 LHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLA-TKKGFTPL 546
Cdd:PLN03192   626 LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAnTDDDFSPT 693
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
528-680 2.89e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 65.66  E-value: 2.89e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  528 LLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLL--LEKGASPHAta 605
Cdd:PLN03192   544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILyhFASISDPHA-- 621
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1229385645  606 knGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLDKGANI-HMSTKSGLTSLHL 680
Cdd:PLN03192   622 --AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVdKANTDDDFSPTEL 695
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
428-509 8.51e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 63.76  E-value: 8.51e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  428 LLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATT 507
Cdd:PTZ00322   100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGA 179

                   ..
gi 1229385645  508 NG 509
Cdd:PTZ00322   180 NA 181
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
366-565 8.69e-10

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 63.95  E-value: 8.69e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  366 KRANPNARALN-------GFTPLHIACKKNRIK-VMELLVKYGASIqaitESGLTPIHVAAFMGHLN---IVLLLLQNGA 434
Cdd:TIGR00870   34 YRDLEEPKKLNincpdrlGRSALFVAAIENENLeLTELLLNLSCRG----AVGDTLLHAISLEYVDAveaILLHLLAAFR 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  435 SPDVTNI----------RGETALHMAARAGQVEVVRCLLRNGALVDARA--------------REEQTPLHIASRLGKTE 490
Cdd:TIGR00870  110 KSGPLELandqytseftPGITALHLAAHRQNYEIVKLLLERGASVPARAcgdffvksqgvdsfYHGESPLNAAACLGSPS 189
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  491 IVQLLLQHMAHPDAATTNGYTPLHISAREG-----------QVDVASVLLEAGAAHSLATK-----KGFTPLHVAAKYGS 554
Cdd:TIGR00870  190 IVALLSEDPADILTADSLGNTLLHLLVMENefkaeyeelscQMYNFALSLLDKLRDSKELEvilnhQGLTPLKLAAKEGR 269
                          250
                   ....*....|.
gi 1229385645  555 LDVAKLLLQRR 565
Cdd:TIGR00870  270 IVLFRLKLAIK 280
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
417-571 8.85e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 63.73  E-value: 8.85e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  417 AAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQlLL 496
Cdd:PLN03192   532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR-IL 610
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1229385645  497 QHMAHPDAATTNGyTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSA 571
Cdd:PLN03192   611 YHFASISDPHAAG-DLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKA 684
Ank_4 pfam13637
Ankyrin repeats (many copies);
575-628 9.04e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.74  E-value: 9.04e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1229385645  575 GLTPLHVAAHYDNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQMQIASTLL 628
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02946 PHA02946
ankyin-like protein; Provisional
546-760 1.30e-09

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 62.76  E-value: 1.30e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  546 LHVAAKYGS--LDVAKLLLQrraAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQMQI 623
Cdd:PHA02946    11 LSLYAKYNSknLDVFRNMLQ---AIEPSGNYHILHAYCGIKGLDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRI 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  624 ASTLLNYGAETNIVTKQGVTPLHLAS--QEGHTDMVTLLLDKGANIHMST-KSGLTSL---------------------- 678
Cdd:PHA02946    88 VAMLLTHGADPNACDKQHKTPLYYLSgtDDEVIERINLLVQYGAKINNSVdEEGCGPLlactdpservfkkimsigfear 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  679 ------------HLAAQEDKVNVADILTKHGADQDAHTKLGYTPLIVACH--YGNVKMVNFLLKQgANVNAKTKNGYTPL 744
Cdd:PHA02946   168 ivdkfgknhihrHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCSktVKNVDIINLLLPS-TDVNKQNKFGDSPL 246
                          250
                   ....*....|....*..
gi 1229385645  745 HQAAQQ-GHTHIINVLL 760
Cdd:PHA02946   247 TLLIKTlSPAHLINKLL 263
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
487-575 1.37e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 62.99  E-value: 1.37e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  487 GKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRA 566
Cdd:PTZ00322    93 GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQ 172

                   ....*....
gi 1229385645  567 AADSAGKNG 575
Cdd:PTZ00322   173 CHFELGANA 181
PHA02875 PHA02875
ankyrin repeat protein; Provisional
9-139 2.10e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.93  E-value: 2.10e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645    9 DSNASFLRAARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQ 88
Cdd:PHA02875   101 DGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGD 180
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1229385645   89 AEVVKVLVKEGANINAQSQNG-FTPLYMAAQENHIDVVKYLLENGANQSTAT 139
Cdd:PHA02875   181 IAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNIMF 232
Ank_4 pfam13637
Ankyrin repeats (many copies);
608-661 3.29e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.20  E-value: 3.29e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1229385645  608 GYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLL 661
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02946 PHA02946
ankyin-like protein; Provisional
479-727 3.50e-09

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 61.22  E-value: 3.50e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  479 PLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPL-HISAREGQV-DVASVLLEAGAA-HSLATKKGFTPLhVAAKYGSL 555
Cdd:PHA02946    75 PLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLyYLSGTDDEViERINLLVQYGAKiNNSVDEEGCGPL-LACTDPSE 153
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  556 DVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALL--LLEKGASPHATAKNGYTPLHIAAKKNQMQI-ASTLLNYGA 632
Cdd:PHA02946   154 RVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNPKASTIswMMKLGISPSKPDHDGNTPLHIVCSKTVKNVdIINLLLPST 233
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  633 ETNIVTKQGVTPLHLASQeghtdmvTLLLDKGANIHMSTKSGLT--SLHLAAQEDKVNVADILTKHGADQDAhtklgyTP 710
Cdd:PHA02946   234 DVNKQNKFGDSPLTLLIK-------TLSPAHLINKLLSTSNVITdqTVNICIFYDRDDVLEIINDKGKQYDS------TD 300
                          250
                   ....*....|....*..
gi 1229385645  711 LIVACHYGNVKMVNFLL 727
Cdd:PHA02946   301 FKMAVEVGSIRCVKYLL 317
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
643-779 3.54e-09

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 61.57  E-value: 3.54e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  643 TPLHLASQEGHTDMV-TLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADILTkhgadqDAHTKL-----------GYTP 710
Cdd:cd22192     19 SPLLLAAKENDVQAIkKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLM------EAAPELvnepmtsdlyqGETA 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  711 LIVACHYGNVKMVNFLLKQGANVNAKTKNGYT--------------PLHQAAQQGHTHIINVLLQHGAKPNATTANGNTA 776
Cdd:cd22192     93 LHIAVVNQNLNLVRELIARGADVVSPRATGTFfrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTV 172

                   ...
gi 1229385645  777 LAI 779
Cdd:cd22192    173 LHI 175
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
408-564 3.96e-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: 61.43  E-value: 3.96e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  408 ESGLTPIHVAAF---MGHLNIVLLLLQngASPDVTNIR-------------GETALHMAARAGQVEVVRCLLRNGALVDA 471
Cdd:cd21882     24 ATGKTCLHKAALnlnDGVNEAIMLLLE--AAPDSGNPKelvnapctdefyqGQTALHIAIENRNLNLVRLLVENGADVSA 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  472 RA-----REEQT--------PLHIASRLGKTEIVQLLLQHMAHPDAATTN---GYTPLHI------SAREGQVDVASV-- 527
Cdd:cd21882    102 RAtgrffRKSPGnlfyfgelPLSLAACTNQEEIVRLLLENGAQPAALEAQdslGNTVLHAlvlqadNTPENSAFVCQMyn 181
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1229385645  528 -LLEAGAA-------HSLATKKGFTPLHVAAKYGSLDVAKLLLQR 564
Cdd:cd21882    182 lLLSYGAHldptqqlEEIPNHQGLTPLKLAAVEGKIVMFQHILQR 226
Ank_4 pfam13637
Ankyrin repeats (many copies);
214-265 4.72e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.82  E-value: 4.72e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1229385645  214 TPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLL 265
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
486-672 5.82e-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: 5.82e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  486 LGKTEIVQLLLQHMAHPDAATtnGYTPLHISA---REGQVDVASVLLEA----GAAHSLATK-------KGFTPLHVAAK 551
Cdd:cd21882      5 LGLLECLRWYLTDSAYQRGAT--GKTCLHKAAlnlNDGVNEAIMLLLEAapdsGNPKELVNApctdefyQGQTALHIAIE 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  552 YGSLDVAKLLLQRRAAADSAGKN-------------GLTPLHVAAHYDNQKVALLLLEKGASPHATAKN---GYTPLHI- 614
Cdd:cd21882     83 NRNLNLVRLLVENGADVSARATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPAALEAQdslGNTVLHAl 162
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1229385645  615 --------AAKKNQMQIASTLLNYGAETN-------IVTKQGVTPLHLASQEGHTDMVTLLLDK---GANIHMSTK 672
Cdd:cd21882    163 vlqadntpENSAFVCQMYNLLLSYGAHLDptqqleeIPNHQGLTPLKLAAVEGKIVMFQHILQRefsGPYQPLSRK 238
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
25-441 6.35e-09

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 61.08  E-value: 6.35e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645   25 KVVEYL--KGGIDIN-TCNQNGLNALHlaakeghvglvqellgrgssvdsaTKKGNTALHIaslagqaEVVKVLVKEGAN 101
Cdd:PHA02716   156 DLIKYMvdVGIVNLNyVCKKTGYGILH------------------------AYLGNMYVDI-------DILEWLCNNGVN 204
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  102 INAQSQNGFTPL--YMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHN---QAVAILLENDTKGKVR-LPA- 174
Cdd:PHA02716   205 VNLQNNHLITPLhtYLITGNVCASVIKKIIELGGDMDMKCVNGMSPIMTYIINIDNinpEITNIYIESLDGNKVKnIPMi 284
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  175 LHI---AARKDDTKSAALLLQNDhnadvqskMMVNRTTESGFTPLH--IAAHYGNVNVATLLLNRGAAVDFTARNGITPL 249
Cdd:PHA02716   285 LHSyitLARNIDISVVYSFLQPG--------VKLHYKDSAGRTCLHqyILRHNISTDIIKLLHEYGNDLNEPDNIGNTVL 356
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  250 HVASKRG--------------NTNMVKLLLDRGGQIDAKTRDGLTPLH---CAARS--GHDQVVELLLERgapLLARTKN 310
Cdd:PHA02716   357 HTYLSMLsvvnildpetdndiRLDVIQCLISLGADITAVNCLGYTPLTsyiCTAQNymYYDIIDCLISDK---VLNMVKH 433
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  311 GLSPLHMAAQGDHVECVKHLL-QHKAPVDDVTLDY----LTALHVAAHCGhyrvtkllLDKRANPNARALNGFTPLHIA- 384
Cdd:PHA02716   434 RILQDLLIRVDDTPCIIHHIIaKYNIPTDLYTDEYepydSTKIHDVYHCA--------IIERYNNAVCETSGMTPLHVSi 505
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1229385645  385 CKKNRIKVMELLVKY----GASIQAITESGLTPIHVA----AFMGH-LNIVLLLLQNgaSPDVTNI 441
Cdd:PHA02716   506 ISHTNANIVMDSFVYllsiQYNINIPTKNGVTPLMLTmrnnRLSGHqWYIVKNILDK--RPNVDIV 569
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
43-153 7.07e-09

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 60.80  E-value: 7.07e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645   43 GLNALHLAAKEGHVGLVQELLGRGSSVDS--AT----KKGNTAL-----HIASLA---GQAEVVKVLVKEGANINAQSQN 108
Cdd:cd22192     89 GETALHIAVVNQNLNLVRELIARGADVVSprATgtffRPGPKNLiyygeHPLSFAacvGNEEIVRLLIEHGADIRAQDSL 168
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1229385645  109 GFTPLYM-AAQENH------IDVVKYLLENGANQSTAT---EDGFTPLAVALQQG 153
Cdd:cd22192    169 GNTVLHIlVLQPNKtfacqmYDLILSYDKEDDLQPLDLvpnNQGLTPFKLAAKEG 223
Ank_4 pfam13637
Ankyrin repeats (many copies);
43-96 7.34e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.43  E-value: 7.34e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1229385645   43 GLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLV 96
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
442-564 9.17e-09

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: 60.59  E-value: 9.17e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  442 RGETALHMAARAGQVEVVRCLLRNGALVDARAREE--------------QTPLHIASRLGKTEIVQLLLQHMAHP---DA 504
Cdd:cd22196     93 KGQTALHIAIERRNMHLVELLVQNGADVHARASGEffkkkkggpgfyfgELPLSLAACTNQLDIVKFLLENPHSPadiSA 172
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1229385645  505 ATTNGYTPLHI---SAREGQVDVASV------LLEAGAA-------HSLATKKGFTPLHVAAKYGSLDVAKLLLQR 564
Cdd:cd22196    173 RDSMGNTVLHAlveVADNTPENTKFVtkmyneILILGAKirpllklEEITNKKGLTPLKLAAKTGKIGIFAYILGR 248
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
346-516 1.21e-08

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 59.89  E-value: 1.21e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  346 TALHVAA---HCGHYRVTKLLLD---KRANP----NARALN----GFTPLHIACKKNRIKVMELLVKYGASIQAITES-- 409
Cdd:cd21882     28 TCLHKAAlnlNDGVNEAIMLLLEaapDSGNPkelvNAPCTDefyqGQTALHIAIENRNLNLVRLLVENGADVSARATGrf 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  410 -----------GLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIR---GETALH----MAARAGQVEVVRCLLRNGALV-D 470
Cdd:cd21882    108 frkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPAALEAQdslGNTVLHalvlQADNTPENSAFVCQMYNLLLSyG 187
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1229385645  471 ARAREEQ-----------TPLHIASRLGKTEIVQLLLQHMAHPDAA------TTNGYTPLHIS 516
Cdd:cd21882    188 AHLDPTQqleeipnhqglTPLKLAAVEGKIVMFQHILQREFSGPYQplsrkfTEWTYGPVTSS 250
Ank_4 pfam13637
Ankyrin repeats (many copies);
478-529 1.23e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.66  E-value: 1.23e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1229385645  478 TPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLL 529
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Death_FADD cd08306
Fas-associated Death Domain protein-protein interaction domain; Death domain (DD) found in ...
1470-1540 1.47e-08

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: 53.45  E-value: 1.47e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1229385645 1470 IADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKInRMDIV 1540
Cdd:cd08306      8 ICENLGRDWRQLARKLGLSETKIESISEAHPRNLREQVRQSLREWKKIKKAEATVADLIKALRDC-QLNLV 77
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
166-332 1.47e-08

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 59.51  E-value: 1.47e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  166 TKGKVRLPALHIAARKDDT---KSAALLLQNDHNADVQSKMMVNRTTES---GFTPLHIAAHYGNVNVATLLLNRGAAVD 239
Cdd:cd21882     21 QRGATGKTCLHKAALNLNDgvnEAIMLLLEAAPDSGNPKELVNAPCTDEfyqGQTALHIAIENRNLNLVRLLVENGADVS 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  240 FTA---------RNGI----TPLHVASKRGNTNMVKLLLDRGGQI-DAKTRDGL--TPLHC----AARSGHD-----QVV 294
Cdd:cd21882    101 ARAtgrffrkspGNLFyfgeLPLSLAACTNQEEIVRLLLENGAQPaALEAQDSLgnTVLHAlvlqADNTPENsafvcQMY 180
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1229385645  295 ELLLERGAPL-------LARTKNGLSPLHMAAQGDHVECVKHLLQ 332
Cdd:cd21882    181 NLLLSYGAHLdptqqleEIPNHQGLTPLKLAAVEGKIVMFQHILQ 225
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
448-536 1.57e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 59.53  E-value: 1.57e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  448 HMAArAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASV 527
Cdd:PTZ00322    88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166

                   ....*....
gi 1229385645  528 LLEAGAAHS 536
Cdd:PTZ00322   167 LSRHSQCHF 175
NESP55 pfam06390
Neuroendocrine-specific golgi protein P55 (NESP55); This family consists of several mammalian ...
1617-1774 1.70e-08

Neuroendocrine-specific golgi protein P55 (NESP55); This family consists of several mammalian neuroendocrine-specific golgi protein P55 (NESP55) sequences. NESP55 is a novel member of the chromogranin family and is a soluble, acidic, heat-stable secretory protein that is expressed exclusively in endocrine and nervous tissues, although less widely than chromogranins.


Pssm-ID: 115071 [Multi-domain]  Cd Length: 261  Bit Score: 57.57  E-value: 1.70e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645 1617 TFQDGVPKTEGDSSATALFPQTHKEQVQQDFSGKMQDLPEESSLEYQQEYFVTTPGTET-------SETQKAMIVPSSPS 1689
Cdd:pfam06390   62 SFLNAHHRSAAAAAAAQVFPEPSEPESDHEDEDFEPELARPECLEYDEDDFDTETDSETepesdieSETEFETEPETEPD 141
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645 1690 KTPE-EVSTPAEEEK--------------------LYLQTPTSSERGGSPIIQEPEEPSEHRE------ESSPR--KTSL 1740
Cdd:pfam06390  142 TAPTtEPETEPEDEPgpvvpkgatfhqslterlhaLKLQSADASPRRAPPSTQEPESAREGEEpergplDKDPRdpEEEE 221
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1229385645 1741 VIVESADNQPETCErldEDAAFEKGDDMPEIPPE 1774
Cdd:pfam06390  222 EEKEEEKQQPHRCK---PKKPARRRDPSPESPPK 252
Ank_5 pfam13857
Ankyrin repeats (many copies);
230-285 1.72e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 52.35  E-value: 1.72e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1229385645  230 LLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCA 285
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
544-661 2.21e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 59.14  E-value: 2.21e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  544 TPLHVAAKYGSLD--VAKLL----LQRRAAADSAGkngltplhvaahydnqkvALLLLEKGASPHATAKNGYTPLHIAAK 617
Cdd:PTZ00322    63 TPDHNLTTEEVIDpvVAHMLtvelCQLAASGDAVG------------------ARILLTGGADPNCRDYDGRTPLHIACA 124
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1229385645  618 KNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLL 661
Cdd:PTZ00322   125 NGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
Ank_5 pfam13857
Ankyrin repeats (many copies);
362-417 3.56e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 51.58  E-value: 3.56e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1229385645  362 LLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVA 417
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
642-773 4.83e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.99  E-value: 4.83e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  642 VTPLHLASQEGHTDMVTLlldkganiHMSTksgLTSLHLAAQEDKVNvADILTKHGADQDAHTKLGYTPLIVACHYGNVK 721
Cdd:PTZ00322    62 ATPDHNLTTEEVIDPVVA--------HMLT---VELCQLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQ 129
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1229385645  722 MVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATTANG 773
Cdd:PTZ00322   130 VVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGANA 181
PHA02791 PHA02791
ankyrin-like protein; Provisional
212-403 5.78e-08

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 56.20  E-value: 5.78e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  212 GFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNgiTPLHVASKRGNTNMVKLLLDRG---GQIDAKtrdGLTPLHCAARS 288
Cdd:PHA02791    30 GHSALYYAIADNNVRLVCTLLNAGALKNLLENE--FPLHQAATLEDTKIVKILLFSGmddSQFDDK---GNTALYYAVDS 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  289 GHDQVVELLLERGAPLLARTKNGL-SPLHMAAQGDHVECVKHLLQHKAPVDDVTLdYLTALHVAAHCGHYRVTKLLLDKR 367
Cdd:PHA02791   105 GNMQTVKLFVKKNWRLMFYGKTGWkTSFYHAVMLNDVSIVSYFLSEIPSTFDLAI-LLSCIHITIKNGHVDMMILLLDYM 183
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1229385645  368 ANPNARALNGFTP-LHIACKKNRIKVMELLVKYGASI 403
Cdd:PHA02791   184 TSTNTNNSLLFIPdIKLAIDNKDLEMLQALFKYDINI 220
Ank_5 pfam13857
Ankyrin repeats (many copies);
528-582 6.22e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.81  E-value: 6.22e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1229385645  528 LLEAG-AAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVA 582
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
219-381 6.93e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 57.57  E-value: 6.93e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  219 AAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLL 298
Cdd:PLN03192   532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY 611
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  299 ErgaplLARTKN---GLSPLHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNARAL 375
Cdd:PLN03192   612 H-----FASISDphaAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANT 686

                   ....*..
gi 1229385645  376 -NGFTPL 381
Cdd:PLN03192   687 dDDFSPT 693
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
604-760 7.71e-08

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 57.46  E-value: 7.71e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  604 TAKN--GYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQ--------------GVTPLHLASQEGHTDMVTLLLDKGANI 667
Cdd:cd22194    135 TEEAyeGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEIVQLLMEKESTD 214
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  668 HMSTKS-GLTSLHLAaqedkVNVADiltkHGADQDAHTKLGYTPLIVACHYGNVKMVnfllkqganvnaKTKNGYTPLHQ 746
Cdd:cd22194    215 ITSQDSrGNTVLHAL-----VTVAE----DSKTQNDFVKRMYDMILLKSENKNLETI------------RNNEGLTPLQL 273
                          170
                   ....*....|....
gi 1229385645  747 AAQQGHTHIINVLL 760
Cdd:cd22194    274 AAKMGKAEILKYIL 287
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
253-333 7.99e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.22  E-value: 7.99e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  253 SKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLLQ 332
Cdd:PTZ00322    90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169

                   .
gi 1229385645  333 H 333
Cdd:PTZ00322   170 H 170
Ank_4 pfam13637
Ankyrin repeats (many copies);
445-496 8.66e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.35  E-value: 8.66e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1229385645  445 TALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLL 496
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02946 PHA02946
ankyin-like protein; Provisional
58-339 9.02e-08

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 56.60  E-value: 9.02e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645   58 LVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLYM--AAQENHIDVVKYLLENGAN- 134
Cdd:PHA02946    54 FVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYlsGTDDEVIERINLLVQYGAKi 133
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  135 QSTATEDGFTPLAVAL---QQGHNQAVAILLENDTKGKVRLPALHIAARKDDTKSAALLLQndhnadVQSKMMVNRTTES 211
Cdd:PHA02946   134 NNSVDEEGCGPLLACTdpsERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNPKASTISWM------MKLGISPSKPDHD 207
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  212 GFTPLHI--AAHYGNVNVATLLLnrgAAVDFTARN--GITPLHVASKR-GNTNMVKLLLDRGGQIDAKTrdgltpLHCAA 286
Cdd:PHA02946   208 GNTPLHIvcSKTVKNVDIINLLL---PSTDVNKQNkfGDSPLTLLIKTlSPAHLINKLLSTSNVITDQT------VNICI 278
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1229385645  287 RSGHDQVVELLLERGapllarTKNGLSPLHMAAQGDHVECVKHLLQHKAPVDD 339
Cdd:PHA02946   279 FYDRDDVLEIINDKG------KQYDSTDFKMAVEVGSIRCVKYLLDNDIICED 325
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
75-234 1.05e-07

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: 56.79  E-value: 1.05e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645   75 KGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGF-------------TPLYMAAQENHIDVVKYLLENGANQstated 141
Cdd:cd22197     93 RGHSALHIAIEKRSLQCVKLLVENGADVHARACGRFfqkkqgtcfyfgeLPLSLAACTKQWDVVNYLLENPHQP------ 166
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  142 gftplavalqqghnqavAILLENDTKGKVRLPALHIAArkDDTKSAALLLQNDHNADVQSKMMVNRTTE-------SGFT 214
Cdd:cd22197    167 -----------------ASLQAQDSLGNTVLHALVMIA--DNSPENSALVIKMYDGLLQAGARLCPTVQleeisnhEGLT 227
                          170       180
                   ....*....|....*....|
gi 1229385645  215 PLHIAAHYGNVNVATLLLNR 234
Cdd:cd22197    228 PLKLAAKEGKIEIFRHILQR 247
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
75-234 1.10e-07

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: 56.73  E-value: 1.10e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645   75 KGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGF--------------TPLYMAAQENHIDVVKYLLENganqstate 140
Cdd:cd22193     75 EGQTALHIAIERRQGDIVALLVENGADVHAHAKGRFfqpkyqgegfyfgeLPLSLAACTNQPDIVQYLLEN--------- 145
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  141 dgftplavalqqghNQAVAILLENDTKGKVRLPALHIAArkDDTKSAA----------LLLQNDHNADVQSKMMVNRtte 210
Cdd:cd22193    146 --------------EHQPADIEAQDSRGNTVLHALVTVA--DNTKENTkfvtrmydmiLIRGAKLCPTVELEEIRNN--- 206
                          170       180
                   ....*....|....*....|....
gi 1229385645  211 SGFTPLHIAAHYGNVNVATLLLNR 234
Cdd:cd22193    207 DGLTPLQLAAKMGKIEILKYILQR 230
PHA02989 PHA02989
ankyrin repeat protein; Provisional
25-267 1.18e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 56.67  E-value: 1.18e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645   25 KVVEYL-KGGIDIN-TCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSatkKGNTALHIASLAGQAEV--------VKV 94
Cdd:PHA02989    17 NALEFLlRTGFDVNeEYRGNSILLLYLKRKDVKIKIVKLLIDNGADVNY---KGYIETPLCAVLRNREItsnkikkiVKL 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645   95 LVKEGANINAQSQNGFTPLYMAAQENHI---DVVKYLLENGAN-QSTATEDGFTPLAVALQQG--HNQAVAILLEN---- 164
Cdd:PHA02989    94 LLKFGADINLKTFNGVSPIVCFIYNSNInncDMLRFLLSKGINvNDVKNSRGYNLLHMYLESFsvKKDVIKILLSFgvnl 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  165 -DTKGKVRLPALHIAARKD----DTKSAALLLQN-------------------DHNADVQSKMM-----------VNRTT 209
Cdd:PHA02989   174 fEKTSLYGLTPMNIYLRNDidviSIKVIKYLIKKgvnietnnngsesvlesflDNNKILSKKEFkvlnfilkyikINKKD 253
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1229385645  210 ESGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDR 267
Cdd:PHA02989   254 KKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNRILQL 311
Death_p75NR cd08311
Death domain of p75 Neurotrophin Receptor; Death Domain (DD) found in p75 neurotrophin ...
1456-1544 1.20e-07

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: 50.75  E-value: 1.20e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645 1456 PQDEQERIEERLAyiADHLGFSWTELARELDFTEEQIHQIrienpNSLQDQSHALLKYWLERDGkhATDTNLVECLTKIN 1535
Cdd:cd08311      1 PPHKQEEVEKLLN--AGREGSDWRALAGELGYSAEEIDSF-----AREADPCRALLTDWSAQDG--ATLGVLLTALRKIG 71

                   ....*....
gi 1229385645 1536 RMDIVHLME 1544
Cdd:cd08311     72 RDDIVEILQ 80
Ank_5 pfam13857
Ankyrin repeats (many copies);
395-450 1.31e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.04  E-value: 1.31e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1229385645  395 LLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMA 450
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02989 PHA02989
ankyrin repeat protein; Provisional
589-790 1.43e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 56.29  E-value: 1.43e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  589 KVALLLLEKGASphaTAKNGY--TPL-------HIAAKKNQmQIASTLLNYGAETNIVTKQGVTPLH---LASQEGHTDM 656
Cdd:PHA02989    51 KIVKLLIDNGAD---VNYKGYieTPLcavlrnrEITSNKIK-KIVKLLLKFGADINLKTFNGVSPIVcfiYNSNINNCDM 126
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  657 VTLLLDKGANIH-MSTKSGLTSLHLAAQEDKVN--VADILTKHGADQDAHTKL-GYTPLIVACHYG----NVKMVNFLLK 728
Cdd:PHA02989   127 LRFLLSKGINVNdVKNSRGYNLLHMYLESFSVKkdVIKILLSFGVNLFEKTSLyGLTPMNIYLRNDidviSIKVIKYLIK 206
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  729 QGAN--------------------------------------VNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATT 770
Cdd:PHA02989   207 KGVNietnnngsesvlesfldnnkilskkefkvlnfilkyikINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVS 286
                          250       260
                   ....*....|....*....|
gi 1229385645  771 ANGNTALAIAKRLGYISVVD 790
Cdd:PHA02989   287 KDGDTVLTYAIKHGNIDMLN 306
Ank_5 pfam13857
Ankyrin repeats (many copies);
692-747 1.47e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 49.65  E-value: 1.47e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1229385645  692 ILTKHGADQDAHTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQA 747
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
337-430 1.54e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.45  E-value: 1.54e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  337 VDDVTLDYLTA--LHVAAHcGHYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPI 414
Cdd:PTZ00322    74 IDPVVAHMLTVelCQLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPL 152
                           90
                   ....*....|....*.
gi 1229385645  415 HVAAFMGHLNIVLLLL 430
Cdd:PTZ00322   153 ELAEENGFREVVQLLS 168
Ank_5 pfam13857
Ankyrin repeats (many copies);
726-780 1.59e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 49.65  E-value: 1.59e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1229385645  726 LLKQG-ANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTALAIA 780
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
171-232 1.67e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.58  E-value: 1.67e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1229385645  171 RLPALHIAARKDDTKSAALLLQNDHNadvqskmmVNRTTESGFTPLHIAAHYGNVNVATLLL 232
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGAD--------INAVDGNGETALHFAASNGNVEVLKLLL 54
Death_RAIDD cd08319
Death domain of RIP-associated ICH-1 homologous protein with a death domain; Death domain (DD) ...
1464-1535 1.72e-07

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: 50.40  E-value: 1.72e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1229385645 1464 EERLAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKIN 1535
Cdd:cd08319      2 DRQLNKLAQRLGPEWEQVLLDLGLSKADIYRCKADHPYNVQSQIVEALVKWKQRQGKKATVQSLIQSLKAVE 73
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
624-696 1.76e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.06  E-value: 1.76e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1229385645  624 ASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADILTKH 696
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
156-298 1.99e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.06  E-value: 1.99e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  156 QAVAILLENDTKGKVRLPALHIAARKDDTKSAALLLQNDHNADVQSKMMVNRTtesgftplHIAAHyGNVNVATLLLNRG 235
Cdd:PTZ00322    35 ERMAAIQEEIARIDTHLEALEATENKDATPDHNLTTEEVIDPVVAHMLTVELC--------QLAAS-GDAVGARILLTGG 105
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1229385645  236 AAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLL 298
Cdd:PTZ00322   106 ADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
Ank_4 pfam13637
Ankyrin repeats (many copies);
111-162 2.67e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.81  E-value: 2.67e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1229385645  111 TPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHNQAVAILL 162
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
6-234 2.80e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 55.40  E-value: 2.80e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645    6 QKSDSNASFLRAARAGNLDKVVEYLK-GGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSS-----VDSATKKGNTA 79
Cdd:cd22192     13 QKRISESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElvnepMTSDLYQGETA 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645   80 LHIASLAGQAEVVKVLVKEGANINAQSQNG--FT------------PLYMAAQENHIDVVKYLLENGANQstatedgftp 145
Cdd:cd22192     93 LHIAVVNQNLNLVRELIARGADVVSPRATGtfFRpgpknliyygehPLSFAACVGNEEIVRLLIEHGADI---------- 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  146 lavalqqgHNQavaillenDTKGKVrlpALHIAARKDDTKSAA----LLLQNDHNADVQSKMMVnrTTESGFTPLHIAAH 221
Cdd:cd22192    163 --------RAQ--------DSLGNT---VLHILVLQPNKTFACqmydLILSYDKEDDLQPLDLV--PNNQGLTPFKLAAK 221
                          250
                   ....*....|...
gi 1229385645  222 YGNVNVATLLLNR 234
Cdd:cd22192    222 EGNIVMFQHLVQK 234
Ank_4 pfam13637
Ankyrin repeats (many copies);
740-792 2.98e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.81  E-value: 2.98e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1229385645  740 GYTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTALAIAKRLGYISVVDTL 792
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank_5 pfam13857
Ankyrin repeats (many copies);
627-681 3.36e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.88  E-value: 3.36e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1229385645  627 LLNYG-AETNIVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLA 681
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
395-503 3.43e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 55.29  E-value: 3.43e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  395 LLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNGAL---VDA 471
Cdd:PTZ00322   100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQChfeLGA 179
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1229385645  472 RAREEqtplhiaSRLGKTEIVQLLLQHMAHPD 503
Cdd:PTZ00322   180 NAKPD-------SFTGKPPSLEDSPISSHHPD 204
Ank_5 pfam13857
Ankyrin repeats (many copies);
429-483 3.70e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.50  E-value: 3.70e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1229385645  429 LLQNG-ASPDVTNIRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIA 483
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
723-792 3.89e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 55.29  E-value: 3.89e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  723 VNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTALAIAKRLGYISVVDTL 792
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
Ank_5 pfam13857
Ankyrin repeats (many copies);
190-252 4.04e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.50  E-value: 4.04e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1229385645  190 LLQNDHNAdvqskmmVNRTTESGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVA 252
Cdd:pfam13857    1 LLEHGPID-------LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
48-129 4.35e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.90  E-value: 4.35e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645   48 HLAAKEGHVGlVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKY 127
Cdd:PTZ00322    88 QLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166

                   ..
gi 1229385645  128 LL 129
Cdd:PTZ00322   167 LS 168
Ank_4 pfam13637
Ankyrin repeats (many copies);
544-595 4.63e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.42  E-value: 4.63e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1229385645  544 TPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLL 595
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
641-693 4.77e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.04  E-value: 4.77e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1229385645  641 GVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADIL 693
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
Death_NMPP84 cd08318
Death domain of Nuclear Matrix Protein P84; Death domain (DD) found in the Nuclear Matrix ...
1460-1539 5.37e-07

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: 49.06  E-value: 5.37e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645 1460 QERIEErlayIADHLGFSWTELARELDFTEEQIHQIRiENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDI 1539
Cdd:cd08318      7 SEQIDV----LANKLGEQWKTLAPYLEMKDKDIRQIE-SDSEDMKMRAKQLLVTWQDREGAQATPEILMTALNAAGLNEI 81
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
84-162 5.76e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.52  E-value: 5.76e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1229385645   84 SLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHNQAVAILL 162
Cdd:PTZ00322    90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
Ank_5 pfam13857
Ankyrin repeats (many copies);
264-318 7.87e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.73  E-value: 7.87e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1229385645  264 LLDRGGQ-IDAKTRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMA 318
Cdd:pfam13857    1 LLEHGPIdLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
9-254 8.26e-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: 8.26e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645    9 DSNASFLRAARAGNLD--KVVEYLKGGIDIntcnqnGLNALHLAAKEGHVGlVQELL--------GRGSS---VDSATK- 74
Cdd:TIGR00870   52 GRSALFVAAIENENLEltELLLNLSCRGAV------GDTLLHAISLEYVDA-VEAILlhllaafrKSGPLelaNDQYTSe 124
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645   75 --KGNTALHIASLAGQAEVVKVLVKEGANINA----------QSQNGF----TPLYMAAQENHIDVVKYLLENGANQSTA 138
Cdd:TIGR00870  125 ftPGITALHLAAHRQNYEIVKLLLERGASVPAracgdffvksQGVDSFyhgeSPLNAAACLGSPSIVALLSEDPADILTA 204
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  139 TEDGFTPLAVALQQGHNQAvaillENDTKG-KVRLPALHIAARKDDTKSAALLLQNDhnadvqskmmvnrttesGFTPLH 217
Cdd:TIGR00870  205 DSLGNTLLHLLVMENEFKA-----EYEELScQMYNFALSLLDKLRDSKELEVILNHQ-----------------GLTPLK 262
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1229385645  218 IAAHYGNVNVATLLLNRGAAV-DFTA-RNGitPLHVASK 254
Cdd:TIGR00870  263 LAAKEGRIVLFRLKLAIKYKQkKFVAwPNG--QQLLSLY 299
Ank_5 pfam13857
Ankyrin repeats (many copies);
32-83 9.12e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.34  E-value: 9.12e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1229385645   32 GGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIA 83
Cdd:pfam13857    5 GPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
594-648 9.21e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.34  E-value: 9.21e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1229385645  594 LLEKG-ASPHATAKNGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLA 648
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02798 PHA02798
ankyrin-like protein; Provisional
225-450 9.60e-07

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 53.69  E-value: 9.60e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  225 VNVATLLLNRGAAVDFTARNGITPL-----HVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLL- 298
Cdd:PHA02798    51 TDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLf 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  299 --ERGAPLLARTKNGLSPLHMAAQGDH---VECVKHLLQHKAPVDDVT-LDYLTALHV----AAHCGHYRVTKLLLD--- 365
Cdd:PHA02798   131 miENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINTHNnKEKYDTLHCyfkyNIDRIDADILKLFVDngf 210
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  366 --KRANPNARA--LNGFTPLHIACKKNRIKVMELLVKYgASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNI 441
Cdd:PHA02798   211 iiNKENKSHKKkfMEYLNSLLYDNKRFKKNILDFIFSY-IDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITE 289

                   ....*....
gi 1229385645  442 RGETALHMA 450
Cdd:PHA02798   290 LGNTCLFTA 298
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
471-633 9.84e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.75  E-value: 9.84e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  471 ARAREEQTPLHIA-SRLG--KTEIVQLLlQHMAHPDAATTNGYTPLHISAREGQVDVAsvlleagAAHSLATKKgftpLH 547
Cdd:PTZ00322    21 TEGSRKRRAKPISfERMAaiQEEIARID-THLEALEATENKDATPDHNLTTEEVIDPV-------VAHMLTVEL----CQ 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  548 VAAKyGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQMQIASTL 627
Cdd:PTZ00322    89 LAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167

                   ....*.
gi 1229385645  628 LNYGAE 633
Cdd:PTZ00322   168 SRHSQC 173
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
75-234 1.01e-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: 53.73  E-value: 1.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645   75 KGNTALHIASLAGQAEVVKVLVKEGANINAQS---------QNGF----TPLYMAAQENHIDVVKYLLENGANqstated 141
Cdd:cd21882     72 QGQTALHIAIENRNLNLVRLLVENGADVSARAtgrffrkspGNLFyfgeLPLSLAACTNQEEIVRLLLENGAQ------- 144
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  142 gftplavalqqghnqaVAILLENDTKGKVRLPALHIAARKDDTKSA------ALLLQNDHNAD--VQSKMMVNRtteSGF 213
Cdd:cd21882    145 ----------------PAALEAQDSLGNTVLHALVLQADNTPENSAfvcqmyNLLLSYGAHLDptQQLEEIPNH---QGL 205
                          170       180
                   ....*....|....*....|.
gi 1229385645  214 TPLHIAAHYGNVNVATLLLNR 234
Cdd:cd21882    206 TPLKLAAVEGKIVMFQHILQR 226
PHA02989 PHA02989
ankyrin repeat protein; Provisional
226-565 1.06e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 53.59  E-value: 1.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  226 NVATLLLNRGAAVDFTAR-NGITPLHVASKRGNTNMVKLLLDRGGQIDAKtrdGL--TPLHCAAR------SGHDQVVEL 296
Cdd:PHA02989    17 NALEFLLRTGFDVNEEYRgNSILLLYLKRKDVKIKIVKLLIDNGADVNYK---GYieTPLCAVLRnreitsNKIKKIVKL 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  297 LLERGAPLLARTKNGLSPLHMAAQGDHVEcvkhllqhkapvddvTLDYLtalhvaahcghyrvtKLLLDKRANPNA-RAL 375
Cdd:PHA02989    94 LLKFGADINLKTFNGVSPIVCFIYNSNIN---------------NCDML---------------RFLLSKGINVNDvKNS 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  376 NGFTPLHIACKK--NRIKVMELLVKYGASIQAITE-SGLTP--IHVAAFMGHLNIVLL--LLQNGASPDVTNIRGETALH 448
Cdd:PHA02989   144 RGYNLLHMYLESfsVKKDVIKILLSFGVNLFEKTSlYGLTPmnIYLRNDIDVISIKVIkyLIKKGVNIETNNNGSESVLE 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  449 maaragqvevvrCLLRNGALVdarAREEQTPLHIASRLGKTEIVQlllqhmahpdaatTNGYTPLHISAREGQVDVASVL 528
Cdd:PHA02989   224 ------------SFLDNNKIL---SKKEFKVLNFILKYIKINKKD-------------KKGFNPLLISAKVDNYEAFNYL 275
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1229385645  529 LEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRR 565
Cdd:PHA02989   276 LKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNRILQLK 312
PHA02884 PHA02884
ankyrin repeat protein; Provisional
546-663 1.23e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 52.29  E-value: 1.23e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  546 LHVAAKYGSLDVAKLLLQRRAAADSAGKNGL----TPLHVAAHYDNQKVALLLLEKGASPHATAKNG-YTPLHIAAKKNQ 620
Cdd:PHA02884    37 LYSSIKFHYTDIIDAILKLGADPEAPFPLSEnsktNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAkITPLYISVLHGC 116
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1229385645  621 MQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLDK 663
Cdd:PHA02884   117 LKCLEILLSYGADINIQTNDMVTPIELALMICNNFLAFMICDN 159
Ank_4 pfam13637
Ankyrin repeats (many copies);
509-562 1.23e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.88  E-value: 1.23e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1229385645  509 GYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLL 562
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
277-309 1.38e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 46.51  E-value: 1.38e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1229385645  277 DGLTPLHCAA-RSGHDQVVELLLERGAPLLARTK 309
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
575-689 1.38e-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: 1.38e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  575 GLTPLHVAAHYDNQKVALLLLEKGASPHATAKN--------------GYTPLHIAAKKNQMQIASTLLNygAETNIVTKQ 640
Cdd:cd22194    141 GQTALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEIVQLLME--KESTDITSQ 218
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1229385645  641 ---GVTPLHL-----ASQEGHTDMVTLLLD------KGANIH-MSTKSGLTSLHLAAQEDKVNV 689
Cdd:cd22194    219 dsrGNTVLHAlvtvaEDSKTQNDFVKRMYDmillksENKNLEtIRNNEGLTPLQLAAKMGKAEI 282
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
75-234 1.46e-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: 1.46e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645   75 KGNTALHIASLAGQAEVVKVLVKEGANINA----------QSQNGF----TPLYMAAQENHIDVVKYLLENganqstate 140
Cdd:cd22196     93 KGQTALHIAIERRNMHLVELLVQNGADVHArasgeffkkkKGGPGFyfgeLPLSLAACTNQLDIVKFLLEN--------- 163
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  141 dGFTPLAVALQqghnqavaillenDTKGKVRLPALHIAA--RKDDTK------SAALLLQNDHNADVQSKMMVNRtteSG 212
Cdd:cd22196    164 -PHSPADISAR-------------DSMGNTVLHALVEVAdnTPENTKfvtkmyNEILILGAKIRPLLKLEEITNK---KG 226
                          170       180
                   ....*....|....*....|..
gi 1229385645  213 FTPLHIAAHYGNVNVATLLLNR 234
Cdd:cd22196    227 LTPLKLAAKTGKIGIFAYILGR 248
PHA02736 PHA02736
Viral ankyrin protein; Provisional
160-272 1.54e-06

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 49.87  E-value: 1.54e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  160 ILLENDTKGKvrlPALHIAARKD--DTKSAALLLQnDHNADVQSKMMVNrttesGFTPLHIAAHYGNVNVATLLLNRgAA 237
Cdd:PHA02736    47 LVLEYNRHGK---QCVHIVSNPDkaDPQEKLKLLM-EWGADINGKERVF-----GNTPLHIAVYTQNYELATWLCNQ-PG 116
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1229385645  238 VDFTARNGI--TPLHVASKRGNTNMVKLLLDRGGQID 272
Cdd:PHA02736   117 VNMEILNYAfkTPYYVACERHDAKMMNILRAKGAQCK 153
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
442-564 2.16e-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: 52.49  E-value: 2.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  442 RGETALHMAARAGQVEVVRCLLRNGALVDARAREE--------------QTPLHIASRLGKTEIVQLLLQHMAHP---DA 504
Cdd:cd22193     75 EGQTALHIAIERRQGDIVALLVENGADVHAHAKGRffqpkyqgegfyfgELPLSLAACTNQPDIVQYLLENEHQPadiEA 154
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1229385645  505 ATTNGYTPLHI------SAREGQVDVASV---LLEAGAA-------HSLATKKGFTPLHVAAKYGSLDVAKLLLQR 564
Cdd:cd22193    155 QDSRGNTVLHAlvtvadNTKENTKFVTRMydmILIRGAKlcptvelEEIRNNDGLTPLQLAAKMGKIEILKYILQR 230
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
519-693 2.16e-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: 52.50  E-value: 2.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  519 EGQVDVASVLLEagaahsLATKKGFTPLHVAAKYgsldvaklllqrraaADSAGKnGLTPLHVAAHYDNQKVALLLLEKG 598
Cdd:cd22196     60 NGQNDTISLLLD------IAEKTGNLKEFVNAAY---------------TDSYYK-GQTALHIAIERRNMHLVELLVQNG 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  599 ASPHATA----------KNGY----TPLHIAAKKNQMQIASTLLN---YGAETNIVTKQGVTPLH---------LASQEG 652
Cdd:cd22196    118 ADVHARAsgeffkkkkgGPGFyfgeLPLSLAACTNQLDIVKFLLEnphSPADISARDSMGNTVLHalvevadntPENTKF 197
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1229385645  653 HTDMVTLLLDKGANIH-------MSTKSGLTSLHLAAQEDKVNV-ADIL 693
Cdd:cd22196    198 VTKMYNEILILGAKIRpllkleeITNKKGLTPLKLAAKTGKIGIfAYIL 246
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
645-781 2.18e-06

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 52.78  E-value: 2.18e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  645 LHLASQEGHTDMVTLLLDKGANIHMstksGLTSLHLAAQEDKVNVADILT---KHGADQDAHTKL----------GYTPL 711
Cdd:TIGR00870   57 FVAAIENENLELTELLLNLSCRGAV----GDTLLHAISLEYVDAVEAILLhllAAFRKSGPLELAndqytseftpGITAL 132
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  712 IVACHYGNVKMVNFLLKQGANVNAKTK--------------NGYTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTAL 777
Cdd:TIGR00870  133 HLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLL 212

                   ....
gi 1229385645  778 AIAK 781
Cdd:TIGR00870  213 HLLV 216
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
687-780 2.34e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 52.56  E-value: 2.34e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  687 VNVADILTKHGADQDahTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKP 766
Cdd:PLN03192   507 LNVGDLLGDNGGEHD--DPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNV 584
                           90
                   ....*....|....*.
gi 1229385645  767 NATTANGNTAL--AIA 780
Cdd:PLN03192   585 HIRDANGNTALwnAIS 600
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
108-134 2.53e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 45.66  E-value: 2.53e-06
                            10        20
                    ....*....|....*....|....*..
gi 1229385645   108 NGFTPLYMAAQENHIDVVKYLLENGAN 134
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
Ank_5 pfam13857
Ankyrin repeats (many copies);
330-384 2.58e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.19  E-value: 2.58e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1229385645  330 LLQHKaPVDDVTLDY--LTALHVAAHCGHYRVTKLLLDKRANPNARALNGFTPLHIA 384
Cdd:pfam13857    1 LLEHG-PIDLNRLDGegYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02798 PHA02798
ankyrin-like protein; Provisional
114-431 3.37e-06

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 51.76  E-value: 3.37e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  114 YMAAQENHIDVVKYLLENGANQSTATEDGFTPLAValqqghnqavaiLLEN--DTKGKVRLPALHIaarkddtksaalll 191
Cdd:PHA02798    43 YLQRDSPSTDIVKLFINLGANVNGLDNEYSTPLCT------------ILSNikDYKHMLDIVKILI-------------- 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  192 qnDHNADVqskmmvNRTTESGFTPLHIAAHYGNVN---VATLLLNRGAAVDFTARNGITPLHVASKRGNT---NMVKLLL 265
Cdd:PHA02798    97 --ENGADI------NKKNSDGETPLYCLLSNGYINnleILLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLL 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  266 DRGGQIDA-KTRDGLTPLHCAARSGHDQ----VVELLLERGAPLLARTKnglsplhmaaqgdhvecvkhllQHKAPVddv 340
Cdd:PHA02798   169 EKGVDINThNNKEKYDTLHCYFKYNIDRidadILKLFVDNGFIINKENK----------------------SHKKKF--- 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  341 tLDYLTALHVAAHcghyRVTKLLLD---KRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVA 417
Cdd:PHA02798   224 -MEYLNSLLYDNK----RFKKNILDfifSYIDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTA 298
                          330
                   ....*....|....
gi 1229385645  418 AFMGHLNIVLLLLQ 431
Cdd:PHA02798   299 FENESKFIFNSILN 312
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
572-729 3.43e-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: 51.80  E-value: 3.43e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  572 GKNGLTPLHVAAHYDNQKV---ALLLLE---KGASPHATAK--------NGYTPLHIAAKKNQMQIASTLLNYGAETNIV 637
Cdd:cd21882     23 GATGKTCLHKAALNLNDGVneaIMLLLEaapDSGNPKELVNapctdefyQGQTALHIAIENRNLNLVRLLVENGADVSAR 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  638 TKQ-------------GVTPLHLASQEGHTDMVTLLLDKGANIHMSTKS---GLTSLH-LAAQEDK--------VNVADI 692
Cdd:cd21882    103 ATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPAALEAQdslGNTVLHaLVLQADNtpensafvCQMYNL 182
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1229385645  693 LTKHGADQDAHTKL-------GYTPLIVACHYGNVKMVNFLLKQ 729
Cdd:cd21882    183 LLSYGAHLDPTQQLeeipnhqGLTPLKLAAVEGKIVMFQHILQR 226
Ank_5 pfam13857
Ankyrin repeats (many copies);
560-615 3.67e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.80  E-value: 3.67e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1229385645  560 LLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHATAKNGYTPLHIA 615
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
707-738 4.65e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 44.97  E-value: 4.65e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1229385645  707 GYTPLIVAC-HYGNVKMVNFLLKQGANVNAKTK 738
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank_4 pfam13637
Ankyrin repeats (many copies);
16-63 5.27e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.34  E-value: 5.27e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1229385645   16 RAARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELL 63
Cdd:pfam13637    7 AAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
509-714 5.58e-06

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 51.24  E-value: 5.58e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  509 GYTPLHISAREGQV-DVASVLLEagaaHSLATKKGFTPLHVAAKyGSLDVAKLLLQRRAAADSAGKN------------- 574
Cdd:TIGR00870   52 GRSALFVAAIENENlELTELLLN----LSCRGAVGDTLLHAISL-EYVDAVEAILLHLLAAFRKSGPlelandqytseft 126
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  575 -GLTPLHVAAHYDNQKVALLLLEKGASPHATAK--------------NGYTPLHIAAKKNQMQIASTLLNYGAETNIVTK 639
Cdd:TIGR00870  127 pGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADS 206
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  640 QGVTPLHLASQEGH---------TDMVTLLLDKGANIHMSTK-------SGLTSLHLAAQEDKVNVADILTKHGADQDAH 703
Cdd:TIGR00870  207 LGNTLLHLLVMENEfkaeyeelsCQMYNFALSLLDKLRDSKElevilnhQGLTPLKLAAKEGRIVLFRLKLAIKYKQKKF 286
                          250
                   ....*....|.
gi 1229385645  704 TKLGYTPLIVA 714
Cdd:TIGR00870  287 VAWPNGQQLLS 297
Ank_4 pfam13637
Ankyrin repeats (many copies);
674-727 5.81e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.96  E-value: 5.81e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1229385645  674 GLTSLHLAAQEDKVNVADILTKHGADQDAHTKLGYTPLIVACHYGNVKMVNFLL 727
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
739-770 6.31e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 44.59  E-value: 6.31e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1229385645  739 NGYTPLHQAAQQ-GHTHIINVLLQHGAKPNATT 770
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
Death_TRAILR_DR4_DR5 cd08315
Death domain of Tumor necrosis factor-Related Apoptosis-Inducing Ligand Receptors; Death ...
1469-1535 6.43e-06

Death domain of Tumor necrosis factor-Related Apoptosis-Inducing Ligand Receptors; Death Domain (DD) found in Tumor necrosis factor-Related Apoptosis-Inducing Ligand (TRAIL) Receptors. In mammals, this family includes TRAILR1 (also called DR4 or TNFRSF10A) and TRAILR2 (also called DR5, TNFRSF10B, or KILLER). They function as receptors for the cytokine TRAIL and are involved in apoptosis signaling pathways. TRAIL preferentially induces apoptosis in cancer cells while exhibiting little toxicity in normal cells. 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: 260027  Cd Length: 88  Bit Score: 46.11  E-value: 6.43e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1229385645 1469 YIADHLGF-SWTELARELDFTEEQIHQIRIENPNSlQDQSHALLKYWLERDGKHATDTNLVECLTKIN 1535
Cdd:cd08315      4 YFEDIVPFkSWKRLMRALGLSDNEIKLAEANDPGS-QEPLYQMLNKWLNKTGRKASVNTLLDALEDLG 70
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
376-403 6.48e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 44.50  E-value: 6.48e-06
                            10        20
                    ....*....|....*....|....*...
gi 1229385645   376 NGFTPLHIACKKNRIKVMELLVKYGASI 403
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
Death_DRs cd08784
Death Domain of Death Receptors; Death domain (DD) found in death receptor proteins. Death ...
1477-1544 7.91e-06

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: 45.65  E-value: 7.91e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1229385645 1477 SWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLtkiNRMDIVHLME 1544
Cdd:cd08784     13 QWKGFVRKLGLNEAEIDEIKNDNVQDTAEAKYQMLRNWHQLTGRKAAYDTLIKDL---KKMNLCTLAE 77
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
377-516 8.36e-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: 8.36e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  377 GFTPLHIACKKNRIKVMELLVKYGASIQAITES--------------GLTPIHVAAFMGHLNIVLLLLQNG---ASPDVT 439
Cdd:cd22193     76 GQTALHIAIERRQGDIVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLSLAACTNQPDIVQYLLENEhqpADIEAQ 155
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  440 NIRGETALH--------------MAARAGQVEVVRC--LLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPD 503
Cdd:cd22193    156 DSRGNTVLHalvtvadntkentkFVTRMYDMILIRGakLCPTVELEEIRNNDGLTPLQLAAKMGKIEILKYILQREIKEP 235
                          170       180
                   ....*....|....*....|
gi 1229385645  504 AA-------TTNGYTPLHIS 516
Cdd:cd22193    236 ELrhlsrkfTDWAYGPVSSS 255
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
450-672 8.81e-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: 8.81e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  450 AARAGQVEVVRCLLRNGALVDARAREEQTPLHI-----ASRLGKTEIVQLLLQHmahpdAATTNGYTPLHISAREGQvDV 524
Cdd:cd22194     52 KVSEAAVEELGELLKELKDLSRRRRKTDVPDFLmhkltASDTGKTCLMKALLNI-----NENTKEIVRILLAFAEEN-GI 125
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  525 ASVLLEAgaAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKN--------------GLTPLHVAAHYDNQKV 590
Cdd:cd22194    126 LDRFINA--EYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEI 203
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  591 ALLLLEKGASPHATAKN-GYTPLH---IAAKKNQMQIAST-------LLNYGAET--NIVTKQGVTPLHLASQEGHTDMV 657
Cdd:cd22194    204 VQLLMEKESTDITSQDSrGNTVLHalvTVAEDSKTQNDFVkrmydmiLLKSENKNleTIRNNEGLTPLQLAAKMGKAEIL 283
                          250       260
                   ....*....|....*....|
gi 1229385645  658 TLLL-----DKGaNIHMSTK 672
Cdd:cd22194    284 KYILsreikEKP-NRSLSRK 302
Ank_5 pfam13857
Ankyrin repeats (many copies);
95-149 9.61e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.64  E-value: 9.61e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1229385645   95 LVKEG-ANINAQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVA 149
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02736 PHA02736
Viral ankyrin protein; Provisional
586-665 1.02e-05

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 47.56  E-value: 1.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  586 DNQKVALLLLEKGASPHAT-AKNGYTPLHIAAKKNQMQIASTLLNY-GAETNIVTKQGVTPLHLASQEGHTDMVTLLLDK 663
Cdd:PHA02736    69 DPQEKLKLLMEWGADINGKeRVFGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERHDAKMMNILRAK 148

                   ..
gi 1229385645  664 GA 665
Cdd:PHA02736   149 GA 150
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
316-399 1.04e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.67  E-value: 1.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  316 HMAAQGDHVEcVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMEL 395
Cdd:PTZ00322    88 QLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166

                   ....
gi 1229385645  396 LVKY 399
Cdd:PTZ00322   167 LSRH 170
Ank_5 pfam13857
Ankyrin repeats (many copies);
462-515 1.07e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.64  E-value: 1.07e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1229385645  462 LLRNG-ALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHI 515
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
210-579 1.08e-05

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 50.68  E-value: 1.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  210 ESGFTPLHiaAHYGNVNVAT----LLLNRGAAVDFTARNGITPLHVASKRGN--TNMVKLLLDRGGQIDAKTRDGLTPLH 283
Cdd:PHA02716   175 KTGYGILH--AYLGNMYVDIdileWLCNNGVNVNLQNNHLITPLHTYLITGNvcASVIKKIIELGGDMDMKCVNGMSPIM 252
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  284 ---CAARSGHDQVVELLLERGAPllARTKNGLSPLHM---AAQGDHVECVKHLLQhkapvDDVTLDY-----LTALH--V 350
Cdd:PHA02716   253 tyiINIDNINPEITNIYIESLDG--NKVKNIPMILHSyitLARNIDISVVYSFLQ-----PGVKLHYkdsagRTCLHqyI 325
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  351 AAHCGHYRVTKLLLDKRANPNARALNGFTPLH----IACKKN----------RIKVMELLVKYGASIQAITESGLTPihv 416
Cdd:PHA02716   326 LRHNISTDIIKLLHEYGNDLNEPDNIGNTVLHtylsMLSVVNildpetdndiRLDVIQCLISLGADITAVNCLGYTP--- 402
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  417 aafmghLNIVLLLLQNGASPDVTN-IRGETALHMaaragqvevvrclLRNGALVDARAREEQTPLHIASRLGKTEIvqll 495
Cdd:PHA02716   403 ------LTSYICTAQNYMYYDIIDcLISDKVLNM-------------VKHRILQDLLIRVDDTPCIIHHIIAKYNI---- 459
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  496 lqhmahPDAATTNGYTPLHISAREgqvDVASVLLEAGAAHSLATKKGFTPLHVAAKYGS-----LDVAKLLLQRRAAADS 570
Cdd:PHA02716   460 ------PTDLYTDEYEPYDSTKIH---DVYHCAIIERYNNAVCETSGMTPLHVSIISHTnanivMDSFVYLLSIQYNINI 530

                   ....*....
gi 1229385645  571 AGKNGLTPL 579
Cdd:PHA02716   531 PTKNGVTPL 539
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
123-300 1.16e-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: 50.26  E-value: 1.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  123 DVVKYLLENGANQSTATedGFTPLAVA---LQQGHNQAVAILLENDTKGKVRLP---------------ALHIAARKDDT 184
Cdd:cd21882      9 ECLRWYLTDSAYQRGAT--GKTCLHKAalnLNDGVNEAIMLLLEAAPDSGNPKElvnapctdefyqgqtALHIAIENRNL 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  185 KSAALLLQNdhNADVQSKM---MVNRTTESGF----TPLHIAAHYGNVNVATLLLNRGAAV-DFTARN--GITPLHVASK 254
Cdd:cd21882     87 NLVRLLVEN--GADVSARAtgrFFRKSPGNLFyfgeLPLSLAACTNQEEIVRLLLENGAQPaALEAQDslGNTVLHALVL 164
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1229385645  255 RGN---------TNMVKLLLDRGGQID-------AKTRDGLTPLHCAARSGHDQVVELLLER 300
Cdd:cd21882    165 QADntpensafvCQMYNLLLSYGAHLDptqqleeIPNHQGLTPLKLAAVEGKIVMFQHILQR 226
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
739-768 1.21e-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: 43.73  E-value: 1.21e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 1229385645   739 NGYTPLHQAAQQGHTHIINVLLQHGAKPNA 768
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
442-564 1.31e-05

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: 50.24  E-value: 1.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  442 RGETALHMAARAGQVEVVRCLLRNGALVDARAREE-------------QTPLHIASRLGKTEIVQLLLQHMAHP---DAA 505
Cdd:cd22197     93 RGHSALHIAIEKRSLQCVKLLVENGADVHARACGRffqkkqgtcfyfgELPLSLAACTKQWDVVNYLLENPHQPaslQAQ 172
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1229385645  506 TTNGYTPLH---ISAREGQVDVASV------LLEAGAA-------HSLATKKGFTPLHVAAKYGSLDVAKLLLQR 564
Cdd:cd22197    173 DSLGNTVLHalvMIADNSPENSALVikmydgLLQAGARlcptvqlEEISNHEGLTPLKLAAKEGKIEIFRHILQR 247
PHA02989 PHA02989
ankyrin repeat protein; Provisional
424-769 1.44e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 49.74  E-value: 1.44e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  424 NIVLLLLQNGAspDVTNI-RGETALHMAARAGQV--EVVRCLLRNGALVDARAREEqTPL-------HIASRLGKtEIVQ 493
Cdd:PHA02989    17 NALEFLLRTGF--DVNEEyRGNSILLLYLKRKDVkiKIVKLLIDNGADVNYKGYIE-TPLcavlrnrEITSNKIK-KIVK 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  494 LLLQHMAHPDAATTNGYTPL-------HISaregQVDVASVLLEAGA-AHSLATKKGFTPLHVAAKYGSL--DVAKLLLq 563
Cdd:PHA02989    93 LLLKFGADINLKTFNGVSPIvcfiynsNIN----NCDMLRFLLSKGInVNDVKNSRGYNLLHMYLESFSVkkDVIKILL- 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  564 rRAAADSAGKN---GLTPLHVAAHYD----NQKVALLLLEKGASphatakngytplhiaakknqmqiastllnygAETNi 636
Cdd:PHA02989   168 -SFGVNLFEKTslyGLTPMNIYLRNDidviSIKVIKYLIKKGVN-------------------------------IETN- 214
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  637 vtkqgvtplhlasQEGHTDMVTLLLDKgaNIHMSTKSgLTSLHLAAQEDKVNVADiltkhgadqdahtKLGYTPLIVACH 716
Cdd:PHA02989   215 -------------NNGSESVLESFLDN--NKILSKKE-FKVLNFILKYIKINKKD-------------KKGFNPLLISAK 265
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1229385645  717 YGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQhgAKPNAT 769
Cdd:PHA02989   266 VDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNRILQ--LKPGKY 316
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
640-669 1.48e-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: 1.48e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 1229385645   640 QGVTPLHLASQEGHTDMVTLLLDKGANIHM 669
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02741 PHA02741
hypothetical protein; Provisional
40-163 1.55e-05

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 47.34  E-value: 1.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645   40 NQNGLNALHLAAKEGHVGLVQELLG--RGSSVDSATK----KGNTALHIASLAGQA----EVVKVLVKEGANINAQ-SQN 108
Cdd:PHA02741    18 NSEGENFFHEAARCGCFDIIARFTPfiRGDCHAAALNatddAGQMCIHIAAEKHEAqlaaEIIDHLIELGADINAQeMLE 97
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1229385645  109 GFTPLYMAAQENHIDVVKYLL-ENGANQSTATEDGFTPLAVALQQGHNQAVAILLE 163
Cdd:PHA02741    98 GDTALHLAAHRRDHDLAEWLCcQPGIDLHFCNADNKSPFELAIDNEDVAMMQILRE 153
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
640-672 1.59e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 43.43  E-value: 1.59e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1229385645  640 QGVTPLHLAS-QEGHTDMVTLLLDKGANIHMSTK 672
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
244-273 1.76e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.96  E-value: 1.76e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 1229385645   244 NGITPLHVASKRGNTNMVKLLLDRGGQIDA 273
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
372-496 1.89e-05

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 49.76  E-value: 1.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  372 ARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITES--------------GLTPIHVAAFMGHLNIVLLLLQNGASP- 436
Cdd:cd22194    136 EEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEIVQLLMEKESTDi 215
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1229385645  437 DVTNIRGETALH---MAARAGQ------VEVVRCLLR---NGALVDARAREEQTPLHIASRLGKTEIVQLLL 496
Cdd:cd22194    216 TSQDSRGNTVLHalvTVAEDSKtqndfvKRMYDMILLkseNKNLETIRNNEGLTPLQLAAKMGKAEILKYIL 287
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
75-104 2.12e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.96  E-value: 2.12e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 1229385645    75 KGNTALHIASLAGQAEVVKVLVKEGANINA 104
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02859 PHA02859
ankyrin repeat protein; Provisional
204-350 2.49e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 47.51  E-value: 2.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  204 MVNRTTESGFTPLH--IAAHYGNVNVATLLLNRGAAVDFTAR-NGITPLH---VASKRGNTNMVKLLLDRGGQIDAKTRD 277
Cdd:PHA02859    43 FVNDCNDLYETPIFscLEKDKVNVEILKFLIENGADVNFKTRdNNLSALHhylSFNKNVEPEILKILIDSGSSITEEDED 122
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1229385645  278 GLTPLH-----CAARSghdQVVELLLERGAPLLARTKNGLSPLHmaaqgdhvecvKHLLQHKapvDDVTLDYLTALHV 350
Cdd:PHA02859   123 GKNLLHmymcnFNVRI---NVIKLLIDSGVSFLNKDFDNNNILY-----------SYILFHS---DKKIFDFLTSLGI 183
PHA02989 PHA02989
ankyrin repeat protein; Provisional
626-770 2.81e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 48.97  E-value: 2.81e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  626 TLLNYGAETNIVTK-QGVTPLHLASQEGHTDMVTLLLDKGANI----HMSTK--SGLTSLHLAAQEDKvNVADILTKHGA 698
Cdd:PHA02989    21 FLLRTGFDVNEEYRgNSILLLYLKRKDVKIKIVKLLIDNGADVnykgYIETPlcAVLRNREITSNKIK-KIVKLLLKFGA 99
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1229385645  699 DQDAHTKLGYTPL---IVACHYGNVKMVNFLLKQGANVNA-KTKNGYTPLHQAAQQG--HTHIINVLLQHGAKPNATT 770
Cdd:PHA02989   100 DINLKTFNGVSPIvcfIYNSNINNCDMLRFLLSKGINVNDvKNSRGYNLLHMYLESFsvKKDVIKILLSFGVNLFEKT 177
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
377-497 2.93e-05

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: 49.08  E-value: 2.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  377 GFTPLHIACKKNRIKVMELLVKYGASIQAITES-------------GLTPIHVAAFMGHLNIVLLLLQNGASP---DVTN 440
Cdd:cd22197     94 GHSALHIAIEKRSLQCVKLLVENGADVHARACGrffqkkqgtcfyfGELPLSLAACTKQWDVVNYLLENPHQPaslQAQD 173
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1229385645  441 IRGETALH----MAARAGQVEVVRC-----LLRNGALVDARAREEQ-------TPLHIASRLGKTEIVQLLLQ 497
Cdd:cd22197    174 SLGNTVLHalvmIADNSPENSALVIkmydgLLQAGARLCPTVQLEEisnheglTPLKLAAKEGKIEIFRHILQ 246
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
410-440 3.31e-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: 3.31e-05
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1229385645  410 GLTPIHVAAFM-GHLNIVLLLLQNGASPDVTN 440
Cdd:pfam00023    2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
707-735 3.86e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.19  E-value: 3.86e-05
                            10        20
                    ....*....|....*....|....*....
gi 1229385645   707 GYTPLIVACHYGNVKMVNFLLKQGANVNA 735
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
68-116 4.32e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.72  E-value: 4.32e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1229385645   68 SVDSATKKGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMA 116
Cdd:pfam13857    8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
75-105 4.49e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 41.89  E-value: 4.49e-05
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1229385645   75 KGNTALHIASL-AGQAEVVKVLVKEGANINAQ 105
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNAR 32
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
277-306 4.70e-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: 4.70e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 1229385645  277 DGLTPLHCAARSGHDQVVELLLERGAPLLA 306
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
376-405 4.75e-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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 41.86  E-value: 4.75e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 1229385645  376 NGFTPLHIACKKNRIKVMELLVKYGASIQA 405
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
244-276 5.25e-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: 5.25e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1229385645  244 NGITPLHVASKR-GNTNMVKLLLDRGGQIDAKTR 276
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
707-735 5.78e-05

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 41.47  E-value: 5.78e-05
                           10        20
                   ....*....|....*....|....*....
gi 1229385645  707 GYTPLIVACHYGNVKMVNFLLKQGANVNA 735
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02859 PHA02859
ankyrin repeat protein; Provisional
90-150 5.84e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 46.35  E-value: 5.84e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1229385645   90 EVVKVLVKEGANINAQSQ-NGFTPL--YMAAQEN-HIDVVKYLLENGANQSTATEDGFTPLAVAL 150
Cdd:PHA02859    67 EILKFLIENGADVNFKTRdNNLSALhhYLSFNKNvEPEILKILIDSGSSITEEDEDGKNLLHMYM 131
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
739-768 6.07e-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: 6.07e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 1229385645  739 NGYTPLHQAAQQGHTHIINVLLQHGAKPNA 768
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
277-302 6.30e-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: 41.42  E-value: 6.30e-05
                            10        20
                    ....*....|....*....|....*.
gi 1229385645   277 DGLTPLHCAARSGHDQVVELLLERGA 302
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
575-689 6.63e-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: 6.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  575 GLTPLHVAAHYDNQKVALLLLEKGASPHATAKN--------------GYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQ 640
Cdd:cd22193     76 GQTALHIAIERRQGDIVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLSLAACTNQPDIVQYLLENEHQPADIEAQ 155
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1229385645  641 ---GVTPLHLA-----SQEGHTDMVT----LLLDKGANIH-------MSTKSGLTSLHLAAQEDKVNV 689
Cdd:cd22193    156 dsrGNTVLHALvtvadNTKENTKFVTrmydMILIRGAKLCptveleeIRNNDGLTPLQLAAKMGKIEI 223
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
691-782 6.69e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 47.94  E-value: 6.69e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  691 DILTKHGADQDAHTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATT 770
Cdd:PLN03192   542 EELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHA 621
                           90
                   ....*....|..
gi 1229385645  771 AnGNTALAIAKR 782
Cdd:PLN03192   622 A-GDLLCTAAKR 632
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
30-113 7.41e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.59  E-value: 7.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645   30 LKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKE-------GANI 102
Cdd:PTZ00322   102 LTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHsqchfelGANA 181
                           90
                   ....*....|.
gi 1229385645  103 NAQSQNGFTPL 113
Cdd:PTZ00322   182 KPDSFTGKPPS 192
PHA02795 PHA02795
ankyrin-like protein; Provisional
90-153 7.53e-05

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 47.30  E-value: 7.53e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1229385645   90 EVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQG 153
Cdd:PHA02795   202 EIYKLCIPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRG 265
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
108-134 7.62e-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: 7.62e-05
                           10        20
                   ....*....|....*....|....*...
gi 1229385645  108 NGFTPLYMAA-QENHIDVVKYLLENGAN 134
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGAD 28
PHA02736 PHA02736
Viral ankyrin protein; Provisional
430-599 7.85e-05

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 44.87  E-value: 7.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  430 LQNGASPDVTNIRGETALHMAARAGqvEVVRCLLRNGALVDARAreeqtplhiasrlgkteivQLLLQHMAHpdaattnG 509
Cdd:PHA02736     4 PEEIIFASEPDIEGENILHYLCRNG--GVTDLLAFKNAISDENR-------------------YLVLEYNRH-------G 55
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  510 YTPLHISAREGQVDVAS---VLLEAGA-AHSLATKKGFTPLHVAAKYGSLDVAKLLLQrRAAADSAGKNGL--TPLHVAA 583
Cdd:PHA02736    56 KQCVHIVSNPDKADPQEklkLLMEWGAdINGKERVFGNTPLHIAVYTQNYELATWLCN-QPGVNMEILNYAfkTPYYVAC 134
                          170
                   ....*....|....*.
gi 1229385645  584 HYDNQKVALLLLEKGA 599
Cdd:PHA02736   135 ERHDAKMMNILRAKGA 150
Ank_5 pfam13857
Ankyrin repeats (many copies);
297-351 8.02e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 8.02e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1229385645  297 LLERG-APLLARTKNGLSPLHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVA 351
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
359-667 8.12e-05

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 47.60  E-value: 8.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  359 VTKLLLDKRANPNARALNGFTPLHIACKKNRI--KVMELLVKYGASIQAITESGLTPI--HVAAFMG-HLNIVLLLLQNG 433
Cdd:PHA02716   194 ILEWLCNNGVNVNLQNNHLITPLHTYLITGNVcaSVIKKIIELGGDMDMKCVNGMSPImtYIINIDNiNPEITNIYIESL 273
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  434 ASPDVTNIRGETALHMA-ARAGQVEVVRCLLRNGALVDARAREEQTPLH--IASRLGKTEIVQLLLQHMAHPDAATTNGY 510
Cdd:PHA02716   274 DGNKVKNIPMILHSYITlARNIDISVVYSFLQPGVKLHYKDSAGRTCLHqyILRHNISTDIIKLLHEYGNDLNEPDNIGN 353
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  511 TPLHI--------------SAREGQVDVASVLLEAGAAHSLATKKGFTPLH----VAAKYGSLDVAKLLL--------QR 564
Cdd:PHA02716   354 TVLHTylsmlsvvnildpeTDNDIRLDVIQCLISLGADITAVNCLGYTPLTsyicTAQNYMYYDIIDCLIsdkvlnmvKH 433
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  565 RAAADSAGKNGLTPL---HVAAHY-----------------DNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQ---- 620
Cdd:PHA02716   434 RILQDLLIRVDDTPCiihHIIAKYniptdlytdeyepydstKIHDVYHCAIIERYNNAVCETSGMTPLHVSIISHTnani 513
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1229385645  621 -MQIASTLLNYGAETNIVTKQGVTPLHLASQE----GHTD-MVTLLLDKGANI 667
Cdd:PHA02716   514 vMDSFVYLLSIQYNINIPTKNGVTPLMLTMRNnrlsGHQWyIVKNILDKRPNV 566
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
525-608 8.63e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.59  E-value: 8.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  525 ASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHAT 604
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFEL 177

                   ....
gi 1229385645  605 AKNG 608
Cdd:PTZ00322   178 GANA 181
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
310-339 9.06e-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: 41.03  E-value: 9.06e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 1229385645   310 NGLSPLHMAAQGDHVECVKHLLQHKAPVDD 339
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02859 PHA02859
ankyrin repeat protein; Provisional
36-134 9.44e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 45.58  E-value: 9.44e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645   36 INTCNQNGLNALH--LAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLA----GQAEVVKVLVKEGANINAQSQNG 109
Cdd:PHA02859    44 VNDCNDLYETPIFscLEKDKVNVEILKFLIENGADVNFKTRDNNLSALHHYLSfnknVEPEILKILIDSGSSITEEDEDG 123
                           90       100
                   ....*....|....*....|....*..
gi 1229385645  110 FTPL--YMAAQENHIDVVKYLLENGAN 134
Cdd:PHA02859   124 KNLLhmYMCNFNVRINVIKLLIDSGVS 150
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
442-472 1.15e-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. 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: 1.15e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1229385645  442 RGETALHMAA-RAGQVEVVRCLLRNGALVDAR 472
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNAR 32
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
188-332 1.29e-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: 46.71  E-value: 1.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  188 ALLLQNDHNADVQSKMMVNRTTES---GFTPLHIAAHYGNVNVATLLLNRGAAVDFTARN--------------GITPLH 250
Cdd:cd22193     49 RILLDIAEKTDNLKRFINAEYTDEyyeGQTALHIAIERRQGDIVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLS 128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  251 VASKRGNTNMVKLLLDRGGQ-IDAKTRD--GLTPLHCAARSGHD---------QVVELLLERGAPLLA-------RTKNG 311
Cdd:cd22193    129 LAACTNQPDIVQYLLENEHQpADIEAQDsrGNTVLHALVTVADNtkentkfvtRMYDMILIRGAKLCPtveleeiRNNDG 208
                          170       180
                   ....*....|....*....|.
gi 1229385645  312 LSPLHMAAQGDHVECVKHLLQ 332
Cdd:cd22193    209 LTPLQLAAKMGKIEILKYILQ 229
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
346-373 1.33e-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. 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: 1.33e-04
                           10        20
                   ....*....|....*....|....*....
gi 1229385645  346 TALHVAA-HCGHYRVTKLLLDKRANPNAR 373
Cdd:pfam00023    4 TPLHLAAgRRGNLEIVKLLLSKGADVNAR 32
PHA02884 PHA02884
ankyrin repeat protein; Provisional
653-747 1.54e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 45.74  E-value: 1.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  653 HTDMVTLLLDKGANIH----MSTKSGLTSLHLAAQEDKVNVADILTKHGADQDAHTK-LGYTPLIVACHYGNVKMVNFLL 727
Cdd:PHA02884    45 YTDIIDAILKLGADPEapfpLSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEeAKITPLYISVLHGCLKCLEILL 124
                           90       100
                   ....*....|....*....|
gi 1229385645  728 KQGANVNAKTKNGYTPLHQA 747
Cdd:PHA02884   125 SYGADINIQTNDMVTPIELA 144
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
607-639 1.69e-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: 1.69e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1229385645  607 NGYTPLHIAAKK-NQMQIASTLLNYGAETNIVTK 639
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
607-636 2.07e-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: 2.07e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 1229385645   607 NGYTPLHIAAKKNQMQIASTLLNYGAETNI 636
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
442-471 2.13e-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: 2.13e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 1229385645   442 RGETALHMAARAGQVEVVRCLLRNGALVDA 471
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
310-341 2.14e-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: 2.14e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1229385645  310 NGLSPLHMAA-QGDHVECVKHLLQHKAPVDDVT 341
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
574-606 2.14e-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: 2.14e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1229385645  574 NGLTPLHVAA-HYDNQKVALLLLEKGASPHATAK 606
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
541-566 2.94e-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: 39.49  E-value: 2.94e-04
                            10        20
                    ....*....|....*....|....*.
gi 1229385645   541 KGFTPLHVAAKYGSLDVAKLLLQRRA 566
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
212-239 3.12e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.49  E-value: 3.12e-04
                            10        20
                    ....*....|....*....|....*...
gi 1229385645   212 GFTPLHIAAHYGNVNVATLLLNRGAAVD 239
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
108-134 3.19e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.55  E-value: 3.19e-04
                           10        20
                   ....*....|....*....|....*..
gi 1229385645  108 NGFTPLYMAAQENHIDVVKYLLENGAN 134
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGAD 27
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
376-408 3.20e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.58  E-value: 3.20e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1229385645  376 NGFTPLHIACKK-NRIKVMELLVKYGASIQAITE 408
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
137-300 3.35e-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: 3.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  137 TATEDGFTPLAVA---LQQGHNQAVAILLENDTKGKVRLP---------------ALHIAARKDDTKSAALLLQNdhNAD 198
Cdd:cd22193     24 TESSTGKTCLMKAllnLNPGTNDTIRILLDIAEKTDNLKRfinaeytdeyyegqtALHIAIERRQGDIVALLVEN--GAD 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  199 VQSK---MMVNRTTES-----GFTPLHIAAHYGNVNVATLLL-NRGAAVDFTARN--GITPLH----VASK-RGNTNMVK 262
Cdd:cd22193    102 VHAHakgRFFQPKYQGegfyfGELPLSLAACTNQPDIVQYLLeNEHQPADIEAQDsrGNTVLHalvtVADNtKENTKFVT 181
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1229385645  263 ----LLLDRGGQI-------DAKTRDGLTPLHCAARSGHDQVVELLLER 300
Cdd:cd22193    182 rmydMILIRGAKLcptveleEIRNNDGLTPLQLAAKMGKIEILKYILQR 230
PHA02736 PHA02736
Viral ankyrin protein; Provisional
639-731 3.49e-04

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 42.94  E-value: 3.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  639 KQGVTPLHLASQEGHTD---MVTLLLDKGANIH-MSTKSGLTSLHLAAQEDKVNVADILTKH-GADQDAHTKLGYTPLIV 713
Cdd:PHA02736    53 RHGKQCVHIVSNPDKADpqeKLKLLMEWGADINgKERVFGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYV 132
                           90
                   ....*....|....*...
gi 1229385645  714 ACHYGNVKMVNFLLKQGA 731
Cdd:PHA02736   133 ACERHDAKMMNILRAKGA 150
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
410-438 3.87e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.49  E-value: 3.87e-04
                            10        20
                    ....*....|....*....|....*....
gi 1229385645   410 GLTPIHVAAFMGHLNIVLLLLQNGASPDV 438
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
442-471 4.00e-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: 4.00e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1229385645  442 RGETALHMAARAGQVEVVRCLLRNGALVDA 471
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
212-239 4.05e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.19  E-value: 4.05e-04
                           10        20
                   ....*....|....*....|....*....
gi 1229385645  212 GFTPLHIAA-HYGNVNVATLLLNRGAAVD 239
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVN 30
TRPV4 cd22195
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed ...
75-136 4.60e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed broadly in neuronal and non-neuronal cells. It is activated by various stimuli, including hypo-osmolarity, warm temperature, and chemical ligands. TRPV4 acts in physiological functions such as osmoregulation and thermoregulation. It also has a role in mechanosensation in the vascular endothelium and urinary tract, and in cell barrier formation in vascular and epidermal tissues. Knockout mice studies suggested the functional importance of TRPV4 in the central nervous system, nociception, and bone formation. TRPV4 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: 411979 [Multi-domain]  Cd Length: 733  Bit Score: 45.23  E-value: 4.60e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1229385645   75 KGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGF--------------TPLYMAAQENHIDVVKYLLENGANQS 136
Cdd:cd22195    136 RGQTALHIAIERRCKHYVELLVEKGADVHAQARGRFfqpkdeggyfyfgeLPLSLAACTNQPDIVHYLTENAHKKA 211
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
343-372 6.65e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.72  E-value: 6.65e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 1229385645   343 DYLTALHVAAHCGHYRVTKLLLDKRANPNA 372
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02736 PHA02736
Viral ankyrin protein; Provisional
640-765 7.39e-04

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 42.17  E-value: 7.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  640 QGVTPLHLASQEGhtDMVTLLLDKGA----NIHMST---KSGLTSLHLAAQEDKV---NVADILTKHGADQDAH-TKLGY 708
Cdd:PHA02736    16 EGENILHYLCRNG--GVTDLLAFKNAisdeNRYLVLeynRHGKQCVHIVSNPDKAdpqEKLKLLMEWGADINGKeRVFGN 93
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1229385645  709 TPLIVACHYGNVKMVNFLLKQ-GANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAK 765
Cdd:PHA02736    94 TPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGAQ 151
Death_PIDD cd08779
Death Domain of p53-induced protein with a death domain; Death domain (DD) found in PIDD ...
1467-1540 7.43e-04

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: 40.38  E-value: 7.43e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1229385645 1467 LAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLErdgKHATDTN----LVECLTKINRMDIV 1540
Cdd:cd08779      5 LLSLAKELGEDWQKLALHLGVSYSRIQRIKRKNRDDLDEQILDMLFSWAK---TLPTSPDkvglLVTALSKSGRSDLA 79
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
75-104 8.77e-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: 8.77e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1229385645   75 KGNTALHIASLAGQAEVVKVLVKEGANINA 104
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
608-761 9.49e-04

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


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 44.08  E-value: 9.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  608 GYTPLHIAAKKNQMQIASTLLNYGAETNIVT-------KQGVT------PLHLASQEGHTDMVTLLLDKG---ANIHMST 671
Cdd:cd22197     94 GHSALHIAIEKRSLQCVKLLVENGADVHARAcgrffqkKQGTCfyfgelPLSLAACTKQWDVVNYLLENPhqpASLQAQD 173
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  672 KSGLTSLHLAaqedkVNVADiltkhgaDQDAHTKLgytplivachygNVKMVNFLLKQGANVNAKTK-------NGYTPL 744
Cdd:cd22197    174 SLGNTVLHAL-----VMIAD-------NSPENSAL------------VIKMYDGLLQAGARLCPTVQleeisnhEGLTPL 229
                          170
                   ....*....|....*..
gi 1229385645  745 HQAAQQGHTHIINVLLQ 761
Cdd:cd22197    230 KLAAKEGKIEIFRHILQ 246
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
477-506 1.10e-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: 38.04  E-value: 1.10e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1229385645  477 QTPLHIAS-RLGKTEIVQLLLQHMAHPDAAT 506
Cdd:pfam00023    3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
Death_RIP1 cd08777
Death Domain of Receptor-Interacting Protein 1; Death domain (DD) found in ...
1464-1543 1.21e-03

Death Domain of Receptor-Interacting Protein 1; Death domain (DD) found in Receptor-Interacting Protein 1 (RIP1) and related proteins. RIP kinases serve as essential sensors of cellular stress. Vertebrates contain several types containing a homologous N-terminal kinase domain and varying C-terminal domains. RIP1 harbors a C-terminal DD, which binds death receptors (DRs) including TNF receptor 1, Fas, TNF-related apoptosis-inducing ligand receptor 1 (TRAILR1), and TRAILR2. It also interacts with other DD-containing adaptor proteins such as TRADD and FADD. RIP1 plays a crucial role in determining a cell's fate, between survival or death, following exposure to stress signals. It is important in the signaling of NF-kappaB and MAPKs, and it links DR-associated signaling to reactive oxygen species (ROS) production. Abnormal RIP1 function may result in ROS accumulation affecting inflammatory responses, innate immunity, stress responses, and cell survival. 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: 260048  Cd Length: 86  Bit Score: 39.72  E-value: 1.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645 1464 EERLAYIADHLGFSWTELARELDFTEEQIHQIRIE-NPNSLQDQSHALLKYWLERDG-KHATDTNLVECLTKINRMDIVH 1541
Cdd:cd08777      2 EKHLDLLRENLGKKWKRCARRLGLTEVEIEEIDHDyERDGLKEKVHQMLEKWKMKEGsKGATVGKLAKALEGCIKSDLLV 81

                   ..
gi 1229385645 1542 LM 1543
Cdd:cd08777     82 SL 83
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
541-566 1.22e-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: 38.04  E-value: 1.22e-03
                           10        20
                   ....*....|....*....|....*..
gi 1229385645  541 KGFTPLHVAA-KYGSLDVAKLLLQRRA 566
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGA 27
PHA02946 PHA02946
ankyin-like protein; Provisional
352-604 1.35e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 43.50  E-value: 1.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  352 AHCG----HYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGH--LNI 425
Cdd:PHA02946    43 AYCGikglDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIER 122
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  426 VLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNG--ALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPD 503
Cdd:PHA02946   123 INLLVQYGAKINNSVDEEGCGPLLACTDPSERVFKKIMSIGfeARIVDKFGKNHIHRHLMSDNPKASTISWMMKLGISPS 202
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  504 AATTNGYTPLHI--SAREGQVDVASVLLEAGAAHSlATKKGFTPLHVAAKYGSLD--VAKLLLQRRAAADSAgkngltpL 579
Cdd:PHA02946   203 KPDHDGNTPLHIvcSKTVKNVDIINLLLPSTDVNK-QNKFGDSPLTLLIKTLSPAhlINKLLSTSNVITDQT-------V 274
                          250       260
                   ....*....|....*....|....*
gi 1229385645  580 HVAAHYDNQKVALLLLEKGASPHAT 604
Cdd:PHA02946   275 NICIFYDRDDVLEIINDKGKQYDST 299
PHA02884 PHA02884
ankyrin repeat protein; Provisional
593-681 1.49e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 42.66  E-value: 1.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  593 LLLEKGASP---HATAKNGYT-PLHIAAKKNQMQIASTLLNYGAETNIVTKQGV-TPLHLASQEGHTDMVTLLLDKGANI 667
Cdd:PHA02884    51 AILKLGADPeapFPLSENSKTnPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLHGCLKCLEILLSYGADI 130
                           90
                   ....*....|....
gi 1229385645  668 HMSTKSGLTSLHLA 681
Cdd:PHA02884   131 NIQTNDMVTPIELA 144
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
608-761 1.52e-03

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 43.25  E-value: 1.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  608 GYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQ--------------GVTPLHLASQEGHTDMVTLLLD---KGANIHMS 670
Cdd:cd22193     76 GQTALHIAIERRQGDIVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLSLAACTNQPDIVQYLLEnehQPADIEAQ 155
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  671 TKSGLTSLHLAaqedkVNVADiltkhgaDQDAHTKLgytplivachygNVKMVNFLLKQGANVNAKTK-------NGYTP 743
Cdd:cd22193    156 DSRGNTVLHAL-----VTVAD-------NTKENTKF------------VTRMYDMILIRGAKLCPTVEleeirnnDGLTP 211
                          170
                   ....*....|....*...
gi 1229385645  744 LHQAAQQGHTHIINVLLQ 761
Cdd:cd22193    212 LQLAAKMGKIEILKYILQ 229
Death_MyD88 cd08312
Death domain of Myeloid Differentation primary response protein MyD88; Death Domain (DD) of ...
1478-1541 1.55e-03

Death domain of Myeloid Differentation primary response protein MyD88; Death Domain (DD) of Myeloid Differentiation primary response protein 88 (MyD88). MyD88 is an adaptor protein involved in interleukin-1 receptor (IL-1R)- and Toll-like receptor (TLR)-induced activation of nuclear factor-kappaB (NF-kB) and mitogen activated protein kinase pathways that lead to the induction of proinflammatory cytokines. It is a key component in the signaling pathway of pathogen recognition in the innate immune system. MyD88 contains an N-terminal DD and a C-terminal Toll/IL-1 Receptor (TIR) homology domain that mediates interaction with TLRs and IL-1R. 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: 260026  Cd Length: 79  Bit Score: 39.12  E-value: 1.55e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1229385645 1478 WTELARELDFTEEQIHQIRIENpnslqDQSHALLKYWLERDgKHATDTNLVECLTKINRMDIVH 1541
Cdd:cd08312     19 WRGLAELMGFDYLEIRNFERQS-----SPTERLLEDWETRP-PGATVGNLLEILEELERKDVLE 76
PHA02859 PHA02859
ankyrin repeat protein; Provisional
610-743 1.57e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 41.73  E-value: 1.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  610 TPLH--IAAKKNQMQIASTLLNYGAETNIVTK-QGVTPLH--LASQEG-HTDMVTLLLDKGANIHMSTKSGLTSLH--LA 681
Cdd:PHA02859    53 TPIFscLEKDKVNVEILKFLIENGADVNFKTRdNNLSALHhyLSFNKNvEPEILKILIDSGSSITEEDEDGKNLLHmyMC 132
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1229385645  682 AQEDKVNVADILTKHGA-----DQDAHTKLgYTPLIvacHYGNVKMVNFLLKQGANVNAKTKNGYTP 743
Cdd:PHA02859   133 NFNVRINVIKLLIDSGVsflnkDFDNNNIL-YSYIL---FHSDKKIFDFLTSLGIDINETNKSGYNC 195
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
574-603 1.61e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.57  E-value: 1.61e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 1229385645   574 NGLTPLHVAAHYDNQKVALLLLEKGASPHA 603
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
244-273 1.76e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.62  E-value: 1.76e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1229385645  244 NGITPLHVASKRGNTNMVKLLLDRGGQIDA 273
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
410-438 1.83e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.24  E-value: 1.83e-03
                           10        20
                   ....*....|....*....|....*....
gi 1229385645  410 GLTPIHVAAFMGHLNIVLLLLQNGASPDV 438
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02736 PHA02736
Viral ankyrin protein; Provisional
361-438 1.98e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 40.63  E-value: 1.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  361 KLLLDKRANPNAR-ALNGFTPLHIACKKNRIKVMELLVKY-GASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDV 438
Cdd:PHA02736    75 KLLMEWGADINGKeRVFGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGAQCKV 154
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
212-239 1.98e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.24  E-value: 1.98e-03
                           10        20
                   ....*....|....*....|....*...
gi 1229385645  212 GFTPLHIAAHYGNVNVATLLLNRGAAVD 239
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADIN 29
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
335-464 2.03e-03

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 42.86  E-value: 2.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  335 APVDDVTLDYLTALHVAAH--CGHYrvTKLLLDKRANPNARALNGF--------------TPLHIACKKNRIKVMELLVK 398
Cdd:cd22193     67 AEYTDEYYEGQTALHIAIErrQGDI--VALLVENGADVHAHAKGRFfqpkyqgegfyfgeLPLSLAACTNQPDIVQYLLE 144
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  399 YG---ASIQAITESGLTPIH----VA-------AFMGHLNIVLLLLQNGASPDV-----TNIRGETALHMAARAGQVEVV 459
Cdd:cd22193    145 NEhqpADIEAQDSRGNTVLHalvtVAdntkentKFVTRMYDMILIRGAKLCPTVeleeiRNNDGLTPLQLAAKMGKIEIL 224

                   ....*
gi 1229385645  460 RCLLR 464
Cdd:cd22193    225 KYILQ 229
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
541-569 2.04e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.24  E-value: 2.04e-03
                           10        20
                   ....*....|....*....|....*....
gi 1229385645  541 KGFTPLHVAAKYGSLDVAKLLLQRRAAAD 569
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
607-636 2.25e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.24  E-value: 2.25e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1229385645  607 NGYTPLHIAAKKNQMQIASTLLNYGAETNI 636
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02989 PHA02989
ankyrin repeat protein; Provisional
216-463 2.33e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 42.81  E-value: 2.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  216 LHIAAHYGNVNVATLLLNRGAAVDFtaRNGI-TPL-------HVASKRGNtNMVKLLLDRGGQIDAKTRDGLTPLHCAAR 287
Cdd:PHA02989    41 LYLKRKDVKIKIVKLLIDNGADVNY--KGYIeTPLcavlrnrEITSNKIK-KIVKLLLKFGADINLKTFNGVSPIVCFIY 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  288 SGH---DQVVELLLERGAPLLArTKN--GLSPLHMAAQGDHV--ECVKHLLQHKA-PVDDVTLDYLTALHV----AAHCG 355
Cdd:PHA02989   118 NSNinnCDMLRFLLSKGINVND-VKNsrGYNLLHMYLESFSVkkDVIKILLSFGVnLFEKTSLYGLTPMNIylrnDIDVI 196
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  356 HYRVTKLLLDKRA---NPNAR---ALNGFTPLHIACKKNRIKVMELLVKYgASIQAITESGLTPIHVAAFMGHLNIVLLL 429
Cdd:PHA02989   197 SIKVIKYLIKKGVnieTNNNGsesVLESFLDNNKILSKKEFKVLNFILKY-IKINKKDKKGFNPLLISAKVDNYEAFNYL 275
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1229385645  430 LQNGASPDVTNIRGETALHMAARAGQVEVVRCLL 463
Cdd:PHA02989   276 LKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNRIL 309
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
140-300 2.47e-03

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


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 42.87  E-value: 2.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  140 EDGFTPLAVA---LQQGHNQAVAILLE------------------NDTKGKVrlpALHIAARKDDTKSAALLLQN--DHN 196
Cdd:cd22196     45 ETGKTCLLKAmlnLHNGQNDTISLLLDiaektgnlkefvnaaytdSYYKGQT---ALHIAIERRNMHLVELLVQNgaDVH 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  197 ADVQSKMMVNRTTESGF----TPLHIAAHYGNVNVATLLL-NRGAAVDFTARN--GITPLH---------VASKRGNTNM 260
Cdd:cd22196    122 ARASGEFFKKKKGGPGFyfgeLPLSLAACTNQLDIVKFLLeNPHSPADISARDsmGNTVLHalvevadntPENTKFVTKM 201
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1229385645  261 VKLLLDRGGQIDAK-------TRDGLTPLHCAARSGHDQVVELLLER 300
Cdd:cd22196    202 YNEILILGAKIRPLlkleeitNKKGLTPLKLAAKTGKIGIFAYILGR 248
Death_TNFR1 cd08313
Death domain of Tumor Necrosis Factor Receptor 1; Death Domain (DD) found in tumor necrosis ...
1478-1544 2.67e-03

Death domain of Tumor Necrosis Factor Receptor 1; Death Domain (DD) found in tumor necrosis factor receptor-1 (TNFR-1). TNFR-1 has many names including TNFRSF1A, CD120a, p55, p60, and TNFR60. It activates two major intracellular signaling pathways that lead to the activation of the transcription factor NF-kB and the induction of cell death. Upon binding of its ligand TNF, TNFR-1 trimerizes which leads to the recruitment of an adaptor protein named TNFR-associated death domain protein (TRADD) through a DD/DD interaction. Mutations in the TNFRSF1A gene causes TNFR-associated periodic syndrome (TRAPS), a rare disorder characterized recurrent fever, myalgia, abdominal pain, conjunctivitis and skin eruptions. 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: 176729  Cd Length: 80  Bit Score: 38.52  E-value: 2.67e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1229385645 1478 WTELARELDFTEEQIHQIRIENpNSLQDQSHALLKYWLERDGKHATDTNLVECltKINRMDIVHLME 1544
Cdd:cd08313     14 WKEFVRRLGLSDNEIERVELDH-RRCRDAQYQMLKVWKERGPRPYATLQHLLS--VLRDMELVGCAE 77
PHA02791 PHA02791
ankyrin-like protein; Provisional
375-530 2.71e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 41.95  E-value: 2.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  375 LNGFTPLHIACKKNRIKVMELLVKYGAsIQAITESGLtPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAG 454
Cdd:PHA02791    28 VHGHSALYYAIADNNVRLVCTLLNAGA-LKNLLENEF-PLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSG 105
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1229385645  455 QVEVVRCLL-RNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHP-DAATTngYTPLHISAREGQVDVASVLLE 530
Cdd:PHA02791   106 NMQTVKLFVkKNWRLMFYGKTGWKTSFYHAVMLNDVSIVSYFLSEIPSTfDLAIL--LSCIHITIKNGHVDMMILLLD 181
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
343-372 2.94e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.85  E-value: 2.94e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1229385645  343 DYLTALHVAAHCGHYRVTKLLLDKRANPNA 372
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
187-332 2.94e-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: 42.53  E-value: 2.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  187 AALLLQNDHNADVQSKMMVNRTTES---------------GFTPLHIAAHYGNVNVATLLLNRGAAV------DFTARN- 244
Cdd:cd22197     54 AVLNLQDGVNACIMPLLEIDKDSGNpkplvnaqctdeyyrGHSALHIAIEKRSLQCVKLLVENGADVharacgRFFQKKq 133
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  245 ------GITPLHVASKRGNTNMVKLLLDRGGQIDA-KTRDGL--TPLHCAARSGHDQ------VVEL---LLERGAPLLA 306
Cdd:cd22197    134 gtcfyfGELPLSLAACTKQWDVVNYLLENPHQPASlQAQDSLgnTVLHALVMIADNSpensalVIKMydgLLQAGARLCP 213
                          170       180       190
                   ....*....|....*....|....*....|...
gi 1229385645  307 RTK-------NGLSPLHMAAQGDHVECVKHLLQ 332
Cdd:cd22197    214 TVQleeisnhEGLTPLKLAAKEGKIEIFRHILQ 246
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
641-669 2.97e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.85  E-value: 2.97e-03
                           10        20
                   ....*....|....*....|....*....
gi 1229385645  641 GVTPLHLASQEGHTDMVTLLLDKGANIHM 669
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02791 PHA02791
ankyrin-like protein; Provisional
47-196 3.20e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 41.57  E-value: 3.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645   47 LHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGF-TPLYMAAQENHIDVV 125
Cdd:PHA02791    65 LHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTGWkTSFYHAVMLNDVSIV 144
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1229385645  126 KYLLengaNQSTATEDGFTPLA---VALQQGHNQAVAILLE-----NDTKGKVRLPALHIAARKDDTKSAALLLQNDHN 196
Cdd:PHA02791   145 SYFL----SEIPSTFDLAILLScihITIKNGHVDMMILLLDymtstNTNNSLLFIPDIKLAIDNKDLEMLQALFKYDIN 219
PHA02859 PHA02859
ankyrin repeat protein; Provisional
708-777 3.65e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 40.96  E-value: 3.65e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1229385645  708 YTPLIVAC---HYGNVKMVNFLLKQGANVNAKTK-NGYTPLH---QAAQQGHTHIINVLLQHGAKPNATTANGNTAL 777
Cdd:PHA02859    51 YETPIFSClekDKVNVEILKFLIENGADVNFKTRdNNLSALHhylSFNKNVEPEILKILIDSGSSITEEDEDGKNLL 127
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
508-533 3.86e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.41  E-value: 3.86e-03
                            10        20
                    ....*....|....*....|....*.
gi 1229385645   508 NGYTPLHISAREGQVDVASVLLEAGA 533
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
PHA02736 PHA02736
Viral ankyrin protein; Provisional
40-133 4.10e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 39.86  E-value: 4.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645   40 NQNGLNALHLAAKEGHVGLVQE---LLGRGSSVDSATKK-GNTALHIASLAGQAEVVKVLVKE-GANINAQSQNGFTPLY 114
Cdd:PHA02736    52 NRHGKQCVHIVSNPDKADPQEKlklLMEWGADINGKERVfGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYY 131
                           90
                   ....*....|....*....
gi 1229385645  115 MAAQENHIDVVKYLLENGA 133
Cdd:PHA02736   132 VACERHDAKMMNILRAKGA 150
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
42-74 4.51e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.50  E-value: 4.51e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1229385645   42 NGLNALHLAA-KEGHVGLVQELLGRGSSVDSATK 74
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA02791 PHA02791
ankyrin-like protein; Provisional
607-777 4.56e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 41.18  E-value: 4.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  607 NGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQgvTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDK 686
Cdd:PHA02791    29 HGHSALYYAIADNNVRLVCTLLNAGALKNLLENE--FPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGN 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  687 VNVADILTKHGADQDAHTKLGY-TPLIVACHYGNVKMVNFLLKQGANvNAKTKNGYTPLHQAAQQGHTHIINVLLQHgak 765
Cdd:PHA02791   107 MQTVKLFVKKNWRLMFYGKTGWkTSFYHAVMLNDVSIVSYFLSEIPS-TFDLAILLSCIHITIKNGHVDMMILLLDY--- 182
                          170
                   ....*....|..
gi 1229385645  766 pnATTANGNTAL 777
Cdd:PHA02791   183 --MTSTNTNNSL 192
PHA03095 PHA03095
ankyrin-like protein; Provisional
720-777 5.02e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 41.55  E-value: 5.02e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1229385645  720 VKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGH---THIINVLLQHGAKPNATTANGNTAL 777
Cdd:PHA03095    27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPL 87
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
42-70 5.14e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.03  E-value: 5.14e-03
                            10        20
                    ....*....|....*....|....*....
gi 1229385645    42 NGLNALHLAAKEGHVGLVQELLGRGSSVD 70
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
575-689 5.38e-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: 41.76  E-value: 5.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  575 GLTPLHVAAHYDNQKVALLLLEKGASPHATA------KN-------GYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQ- 640
Cdd:cd22197     94 GHSALHIAIEKRSLQCVKLLVENGADVHARAcgrffqKKqgtcfyfGELPLSLAACTKQWDVVNYLLENPHQPASLQAQd 173
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1229385645  641 --GVTPLHLA-----SQEGHTDMVTL----LLDKGANI-------HMSTKSGLTSLHLAAQEDKVNV 689
Cdd:cd22197    174 slGNTVLHALvmiadNSPENSALVIKmydgLLQAGARLcptvqleEISNHEGLTPLKLAAKEGKIEI 240
Death_FAS_TNFRSF6 cd08316
Death domain of FAS or TNF receptor superfamily member 6; Death Domain (DD) found in the ...
1463-1541 6.20e-03

Death domain of FAS or TNF receptor superfamily member 6; Death Domain (DD) found in the FS7-associated cell surface antigen (FAS). FAS, also known as TNFRSF6 (TNF receptor superfamily member 6), APT1, CD95, FAS1, or APO-1, together with FADD (Fas-associating via Death Domain) and caspase 8, is an integral part of the death inducing signalling complex (DISC), which plays an important role in the induction of apoptosis and is activated by binding of the ligand FasL to FAS. FAS also plays a critical role in self-tolerance by eliminating cell types (autoreactive T and B cells) that contribute to autoimmunity. 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: 260028  Cd Length: 94  Bit Score: 37.66  E-value: 6.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645 1463 IEERLAYIADHLGfsWTE---LARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINR--- 1536
Cdd:cd08316      4 LSKHIPDIAEIMG--WKDvkkFARKSGISETKIDEIQLDNPNDTAEQKVQLLRAWYQKHGKKGAYRTLIKTLRKAGKrak 81

                   ....*....
gi 1229385645 1537 ----MDIVH 1541
Cdd:cd08316     82 adkiQDIIK 90
PHA02859 PHA02859
ankyrin repeat protein; Provisional
359-436 6.26e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 40.19  E-value: 6.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  359 VTKLLLDKRANPNARAL-NGFTPLH--IACKKN-RIKVMELLVKYGASIQAITESGLTPIHV--AAFMGHLNIVLLLLQN 432
Cdd:PHA02859    68 ILKFLIENGADVNFKTRdNNLSALHhyLSFNKNvEPEILKILIDSGSSITEEDEDGKNLLHMymCNFNVRINVIKLLIDS 147

                   ....
gi 1229385645  433 GASP 436
Cdd:PHA02859   148 GVSF 151
PHA02884 PHA02884
ankyrin repeat protein; Provisional
214-287 7.61e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 40.35  E-value: 7.61e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1229385645  214 TPLHIAAHYGNVNVATLLLNRGAAVD-FTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAAR 287
Cdd:PHA02884    72 NPLIYAIDCDNDDAAKLLIRYGADVNrYAEEAKITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELALM 146
PHA02859 PHA02859
ankyrin repeat protein; Provisional
511-647 7.73e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 39.80  E-value: 7.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  511 TPLH--ISAREGQVDVASVLLEAGAAHSLATK-KGFTPLHVAAKYG---SLDVAKLLLQRRAAADSAGKNGLTPLHVaaH 584
Cdd:PHA02859    53 TPIFscLEKDKVNVEILKFLIENGADVNFKTRdNNLSALHHYLSFNknvEPEILKILIDSGSSITEEDEDGKNLLHM--Y 130
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1229385645  585 YDNQKVAL----LLLEKGASPHATAKNGYTPLH--IAAKKNQmQIASTLLNYGAETNIVTKQGVTPLHL 647
Cdd:PHA02859   131 MCNFNVRInvikLLIDSGVSFLNKDFDNNNILYsyILFHSDK-KIFDFLTSLGIDINETNKSGYNCYDL 198
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
606-792 8.03e-03

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 41.05  E-value: 8.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  606 KNGYTPLH--IAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGH--TDMVTLLLDKGANIHMSTKSGLTSLhLA 681
Cdd:PHA02716   175 KTGYGILHayLGNMYVDIDILEWLCNNGVNVNLQNNHLITPLHTYLITGNvcASVIKKIIELGGDMDMKCVNGMSPI-MT 253
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  682 AQEDKVNVADILTKHGADQDAHTKLGYTPLIVACH-----YGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGH--TH 754
Cdd:PHA02716   254 YIINIDNINPEITNIYIESLDGNKVKNIPMILHSYitlarNIDISVVYSFLQPGVKLHYKDSAGRTCLHQYILRHNisTD 333
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1229385645  755 IINVLLQHGAKPNATTANGNTALaiAKRLGYISVVDTL 792
Cdd:PHA02716   334 IIKLLHEYGNDLNEPDNIGNTVL--HTYLSMLSVVNIL 369
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
346-464 9.75e-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: 40.61  E-value: 9.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385645  346 TALHVAAHCGHYRVTKLLLDKRANPNARALNGF-------------TPLHIACKKNRIKVMELLVKYG---ASIQAITES 409
Cdd:cd22197     96 SALHIAIEKRSLQCVKLLVENGADVHARACGRFfqkkqgtcfyfgeLPLSLAACTKQWDVVNYLLENPhqpASLQAQDSL 175
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1229385645  410 GLTPIHVAAFMG---HLNIVLL------LLQNGASPD-------VTNIRGETALHMAARAGQVEVVRCLLR 464
Cdd:cd22197    176 GNTVLHALVMIAdnsPENSALVikmydgLLQAGARLCptvqleeISNHEGLTPLKLAAKEGKIEIFRHILQ 246
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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