NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1229385538|ref|NP_001341206|]
View 

ankyrin-2 isoform 44 [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
UPA_2 super family cl39303
UPA domain; The UPA domain is conserved in UNC5, PIDD, and Ankyrins. It has a beta sandwich ...
 1196-1325 2.59e-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: 202.70  E-value: 2.59e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538 1196 VPYMAKFVVFAKSHDPIEARLRCFCMTDDKVDKTLEQQENFAEVARSRDVEVLEGKPIYVDCFGNLVPLTKSGQHHIFSF 1275
Cdd:pfam17809    1 VPYLAKFVVFAKRYDPGEARLRCACMTDDGEDKTLEFHEGFTEVARSRDVEVLEGSPVSIELSGNLVPIKKKSQSRQMDF 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1229385538 1276 FAFKENRLPLFVKVRDTTQEPCGRLSFMKEPKSTRGLVHQAICNLNITLP 1325
Cdd:pfam17809   81 KAFRENRLDGSVRVKDPSDPPKGLLSFMRDAKVDGGTVSQPLCTLNIVLP 130
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
454-719 3.76e-59

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 205.96  E-value: 3.76e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  454 LLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHATAKN 533
Cdd:COG0666      7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  534 GYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKV 613
Cdd:COG0666     87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  614 NVADILTKHGADQDAHTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPN 693
Cdd:COG0666    167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246

                          250       260
                   ....*....|....*....|....*.
gi 1229385538  694 ATTANGNTALAIAKRLGYISVVDTLK 719
Cdd:COG0666    247 AKDKDGLTALLLAAAAGAALIVKLLL 272
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
217-505 1.24e-58

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 204.42  E-value: 1.24e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  217 VNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAPL 296
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  297 LARTKNGLSPLHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNARALRGETALHMA 376
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  377 ARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLE 456
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1229385538  457 AGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPL 505
Cdd:COG0666    241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
5-340 9.25e-54

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 190.55  E-value: 9.25e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538    5 LQKSDSNASFLRAARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIAS 84
Cdd:COG0666     16 LLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAA 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538   85 LAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGAnqstatedgftplavalqqghnqavaillen 164
Cdd:COG0666     96 RNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGA------------------------------- 144

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  165 dtkgkvrlpalhiaarkddtksaalllqndhNADVQSKSGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVA 244
Cdd:COG0666    145 -------------------------------DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLA 193

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  245 SKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLLQ 324
Cdd:COG0666    194 AENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLL 273

                          330
                   ....*....|....*.
gi 1229385538  325 HKAPVDDVTLDYLTAL 340
Cdd:COG0666    274 ALLLLAAALLDLLTLL 289
Death_ank2 cd08804
Death domain of Ankyrin-2; Death Domain (DD) of Ankyrin-2 (ANK-2) and related proteins. ...
 1354-1437 1.83e-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: 175.66  E-value: 1.83e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538 1354 ERIEERLAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIV 1433
Cdd:cd08804      1 ERTEERLAHIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLTQCLTKINRMDIV 80


                   ....
gi 1229385538 1434 HLME 1437
Cdd:cd08804     81 HLME 84
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
 871-975 2.80e-50

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


:

Pssm-ID: 128514  Cd Length: 104  Bit Score: 172.92  E-value: 2.80e-50
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538   871 SGFLVSFMVDARGGAMRGCRhNGLRIIIPPRKCTAPTRVTCRLVKRHRLATMPPMVEGEGLASRLIEVGPSGAQFLGPVI 950
Cdd:smart00218    1 PSFLVSGTFDARGGRLRGPR-TGVRLIIPPGAIPQGTRYTCYLVVHKTLSTPPPLEEGETLLSPVVECGPHGALFLRPVI 79

                            90       100
                    ....*....|....*....|....*
gi 1229385538   951 VEIPHFAALRGKERELVVLRSENGD 975
Cdd:smart00218   80 LEVPHCASLRPRDWEIVLLRSENGG 104
NESP55 super family cl25759
Neuroendocrine-specific golgi protein P55 (NESP55); This family consists of several mammalian ...
 1510-1667 1.76e-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: 1.76e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538 1510 TFQDGVPKTEGDSSATALFPQTHKEQVQQDFSGKMQDLPEESSLEYQQEYFVTTPGTET-------SETQKAMIVPSSPS 1582
Cdd:pfam06390   62 SFLNAHHRSAAAAAAAQVFPEPSEPESDHEDEDFEPELARPECLEYDEDDFDTETDSETepesdieSETEFETEPETEPD 141

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538 1583 KTPE-EVSTPAEEEK--------------------LYLQTPTSSERGGSPIIQEPEEPSEHRE------ESSPR--KTSL 1633
Cdd:pfam06390  142 TAPTtEPETEPEDEPgpvvpkgatfhqslterlhaLKLQSADASPRRAPPSTQEPESAREGEEpergplDKDPRdpEEEE 221

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1229385538 1634 VIVESADNQPETCErldEDAAFEKGDDMPEIPPE 1667
Cdd:pfam06390  222 EEKEEEKQQPHRCK---PKKPARRRDPSPESPPK 252
Ank_4 pfam13637
Ankyrin repeats (many copies);
111-162 3.02e-07

Ankyrin repeats (many copies);


:

Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.81  E-value: 3.02e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1229385538  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 ...
 1196-1325 2.59e-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: 202.70  E-value: 2.59e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538 1196 VPYMAKFVVFAKSHDPIEARLRCFCMTDDKVDKTLEQQENFAEVARSRDVEVLEGKPIYVDCFGNLVPLTKSGQHHIFSF 1275
Cdd:pfam17809    1 VPYLAKFVVFAKRYDPGEARLRCACMTDDGEDKTLEFHEGFTEVARSRDVEVLEGSPVSIELSGNLVPIKKKSQSRQMDF 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1229385538 1276 FAFKENRLPLFVKVRDTTQEPCGRLSFMKEPKSTRGLVHQAICNLNITLP 1325
Cdd:pfam17809   81 KAFRENRLDGSVRVKDPSDPPKGLLSFMRDAKVDGGTVSQPLCTLNIVLP 130
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
454-719 3.76e-59

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 205.96  E-value: 3.76e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  454 LLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHATAKN 533
Cdd:COG0666      7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  534 GYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKV 613
Cdd:COG0666     87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  614 NVADILTKHGADQDAHTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPN 693
Cdd:COG0666    167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246

                          250       260
                   ....*....|....*....|....*.
gi 1229385538  694 ATTANGNTALAIAKRLGYISVVDTLK 719
Cdd:COG0666    247 AKDKDGLTALLLAAAAGAALIVKLLL 272
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
217-505 1.24e-58

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 204.42  E-value: 1.24e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  217 VNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAPL 296
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  297 LARTKNGLSPLHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNARALRGETALHMA 376
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  377 ARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLE 456
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1229385538  457 AGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPL 505
Cdd:COG0666    241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
5-340 9.25e-54

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 190.55  E-value: 9.25e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538    5 LQKSDSNASFLRAARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIAS 84
Cdd:COG0666     16 LLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAA 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538   85 LAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGAnqstatedgftplavalqqghnqavaillen 164
Cdd:COG0666     96 RNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGA------------------------------- 144

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  165 dtkgkvrlpalhiaarkddtksaalllqndhNADVQSKSGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVA 244
Cdd:COG0666    145 -------------------------------DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLA 193

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  245 SKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLLQ 324
Cdd:COG0666    194 AENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLL 273

                          330
                   ....*....|....*.
gi 1229385538  325 HKAPVDDVTLDYLTAL 340
Cdd:COG0666    274 ALLLLAAALLDLLTLL 289
Death_ank2 cd08804
Death domain of Ankyrin-2; Death Domain (DD) of Ankyrin-2 (ANK-2) and related proteins. ...
 1354-1437 1.83e-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: 175.66  E-value: 1.83e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538 1354 ERIEERLAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIV 1433
Cdd:cd08804      1 ERTEERLAHIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLTQCLTKINRMDIV 80


                   ....
gi 1229385538 1434 HLME 1437
Cdd:cd08804     81 HLME 84
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
 871-975 2.80e-50

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


Pssm-ID: 128514  Cd Length: 104  Bit Score: 172.92  E-value: 2.80e-50
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538   871 SGFLVSFMVDARGGAMRGCRhNGLRIIIPPRKCTAPTRVTCRLVKRHRLATMPPMVEGEGLASRLIEVGPSGAQFLGPVI 950
Cdd:smart00218    1 PSFLVSGTFDARGGRLRGPR-TGVRLIIPPGAIPQGTRYTCYLVVHKTLSTPPPLEEGETLLSPVVECGPHGALFLRPVI 79

                            90       100
                    ....*....|....*....|....*
gi 1229385538   951 VEIPHFAALRGKERELVVLRSENGD 975
Cdd:smart00218   80 LEVPHCASLRPRDWEIVLLRSENGG 104
ZU5 pfam00791
ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.
 875-972 5.46e-41

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


Pssm-ID: 459941  Cd Length: 97  Bit Score: 146.13  E-value: 5.46e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  875 VSFMVDARGGAMRGCrHNGLRIIIPPRKCTAPTRVTCRLVKRHRLATMPPMVEGEGLASRLIEVGPSGAQFLGPVIVEIP 954
Cdd:pfam00791    1 VSGLVDSRGGRLVLP-NSGVSLLIPPGAIPEGTRIECYLAVNRDESSRPPLEEGETLLSPVVECGPPGLKFLKPVILEVP 79

                           90
                   ....*....|....*...
gi 1229385538  955 HFAALRGKERELVVLRSE 972
Cdd:pfam00791   80 HCASLRPEEWEIVLKRSD 97
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 466-690 2.99e-40

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 155.21  E-value: 2.99e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  466 KKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHY-----DNQKVALLLLEKGASPHATAKNGYTPLHI 540
Cdd:PHA03100    33 KKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIkynltDVKEIVKLLLEYGANVNAPDNNGITPLLY 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  541 AA--KKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTD--MVTLLLDKGANIhmstksgltslhlaaqeDKVNVA 616
Cdd:PHA03100   113 AIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDI-----------------NAKNRV 175

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1229385538  617 DILTKHGADQDAHTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGA 690
Cdd:PHA03100   176 NYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 219-559 8.10e-33

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 137.50  E-value: 8.10e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  219 VATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAPLla 298
Cdd:PHA02876   160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNI-- 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  299 rTKNGLSPLHmAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHY-RVTKLLLDKRANPNARALRGETALHMAA 377
Cdd:PHA02876   238 -NKNDLSLLK-AIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMA 315

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  378 RAG-QVEVVRCLLRNGALVDARAREEQTPLHIASRLGK-TEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLL 455
Cdd:PHA02876   316 KNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLDRnKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLL 395

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  456 EAGAAHSLATKKGFTPLHVAAkYGS--LDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQ-KVALLLLEKGASPHATAK 532
Cdd:PHA02876   396 DYGADIEALSQKIGTALHFAL-CGTnpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAINI 474

                          330       340
                   ....*....|....*....|....*..
gi 1229385538  533 NGYTPLHIAAKKNqmQIASTLLNYGAE 559
Cdd:PHA02876   475 QNQYPLLIALEYH--GIVNILLHYGAE 499
PHA03095 PHA03095
ankyrin-like protein; Provisional
 8-327 4.53e-29

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 123.21  E-value: 4.53e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538    8 SDSNASFLRAARAGN--LDKVVEYLKGGIDINTCNQNGLNALHLAAKEGH---VGLVQELLGRGSSVDSATKKGNTALHI 82
Cdd:PHA03095    10 IMEAALYDYLLNASNvtVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHL 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538   83 -ASLAGQAEVVKVLVKEGANINAQSQNGFTPL--YMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQgHNQAVA 159
Cdd:PHA03095    90 yLYNATTLDVIKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKS-RNANVE 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  160 I---LLEND----TKGKVRLPALHIAAR--KDDTKSAALLLQNDHNADVQSKSGFTPLHIAAHYG---NVNVATLLLNrG 227
Cdd:PHA03095   169 LlrlLIDAGadvyAVDDRFRSLLHHHLQsfKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSsckRSLVLPLLIA-G 247

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  228 AAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAP--LLARTKNGLS 305
Cdd:PHA03095   248 ISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSaeTVAATLNTAS 327

                          330       340
                   ....*....|....*....|...
gi 1229385538  306 PLHMAAQGDHV-ECVKHLLQHKA 327
Cdd:PHA03095   328 VAGGDIPSDATrLCVAKVVLRGA 350
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
 1353-1438 8.94e-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: 96.71  E-value: 8.94e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  1353 QERIEERLAYIADH-LGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMD 1431
Cdd:smart00005    1 PELTRQKLAKLLDHpLGLDWRELARKLGLSEADIDQIRTEAPRDLAEQSVQLLRLWEQREGKNATLGTLLEALRKMGRDD 80


                    ....*..
gi 1229385538  1432 IVHLMET 1438
Cdd:smart00005   81 AVELLRS 87
Ank_2 pfam12796
Ankyrin repeats (3 copies);
47-134 1.80e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 95.95  E-value: 1.80e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538   47 LHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEgANINAQSqNGFTPLYMAAQENHIDVVK 126
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78


                   ....*...
gi 1229385538  127 YLLENGAN 134
Cdd:pfam12796   79 LLLEKGAD 86
Ank_2 pfam12796
Ankyrin repeats (3 copies);
208-294 2.85e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 95.57  E-value: 2.85e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  208 LHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRgGQIDAKTrDGLTPLHCAARSGHDQVVE 287
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78


                   ....*..
gi 1229385538  288 LLLERGA 294
Cdd:pfam12796   79 LLLEKGA 85
Death pfam00531
Death domain;
1357-1437 2.31e-21

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 89.73  E-value: 2.31e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538 1357 EERLAYIADH---LGFSWTELARELDFTEEQIHQIRIENPNsLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIV 1433
Cdd:pfam00531    1 RKQLDRLLDPpppLGKDWRELARKLGLSENEIDEIESENPR-LRSQTYELLRLWEQREGKNATVGTLLEALRKLGRRDAA 79


                   ....
gi 1229385538 1434 HLME 1437
Cdd:pfam00531   80 EKIQ 83
Ank_2 pfam12796
Ankyrin repeats (3 copies);
604-695 4.31e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.40  E-value: 4.31e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  604 LHLAAQEDKVNVADILTKHGADQDAHTKLGYTPLIVACHYGNVKMVNFLLKQgANVNAKTkNGYTPLHQAAQQGHTHIIN 683
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 1229385538  684 VLLQHGAKPNAT 695
Cdd:pfam12796   79 LLLEKGADINVK 90
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 460-654 3.41e-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: 3.41e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  460 AHSLATKKGF-TPLHVAAKYGSLD-VAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEkgASPH-----ATAK 532
Cdd:cd22192      8 LHLLQQKRISeSPLLLAAKENDVQaIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPElvnepMTSD 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  533 --NGYTPLHIAAKKNQMQIASTLLNYGAEtniVTKQGVT-----------------PLHLASQEGHTDMVTLLLDKGANI 593
Cdd:cd22192     86 lyQGETALHIAVVNQNLNLVRELIARGAD---VVSPRATgtffrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADI 162

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1229385538  594 HMSTKSGLTSLH-LAAQEDKV---NVADILTKHGADQDAHT------KLGYTPLIVACHYGNVKMVNFLLK 654
Cdd:cd22192    163 RAQDSLGNTVLHiLVLQPNKTfacQMYDLILSYDKEDDLQPldlvpnNQGLTPFKLAAKEGNIVMFQHLVQ 233
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 296-491 1.02e-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: 82.75  E-value: 1.02e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  296 LLARTKNGLSPLHMAAQGDHVECVKHLLQHKApVDDVTLDYL--TALHVAAHCGHYRVTKLLLDkranpNARAL------ 367
Cdd:cd22192     10 LLQQKRISESPLLLAAKENDVQAIKKLLKCPS-CDLFQRGALgeTALHVAALYDNLEAAVVLME-----AAPELvnepmt 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  368 ----RGETALHMAARAGQVEVVRCLLRNGA-LVDARA-----REEQT--------PLHIASRLGKTEIVQLLLQHMAHPD 429
Cdd:cd22192     84 sdlyQGETALHIAVVNQNLNLVRELIARGAdVVSPRAtgtffRPGPKnliyygehPLSFAACVGNEEIVRLLIEHGADIR 163

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1229385538  430 AATTNGYTPLHISAREGQVDVA----SVLLEA---GAAHSLAT---KKGFTPLHVAAKYGSLDVAKLLLQRR 491
Cdd:cd22192    164 AQDSLGNTVLHILVLQPNKTFAcqmyDLILSYdkeDDLQPLDLvpnNQGLTPFKLAAKEGNIVMFQHLVQKR 235
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 262-491 5.03e-13

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: 74.35  E-value: 5.03e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  262 QIDAKTRDGLTPLHCAA-RSGHDQVVELLLERGAplLARTknGLSPLHMAAQGdHVECVKHLLQH--KAPVDDVTLDYL- 337
Cdd:TIGR00870   44 NINCPDRLGRSALFVAAiENENLELTELLLNLSC--RGAV--GDTLLHAISLE-YVDAVEAILLHllAAFRKSGPLELAn 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  338 -----------TALHVAAHCGHYRVTKLLLDKRANPNARA-------------LR-GETALHMAARAGQVEVVRCLLRNG 392
Cdd:TIGR00870  119 dqytseftpgiTALHLAAHRQNYEIVKLLLERGASVPARAcgdffvksqgvdsFYhGESPLNAAACLGSPSIVALLSEDP 198

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  393 ALVDArareeqtplhiASRLGKTeivqllLQHMAHPDAATTNGYTPLHISAREGQVDvasvlLEAGAAHSLATK-----K 467
Cdd:TIGR00870  199 ADILT-----------ADSLGNT------LLHLLVMENEFKAEYEELSCQMYNFALS-----LLDKLRDSKELEvilnhQ 256

                          250       260
                   ....*....|....*....|....
gi 1229385538  468 GFTPLHVAAKYGSLDVAKLLLQRR 491
Cdd:TIGR00870  257 GLTPLKLAAKEGRIVLFRLKLAIK 280
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 75-226 8.32e-12

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: 70.17  E-value: 8.32e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538   75 KGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGF--------------TPLYMAAQENHIDVVKYLLENGANQSTAte 140
Cdd:cd22194    140 EGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVFfnpkykhegfyfgeTPLALAACTNQPEIVQLLMEKESTDITS-- 217

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  141 dgftplavalqqghnqavailleNDTKGKVRLPALHIAArkDDTKS----------AALLLQNDHNAD-VQSKSGFTPLH 209
Cdd:cd22194    218 -----------------------QDSRGNTVLHALVTVA--EDSKTqndfvkrmydMILLKSENKNLEtIRNNEGLTPLQ 272

                          170
                   ....*....|....*..
gi 1229385538  210 IAAHYGNVNVATLLLNR 226
Cdd:cd22194    273 LAAKMGKAEILKYILSR 289
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 104-326 5.76e-09

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 60.87  E-value: 5.76e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  104 AQSQNGFTPlymAAQENHIDVVKYLLENGA--NQSTATEDGFTPLAVALQQGHNQAVAILLEN-DTKGKVRLPALHIAAR 180
Cdd:TIGR00870   15 SDEEKAFLP---AAERGDLASVYRDLEEPKklNINCPDRLGRSALFVAAIENENLELTELLLNlSCRGAVGDTLLHAISL 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  181 --------------KDDTKSAALLLQNDHNADVQSKsGFTPLHIAAHYGNVNVATLLLNRGAAVDFTA------------ 234
Cdd:TIGR00870   92 eyvdaveaillhllAAFRKSGPLELANDQYTSEFTP-GITALHLAAHRQNYEIVKLLLERGASVPARAcgdffvksqgvd 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  235 --RNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCA-------------ARSGHDQVVElLLERGAPL--- 296
Cdd:TIGR00870  171 sfYHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLvmenefkaeyeelSCQMYNFALS-LLDKLRDSkel 249

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1229385538  297 -LARTKNGLSPLHMAAQGDHVECVKHLLQHK 326
Cdd:TIGR00870  250 eVILNHQGLTPLKLAAKEGRIVLFRLKLAIK 280
NESP55 pfam06390
Neuroendocrine-specific golgi protein P55 (NESP55); This family consists of several mammalian ...
 1510-1667 1.76e-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: 1.76e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538 1510 TFQDGVPKTEGDSSATALFPQTHKEQVQQDFSGKMQDLPEESSLEYQQEYFVTTPGTET-------SETQKAMIVPSSPS 1582
Cdd:pfam06390   62 SFLNAHHRSAAAAAAAQVFPEPSEPESDHEDEDFEPELARPECLEYDEDDFDTETDSETepesdieSETEFETEPETEPD 141

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538 1583 KTPE-EVSTPAEEEK--------------------LYLQTPTSSERGGSPIIQEPEEPSEHRE------ESSPR--KTSL 1633
Cdd:pfam06390  142 TAPTtEPETEPEDEPgpvvpkgatfhqslterlhaLKLQSADASPRRAPPSTQEPESAREGEEpergplDKDPRdpEEEE 221

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1229385538 1634 VIVESADNQPETCErldEDAAFEKGDDMPEIPPE 1667
Cdd:pfam06390  222 EEKEEEKQQPHRCK---PKKPARRRDPSPESPPK 252
Ank_4 pfam13637
Ankyrin repeats (many copies);
111-162 3.02e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.81  E-value: 3.02e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1229385538  111 TPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHNQAVAILL 162
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 571-707 1.96e-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: 1.96e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  571 LHLASQEGHTDMVTLLLDKGANIHMstksGLTSLHLAAQEDKVNVADILT---KHGADQDAHTKL----------GYTPL 637
Cdd:TIGR00870   57 FVAAIENENLELTELLLNLSCRGAV----GDTLLHAISLEYVDAVEAILLhllAAFRKSGPLELAndqytseftpGITAL 132

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  638 IVACHYGNVKMVNFLLKQGANVNAKTK--------------NGYTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTAL 703
Cdd:TIGR00870  133 HLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLL 212


                   ....
gi 1229385538  704 AIAK 707
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 2.38e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 45.27  E-value: 2.38e-06
                            10        20
                    ....*....|....*....|....*..
gi 1229385538   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 ...
 665-694 1.14e-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: 1.14e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 1229385538   665 NGYTPLHQAAQQGHTHIINVLLQHGAKPNA 694
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 236-265 1.64e-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: 1.64e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 1229385538   236 NGITPLHVASKRGNTNMVKLLLDRGGQIDA 265
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 ...
 1196-1325 2.59e-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: 202.70  E-value: 2.59e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538 1196 VPYMAKFVVFAKSHDPIEARLRCFCMTDDKVDKTLEQQENFAEVARSRDVEVLEGKPIYVDCFGNLVPLTKSGQHHIFSF 1275
Cdd:pfam17809    1 VPYLAKFVVFAKRYDPGEARLRCACMTDDGEDKTLEFHEGFTEVARSRDVEVLEGSPVSIELSGNLVPIKKKSQSRQMDF 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1229385538 1276 FAFKENRLPLFVKVRDTTQEPCGRLSFMKEPKSTRGLVHQAICNLNITLP 1325
Cdd:pfam17809   81 KAFRENRLDGSVRVKDPSDPPKGLLSFMRDAKVDGGTVSQPLCTLNIVLP 130
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
454-719 3.76e-59

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 205.96  E-value: 3.76e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  454 LLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHATAKN 533
Cdd:COG0666      7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  534 GYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKV 613
Cdd:COG0666     87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  614 NVADILTKHGADQDAHTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPN 693
Cdd:COG0666    167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246

                          250       260
                   ....*....|....*....|....*.
gi 1229385538  694 ATTANGNTALAIAKRLGYISVVDTLK 719
Cdd:COG0666    247 AKDKDGLTALLLAAAAGAALIVKLLL 272
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
217-505 1.24e-58

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 204.42  E-value: 1.24e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  217 VNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAPL 296
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  297 LARTKNGLSPLHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNARALRGETALHMA 376
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  377 ARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLE 456
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1229385538  457 AGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPL 505
Cdd:COG0666    241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
155-439 1.81e-58

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 204.03  E-value: 1.81e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  155 NQAVAILLENDTKGKVRLPALHIAARKDDTKSAALLLQNDHNADVQSKSGFTPLHIAAHYGNVNVATLLLNRGAAVDFTA 234
Cdd:COG0666      5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  235 RNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGD 314
Cdd:COG0666     85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANG 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  315 HVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNARALRGETALHMAARAGQVEVVRCLLRNGAL 394
Cdd:COG0666    165 NLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD 244

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1229385538  395 VDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPL 439
Cdd:COG0666    245 LNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
416-703 1.54e-57

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 201.34  E-value: 1.54e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  416 EIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAAD 495
Cdd:COG0666      2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  496 SAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLAS 575
Cdd:COG0666     82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  576 QEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADILTKHGADQDAHTKLGYTPLIVACHYGNVKMVNFLLKQ 655
Cdd:COG0666    162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1229385538  656 GANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTAL 703
Cdd:COG0666    242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
187-472 4.90e-57

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 199.80  E-value: 4.90e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  187 AALLLQNDHNADVQSKSGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAK 266
Cdd:COG0666      4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  267 TRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHC 346
Cdd:COG0666     84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  347 GHYRVTKLLLDKRANPNARALRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMA 426
Cdd:COG0666    164 GNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1229385538  427 HPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPL 472
Cdd:COG0666    244 DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
122-406 1.66e-56

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 198.25  E-value: 1.66e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  122 IDVVKYLLENGANQSTATEDGFTPLAVALQQGHNQAVAILLENDTKGKVRL----PALHIAARKDDTKSAALLLQNDHNA 197
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADalgaLLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  198 DVQSKSGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCA 277
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  278 ARSGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLD 357
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1229385538  358 KRANPNARALRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPL 406
Cdd:COG0666    241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
322-602 6.22e-56

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 196.71  E-value: 6.22e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  322 LLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNARALRGETALHMAARAGQVEVVRCLLRNGALVDARARE 401
Cdd:COG0666      7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  402 EQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSL 481
Cdd:COG0666     87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  482 DVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQMQIASTLLNYGAETN 561
Cdd:COG0666    167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1229385538  562 IVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLT 602
Cdd:COG0666    247 AKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
388-670 7.39e-56

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 196.33  E-value: 7.39e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  388 LLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKK 467
Cdd:COG0666      7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  468 GFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQM 547
Cdd:COG0666     87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  548 QIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADILTKHGADQD 627
Cdd:COG0666    167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1229385538  628 AHTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPL 670
Cdd:COG0666    247 AKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
251-538 4.26e-55

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 194.40  E-value: 4.26e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  251 NMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLLQHKAPVD 330
Cdd:COG0666      2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  331 DVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNARALRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIAS 410
Cdd:COG0666     82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  411 RLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQR 490
Cdd:COG0666    162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1229385538  491 RAAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHATAKNGYTPL 538
Cdd:COG0666    242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
481-719 8.59e-55

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 193.25  E-value: 8.59e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  481 LDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQMQIASTLLNYGAET 560
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  561 NIVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADILTKHGADQDAHTKLGYTPLIVA 640
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1229385538  641 CHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTALAIAKRLGYISVVDTLK 719
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
23-373 2.21e-54

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 192.09  E-value: 2.21e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538   23 LDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGANI 102
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  103 NAQSQNGFTPLYMAAQENHIDVVKYLLENGAnqstatedgftplavalqqghnqavaillendtkgkvrlpalhiaarkd 182
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGA------------------------------------------------- 111

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  183 dtksaalllqndhNADVQSKSGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQ 262
Cdd:COG0666    112 -------------DVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGAD 178

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  263 IDAKTRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHV 342
Cdd:COG0666    179 VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLL 258

                          330       340       350
                   ....*....|....*....|....*....|.
gi 1229385538  343 AAHCGHYRVTKLLLDKRANPNARALRGETAL 373
Cdd:COG0666    259 AAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
283-571 6.48e-54

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 190.94  E-value: 6.48e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  283 DQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANP 362
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  363 NARALRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHIS 442
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  443 AREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLE 522
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1229385538  523 KGASPHATAKNGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPL 571
Cdd:COG0666    241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
5-340 9.25e-54

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 190.55  E-value: 9.25e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538    5 LQKSDSNASFLRAARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIAS 84
Cdd:COG0666     16 LLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAA 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538   85 LAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGAnqstatedgftplavalqqghnqavaillen 164
Cdd:COG0666     96 RNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGA------------------------------- 144

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  165 dtkgkvrlpalhiaarkddtksaalllqndhNADVQSKSGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVA 244
Cdd:COG0666    145 -------------------------------DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLA 193

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  245 SKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLLQ 324
Cdd:COG0666    194 AENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLL 273

                          330
                   ....*....|....*.
gi 1229385538  325 HKAPVDDVTLDYLTAL 340
Cdd:COG0666    274 ALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
354-637 1.43e-52

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 187.08  E-value: 1.43e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  354 LLLDKRANPNARALRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATT 433
Cdd:COG0666      6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  434 NGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDN 513
Cdd:COG0666     86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  514 QKVALLLLEKGASPHATAKNGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLDKGANI 593
Cdd:COG0666    166 LEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADL 245

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1229385538  594 HMSTKSGLTSLHLAAQEDKVNVADILTKHGADQDAHTKLGYTPL 637
Cdd:COG0666    246 NAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Death_ank2 cd08804
Death domain of Ankyrin-2; Death Domain (DD) of Ankyrin-2 (ANK-2) and related proteins. ...
 1354-1437 1.83e-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: 175.66  E-value: 1.83e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538 1354 ERIEERLAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIV 1433
Cdd:cd08804      1 ERTEERLAHIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLTQCLTKINRMDIV 80


                   ....
gi 1229385538 1434 HLME 1437
Cdd:cd08804     81 HLME 84
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
3-304 2.00e-50

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 180.92  E-value: 2.00e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538    3 TMLQKSDSNASFLRAARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHI 82
Cdd:COG0666     47 LALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHL 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538   83 ASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGAnqstatedgftplavalqqghnqavaill 162
Cdd:COG0666    127 AAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA----------------------------- 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  163 endtkgkvrlpalhiaarkddtksaalllqndhNADVQSKSGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLH 242
Cdd:COG0666    178 ---------------------------------DVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALD 224

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1229385538  243 VASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGL 304
Cdd:COG0666    225 LAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLL 286
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
 871-975 2.80e-50

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


Pssm-ID: 128514  Cd Length: 104  Bit Score: 172.92  E-value: 2.80e-50
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538   871 SGFLVSFMVDARGGAMRGCRhNGLRIIIPPRKCTAPTRVTCRLVKRHRLATMPPMVEGEGLASRLIEVGPSGAQFLGPVI 950
Cdd:smart00218    1 PSFLVSGTFDARGGRLRGPR-TGVRLIIPPGAIPQGTRYTCYLVVHKTLSTPPPLEEGETLLSPVVECGPHGALFLRPVI 79

                            90       100
                    ....*....|....*....|....*
gi 1229385538   951 VEIPHFAALRGKERELVVLRSENGD 975
Cdd:smart00218   80 LEVPHCASLRPRDWEIVLLRSENGG 104
ZU5 pfam00791
ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.
 875-972 5.46e-41

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


Pssm-ID: 459941  Cd Length: 97  Bit Score: 146.13  E-value: 5.46e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  875 VSFMVDARGGAMRGCrHNGLRIIIPPRKCTAPTRVTCRLVKRHRLATMPPMVEGEGLASRLIEVGPSGAQFLGPVIVEIP 954
Cdd:pfam00791    1 VSGLVDSRGGRLVLP-NSGVSLLIPPGAIPEGTRIECYLAVNRDESSRPPLEEGETLLSPVVECGPPGLKFLKPVILEVP 79

                           90
                   ....*....|....*...
gi 1229385538  955 HFAALRGKERELVVLRSE 972
Cdd:pfam00791   80 HCASLRPEEWEIVLKRSD 97
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 466-690 2.99e-40

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 155.21  E-value: 2.99e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  466 KKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHY-----DNQKVALLLLEKGASPHATAKNGYTPLHI 540
Cdd:PHA03100    33 KKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIkynltDVKEIVKLLLEYGANVNAPDNNGITPLLY 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  541 AA--KKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTD--MVTLLLDKGANIhmstksgltslhlaaqeDKVNVA 616
Cdd:PHA03100   113 AIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDI-----------------NAKNRV 175

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1229385538  617 DILTKHGADQDAHTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGA 690
Cdd:PHA03100   176 NYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
Death_ank cd08317
Death domain associated with Ankyrins; Death Domain (DD) associated with Ankyrins. Ankyrins ...
 1354-1437 2.77e-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: 2.77e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538 1354 ERIEERLAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIV 1433
Cdd:cd08317      1 HRADLRLSDIANLLGSDWPELARELGVSEEDIDLIRSENPNSLAQQAMAMLRLWLEREGEKATGNALESALKKIGRDDIV 80


                   ....
gi 1229385538 1434 HLME 1437
Cdd:cd08317     81 EKCE 84
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 503-712 6.92e-34

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 136.33  E-value: 6.92e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  503 TPLHVAAHYDNQKVALLLLEKGASPHATAKNGYTPLHIAA-----KKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQE 577
Cdd:PHA03100    37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISK 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  578 --GHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQ--EDKVNVADILTKHGADQDAHTKlgytplivachygnvkmVNFLL 653
Cdd:PHA03100   117 ksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLEsnKIDLKILKLLIDKGVDINAKNR-----------------VNYLL 179

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1229385538  654 KQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTAL--AIAKRLGYI 712
Cdd:PHA03100   180 SYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLhiAILNNNKEI 240
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 219-559 8.10e-33

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 137.50  E-value: 8.10e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  219 VATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAPLla 298
Cdd:PHA02876   160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNI-- 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  299 rTKNGLSPLHmAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHY-RVTKLLLDKRANPNARALRGETALHMAA 377
Cdd:PHA02876   238 -NKNDLSLLK-AIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMA 315

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  378 RAG-QVEVVRCLLRNGALVDARAREEQTPLHIASRLGK-TEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLL 455
Cdd:PHA02876   316 KNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLDRnKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLL 395

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  456 EAGAAHSLATKKGFTPLHVAAkYGS--LDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQ-KVALLLLEKGASPHATAK 532
Cdd:PHA02876   396 DYGADIEALSQKIGTALHFAL-CGTnpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAINI 474

                          330       340
                   ....*....|....*....|....*..
gi 1229385538  533 NGYTPLHIAAKKNqmQIASTLLNYGAE 559
Cdd:PHA02876   475 QNQYPLLIALEYH--GIVNILLHYGAE 499
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 285-659 1.16e-32

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 137.12  E-value: 1.16e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  285 VVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNa 364
Cdd:PHA02876   160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNIN- 238

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  365 ralRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGK-TEIVQLLLQHMAHPDAATTNGYTPLHISA 443
Cdd:PHA02876   239 ---KNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMA 315

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  444 REGqvdvasvlleagaahslatkkgftplhvaakYGSLDVaKLLLQRRAAADSAGKNGLTPLHVAAHYD-NQKVALLLLE 522
Cdd:PHA02876   316 KNG-------------------------------YDTENI-RTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLE 363

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  523 KGASPHATAKNGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDM-VTLLLDKGANIHMSTKSGL 601
Cdd:PHA02876   364 LGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVNSKNKDLS 443

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1229385538  602 TSLHLAAQED-KVNVADILTKHGADQDAHTKLGYTPLIVACHYGNVkmVNFLLKQGANV 659
Cdd:PHA02876   444 TPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIALEYHGI--VNILLHYGAEL 500
PHA03095 PHA03095
ankyrin-like protein; Provisional
 316-594 1.99e-32

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 133.23  E-value: 1.99e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  316 VECVKHLLQHKAPVD-DVTLDYlTALHVAAHCGHYRVTK---LLLDKRANPNARALRGETALHMAARAGQVE-VVRCLLR 390
Cdd:PHA03095    27 VEEVRRLLAAGADVNfRGEYGK-TPLHLYLHYSSEKVKDivrLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIK 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  391 NGALVDARAREEQTPLHI--ASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASV--LLEAGAahSLATK 466
Cdd:PHA03095   106 AGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVELLrlLIDAGA--DVYAV 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  467 K--GFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKN--GLTPLHVAAHYDNQKVALL--LLEKGASPHATAKNGYTPLHI 540
Cdd:PHA03095   184 DdrFRSLLHHHLQSFKPRARIVRELIRAGCDPAATDmlGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHY 263

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1229385538  541 AAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLDKGANIH 594
Cdd:PHA03095   264 AAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAE 317
PHA03095 PHA03095
ankyrin-like protein; Provisional
 416-719 5.48e-30

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 125.91  E-value: 5.48e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  416 EIVQLLLQHMAHPDAATTNGYTPLHI---SAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGS-LDVAKLLLQRR 491
Cdd:PHA03095    28 EEVRRLLAAGADVNFRGEYGKTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAG 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  492 AAADSAGKNGLTPLHVAAHYDN--QKVALLLLEKGASPHATAKNGYTPLHIAAKKNQ--MQIASTLLNYGAETNIVTKQG 567
Cdd:PHA03095   108 ADVNAKDKVGRTPLHVYLSGFNinPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanVELLRLLIDAGADVYAVDDRF 187

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  568 VTPLH--LASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADI--LTKHGADQDAHTKLGYTPLIVACHY 643
Cdd:PHA03095   188 RSLLHhhLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVF 267

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1229385538  644 GNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQhgAKPNATT-ANgntALAIAKRLGYISVVDTLK 719
Cdd:PHA03095   268 NNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALA--KNPSAETvAA---TLNTASVAGGDIPSDATR 339
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 90-397 7.19e-30

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 124.39  E-value: 7.19e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538   90 EVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHNQavaillendtkgk 169
Cdd:PHA03100    16 KNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNL------------- 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  170 vrlpalhiaarKDDTKSAALLLQNDHNADVQSKSGFTPLHIAA--HYGNVNVATLLLNRGAAVDFTARNGITPLHVA--S 245
Cdd:PHA03100    83 -----------TDVKEIVKLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYleS 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  246 KRGNTNMVKLLLDRGGQIDAKTRdgltplhcaarsghdqvVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVkhllqh 325
Cdd:PHA03100   152 NKIDLKILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFV------ 208

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1229385538  326 kapvddvtldyltalhvaahcghyrvtKLLLDKRANPNARALRGETALHMAARAGQVEVVRCLLRNGALVDA 397
Cdd:PHA03100   209 ---------------------------KYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 23-426 2.05e-29

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 126.72  E-value: 2.05e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538   23 LDKV-VEYLKGGIDINTCNQNGLN-------ALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKV 94
Cdd:PHA02876   117 LDEAcIHILKEAISGNDIHYDKINesieymkLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNL 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538   95 LVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGANqstatedgftplavalqqghnqavaiLLENDTkgkvrlpA 174
Cdd:PHA02876   197 LLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSN--------------------------INKNDL-------S 243

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  175 LHIAARKDDTKSAALLLQNDHNADVQSKSGFTPLHIAAHYGNVN-VATLLLNRGAAVDFTARNGITPLHVASKRG-NTNM 252
Cdd:PHA02876   244 LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGyDTEN 323

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  253 VKLLLDRGGQIDAKTRDGLTPLHCAAR-SGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLLQHKAPVDD 331
Cdd:PHA02876   324 IRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEA 403

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  332 VTLDYLTALHVAAhCGH--YRVTKLLLDKRANPNARALRGETALHMAARAG-QVEVVRCLLRNGALVDARAREEQTPLHI 408
Cdd:PHA02876   404 LSQKIGTALHFAL-CGTnpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLI 482

                          410
                   ....*....|....*...
gi 1229385538  409 AsrLGKTEIVQLLLQHMA 426
Cdd:PHA02876   483 A--LEYHGIVNILLHYGA 498
PHA03095 PHA03095
ankyrin-like protein; Provisional
 8-327 4.53e-29

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 123.21  E-value: 4.53e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538    8 SDSNASFLRAARAGN--LDKVVEYLKGGIDINTCNQNGLNALHLAAKEGH---VGLVQELLGRGSSVDSATKKGNTALHI 82
Cdd:PHA03095    10 IMEAALYDYLLNASNvtVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHL 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538   83 -ASLAGQAEVVKVLVKEGANINAQSQNGFTPL--YMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQgHNQAVA 159
Cdd:PHA03095    90 yLYNATTLDVIKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKS-RNANVE 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  160 I---LLEND----TKGKVRLPALHIAAR--KDDTKSAALLLQNDHNADVQSKSGFTPLHIAAHYG---NVNVATLLLNrG 227
Cdd:PHA03095   169 LlrlLIDAGadvyAVDDRFRSLLHHHLQsfKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSsckRSLVLPLLIA-G 247

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  228 AAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAP--LLARTKNGLS 305
Cdd:PHA03095   248 ISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSaeTVAATLNTAS 327

                          330       340
                   ....*....|....*....|...
gi 1229385538  306 PLHMAAQGDHV-ECVKHLLQHKA 327
Cdd:PHA03095   328 VAGGDIPSDATrLCVAKVVLRGA 350
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 254-574 1.48e-28

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 120.84  E-value: 1.48e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  254 KLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGApllartknglsplhmaaQGDHVEC-VKHLLqhkapvddv 332
Cdd:PHA02874    19 KIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGA-----------------DINHINTkIPHPL--------- 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  333 tldyLTALHVAAHcghyRVTKLLLDKRANPNAralrgetalhMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRL 412
Cdd:PHA02874    73 ----LTAIKIGAH----DIIKLLIDNGVDTSI----------LPIPCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKK 134

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  413 GKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRA 492
Cdd:PHA02874   135 GDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGN 214

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  493 AADSAGKNGLTPLHVAAHYDNQKVALLLleKGASPHATAKNGYTPLHIAAKKN-QMQIASTLLNYGAETNIVTKQGVTPL 571
Cdd:PHA02874   215 HIMNKCKNGFTPLHNAIIHNRSAIELLI--NNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPI 292


                   ...
gi 1229385538  572 HLA 574
Cdd:PHA02874   293 DTA 295
Death_ank3 cd08803
Death domain of Ankyrin-3; Death Domain (DD) of the human protein ankyrin-3 (ANK-3) and ...
 1354-1437 5.44e-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: 5.44e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538 1354 ERIEERLAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIV 1433
Cdd:cd08803      1 ERTDIRMAIVADHLGLSWTELARELNFSVDEINQIRVENPNSLIAQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIV 80


                   ....
gi 1229385538 1434 HLME 1437
Cdd:cd08803     81 TLLE 84
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 382-593 5.86e-28

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 119.00  E-value: 5.86e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  382 VEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQV-----DVASVLLE 456
Cdd:PHA03100    15 VKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLE 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  457 AGAAHSLATKKGFTPLHVAA--KYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHY--DNQKVALLLLEKGAspHATAK 532
Cdd:PHA03100    95 YGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESnkIDLKILKLLIDKGV--DINAK 172

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1229385538  533 N------------------GYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLDKGANI 593
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 ...
 1354-1437 7.43e-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: 7.43e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538 1354 ERIEERLAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIV 1433
Cdd:cd08805      1 ERVEMKMAVIREHLGLSWAELARELQFSVEDINRIRVENPNSLLEQSTALLNLWVDREGENAKMEPLYPALYSIDRLTIV 80


                   ....
gi 1229385538 1434 HLME 1437
Cdd:cd08805     81 NILE 84
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 475-696 1.27e-27

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 117.78  E-value: 1.27e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  475 AAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQMQIASTLL 554
Cdd:PHA02875     9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  555 NYGAETN-IVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADILTKHGADQDAHTKLG 633
Cdd:PHA02875    89 DLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCG 168

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1229385538  634 YTPLIVACHYGNVKMVNFLLKQGANVNAKTKNG-YTPLHQAAQQGHTHIINVLLQHGAKPNATT 696
Cdd:PHA02875   169 CTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNIMF 232
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 370-597 3.97e-27

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 116.24  E-value: 3.97e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  370 ETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVD 449
Cdd:PHA02875     3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  450 VASVLLEAGA-AHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASPH 528
Cdd:PHA02875    83 AVEELLDLGKfADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLD 162

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  529 ATAKNGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQG-VTPLHLASQEGHTDMVTLLLDKGANIHMST 597
Cdd:PHA02875   163 IEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNIMF 232
PHA03095 PHA03095
ankyrin-like protein; Provisional
 56-420 9.61e-27

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 115.89  E-value: 9.61e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538   56 VGLVQELLGRGSSVDSATKKGNTALHI---ASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQ-ENHIDVVKYLLEN 131
Cdd:PHA03095    27 VEEVRRLLAAGADVNFRGEYGKTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYnATTLDVIKLLIKA 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  132 GANQSTATEDGFTPLAVALQqghNQAVaillendtkgkvrlpalhiaarkdDTKSAALLLqnDHNADVQSK--SGFTPLH 209
Cdd:PHA03095   107 GADVNAKDKVGRTPLHVYLS---GFNI------------------------NPKVIRLLL--RKGADVNALdlYGMTPLA 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  210 IAAHYGNVNVATL--LLNRGA---AVDFtarNGITPLHV--ASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAAR--S 280
Cdd:PHA03095   158 VLLKSRNANVELLrlLIDAGAdvyAVDD---RFRSLLHHhlQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATgsS 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  281 GHDQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKra 360
Cdd:PHA03095   235 CKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAK-- 312

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1229385538  361 NPNARALrgETALHMAARAGQVEVVRC--------LLRNGALVDArarEEQTPLHIAS-RLGKTEIVQL 420
Cdd:PHA03095   313 NPSAETV--AATLNTASVAGGDIPSDAtrlcvakvVLRGAFSLLP---EPIRAYHADFiRECEAEIAVM 376
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 373-563 1.04e-26

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 115.15  E-value: 1.04e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  373 LHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKT-----EIVQLLLQHMAHPDAATTNGYTPLH--ISARE 445
Cdd:PHA03100    39 LYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLyaISKKS 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  446 GQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGS--LDVAKLLLQRRA----------------AADSAGKNGLTPLHV 507
Cdd:PHA03100   119 NSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVdinaknrvnyllsygvPINIKDVYGFTPLHY 198

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1229385538  508 AAHYDNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQMQIASTLLNYGAETNIV 563
Cdd:PHA03100   199 AVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTI 254
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 47-265 1.34e-26

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 114.76  E-value: 1.34e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538   47 LHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQA-----EVVKVLVKEGANINAQSQNGFTPLYMAAQE-- 119
Cdd:PHA03100    39 LYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKks 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  120 NHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHN--QAVAILLEN----DTKGKVRLpalhiaarkddtksaalLLQN 193
Cdd:PHA03100   119 NSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKgvdiNAKNRVNY-----------------LLSY 181

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1229385538  194 DHNADVQSKSGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDA 265
Cdd:PHA03100   182 GVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 80-369 1.04e-25

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 113.05  E-value: 1.04e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538   80 LHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLenganqSTATEDGFTPLAVALQQG-HNQAV 158
Cdd:PHA02878    41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMI------RSINKCSVFYTLVAIKDAfNNRNV 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  159 AI---LLENDTKGKVRLPALHIAARKDD----TKSAALLLQndHNADVQSK---SGFTPLHIAAHYGNVNVATLLLNRGA 228
Cdd:PHA02878   115 EIfkiILTNRYKNIQTIDLVYIDKKSKDdiieAEITKLLLS--YGADINMKdrhKGNTALHYATENKDQRLTELLLSYGA 192

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  229 AVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHD-QVVELLLERGAPLLAR-TKNGLSP 306
Cdd:PHA02878   193 NVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDyDILKLLLEHGVDVNAKsYILGLTA 272

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1229385538  307 LHMAAQGDHVecVKHLLQHKAPVDDVTLDYLTALHVAA------HCGHYRVTKLLLDKRANPNARALRG 369
Cdd:PHA02878   273 LHSSIKSERK--LKLLLEYGADINSLNSYKLTPLSSAVkqylciNIGRILISNICLLKRIKPDIKNSEG 339
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 54-329 2.15e-25

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 111.21  E-value: 2.15e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538   54 GHVGLVQELL-GRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENG 132
Cdd:PHA02874    12 GDIEAIEKIIkNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  133 ANQSTatedgftplaVALQQGHNQAVAILLEN----DTKGKVRLPALHIAARKDDTKSAALLLQNDHNADVQSKSGFTPL 208
Cdd:PHA02874    92 VDTSI----------LPIPCIEKDMIKTILDCgidvNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPI 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  209 HIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARsgHDQVVEL 288
Cdd:PHA02874   162 HIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIE 239

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1229385538  289 LLERGAPLLARTKNGLSPLHMAAQGD-HVECVKHLLQHKAPV 329
Cdd:PHA02874   240 LLINNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADI 281
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 373-645 2.44e-25

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 111.21  E-value: 2.44e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  373 LHMAARAGQVEVVRCLLRN-GALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVA 451
Cdd:PHA02874     5 LRMCIYSGDIEAIEKIIKNkGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDII 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  452 SVL-----------------------LEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVA 508
Cdd:PHA02874    85 KLLidngvdtsilpipciekdmiktiLDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIA 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  509 AHYDNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQegHTDMVTLLLD 588
Cdd:PHA02874   165 IKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLI 242

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1229385538  589 KGANIHMSTKSGLTSLHLAAQED-KVNVADILTKHGADQDAHTKLGYTPLIVACHYGN 645
Cdd:PHA02874   243 NNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAFKYIN 300
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 206-499 3.04e-25

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 110.82  E-value: 3.04e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  206 TPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGgqIDAKtrdgLTPLHCAarsgHDQV 285
Cdd:PHA02874    37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG--VDTS----ILPIPCI----EKDM 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  286 VELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNAR 365
Cdd:PHA02874   107 IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVK 186

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  366 ALRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASrLGKTEIVQLLLQHmAHPDAATTNGYTPLHISAR- 444
Cdd:PHA02874   187 DNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI-IHNRSAIELLINN-ASINDQDIDGSTPLHHAINp 264

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1229385538  445 EGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLD-VAKLLLQRRAAADSAGK 499
Cdd:PHA02874   265 PCDIDIIDILLYHKADISIKDNKGENPIDTAFKYINKDpVIKDIIANAVLIKEADK 320
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 211-433 3.72e-25

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 110.47  E-value: 3.72e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  211 AAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLL 290
Cdd:PHA02875     9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  291 ERGAPLL-ARTKNGLSPLHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNARALRG 369
Cdd:PHA02875    89 DLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCG 168

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1229385538  370 ETALHMAARAGQVEVVRCLLRNGALVDARARE-EQTPLHIASRLGKTEIVQLLLQHMAHPDAATT 433
Cdd:PHA02875   169 CTPLIIAMAKGDIAICKMLLDSGANIDYFGKNgCVAALCYAIENNKIDIVRLFIKRGADCNIMFM 233
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 508-703 7.56e-25

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 109.31  E-value: 7.56e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  508 AAHYDNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLL 587
Cdd:PHA02875     9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  588 DKGANIH-MSTKSGLTSLHLAAQEDKVNVADILTKHGADQDAHTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNG 666
Cdd:PHA02875    89 DLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCG 168

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1229385538  667 YTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTAL 703
Cdd:PHA02875   169 CTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAA 205
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 219-546 1.05e-24

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 109.28  E-value: 1.05e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  219 VATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLErgaplla 298
Cdd:PHA02874    17 IEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLID------- 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  299 rtkNGLSPLHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNARALRGETALHMAAR 378
Cdd:PHA02874    90 ---NGVDTSILPIPCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIK 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  379 AGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVAsvLLEAG 458
Cdd:PHA02874   167 HNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIE--LLINN 244

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  459 AAHSLATKKGFTPLHVAAKYG-SLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKV--------ALLLLEKGASPHA 529
Cdd:PHA02874   245 ASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAFKYINKDPvikdiianAVLIKEADKLKDS 324

                          330
                   ....*....|....*..
gi 1229385538  530 TAKNgytplHIAAKKNQ 546
Cdd:PHA02874   325 DFLE-----HIEIKDNK 336
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 205-488 3.27e-24

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 108.43  E-value: 3.27e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  205 FTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLldrggqIDAKTRDGLTPLHCAARSG-HD 283
Cdd:PHA02878    38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEM------IRSINKCSVFYTLVAIKDAfNN 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  284 QVVELLlerGAPLLARTKN----GLSPLHMAAQGDHVEC--VKHLLQHKAPVDDVTLDYL-TALHVAAHCGHYRVTKLLL 356
Cdd:PHA02878   112 RNVEIF---KIILTNRYKNiqtiDLVYIDKKSKDDIIEAeiTKLLLSYGADINMKDRHKGnTALHYATENKDQRLTELLL 188

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  357 DKRANPNARALRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIA-SRLGKTEIVQLLLQHMAHPDAATT-N 434
Cdd:PHA02878   189 SYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYiL 268

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1229385538  435 GYTPLHISAREGQvdVASVLLEAGAAHSLATKKGFTPLHVAAK-YGSLDVAKLLL 488
Cdd:PHA02878   269 GLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPLSSAVKqYLCINIGRILI 321
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 422-711 3.39e-24

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 108.43  E-value: 3.39e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  422 LQHMAH-PDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLqRRAAADSAGkN 500
Cdd:PHA02878    23 IDHTENySTSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMI-RSINKCSVF-Y 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  501 GLTPLHVAAHYDNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQMQIASTLLNYGAETNIVTK-QGVTPLHLASQEGH 579
Cdd:PHA02878   101 TLVAIKDAFNNRNVEIFKIILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDRhKGNTALHYATENKD 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  580 TDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADILTKHGADQDAHTKLGYTPLIVACHY-GNVKMVNFLLKQGAN 658
Cdd:PHA02878   181 QRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVD 260

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1229385538  659 VNAK-TKNGYTPLHQAAQQghTHIINVLLQHGAKPNATTANGNTALAIA--KRLGY 711
Cdd:PHA02878   261 VNAKsYILGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAvkQYLCI 314
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
 1353-1438 8.94e-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: 96.71  E-value: 8.94e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  1353 QERIEERLAYIADH-LGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMD 1431
Cdd:smart00005    1 PELTRQKLAKLLDHpLGLDWRELARKLGLSEADIDQIRTEAPRDLAEQSVQLLRLWEQREGKNATLGTLLEALRKMGRDD 80


                    ....*..
gi 1229385538  1432 IVHLMET 1438
Cdd:smart00005   81 AVELLRS 87
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 120-342 1.53e-23

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 105.46  E-value: 1.53e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  120 NHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHNQAVAILLENDTKGKVRLPA----LHIAARKDDTKSAALLLQ-ND 194
Cdd:PHA02875    13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDieseLHDAVEEGDVKAVEELLDlGK 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  195 HNADVQSKSGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPL 274
Cdd:PHA02875    93 FADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPL 172

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1229385538  275 HCAARSGHDQVVELLLERGAPLLARTKNG-LSPLHMAAQGDHVECVKHLLQHKAPVDDVTL---DYLTALHV 342
Cdd:PHA02875   173 IIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNIMFMiegEECTILDM 244
Ank_2 pfam12796
Ankyrin repeats (3 copies);
47-134 1.80e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 95.95  E-value: 1.80e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538   47 LHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEgANINAQSqNGFTPLYMAAQENHIDVVK 126
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78


                   ....*...
gi 1229385538  127 YLLENGAN 134
Cdd:pfam12796   79 LLLEKGAD 86
Ank_2 pfam12796
Ankyrin repeats (3 copies);
208-294 2.85e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 95.57  E-value: 2.85e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  208 LHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRgGQIDAKTrDGLTPLHCAARSGHDQVVE 287
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78


                   ....*..
gi 1229385538  288 LLLERGA 294
Cdd:pfam12796   79 LLLEKGA 85
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 83-294 2.19e-22

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 101.99  E-value: 2.19e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538   83 ASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHNQAVAILL 162
Cdd:PHA02875     9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  163 E-----NDTKGKVRLPALHIAARKDDTKSAALLLQNDHNADVQSKSGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNG 237
Cdd:PHA02875    89 DlgkfaDDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCG 168

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1229385538  238 ITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAA-RSGHDQVVELLLERGA 294
Cdd:PHA02875   169 CTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAiENNKIDIVRLFIKRGA 226
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 17-279 2.83e-22

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 101.96  E-value: 2.83e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538   17 AARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRG---------------------SSVDSATK- 74
Cdd:PHA02874    42 AIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGvdtsilpipciekdmiktildCGIDVNIKd 121

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538   75 -KGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPlavalqqg 153
Cdd:PHA02874   122 aELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESP-------- 193

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  154 hnqavaillendtkgkvrlpaLHIAARKDDTKSAALLLQNDHNADVQSKSGFTPLHIAAHYgNVNVATLLLNrGAAVDFT 233
Cdd:PHA02874   194 ---------------------LHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIH-NRSAIELLIN-NASINDQ 250

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1229385538  234 ARNGITPLHVA-SKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAAR 279
Cdd:PHA02874   251 DIDGSTPLHHAiNPPCDIDIIDILLYHKADISIKDNKGENPIDTAFK 297
Ank_2 pfam12796
Ankyrin repeats (3 copies);
241-327 1.52e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.56  E-value: 1.52e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  241 LHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAplLARTKNGLSPLHMAAQGDHVECVK 320
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78


                   ....*..
gi 1229385538  321 HLLQHKA 327
Cdd:pfam12796   79 LLLEKGA 85
Death pfam00531
Death domain;
1357-1437 2.31e-21

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 89.73  E-value: 2.31e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538 1357 EERLAYIADH---LGFSWTELARELDFTEEQIHQIRIENPNsLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIV 1433
Cdd:pfam00531    1 RKQLDRLLDPpppLGKDWRELARKLGLSENEIDEIESENPR-LRSQTYELLRLWEQREGKNATVGTLLEALRKLGRRDAA 79


                   ....
gi 1229385538 1434 HLME 1437
Cdd:pfam00531   80 EKIQ 83
Ank_2 pfam12796
Ankyrin repeats (3 copies);
604-695 4.31e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.40  E-value: 4.31e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  604 LHLAAQEDKVNVADILTKHGADQDAHTKLGYTPLIVACHYGNVKMVNFLLKQgANVNAKTkNGYTPLHQAAQQGHTHIIN 683
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 1229385538  684 VLLQHGAKPNAT 695
Cdd:pfam12796   79 LLLEKGADINVK 90
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 408-706 6.02e-21

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 99.75  E-value: 6.02e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  408 IASRLGKTE--IVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAK 485
Cdd:PHA02876   149 IKERIQQDEllIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIK 228

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  486 LLLQRRAaadSAGKNGLTPLHVAAHYDnQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQM-QIASTLLNYGAETNIVT 564
Cdd:PHA02876   229 AIIDNRS---NINKNDLSLLKAIRNED-LETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKN 304

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  565 KQGVTPLHLASQEGH-TDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKvnvadiltkhgadqdahtklgytplivachy 643
Cdd:PHA02876   305 IKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDR------------------------------- 353

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1229385538  644 gNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTALAIA 706
Cdd:PHA02876   354 -NKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFA 415
Ank_2 pfam12796
Ankyrin repeats (3 copies);
175-266 1.24e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.86  E-value: 1.24e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  175 LHIAARKDDTKSAALLLQNDHNADVQSKSGFTPLHIAAHYGNVNVATLLLNRGAAVDFTarNGITPLHVASKRGNTNMVK 254
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD--NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 1229385538  255 LLLDRGGQIDAK 266
Cdd:pfam12796   79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
373-459 1.41e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.86  E-value: 1.41e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  373 LHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMaHPDaATTNGYTPLHISAREGQVDVAS 452
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVN-LKDNGRTALHYAARSGHLEIVK 78


                   ....*..
gi 1229385538  453 VLLEAGA 459
Cdd:pfam12796   79 LLLEKGA 85
Ank_2 pfam12796
Ankyrin repeats (3 copies);
307-398 1.45e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.86  E-value: 1.45e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  307 LHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKrANPNARaLRGETALHMAARAGQVEVVR 386
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLK-DNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 1229385538  387 CLLRNGALVDAR 398
Cdd:pfam12796   79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
80-167 1.45e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.86  E-value: 1.45e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538   80 LHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENgaNQSTATEDGFTPLAVALQQGHNQAVA 159
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH--ADVNLKDNGRTALHYAARSGHLEIVK 78


                   ....*...
gi 1229385538  160 ILLENDTK 167
Cdd:pfam12796   79 LLLEKGAD 86
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 353-564 2.27e-20

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 95.83  E-value: 2.27e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  353 KLLLDKRANPNARALRGETALHMAARAGQVEVVRCLLRNGALV-DARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAA 431
Cdd:PHA02875    52 KLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAdDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIP 131

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  432 TTNgytplhisaregqvdvasvlleagaahslatkkGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHY 511
Cdd:PHA02875   132 NTD---------------------------------KFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAK 178

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1229385538  512 DNQKVALLLLEKGASPHATAKNG-YTPLHIAAKKNQMQIASTLLNYGAETNIVT 564
Cdd:PHA02875   179 GDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNIMF 232
Ank_2 pfam12796
Ankyrin repeats (3 copies);
340-430 2.90e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.09  E-value: 2.90e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  340 LHVAAHCGHYRVTKLLLDKRANPNARALRGETALHMAARAGQVEVVRCLLRNgalVDARAREE-QTPLHIASRLGKTEIV 418
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNgRTALHYAARSGHLEIV 77

                           90
                   ....*....|..
gi 1229385538  419 QLLLQHMAHPDA 430
Cdd:pfam12796   78 KLLLEKGADINV 89
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 373-667 7.06e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 94.95  E-value: 7.06e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  373 LHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIA----SRLGKTEIVQLLLQhmahpdAATTNGYTPLHISAREGQV 448
Cdd:PHA02878    41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIIckepNKLGMKEMIRSINK------CSVFYTLVAIKDAFNNRNV 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  449 DVASVLLEAgaahslATKKGFTPLHVAAKYGSLD------VAKLLLQRRAAADSAGKNGL-TPLHVAAHYDNQKVALLLL 521
Cdd:PHA02878   115 EIFKIILTN------RYKNIQTIDLVYIDKKSKDdiieaeITKLLLSYGADINMKDRHKGnTALHYATENKDQRLTELLL 188

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  522 EKGASPHATAKNGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQE-GHTDMVTLLLDKGANIHM-STKS 599
Cdd:PHA02878   189 SYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAkSYIL 268

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1229385538  600 GLTSLHLAAQ-EDKVNvadILTKHGADQDAHTKLGYTPLIVAC------HYGNVKMVNFLLKQGANVNAKTKNGY 667
Cdd:PHA02878   269 GLTALHSSIKsERKLK---LLLEYGADINSLNSYKLTPLSSAVkqylciNIGRILISNICLLKRIKPDIKNSEGF 340
Ank_2 pfam12796
Ankyrin repeats (3 copies);
472-562 8.71e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.55  E-value: 8.71e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  472 LHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHATakNGYTPLHIAAKKNQMQIAS 551
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD--NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|.
gi 1229385538  552 TLLNYGAETNI 562
Cdd:pfam12796   79 LLLEKGADINV 89
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 306-574 9.39e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 94.56  E-value: 9.39e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  306 PLHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLdkrANPNARAL-RGETALHMAARAGQVEV 384
Cdd:PHA02878    40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMI---RSINKCSVfYTLVAIKDAFNNRNVEI 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  385 VRCLLRNG-----ALVDARAREEQTPLHIasrlgKTEIVQLLLQHMAHPDAATTN-GYTPLHISAREGQVDVASVLLEAG 458
Cdd:PHA02878   117 FKIILTNRykniqTIDLVYIDKKSKDDII-----EAEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYG 191

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  459 AAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHY-DNQKVALLLLEKGASPHATAK-NGYT 536
Cdd:PHA02878   192 ANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYiLGLT 271

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1229385538  537 PLHIAAKKNqmQIASTLLNYGAETNIVTKQGVTPLHLA 574
Cdd:PHA02878   272 ALHSSIKSE--RKLKLLLEYGADINSLNSYKLTPLSSA 307
Ank_2 pfam12796
Ankyrin repeats (3 copies);
14-105 1.53e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.78  E-value: 1.53e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538   14 FLRAARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSvdSATKKGNTALHIASLAGQAEVVK 93
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 1229385538   94 VLVKEGANINAQ 105
Cdd:pfam12796   79 LLLEKGADINVK 90
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 21-260 1.88e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 93.13  E-value: 1.88e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538   21 GNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGA 100
Cdd:PHA02875    13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  101 NIN-AQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPlavalqqghnqavaillendtkgkvrlpaLHIAA 179
Cdd:PHA02875    93 FADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSP-----------------------------LHLAV 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  180 RKDDTKSAALLLQNDHNADVQSKSGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNG-ITPLHVASKRGNTNMVKLLLD 258
Cdd:PHA02875   144 MMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIK 223


                   ..
gi 1229385538  259 RG 260
Cdd:PHA02875   224 RG 225
Ank_2 pfam12796
Ankyrin repeats (3 copies);
439-530 3.44e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.01  E-value: 3.44e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  439 LHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAgkNGLTPLHVAAHYDNQKVAL 518
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD--NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 1229385538  519 LLLEKGASPHAT 530
Cdd:pfam12796   79 LLLEKGADINVK 90
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 17-331 5.30e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 93.59  E-value: 5.30e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538   17 AARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDsatkKGNTALHIASLAGQAEVVKVLV 96
Cdd:PHA02876   185 AAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNIN----KNDLSLLKAIRNEDLETSLLLY 260

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538   97 KEGANINAQSQNGFTPLYMAAQENHID-VVKYLLENGANQSTATEDGFTPLAVALQQGH---NQAVAILLENDTKGKVRL 172
Cdd:PHA02876   261 DAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGYdteNIRTLIMLGADVNAADRL 340

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  173 --PALHIAARKDDTKSAAL-LLQNDHNADVQSKSGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGN 249
Cdd:PHA02876   341 yiTPLHQASTLDRNKDIVItLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTN 420

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  250 TNM-VKLLLDRGGQIDAKTRDGLTPLHCAARSG-HDQVVELLLERGAPLLARTKNGLSPLhMAAQGDHvECVKHLLQHKA 327
Cdd:PHA02876   421 PYMsVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPL-LIALEYH-GIVNILLHYGA 498


                   ....
gi 1229385538  328 PVDD 331
Cdd:PHA02876   499 ELRD 502
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 86-409 8.46e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 91.18  E-value: 8.46e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538   86 AGQAEVVKVLVKEGAN-INAQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHNQAVAILLEN 164
Cdd:PHA02874    11 SGDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDN 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  165 DTKGKVrLPALHIaaRKDDTKSaalllqndhnadvqsksgftplhiaahygnvnvatlLLNRGAAVDFTARNGITPLHVA 244
Cdd:PHA02874    91 GVDTSI-LPIPCI--EKDMIKT------------------------------------ILDCGIDVNIKDAELKTFLHYA 131

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  245 SKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLLQ 324
Cdd:PHA02874   132 IKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLID 211

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  325 HKAPVDDVTLDYLTALHVAAHcgHYRVTKLLLDKRANPNARALRGETALHMAAR-AGQVEVVRCLLRNGALVDARAREEQ 403
Cdd:PHA02874   212 HGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAINpPCDIDIIDILLYHKADISIKDNKGE 289


                   ....*.
gi 1229385538  404 TPLHIA 409
Cdd:PHA02874   290 NPIDTA 295
PHA03095 PHA03095
ankyrin-like protein; Provisional
 540-703 8.54e-19

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 91.62  E-value: 8.54e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  540 IAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHL---ASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKV-NV 615
Cdd:PHA03095    20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDV 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  616 ADILTKHGADQDAHTKLGYTPLIVACHYGNV--KMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHI--INVLLQHGAK 691
Cdd:PHA03095   100 IKLLIKAGADVNAKDKVGRTPLHVYLSGFNInpKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGAD 179

                          170
                   ....*....|..
gi 1229385538  692 PNATTANGNTAL 703
Cdd:PHA03095   180 VYAVDDRFRSLL 191
Death cd01670
Death Domain: a protein-protein interaction domain; Death Domains (DDs) are protein-protein ...
 1360-1437 9.67e-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: 81.94  E-value: 9.67e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1229385538 1360 LAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIVHLME 1437
Cdd:cd01670      2 FDLVAEELGRDWKKLARKLGLSEGDIDQIEEDNRDDLKEQAYQMLERWREREGDEATLGRLIQALREIGRRDLAEKLE 79
Ank_2 pfam12796
Ankyrin repeats (3 copies);
538-628 2.34e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 81.32  E-value: 2.34e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  538 LHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLDKgANIHMSTKsGLTSLHLAAQEDKVNVAD 617
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                           90
                   ....*....|.
gi 1229385538  618 ILTKHGADQDA 628
Cdd:pfam12796   79 LLLEKGADINV 89
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 14-325 3.80e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 89.55  E-value: 3.80e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538   14 FLRAARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGR--GSSVDSATKKGNTALHIASLagqaEV 91
Cdd:PHA02878    41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSinKCSVFYTLVAIKDAFNNRNV----EI 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538   92 VKVLVKEGANINAQSQngFTPLYMAAQENHID--VVKYLLENGANQSTATEDgftplavalqqghnqavaillendtKGK 169
Cdd:PHA02878   117 FKIILTNRYKNIQTID--LVYIDKKSKDDIIEaeITKLLLSYGADINMKDRH-------------------------KGN 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  170 VrlpALHIAARKDDTKSAALLLQNDHNADVQSKSGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKR-G 248
Cdd:PHA02878   170 T---ALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcK 246

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1229385538  249 NTNMVKLLLDRGGQIDAK-TRDGLTPLHCAARSghDQVVELLLERGAPLLARTKNGLSPLHMAA-QGDHVECVKHLLQH 325
Cdd:PHA02878   247 DYDILKLLLEHGVDVNAKsYILGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAVkQYLCINIGRILISN 323
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 512-718 6.98e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 89.74  E-value: 6.98e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  512 DNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLDKGA 591
Cdd:PHA02876   156 DELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRS 235

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  592 NIHmstKSGLTSLHLAAQEDkVNVADILTKHGADQDAHTKLGYTPLIVACHYGNV-KMVNFLLKQGANVNAKTKNGYTPL 670
Cdd:PHA02876   236 NIN---KNDLSLLKAIRNED-LETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPL 311

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1229385538  671 HQAAQQGH-THIINVLLQHGAKPNATTANGNTALAIAKRLG-YISVVDTL 718
Cdd:PHA02876   312 YLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITL 361
Ank_2 pfam12796
Ankyrin repeats (3 copies);
637-718 4.55e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.85  E-value: 4.55e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  637 LIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHgAKPNATTaNGNTALAIAKRLGYISVVD 716
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78


                   ..
gi 1229385538  717 TL 718
Cdd:pfam12796   79 LL 80
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 460-654 3.41e-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: 3.41e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  460 AHSLATKKGF-TPLHVAAKYGSLD-VAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEkgASPH-----ATAK 532
Cdd:cd22192      8 LHLLQQKRISeSPLLLAAKENDVQaIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPElvnepMTSD 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  533 --NGYTPLHIAAKKNQMQIASTLLNYGAEtniVTKQGVT-----------------PLHLASQEGHTDMVTLLLDKGANI 593
Cdd:cd22192     86 lyQGETALHIAVVNQNLNLVRELIARGAD---VVSPRATgtffrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADI 162

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1229385538  594 HMSTKSGLTSLH-LAAQEDKV---NVADILTKHGADQDAHT------KLGYTPLIVACHYGNVKMVNFLLK 654
Cdd:cd22192    163 RAQDSLGNTVLHiLVLQPNKTfacQMYDLILSYDKEDDLQPldlvpnNQGLTPFKLAAKEGNIVMFQHLVQ 233
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 296-491 1.02e-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: 82.75  E-value: 1.02e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  296 LLARTKNGLSPLHMAAQGDHVECVKHLLQHKApVDDVTLDYL--TALHVAAHCGHYRVTKLLLDkranpNARAL------ 367
Cdd:cd22192     10 LLQQKRISESPLLLAAKENDVQAIKKLLKCPS-CDLFQRGALgeTALHVAALYDNLEAAVVLME-----AAPELvnepmt 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  368 ----RGETALHMAARAGQVEVVRCLLRNGA-LVDARA-----REEQT--------PLHIASRLGKTEIVQLLLQHMAHPD 429
Cdd:cd22192     84 sdlyQGETALHIAVVNQNLNLVRELIARGAdVVSPRAtgtffRPGPKnliyygehPLSFAACVGNEEIVRLLIEHGADIR 163

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1229385538  430 AATTNGYTPLHISAREGQVDVA----SVLLEA---GAAHSLAT---KKGFTPLHVAAKYGSLDVAKLLLQRR 491
Cdd:cd22192    164 AQDSLGNTVLHILVLQPNKTFAcqmyDLILSYdkeDDLQPLDLvpnNQGLTPFKLAAKEGNIVMFQHLVQKR 235
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 400-589 1.30e-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: 1.30e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  400 REEQTPLHIASRLGKTEIVQ-LLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAgaAHSLATK-------KGFTP 471
Cdd:cd22192     15 RISESPLLLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEA--APELVNEpmtsdlyQGETA 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  472 LHVAAKYGSLDVAKLLLQRRAAADSA---------GKNGLT-----PLHVAAHYDNQKVALLLLEKGASPHATAKNGYTP 537
Cdd:cd22192     93 LHIAVVNQNLNLVRELIARGADVVSPratgtffrpGPKNLIyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTV 172

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1229385538  538 LHI----AAKKNQMQIASTLLNYGAETNIVT------KQGVTPLHLASQEGHTDMVTLLLDK 589
Cdd:cd22192    173 LHIlvlqPNKTFACQMYDLILSYDKEDDLQPldlvpnNQGLTPFKLAAKEGNIVMFQHLVQK 234
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 25-164 1.76e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 80.86  E-value: 1.76e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538   25 KVVEYLKG-GIDINTCNQNGLNALHLAAKEGHVGL--VQELLGRGSSVDSATKkgntalhiaslagqaevVKVLVKEGAN 101
Cdd:PHA03100   122 SIVEYLLDnGANVNIKNSDGENLLHLYLESNKIDLkiLKLLIDKGVDINAKNR-----------------VNYLLSYGVP 184

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1229385538  102 INAQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHNQAVAILLEN 164
Cdd:PHA03100   185 INIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNN 247
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 144-326 8.47e-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: 79.67  E-value: 8.47e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  144 TPLAVALQQGHNQAVAILLENDT-----KGKVRLPALHIAARKDDTKSAALLLQNDH---NADVQSK--SGFTPLHIAAH 213
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLLKCPScdlfqRGALGETALHVAALYDNLEAAVVLMEAAPelvNEPMTSDlyQGETALHIAVV 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  214 YGNVNVATLLLNRGAAVdFTARN---------------GITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHC-- 276
Cdd:cd22192     99 NQNLNLVRELIARGADV-VSPRAtgtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHIlv 177

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1229385538  277 --AARSGHDQVVELLL-----ERGAPL-LARTKNGLSPLHMAAQGDHVECVKHLLQHK 326
Cdd:cd22192    178 lqPNKTFACQMYDLILsydkeDDLQPLdLVPNNQGLTPFKLAAKEGNIVMFQHLVQKR 235
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 545-718 1.55e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 77.72  E-value: 1.55e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  545 NQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADILTKHGA 624
Cdd:PHA02875    13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  625 -DQDAHTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTAL 703
Cdd:PHA02875    93 fADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPL 172

                          170
                   ....*....|....*
gi 1229385538  704 AIAKRLGYISVVDTL 718
Cdd:PHA02875   173 IIAMAKGDIAICKML 187
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 553-690 1.11e-13

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 76.45  E-value: 1.11e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  553 LLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADILTKHGADQDAHTkl 632
Cdd:PLN03192   544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHA-- 621

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1229385538  633 GYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGA 690
Cdd:PLN03192   622 AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGA 679
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 469-719 3.74e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 73.76  E-value: 3.74e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  469 FTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDN-QKVALLLLEKGaspHATAKNGYTPLHIAAKKNQM 547
Cdd:PHA02878    38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNkLGMKEMIRSIN---KCSVFYTLVAIKDAFNNRNV 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  548 QIASTLL--NYGAETNIVTKQGVTPLHLASQEghTDMVTLLLDKGANIHMSTK-SGLTSLHLAAqEDKvnvadiltkhga 624
Cdd:PHA02878   115 EIFKIILtnRYKNIQTIDLVYIDKKSKDDIIE--AEITKLLLSYGADINMKDRhKGNTALHYAT-ENK------------ 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  625 dqdahtklgytplivachygNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTALA 704
Cdd:PHA02878   180 --------------------DQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLH 239

                          250
                   ....*....|....*
gi 1229385538  705 IAkrLGYISVVDTLK 719
Cdd:PHA02878   240 IS--VGYCKDYDILK 252
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 262-491 5.03e-13

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: 74.35  E-value: 5.03e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  262 QIDAKTRDGLTPLHCAA-RSGHDQVVELLLERGAplLARTknGLSPLHMAAQGdHVECVKHLLQH--KAPVDDVTLDYL- 337
Cdd:TIGR00870   44 NINCPDRLGRSALFVAAiENENLELTELLLNLSC--RGAV--GDTLLHAISLE-YVDAVEAILLHllAAFRKSGPLELAn 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  338 -----------TALHVAAHCGHYRVTKLLLDKRANPNARA-------------LR-GETALHMAARAGQVEVVRCLLRNG 392
Cdd:TIGR00870  119 dqytseftpgiTALHLAAHRQNYEIVKLLLERGASVPARAcgdffvksqgvdsFYhGESPLNAAACLGSPSIVALLSEDP 198

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  393 ALVDArareeqtplhiASRLGKTeivqllLQHMAHPDAATTNGYTPLHISAREGQVDvasvlLEAGAAHSLATK-----K 467
Cdd:TIGR00870  199 ADILT-----------ADSLGNT------LLHLLVMENEFKAEYEELSCQMYNFALS-----LLDKLRDSKELEvilnhQ 256

                          250       260
                   ....*....|....*....|....
gi 1229385538  468 GFTPLHVAAKYGSLDVAKLLLQRR 491
Cdd:TIGR00870  257 GLTPLKLAAKEGRIVLFRLKLAIK 280
PHA02798 PHA02798
ankyrin-like protein; Provisional
 477-696 1.25e-12

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 72.17  E-value: 1.25e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  477 KYGS-LDVAKLLLQRRAAADSAGKNGLTPLHVAAH---YDNQKVALLLLEKGASPHATAKNGYTPLHIAAKKN---QMQI 549
Cdd:PHA02798    84 DYKHmLDIVKILIENGADINKKNSDGETPLYCLLSngyINNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNhhiDIEI 163

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  550 ASTLLNYGAETNIVT-KQGVTPLHLASQEGHT----DMVTLLLDKGANIHMSTKSG-------LTSLHLAAQEDKVNVAD 617
Cdd:PHA02798   164 IKLLLEKGVDINTHNnKEKYDTLHCYFKYNIDridaDILKLFVDNGFIINKENKSHkkkfmeyLNSLLYDNKRFKKNILD 243

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1229385538  618 ILTKHgADQDAHTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHgaKPNATT 696
Cdd:PHA02798   244 FIFSY-IDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNK--KPNKNT 319
PHA02798 PHA02798
ankyrin-like protein; Provisional
 480-706 1.97e-12

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 71.79  E-value: 1.97e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  480 SLDVAKLLLQRRAAADSAGKNGLTPL-----HVAAHYDNQKVALLLLEKGASPHATAKNGYTPLHIAAKK---NQMQIAS 551
Cdd:PHA02798    50 STDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNgyiNNLEILL 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  552 TLLNYGAETNIVTKQGVTPLHLASQEGHT---DMVTLLLDKGANIHM-STKSGLTSLHLAAQED----KVNVADILTKHG 623
Cdd:PHA02798   130 FMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDINThNNKEKYDTLHCYFKYNidriDADILKLFVDNG 209

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  624 ---ADQDAHTKLGYTPLIVACHYGNVK----MVNFLLKQgANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATT 696
Cdd:PHA02798   210 fiiNKENKSHKKKFMEYLNSLLYDNKRfkknILDFIFSY-IDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIIT 288

                          250
                   ....*....|
gi 1229385538  697 ANGNTALAIA 706
Cdd:PHA02798   289 ELGNTCLFTA 298
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 12-146 3.24e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 71.82  E-value: 3.24e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538   12 ASFLRAARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTAL----------- 80
Cdd:PLN03192   527 SNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnaisakhhki 606

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538   81 -----HIASLA---------------GQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTA-T 139
Cdd:PLN03192   607 frilyHFASISdphaagdllctaakrNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAnT 686


                   ....*..
gi 1229385538  140 EDGFTPL 146
Cdd:PLN03192   687 DDDFSPT 693
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 50-164 6.28e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 70.67  E-value: 6.28e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538   50 AAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLY--------------- 114
Cdd:PLN03192   532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWnaisakhhkifrily 611

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1229385538  115 ----------------MAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHNQAVAILLEN 164
Cdd:PLN03192   612 hfasisdphaagdllcTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMN 677
Ank_4 pfam13637
Ankyrin repeats (many copies);
336-389 7.93e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 61.52  E-value: 7.93e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1229385538  336 YLTALHVAAHCGHYRVTKLLLDKRANPNARALRGETALHMAARAGQVEVVRCLL 389
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 75-226 8.32e-12

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: 70.17  E-value: 8.32e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538   75 KGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGF--------------TPLYMAAQENHIDVVKYLLENGANQSTAte 140
Cdd:cd22194    140 EGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVFfnpkykhegfyfgeTPLALAACTNQPEIVQLLMEKESTDITS-- 217

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  141 dgftplavalqqghnqavailleNDTKGKVRLPALHIAArkDDTKS----------AALLLQNDHNAD-VQSKSGFTPLH 209
Cdd:cd22194    218 -----------------------QDSRGNTVLHALVTVA--EDSKTqndfvkrmydMILLKSENKNLEtIRNNEGLTPLQ 272

                          170
                   ....*....|....*..
gi 1229385538  210 IAAHYGNVNVATLLLNR 226
Cdd:cd22194    273 LAAKMGKAEILKYILSR 289
Ank_4 pfam13637
Ankyrin repeats (many copies);
270-323 3.14e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.98  E-value: 3.14e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1229385538  270 GLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLL 323
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 249-439 6.07e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 67.59  E-value: 6.07e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  249 NTNMVKLLLDRGGQIDAKTRDglTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLLQHKAP 328
Cdd:PLN03192   506 DLNVGDLLGDNGGEHDDPNMA--SNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACN 583

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  329 VDDVTLDYLTALHVAAHCGHYRVTKLL--LDKRANPNAralrGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPL 406
Cdd:PLN03192   584 VHIRDANGNTALWNAISAKHHKIFRILyhFASISDPHA----AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATAL 659

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1229385538  407 HIASRLGKTEIVQLLLQHMAHPDAATT-NGYTPL 439
Cdd:PLN03192   660 QVAMAEDHVDMVRLLIMNGADVDKANTdDDFSPT 693
Ank_4 pfam13637
Ankyrin repeats (many copies);
239-290 6.17e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.21  E-value: 6.17e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1229385538  239 TPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLL 290
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02798 PHA02798
ankyrin-like protein; Provisional
 25-277 6.44e-11

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 66.78  E-value: 6.44e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538   25 KVVEYLKGGIDIN-TCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTAL-----HIASLAGQAEVVKVLVKE 98
Cdd:PHA02798    19 STVKLLIKSCNPNeIVNEYSIFQKYLQRDSPSTDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIEN 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538   99 GANINAQSQNGFTPLYMAAQE---NHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHN---QAVAILLE-----NDTK 167
Cdd:PHA02798    99 GADINKKNSDGETPLYCLLSNgyiNNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEkgvdiNTHN 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  168 GKVRLPALHIAARKD----DTKSAALLLQND---HNADVQSKSGFTPLHIAAHYGNVNVATLLLNR-GAAVDFTARN--G 237
Cdd:PHA02798   179 NKEKYDTLHCYFKYNidriDADILKLFVDNGfiiNKENKSHKKKFMEYLNSLLYDNKRFKKNILDFiFSYIDINQVDelG 258

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1229385538  238 ITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCA 277
Cdd:PHA02798   259 FNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTA 298
Ank_4 pfam13637
Ankyrin repeats (many copies);
303-356 8.78e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.83  E-value: 8.78e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1229385538  303 GLSPLHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLL 356
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 17-163 8.82e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 66.17  E-value: 8.82e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538   17 AARAGNLDKVVEYLKGGIDIN-TCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVL 95
Cdd:PHA02875    75 AVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELL 154

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1229385538   96 VKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTATEDG-FTPLAVALQQGHNQAVAILLE 163
Cdd:PHA02875   155 IDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIK 223
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 364-490 1.14e-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: 66.32  E-value: 1.14e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  364 ARALRGETALHMAARAGQVEVVRCLLRNGALVDARA---------REE-----QTPLHIASRLGKTEIVQLLLQHMAHPD 429
Cdd:cd22194    136 EEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAkgvffnpkyKHEgfyfgETPLALAACTNQPEIVQLLMEKESTDI 215

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1229385538  430 AAT-TNGYTPLH---ISAREGQVDVASV------LLEAGAAHSLAT---KKGFTPLHVAAKYGSLDVAKLLLQR 490
Cdd:cd22194    216 TSQdSRGNTVLHalvTVAEDSKTQNDFVkrmydmILLKSENKNLETirnNEGLTPLQLAAKMGKAEILKYILSR 289
Ank_4 pfam13637
Ankyrin repeats (many copies);
76-129 1.45e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.05  E-value: 1.45e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1229385538   76 GNTALHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLL 129
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
633-686 1.55e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.05  E-value: 1.55e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1229385538  633 GYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLL 686
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 454-606 2.61e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 65.66  E-value: 2.61e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  454 LLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLL--LEKGASPHAta 531
Cdd:PLN03192   544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILyhFASISDPHA-- 621

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1229385538  532 knGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLDKGANI-HMSTKSGLTSLHL 606
Cdd:PLN03192   622 --AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVdKANTDDDFSPTEL 695
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 329-435 6.23e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 64.15  E-value: 6.23e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  329 VDDVTLDYLTA--LHVAAHcGHYRVTKLLLDKRANPNARALRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPL 406
Cdd:PTZ00322    74 IDPVVAHMLTVelCQLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPL 152

                           90       100
                   ....*....|....*....|....*....
gi 1229385538  407 HIASRLGKTEIVQLLLQHMAHPDAATTNG 435
Cdd:PTZ00322   153 ELAEENGFREVVQLLSRHSQCHFELGANA 181
Ank_4 pfam13637
Ankyrin repeats (many copies);
501-554 9.73e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.74  E-value: 9.73e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1229385538  501 GLTPLHVAAHYDNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQMQIASTLL 554
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 413-501 1.24e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 62.99  E-value: 1.24e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  413 GKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRA 492
Cdd:PTZ00322    93 GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQ 172


                   ....*....
gi 1229385538  493 AADSAGKNG 501
Cdd:PTZ00322   173 CHFELGANA 181
PHA02946 PHA02946
ankyin-like protein; Provisional
 472-686 1.30e-09

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 62.38  E-value: 1.30e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  472 LHVAAKYGS--LDVAKLLLQrraAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQMQI 549
Cdd:PHA02946    11 LSLYAKYNSknLDVFRNMLQ---AIEPSGNYHILHAYCGIKGLDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRI 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  550 ASTLLNYGAETNIVTKQGVTPLHLAS--QEGHTDMVTLLLDKGANIHMST-KSGLTSL---------------------- 604
Cdd:PHA02946    88 VAMLLTHGADPNACDKQHKTPLYYLSgtDDEVIERINLLVQYGAKINNSVdEEGCGPLlactdpservfkkimsigfear 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  605 ------------HLAAQEDKVNVADILTKHGADQDAHTKLGYTPLIVACH--YGNVKMVNFLLKQgANVNAKTKNGYTPL 670
Cdd:PHA02946   168 ivdkfgknhihrHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCSktVKNVDIINLLLPS-TDVNKQNKFGDSPL 246

                          250
                   ....*....|....*..
gi 1229385538  671 HQAAQQ-GHTHIINVLL 686
Cdd:PHA02946   247 TLLIKTlSPAHLINKLL 263
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 9-139 1.88e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.93  E-value: 1.88e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538    9 DSNASFLRAARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQ 88
Cdd:PHA02875   101 DGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGD 180

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1229385538   89 AEVVKVLVKEGANINAQSQNG-FTPLYMAAQENHIDVVKYLLENGANQSTAT 139
Cdd:PHA02875   181 IAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNIMF 232
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 569-705 3.18e-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: 3.18e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  569 TPLHLASQEGHTDMV-TLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADILTkhgadqDAHTKL-----------GYTP 636
Cdd:cd22192     19 SPLLLAAKENDVQAIkKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLM------EAAPELvnepmtsdlyqGETA 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  637 LIVACHYGNVKMVNFLLKQGANVNAKTKNGYT--------------PLHQAAQQGHTHIINVLLQHGAKPNATTANGNTA 702
Cdd:cd22192     93 LHIAVVNQNLNLVRELIARGADVVSPRATGTFfrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTV 172


                   ...
gi 1229385538  703 LAI 705
Cdd:cd22192    173 LHI 175
PHA02946 PHA02946
ankyin-like protein; Provisional
 405-653 3.59e-09

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 61.22  E-value: 3.59e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  405 PLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPL-HISAREGQV-DVASVLLEAGAA-HSLATKKGFTPLhVAAKYGSL 481
Cdd:PHA02946    75 PLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLyYLSGTDDEViERINLLVQYGAKiNNSVDEEGCGPL-LACTDPSE 153

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  482 DVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALL--LLEKGASPHATAKNGYTPLHIAAKKNQMQI-ASTLLNYGA 558
Cdd:PHA02946   154 RVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNPKASTIswMMKLGISPSKPDHDGNTPLHIVCSKTVKNVdIINLLLPST 233

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  559 ETNIVTKQGVTPLHLASQeghtdmvTLLLDKGANIHMSTKSGLT--SLHLAAQEDKVNVADILTKHGADQDAhtklgyTP 636
Cdd:PHA02946   234 DVNKQNKFGDSPLTLLIK-------TLSPAHLINKLLSTSNVITdqTVNICIFYDRDDVLEIINDKGKQYDS------TD 300

                          250
                   ....*....|....*..
gi 1229385538  637 LIVACHYGNVKMVNFLL 653
Cdd:PHA02946   301 FKMAVEVGSIRCVKYLL 317
Ank_4 pfam13637
Ankyrin repeats (many copies);
534-587 3.68e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.20  E-value: 3.68e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1229385538  534 GYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLL 587
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
171-224 3.79e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.20  E-value: 3.79e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1229385538  171 RLPALHIAARKDDTKSAALLLQNDHNADVQSKSGFTPLHIAAHYGNVNVATLLL 224
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
206-257 5.19e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.82  E-value: 5.19e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1229385538  206 TPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLL 257
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 412-598 5.24e-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: 5.24e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  412 LGKTEIVQLLLQHMAHPDAATtnGYTPLHISA---REGQVDVASVLLEA----GAAHSLATK-------KGFTPLHVAAK 477
Cdd:cd21882      5 LGLLECLRWYLTDSAYQRGAT--GKTCLHKAAlnlNDGVNEAIMLLLEAapdsGNPKELVNApctdefyQGQTALHIAIE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  478 YGSLDVAKLLLQRRAAADSAGKN-------------GLTPLHVAAHYDNQKVALLLLEKGASPHATAKN---GYTPLHI- 540
Cdd:cd21882     83 NRNLNLVRLLVENGADVSARATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPAALEAQdslGNTVLHAl 162

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1229385538  541 --------AAKKNQMQIASTLLNYGAETN-------IVTKQGVTPLHLASQEGHTDMVTLLLDK---GANIHMSTK 598
Cdd:cd21882    163 vlqadntpENSAFVCQMYNLLLSYGAHLDptqqleeIPNHQGLTPLKLAAVEGKIVMFQHILQRefsGPYQPLSRK 238
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 338-490 5.66e-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: 5.66e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  338 TALHVAA---HCGHYRVTKLLLD---KRANP----NARAL----RGETALHMAARAGQVEVVRCLLRNGALVDARA---- 399
Cdd:cd21882     28 TCLHKAAlnlNDGVNEAIMLLLEaapDSGNPkelvNAPCTdefyQGQTALHIAIENRNLNLVRLLVENGADVSARAtgrf 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  400 -REEQT--------PLHIASRLGKTEIVQLLLQHMAHPDAATTN---GYTPLHI------SAREGQVDVASV---LLEAG 458
Cdd:cd21882    108 fRKSPGnlfyfgelPLSLAACTNQEEIVRLLLENGAQPAALEAQdslGNTVLHAlvlqadNTPENSAFVCQMynlLLSYG 187

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1229385538  459 AA-------HSLATKKGFTPLHVAAKYGSLDVAKLLLQR 490
Cdd:cd21882    188 AHldptqqlEEIPNHQGLTPLKLAAVEGKIVMFQHILQR 226
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 104-326 5.76e-09

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 60.87  E-value: 5.76e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  104 AQSQNGFTPlymAAQENHIDVVKYLLENGA--NQSTATEDGFTPLAVALQQGHNQAVAILLEN-DTKGKVRLPALHIAAR 180
Cdd:TIGR00870   15 SDEEKAFLP---AAERGDLASVYRDLEEPKklNINCPDRLGRSALFVAAIENENLELTELLLNlSCRGAVGDTLLHAISL 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  181 --------------KDDTKSAALLLQNDHNADVQSKsGFTPLHIAAHYGNVNVATLLLNRGAAVDFTA------------ 234
Cdd:TIGR00870   92 eyvdaveaillhllAAFRKSGPLELANDQYTSEFTP-GITALHLAAHRQNYEIVKLLLERGASVPARAcgdffvksqgvd 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  235 --RNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCA-------------ARSGHDQVVElLLERGAPL--- 296
Cdd:TIGR00870  171 sfYHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLvmenefkaeyeelSCQMYNFALS-LLDKLRDSkel 249

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1229385538  297 -LARTKNGLSPLHMAAQGDHVECVKHLLQHK 326
Cdd:TIGR00870  250 eVILNHQGLTPLKLAAKEGRIVLFRLKLAIK 280
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 43-153 6.36e-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: 6.36e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538   43 GLNALHLAAKEGHVGLVQELLGRGSSVDS--AT----KKGNTAL-----HIASLA---GQAEVVKVLVKEGANINAQSQN 108
Cdd:cd22192     89 GETALHIAVVNQNLNLVRELIARGADVVSprATgtffRPGPKNLiyygeHPLSFAacvGNEEIVRLLIEHGADIRAQDSL 168

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1229385538  109 GFTPLYM-AAQENH------IDVVKYLLENGANQSTAT---EDGFTPLAVALQQG 153
Cdd:cd22192    169 GNTVLHIlVLQPNKtfacqmYDLILSYDKEDDLQPLDLvpnNQGLTPFKLAAKEG 223
Ank_4 pfam13637
Ankyrin repeats (many copies);
43-96 8.06e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.05  E-value: 8.06e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1229385538   43 GLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLV 96
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 368-490 8.25e-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: 8.25e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  368 RGETALHMAARAGQVEVVRCLLRNGALVDARAREE--------------QTPLHIASRLGKTEIVQLLLQHMAHP---DA 430
Cdd:cd22196     93 KGQTALHIAIERRNMHLVELLVQNGADVHARASGEffkkkkggpgfyfgELPLSLAACTNQLDIVKFLLENPHSPadiSA 172

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1229385538  431 ATTNGYTPLHI---SAREGQVDVASV------LLEAGAA-------HSLATKKGFTPLHVAAKYGSLDVAKLLLQR 490
Cdd:cd22196    173 RDSMGNTVLHAlveVADNTPENTKFVtkmyneILILGAKirpllklEEITNKKGLTPLKLAAKTGKIGIFAYILGR 248
Ank_4 pfam13637
Ankyrin repeats (many copies);
404-455 1.34e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.66  E-value: 1.34e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1229385538  404 TPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLL 455
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 374-462 1.49e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 59.53  E-value: 1.49e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  374 HMAArAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASV 453
Cdd:PTZ00322    88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                   ....*....
gi 1229385538  454 LLEAGAAHS 462
Cdd:PTZ00322   167 LSRHSQCHF 175
Death_FADD cd08306
Fas-associated Death Domain protein-protein interaction domain; Death domain (DD) found in ...
 1363-1433 1.52e-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: 1.52e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1229385538 1363 IADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKInRMDIV 1433
Cdd:cd08306      8 ICENLGRDWRQLARKLGLSETKIESISEAHPRNLREQVRQSLREWKKIKKAEATVADLIKALRDC-QLNLV 77
NESP55 pfam06390
Neuroendocrine-specific golgi protein P55 (NESP55); This family consists of several mammalian ...
 1510-1667 1.76e-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: 1.76e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538 1510 TFQDGVPKTEGDSSATALFPQTHKEQVQQDFSGKMQDLPEESSLEYQQEYFVTTPGTET-------SETQKAMIVPSSPS 1582
Cdd:pfam06390   62 SFLNAHHRSAAAAAAAQVFPEPSEPESDHEDEDFEPELARPECLEYDEDDFDTETDSETepesdieSETEFETEPETEPD 141

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538 1583 KTPE-EVSTPAEEEK--------------------LYLQTPTSSERGGSPIIQEPEEPSEHRE------ESSPR--KTSL 1633
Cdd:pfam06390  142 TAPTtEPETEPEDEPgpvvpkgatfhqslterlhaLKLQSADASPRRAPPSTQEPESAREGEEpergplDKDPRdpEEEE 221

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1229385538 1634 VIVESADNQPETCErldEDAAFEKGDDMPEIPPE 1667
Cdd:pfam06390  222 EEKEEEKQQPHRCK---PKKPARRRDPSPESPPK 252
Ank_5 pfam13857
Ankyrin repeats (many copies);
222-277 1.84e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 52.35  E-value: 1.84e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1229385538  222 LLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCA 277
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 470-587 2.02e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 59.14  E-value: 2.02e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  470 TPLHVAAKYGSLD--VAKLL----LQRRAAADSAGkngltplhvaahydnqkvALLLLEKGASPHATAKNGYTPLHIAAK 543
Cdd:PTZ00322    63 TPDHNLTTEEVIDpvVAHMLtvelCQLAASGDAVG------------------ARILLTGGADPNCRDYDGRTPLHIACA 124

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1229385538  544 KNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLL 587
Cdd:PTZ00322   125 NGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PHA02946 PHA02946
ankyin-like protein; Provisional
 58-331 2.20e-08

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 58.53  E-value: 2.20e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538   58 LVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLYM--AAQENHIDVVKYLLENGAN- 134
Cdd:PHA02946    54 FVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYlsGTDDEVIERINLLVQYGAKi 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  135 QSTATEDGFTPLAVAL---QQGHNQAVAILLENDTKGKVRLPALHIAARKDDTKSAAL--LLQNDHNADVQSKSGFTPLH 209
Cdd:PHA02946   134 NNSVDEEGCGPLLACTdpsERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNPKASTIswMMKLGISPSKPDHDGNTPLH 213

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  210 I--AAHYGNVNVATLLLnrgAAVDFTARN--GITPLHVASKR-GNTNMVKLLLDRGGQIDAKTrdgltpLHCAARSGHDQ 284
Cdd:PHA02946   214 IvcSKTVKNVDIINLLL---PSTDVNKQNkfGDSPLTLLIKTlSPAHLINKLLSTSNVITDQT------VNICIFYDRDD 284

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1229385538  285 VVELLLERGapllarTKNGLSPLHMAAQGDHVECVKHLLQHKAPVDD 331
Cdd:PHA02946   285 VLEIINDKG------KQYDSTDFKMAVEVGSIRCVKYLLDNDIICED 325
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 156-290 3.64e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 58.37  E-value: 3.64e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  156 QAVAILLENDTKGKVRLPALHIAARKDDTKSAALLLQNDHNADVQSKSGFTPLHIAAHyGNVNVATLLLNRGAAVDFTAR 235
Cdd:PTZ00322    35 ERMAAIQEEIARIDTHLEALEATENKDATPDHNLTTEEVIDPVVAHMLTVELCQLAAS-GDAVGARILLTGGADPNCRDY 113

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1229385538  236 NGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLL 290
Cdd:PTZ00322   114 DGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 568-699 4.24e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.99  E-value: 4.24e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  568 VTPLHLASQEGHTDMVTLlldkganiHMSTksgLTSLHLAAQEDKVNvADILTKHGADQDAHTKLGYTPLIVACHYGNVK 647
Cdd:PTZ00322    62 ATPDHNLTTEEVIDPVVA--------HMLT---VELCQLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQ 129

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1229385538  648 MVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATTANG 699
Cdd:PTZ00322   130 VVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGANA 181
PHA02798 PHA02798
ankyrin-like protein; Provisional
 316-593 4.41e-08

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 57.92  E-value: 4.41e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  316 VECVKHLLQHKAPVDDVTLDYLTAL-HVAAHCGHYR----VTKLLLDKRANPNARALRGETALHmaaragqvevvrCLLR 390
Cdd:PHA02798    51 TDIVKLFINLGANVNGLDNEYSTPLcTILSNIKDYKhmldIVKILIENGADINKKNSDGETPLY------------CLLS 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  391 NGAlvdarareeqtplhiasrLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREG---QVDVASVLLEAGA-AHSLATK 466
Cdd:PHA02798   119 NGY------------------INNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNhhiDIEIIKLLLEKGVdINTHNNK 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  467 KGFTPLHVAAKYG----SLDVAKLLLQRR---AAADSAGKNGLTPLHVAAHYDNQKV---ALLLLEKGASPHATAKNGYT 536
Cdd:PHA02798   181 EKYDTLHCYFKYNidriDADILKLFVDNGfiiNKENKSHKKKFMEYLNSLLYDNKRFkknILDFIFSYIDINQVDELGFN 260

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1229385538  537 PLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLDKGANI 593
Cdd:PHA02798   261 PLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKPNK 317
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 152-417 4.87e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 57.96  E-value: 4.87e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  152 QGHNQAVAILLENDTKGKVRLPALHIAARKDDtksaalllQNDHNADVQSKSGftpLHIAAHYGNVNVATLLLNRGAAVD 231
Cdd:PLN03192   484 QTRQEDNVVILKNFLQHHKELHDLNVGDLLGD--------NGGEHDDPNMASN---LLTVASTGNAALLEELLKAKLDPD 552

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  232 FTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLErgaplLARTKN---GLSPLH 308
Cdd:PLN03192   553 IGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYH-----FASISDphaAGDLLC 627

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  309 MAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAahcghyrvtkllldkranpnaralrgetalhMAarAGQVEVVRCL 388
Cdd:PLN03192   628 TAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVA-------------------------------MA--EDHVDMVRLL 674

                          250       260       270
                   ....*....|....*....|....*....|
gi 1229385538  389 LRNGALVD-ARAREEQTPLHIASRLGKTEI 417
Cdd:PLN03192   675 IMNGADVDkANTDDDFSPTELRELLQKREL 704
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 530-686 6.66e-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: 6.66e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  530 TAKN--GYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQ--------------GVTPLHLASQEGHTDMVTLLLDKGANI 593
Cdd:cd22194    135 TEEAyeGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEIVQLLMEKESTD 214

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  594 HMSTKS-GLTSLHLAaqedkVNVADiltkHGADQDAHTKLGYTPLIVACHYGNVKMVnfllkqganvnaKTKNGYTPLHQ 672
Cdd:cd22194    215 ITSQDSrGNTVLHAL-----VTVAE----DSKTQNDFVKRMYDMILLKSENKNLETI------------RNNEGLTPLQL 273

                          170
                   ....*....|....
gi 1229385538  673 AAQQGHTHIINVLL 686
Cdd:cd22194    274 AAKMGKAEILKYIL 287
Ank_5 pfam13857
Ankyrin repeats (many copies);
454-508 6.70e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.42  E-value: 6.70e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1229385538  454 LLEAG-AAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVA 508
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 245-325 7.13e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.22  E-value: 7.13e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  245 SKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLLQ 324
Cdd:PTZ00322    90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169


                   .
gi 1229385538  325 H 325
Cdd:PTZ00322   170 H 170
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 9-246 8.46e-08

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 57.40  E-value: 8.46e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538    9 DSNASFLRAARAGNLD--KVVEYLKGGIDIntcnqnGLNALHLAAKEGHVGlVQELL--------GRGSS---VDSATK- 74
Cdd:TIGR00870   52 GRSALFVAAIENENLEltELLLNLSCRGAV------GDTLLHAISLEYVDA-VEAILlhllaafrKSGPLelaNDQYTSe 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538   75 --KGNTALHIASLAGQAEVVKVLVKEGANINA----------QSQNGF----TPLYMAAQENHIDVVKYLLENGANQSTA 138
Cdd:TIGR00870  125 ftPGITALHLAAHRQNYEIVKLLLERGASVPAracgdffvksQGVDSFyhgeSPLNAAACLGSPSIVALLSEDPADILTA 204

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  139 TEDGFTPLAVALQQGHNQAvaillENDTKG-KVRLPALHIAARKDDTKSAALLLQNDhnadvqsksGFTPLHIAAHYGNV 217
Cdd:TIGR00870  205 DSLGNTLLHLLVMENEFKA-----EYEELScQMYNFALSLLDKLRDSKELEVILNHQ---------GLTPLKLAAKEGRI 270

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1229385538  218 NVATLLLNRGAAV-DFTA-RNGitPLHVASK 246
Cdd:TIGR00870  271 VLFRLKLAIKYKQkKFVAwPNG--QQLLSLY 299
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 6-226 8.76e-08

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 56.94  E-value: 8.76e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538    6 QKSDSNASFLRAARAGNLDKVVEYLK-GGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSS-----VDSATKKGNTA 79
Cdd:cd22192     13 QKRISESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElvnepMTSDLYQGETA 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538   80 LHIASLAGQAEVVKVLVKEGANINAQSQNG--FT------------PLYMAAQENHIDVVKYLLENGANQSTATEDGFTP 145
Cdd:cd22192     93 LHIAVVNQNLNLVRELIARGADVVSPRATGtfFRpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTV 172

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  146 LAV-ALQQGHN---QAVAILLENDTKGkvRLPALhiaarkddtksaalllqnDHnadVQSKSGFTPLHIAAHYGNVNVAT 221
Cdd:cd22192    173 LHIlVLQPNKTfacQMYDLILSYDKED--DLQPL------------------DL---VPNNQGLTPFKLAAKEGNIVMFQ 229


                   ....*
gi 1229385538  222 LLLNR 226
Cdd:cd22192    230 HLVQK 234
Ank_4 pfam13637
Ankyrin repeats (many copies);
371-422 9.24e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.97  E-value: 9.24e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1229385538  371 TALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLL 422
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Death_p75NR cd08311
Death domain of p75 Neurotrophin Receptor; Death Domain (DD) found in p75 neurotrophin ...
 1349-1437 1.14e-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: 1.14e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538 1349 PQDEQERIEERLAyiADHLGFSWTELARELDFTEEQIHQIrienpNSLQDQSHALLKYWLERDGkhATDTNLVECLTKIN 1428
Cdd:cd08311      1 PPHKQEEVEKLLN--AGREGSDWRALAGELGYSAEEIDSF-----AREADPCRALLTDWSAQDG--ATLGVLLTALRKIG 71


                   ....*....
gi 1229385538 1429 RMDIVHLME 1437
Cdd:cd08311     72 RDDIVEILQ 80
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 515-716 1.29e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 56.29  E-value: 1.29e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  515 KVALLLLEKGASphaTAKNGY--TPL-------HIAAKKNQmQIASTLLNYGAETNIVTKQGVTPLH---LASQEGHTDM 582
Cdd:PHA02989    51 KIVKLLIDNGAD---VNYKGYieTPLcavlrnrEITSNKIK-KIVKLLLKFGADINLKTFNGVSPIVcfiYNSNINNCDM 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  583 VTLLLDKGANIH-MSTKSGLTSLHLAAQEDKVN--VADILTKHGADQDAHTKL-GYTPLIVACHYG----NVKMVNFLLK 654
Cdd:PHA02989   127 LRFLLSKGINVNdVKNSRGYNLLHMYLESFSVKkdVIKILLSFGVNLFEKTSLyGLTPMNIYLRNDidviSIKVIKYLIK 206

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  655 QGAN--------------------------------------VNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATT 696
Cdd:PHA02989   207 KGVNietnnngsesvlesfldnnkilskkefkvlnfilkyikINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVS 286

                          250       260
                   ....*....|....*....|
gi 1229385538  697 ANGNTALAIAKRLGYISVVD 716
Cdd:PHA02989   287 KDGDTVLTYAIKHGNIDMLN 306
Ank_5 pfam13857
Ankyrin repeats (many copies);
618-673 1.54e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 49.65  E-value: 1.54e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1229385538  618 ILTKHGADQDAHTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQA 673
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 550-622 1.62e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.06  E-value: 1.62e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1229385538  550 ASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADILTKH 622
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
Death_RAIDD cd08319
Death domain of RIP-associated ICH-1 homologous protein with a death domain; Death domain (DD) ...
 1357-1428 1.68e-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: 1.68e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1229385538 1357 EERLAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKIN 1428
Cdd:cd08319      2 DRQLNKLAQRLGPEWEQVLLDLGLSKADIYRCKADHPYNVQSQIVEALVKWKQRQGKKATVQSLIQSLKAVE 73
Ank_5 pfam13857
Ankyrin repeats (many copies);
652-706 1.72e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 49.27  E-value: 1.72e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1229385538  652 LLKQG-ANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTALAIA 706
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 312-497 1.83e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 56.03  E-value: 1.83e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  312 QGDHVECVKHLLQHKAPVDDVTLDYLTA--------------LHVAAHCGHYRVTKLLLDKRANPNARALRGETALHMAA 377
Cdd:PLN03192   487 QEDNVVILKNFLQHHKELHDLNVGDLLGdnggehddpnmasnLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAA 566

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  378 RAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLlQHMAHPDAATTNGyTPLHISAREGQVDVASVLLEA 457
Cdd:PLN03192   567 SKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL-YHFASISDPHAAG-DLLCTAAKRNDLTAMKELLKQ 644

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1229385538  458 GAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSA 497
Cdd:PLN03192   645 GLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKA 684
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 75-259 2.68e-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: 55.63  E-value: 2.68e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538   75 KGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGF-------------TPLYMAAQENHIDVVKYLLENGANQstated 141
Cdd:cd22197     93 RGHSALHIAIEKRSLQCVKLLVENGADVHARACGRFfqkkqgtcfyfgeLPLSLAACTKQWDVVNYLLENPHQP------ 166

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  142 gftplavalqqghnqavAILLENDTKGKVRLPALHIAArkDDTKSAALLLQNDHNADVQSKSGFTPlhiaahygnvnvaT 221
Cdd:cd22197    167 -----------------ASLQAQDSLGNTVLHALVMIA--DNSPENSALVIKMYDGLLQAGARLCP-------------T 214

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1229385538  222 LLLNrgaavDFTARNGITPLHVASKRGNTNMVKLLLDR 259
Cdd:cd22197    215 VQLE-----EISNHEGLTPLKLAAKEGKIEIFRHILQR 247
Ank_4 pfam13637
Ankyrin repeats (many copies);
111-162 3.02e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.81  E-value: 3.02e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1229385538  111 TPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHNQAVAILL 162
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
666-718 3.24e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.42  E-value: 3.24e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1229385538  666 GYTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTALAIAKRLGYISVVDTL 718
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 605-718 3.51e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 55.29  E-value: 3.51e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  605 HLAAQEDKVNVADILTKHGADQDAHTKLGYTPLIVA-CHY---GNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTH 680
Cdd:PTZ00322    50 HLEALEATENKDATPDHNLTTEEVIDPVVAHMLTVElCQLaasGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQ 129

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1229385538  681 IINVLLQHGAKPNATTANGNTALAIAKRLGYISVVDTL 718
Cdd:PTZ00322   130 VVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
Ank_5 pfam13857
Ankyrin repeats (many copies);
553-607 3.51e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.50  E-value: 3.51e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1229385538  553 LLNYG-AETNIVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLA 607
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 48-129 3.88e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.90  E-value: 3.88e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538   48 HLAAKEGHVGlVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKY 127
Cdd:PTZ00322    88 QLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                   ..
gi 1229385538  128 LL 129
Cdd:PTZ00322   167 LS 168
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 25-376 4.00e-07

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 54.92  E-value: 4.00e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538   25 KVVEYL--KGGIDIN-TCNQNGLNALHlaakeghvglvqellgrgssvdsaTKKGNTALHIaslagqaEVVKVLVKEGAN 101
Cdd:PHA02716   156 DLIKYMvdVGIVNLNyVCKKTGYGILH------------------------AYLGNMYVDI-------DILEWLCNNGVN 204

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  102 INAQSQNGFTPL--YMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHN---QAVAILLENDTKGKVR-LPA- 174
Cdd:PHA02716   205 VNLQNNHLITPLhtYLITGNVCASVIKKIIELGGDMDMKCVNGMSPIMTYIINIDNinpEITNIYIESLDGNKVKnIPMi 284

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  175 LHI---AARKDDTKSAALLLQNDHNADVQSKSGFTPLH--IAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRG- 248
Cdd:PHA02716   285 LHSyitLARNIDISVVYSFLQPGVKLHYKDSAGRTCLHqyILRHNISTDIIKLLHEYGNDLNEPDNIGNTVLHTYLSMLs 364

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  249 -------------NTNMVKLLLDRGGQIDAKTRDGLTPLH---CAARS--GHDQVVELLLERgapLLARTKNGLSPlHMA 310
Cdd:PHA02716   365 vvnildpetdndiRLDVIQCLISLGADITAVNCLGYTPLTsyiCTAQNymYYDIIDCLISDK---VLNMVKHRILQ-DLL 440

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1229385538  311 AQGDHVECVKH--LLQHKAPVDDVTLDY----LTALHVAAHCGhyrvtkllLDKRANPNARALRGETALHMA 376
Cdd:PHA02716   441 IRVDDTPCIIHhiIAKYNIPTDLYTDEYepydSTKIHDVYHCA--------IIERYNNAVCETSGMTPLHVS 504
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 75-226 5.06e-07

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: 54.43  E-value: 5.06e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538   75 KGNTALHIASLAGQAEVVKVLVKEGANINA----------QSQNGF----TPLYMAAQENHIDVVKYLLEN---GANQST 137
Cdd:cd22196     93 KGQTALHIAIERRNMHLVELLVQNGADVHArasgeffkkkKGGPGFyfgeLPLSLAACTNQLDIVKFLLENphsPADISA 172

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  138 ATEDGFTPL----AVALQQGHNQAVAILLEND--TKGKVRLPALHIAArkddtksaalllqndhnadVQSKSGFTPLHIA 211
Cdd:cd22196    173 RDSMGNTVLhalvEVADNTPENTKFVTKMYNEilILGAKIRPLLKLEE-------------------ITNKKGLTPLKLA 233

                          170
                   ....*....|....*
gi 1229385538  212 AHYGNVNVATLLLNR 226
Cdd:cd22196    234 AKTGKIGIFAYILGR 248
Ank_4 pfam13637
Ankyrin repeats (many copies);
567-619 5.08e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.04  E-value: 5.08e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1229385538  567 GVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADIL 619
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank_4 pfam13637
Ankyrin repeats (many copies);
470-521 5.19e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.04  E-value: 5.19e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1229385538  470 TPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLL 521
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Death_NMPP84 cd08318
Death domain of Nuclear Matrix Protein P84; Death domain (DD) found in the Nuclear Matrix ...
 1353-1432 5.24e-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: 5.24e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538 1353 QERIEErlayIADHLGFSWTELARELDFTEEQIHQIRiENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDI 1432
Cdd:cd08318      7 SEQIDV----LANKLGEQWKTLAPYLEMKDKDIRQIE-SDSEDMKMRAKQLLVTWQDREGAQATPEILMTALNAAGLNEI 81
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 84-162 5.28e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.52  E-value: 5.28e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1229385538   84 SLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHNQAVAILL 162
Cdd:PTZ00322    90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
Ank_5 pfam13857
Ankyrin repeats (many copies);
322-376 5.35e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.11  E-value: 5.35e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1229385538  322 LLQHKaPVDDVTLDY--LTALHVAAHCGHYRVTKLLLDKRANPNARALRGETALHMA 376
Cdd:pfam13857    1 LLEHG-PIDLNRLDGegYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 381-607 7.77e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 53.59  E-value: 7.77e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  381 QVEVVRCLLRNGALVDARAREEqTPL-------HIASRLGKtEIVQLLLQHMAHPDAATTNGYTPL-------HISareg 446
Cdd:PHA02989    49 KIKIVKLLIDNGADVNYKGYIE-TPLcavlrnrEITSNKIK-KIVKLLLKFGADINLKTFNGVSPIvcfiynsNIN---- 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  447 QVDVASVLLEAGA-AHSLATKKGFTPLHVAAKYGSL--DVAKLLLqrRAAADSAGKN---GLTPLHVAAHYD----NQKV 516
Cdd:PHA02989   123 NCDMLRFLLSKGInVNDVKNSRGYNLLHMYLESFSVkkDVIKILL--SFGVNLFEKTslyGLTPMNIYLRNDidviSIKV 200

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  517 ALLLLEKGAS------PHATAKNGYTPLHIAAKKNQMQIASTLLNYgAETNIVTKQGVTPLHLASQEGHTDMVTLLLDKG 590
Cdd:PHA02989   201 IKYLIKKGVNietnnnGSESVLESFLDNNKILSKKEFKVLNFILKY-IKINKKDKKGFNPLLISAKVDNYEAFNYLLKLG 279

                          250
                   ....*....|....*..
gi 1229385538  591 ANIHMSTKSGLTSLHLA 607
Cdd:PHA02989   280 DDIYNVSKDGDTVLTYA 296
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 75-226 7.80e-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: 54.03  E-value: 7.80e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538   75 KGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGF--------------TPLYMAAQENHIDVVKYLLENganqstate 140
Cdd:cd22193     75 EGQTALHIAIERRQGDIVALLVENGADVHAHAKGRFfqpkyqgegfyfgeLPLSLAACTNQPDIVQYLLEN--------- 145

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  141 dgftplavalqqghNQAVAILLENDTKGKVRLPALHIAArkDDTKSAALLLQNDHNADVQ---------------SKSGF 205
Cdd:cd22193    146 --------------EHQPADIEAQDSRGNTVLHALVTVA--DNTKENTKFVTRMYDMILIrgaklcptveleeirNNDGL 209

                          170       180
                   ....*....|....*....|.
gi 1229385538  206 TPLHIAAHYGNVNVATLLLNR 226
Cdd:cd22193    210 TPLQLAAKMGKIEILKYILQR 230
Ank_5 pfam13857
Ankyrin repeats (many copies);
256-310 8.48e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.34  E-value: 8.48e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1229385538  256 LLDRGGQ-IDAKTRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMA 310
Cdd:pfam13857    1 LLEHGPIdLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 75-226 8.75e-07

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 53.73  E-value: 8.75e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538   75 KGNTALHIASLAGQAEVVKVLVKEGANINAQS---------QNGF----TPLYMAAQENHIDVVKYLLENGANqstated 141
Cdd:cd21882     72 QGQTALHIAIENRNLNLVRLLVENGADVSARAtgrffrkspGNLFyfgeLPLSLAACTNQEEIVRLLLENGAQ------- 144

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  142 gftplavalqqghnqaVAILLENDTKGKVRLPALHIAARKDDTKSA------ALLLQNDHNAD-------VQSKSGFTPL 208
Cdd:cd21882    145 ----------------PAALEAQDSLGNTVLHALVLQADNTPENSAfvcqmyNLLLSYGAHLDptqqleeIPNHQGLTPL 208

                          170
                   ....*....|....*...
gi 1229385538  209 HIAAHYGNVNVATLLLNR 226
Cdd:cd21882    209 KLAAVEGKIVMFQHILQR 226
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 397-559 9.03e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.75  E-value: 9.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  397 ARAREEQTPLHIA-SRLG--KTEIVQLLlQHMAHPDAATTNGYTPLHISAREGQVDVAsvlleagAAHSLATKKgftpLH 473
Cdd:PTZ00322    21 TEGSRKRRAKPISfERMAaiQEEIARID-THLEALEATENKDATPDHNLTTEEVIDPV-------VAHMLTVEL----CQ 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  474 VAAKyGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQMQIASTL 553
Cdd:PTZ00322    89 LAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167


                   ....*.
gi 1229385538  554 LNYGAE 559
Cdd:PTZ00322   168 SRHSQC 173
Ank_5 pfam13857
Ankyrin repeats (many copies);
32-83 9.54e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.34  E-value: 9.54e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1229385538   32 GGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIA 83
Cdd:pfam13857    5 GPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
520-574 9.64e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.34  E-value: 9.64e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1229385538  520 LLEKG-ASPHATAKNGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLA 574
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 199-593 1.00e-06

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 53.76  E-value: 1.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  199 VQSKSGFTPLHiaAHYGNVNVAT----LLLNRGAAVDFTARNGITPLHVASKRGN--TNMVKLLLDRGGQIDAKTRDGLT 272
Cdd:PHA02716   172 VCKKTGYGILH--AYLGNMYVDIdileWLCNNGVNVNLQNNHLITPLHTYLITGNvcASVIKKIIELGGDMDMKCVNGMS 249

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  273 PLH---CAARSGHDQVVELLLERGAPllARTKNGLSPLHM---AAQGDHVECVKHLLQhkapvDDVTLDY-----LTALH 341
Cdd:PHA02716   250 PIMtyiINIDNINPEITNIYIESLDG--NKVKNIPMILHSyitLARNIDISVVYSFLQ-----PGVKLHYkdsagRTCLH 322

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  342 --VAAHCGHYRVTKLLLDKRANPNARALRGETALHMaaragqvevvrcLLRNGALVDARAREEQTPLHIasrlgktEIVQ 419
Cdd:PHA02716   323 qyILRHNISTDIIKLLHEYGNDLNEPDNIGNTVLHT------------YLSMLSVVNILDPETDNDIRL-------DVIQ 383

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  420 LLLQHMAHPDAATTNGYTPL--HISAREGQV--DVASVLLEAGAAH--------SLATKKGFTPL---HVAAKYGSldVA 484
Cdd:PHA02716   384 CLISLGADITAVNCLGYTPLtsYICTAQNYMyyDIIDCLISDKVLNmvkhrilqDLLIRVDDTPCiihHIIAKYNI--PT 461

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  485 KLLLQRRAAADSAGKNGLTPLHVAAHYDNQkvallLLEkgasphataKNGYTPLHIAAKKNQ-----MQIASTLLNYGAE 559
Cdd:PHA02716   462 DLYTDEYEPYDSTKIHDVYHCAIIERYNNA-----VCE---------TSGMTPLHVSIISHTnanivMDSFVYLLSIQYN 527

                          410       420       430
                   ....*....|....*....|....*....|....*....
gi 1229385538  560 TNIVTKQGVTPLHLASQE----GHTD-MVTLLLDKGANI 593
Cdd:PHA02716   528 INIPTKNGVTPLMLTMRNnrlsGHQWyIVKNILDKRPNV 566
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 472-589 1.11e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 52.29  E-value: 1.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  472 LHVAAKYGSLDVAKLLLQRRAAADSAGKNGL----TPLHVAAHYDNQKVALLLLEKGASPHATAKNG-YTPLHIAAKKNQ 546
Cdd:PHA02884    37 LYSSIKFHYTDIIDAILKLGADPEAPFPLSEnsktNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAkITPLYISVLHGC 116

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1229385538  547 MQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLDK 589
Cdd:PHA02884   117 LKCLEILLSYGADINIQTNDMVTPIELALMICNNFLAFMICDN 159
Ank_5 pfam13857
Ankyrin repeats (many copies);
354-409 1.15e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.96  E-value: 1.15e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1229385538  354 LLLDKRANPNARALRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIA 409
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 501-615 1.22e-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: 1.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  501 GLTPLHVAAHYDNQKVALLLLEKGASPHATAKN--------------GYTPLHIAAKKNQMQIASTLLNygAETNIVTKQ 566
Cdd:cd22194    141 GQTALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEIVQLLME--KESTDITSQ 218

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1229385538  567 ---GVTPLHL-----ASQEGHTDMVTLLLD------KGANIH-MSTKSGLTSLHLAAQEDKVNV 615
Cdd:cd22194    219 dsrGNTVLHAlvtvaEDSKTQNDFVKRMYDmillksENKNLEtIRNNEGLTPLQLAAKMGKAEI 282
Ank_5 pfam13857
Ankyrin repeats (many copies);
190-244 1.26e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.96  E-value: 1.26e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1229385538  190 LLQNDH-NADVQSKSGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVA 244
Cdd:pfam13857    1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
435-488 1.33e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.88  E-value: 1.33e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1229385538  435 GYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLL 488
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 269-301 1.49e-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: 46.13  E-value: 1.49e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1229385538  269 DGLTPLHCAA-RSGHDQVVELLLERGAPLLARTK 301
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 366-490 1.93e-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: 1.93e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  366 ALRGETALHMAARAGQVEVVRCLLRNGALVDARAREE--------------QTPLHIASRLGKTEIVQLLLQHMAHP--- 428
Cdd:cd22193     73 YYEGQTALHIAIERRQGDIVALLVENGADVHAHAKGRffqpkyqgegfyfgELPLSLAACTNQPDIVQYLLENEHQPadi 152

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1229385538  429 DAATTNGYTPLHI------SAREGQVDVASV---LLEAGAA-------HSLATKKGFTPLHVAAKYGSLDVAKLLLQR 490
Cdd:cd22193    153 EAQDSRGNTVLHAlvtvadNTKENTKFVTRMydmILIRGAKlcptvelEEIRNNDGLTPLQLAAKMGKIEILKYILQR 230
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 445-619 1.95e-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: 1.95e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  445 EGQVDVASVLLEagaahsLATKKGFTPLHVAAKYgsldvaklllqrraaADSAGKnGLTPLHVAAHYDNQKVALLLLEKG 524
Cdd:cd22196     60 NGQNDTISLLLD------IAEKTGNLKEFVNAAY---------------TDSYYK-GQTALHIAIERRNMHLVELLVQNG 117

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  525 ASPHATA----------KNGY----TPLHIAAKKNQMQIASTLLN---YGAETNIVTKQGVTPLH---------LASQEG 578
Cdd:cd22196    118 ADVHARAsgeffkkkkgGPGFyfgeLPLSLAACTNQLDIVKFLLEnphSPADISARDSMGNTVLHalvevadntPENTKF 197

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1229385538  579 HTDMVTLLLDKGANIH-------MSTKSGLTSLHLAAQEDKVNV-ADIL 619
Cdd:cd22196    198 VTKMYNEILILGAKIRpllkleeITNKKGLTPLKLAAKTGKIGIfAYIL 246
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 571-707 1.96e-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: 1.96e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  571 LHLASQEGHTDMVTLLLDKGANIHMstksGLTSLHLAAQEDKVNVADILT---KHGADQDAHTKL----------GYTPL 637
Cdd:TIGR00870   57 FVAAIENENLELTELLLNLSCRGAV----GDTLLHAISLEYVDAVEAILLhllAAFRKSGPLELAndqytseftpGITAL 132

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  638 IVACHYGNVKMVNFLLKQGANVNAKTK--------------NGYTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTAL 703
Cdd:TIGR00870  133 HLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLL 212


                   ....
gi 1229385538  704 AIAK 707
Cdd:TIGR00870  213 HLLV 216
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 160-264 2.06e-06

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 49.49  E-value: 2.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  160 ILLENDTKGKvrlPALHIAARKD--DTKSAALLLQnDHNADVQSKS---GFTPLHIAAHYGNVNVATLLLNRgAAVDFTA 234
Cdd:PHA02736    47 LVLEYNRHGK---QCVHIVSNPDkaDPQEKLKLLM-EWGADINGKErvfGNTPLHIAVYTQNYELATWLCNQ-PGVNMEI 121

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1229385538  235 RNGI--TPLHVASKRGNTNMVKLLLDRGGQID 264
Cdd:PHA02736   122 LNYAfkTPYYVACERHDAKMMNILRAKGAQCK 153
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 613-706 2.11e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 52.56  E-value: 2.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  613 VNVADILTKHGADQDahTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKP 692
Cdd:PLN03192   507 LNVGDLLGDNGGEHD--DPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNV 584

                           90
                   ....*....|....*.
gi 1229385538  693 NATTANGNTAL--AIA 706
Cdd:PLN03192   585 HIRDANGNTALwnAIS 600
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 30-259 2.30e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 52.05  E-value: 2.30e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538   30 LKGGIDINTCNQNGLNALHLAAKEGHVG---LVQELLGRGSSVDSATK-KGNTALHI--ASLAGQAEVVKVLVKEGANI- 102
Cdd:PHA02989    95 LKFGADINLKTFNGVSPIVCFIYNSNINncdMLRFLLSKGINVNDVKNsRGYNLLHMylESFSVKKDVIKILLSFGVNLf 174

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  103 NAQSQNGFTPL--YMAAQEN--HIDVVKYLLENGANQSTATedgftplavalqQGHNQAVAILLENdtkgkvrlpalHIA 178
Cdd:PHA02989   175 EKTSLYGLTPMniYLRNDIDviSIKVIKYLIKKGVNIETNN------------NGSESVLESFLDN-----------NKI 231

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  179 ARKDDTKSAALLLQ--NDHNADvqsKSGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLL 256
Cdd:PHA02989   232 LSKKEFKVLNFILKyiKINKKD---KKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNRI 308


                   ...
gi 1229385538  257 LDR 259
Cdd:PHA02989   309 LQL 311
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 108-134 2.38e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 45.27  E-value: 2.38e-06
                            10        20
                    ....*....|....*....|....*..
gi 1229385538   108 NGFTPLYMAAQENHIDVVKYLLENGAN 134
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 13-292 2.99e-06

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 52.22  E-value: 2.99e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538   13 SFLRAARAGNLDKVVEYLKGGIDINTCNQNGLNALH--LAAKEGHVGLVQELLGRGSSVDSATKKGNTALHiaSLAGQAE 90
Cdd:PHA02716   287 SYITLARNIDISVVYSFLQPGVKLHYKDSAGRTCLHqyILRHNISTDIIKLLHEYGNDLNEPDNIGNTVLH--TYLSMLS 364

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538   91 VVKVLVKEGAN-INaqsqngftplymaaqenhIDVVKYLLENGANQSTATEDGFTPLAVALQQGHN----QAVAILLEND 165
Cdd:PHA02716   365 VVNILDPETDNdIR------------------LDVIQCLISLGADITAVNCLGYTPLTSYICTAQNymyyDIIDCLISDK 426

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  166 TKGKVRLPALH-IAARKDDTKS------AALLLQNDHNADVQSKSGFTPLHIAAHYgnvnvATLLLNRGAAVDFTarnGI 238
Cdd:PHA02716   427 VLNMVKHRILQdLLIRVDDTPCiihhiiAKYNIPTDLYTDEYEPYDSTKIHDVYHC-----AIIERYNNAVCETS---GM 498

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1229385538  239 TPLHVA-SKRGNTNMV----KLLLDRGGQIDAKTRDGLTPLHCAAR----SGHD-QVVELLLER 292
Cdd:PHA02716   499 TPLHVSiISHTNANIVmdsfVYLLSIQYNINIPTKNGVTPLMLTMRnnrlSGHQwYIVKNILDK 562
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 498-655 3.09e-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: 3.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  498 GKNGLTPLHVAAHYDNQKV---ALLLLE---KGASPHATAK--------NGYTPLHIAAKKNQMQIASTLLNYGAETNIV 563
Cdd:cd21882     23 GATGKTCLHKAALNLNDGVneaIMLLLEaapDSGNPKELVNapctdefyQGQTALHIAIENRNLNLVRLLVENGADVSAR 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  564 TKQ-------------GVTPLHLASQEGHTDMVTLLLDKGANIHMSTKS---GLTSLH-LAAQEDK--------VNVADI 618
Cdd:cd21882    103 ATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPAALEAQdslGNTVLHaLVLQADNtpensafvCQMYNL 182

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1229385538  619 LTKHGADQDAHTKL-------GYTPLIVACHYGNVKMVNFLLKQ 655
Cdd:cd21882    183 LLSYGAHLDPTQQLeeipnhqGLTPLKLAAVEGKIVMFQHILQR 226
Ank_5 pfam13857
Ankyrin repeats (many copies);
486-541 3.92e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.42  E-value: 3.92e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1229385538  486 LLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHATAKNGYTPLHIA 541
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 435-640 5.03e-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: 5.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  435 GYTPLHISAREGQV-DVASVLLEagaaHSLATKKGFTPLHVAAKyGSLDVAKLLLQRRAAADSAGKN------------- 500
Cdd:TIGR00870   52 GRSALFVAAIENENlELTELLLN----LSCRGAVGDTLLHAISL-EYVDAVEAILLHLLAAFRKSGPlelandqytseft 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  501 -GLTPLHVAAHYDNQKVALLLLEKGASPHATAK--------------NGYTPLHIAAKKNQMQIASTLLNYGAETNIVTK 565
Cdd:TIGR00870  127 pGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADS 206

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  566 QGVTPLHLASQEGH---------TDMVTLLLDKGANIHMSTK-------SGLTSLHLAAQEDKVNVADILTKHGADQDAH 629
Cdd:TIGR00870  207 LGNTLLHLLVMENEfkaeyeelsCQMYNFALSLLDKLRDSKElevilnhQGLTPLKLAAKEGRIVLFRLKLAIKYKQKKF 286

                          250
                   ....*....|.
gi 1229385538  630 TKLGYTPLIVA 640
Cdd:TIGR00870  287 VAWPNGQQLLS 297
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 633-664 5.12e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 44.59  E-value: 5.12e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1229385538  633 GYTPLIVAC-HYGNVKMVNFLLKQGANVNAKTK 664
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank_4 pfam13637
Ankyrin repeats (many copies);
16-63 5.85e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.96  E-value: 5.85e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1229385538   16 RAARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELL 63
Cdd:pfam13637    7 AAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
600-653 6.21e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.96  E-value: 6.21e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1229385538  600 GLTSLHLAAQEDKVNVADILTKHGADQDAHTKLGYTPLIVACHYGNVKMVNFLL 653
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Death_TRAILR_DR4_DR5 cd08315
Death domain of Tumor necrosis factor-Related Apoptosis-Inducing Ligand Receptors; Death ...
 1362-1428 6.27e-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: 6.27e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1229385538 1362 YIADHLGF-SWTELARELDFTEEQIHQIRIENPNSlQDQSHALLKYWLERDGKHATDTNLVECLTKIN 1428
Cdd:cd08315      4 YFEDIVPFkSWKRLMRALGLSDNEIKLAEANDPGS-QEPLYQMLNKWLNKTGRKASVNTLLDALEDLG 70
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 665-696 6.67e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 44.20  E-value: 6.67e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1229385538  665 NGYTPLHQAAQQ-GHTHIINVLLQHGAKPNATT 696
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
PHA02791 PHA02791
ankyrin-like protein; Provisional
 197-363 7.06e-06

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 49.66  E-value: 7.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  197 ADVQsksGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNgiTPLHVASKRGNTNMVKLLLDRG---GQIDAKtrdGLTP 273
Cdd:PHA02791    26 ADVH---GHSALYYAIADNNVRLVCTLLNAGALKNLLENE--FPLHQAATLEDTKIVKILLFSGmddSQFDDK---GNTA 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  274 LHCAARSGHDQVVELLLERGAPLLARTKNGL-SPLHMAAQGDHVECVKHLLQHKAPVDDVTLdYLTALHVAAHCGHYRVT 352
Cdd:PHA02791    98 LYYAVDSGNMQTVKLFVKKNWRLMFYGKTGWkTSFYHAVMLNDVSIVSYFLSEIPSTFDLAI-LLSCIHITIKNGHVDMM 176

                          170
                   ....*....|.
gi 1229385538  353 KLLLDKRANPN 363
Cdd:PHA02791   177 ILLLDYMTSTN 187
Death_DRs cd08784
Death Domain of Death Receptors; Death domain (DD) found in death receptor proteins. Death ...
 1370-1437 7.13e-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: 7.13e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1229385538 1370 SWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLtkiNRMDIVHLME 1437
Cdd:cd08784     13 QWKGFVRKLGLNEAEIDEIKNDNVQDTAEAKYQMLRNWHQLTGRKAAYDTLIKDL---KKMNLCTLAE 77
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 376-598 7.62e-06

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 50.91  E-value: 7.62e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  376 AARAGQVEVVRCLLRNGALVDARAREEQTPLHI-----ASRLGKTEIVQLLLQHmahpdAATTNGYTPLHISAREGQvDV 450
Cdd:cd22194     52 KVSEAAVEELGELLKELKDLSRRRRKTDVPDFLmhkltASDTGKTCLMKALLNI-----NENTKEIVRILLAFAEEN-GI 125

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  451 ASVLLEAgaAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKN--------------GLTPLHVAAHYDNQKV 516
Cdd:cd22194    126 LDRFINA--EYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEI 203

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  517 ALLLLEKGASPHATAKN-GYTPLH---IAAKKNQMQIAST-------LLNYGAET--NIVTKQGVTPLHLASQEGHTDMV 583
Cdd:cd22194    204 VQLLMEKESTDITSQDSrGNTVLHalvTVAEDSKTQNDFVkrmydmiLLKSENKNleTIRNNEGLTPLQLAAKMGKAEIL 283

                          250       260
                   ....*....|....*....|
gi 1229385538  584 TLLL-----DKGaNIHMSTK 598
Cdd:cd22194    284 KYILsreikEKP-NRSLSRK 302
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 512-591 9.56e-06

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 47.18  E-value: 9.56e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  512 DNQKVALLLLEKGASPHAT-AKNGYTPLHIAAKKNQMQIASTLLNY-GAETNIVTKQGVTPLHLASQEGHTDMVTLLLDK 589
Cdd:PHA02736    69 DPQEKLKLLMEWGADINGKeRVFGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERHDAKMMNILRAK 148


                   ..
gi 1229385538  590 GA 591
Cdd:PHA02736   149 GA 150
Ank_5 pfam13857
Ankyrin repeats (many copies);
95-149 1.04e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.26  E-value: 1.04e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1229385538   95 LVKEG-ANINAQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVA 149
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 665-694 1.14e-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: 1.14e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 1229385538   665 NGYTPLHQAAQQGHTHIINVLLQHGAKPNA 694
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
388-441 1.14e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.26  E-value: 1.14e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1229385538  388 LLRNG-ALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHI 441
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 368-490 1.17e-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: 1.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  368 RGETALHMAARAGQVEVVRCLLRNGALVDARAREE-------------QTPLHIASRLGKTEIVQLLLQHMAHP---DAA 431
Cdd:cd22197     93 RGHSALHIAIEKRSLQCVKLLVENGADVHARACGRffqkkqgtcfyfgELPLSLAACTKQWDVVNYLLENPHQPaslQAQ 172

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1229385538  432 TTNGYTPLH---ISAREGQVDVASV------LLEAGAA-------HSLATKKGFTPLHVAAKYGSLDVAKLLLQR 490
Cdd:cd22197    173 DSLGNTVLHalvMIADNSPENSALVikmydgLLQAGARlcptvqlEEISNHEGLTPLKLAAKEGKIEIFRHILQR 247
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 566-595 1.36e-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: 1.36e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 1229385538   566 QGVTPLHLASQEGHTDMVTLLLDKGANIHM 595
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 236-265 1.64e-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: 1.64e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 1229385538   236 NGITPLHVASKRGNTNMVKLLLDRGGQIDA 265
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02741 PHA02741
hypothetical protein; Provisional
 40-163 1.66e-05

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 46.96  E-value: 1.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538   40 NQNGLNALHLAAKEGHVGLVQELLG--RGSSVDSATK----KGNTALHIASLAGQA----EVVKVLVKEGANINAQ-SQN 108
Cdd:PHA02741    18 NSEGENFFHEAARCGCFDIIARFTPfiRGDCHAAALNatddAGQMCIHIAAEKHEAqlaaEIIDHLIELGADINAQeMLE 97

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1229385538  109 GFTPLYMAAQENHIDVVKYLL-ENGANQSTATEDGFTPLAVALQQGHNQAVAILLE 163
Cdd:PHA02741    98 GDTALHLAAHRRDHDLAEWLCcQPGIDLHFCNADNKSPFELAIDNEDVAMMQILRE 153
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 566-598 1.76e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 43.05  E-value: 1.76e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1229385538  566 QGVTPLHLAS-QEGHTDMVTLLLDKGANIHMSTK 598
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 308-429 1.90e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.51  E-value: 1.90e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  308 HMAAQGDHVEcVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNARALRGETALHMAARAGQVEVVRC 387
Cdd:PTZ00322    88 QLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1229385538  388 LLRNGAL---VDARAREEqtplhiaSRLGKTEIVQLLLQHMAHPD 429
Cdd:PTZ00322   167 LSRHSQChfeLGANAKPD-------SFTGKPPSLEDSPISSHHPD 204
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 75-104 2.01e-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: 2.01e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 1229385538    75 KGNTALHIASLAGQAEVVKVLVKEGANINA 104
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 27-104 2.17e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 48.89  E-value: 2.17e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1229385538   27 VEYL-KGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGANINA 104
Cdd:PHA03100   175 VNYLlSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 414-695 2.39e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 48.97  E-value: 2.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  414 KTEIVQLLLQHMAHpdaATTNGY--TPLHISAREGQVD------VASVLLEAGAAHSLATKKGFTPLhVAAKYGSldvak 485
Cdd:PHA02989    49 KIKIVKLLIDNGAD---VNYKGYieTPLCAVLRNREITsnkikkIVKLLLKFGADINLKTFNGVSPI-VCFIYNS----- 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  486 lllqrraaadsagkngltplhvaaHYDNQKVALLLLEKGASPHaTAKN--GYTPLHI-----AAKKNQMQIastLLNYGA 558
Cdd:PHA02989   120 ------------------------NINNCDMLRFLLSKGINVN-DVKNsrGYNLLHMylesfSVKKDVIKI---LLSFGV 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  559 ---ETNIVtkQGVTPLHLASQEG----HTDMVTLLLDKGANIHMST---KSGLTSL---HLAAQEDKVNVADILTKHgAD 625
Cdd:PHA02989   172 nlfEKTSL--YGLTPMNIYLRNDidviSIKVIKYLIKKGVNIETNNngsESVLESFldnNKILSKKEFKVLNFILKY-IK 248

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  626 QDAHTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQhgAKPNAT 695
Cdd:PHA02989   249 INKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNRILQ--LKPGKY 316
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 552-696 2.54e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 48.97  E-value: 2.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  552 TLLNYGAETNIVTK-QGVTPLHLASQEGHTDMVTLLLDKGANI----HMSTK--SGLTSLHLAAQEDKvNVADILTKHGA 624
Cdd:PHA02989    21 FLLRTGFDVNEEYRgNSILLLYLKRKDVKIKIVKLLIDNGADVnykgYIETPlcAVLRNREITSNKIK-KIVKLLLKFGA 99

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1229385538  625 DQDAHTKLGYTPL---IVACHYGNVKMVNFLLKQGANVNA-KTKNGYTPLHQAAQQG--HTHIINVLLQHGAKPNATT 696
Cdd:PHA02989   100 DINLKTFNGVSPIvcfIYNSNINNCDMLRFLLSKGINVNDvKNSRGYNLLHMYLESFsvKKDVIKILLSFGVNLFEKT 177
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 633-661 3.63e-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: 3.63e-05
                            10        20
                    ....*....|....*....|....*....
gi 1229385538   633 GYTPLIVACHYGNVKMVNFLLKQGANVNA 661
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
68-116 4.35e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.72  E-value: 4.35e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1229385538   68 SVDSATKKGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMA 116
Cdd:pfam13857    8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 269-298 4.51e-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: 4.51e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 1229385538  269 DGLTPLHCAARSGHDQVVELLLERGAPLLA 298
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 75-105 4.84e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 41.89  E-value: 4.84e-05
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1229385538   75 KGNTALHIASL-AGQAEVVKVLVKEGANINAQ 105
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNAR 32
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 206-342 4.87e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 46.35  E-value: 4.87e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  206 TPLH--IAAHYGNVNVATLLLNRGAAVDFTAR-NGITPLH---VASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLH---- 275
Cdd:PHA02859    53 TPIFscLEKDKVNVEILKFLIENGADVNFKTRdNNLSALHhylSFNKNVEPEILKILIDSGSSITEEDEDGKNLLHmymc 132

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1229385538  276 -CAARSghdQVVELLLERGAPLLARTKNGLSPLHmaaqgdhvecvKHLLQHKapvDDVTLDYLTALHV 342
Cdd:PHA02859   133 nFNVRI---NVIKLLIDSGVSFLNKDFDNNNILY-----------SYILFHS---DKKIFDFLTSLGI 183
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 90-150 5.29e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 46.35  E-value: 5.29e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1229385538   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 ...
 633-661 5.49e-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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 41.47  E-value: 5.49e-05
                           10        20
                   ....*....|....*....|....*....
gi 1229385538  633 GYTPLIVACHYGNVKMVNFLLKQGANVNA 661
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 236-268 5.55e-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: 5.55e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1229385538  236 NGITPLHVASKR-GNTNMVKLLLDRGGQIDAKTR 268
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 665-694 5.82e-05

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 41.47  E-value: 5.82e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 1229385538  665 NGYTPLHQAAQQGHTHIINVLLQHGAKPNA 694
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 269-294 5.87e-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: 5.87e-05
                            10        20
                    ....*....|....*....|....*.
gi 1229385538   269 DGLTPLHCAARSGHDQVVELLLERGA 294
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 501-615 5.99e-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: 5.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  501 GLTPLHVAAHYDNQKVALLLLEKGASPHATAKN--------------GYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQ 566
Cdd:cd22193     76 GQTALHIAIERRQGDIVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLSLAACTNQPDIVQYLLENEHQPADIEAQ 155

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1229385538  567 ---GVTPLHLA-----SQEGHTDMVT----LLLDKGANIH-------MSTKSGLTSLHLAAQEDKVNV 615
Cdd:cd22193    156 dsrGNTVLHALvtvadNTKENTKFVTrmydMILIRGAKLCptveleeIRNNDGLTPLQLAAKMGKIEI 223
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 617-708 6.04e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 47.94  E-value: 6.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  617 DILTKHGADQDAHTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATT 696
Cdd:PLN03192   542 EELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHA 621

                           90
                   ....*....|..
gi 1229385538  697 AnGNTALAIAKR 708
Cdd:PLN03192   622 A-GDLLCTAAKR 632
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 30-113 6.52e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.59  E-value: 6.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538   30 LKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKE-------GANI 102
Cdd:PTZ00322   102 LTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHsqchfelGANA 181

                           90
                   ....*....|.
gi 1229385538  103 NAQSQNGFTPL 113
Cdd:PTZ00322   182 KPDSFTGKPPS 192
PHA02795 PHA02795
ankyrin-like protein; Provisional
 90-153 7.29e-05

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 47.30  E-value: 7.29e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1229385538   90 EVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQG 153
Cdd:PHA02795   202 EIYKLCIPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRG 265
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 451-534 7.93e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.59  E-value: 7.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  451 ASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHAT 530
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFEL 177


                   ....
gi 1229385538  531 AKNG 534
Cdd:PTZ00322   178 GANA 181
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 108-134 8.14e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 41.12  E-value: 8.14e-05
                           10        20
                   ....*....|....*....|....*...
gi 1229385538  108 NGFTPLYMAA-QENHIDVVKYLLENGAN 134
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGAD 28
Ank_5 pfam13857
Ankyrin repeats (many copies);
289-343 8.15e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 8.15e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1229385538  289 LLERG-APLLARTKNGLSPLHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVA 343
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 36-134 8.56e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 45.58  E-value: 8.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538   36 INTCNQNGLNALH--LAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLA----GQAEVVKVLVKEGANINAQSQNG 109
Cdd:PHA02859    44 VNDCNDLYETPIFscLEKDKVNVEILKFLIENGADVNFKTRDNNLSALHHYLSfnknVEPEILKILIDSGSSITEEDEDG 123

                           90       100
                   ....*....|....*....|....*..
gi 1229385538  110 FTPL--YMAAQENHIDVVKYLLENGAN 134
Cdd:PHA02859   124 KNLLhmYMCNFNVRINVIKLLIDSGVS 150
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 302-331 8.69e-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: 8.69e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 1229385538   302 NGLSPLHMAAQGDHVECVKHLLQHKAPVDD 331
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 137-324 1.25e-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: 1.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  137 TATEDGFTPLAVA---LQQGHNQAVAILLEndtkgkvrlpalhIAARKDDTKSaallLQNDHNADVQSKsGFTPLHIAAH 213
Cdd:cd22193     24 TESSTGKTCLMKAllnLNPGTNDTIRILLD-------------IAEKTDNLKR----FINAEYTDEYYE-GQTALHIAIE 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  214 YGNVNVATLLLNRGAAVDFTARN--------------GITPLHVASKRGNTNMVKLLLDRGGQ-IDAKTRD--GLTPLHC 276
Cdd:cd22193     86 RRQGDIVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLSLAACTNQPDIVQYLLENEHQpADIEAQDsrGNTVLHA 165

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1229385538  277 AARSGHD---------QVVELLLERGAPLLA-------RTKNGLSPLHMAAQGDHVECVKHLLQ 324
Cdd:cd22193    166 LVTVADNtkentkfvtRMYDMILIRGAKLCPtveleeiRNNDGLTPLQLAAKMGKIEILKYILQ 229
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 368-398 1.25e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. 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: 1.25e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1229385538  368 RGETALHMAA-RAGQVEVVRCLLRNGALVDAR 398
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNAR 32
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 338-365 1.37e-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: 1.37e-04
                           10        20
                   ....*....|....*....|....*....
gi 1229385538  338 TALHVAA-HCGHYRVTKLLLDKRANPNAR 365
Cdd:pfam00023    4 TPLHLAAgRRGNLEIVKLLLSKGADVNAR 32
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 579-673 1.40e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 45.74  E-value: 1.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  579 HTDMVTLLLDKGANIH----MSTKSGLTSLHLAAQEDKVNVADILTKHGADQDAHTK-LGYTPLIVACHYGNVKMVNFLL 653
Cdd:PHA02884    45 YTDIIDAILKLGADPEapfpLSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEeAKITPLYISVLHGCLKCLEILL 124

                           90       100
                   ....*....|....*....|
gi 1229385538  654 KQGANVNAKTKNGYTPLHQA 673
Cdd:PHA02884   125 SYGADINIQTNDMVTPIELA 144
TRPV4 cd22195
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed ...
 75-226 1.62e-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: 46.38  E-value: 1.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538   75 KGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGF--------------TPLYMAAQENHIDVVKYLLENganqstate 140
Cdd:cd22195    136 RGQTALHIAIERRCKHYVELLVEKGADVHAQARGRFfqpkdeggyfyfgeLPLSLAACTNQPDIVHYLTEN--------- 206

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  141 dgftplavalqqGHNQavAILLENDTKGKVRLPAL-HIAARKDD-----TKSAALLLQN------DHNAD-VQSKSGFTP 207
Cdd:cd22195    207 ------------AHKK--ADLRRQDSRGNTVLHALvAIADNTREntkfvTKMYDLLLIKcaklypDCNLEaILNNDGMSP 272

                          170
                   ....*....|....*....
gi 1229385538  208 LHIAAHYGNVNVATLLLNR 226
Cdd:cd22195    273 LMMAAKLGKIGIFQHIIRR 291
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 533-565 1.77e-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. 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: 1.77e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1229385538  533 NGYTPLHIAAKK-NQMQIASTLLNYGAETNIVTK 565
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 533-562 1.98e-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: 1.98e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 1229385538   533 NGYTPLHIAAKKNQMQIASTLLNYGAETNI 562
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 368-397 2.00e-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: 2.00e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 1229385538   368 RGETALHMAARAGQVEVVRCLLRNGALVDA 397
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 302-333 2.24e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.97  E-value: 2.24e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1229385538  302 NGLSPLHMAA-QGDHVECVKHLLQHKAPVDDVT 333
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 500-532 2.26e-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: 2.26e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1229385538  500 NGLTPLHVAA-HYDNQKVALLLLEKGASPHATAK 532
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 467-492 2.74e-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: 2.74e-04
                            10        20
                    ....*....|....*....|....*.
gi 1229385538   467 KGFTPLHVAAKYGSLDVAKLLLQRRA 492
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 204-231 2.88e-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: 2.88e-04
                            10        20
                    ....*....|....*....|....*...
gi 1229385538   204 GFTPLHIAAHYGNVNVATLLLNRGAAVD 231
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 108-134 3.03e-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: 3.03e-04
                           10        20
                   ....*....|....*....|....*..
gi 1229385538  108 NGFTPLYMAAQENHIDVVKYLLENGAN 134
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGAD 27
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 565-657 3.26e-04

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 42.94  E-value: 3.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  565 KQGVTPLHLASQEGHTD---MVTLLLDKGANIH-MSTKSGLTSLHLAAQEDKVNVADILTKH-GADQDAHTKLGYTPLIV 639
Cdd:PHA02736    53 RHGKQCVHIVSNPDKADpqeKLKLLMEWGADINgKERVFGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYV 132

                           90
                   ....*....|....*...
gi 1229385538  640 ACHYGNVKMVNFLLKQGA 657
Cdd:PHA02736   133 ACERHDAKMMNILRAKGA 150
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 368-397 3.83e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.16  E-value: 3.83e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1229385538  368 RGETALHMAARAGQVEVVRCLLRNGALVDA 397
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 204-231 4.41e-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: 4.41e-04
                           10        20
                   ....*....|....*....|....*....
gi 1229385538  204 GFTPLHIAA-HYGNVNVATLLLNRGAAVD 231
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVN 30
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 204-411 5.51e-04

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 44.49  E-value: 5.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  204 GFTPLHIAA---HYGNVNVATLLLNRGAAVDFTAR-----------NGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRD 269
Cdd:cd21882     26 GKTCLHKAAlnlNDGVNEAIMLLLEAAPDSGNPKElvnapctdefyQGQTALHIAIENRNLNLVRLLVENGADVSARATG 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  270 -------------GLTPLHCAARSGHDQVVELLLERG---APLLARTKNGLSPLH-MAAQGDHVECVKHLLQHKapvddv 332
Cdd:cd21882    106 rffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGaqpAALEAQDSLGNTVLHaLVLQADNTPENSAFVCQM------ 179

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1229385538  333 tldYLTALHVAAHCGHYRVTKLLldkranPNARALrgeTALHMAARAGQVEVVRCLLRngalvdaraREEQTPLHIASR 411
Cdd:cd21882    180 ---YNLLLSYGAHLDPTQQLEEI------PNHQGL---TPLKLAAVEGKIVMFQHILQ---------REFSGPYQPLSR 237
PHA02798 PHA02798
ankyrin-like protein; Provisional
 217-324 6.25e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 44.44  E-value: 6.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  217 VNVATLLLNRGAAVDFTARNGITPL-----HVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLL- 290
Cdd:PHA02798    51 TDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLf 130

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1229385538  291 --ERGAPLLARTKNGLSPLHMAAQGDH---VECVKHLLQ 324
Cdd:PHA02798   131 miENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLE 169
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 335-364 6.25e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.72  E-value: 6.25e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 1229385538   335 DYLTALHVAAHCGHYRVTKLLLDKRANPNA 364
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 566-691 6.71e-04

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 42.17  E-value: 6.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  566 QGVTPLHLASQEGhtDMVTLLLDKGA----NIHMST---KSGLTSLHLAAQEDKV---NVADILTKHGADQDAH-TKLGY 634
Cdd:PHA02736    16 EGENILHYLCRNG--GVTDLLAFKNAisdeNRYLVLeynRHGKQCVHIVSNPDKAdpqEKLKLLMEWGADINGKeRVFGN 93

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1229385538  635 TPLIVACHYGNVKMVNFLLKQ-GANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAK 691
Cdd:PHA02736    94 TPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGAQ 151
Death_PIDD cd08779
Death Domain of p53-induced protein with a death domain; Death domain (DD) found in PIDD ...
 1360-1433 6.77e-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: 6.77e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1229385538 1360 LAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLErdgKHATDTN----LVECLTKINRMDIV 1433
Cdd:cd08779      5 LLSLAKELGEDWQKLALHLGVSYSRIQRIKRKNRDDLDEQILDMLFSWAK---TLPTSPDkvglLVTALSKSGRSDLA 79
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 75-104 8.33e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.39  E-value: 8.33e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1229385538   75 KGNTALHIASLAGQAEVVKVLVKEGANINA 104
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 534-687 8.36e-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: 8.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  534 GYTPLHIAAKKNQMQIASTLLNYGAETNIVT-------KQGVT------PLHLASQEGHTDMVTLLLDKG---ANIHMST 597
Cdd:cd22197     94 GHSALHIAIEKRSLQCVKLLVENGADVHARAcgrffqkKQGTCfyfgelPLSLAACTKQWDVVNYLLENPhqpASLQAQD 173

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  598 KSGLTSLHLAaqedkVNVADiltkhgaDQDAHTKLgytplivachygNVKMVNFLLKQGANVNAKTK-------NGYTPL 670
Cdd:cd22197    174 SLGNTVLHAL-----VMIAD-------NSPENSAL------------VIKMYDGLLQAGARLCPTVQleeisnhEGLTPL 229

                          170
                   ....*....|....*..
gi 1229385538  671 HQAAQQGHTHIINVLLQ 687
Cdd:cd22197    230 KLAAKEGKIEIFRHILQ 246
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 140-292 1.10e-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: 43.64  E-value: 1.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  140 EDGFTPLAVA---LQQGHNQAVAILLE------------------NDTKGKVrlpALHIAARKDDTKSAALLLQNdhNAD 198
Cdd:cd22196     45 ETGKTCLLKAmlnLHNGQNDTISLLLDiaektgnlkefvnaaytdSYYKGQT---ALHIAIERRNMHLVELLVQN--GAD 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  199 VQ------------SKSGF----TPLHIAAHYGNVNVATLLL-NRGAAVDFTARN--GITPLH---------VASKRGNT 250
Cdd:cd22196    120 VHarasgeffkkkkGGPGFyfgeLPLSLAACTNQLDIVKFLLeNPHSPADISARDsmGNTVLHalvevadntPENTKFVT 199

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1229385538  251 NMVKLLLDRGGQIDAK-------TRDGLTPLHCAARSGHDQVVELLLER 292
Cdd:cd22196    200 KMYNEILILGAKIRPLlkleeitNKKGLTPLKLAAKTGKIGIFAYILGR 248
Death_RIP1 cd08777
Death Domain of Receptor-Interacting Protein 1; Death domain (DD) found in ...
 1357-1436 1.12e-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: 1.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538 1357 EERLAYIADHLGFSWTELARELDFTEEQIHQIRIE-NPNSLQDQSHALLKYWLERDG-KHATDTNLVECLTKINRMDIVH 1434
Cdd:cd08777      2 EKHLDLLRENLGKKWKRCARRLGLTEVEIEEIDHDyERDGLKEKVHQMLEKWKMKEGsKGATVGKLAKALEGCIKSDLLV 81


                   ..
gi 1229385538 1435 LM 1436
Cdd:cd08777     82 SL 83
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 403-432 1.16e-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: 1.16e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1229385538  403 QTPLHIAS-RLGKTEIVQLLLQHMAHPDAAT 432
Cdd:pfam00023    3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 467-492 1.28e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 37.65  E-value: 1.28e-03
                           10        20
                   ....*....|....*....|....*..
gi 1229385538  467 KGFTPLHVAA-KYGSLDVAKLLLQRRA 492
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGA 27
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 519-607 1.35e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 42.66  E-value: 1.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  519 LLLEKGASP---HATAKNGYT-PLHIAAKKNQMQIASTLLNYGAETNIVTKQGV-TPLHLASQEGHTDMVTLLLDKGANI 593
Cdd:PHA02884    51 AILKLGADPeapFPLSENSKTnPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLHGCLKCLEILLSYGADI 130

                           90
                   ....*....|....
gi 1229385538  594 HMSTKSGLTSLHLA 607
Cdd:PHA02884   131 NIQTNDMVTPIELA 144
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 534-687 1.38e-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: 1.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  534 GYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQ--------------GVTPLHLASQEGHTDMVTLLLD---KGANIHMS 596
Cdd:cd22193     76 GQTALHIAIERRQGDIVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLSLAACTNQPDIVQYLLEnehQPADIEAQ 155

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  597 TKSGLTSLHLAaqedkVNVADiltkhgaDQDAHTKLgytplivachygNVKMVNFLLKQGANVNAKTK-------NGYTP 669
Cdd:cd22193    156 DSRGNTVLHAL-----VTVAD-------NTKENTKF------------VTRMYDMILIRGAKLCPTVEleeirnnDGLTP 211

                          170
                   ....*....|....*...
gi 1229385538  670 LHQAAQQGHTHIINVLLQ 687
Cdd:cd22193    212 LQLAAKMGKIEILKYILQ 229
Death_MyD88 cd08312
Death domain of Myeloid Differentation primary response protein MyD88; Death Domain (DD) of ...
 1371-1434 1.41e-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: 1.41e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1229385538 1371 WTELARELDFTEEQIHQIRIENpnslqDQSHALLKYWLERDgKHATDTNLVECLTKINRMDIVH 1434
Cdd:cd08312     19 WRGLAELMGFDYLEIRNFERQS-----SPTERLLEDWETRP-PGATVGNLLEILEELERKDVLE 76
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 536-669 1.43e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 41.73  E-value: 1.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  536 TPLH--IAAKKNQMQIASTLLNYGAETNIVTK-QGVTPLH--LASQEG-HTDMVTLLLDKGANIHMSTKSGLTSLH--LA 607
Cdd:PHA02859    53 TPIFscLEKDKVNVEILKFLIENGADVNFKTRdNNLSALHhyLSFNKNvEPEILKILIDSGSSITEEDEDGKNLLHmyMC 132

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1229385538  608 AQEDKVNVADILTKHGA-----DQDAHTKLgYTPLIvacHYGNVKMVNFLLKQGANVNAKTKNGYTP 669
Cdd:PHA02859   133 NFNVRINVIKLLIDSGVsflnkDFDNNNIL-YSYIL---FHSDKKIFDFLTSLGIDINETNKSGYNC 195
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 398-525 1.46e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 41.02  E-value: 1.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  398 RAREEQTPLHIASRLGktEIVQLLLQHMAHPDAA-------TTNGYTPLHISAREGQVDVAS---VLLEAGA-AHSLATK 466
Cdd:PHA02736    13 PDIEGENILHYLCRNG--GVTDLLAFKNAISDENrylvleyNRHGKQCVHIVSNPDKADPQEklkLLMEWGAdINGKERV 90

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1229385538  467 KGFTPLHVAAKYGSLDVAKLLLQrRAAADSAGKNGL--TPLHVAAHYDNQKVALLLLEKGA 525
Cdd:PHA02736    91 FGNTPLHIAVYTQNYELATWLCN-QPGVNMEILNYAfkTPYYVACERHDAKMMNILRAKGA 150
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 500-529 1.51e-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: 1.51e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 1229385538   500 NGLTPLHVAAHYDNQKVALLLLEKGASPHA 529
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 236-265 1.69e-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: 1.69e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1229385538  236 NGITPLHVASKRGNTNMVKLLLDRGGQIDA 265
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 204-231 1.86e-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: 1.86e-03
                           10        20
                   ....*....|....*....|....*...
gi 1229385538  204 GFTPLHIAAHYGNVNVATLLLNRGAAVD 231
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADIN 29
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 467-495 1.96e-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: 1.96e-03
                           10        20
                   ....*....|....*....|....*....
gi 1229385538  467 KGFTPLHVAAKYGSLDVAKLLLQRRAAAD 495
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 533-562 2.14e-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: 2.14e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1229385538  533 NGYTPLHIAAKKNQMQIASTLLNYGAETNI 562
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Death_TNFR1 cd08313
Death domain of Tumor Necrosis Factor Receptor 1; Death Domain (DD) found in tumor necrosis ...
 1371-1437 2.46e-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: 2.46e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1229385538 1371 WTELARELDFTEEQIHQIRIENpNSLQDQSHALLKYWLERDGKHATDTNLVECltKINRMDIVHLME 1437
Cdd:cd08313     14 WKEFVRRLGLSDNEIERVELDH-RRCRDAQYQMLKVWKERGPRPYATLQHLLS--VLRDMELVGCAE 77
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 335-364 2.82e-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: 2.82e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1229385538  335 DYLTALHVAAHCGHYRVTKLLLDKRANPNA 364
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 567-595 2.82e-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: 2.82e-03
                           10        20
                   ....*....|....*....|....*....
gi 1229385538  567 GVTPLHLASQEGHTDMVTLLLDKGANIHM 595
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 634-703 3.31e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 40.96  E-value: 3.31e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1229385538  634 YTPLIVAC---HYGNVKMVNFLLKQGANVNAKTK-NGYTPLH---QAAQQGHTHIINVLLQHGAKPNATTANGNTAL 703
Cdd:PHA02859    51 YETPIFSClekDKVNVEILKFLIENGADVNFKTRdNNLSALHhylSFNKNVEPEILKILIDSGSSITEEDEDGKNLL 127
PHA02791 PHA02791
ankyrin-like protein; Provisional
 47-196 3.40e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 41.57  E-value: 3.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538   47 LHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGF-TPLYMAAQENHIDVV 125
Cdd:PHA02791    65 LHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTGWkTSFYHAVMLNDVSIV 144

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1229385538  126 KYLLengaNQSTATEDGFTPLA---VALQQGHNQAVAILLE-----NDTKGKVRLPALHIAARKDDTKSAALLLQNDHN 196
Cdd:PHA02791   145 SYFL----SEIPSTFDLAILLScihITIKNGHVDMMILLLDymtstNTNNSLLFIPDIKLAIDNKDLEMLQALFKYDIN 219
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 434-459 3.60e-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: 3.60e-03
                            10        20
                    ....*....|....*....|....*.
gi 1229385538   434 NGYTPLHISAREGQVDVASVLLEAGA 459
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 40-133 3.87e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 39.86  E-value: 3.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538   40 NQNGLNALHLAAKEGHVGLVQE---LLGRGSSVDSATKK-GNTALHIASLAGQAEVVKVLVKE-GANINAQSQNGFTPLY 114
Cdd:PHA02736    52 NRHGKQCVHIVSNPDKADPQEKlklLMEWGADINGKERVfGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYY 131

                           90
                   ....*....|....*....
gi 1229385538  115 MAAQENHIDVVKYLLENGA 133
Cdd:PHA02736   132 VACERHDAKMMNILRAKGA 150
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 501-615 4.66e-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: 4.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  501 GLTPLHVAAHYDNQKVALLLLEKGASPHATA------KN-------GYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQ- 566
Cdd:cd22197     94 GHSALHIAIEKRSLQCVKLLVENGADVHARAcgrffqKKqgtcfyfGELPLSLAACTKQWDVVNYLLENPHQPASLQAQd 173

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1229385538  567 --GVTPLHLA-----SQEGHTDMVTL----LLDKGANI-------HMSTKSGLTSLHLAAQEDKVNV 615
Cdd:cd22197    174 slGNTVLHALvmiadNSPENSALVIKmydgLLQAGARLcptvqleEISNHEGLTPLKLAAKEGKIEI 240
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 42-74 4.72e-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: 36.11  E-value: 4.72e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1229385538   42 NGLNALHLAA-KEGHVGLVQELLGRGSSVDSATK 74
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 42-70 4.83e-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: 4.83e-03
                            10        20
                    ....*....|....*....|....*....
gi 1229385538    42 NGLNALHLAAKEGHVGLVQELLGRGSSVD 70
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02791 PHA02791
ankyrin-like protein; Provisional
 533-703 4.93e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 40.80  E-value: 4.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  533 NGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQgvTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDK 612
Cdd:PHA02791    29 HGHSALYYAIADNNVRLVCTLLNAGALKNLLENE--FPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGN 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  613 VNVADILTKHGADQDAHTKLGY-TPLIVACHYGNVKMVNFLLKQGANvNAKTKNGYTPLHQAAQQGHTHIINVLLQHgak 691
Cdd:PHA02791   107 MQTVKLFVKKNWRLMFYGKTGWkTSFYHAVMLNDVSIVSYFLSEIPS-TFDLAILLSCIHITIKNGHVDMMILLLDY--- 182

                          170
                   ....*....|..
gi 1229385538  692 pnATTANGNTAL 703
Cdd:PHA02791   183 --MTSTNTNNSL 192
Death_FAS_TNFRSF6 cd08316
Death domain of FAS or TNF receptor superfamily member 6; Death Domain (DD) found in the ...
 1356-1434 5.81e-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: 5.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538 1356 IEERLAYIADHLGfsWTE---LARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINR--- 1429
Cdd:cd08316      4 LSKHIPDIAEIMG--WKDvkkFARKSGISETKIDEIQLDNPNDTAEQKVQLLRAWYQKHGKKGAYRTLIKTLRKAGKrak 81


                   ....*....
gi 1229385538 1430 ----MDIVH 1434
Cdd:cd08316     82 adkiQDIIK 90
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 532-718 6.73e-03

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 41.05  E-value: 6.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  532 KNGYTPLH--IAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGH--TDMVTLLLDKGANIHMSTKSGLTSLhLA 607
Cdd:PHA02716   175 KTGYGILHayLGNMYVDIDILEWLCNNGVNVNLQNNHLITPLHTYLITGNvcASVIKKIIELGGDMDMKCVNGMSPI-MT 253

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  608 AQEDKVNVADILTKHGADQDAHTKLGYTPLIVACH-----YGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGH--TH 680
Cdd:PHA02716   254 YIINIDNINPEITNIYIESLDGNKVKNIPMILHSYitlarNIDISVVYSFLQPGVKLHYKDSAGRTCLHQYILRHNisTD 333

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1229385538  681 IINVLLQHGAKPNATTANGNTALaiAKRLGYISVVDTL 718
Cdd:PHA02716   334 IIKLLHEYGNDLNEPDNIGNTVL--HTYLSMLSVVNIL 369
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 206-279 6.90e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 40.35  E-value: 6.90e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1229385538  206 TPLHIAAHYGNVNVATLLLNRGAAVD-FTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAAR 279
Cdd:PHA02884    72 NPLIYAIDCDNDDAAKLLIRYGADVNrYAEEAKITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELALM 146
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 437-573 7.01e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 39.80  E-value: 7.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385538  437 TPLH--ISAREGQVDVASVLLEAGAAHSLATK-KGFTPLHVAAKYG---SLDVAKLLLQRRAAADSAGKNGLTPLHVaaH 510
Cdd:PHA02859    53 TPIFscLEKDKVNVEILKFLIENGADVNFKTRdNNLSALHHYLSFNknvEPEILKILIDSGSSITEEDEDGKNLLHM--Y 130

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1229385538  511 YDNQKVAL----LLLEKGASPHATAKNGYTPLH--IAAKKNQmQIASTLLNYGAETNIVTKQGVTPLHL 573
Cdd:PHA02859   131 MCNFNVRInvikLLIDSGVSFLNKDFDNNNILYsyILFHSDK-KIFDFLTSLGIDINETNKSGYNCYDL 198
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 302-330 9.92e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 35.31  E-value: 9.92e-03
                           10        20
                   ....*....|....*....|....*....
gi 1229385538  302 NGLSPLHMAAQGDHVECVKHLLQHKAPVD 330
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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