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Conserved domains on  [gi|1887789594|ref|NP_001373080|]
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ankyrin-2 isoform 58 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UPA_2 super family cl39303
UPA domain; The UPA domain is conserved in UNC5, PIDD, and Ankyrins. It has a beta sandwich ...
 1229-1358 3.48e-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: 3.48e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594 1229 VPYMAKFVVFAKSHDPIEARLRCFCMTDDKVDKTLEQQENFAEVARSRDVEVLEGKPIYVDCFGNLVPLTKSGQHHIFSF 1308
Cdd:pfam17809    1 VPYLAKFVVFAKRYDPGEARLRCACMTDDGEDKTLEFHEGFTEVARSRDVEVLEGSPVSIELSGNLVPIKKKSQSRQMDF 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1887789594 1309 FAFKENRLPLFVKVRDTTQEPCGRLSFMKEPKSTRGLVHQAICNLNITLP 1358
Cdd:pfam17809   81 KAFRENRLDGSVRVKDPSDPPKGLLSFMRDAKVDGGTVSQPLCTLNIVLP 130
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
155-439 4.83e-59

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 205.57  E-value: 4.83e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  155 NQAVAILLENDTKGKVRLPALHIAARKDDTKSAALLLQNDHNADVQSKSGFTPLHIAAHYGNVNVATLLLNRGAAVDFTA 234
Cdd:COG0666      5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  235 RNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGD 314
Cdd:COG0666     85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANG 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  315 HVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGAS 394
Cdd:COG0666    165 NLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD 244

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1887789594  395 IQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETAL 439
Cdd:COG0666    245 LNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
482-752 7.17e-59

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 205.19  E-value: 7.17e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  482 EIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAAD 561
Cdd:COG0666      2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  562 SAGKNGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAA 641
Cdd:COG0666     82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  642 QEDKVNVADILTKHGADQDAHTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQH 721
Cdd:COG0666    162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1887789594  722 GAKPNATTANGNTALAIAKRLGYISVVDTLK 752
Cdd:COG0666    242 GADLNAKDKDGLTALLLAAAAGAALIVKLLL 272
Death_ank2 cd08804
Death domain of Ankyrin-2; Death Domain (DD) of Ankyrin-2 (ANK-2) and related proteins. ...
 1387-1470 1.65e-51

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


:

Pssm-ID: 260066  Cd Length: 84  Bit Score: 176.04  E-value: 1.65e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594 1387 ERIEERLAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIV 1466
Cdd:cd08804      1 ERTEERLAHIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLTQCLTKINRMDIV 80


                   ....
gi 1887789594 1467 HLME 1470
Cdd:cd08804     81 HLME 84
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
3-307 5.12e-51

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 182.46  E-value: 5.12e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594    3 TMLQKSDSNASFLRAARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHI 82
Cdd:COG0666     47 LALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHL 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594   83 ASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGAnqstatedgftplavalqqghnqavaill 162
Cdd:COG0666    127 AAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA----------------------------- 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  163 endtkgkvrlpalhiaarkddtksaalllqndhNADVQSKSGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLH 242
Cdd:COG0666    178 ---------------------------------DVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALD 224

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1887789594  243 VASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPL 307
Cdd:COG0666    225 LAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
 904-1008 3.00e-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: 3.00e-50
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594   904 SGFLVSFMVDARGGAMRGCRhNGLRIIIPPRKCTAPTRVTCRLVKRHRLATMPPMVEGEGLASRLIEVGPSGAQFLGPVI 983
Cdd:smart00218    1 PSFLVSGTFDARGGRLRGPR-TGVRLIIPPGAIPQGTRYTCYLVVHKTLSTPPPLEEGETLLSPVVECGPHGALFLRPVI 79

                            90       100
                    ....*....|....*....|....*
gi 1887789594   984 VEIPHFAALRGKERELVVLRSENGD 1008
Cdd:smart00218   80 LEVPHCASLRPRDWEIVLLRSENGG 104
PTZ00322 super family cl31426
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 420-501 7.93e-10

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


The actual alignment was detected with superfamily member PTZ00322:

Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 63.76  E-value: 7.93e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  420 LLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATT 499
Cdd:PTZ00322   100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGA 179


                   ..
gi 1887789594  500 NG 501
Cdd:PTZ00322   180 NA 181
NESP55 super family cl25759
Neuroendocrine-specific golgi protein P55 (NESP55); This family consists of several mammalian ...
 1543-1680 2.19e-07

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: 54.10  E-value: 2.19e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594 1543 TFQDGVPKTEGDSSATALFPQTHKEQVQQDFSGKMQDLPEESSLEYQQEYFVTTPGTET-------SETQKAMIVPSSPS 1615
Cdd:pfam06390   62 SFLNAHHRSAAAAAAAQVFPEPSEPESDHEDEDFEPELARPECLEYDEDDFDTETDSETepesdieSETEFETEPETEPD 141

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594 1616 KTPE-EVSTPAEEEK--------------------LYLQTPTSSERGGSPIIQEPEEPSEHRE------ESSPR--KTSL 1666
Cdd:pfam06390  142 TAPTtEPETEPEDEPgpvvpkgatfhqslterlhaLKLQSADASPRRAPPSTQEPESAREGEEpergplDKDPRdpEEEE 221

                          170
                   ....*....|....
gi 1887789594 1667 VIVESADNQPETCE 1680
Cdd:pfam06390  222 EEKEEEKQQPHRCK 235
 
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 ...
 1229-1358 3.48e-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: 3.48e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594 1229 VPYMAKFVVFAKSHDPIEARLRCFCMTDDKVDKTLEQQENFAEVARSRDVEVLEGKPIYVDCFGNLVPLTKSGQHHIFSF 1308
Cdd:pfam17809    1 VPYLAKFVVFAKRYDPGEARLRCACMTDDGEDKTLEFHEGFTEVARSRDVEVLEGSPVSIELSGNLVPIKKKSQSRQMDF 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1887789594 1309 FAFKENRLPLFVKVRDTTQEPCGRLSFMKEPKSTRGLVHQAICNLNITLP 1358
Cdd:pfam17809   81 KAFRENRLDGSVRVKDPSDPPKGLLSFMRDAKVDGGTVSQPLCTLNIVLP 130
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
155-439 4.83e-59

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 205.57  E-value: 4.83e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  155 NQAVAILLENDTKGKVRLPALHIAARKDDTKSAALLLQNDHNADVQSKSGFTPLHIAAHYGNVNVATLLLNRGAAVDFTA 234
Cdd:COG0666      5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  235 RNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGD 314
Cdd:COG0666     85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANG 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  315 HVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGAS 394
Cdd:COG0666    165 NLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD 244

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1887789594  395 IQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETAL 439
Cdd:COG0666    245 LNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
482-752 7.17e-59

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 205.19  E-value: 7.17e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  482 EIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAAD 561
Cdd:COG0666      2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  562 SAGKNGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAA 641
Cdd:COG0666     82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  642 QEDKVNVADILTKHGADQDAHTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQH 721
Cdd:COG0666    162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1887789594  722 GAKPNATTANGNTALAIAKRLGYISVVDTLK 752
Cdd:COG0666    242 GADLNAKDKDGLTALLLAAAAGAALIVKLLL 272
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
322-604 8.59e-58

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 202.11  E-value: 8.59e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  322 LLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITES 401
Cdd:COG0666      7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  402 GLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKT 481
Cdd:COG0666     87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  482 EIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAAD 561
Cdd:COG0666    167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1887789594  562 SAGKNGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPL 604
Cdd:COG0666    247 AKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Death_ank2 cd08804
Death domain of Ankyrin-2; Death Domain (DD) of Ankyrin-2 (ANK-2) and related proteins. ...
 1387-1470 1.65e-51

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


Pssm-ID: 260066  Cd Length: 84  Bit Score: 176.04  E-value: 1.65e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594 1387 ERIEERLAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIV 1466
Cdd:cd08804      1 ERTEERLAHIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLTQCLTKINRMDIV 80


                   ....
gi 1887789594 1467 HLME 1470
Cdd:cd08804     81 HLME 84
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
3-307 5.12e-51

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 182.46  E-value: 5.12e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594    3 TMLQKSDSNASFLRAARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHI 82
Cdd:COG0666     47 LALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHL 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594   83 ASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGAnqstatedgftplavalqqghnqavaill 162
Cdd:COG0666    127 AAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA----------------------------- 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  163 endtkgkvrlpalhiaarkddtksaalllqndhNADVQSKSGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLH 242
Cdd:COG0666    178 ---------------------------------DVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALD 224

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1887789594  243 VASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPL 307
Cdd:COG0666    225 LAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
 904-1008 3.00e-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: 3.00e-50
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594   904 SGFLVSFMVDARGGAMRGCRhNGLRIIIPPRKCTAPTRVTCRLVKRHRLATMPPMVEGEGLASRLIEVGPSGAQFLGPVI 983
Cdd:smart00218    1 PSFLVSGTFDARGGRLRGPR-TGVRLIIPPGAIPQGTRYTCYLVVHKTLSTPPPLEEGETLLSPVVECGPHGALFLRPVI 79

                            90       100
                    ....*....|....*....|....*
gi 1887789594   984 VEIPHFAALRGKERELVVLRSENGD 1008
Cdd:smart00218   80 LEVPHCASLRPRDWEIVLLRSENGG 104
ZU5 pfam00791
ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.
 908-1005 6.91e-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: 6.91e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  908 VSFMVDARGGAMRGCrHNGLRIIIPPRKCTAPTRVTCRLVKRHRLATMPPMVEGEGLASRLIEVGPSGAQFLGPVIVEIP 987
Cdd:pfam00791    1 VSGLVDSRGGRLVLP-NSGVSLLIPPGAIPEGTRIECYLAVNRDESSRPPLEEGETLLSPVVECGPPGLKFLKPVILEVP 79

                           90
                   ....*....|....*...
gi 1887789594  988 HFAALRGKERELVVLRSE 1005
Cdd:pfam00791   80 HCASLRPEEWEIVLKRSD 97
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 448-723 4.53e-37

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 145.96  E-value: 4.53e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  448 VEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHIsaregqvdvasvlleagaah 527
Cdd:PHA03100    15 VKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHY-------------------- 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  528 slatkkgftplHVAAKYGSLDV---AKLLLQRRAAADSAGKNGYTPLHIAA--KKNQMQIASTLLNYGAETNIVTKQGVT 602
Cdd:PHA03100    75 -----------LSNIKYNLTDVkeiVKLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGEN 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  603 PLHLASQEGHTD--MVTLLLDKGANIhmstksgltslhlaaqeDKVNVADILTKHGADQDAHTKLGYTPLIVACHYGNVK 680
Cdd:PHA03100   144 LLHLYLESNKIDlkILKLLIDKGVDI-----------------NAKNRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPE 206

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1887789594  681 MVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGA 723
Cdd:PHA03100   207 FVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 90-398 4.94e-34

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 137.10  E-value: 4.94e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594   90 EVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHNQavaillendtkgk 169
Cdd:PHA03100    16 KNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNL------------- 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  170 vrlpalhiaarKDDTKSAALLLQNDHNADVQSKSGFTPLHIAA--HYGNVNVATLLLNRGAAVDFTARNGITPLHVA--S 245
Cdd:PHA03100    83 -----------TDVKEIVKLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYleS 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  246 KRGNTNMVKLLLDRGGQIDAKTRdgltplhcaarsghdqvVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKhllqh 325
Cdd:PHA03100   152 NKIDLKILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVK----- 209

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1887789594  326 kapvddvtldyltalhvaahcghyrvtkLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAI 398
Cdd:PHA03100   210 ----------------------------YLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTI 254
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 219-629 5.51e-32

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 134.81  E-value: 5.51e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  219 VATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAarsghdqvvelllergaplla 298
Cdd:PHA02876   160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECA--------------------- 218

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  299 rtknglsplhmaaqgdhvecvkhllqhkapVDDVTLDYLTAlhvaahcghyrvtklLLDKRANPNARALNgftpLHIACK 378
Cdd:PHA02876   219 ------------------------------VDSKNIDTIKA---------------IIDNRSNINKNDLS----LLKAIR 249

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  379 KNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGHLN-IVLLLLQNGASPDVTNIRGETALHMAARAG-QVEVVRCLLR 456
Cdd:PHA02876   250 NEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIM 329

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  457 NGALVDARAREEQTPLHIASRLGK-TEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGF 535
Cdd:PHA02876   330 LGADVNAADRLYITPLHQASTLDRnKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIG 409

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  536 TPLHVAAkYGS--LDVAKLLLQRRAAADSAGKNGYTPLHIAAKKN-QMQIASTLLNYGAETNIVTKQGVTPLHLASqeGH 612
Cdd:PHA02876   410 TALHFAL-CGTnpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EY 486

                          410
                   ....*....|....*..
gi 1887789594  613 TDMVTLLLDKGANIHMS 629
Cdd:PHA02876   487 HGIVNILLHYGAELRDS 503
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 16-265 3.37e-26

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 113.61  E-value: 3.37e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594   16 RAARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVglvqelLGRGssvdsatkkgntalhiaslagqAEVVKVL 95
Cdd:PHA03100    41 LAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYN------LTDV----------------------KEIVKLL 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594   96 VKEGANINAQSQNGFTPLYMAAQE--NHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHN--QAVAILLEN----DTK 167
Cdd:PHA03100    93 LEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKgvdiNAK 172

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  168 GKVRlpalhiaarkddtksaaLLLQNDHNADVQSKSGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKR 247
Cdd:PHA03100   173 NRVN-----------------YLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILN 235

                          250
                   ....*....|....*...
gi 1887789594  248 GNTNMVKLLLDRGGQIDA 265
Cdd:PHA03100   236 NNKEIFKLLLNNGPSIKT 253
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
 1386-1471 7.44e-24

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


Pssm-ID: 214467 [Multi-domain]  Cd Length: 88  Bit Score: 97.10  E-value: 7.44e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  1386 QERIEERLAYIADH-LGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMD 1464
Cdd:smart00005    1 PELTRQKLAKLLDHpLGLDWRELARKLGLSEADIDQIRTEAPRDLAEQSVQLLRLWEQREGKNATLGTLLEALRKMGRDD 80


                    ....*..
gi 1887789594  1465 IVHLMET 1471
Cdd:smart00005   81 AVELLRS 87
Ank_2 pfam12796
Ankyrin repeats (3 copies);
47-134 1.39e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 96.34  E-value: 1.39e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594   47 LHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEgANINAQSqNGFTPLYMAAQENHIDVVK 126
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78


                   ....*...
gi 1887789594  127 YLLENGAN 134
Cdd:pfam12796   79 LLLEKGAD 86
Ank_2 pfam12796
Ankyrin repeats (3 copies);
208-294 2.15e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 95.95  E-value: 2.15e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  208 LHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRgGQIDAKTrDGLTPLHCAARSGHDQVVE 287
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78


                   ....*..
gi 1887789594  288 LLLERGA 294
Cdd:pfam12796   79 LLLEKGA 85
Ank_2 pfam12796
Ankyrin repeats (3 copies);
538-627 1.26e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 93.64  E-value: 1.26e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  538 LHVAAKYGSLDVAKLLLQRRAAADSAGKNGYTPLHIAAKKNQMQIASTLLNYgAETNIVTkQGVTPLHLASQEGHTDMVT 617
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|
gi 1887789594  618 LLLDKGANIH 627
Cdd:pfam12796   79 LLLEKGADIN 88
Death pfam00531
Death domain;
1390-1470 2.48e-21

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 89.73  E-value: 2.48e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594 1390 EERLAYIADH---LGFSWTELARELDFTEEQIHQIRIENPNsLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIV 1466
Cdd:pfam00531    1 RKQLDRLLDPpppLGKDWRELARKLGLSENEIDEIESENPR-LRSQTYELLRLWEQREGKNATVGTLLEALRKLGRRDAA 79


                   ....
gi 1887789594 1467 HLME 1470
Cdd:pfam00531   80 EKIQ 83
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 371-557 3.57e-15

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 81.21  E-value: 3.57e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  371 TPLHIACKKNRIKVMELLVKY-GASIQAITESGLTPIHVAAFMGHLNIVLLLLQngASPDVTNI-------RGETALHMA 442
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNEpmtsdlyQGETALHIA 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  443 ARAGQVEVVRCLLRNGA-LVDARA-----REEQT--------PLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHIS 508
Cdd:cd22192     97 VVNQNLNLVRELIARGAdVVSPRAtgtffRPGPKnliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHIL 176

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1887789594  509 AREGQVDVA----SVLLEA---GAAHSLAT---KKGFTPLHVAAKYGSLDVAKLLLQRR 557
Cdd:cd22192    177 VLQPNKTFAcqmyDLILSYdkeDDLQPLDLvpnNQGLTPFKLAAKEGNIVMFQHLVQKR 235
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 175-390 4.47e-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: 80.83  E-value: 4.47e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  175 LHIAARKDDTKSAALLLQNDHnADVQSKS--GFTPLHIAAHYGNVNVATLLL-------NRGAAVDFTArnGITPLHVAS 245
Cdd:cd22192     21 LLLAAKENDVQAIKKLLKCPS-CDLFQRGalGETALHVAALYDNLEAAVVLMeaapelvNEPMTSDLYQ--GETALHIAV 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  246 KRGNTNMVKLLLDRGGQIDA---------KTRDGLT-----PLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMAA 311
Cdd:cd22192     98 VNQNLNLVRELIARGADVVSpratgtffrPGPKNLIyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILV 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  312 QGDHVECVKH----LLQHKAPVDDVTLDYLtalhvaahcghyrvtkllldkranPNARalnGFTPLHIACKKNRIKVMEL 387
Cdd:cd22192    178 LQPNKTFACQmydlILSYDKEDDLQPLDLV------------------------PNNQ---GLTPFKLAAKEGNIVMFQH 230


                   ...
gi 1887789594  388 LVK 390
Cdd:cd22192    231 LVQ 233
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 503-687 4.32e-13

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: 74.28  E-value: 4.32e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  503 TPLHISAREGQVDVASVLLEAGAAHSLATKK-GFTPLHVAAKYGSLDVAKLLLqrRAAAD-------SAGKNGYTPLHIA 574
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGAlGETALHVAALYDNLEAAVVLM--EAAPElvnepmtSDLYQGETALHIA 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  575 AKKNQMQIASTLLNYGAEtniVTKQGVT-----------------PLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSL 637
Cdd:cd22192     97 VVNQNLNLVRELIARGAD---VVSPRATgtffrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  638 H-LAAQEDKV---NVADILTKHGADQDAHT------KLGYTPLIVACHYGNVKMVNFLLK 687
Cdd:cd22192    174 HiLVLQPNKTfacQMYDLILSYDKEDDLQPldlvpnNQGLTPFKLAAKEGNIVMFQHLVQ 233
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 262-510 1.17e-12

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 73.19  E-value: 1.17e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  262 QIDAKTRDGLTPLHCAA-RSGHDQVVELLLERGAplLARTknGLSPLHMAAQGdHVECVKHLLQH--KAPVDDVTLDYL- 337
Cdd:TIGR00870   44 NINCPDRLGRSALFVAAiENENLELTELLLNLSC--RGAV--GDTLLHAISLE-YVDAVEAILLHllAAFRKSGPLELAn 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  338 -----------TALHVAAHCGHYRVTKLLLDKRANPNARALNGFtplhiaCKKnriKVMELLVKYGASiqaitesgltPI 406
Cdd:TIGR00870  119 dqytseftpgiTALHLAAHRQNYEIVKLLLERGASVPARACGDF------FVK---SQGVDSFYHGES----------PL 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  407 HVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAA----RAGQVEVVRCLLRNGAL-VDARAREEQ-----------T 470
Cdd:TIGR00870  180 NAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVmeneFKAEYEELSCQMYNFALsLLDKLRDSKelevilnhqglT 259

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1887789594  471 PLHIASRLGKTEIVQLLLQ-------HMAHPdaattngYTPLHISAR 510
Cdd:TIGR00870  260 PLKLAAKEGRIVLFRLKLAikykqkkFVAWP-------NGQQLLSLY 299
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 75-226 9.67e-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: 9.67e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594   75 KGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGF--------------TPLYMAAQENHIDVVKYLLENGANQSTAte 140
Cdd:cd22194    140 EGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVFfnpkykhegfyfgeTPLALAACTNQPEIVQLLMEKESTDITS-- 217

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  141 dgftplavalqqghnqavailleNDTKGKVRLPALHIAArkDDTKS----------AALLLQNDHNAD-VQSKSGFTPLH 209
Cdd:cd22194    218 -----------------------QDSRGNTVLHALVTVA--EDSKTqndfvkrmydMILLKSENKNLEtIRNNEGLTPLQ 272

                          170
                   ....*....|....*..
gi 1887789594  210 IAAHYGNVNVATLLLNR 226
Cdd:cd22194    273 LAAKMGKAEILKYILSR 289
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 420-501 7.93e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 63.76  E-value: 7.93e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  420 LLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATT 499
Cdd:PTZ00322   100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGA 179


                   ..
gi 1887789594  500 NG 501
Cdd:PTZ00322   180 NA 181
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 358-557 8.46e-10

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 63.95  E-value: 8.46e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  358 KRANPNARALN-------GFTPLHIACKKNRIK-VMELLVKYGASIqaitESGLTPIHVAAFMGHLN---IVLLLLQNGA 426
Cdd:TIGR00870   34 YRDLEEPKKLNincpdrlGRSALFVAAIENENLeLTELLLNLSCRG----AVGDTLLHAISLEYVDAveaILLHLLAAFR 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  427 SPDVTNI----------RGETALHMAARAGQVEVVRCLLRNGALVDARA--------------REEQTPLHIASRLGKTE 482
Cdd:TIGR00870  110 KSGPLELandqytseftPGITALHLAAHRQNYEIVKLLLERGASVPARAcgdffvksqgvdsfYHGESPLNAAACLGSPS 189

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  483 IVQLLLQHMAHPDAATTNGYTPLHISAREG-----------QVDVASVLLEAGAAHSLATK-----KGFTPLHVAAKYGS 546
Cdd:TIGR00870  190 IVALLSEDPADILTADSLGNTLLHLLVMENefkaeyeelscQMYNFALSLLDKLRDSKELEvilnhQGLTPLKLAAKEGR 269

                          250
                   ....*....|.
gi 1887789594  547 LDVAKLLLQRR 557
Cdd:TIGR00870  270 IVLFRLKLAIK 280
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 400-556 3.86e-09

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 61.43  E-value: 3.86e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  400 ESGLTPIHVAAF---MGHLNIVLLLLQngASPDVTNIR-------------GETALHMAARAGQVEVVRCLLRNGALVDA 463
Cdd:cd21882     24 ATGKTCLHKAALnlnDGVNEAIMLLLE--AAPDSGNPKelvnapctdefyqGQTALHIAIENRNLNLVRLLVENGADVSA 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  464 RA-----REEQT--------PLHIASRLGKTEIVQLLLQHMAHPDAATTN---GYTPLHI------SAREGQVDVASV-- 519
Cdd:cd21882    102 RAtgrffRKSPGnlfyfgelPLSLAACTNQEEIVRLLLENGAQPAALEAQdslGNTVLHAlvlqadNTPENSAFVCQMyn 181

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1887789594  520 -LLEAGAA-------HSLATKKGFTPLHVAAKYGSLDVAKLLLQR 556
Cdd:cd21882    182 lLLSYGAHldptqqlEEIPNHQGLTPLKLAAVEGKIVMFQHILQR 226
Ank_4 pfam13637
Ankyrin repeats (many copies);
437-488 7.74e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.35  E-value: 7.74e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1887789594  437 TALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLL 488
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 9-246 9.15e-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: 9.15e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594    9 DSNASFLRAARAGNLD--KVVEYLKGGIDIntcnqnGLNALHLAAKEGHVGlVQELL--------GRGSS---VDSATK- 74
Cdd:TIGR00870   52 GRSALFVAAIENENLEltELLLNLSCRGAV------GDTLLHAISLEYVDA-VEAILlhllaafrKSGPLelaNDQYTSe 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594   75 --KGNTALHIASLAGQAEVVKVLVKEGANINA----------QSQNGF----TPLYMAAQENHIDVVKYLLENGANQSTA 138
Cdd:TIGR00870  125 ftPGITALHLAAHRQNYEIVKLLLERGASVPAracgdffvksQGVDSFyhgeSPLNAAACLGSPSIVALLSEDPADILTA 204

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  139 TEDGFTPLAVALQQGHNQAvaillENDTKG-KVRLPALHIAARKDDTKSAALLLQNDhnadvqsksGFTPLHIAAHYGNV 217
Cdd:TIGR00870  205 DSLGNTLLHLLVMENEFKA-----EYEELScQMYNFALSLLDKLRDSKELEVILNHQ---------GLTPLKLAAKEGRI 270

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1887789594  218 NVATLLLNRGAAV-DFTA-RNGitPLHVASK 246
Cdd:TIGR00870  271 VLFRLKLAIKYKQkKFVAwPNG--QQLLSLY 299
NESP55 pfam06390
Neuroendocrine-specific golgi protein P55 (NESP55); This family consists of several mammalian ...
 1543-1680 2.19e-07

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: 54.10  E-value: 2.19e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594 1543 TFQDGVPKTEGDSSATALFPQTHKEQVQQDFSGKMQDLPEESSLEYQQEYFVTTPGTET-------SETQKAMIVPSSPS 1615
Cdd:pfam06390   62 SFLNAHHRSAAAAAAAQVFPEPSEPESDHEDEDFEPELARPECLEYDEDDFDTETDSETepesdieSETEFETEPETEPD 141

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594 1616 KTPE-EVSTPAEEEK--------------------LYLQTPTSSERGGSPIIQEPEEPSEHRE------ESSPR--KTSL 1666
Cdd:pfam06390  142 TAPTtEPETEPEDEPgpvvpkgatfhqslterlhaLKLQSADASPRRAPPSTQEPESAREGEEpergplDKDPRdpEEEE 221

                          170
                   ....*....|....
gi 1887789594 1667 VIVESADNQPETCE 1680
Cdd:pfam06390  222 EEKEEEKQQPHRCK 235
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: 45.66  E-value: 2.38e-06
                            10        20
                    ....*....|....*....|....*..
gi 1887789594   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 ...
 368-395 6.15e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 44.50  E-value: 6.15e-06
                            10        20
                    ....*....|....*....|....*...
gi 1887789594   368 NGFTPLHIACKKNRIKVMELLVKYGASI 395
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 698-727 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: 43.73  E-value: 1.14e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 1887789594   698 NGYTPLHQAAQQGHTHIINVLLQHGAKPNA 727
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 434-463 2.02e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 40.26  E-value: 2.02e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 1887789594   434 RGETALHMAARAGQVEVVRCLLRNGALVDA 463
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 501-747 5.41e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 45.07  E-value: 5.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  501 GYTPLHISAREGQV-DVASVLLEagaaHSLATKKGFTPLHVAAKyGSLDVAKLLLQRRAAADsaGKNGYTPLHIAAKKNQ 579
Cdd:TIGR00870   52 GRSALFVAAIENENlELTELLLN----LSCRGAVGDTLLHAISL-EYVDAVEAILLHLLAAF--RKSGPLELANDQYTSE 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  580 MQiastllnygaetnivtkQGVTPLHLASQEGHTDMVTLLLDKGANIHMstksgltslhlaaqedKVNVADILTKHGADQ 659
Cdd:TIGR00870  125 FT-----------------PGITALHLAAHRQNYEIVKLLLERGASVPA----------------RACGDFFVKSQGVDS 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  660 DAHTKLgytPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGH---------THIINVLLQHGAKPNATTA 730
Cdd:TIGR00870  172 FYHGES---PLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVMENEfkaeyeelsCQMYNFALSLLDKLRDSKE 248

                          250       260
                   ....*....|....*....|....
gi 1887789594  731 -------NGNTALAIAKRLGYISV 747
Cdd:TIGR00870  249 levilnhQGLTPLKLAAKEGRIVL 272
 
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 ...
 1229-1358 3.48e-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: 3.48e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594 1229 VPYMAKFVVFAKSHDPIEARLRCFCMTDDKVDKTLEQQENFAEVARSRDVEVLEGKPIYVDCFGNLVPLTKSGQHHIFSF 1308
Cdd:pfam17809    1 VPYLAKFVVFAKRYDPGEARLRCACMTDDGEDKTLEFHEGFTEVARSRDVEVLEGSPVSIELSGNLVPIKKKSQSRQMDF 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1887789594 1309 FAFKENRLPLFVKVRDTTQEPCGRLSFMKEPKSTRGLVHQAICNLNITLP 1358
Cdd:pfam17809   81 KAFRENRLDGSVRVKDPSDPPKGLLSFMRDAKVDGGTVSQPLCTLNIVLP 130
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
155-439 4.83e-59

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 205.57  E-value: 4.83e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  155 NQAVAILLENDTKGKVRLPALHIAARKDDTKSAALLLQNDHNADVQSKSGFTPLHIAAHYGNVNVATLLLNRGAAVDFTA 234
Cdd:COG0666      5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  235 RNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGD 314
Cdd:COG0666     85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANG 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  315 HVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGAS 394
Cdd:COG0666    165 NLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD 244

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1887789594  395 IQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETAL 439
Cdd:COG0666    245 LNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
187-472 6.84e-59

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 205.19  E-value: 6.84e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  187 AALLLQNDHNADVQSKSGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAK 266
Cdd:COG0666      4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  267 TRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHC 346
Cdd:COG0666     84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  347 GHYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGA 426
Cdd:COG0666    164 GNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1887789594  427 SPDVTNIRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPL 472
Cdd:COG0666    244 DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
283-571 6.90e-59

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 205.19  E-value: 6.90e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  283 DQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANP 362
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  363 NARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMA 442
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  443 ARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLE 522
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1887789594  523 AGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGYTPL 571
Cdd:COG0666    241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
482-752 7.17e-59

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 205.19  E-value: 7.17e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  482 EIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAAD 561
Cdd:COG0666      2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  562 SAGKNGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAA 641
Cdd:COG0666     82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  642 QEDKVNVADILTKHGADQDAHTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQH 721
Cdd:COG0666    162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1887789594  722 GAKPNATTANGNTALAIAKRLGYISVVDTLK 752
Cdd:COG0666    242 GADLNAKDKDGLTALLLAAAAGAALIVKLLL 272
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
217-505 1.15e-58

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 204.80  E-value: 1.15e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  217 VNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAPL 296
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  297 LARTKNGLSPLHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNARALNGFTPLHIA 376
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  377 CKKNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLR 456
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1887789594  457 NGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPL 505
Cdd:COG0666    241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
322-604 8.59e-58

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 202.11  E-value: 8.59e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  322 LLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITES 401
Cdd:COG0666      7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  402 GLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKT 481
Cdd:COG0666     87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  482 EIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAAD 561
Cdd:COG0666    167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1887789594  562 SAGKNGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPL 604
Cdd:COG0666    247 AKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
122-406 1.59e-56

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 198.64  E-value: 1.59e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  122 IDVVKYLLENGANQSTATEDGFTPLAVALQQGHNQAVAILLENDTKGKVRL----PALHIAARKDDTKSAALLLQNDHNA 197
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADalgaLLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  198 DVQSKSGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCA 277
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  278 ARSGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLD 357
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1887789594  358 KRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPI 406
Cdd:COG0666    241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
251-538 2.31e-56

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 197.87  E-value: 2.31e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  251 NMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLLQHKAPVD 330
Cdd:COG0666      2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  331 DVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAA 410
Cdd:COG0666     82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  411 FMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQH 490
Cdd:COG0666    162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1887789594  491 MAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPL 538
Cdd:COG0666    242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
454-736 8.97e-56

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 196.33  E-value: 8.97e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  454 LLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKK 533
Cdd:COG0666      7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  534 GFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHT 613
Cdd:COG0666     87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  614 DMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADILTKHGADQDAHTKLGYTPLIVACHYGNVKMVNFLLKQGANVN 693
Cdd:COG0666    167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1887789594  694 AKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTAL 736
Cdd:COG0666    247 AKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
354-635 1.45e-55

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 195.56  E-value: 1.45e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  354 LLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNI 433
Cdd:COG0666      6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  434 RGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQ 513
Cdd:COG0666     86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  514 VDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGYTPLHIAAKKNQMQIASTLLNYGAET 593
Cdd:COG0666    166 LEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADL 245

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1887789594  594 NIVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLT 635
Cdd:COG0666    246 NAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
23-373 4.74e-55

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 194.40  E-value: 4.74e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594   23 LDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGANI 102
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  103 NAQSQNGFTPLYMAAQENHIDVVKYLLENGAnqstatedgftplavalqqghnqavaillendtkgkvrlpalhiaarkd 182
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGA------------------------------------------------- 111

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  183 dtksaalllqndhNADVQSKSGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQ 262
Cdd:COG0666    112 -------------DVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGAD 178

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  263 IDAKTRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHV 342
Cdd:COG0666    179 VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLL 258

                          330       340       350
                   ....*....|....*....|....*....|.
gi 1887789594  343 AAHCGHYRVTKLLLDKRANPNARALNGFTPL 373
Cdd:COG0666    259 AAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
382-670 5.63e-55

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 194.02  E-value: 5.63e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  382 IKVMELLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNGALV 461
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  462 DARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVA 541
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  542 AKYGSLDVAKLLLQRRAAADSAGKNGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLD 621
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1887789594  622 KGANIHMSTKSGLTSLHLAAQEDKVNVADILTKHGADQDAHTKLGYTPL 670
Cdd:COG0666    241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
415-703 8.36e-55

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 193.63  E-value: 8.36e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  415 LNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHP 494
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  495 DAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGYTPLHIA 574
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  575 AKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADILTK 654
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1887789594  655 HGADQDAHTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPL 703
Cdd:COG0666    241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
5-340 2.08e-54

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 192.48  E-value: 2.08e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594    5 LQKSDSNASFLRAARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIAS 84
Cdd:COG0666     16 LLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAA 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594   85 LAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGAnqstatedgftplavalqqghnqavaillen 164
Cdd:COG0666     96 RNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGA------------------------------- 144

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  165 dtkgkvrlpalhiaarkddtksaalllqndhNADVQSKSGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVA 244
Cdd:COG0666    145 -------------------------------DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLA 193

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  245 SKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLLQ 324
Cdd:COG0666    194 AENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLL 273

                          330
                   ....*....|....*.
gi 1887789594  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. ...
 1387-1470 1.65e-51

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


Pssm-ID: 260066  Cd Length: 84  Bit Score: 176.04  E-value: 1.65e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594 1387 ERIEERLAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIV 1466
Cdd:cd08804      1 ERTEERLAHIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLTQCLTKINRMDIV 80


                   ....
gi 1887789594 1467 HLME 1470
Cdd:cd08804     81 HLME 84
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
3-307 5.12e-51

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 182.46  E-value: 5.12e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594    3 TMLQKSDSNASFLRAARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHI 82
Cdd:COG0666     47 LALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHL 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594   83 ASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGAnqstatedgftplavalqqghnqavaill 162
Cdd:COG0666    127 AAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA----------------------------- 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  163 endtkgkvrlpalhiaarkddtksaalllqndhNADVQSKSGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLH 242
Cdd:COG0666    178 ---------------------------------DVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALD 224

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1887789594  243 VASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPL 307
Cdd:COG0666    225 LAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
 904-1008 3.00e-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: 3.00e-50
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594   904 SGFLVSFMVDARGGAMRGCRhNGLRIIIPPRKCTAPTRVTCRLVKRHRLATMPPMVEGEGLASRLIEVGPSGAQFLGPVI 983
Cdd:smart00218    1 PSFLVSGTFDARGGRLRGPR-TGVRLIIPPGAIPQGTRYTCYLVVHKTLSTPPPLEEGETLLSPVVECGPHGALFLRPVI 79

                            90       100
                    ....*....|....*....|....*
gi 1887789594   984 VEIPHFAALRGKERELVVLRSENGD 1008
Cdd:smart00218   80 LEVPHCASLRPRDWEIVLLRSENGG 104
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
547-751 4.80e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 159.73  E-value: 4.80e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  547 LDVAKLLLQRRAAADSAGKNGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLDKGANI 626
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  627 HMSTKSGLTSLHLAAQEDKVNVADILTKHGADQDAHTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQA 706
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1887789594  707 AQQGHTHIINVLLQHGAKPNATTANGNTALAIAKRLGYISVVDTL 751
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
ZU5 pfam00791
ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.
 908-1005 6.91e-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: 6.91e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  908 VSFMVDARGGAMRGCrHNGLRIIIPPRKCTAPTRVTCRLVKRHRLATMPPMVEGEGLASRLIEVGPSGAQFLGPVIVEIP 987
Cdd:pfam00791    1 VSGLVDSRGGRLVLP-NSGVSLLIPPGAIPEGTRIECYLAVNRDESSRPPLEEGETLLSPVVECGPPGLKFLKPVILEVP 79

                           90
                   ....*....|....*...
gi 1887789594  988 HFAALRGKERELVVLRSE 1005
Cdd:pfam00791   80 HCASLRPEEWEIVLKRSD 97
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 448-723 4.53e-37

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 145.96  E-value: 4.53e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  448 VEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHIsaregqvdvasvlleagaah 527
Cdd:PHA03100    15 VKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHY-------------------- 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  528 slatkkgftplHVAAKYGSLDV---AKLLLQRRAAADSAGKNGYTPLHIAA--KKNQMQIASTLLNYGAETNIVTKQGVT 602
Cdd:PHA03100    75 -----------LSNIKYNLTDVkeiVKLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGEN 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  603 PLHLASQEGHTD--MVTLLLDKGANIhmstksgltslhlaaqeDKVNVADILTKHGADQDAHTKLGYTPLIVACHYGNVK 680
Cdd:PHA03100   144 LLHLYLESNKIDlkILKLLIDKGVDI-----------------NAKNRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPE 206

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1887789594  681 MVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGA 723
Cdd:PHA03100   207 FVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
Death_ank cd08317
Death domain associated with Ankyrins; Death Domain (DD) associated with Ankyrins. Ankyrins ...
 1387-1470 3.51e-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: 132.00  E-value: 3.51e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594 1387 ERIEERLAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIV 1466
Cdd:cd08317      1 HRADLRLSDIANLLGSDWPELARELGVSEEDIDLIRSENPNSLAQQAMAMLRLWLEREGEKATGNALESALKKIGRDDIV 80


                   ....
gi 1887789594 1467 HLME 1470
Cdd:cd08317     81 EKCE 84
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 90-398 4.94e-34

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 137.10  E-value: 4.94e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594   90 EVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHNQavaillendtkgk 169
Cdd:PHA03100    16 KNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNL------------- 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  170 vrlpalhiaarKDDTKSAALLLQNDHNADVQSKSGFTPLHIAA--HYGNVNVATLLLNRGAAVDFTARNGITPLHVA--S 245
Cdd:PHA03100    83 -----------TDVKEIVKLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYleS 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  246 KRGNTNMVKLLLDRGGQIDAKTRdgltplhcaarsghdqvVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKhllqh 325
Cdd:PHA03100   152 NKIDLKILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVK----- 209

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1887789594  326 kapvddvtldyltalhvaahcghyrvtkLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAI 398
Cdd:PHA03100   210 ----------------------------YLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTI 254
PHA03095 PHA03095
ankyrin-like protein; Provisional
 217-498 2.26e-33

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 136.31  E-value: 2.26e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  217 VNVATLLLNRGAAVDFTARNGITPLHVASKRGN---TNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHD-QVVELLLER 292
Cdd:PHA03095    27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKA 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  293 GAPLLARTKNGLSPLHMAAQGD--HVECVKHLLQHKAPVDDVTLDYLTALHV--AAHCGHYRVTKLLLDKRANPNARALN 368
Cdd:PHA03095   107 GADVNAKDKVGRTPLHVYLSGFniNPKVIRLLLRKGADVNALDLYGMTPLAVllKSRNANVELLRLLIDAGADVYAVDDR 186

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  369 GFTPLHIACK--KNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGHLN--IVLLLLQNGASPDVTNIRGETALHMAAR 444
Cdd:PHA03095   187 FRSLLHHHLQsfKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLHYAAV 266

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1887789594  445 AGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQhmAHPDAAT 498
Cdd:PHA03095   267 FNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALA--KNPSAET 318
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 190-427 1.28e-32

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 132.87  E-value: 1.28e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  190 LLQNDHNADVQSKSGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLH-----VASKRGNTNMVKLLLDRGGQID 264
Cdd:PHA03100    21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGANVN 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  265 AKTRDGLTPLHCAA--RSGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGDHV--ECVKHLLQHKAPVDDVTldyltal 340
Cdd:PHA03100   101 APDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKN------- 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  341 hvaahcghyRVtKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGHLNIVLL 420
Cdd:PHA03100   174 ---------RV-NYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKL 243


                   ....*..
gi 1887789594  421 LLQNGAS 427
Cdd:PHA03100   244 LLNNGPS 250
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 219-629 5.51e-32

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 134.81  E-value: 5.51e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  219 VATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAarsghdqvvelllergaplla 298
Cdd:PHA02876   160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECA--------------------- 218

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  299 rtknglsplhmaaqgdhvecvkhllqhkapVDDVTLDYLTAlhvaahcghyrvtklLLDKRANPNARALNgftpLHIACK 378
Cdd:PHA02876   219 ------------------------------VDSKNIDTIKA---------------IIDNRSNINKNDLS----LLKAIR 249

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  379 KNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGHLN-IVLLLLQNGASPDVTNIRGETALHMAARAG-QVEVVRCLLR 456
Cdd:PHA02876   250 NEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIM 329

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  457 NGALVDARAREEQTPLHIASRLGK-TEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGF 535
Cdd:PHA02876   330 LGADVNAADRLYITPLHQASTLDRnKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIG 409

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  536 TPLHVAAkYGS--LDVAKLLLQRRAAADSAGKNGYTPLHIAAKKN-QMQIASTLLNYGAETNIVTKQGVTPLHLASqeGH 612
Cdd:PHA02876   410 TALHFAL-CGTnpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EY 486

                          410
                   ....*....|....*..
gi 1887789594  613 TDMVTLLLDKGANIHMS 629
Cdd:PHA02876   487 HGIVNILLHYGAELRDS 503
PHA03095 PHA03095
ankyrin-like protein; Provisional
 56-395 6.16e-32

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 131.69  E-value: 6.16e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594   56 VGLVQELLGRGSSVDSATKKGNTALHI---ASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQ-ENHIDVVKYLLEN 131
Cdd:PHA03095    27 VEEVRRLLAAGADVNFRGEYGKTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYnATTLDVIKLLIKA 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  132 GANQSTATEDGFTPLAVALQqghNQAVaillendtkgkvrlpalhiaarkdDTKSAALLLqnDHNADVQSK--SGFTPLH 209
Cdd:PHA03095   107 GADVNAKDKVGRTPLHVYLS---GFNI------------------------NPKVIRLLL--RKGADVNALdlYGMTPLA 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  210 IAAHYGNVNVATL--LLNRGA---AVDFtarNGITPLHV--ASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAAR--S 280
Cdd:PHA03095   158 VLLKSRNANVELLrlLIDAGAdvyAVDD---RFRSLLHHhlQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATgsS 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  281 GHDQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRA 360
Cdd:PHA03095   235 CKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNP 314

                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 1887789594  361 NPN--ARALNGFTPLH--IACKKNRIKVMELLVKYGASI 395
Cdd:PHA03095   315 SAEtvAATLNTASVAGgdIPSDATRLCVAKVVLRGAFSL 353
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 23-426 8.27e-32

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 134.42  E-value: 8.27e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594   23 LDKV-VEYLKGGIDINTCNQNGLN-------ALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKV 94
Cdd:PHA02876   117 LDEAcIHILKEAISGNDIHYDKINesieymkLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNL 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594   95 LVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGANqstatedgftplavalqqghnqavaiLLENDTkgkvrlpA 174
Cdd:PHA02876   197 LLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSN--------------------------INKNDL-------S 243

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  175 LHIAARKDDTKSAALLLQNDHNADVQSKSGFTPLHIAAHYGNVN-VATLLLNRGAAVDFTARNGITPLHVASKRG-NTNM 252
Cdd:PHA02876   244 LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGyDTEN 323

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  253 VKLLLDRGGQIDAKTRDGLTPLHCAAR-SGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLLQHKAPVDD 331
Cdd:PHA02876   324 IRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEA 403

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  332 VTLDYLTALHVAAhCGH--YRVTKLLLDKRANPNARALNGFTPLHIACKKN-RIKVMELLVKYGASIQAITESGLTPIHV 408
Cdd:PHA02876   404 LSQKIGTALHFAL-CGTnpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLI 482

                          410
                   ....*....|....*...
gi 1887789594  409 AafMGHLNIVLLLLQNGA 426
Cdd:PHA02876   483 A--LEYHGIVNILLHYGA 498
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 532-745 1.31e-31

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 129.78  E-value: 1.31e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  532 KKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGYTPLHIAA-----KKNQMQIASTLLNYGAETNIVTKQGVTPLHL 606
Cdd:PHA03100    33 KKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGANVNAPDNNGITPLLY 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  607 ASQE--GHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQ--EDKVNVADILTKHGADQDAHTKlgytplivachygnvkmV 682
Cdd:PHA03100   113 AISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLEsnKIDLKILKLLIDKGVDINAKNR-----------------V 175

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1887789594  683 NFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTAL--AIAKRLGYI 745
Cdd:PHA03100   176 NYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLhiAILNNNKEI 240
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 223-463 2.04e-31

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 129.40  E-value: 2.04e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  223 LLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQ-----VVELLLERGAPLL 297
Cdd:PHA03100    21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLtdvkeIVKLLLEYGANVN 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  298 ARTKNGLSPLHMAAQG--DHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHY--RVTKLLLDKRANPNAralngftpl 373
Cdd:PHA03100   101 APDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINA--------- 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  374 hiackKNRIKvmeLLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRC 453
Cdd:PHA03100   172 -----KNRVN---YLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKL 243

                          250
                   ....*....|
gi 1887789594  454 LLRNGALVDA 463
Cdd:PHA03100   244 LLNNGPSIKT 253
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 333-692 3.25e-31

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 132.49  E-value: 3.25e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  333 TLDYLTALHVAAHCGHYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAAFM 412
Cdd:PHA02876   142 SIEYMKLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDS 221

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  413 GHLNIVLLLLQNGASPDvtniRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGK-TEIVQLLLQHM 491
Cdd:PHA02876   222 KNIDTIKAIIDNRSNIN----KNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERG 297

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  492 AHPDAATTNGYTPLHISAREG-QVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSL-DVAKLLLQRRAAADSAGKNGYT 569
Cdd:PHA02876   298 ADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNkDIVITLLELGANVNARDYCDKT 377

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  570 PLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDM-VTLLLDKGANIHMSTKSGLTSLHLAAQED-KVN 647
Cdd:PHA02876   378 PIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLD 457

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 1887789594  648 VADILTKHGADQDAHTKLGYTPLIVACHYGNVkmVNFLLKQGANV 692
Cdd:PHA02876   458 VIEMLLDNGADVNAINIQNQYPLLIALEYHGI--VNILLHYGAEL 500
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 180-492 1.61e-30

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 130.18  E-value: 1.61e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  180 RKDDTKSAALLLQNdhNADVQSKSGF--TPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLL 257
Cdd:PHA02876   154 QQDELLIAEMLLEG--GADVNAKDIYciTPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII 231

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  258 DRGGQIDAKTRDGL-----------------------------TPLHCAARSGH-DQVVELLLERGAPLLARTKNGLSPL 307
Cdd:PHA02876   232 DNRSNINKNDLSLLkairnedletslllydagfsvnsiddcknTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPL 311

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  308 H-MAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKL-LLDKRANPNARALNGFTPLHIACKKNRIKVM 385
Cdd:PHA02876   312 YlMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVItLLELGANVNARDYCDKTPIHYAAVRNNVVII 391

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  386 ELLVKYGASIQAITESGLTPIHVAAF-MGHLNIVLLLLQNGASPDVTNIRGETALHMAARAG-QVEVVRCLLRNGALVDA 463
Cdd:PHA02876   392 NTLLDYGADIEALSQKIGTALHFALCgTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNA 471

                          330       340
                   ....*....|....*....|....*....
gi 1887789594  464 RAREEQTPLHIAsrLGKTEIVQLLLQHMA 492
Cdd:PHA02876   472 INIQNQYPLLIA--LEYHGIVNILLHYGA 498
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 378-751 2.73e-29

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 126.33  E-value: 2.73e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  378 KKNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRcllrn 457
Cdd:PHA02876   154 QQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIK----- 228

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  458 gALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGY--TPLHISAREGQVD-VASVLLEAGAAHSLATKKG 534
Cdd:PHA02876   229 -AIIDNRSNINKNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCknTPLHHASQAPSLSrLVPKLLERGADVNAKNIKG 307

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  535 FTPLHVAAKygsldvaklllqrraaadsagkNGYTPLHIaakknqmqiaSTLLNYGAETNIVTKQGVTPLHLASQ-EGHT 613
Cdd:PHA02876   308 ETPLYLMAK----------------------NGYDTENI----------RTLIMLGADVNAADRLYITPLHQASTlDRNK 355

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  614 DMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADILTKHGADQDAHTKLGYTPLIVACHYGNVKM-VNFLLKQGANV 692
Cdd:PHA02876   356 DIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANV 435

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  693 NAKTKNGYTPLHQAAQQG-HTHIINVLLQHGAKPNATTANGNTALAIAkrLGYISVVDTL 751
Cdd:PHA02876   436 NSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIA--LEYHGIVNIL 493
PHA03095 PHA03095
ankyrin-like protein; Provisional
 8-327 4.03e-29

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 123.21  E-value: 4.03e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594    8 SDSNASFLRAARAGN--LDKVVEYLKGGIDINTCNQNGLNALHLAAKEGH---VGLVQELLGRGSSVDSATKKGNTALHI 82
Cdd:PHA03095    10 IMEAALYDYLLNASNvtVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHL 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594   83 -ASLAGQAEVVKVLVKEGANINAQSQNGFTPL--YMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQgHNQAVA 159
Cdd:PHA03095    90 yLYNATTLDVIKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKS-RNANVE 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  160 I---LLEND----TKGKVRLPALHIAAR--KDDTKSAALLLQNDHNADVQSKSGFTPLHIAAHYG---NVNVATLLLNrG 227
Cdd:PHA03095   169 LlrlLIDAGadvyAVDDRFRSLLHHHLQsfKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSsckRSLVLPLLIA-G 247

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  228 AAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAP--LLARTKNGLS 305
Cdd:PHA03095   248 ISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSaeTVAATLNTAS 327

                          330       340
                   ....*....|....*....|...
gi 1887789594  306 PLHMAAQGDHV-ECVKHLLQHKA 327
Cdd:PHA03095   328 VAGGDIPSDATrLCVAKVVLRGA 350
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 371-640 8.68e-29

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 121.61  E-value: 8.68e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  371 TPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGAS------PDVTNirgetalhmaar 444
Cdd:PHA02874    37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDtsilpiPCIEK------------ 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  445 agqvEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAG 524
Cdd:PHA02874   105 ----DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKG 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  525 AAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGYTPLHIAAKKNQMQIAstLLNYGAETNIVTKQGVTPL 604
Cdd:PHA02874   181 AYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIE--LLINNASINDQDIDGSTPL 258

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1887789594  605 HLASQ-EGHTDMVTLLLDKGANIHMSTKSGLTSLHLA 640
Cdd:PHA02874   259 HHAINpPCDIDIIDILLYHKADISIKDNKGENPIDTA 295
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 512-729 4.22e-28

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 119.33  E-value: 4.22e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  512 GQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGYTPLHIAAKKNQMQIASTLLNYGA 591
Cdd:PHA02875    13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  592 ETN-IVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADILTKHGADQDAHTKLGYTPL 670
Cdd:PHA02875    93 FADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPL 172

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  671 IVACHYGNVKMVNFLLKQGANVNAKTKNG-YTPLHQAAQQGHTHIINVLLQHGAKPNATT 729
Cdd:PHA02875   173 IIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNIMF 232
Death_ank3 cd08803
Death domain of Ankyrin-3; Death Domain (DD) of the human protein ankyrin-3 (ANK-3) and ...
 1387-1470 7.08e-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: 7.08e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594 1387 ERIEERLAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIV 1466
Cdd:cd08803      1 ERTDIRMAIVADHLGLSWTELARELNFSVDEINQIRVENPNSLIAQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIV 80


                   ....
gi 1887789594 1467 HLME 1470
Cdd:cd08803     81 TLLE 84
Death_ank1 cd08805
Death domain of Ankyrin-1; Death Domain (DD) of the human protein ankyrin-1 (ANK-1) and ...
 1387-1470 1.06e-27

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: 1.06e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594 1387 ERIEERLAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIV 1466
Cdd:cd08805      1 ERVEMKMAVIREHLGLSWAELARELQFSVEDINRIRVENPNSLLEQSTALLNLWVDREGENAKMEPLYPALYSIDRLTIV 80


                   ....
gi 1887789594 1467 HLME 1470
Cdd:cd08805     81 NILE 84
PHA03095 PHA03095
ankyrin-like protein; Provisional
 448-752 1.67e-27

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 118.59  E-value: 1.67e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  448 VEVVRCLLRNGALVDARAREEQTPLH--IASRLGK-TEIVQLLLQHMAHPDAATTNGYTPLHISAREGQV-DVASVLLEA 523
Cdd:PHA03095    27 VEEVRRLLAAGADVNFRGEYGKTPLHlyLHYSSEKvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKA 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  524 GAAHSLATKKGFTPLHVAAKYGSLD--VAKLLLQRRAAADSAGKNGYTPLHIAAKKNQ--MQIASTLLNYGAETNIVTKQ 599
Cdd:PHA03095   107 GADVNAKDKVGRTPLHVYLSGFNINpkVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanVELLRLLIDAGADVYAVDDR 186

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  600 GVTPLH--LASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADI--LTKHGADQDAHTKLGYTPLIVACH 675
Cdd:PHA03095   187 FRSLLHhhLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAV 266

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1887789594  676 YGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQhgAKPNATT-ANgntALAIAKRLGYISVVDTLK 752
Cdd:PHA03095   267 FNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALA--KNPSAETvAA---TLNTASVAGGDIPSDATR 339
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 409-630 1.88e-27

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 117.40  E-value: 1.88e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  409 AAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLL 488
Cdd:PHA02875     9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  489 QHMAHP-DAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNG 567
Cdd:PHA02875    89 DLGKFAdDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCG 168

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1887789594  568 YTPLHIAAKKNQMQIASTLLNYGAETNIVTKQG-VTPLHLASQEGHTDMVTLLLDKGANIHMST 630
Cdd:PHA02875   169 CTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNIMF 232
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 211-441 2.24e-27

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 117.01  E-value: 2.24e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  211 AAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLL 290
Cdd:PHA02875     9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  291 ERGAPLL-ARTKNGLSPLHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNARALNG 369
Cdd:PHA02875    89 DLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCG 168

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1887789594  370 FTPLHIACKKNRIKVMELLVKYGASIQAITESG-LTPIHVAAFMGHLNIVLLLLQNGASPD-VTNIRGE--TALHM 441
Cdd:PHA02875   169 CTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNiMFMIEGEecTILDM 244
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 254-579 2.89e-27

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 116.99  E-value: 2.89e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  254 KLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLLQHKapVDDVT 333
Cdd:PHA02874    19 KIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG--VDTSI 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  334 LdyltalhvAAHCGHYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAAFMG 413
Cdd:PHA02874    97 L--------PIPCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHN 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  414 HLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASrLGKTEIVQLLLQHmAH 493
Cdd:PHA02874   169 FFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI-IHNRSAIELLINN-AS 246

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  494 PDAATTNGYTPLHISAR-EGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLD-VAKLLLQRRAAADSAGKNGYTPL 571
Cdd:PHA02874   247 INDQDIDGSTPLHHAINpPCDIDIIDILLYHKADISIKDNKGENPIDTAFKYINKDpVIKDIIANAVLIKEADKLKDSDF 326

                          330
                   ....*....|
gi 1887789594  572 --HIAAKKNQ 579
Cdd:PHA02874   327 leHIEIKDNK 336
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 347-597 4.77e-27

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 116.24  E-value: 4.77e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  347 GHYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGAsiqaitesgltpihvaafmghlnivlllLQNGA 426
Cdd:PHA02875    13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGA----------------------------IPDVK 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  427 SPDVtnirgETALHMAARAGQVEVVRCLLRNGALV-DARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPL 505
Cdd:PHA02875    65 YPDI-----ESELHDAVEEGDVKAVEELLDLGKFAdDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPL 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  506 HISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNG-YTPLHIAAKKNQMQIAS 584
Cdd:PHA02875   140 HLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVR 219

                          250
                   ....*....|...
gi 1887789594  585 TLLNYGAETNIVT 597
Cdd:PHA02875   220 LFIKRGADCNIMF 232
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 314-561 8.54e-27

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 115.53  E-value: 8.54e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  314 DHVECVKHLLQHKAPVDDVTLDYLTALHVAahCGHYRVT-------KLLLDKRANPNARALNGFTPLHIAC-----KKNR 381
Cdd:PHA03100     8 TKSRIIKVKNIKYIIMEDDLNDYSYKKPVL--PLYLAKEarnidvvKILLDNGADINSSTKNNSTPLHYLSnikynLTDV 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  382 IKVMELLVKYGASIQAITESGLTPIHVAAF--MGHLNIVLLLLQNGASPDVTNIRGETALHMAARAGQV--EVVRCLLRN 457
Cdd:PHA03100    86 KEIVKLLLEYGANVNAPDNNGITPLLYAISkkSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDK 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  458 GALVDARAReeqtplhiasrlgkteiVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTP 537
Cdd:PHA03100   166 GVDINAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTP 228

                          250       260
                   ....*....|....*....|....
gi 1887789594  538 LHVAAKYGSLDVAKLLLQRRAAAD 561
Cdd:PHA03100   229 LHIAILNNNKEIFKLLLNNGPSIK 252
PHA03095 PHA03095
ankyrin-like protein; Provisional
 375-750 1.04e-26

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 115.89  E-value: 1.04e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  375 IACKKNRIKVMELLVKYGASIQAITESGLTPIHVaafmghlnivllLLQNGASPDvtnirgetalhmaaragqVEVVRCL 454
Cdd:PHA03095    20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHL------------YLHYSSEKV------------------KDIVRLL 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  455 LRNGALVDARAREEQTPLHIASRLGKTE-IVQLLLQHMAHPDAATTNGYTPLHISARegqvdvasvlleagaahSLATKK 533
Cdd:PHA03095    70 LEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAGADVNAKDKVGRTPLHVYLS-----------------GFNINP 132

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  534 gftplhvaakygslDVAKLLLQRRAAADSAGKNGYTPLHIAAKKNqmqiastllnygaetnivtkqGVTPlhlasqeght 613
Cdd:PHA03095   133 --------------KVIRLLLRKGADVNALDLYGMTPLAVLLKSR---------------------NANV---------- 167

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  614 DMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNvADI---LTKHGADQDAHTKLGYTPLIVACHYGNVK---MVNFLLK 687
Cdd:PHA03095   168 ELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPR-ARIvreLIRAGCDPAATDMLGNTPLHSMATGSSCKrslVLPLLIA 246

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1887789594  688 qGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTALAIAKRLGYISVVDT 750
Cdd:PHA03095   247 -GISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRA 308
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 439-626 1.45e-26

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 114.76  E-value: 1.45e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  439 LHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKT-----EIVQLLLQHMAHPDAATTNGYTPLH--ISARE 511
Cdd:PHA03100    39 LYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLyaISKKS 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  512 GQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGS--LDVAKLLLQRRA----------------AADSAGKNGYTPLHI 573
Cdd:PHA03100   119 NSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVdinaknrvnyllsygvPINIKDVYGFTPLHY 198

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1887789594  574 AAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLDKGANI 626
Cdd:PHA03100   199 AVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSI 251
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 80-420 2.79e-26

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 114.98  E-value: 2.79e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594   80 LHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLenganqSTATEDGFTPLAVALQQG-HNQAV 158
Cdd:PHA02878    41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMI------RSINKCSVFYTLVAIKDAfNNRNV 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  159 AI---LLENDTKGKVRLPALHIAARKDD----TKSAALLLQndHNADVQSK---SGFTPLHIAAHYGNVNVATLLLNRGA 228
Cdd:PHA02878   115 EIfkiILTNRYKNIQTIDLVYIDKKSKDdiieAEITKLLLS--YGADINMKdrhKGNTALHYATENKDQRLTELLLSYGA 192

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  229 AVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHD-QVVELLLERGAPLLAR-TKNGLSP 306
Cdd:PHA02878   193 NVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDyDILKLLLEHGVDVNAKsYILGLTA 272

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  307 LHMAAQGDHVecVKHLLQHKAPVDDVTLDYLTALHVAA------HCGHYRVTKLLLDKRANPNARALNGFTpLHIACKKN 380
Cdd:PHA02878   273 LHSSIKSERK--LKLLLEYGADINSLNSYKLTPLSSAVkqylciNIGRILISNICLLKRIKPDIKNSEGFI-DNMDCITS 349

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 1887789594  381 RIKVMELLVKYGASIQAITESGLTPIHVAA-FMGHLNIVLL 420
Cdd:PHA02878   350 NKRLNQIKDKCEDELNRLASIKITNTYSFDdFLKCDNSTLL 390
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 16-265 3.37e-26

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 113.61  E-value: 3.37e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594   16 RAARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVglvqelLGRGssvdsatkkgntalhiaslagqAEVVKVL 95
Cdd:PHA03100    41 LAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYN------LTDV----------------------KEIVKLL 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594   96 VKEGANINAQSQNGFTPLYMAAQE--NHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHN--QAVAILLEN----DTK 167
Cdd:PHA03100    93 LEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKgvdiNAK 172

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  168 GKVRlpalhiaarkddtksaaLLLQNDHNADVQSKSGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKR 247
Cdd:PHA03100   173 NRVN-----------------YLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILN 235

                          250
                   ....*....|....*...
gi 1887789594  248 GNTNMVKLLLDRGGQIDA 265
Cdd:PHA03100   236 NNKEIFKLLLNNGPSIKT 253
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 205-502 7.17e-26

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 113.44  E-value: 7.17e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  205 FTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLldrggqIDAKTRDGLTPLHCAARSG-HD 283
Cdd:PHA02878    38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEM------IRSINKCSVFYTLVAIKDAfNN 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  284 QVVELLlerGAPLLARTKN----GLSPLHMAAQGDHVEC--VKHLLQHKAPVDDVTLDYL-TALHVAAHCGHYRVTKLLL 356
Cdd:PHA02878   112 RNVEIF---KIILTNRYKNiqtiDLVYIDKKSKDDIIEAeiTKLLLSYGADINMKDRHKGnTALHYATENKDQRLTELLL 188

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  357 DKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVA-AFMGHLNIVLLLLQNGASPDV-TNIR 434
Cdd:PHA02878   189 SYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAkSYIL 268

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1887789594  435 GETALHMAARAGQveVVRCLLRNGALVDARAREEQTPLHIASR------LGKTEIVQLLLQHMAHPDAATTNGY 502
Cdd:PHA02878   269 GLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPLSSAVKqylcinIGRILISNICLLKRIKPDIKNSEGF 340
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 54-329 2.93e-25

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 111.21  E-value: 2.93e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594   54 GHVGLVQELL-GRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENG 132
Cdd:PHA02874    12 GDIEAIEKIIkNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  133 ANQSTatedgftplaVALQQGHNQAVAILLEN----DTKGKVRLPALHIAARKDDTKSAALLLQNDHNADVQSKSGFTPL 208
Cdd:PHA02874    92 VDTSI----------LPIPCIEKDMIKTILDCgidvNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPI 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  209 HIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARsgHDQVVEL 288
Cdd:PHA02874   162 HIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIE 239

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1887789594  289 LLERGAPLLARTKNGLSPLHMAAQGD-HVECVKHLLQHKAPV 329
Cdd:PHA02874   240 LLINNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADI 281
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 110-435 7.51e-25

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 110.35  E-value: 7.51e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  110 FTPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHNQAVAILLENDTKGKV--RLPALHIAARKDDTKSA 187
Cdd:PHA02878    38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVfyTLVAIKDAFNNRNVEIF 117

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  188 ALLLQNDHNA-----DVQSKSGFTPLHIAAhygnvNVATLLLNRGAAVDFTARN-GITPLHVASKRGNTNMVKLLLDRGG 261
Cdd:PHA02878   118 KIILTNRYKNiqtidLVYIDKKSKDDIIEA-----EITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGA 192

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  262 QIDAKTRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMAaqgdhvecvkhllqhkapvddvtldyltalh 341
Cdd:PHA02878   193 NVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIS------------------------------- 241

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  342 vAAHCGHYRVTKLLLDKRANPNARA-LNGFTPLHIACKKNRikVMELLVKYGASIQAITESGLTPIHVAAF------MGH 414
Cdd:PHA02878   242 -VGYCKDYDILKLLLEHGVDVNAKSyILGLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPLSSAVKqylcinIGR 318

                          330       340
                   ....*....|....*....|.
gi 1887789594  415 LNIVLLLLQNGASPDVTNIRG 435
Cdd:PHA02878   319 ILISNICLLKRIKPDIKNSEG 339
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 439-751 2.92e-24

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 108.13  E-value: 2.92e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  439 LHMAARAGQVEVVRCLLRN-GALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVA 517
Cdd:PHA02874     5 LRMCIYSGDIEAIEKIIKNkGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDII 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  518 SVLLEAGAAHSLatkkgfTPLHVAAKygslDVAKLLLQRRAAADSAGKNGYTPLHIAAKKNQMQIASTLLNYGAETNIVT 597
Cdd:PHA02874    85 KLLIDNGVDTSI------LPIPCIEK----DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIED 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  598 KQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQedkvnvadiltkhgadqdahtklgytplivachYG 677
Cdd:PHA02874   155 DNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAE---------------------------------YG 201

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1887789594  678 NVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIinVLLQHGAKPNATTANGNTALAIAkrLGY---ISVVDTL 751
Cdd:PHA02874   202 DYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAI--ELLINNASINDQDIDGSTPLHHA--INPpcdIDIIDIL 274
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
 1386-1471 7.44e-24

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


Pssm-ID: 214467 [Multi-domain]  Cd Length: 88  Bit Score: 97.10  E-value: 7.44e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  1386 QERIEERLAYIADH-LGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMD 1464
Cdd:smart00005    1 PELTRQKLAKLLDHpLGLDWRELARKLGLSEADIDQIRTEAPRDLAEQSVQLLRLWEQREGKNATLGTLLEALRKMGRDD 80


                    ....*..
gi 1887789594  1465 IVHLMET 1471
Cdd:smart00005   81 AVELLRS 87
Ank_2 pfam12796
Ankyrin repeats (3 copies);
47-134 1.39e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 96.34  E-value: 1.39e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594   47 LHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEgANINAQSqNGFTPLYMAAQENHIDVVK 126
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78


                   ....*...
gi 1887789594  127 YLLENGAN 134
Cdd:pfam12796   79 LLLEKGAD 86
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 120-342 1.83e-23

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 105.46  E-value: 1.83e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  120 NHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHNQAVAILLENDTKGKVRLPA----LHIAARKDDTKSAALLLQ-ND 194
Cdd:PHA02875    13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDieseLHDAVEEGDVKAVEELLDlGK 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  195 HNADVQSKSGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPL 274
Cdd:PHA02875    93 FADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPL 172

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1887789594  275 HCAARSGHDQVVELLLERGAPLLARTKNG-LSPLHMAAQGDHVECVKHLLQHKAPVDDVTL---DYLTALHV 342
Cdd:PHA02875   173 IIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNIMFMiegEECTILDM 244
Ank_2 pfam12796
Ankyrin repeats (3 copies);
208-294 2.15e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 95.95  E-value: 2.15e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  208 LHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRgGQIDAKTrDGLTPLHCAARSGHDQVVE 287
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78


                   ....*..
gi 1887789594  288 LLLERGA 294
Cdd:pfam12796   79 LLLEKGA 85
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 541-736 2.67e-23

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 104.69  E-value: 2.67e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  541 AAKYGSLDVAKLLLQRRAAADSAGKNGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLL 620
Cdd:PHA02875     9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  621 DKGANIH-MSTKSGLTSLHLAAQEDKVNVADILTKHGADQDAHTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNG 699
Cdd:PHA02875    89 DLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCG 168

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1887789594  700 YTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTAL 736
Cdd:PHA02875   169 CTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAA 205
Ank_2 pfam12796
Ankyrin repeats (3 copies);
538-627 1.26e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 93.64  E-value: 1.26e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  538 LHVAAKYGSLDVAKLLLQRRAAADSAGKNGYTPLHIAAKKNQMQIASTLLNYgAETNIVTkQGVTPLHLASQEGHTDMVT 617
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|
gi 1887789594  618 LLLDKGANIH 627
Cdd:pfam12796   79 LLLEKGADIN 88
Ank_2 pfam12796
Ankyrin repeats (3 copies);
340-432 2.31e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.87  E-value: 2.31e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  340 LHVAAHCGHYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGAsiQAITESGLTPIHVAAFMGHLNIVL 419
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 1887789594  420 LLLQNGASPDVTN 432
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 83-294 2.66e-22

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 101.61  E-value: 2.66e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594   83 ASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHNQAVAILL 162
Cdd:PHA02875     9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  163 E-----NDTKGKVRLPALHIAARKDDTKSAALLLQNDHNADVQSKSGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNG 237
Cdd:PHA02875    89 DlgkfaDDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCG 168

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1887789594  238 ITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAA-RSGHDQVVELLLERGA 294
Cdd:PHA02875   169 CTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAiENNKIDIVRLFIKRGA 226
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 17-279 3.76e-22

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 101.58  E-value: 3.76e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594   17 AARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRG---------------------SSVDSATK- 74
Cdd:PHA02874    42 AIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGvdtsilpipciekdmiktildCGIDVNIKd 121

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594   75 -KGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPlavalqqg 153
Cdd:PHA02874   122 aELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESP-------- 193

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  154 hnqavaillendtkgkvrlpaLHIAARKDDTKSAALLLQNDHNADVQSKSGFTPLHIAAHYgNVNVATLLLNrGAAVDFT 233
Cdd:PHA02874   194 ---------------------LHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIH-NRSAIELLIN-NASINDQ 250

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1887789594  234 ARNGITPLHVA-SKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAAR 279
Cdd:PHA02874   251 DIDGSTPLHHAiNPPCDIDIIDILLYHKADISIKDNKGENPIDTAFK 297
Ank_2 pfam12796
Ankyrin repeats (3 copies);
274-365 5.99e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 91.72  E-value: 5.99e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  274 LHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLLQHKAPvdDVTLDYLTALHVAAHCGHYRVTK 353
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 1887789594  354 LLLDKRANPNAR 365
Cdd:pfam12796   79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
406-496 7.79e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 91.33  E-value: 7.79e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  406 IHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNgalVDARAREE-QTPLHIASRLGKTEIV 484
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNgRTALHYAARSGHLEIV 77

                           90
                   ....*....|..
gi 1887789594  485 QLLLQHMAHPDA 496
Cdd:pfam12796   78 KLLLEKGADINV 89
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 471-744 8.29e-22

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 101.11  E-value: 8.29e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  471 PLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKkgFTPLHVAAKYGSLDVA 550
Cdd:PHA02878    40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFYT--LVAIKDAFNNRNVEIF 117

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  551 KLLLQRRAAADSAGKNGYTPLHIAAKKNQMQIASTLLNYGAETNIVTK-QGVTPLHLASQEGHTDMVTLLLDKGANIHMS 629
Cdd:PHA02878   118 KIILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIP 197

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  630 TKSGLTSLHLAAQEDKVNVADILTKHGADQDAHTKLGYTPLIVACHY-GNVKMVNFLLKQGANVNAK-TKNGYTPLHQAA 707
Cdd:PHA02878   198 DKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKsYILGLTALHSSI 277

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1887789594  708 QQghTHIINVLLQHGAKPNATTANGNTALAIA--KRLGY 744
Cdd:PHA02878   278 KS--ERKLKLLLEYGADINSLNSYKLTPLSSAvkQYLCI 314
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 601-751 1.17e-21

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 99.74  E-value: 1.17e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  601 VTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQE-----DKVNVADILTKHGADQDAHTKLGYTPLIVA-- 673
Cdd:PHA03100    36 VLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIkynltDVKEIVKLLLEYGANVNAPDNNGITPLLYAis 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  674 CHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGH--THIINVLLQHGAKPNATT----------------ANGNTA 735
Cdd:PHA03100   116 KKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKNrvnyllsygvpinikdVYGFTP 195

                          170
                   ....*....|....*.
gi 1887789594  736 LAIAKRLGYISVVDTL 751
Cdd:PHA03100   196 LHYAVYNNNPEFVKYL 211
Ank_2 pfam12796
Ankyrin repeats (3 copies);
241-327 1.20e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.95  E-value: 1.20e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  241 LHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAplLARTKNGLSPLHMAAQGDHVECVK 320
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78


                   ....*..
gi 1887789594  321 HLLQHKA 327
Cdd:pfam12796   79 LLLEKGA 85
Ank_2 pfam12796
Ankyrin repeats (3 copies);
307-397 1.42e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.56  E-value: 1.42e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  307 LHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKrANPNARaLNGFTPLHIACKKNRIKVME 386
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLK-DNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|.
gi 1887789594  387 LLVKYGASIQA 397
Cdd:pfam12796   79 LLLEKGADINV 89
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 86-462 1.87e-21

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 99.65  E-value: 1.87e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594   86 AGQAEVVKVLVKEGAN-INAQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHNQAVAILLEN 164
Cdd:PHA02874    11 SGDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDN 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  165 DTKGKVrLPALHIaaRKDDTKSaalllqndhnadvqsksgftplhiaahygnvnvatlLLNRGAAVDFTARNGITPLHVA 244
Cdd:PHA02874    91 GVDTSI-LPIPCI--EKDMIKT------------------------------------ILDCGIDVNIKDAELKTFLHYA 131

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  245 SKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLLQ 324
Cdd:PHA02874   132 IKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLID 211

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  325 HKApvddvtldyltalHVAAHCGhyrvtkllldkranpnaralNGFTPLHIACKKNRiKVMELLVKyGASIQAITESGLT 404
Cdd:PHA02874   212 HGN-------------HIMNKCK--------------------NGFTPLHNAIIHNR-SAIELLIN-NASINDQDIDGST 256

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  405 PIHVA-AFMGHLNIVLLLLQNGASPDVTNIRGETALHMAAR-AGQVEVVRCLLRNGALVD 462
Cdd:PHA02874   257 PLHHAiNPPCDIDIIDILLYHKADISIKDNKGENPIDTAFKyINKDPVIKDIIANAVLIK 316
Death pfam00531
Death domain;
1390-1470 2.48e-21

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 89.73  E-value: 2.48e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594 1390 EERLAYIADH---LGFSWTELARELDFTEEQIHQIRIENPNsLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIV 1466
Cdd:pfam00531    1 RKQLDRLLDPpppLGKDWRELARKLGLSENEIDEIESENPR-LRSQTYELLRLWEQREGKNATVGTLLEALRKLGRRDAA 79


                   ....
gi 1887789594 1467 HLME 1470
Cdd:pfam00531   80 EKIQ 83
Ank_2 pfam12796
Ankyrin repeats (3 copies);
637-728 3.29e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.79  E-value: 3.29e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  637 LHLAAQEDKVNVADILTKHGADQDAHTKLGYTPLIVACHYGNVKMVNFLLKQgANVNAKTkNGYTPLHQAAQQGHTHIIN 716
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 1887789594  717 VLLQHGAKPNAT 728
Cdd:pfam12796   79 LLLEKGADINVK 90
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 474-739 7.48e-21

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 99.37  E-value: 7.48e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  474 IASRLGKTE--IVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAK 551
Cdd:PHA02876   149 IKERIQQDEllIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIK 228

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  552 LLLQRRAaadSAGKNGYTPLHiAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGH-TDMVTLLLDKGANIHMST 630
Cdd:PHA02876   229 AIIDNRS---NINKNDLSLLK-AIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKN 304

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  631 KSGLTSLHLAAQE--DKVNVADILTKhGADQDAHTKLGYTPLIVACHYGNVK-MVNFLLKQGANVNAKTKNGYTPLHQAA 707
Cdd:PHA02876   305 IKGETPLYLMAKNgyDTENIRTLIML-GADVNAADRLYITPLHQASTLDRNKdIVITLLELGANVNARDYCDKTPIHYAA 383

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1887789594  708 QQGHTHIINVLLQHGAKPNATTANGNTALAIA 739
Cdd:PHA02876   384 VRNNVVIINTLLDYGADIEALSQKIGTALHFA 415
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 306-577 8.01e-21

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 98.03  E-value: 8.01e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  306 PLHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLdkrANPNARAL-NGFTPLHIACKKNRIKV 384
Cdd:PHA02878    40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMI---RSINKCSVfYTLVAIKDAFNNRNVEI 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  385 ME-LLVKYGASIQAITESGLTPIHVAAFMgHLNIVLLLLQNGASPD-VTNIRGETALHMAARAGQVEVVRCLLRNGALVD 462
Cdd:PHA02878   117 FKiILTNRYKNIQTIDLVYIDKKSKDDII-EAEITKLLLSYGADINmKDRHKGNTALHYATENKDQRLTELLLSYGANVN 195

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  463 ARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHIS-AREGQVDVASVLLEAGAA-HSLATKKGFTPLHV 540
Cdd:PHA02878   196 IPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDvNAKSYILGLTALHS 275

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1887789594  541 AAKygSLDVAKLLLQRRAAADSAGKNGYTPLHIAAKK 577
Cdd:PHA02878   276 SIK--SERKLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
Ank_2 pfam12796
Ankyrin repeats (3 copies);
175-266 9.68e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 88.25  E-value: 9.68e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  175 LHIAARKDDTKSAALLLQNDHNADVQSKSGFTPLHIAAHYGNVNVATLLLNRGAAVDFTarNGITPLHVASKRGNTNMVK 254
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD--NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 1887789594  255 LLLDRGGQIDAK 266
Cdd:pfam12796   79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
80-167 1.09e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 88.25  E-value: 1.09e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594   80 LHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENgaNQSTATEDGFTPLAVALQQGHNQAVA 159
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH--ADVNLKDNGRTALHYAARSGHLEIVK 78


                   ....*...
gi 1887789594  160 ILLENDTK 167
Cdd:pfam12796   79 LLLEKGAD 86
Ank_2 pfam12796
Ankyrin repeats (3 copies);
472-558 5.31e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.32  E-value: 5.31e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  472 LHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEagAAHSLATKKGFTPLHVAAKYGSLDVAK 551
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE--HADVNLKDNGRTALHYAARSGHLEIVK 78


                   ....*..
gi 1887789594  552 LLLQRRA 558
Cdd:pfam12796   79 LLLEKGA 85
Ank_2 pfam12796
Ankyrin repeats (3 copies);
604-695 6.09e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.94  E-value: 6.09e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  604 LHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADILTKHgADQDAHTKlGYTPLIVACHYGNVKMVN 683
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 1887789594  684 FLLKQGANVNAK 695
Cdd:pfam12796   79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
14-105 1.24e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.17  E-value: 1.24e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594   14 FLRAARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSvdSATKKGNTALHIASLAGQAEVVK 93
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 1887789594   94 VLVKEGANINAQ 105
Cdd:pfam12796   79 LLLEKGADINVK 90
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 21-260 2.32e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 92.75  E-value: 2.32e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594   21 GNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGA 100
Cdd:PHA02875    13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  101 NIN-AQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPlavalqqghnqavaillendtkgkvrlpaLHIAA 179
Cdd:PHA02875    93 FADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSP-----------------------------LHLAV 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  180 RKDDTKSAALLLQNDHNADVQSKSGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNG-ITPLHVASKRGNTNMVKLLLD 258
Cdd:PHA02875   144 MMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIK 223


                   ..
gi 1887789594  259 RG 260
Cdd:PHA02875   224 RG 225
Ank_2 pfam12796
Ankyrin repeats (3 copies);
373-464 4.26e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 83.63  E-value: 4.26e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  373 LHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNirGETALHMAARAGQVEVVR 452
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN--GRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 1887789594  453 CLLRNGALVDAR 464
Cdd:pfam12796   79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
505-595 5.82e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 83.24  E-value: 5.82e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  505 LHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAgkNGYTPLHIAAKKNQMQIAS 584
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD--NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|.
gi 1887789594  585 TLLNYGAETNI 595
Cdd:pfam12796   79 LLLEKGADINV 89
Death cd01670
Death Domain: a protein-protein interaction domain; Death Domains (DDs) are protein-protein ...
 1393-1470 1.02e-18

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


Pssm-ID: 260017 [Multi-domain]  Cd Length: 79  Bit Score: 82.33  E-value: 1.02e-18
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1887789594 1393 LAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIVHLME 1470
Cdd:cd01670      2 FDLVAEELGRDWKKLARKLGLSEGDIDQIEEDNRDDLKEQAYQMLERWREREGDEATLGRLIQALREIGRRDLAEKLE 79
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 439-700 2.97e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 86.86  E-value: 2.97e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  439 LHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIA----SRLGKTEIVQLLLQ------HMAHPDAATTNG------- 501
Cdd:PHA02878    41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIIckepNKLGMKEMIRSINKcsvfytLVAIKDAFNNRNveifkii 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  502 --------YTPLHISAREGQVD------VASVLLEAGAAHSLATK-KGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKN 566
Cdd:PHA02878   121 ltnrykniQTIDLVYIDKKSKDdiieaeITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKT 200

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  567 GYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQE-GHTDMVTLLLDKGANIHM-STKSGLTSLHLAAQ-E 643
Cdd:PHA02878   201 NNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAkSYILGLTALHSSIKsE 280

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1887789594  644 DKVNvadILTKHGADQDAHTKLGYTPLIVAC------HYGNVKMVNFLLKQGANVNAKTKNGY 700
Cdd:PHA02878   281 RKLK---LLLEYGADINSLNSYKLTPLSSAVkqylciNIGRILISNICLLKRIKPDIKNSEGF 340
Ank_2 pfam12796
Ankyrin repeats (3 copies);
670-751 3.50e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.23  E-value: 3.50e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  670 LIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHgAKPNATTaNGNTALAIAKRLGYISVVD 749
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78


                   ..
gi 1887789594  750 TL 751
Cdd:pfam12796   79 LL 80
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 371-557 3.57e-15

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 81.21  E-value: 3.57e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  371 TPLHIACKKNRIKVMELLVKY-GASIQAITESGLTPIHVAAFMGHLNIVLLLLQngASPDVTNI-------RGETALHMA 442
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNEpmtsdlyQGETALHIA 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  443 ARAGQVEVVRCLLRNGA-LVDARA-----REEQT--------PLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHIS 508
Cdd:cd22192     97 VVNQNLNLVRELIARGAdVVSPRAtgtffRPGPKnliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHIL 176

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1887789594  509 AREGQVDVA----SVLLEA---GAAHSLAT---KKGFTPLHVAAKYGSLDVAKLLLQRR 557
Cdd:cd22192    177 VLQPNKTFAcqmyDLILSYdkeDDLQPLDLvpnNQGLTPFKLAAKEGNIVMFQHLVQKR 235
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 175-390 4.47e-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: 80.83  E-value: 4.47e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  175 LHIAARKDDTKSAALLLQNDHnADVQSKS--GFTPLHIAAHYGNVNVATLLL-------NRGAAVDFTArnGITPLHVAS 245
Cdd:cd22192     21 LLLAAKENDVQAIKKLLKCPS-CDLFQRGalGETALHVAALYDNLEAAVVLMeaapelvNEPMTSDLYQ--GETALHIAV 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  246 KRGNTNMVKLLLDRGGQIDA---------KTRDGLT-----PLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMAA 311
Cdd:cd22192     98 VNQNLNLVRELIARGADVVSpratgtffrPGPKNLIyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILV 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  312 QGDHVECVKH----LLQHKAPVDDVTLDYLtalhvaahcghyrvtkllldkranPNARalnGFTPLHIACKKNRIKVMEL 387
Cdd:cd22192    178 LQPNKTFACQmydlILSYDKEDDLQPLDLV------------------------PNNQ---GLTPFKLAAKEGNIVMFQH 230


                   ...
gi 1887789594  388 LVK 390
Cdd:cd22192    231 LVQ 233
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 144-326 9.20e-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: 9.20e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  144 TPLAVALQQGHNQAVAILLENDT-----KGKVRLPALHIAARKDDTKSAALLLQNDH---NADVQSK--SGFTPLHIAAH 213
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLLKCPScdlfqRGALGETALHVAALYDNLEAAVVLMEAAPelvNEPMTSDlyQGETALHIAVV 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  214 YGNVNVATLLLNRGAAVdFTARN---------------GITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHC-- 276
Cdd:cd22192     99 NQNLNLVRELIARGADV-VSPRAtgtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHIlv 177

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1887789594  277 --AARSGHDQVVELLL-----ERGAPL-LARTKNGLSPLHMAAQGDHVECVKHLLQHK 326
Cdd:cd22192    178 lqPNKTFACQMYDLILsydkeDDLQPLdLVPNNQGLTPFKLAAKEGNIVMFQHLVQKR 235
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 578-751 1.80e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 77.72  E-value: 1.80e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  578 NQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADILTKHGA 657
Cdd:PHA02875    13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  658 -DQDAHTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTAL 736
Cdd:PHA02875    93 fADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPL 172

                          170
                   ....*....|....*
gi 1887789594  737 AIAKRLGYISVVDTL 751
Cdd:PHA02875   173 IIAMAKGDIAICKML 187
PHA02798 PHA02798
ankyrin-like protein; Provisional
 448-729 4.05e-14

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 77.18  E-value: 4.05e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  448 VEVVRCLLRNGALVDARAREEQTPL-----HIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQV---DVASV 519
Cdd:PHA02798    51 TDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYInnlEILLF 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  520 LLEAGAAHSLATKKGFTPLHVAAKYG---SLDVAKLLLQRRAAADS-AGKNGYTPLHIAAKKNQMQIastllnygaetni 595
Cdd:PHA02798   131 MIENGADTTLLDKDGFTMLQVYLQSNhhiDIEIIKLLLEKGVDINThNNKEKYDTLHCYFKYNIDRI------------- 197

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  596 vtkqgvtplhlasqegHTDMVTLLLDKGANIHMSTKSG-------LTSLHLAAQEDKVNVADILTKHgADQDAHTKLGYT 668
Cdd:PHA02798   198 ----------------DADILKLFVDNGFIINKENKSHkkkfmeyLNSLLYDNKRFKKNILDFIFSY-IDINQVDELGFN 260

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1887789594  669 PLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHgaKPNATT 729
Cdd:PHA02798   261 PLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNK--KPNKNT 319
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 535-752 4.73e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 76.84  E-value: 4.73e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  535 FTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGYTPLHIAAKKNQMQIASTLLNygaetnIVTKQGVTPLHLASQEG-HT 613
Cdd:PHA02878    38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIR------SINKCSVFYTLVAIKDAfNN 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  614 DMV----TLLLDKGANIHmstKSGLTSLHLAAQEDKVN--VADILTKHGADQDAHTK-LGYTPLIVACHYGNVKMVNFLL 686
Cdd:PHA02878   112 RNVeifkIILTNRYKNIQ---TIDLVYIDKKSKDDIIEaeITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLL 188

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1887789594  687 KQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTALAIAkrLGYISVVDTLK 752
Cdd:PHA02878   189 SYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIS--VGYCKDYDILK 252
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 528-723 1.29e-13

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 76.45  E-value: 1.29e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  528 SLATKKGFTPLHVAAKygSLDVAKLLlqrraaADSAGKNGytplHIAAKKNQMQIAST--------LLNYGAETNIVTKQ 599
Cdd:PLN03192   490 NVVILKNFLQHHKELH--DLNVGDLL------GDNGGEHD----DPNMASNLLTVASTgnaalleeLLKAKLDPDIGDSK 557

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  600 GVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADILTKHGADQDAHTklGYTPLIVACHYGNV 679
Cdd:PLN03192   558 GRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHA--AGDLLCTAAKRNDL 635

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1887789594  680 KMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGA 723
Cdd:PLN03192   636 TAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGA 679
Ank_4 pfam13637
Ankyrin repeats (many copies);
402-455 2.40e-13

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 66.14  E-value: 2.40e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1887789594  402 GLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLL 455
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 503-687 4.32e-13

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: 74.28  E-value: 4.32e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  503 TPLHISAREGQVDVASVLLEAGAAHSLATKK-GFTPLHVAAKYGSLDVAKLLLqrRAAAD-------SAGKNGYTPLHIA 574
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGAlGETALHVAALYDNLEAAVVLM--EAAPElvnepmtSDLYQGETALHIA 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  575 AKKNQMQIASTLLNYGAEtniVTKQGVT-----------------PLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSL 637
Cdd:cd22192     97 VVNQNLNLVRELIARGAD---VVSPRATgtffrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  638 H-LAAQEDKV---NVADILTKHGADQDAHT------KLGYTPLIVACHYGNVKMVNFLLK 687
Cdd:cd22192    174 HiLVLQPNKTfacQMYDLILSYDKEDDLQPldlvpnNQGLTPFKLAAKEGNIVMFQHLVQ 233
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 262-510 1.17e-12

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 73.19  E-value: 1.17e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  262 QIDAKTRDGLTPLHCAA-RSGHDQVVELLLERGAplLARTknGLSPLHMAAQGdHVECVKHLLQH--KAPVDDVTLDYL- 337
Cdd:TIGR00870   44 NINCPDRLGRSALFVAAiENENLELTELLLNLSC--RGAV--GDTLLHAISLE-YVDAVEAILLHllAAFRKSGPLELAn 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  338 -----------TALHVAAHCGHYRVTKLLLDKRANPNARALNGFtplhiaCKKnriKVMELLVKYGASiqaitesgltPI 406
Cdd:TIGR00870  119 dqytseftpgiTALHLAAHRQNYEIVKLLLERGASVPARACGDF------FVK---SQGVDSFYHGES----------PL 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  407 HVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAA----RAGQVEVVRCLLRNGAL-VDARAREEQ-----------T 470
Cdd:TIGR00870  180 NAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVmeneFKAEYEELSCQMYNFALsLLDKLRDSKelevilnhqglT 259

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1887789594  471 PLHIASRLGKTEIVQLLLQ-------HMAHPdaattngYTPLHISAR 510
Cdd:TIGR00870  260 PLKLAAKEGRIVLFRLKLAikykqkkFVAWP-------NGQQLLSLY 299
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 436-622 1.25e-12

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 72.74  E-value: 1.25e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  436 ETALHMAARAGQVEVVRCLLR-NGALVDARAREEQTPLHIASRLGKTEIVQLLLQhmAHPD----AATTN---GYTPLHI 507
Cdd:cd22192     18 ESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPElvnePMTSDlyqGETALHI 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  508 SAREGQVDVASVLLEAGA--AHSLATKKGFT------------PLHVAAKYGSLDVAKLLLQRRA---AADSAGKngyTP 570
Cdd:cd22192     96 AVVNQNLNLVRELIARGAdvVSPRATGTFFRpgpknliyygehPLSFAACVGNEEIVRLLIEHGAdirAQDSLGN---TV 172

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1887789594  571 LHI----AAKKNQMQIASTLLNYGAETNIVT------KQGVTPLHLASQEGHTDMVTLLLDK 622
Cdd:cd22192    173 LHIlvlqPNKTFACQMYDLILSYDKEDDLQPldlvpnNQGLTPFKLAAKEGNIVMFQHLVQK 234
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 296-489 2.98e-12

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 71.58  E-value: 2.98e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  296 LLARTKNGLSPLHMAAQGDHVECVKHLLQHKApVDDVTLDYL--TALHVAAHCGHYRVTKLLLDkranpNARAL------ 367
Cdd:cd22192     10 LLQQKRISESPLLLAAKENDVQAIKKLLKCPS-CDLFQRGALgeTALHVAALYDNLEAAVVLME-----AAPELvnepmt 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  368 ----NGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLT--------------PIHVAAFMGHLNIVLLLLQNGASPD 429
Cdd:cd22192     84 sdlyQGETALHIAVVNQNLNLVRELIARGADVVSPRATGTFfrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIR 163

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1887789594  430 VTNIRGETALHMAARAGQVEVVrCLLRNGAL-VDARAREEQ----------TPLHIASRLGKTEIVQLLLQ 489
Cdd:cd22192    164 AQDSLGNTVLHILVLQPNKTFA-CQMYDLILsYDKEDDLQPldlvpnnqglTPFKLAAKEGNIVMFQHLVQ 233
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 12-146 3.86e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 71.44  E-value: 3.86e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594   12 ASFLRAARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTAL----------- 80
Cdd:PLN03192   527 SNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnaisakhhki 606

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594   81 -----HIASLA---------------GQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTA-T 139
Cdd:PLN03192   607 frilyHFASISdphaagdllctaakrNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAnT 686


                   ....*..
gi 1887789594  140 EDGFTPL 146
Cdd:PLN03192   687 DDDFSPT 693
PHA02798 PHA02798
ankyrin-like protein; Provisional
 543-739 5.31e-12

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 70.25  E-value: 5.31e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  543 KYGS-LDVAKLLLQRRAAADSAGKNGYTPLHIAAKK---NQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHT---DM 615
Cdd:PHA02798    84 DYKHmLDIVKILIENGADINKKNSDGETPLYCLLSNgyiNNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEI 163

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  616 VTLLLDKGANIHM-STKSGLTSLHLAAQED----KVNVADILTKHG---ADQDAHTKLGYTPLIVACHYGNVK----MVN 683
Cdd:PHA02798   164 IKLLLEKGVDINThNNKEKYDTLHCYFKYNidriDADILKLFVDNGfiiNKENKSHKKKFMEYLNSLLYDNKRfkknILD 243

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1887789594  684 FLLKQgANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTALAIA 739
Cdd:PHA02798   244 FIFSY-IDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTA 298
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 526-720 6.61e-12

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 70.43  E-value: 6.61e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  526 AHSLATKKGF-TPLHVAAKYGSLD-VAKLLLQRRAAADSAGKNGYTPLHIAAKKNQMQIASTLLNYGAE--TNIVTK--- 598
Cdd:cd22192      8 LHLLQQKRISeSPLLLAAKENDVQaIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElvNEPMTSdly 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  599 QGVTPLHLASQEGHTDMVTLLLDKGANI----------HMSTKS----GLTSLHLAA---QEDKVNvadILTKHGADQDA 661
Cdd:cd22192     88 QGETALHIAVVNQNLNLVRELIARGADVvspratgtffRPGPKNliyyGEHPLSFAAcvgNEEIVR---LLIEHGADIRA 164

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1887789594  662 HTKLGYTPL---------IVACHygnvkMVNFLLKQGANVNAKT------KNGYTPLHQAAQQGHTHIINVLLQ 720
Cdd:cd22192    165 QDSLGNTVLhilvlqpnkTFACQ-----MYDLILSYDKEDDLQPldlvpnNQGLTPFKLAAKEGNIVMFQHLVQ 233
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 50-164 7.35e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 70.67  E-value: 7.35e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594   50 AAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLY--------------- 114
Cdd:PLN03192   532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWnaisakhhkifrily 611

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1887789594  115 ----------------MAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHNQAVAILLEN 164
Cdd:PLN03192   612 hfasisdphaagdllcTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMN 677
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 75-226 9.67e-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: 9.67e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594   75 KGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGF--------------TPLYMAAQENHIDVVKYLLENGANQSTAte 140
Cdd:cd22194    140 EGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVFfnpkykhegfyfgeTPLALAACTNQPEIVQLLMEKESTDITS-- 217

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  141 dgftplavalqqghnqavailleNDTKGKVRLPALHIAArkDDTKS----------AALLLQNDHNAD-VQSKSGFTPLH 209
Cdd:cd22194    218 -----------------------QDSRGNTVLHALVTVA--EDSKTqndfvkrmydMILLKSENKNLEtIRNNEGLTPLQ 272

                          170
                   ....*....|....*..
gi 1887789594  210 IAAHYGNVNVATLLLNR 226
Cdd:cd22194    273 LAAKMGKAEILKYILSR 289
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 22-162 1.15e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 69.71  E-value: 1.15e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594   22 NLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIAsLAGQAEV--VKVLVKEG 99
Cdd:PHA02876   354 NKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFA-LCGTNPYmsVKTLIDRG 432

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1887789594  100 ANINAQSQNGFTPLYMAAQEN-HIDVVKYLLENGANQSTATEDGFTPLAVALqqGHNQAVAILL 162
Cdd:PHA02876   433 ANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILL 494
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 58-257 1.30e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 69.14  E-value: 1.30e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594   58 LVQELLGRGSSVDSATK-KGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGANQS 136
Cdd:PHA02878   149 ITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTD 228

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  137 TATEDGFTPLAVALQQGHNQAV-AILLEndtkgkvrlpalhiaarkddtksaalllqndHNADVQSKS---GFTPLHIAA 212
Cdd:PHA02878   229 ARDKCGNTPLHISVGYCKDYDIlKLLLE-------------------------------HGVDVNAKSyilGLTALHSSI 277

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1887789594  213 HygNVNVATLLLNRGAAVDFTARNGITPLHVASK-RGNTNMVKLLL 257
Cdd:PHA02878   278 K--SERKLKLLLEYGADINSLNSYKLTPLSSAVKqYLCINIGRILI 321
Ank_4 pfam13637
Ankyrin repeats (many copies);
270-323 2.41e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 60.37  E-value: 2.41e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1887789594  270 GLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLL 323
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 25-433 4.70e-11

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 68.01  E-value: 4.70e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594   25 KVVEYL--KGGIDIN-TCNQNGLNALHlaakeghvglvqellgrgssvdsaTKKGNTALHIaslagqaEVVKVLVKEGAN 101
Cdd:PHA02716   156 DLIKYMvdVGIVNLNyVCKKTGYGILH------------------------AYLGNMYVDI-------DILEWLCNNGVN 204

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  102 INAQSQNGFTPL--YMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHN---QAVAILLENDTKGKVR-LPA- 174
Cdd:PHA02716   205 VNLQNNHLITPLhtYLITGNVCASVIKKIIELGGDMDMKCVNGMSPIMTYIINIDNinpEITNIYIESLDGNKVKnIPMi 284

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  175 LHI---AARKDDTKSAALLLQNDHNADVQSKSGFTPLH--IAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRG- 248
Cdd:PHA02716   285 LHSyitLARNIDISVVYSFLQPGVKLHYKDSAGRTCLHqyILRHNISTDIIKLLHEYGNDLNEPDNIGNTVLHTYLSMLs 364

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  249 -------------NTNMVKLLLDRGGQIDAKTRDGLTPLH---CAARS--GHDQVVELLLERgapLLARTKNGLSPLHMA 310
Cdd:PHA02716   365 vvnildpetdndiRLDVIQCLISLGADITAVNCLGYTPLTsyiCTAQNymYYDIIDCLISDK---VLNMVKHRILQDLLI 441

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  311 AQGDHVECVKHLL-QHKAPVDDVTLDY----LTALHVAAHCGhyrvtkllLDKRANPNARALNGFTPLHIA-CKKNRIKV 384
Cdd:PHA02716   442 RVDDTPCIIHHIIaKYNIPTDLYTDEYepydSTKIHDVYHCA--------IIERYNNAVCETSGMTPLHVSiISHTNANI 513

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1887789594  385 MELLVKY----GASIQAITESGLTPIHVA----AFMGH-LNIVLLLLQNgaSPDVTNI 433
Cdd:PHA02716   514 VMDSFVYllsiQYNINIPTKNGVTPLMLTmrnnRLSGHqWYIVKNILDK--RPNVDIV 569
Ank_4 pfam13637
Ankyrin repeats (many copies);
239-290 4.88e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.60  E-value: 4.88e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1887789594  239 TPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLL 290
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
303-356 6.94e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.21  E-value: 6.94e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1887789594  303 GLSPLHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLL 356
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02798 PHA02798
ankyrin-like protein; Provisional
 25-277 6.97e-11

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 66.78  E-value: 6.97e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594   25 KVVEYLKGGIDIN-TCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTAL-----HIASLAGQAEVVKVLVKE 98
Cdd:PHA02798    19 STVKLLIKSCNPNeIVNEYSIFQKYLQRDSPSTDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIEN 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594   99 GANINAQSQNGFTPLYMAAQE---NHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHN---QAVAILLE-----NDTK 167
Cdd:PHA02798    99 GADINKKNSDGETPLYCLLSNgyiNNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEkgvdiNTHN 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  168 GKVRLPALHIAARKD----DTKSAALLLQND---HNADVQSKSGFTPLHIAAHYGNVNVATLLLNR-GAAVDFTARN--G 237
Cdd:PHA02798   179 NKEKYDTLHCYFKYNidriDADILKLFVDNGfiiNKENKSHKKKFMEYLNSLLYDNKRFKKNILDFiFSYIDINQVDelG 258

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1887789594  238 ITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCA 277
Cdd:PHA02798   259 FNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTA 298
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 17-163 9.63e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 66.17  E-value: 9.63e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594   17 AARAGNLDKVVEYLKGGIDIN-TCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVL 95
Cdd:PHA02875    75 AVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELL 154

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1887789594   96 VKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTATEDG-FTPLAVALQQGHNQAVAILLE 163
Cdd:PHA02875   155 IDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIK 223
Ank_4 pfam13637
Ankyrin repeats (many copies);
371-422 1.02e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.44  E-value: 1.02e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1887789594  371 TPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLL 422
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
76-129 1.17e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.44  E-value: 1.17e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1887789594   76 GNTALHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLL 129
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
666-719 1.22e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.44  E-value: 1.22e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1887789594  666 GYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLL 719
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
336-389 1.32e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.05  E-value: 1.32e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1887789594  336 YLTALHVAAHCGHYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLV 389
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 432-556 1.73e-10

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 65.94  E-value: 1.73e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  432 NIRGETALHMAARAGQVEVVRCLLRNGALVDARA---------REE-----QTPLHIASRLGKTEIVQLLLQHMAHPDAA 497
Cdd:cd22194    138 AYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAkgvffnpkyKHEgfyfgETPLALAACTNQPEIVQLLMEKESTDITS 217

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1887789594  498 T-TNGYTPLH---ISAREGQVDVASV------LLEAGAAHSLAT---KKGFTPLHVAAKYGSLDVAKLLLQR 556
Cdd:cd22194    218 QdSRGNTVLHalvTVAEDSKTQNDFVkrmydmILLKSENKNLETirnNEGLTPLQLAAKMGKAEILKYILSR 289
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 33-163 2.16e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 65.29  E-value: 2.16e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594   33 GIDINTCNQNGLN-ALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGFT 111
Cdd:PHA02878   157 GADINMKDRHKGNtALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNT 236

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1887789594  112 PLYMAAQE-NHIDVVKYLLENGAN-QSTATEDGFTPLAVALQQghNQAVAILLE 163
Cdd:PHA02878   237 PLHISVGYcKDYDILKLLLEHGVDvNAKSYILGLTALHSSIKS--ERKLKLLLE 288
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 312-538 2.27e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 65.66  E-value: 2.27e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  312 QGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHcghyrvtkllldkrANPNAralnGFTPLHIACKKNRiKVMELLVKY 391
Cdd:PLN03192   487 QEDNVVILKNFLQHHKELHDLNVGDLLGDNGGEH--------------DDPNM----ASNLLTVASTGNA-ALLEELLKA 547

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  392 GASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQtp 471
Cdd:PLN03192   548 KLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAGDL-- 625

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1887789594  472 LHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLA-TKKGFTPL 538
Cdd:PLN03192   626 LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAnTDDDFSPT 693
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 420-501 7.93e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 63.76  E-value: 7.93e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  420 LLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATT 499
Cdd:PTZ00322   100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGA 179


                   ..
gi 1887789594  500 NG 501
Cdd:PTZ00322   180 NA 181
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 358-557 8.46e-10

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 63.95  E-value: 8.46e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  358 KRANPNARALN-------GFTPLHIACKKNRIK-VMELLVKYGASIqaitESGLTPIHVAAFMGHLN---IVLLLLQNGA 426
Cdd:TIGR00870   34 YRDLEEPKKLNincpdrlGRSALFVAAIENENLeLTELLLNLSCRG----AVGDTLLHAISLEYVDAveaILLHLLAAFR 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  427 SPDVTNI----------RGETALHMAARAGQVEVVRCLLRNGALVDARA--------------REEQTPLHIASRLGKTE 482
Cdd:TIGR00870  110 KSGPLELandqytseftPGITALHLAAHRQNYEIVKLLLERGASVPARAcgdffvksqgvdsfYHGESPLNAAACLGSPS 189

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  483 IVQLLLQHMAHPDAATTNGYTPLHISAREG-----------QVDVASVLLEAGAAHSLATK-----KGFTPLHVAAKYGS 546
Cdd:TIGR00870  190 IVALLSEDPADILTADSLGNTLLHLLVMENefkaeyeelscQMYNFALSLLDKLRDSKELEvilnhQGLTPLKLAAKEGR 269

                          250
                   ....*....|.
gi 1887789594  547 LDVAKLLLQRR 557
Cdd:TIGR00870  270 IVLFRLKLAIK 280
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 409-563 9.22e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 63.73  E-value: 9.22e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  409 AAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQlLL 488
Cdd:PLN03192   532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR-IL 610

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1887789594  489 QHMAHPDAATTNGyTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSA 563
Cdd:PLN03192   611 YHFASISDPHAAG-DLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKA 684
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 479-567 1.32e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 62.99  E-value: 1.32e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  479 GKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRA 558
Cdd:PTZ00322    93 GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQ 172


                   ....*....
gi 1887789594  559 AADSAGKNG 567
Cdd:PTZ00322   173 CHFELGANA 181
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 104-389 1.91e-09

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 62.79  E-value: 1.91e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  104 AQSQNGFTPlymAAQENHIDVVKYLLENGA--NQSTATEDGFTPLAVALQQGHNQAVAILLEN-DTKGKVRLPALHIAAR 180
Cdd:TIGR00870   15 SDEEKAFLP---AAERGDLASVYRDLEEPKklNINCPDRLGRSALFVAAIENENLELTELLLNlSCRGAVGDTLLHAISL 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  181 --------------KDDTKSAALLLQNDHNADVQSKsGFTPLHIAAHYGNVNVATLLLNRGAAVDFTArNGitplhVASK 246
Cdd:TIGR00870   92 eyvdaveaillhllAAFRKSGPLELANDQYTSEFTP-GITALHLAAHRQNYEIVKLLLERGASVPARA-CG-----DFFV 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  247 RgnTNMVKLLldrggqidaktRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMAAqgdhvecvkhlLQHK 326
Cdd:TIGR00870  165 K--SQGVDSF-----------YHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLV-----------MENE 220

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1887789594  327 APVDDVTLD---YLTALHVAAHCGHYRVTKLLLDkranpnaraLNGFTPLHIACKKNRIKVMELLV 389
Cdd:TIGR00870  221 FKAEYEELScqmYNFALSLLDKLRDSKELEVILN---------HQGLTPLKLAAKEGRIVLFRLKL 277
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 9-139 2.08e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.93  E-value: 2.08e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594    9 DSNASFLRAARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQ 88
Cdd:PHA02875   101 DGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGD 180

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1887789594   89 AEVVKVLVKEGANINAQSQNG-FTPLYMAAQENHIDVVKYLLENGANQSTAT 139
Cdd:PHA02875   181 IAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNIMF 232
Ank_4 pfam13637
Ankyrin repeats (many copies);
567-620 3.00e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.59  E-value: 3.00e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1887789594  567 GYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLL 620
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
171-224 3.12e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.20  E-value: 3.12e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1887789594  171 RLPALHIAARKDDTKSAALLLQNDHNADVQSKSGFTPLHIAAHYGNVNVATLLL 224
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 602-738 3.44e-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: 3.44e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  602 TPLHLASQEGHTDMV-TLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADILTkhgadqDAHTKL-----------GYTP 669
Cdd:cd22192     19 SPLLLAAKENDVQAIkKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLM------EAAPELvnepmtsdlyqGETA 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  670 LIVACHYGNVKMVNFLLKQGANVNAKTKNGYT--------------PLHQAAQQGHTHIINVLLQHGAKPNATTANGNTA 735
Cdd:cd22192     93 LHIAVVNQNLNLVRELIARGADVVSPRATGTFfrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTV 172


                   ...
gi 1887789594  736 LAI 738
Cdd:cd22192    173 LHI 175
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 400-556 3.86e-09

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 61.43  E-value: 3.86e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  400 ESGLTPIHVAAF---MGHLNIVLLLLQngASPDVTNIR-------------GETALHMAARAGQVEVVRCLLRNGALVDA 463
Cdd:cd21882     24 ATGKTCLHKAALnlnDGVNEAIMLLLE--AAPDSGNPKelvnapctdefyqGQTALHIAIENRNLNLVRLLVENGADVSA 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  464 RA-----REEQT--------PLHIASRLGKTEIVQLLLQHMAHPDAATTN---GYTPLHI------SAREGQVDVASV-- 519
Cdd:cd21882    102 RAtgrffRKSPGnlfyfgelPLSLAACTNQEEIVRLLLENGAQPAALEAQdslGNTVLHAlvlqadNTPENSAFVCQMyn 181

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1887789594  520 -LLEAGAA-------HSLATKKGFTPLHVAAKYGSLDVAKLLLQR 556
Cdd:cd21882    182 lLLSYGAHldptqqlEEIPNHQGLTPLKLAAVEGKIVMFQHILQR 226
Ank_4 pfam13637
Ankyrin repeats (many copies);
206-257 4.18e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.82  E-value: 4.18e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1887789594  206 TPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLL 257
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
43-96 6.56e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.43  E-value: 6.56e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1887789594   43 GLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLV 96
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 43-153 6.88e-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: 6.88e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594   43 GLNALHLAAKEGHVGLVQELLGRGSSVDS--AT----KKGNTAL-----HIASLA---GQAEVVKVLVKEGANINAQSQN 108
Cdd:cd22192     89 GETALHIAVVNQNLNLVRELIARGADVVSprATgtffRPGPKNLiyygeHPLSFAacvGNEEIVRLLIEHGADIRAQDSL 168

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1887789594  109 GFTPLYM-AAQENH------IDVVKYLLENGANQSTAT---EDGFTPLAVALQQG 153
Cdd:cd22192    169 GNTVLHIlVLQPNKtfacqmYDLILSYDKEDDLQPLDLvpnNQGLTPFKLAAKEG 223
Ank_4 pfam13637
Ankyrin repeats (many copies);
536-587 8.80e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.05  E-value: 8.80e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1887789594  536 TPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGYTPLHIAAKKNQMQIASTLL 587
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 434-556 8.92e-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: 8.92e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  434 RGETALHMAARAGQVEVVRCLLRNGALVDARAREE--------------QTPLHIASRLGKTEIVQLLLQHMAHP---DA 496
Cdd:cd22196     93 KGQTALHIAIERRNMHLVELLVQNGADVHARASGEffkkkkggpgfyfgELPLSLAACTNQLDIVKFLLENPHSPadiSA 172

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1887789594  497 ATTNGYTPLHI---SAREGQVDVASV------LLEAGAA-------HSLATKKGFTPLHVAAKYGSLDVAKLLLQR 556
Cdd:cd22196    173 RDSMGNTVLHAlveVADNTPENTKFVtkmyneILILGAKirpllklEEITNKKGLTPLKLAAKTGKIGIFAYILGR 248
Ank_4 pfam13637
Ankyrin repeats (many copies);
470-521 1.11e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.66  E-value: 1.11e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1887789594  470 TPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLL 521
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 338-508 1.18e-08

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 59.89  E-value: 1.18e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  338 TALHVAA---HCGHYRVTKLLLD---KRANP----NARALN----GFTPLHIACKKNRIKVMELLVKYGASIQAITES-- 401
Cdd:cd21882     28 TCLHKAAlnlNDGVNEAIMLLLEaapDSGNPkelvNAPCTDefyqGQTALHIAIENRNLNLVRLLVENGADVSARATGrf 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  402 -----------GLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIR---GETALH----MAARAGQVEVVRCLLRNGALV-D 462
Cdd:cd21882    108 frkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPAALEAQdslGNTVLHalvlQADNTPENSAFVCQMYNLLLSyG 187

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1887789594  463 ARAREEQ-----------TPLHIASRLGKTEIVQLLLQHMAHPDAA------TTNGYTPLHIS 508
Cdd:cd21882    188 AHLDPTQqleeipnhqglTPLKLAAVEGKIVMFQHILQREFSGPYQplsrkfTEWTYGPVTSS 250
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 440-528 1.55e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 59.53  E-value: 1.55e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  440 HMAArAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASV 519
Cdd:PTZ00322    88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                   ....*....
gi 1887789594  520 LLEAGAAHS 528
Cdd:PTZ00322   167 LSRHSQCHF 175
Ank_5 pfam13857
Ankyrin repeats (many copies);
222-277 1.56e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 52.35  E-value: 1.56e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1887789594  222 LLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCA 277
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Death_FADD cd08306
Fas-associated Death Domain protein-protein interaction domain; Death domain (DD) found in ...
 1396-1466 1.66e-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: 1.66e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1887789594 1396 IADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKInRMDIV 1466
Cdd:cd08306      8 ICENLGRDWRQLARKLGLSETKIESISEAHPRNLREQVRQSLREWKKIKKAEATVADLIKALRDC-QLNLV 77
PHA02946 PHA02946
ankyin-like protein; Provisional
 58-331 2.30e-08

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 58.53  E-value: 2.30e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594   58 LVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLYM--AAQENHIDVVKYLLENGAN- 134
Cdd:PHA02946    54 FVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYlsGTDDEVIERINLLVQYGAKi 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  135 QSTATEDGFTPLAVAL---QQGHNQAVAILLENDTKGKVRLPALHIAARKDDTKSAAL--LLQNDHNADVQSKSGFTPLH 209
Cdd:PHA02946   134 NNSVDEEGCGPLLACTdpsERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNPKASTIswMMKLGISPSKPDHDGNTPLH 213

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  210 I--AAHYGNVNVATLLLnrgAAVDFTARN--GITPLHVASKR-GNTNMVKLLLDRGGQIDAKTrdgltpLHCAARSGHDQ 284
Cdd:PHA02946   214 IvcSKTVKNVDIINLLL---PSTDVNKQNkfGDSPLTLLIKTlSPAHLINKLLSTSNVITDQT------VNICIFYDRDD 284

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1887789594  285 VVELLLERGapllarTKNGLSPLHMAAQGDHVECVKHLLQHKAPVDD 331
Cdd:PHA02946   285 VLEIINDKG------KQYDSTDFKMAVEVGSIRCVKYLLDNDIICED 325
Ank_5 pfam13857
Ankyrin repeats (many copies);
520-574 2.42e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 51.96  E-value: 2.42e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1887789594  520 LLEAG-AAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGYTPLHIA 574
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
354-409 3.31e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 51.58  E-value: 3.31e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1887789594  354 LLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVA 409
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 156-290 3.80e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 58.37  E-value: 3.80e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  156 QAVAILLENDTKGKVRLPALHIAARKDDTKSAALLLQNDHNADVQSKSGFTPLHIAAHyGNVNVATLLLNRGAAVDFTAR 235
Cdd:PTZ00322    35 ERMAAIQEEIARIDTHLEALEATENKDATPDHNLTTEEVIDPVVAHMLTVELCQLAAS-GDAVGARILLTGGADPNCRDY 113

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1887789594  236 NGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLL 290
Cdd:PTZ00322   114 DGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 601-732 4.51e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.99  E-value: 4.51e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  601 VTPLHLASQEGHTDMVTLlldkganiHMSTksgLTSLHLAAQEDKVNvADILTKHGADQDAHTKLGYTPLIVACHYGNVK 680
Cdd:PTZ00322    62 ATPDHNLTTEEVIDPVVA--------HMLT---VELCQLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQ 129

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1887789594  681 MVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATTANG 732
Cdd:PTZ00322   130 VVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGANA 181
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 152-373 5.94e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 57.96  E-value: 5.94e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  152 QGHNQAVAILLENDTKGKVRLPALHIAARKDDtksaalllQNDHNADVQSKSGftpLHIAAHYGNVNVATLLLNRGAAVD 231
Cdd:PLN03192   484 QTRQEDNVVILKNFLQHHKELHDLNVGDLLGD--------NGGEHDDPNMASN---LLTVASTGNAALLEELLKAKLDPD 552

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  232 FTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLErgaplLARTKN---GLSPLH 308
Cdd:PLN03192   553 IGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYH-----FASISDphaAGDLLC 627

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1887789594  309 MAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNARAL-NGFTPL 373
Cdd:PLN03192   628 TAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTdDDFSPT 693
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 480-728 5.99e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 57.44  E-value: 5.99e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  480 KTEIVQLLLQHMAHpdaATTNGY--TPLHISAREGQVD------VASVLLEAGAAHSLATKKGFTPLhVAAKYGS----L 547
Cdd:PHA02989    49 KIKIVKLLIDNGAD---VNYKGYieTPLCAVLRNREITsnkikkIVKLLLKFGADINLKTFNGVSPI-VCFIYNSninnC 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  548 DVAKLLLQRRAAADSAgKN--GYTPLHI-----AAKKNQMQIastLLNYGA---ETNIVtkQGVTPLHLASQEG----HT 613
Cdd:PHA02989   125 DMLRFLLSKGINVNDV-KNsrGYNLLHMylesfSVKKDVIKI---LLSFGVnlfEKTSL--YGLTPMNIYLRNDidviSI 198

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  614 DMVTLLLDKGANIHMST---KSGLTSL---HLAAQEDKVNVADILTKHgADQDAHTKLGYTPLIVACHYGNVKMVNFLLK 687
Cdd:PHA02989   199 KVIKYLIKKGVNIETNNngsESVLESFldnNKILSKKEFKVLNFILKY-IKINKKDKKGFNPLLISAKVDNYEAFNYLLK 277

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1887789594  688 QGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQhgAKPNAT 728
Cdd:PHA02989   278 LGDDIYNVSKDGDTVLTYAIKHGNIDMLNRILQ--LKPGKY 316
PHA02791 PHA02791
ankyrin-like protein; Provisional
 197-395 6.11e-08

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 56.20  E-value: 6.11e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  197 ADVQsksGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNgiTPLHVASKRGNTNMVKLLLDRG---GQIDAKtrdGLTP 273
Cdd:PHA02791    26 ADVH---GHSALYYAIADNNVRLVCTLLNAGALKNLLENE--FPLHQAATLEDTKIVKILLFSGmddSQFDDK---GNTA 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  274 LHCAARSGHDQVVELLLERGAPLLARTKNGL-SPLHMAAQGDHVECVKHLLQHKAPVDDVTLdYLTALHVAAHCGHYRVT 352
Cdd:PHA02791    98 LYYAVDSGNMQTVKLFVKKNWRLMFYGKTGWkTSFYHAVMLNDVSIVSYFLSEIPSTFDLAI-LLSCIHITIKNGHVDMM 176

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1887789594  353 KLLLDKRANPNARALNGFTP-LHIACKKNRIKVMELLVKYGASI 395
Cdd:PHA02791   177 ILLLDYMTSTNTNNSLLFIPdIKLAIDNKDLEMLQALFKYDINI 220
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 245-325 7.65e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.22  E-value: 7.65e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  245 SKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLLQ 324
Cdd:PTZ00322    90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169


                   .
gi 1887789594  325 H 325
Cdd:PTZ00322   170 H 170
Ank_4 pfam13637
Ankyrin repeats (many copies);
437-488 7.74e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.35  E-value: 7.74e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1887789594  437 TALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLL 488
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 9-246 9.15e-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: 9.15e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594    9 DSNASFLRAARAGNLD--KVVEYLKGGIDIntcnqnGLNALHLAAKEGHVGlVQELL--------GRGSS---VDSATK- 74
Cdd:TIGR00870   52 GRSALFVAAIENENLEltELLLNLSCRGAV------GDTLLHAISLEYVDA-VEAILlhllaafrKSGPLelaNDQYTSe 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594   75 --KGNTALHIASLAGQAEVVKVLVKEGANINA----------QSQNGF----TPLYMAAQENHIDVVKYLLENGANQSTA 138
Cdd:TIGR00870  125 ftPGITALHLAAHRQNYEIVKLLLERGASVPAracgdffvksQGVDSFyhgeSPLNAAACLGSPSIVALLSEDPADILTA 204

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  139 TEDGFTPLAVALQQGHNQAvaillENDTKG-KVRLPALHIAARKDDTKSAALLLQNDhnadvqsksGFTPLHIAAHYGNV 217
Cdd:TIGR00870  205 DSLGNTLLHLLVMENEFKA-----EYEELScQMYNFALSLLDKLRDSKELEVILNHQ---------GLTPLKLAAKEGRI 270

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1887789594  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 9.47e-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: 9.47e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594    6 QKSDSNASFLRAARAGNLDKVVEYLK-GGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSS-----VDSATKKGNTA 79
Cdd:cd22192     13 QKRISESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElvnepMTSDLYQGETA 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594   80 LHIASLAGQAEVVKVLVKEGANINAQSQNG--FT------------PLYMAAQENHIDVVKYLLENGANQSTATEDGFTP 145
Cdd:cd22192     93 LHIAVVNQNLNLVRELIARGADVVSPRATGtfFRpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTV 172

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  146 LAV-ALQQGHN---QAVAILLENDTKGkvRLPALhiaarkddtksaalllqnDHnadVQSKSGFTPLHIAAHYGNVNVAT 221
Cdd:cd22192    173 LHIlVLQPNKTfacQMYDLILSYDKED--DLQPL------------------DL---VPNNQGLTPFKLAAKEGNIVMFQ 229


                   ....*
gi 1887789594  222 LLLNR 226
Cdd:cd22192    230 HLVQK 234
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 567-719 1.08e-07

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: 57.08  E-value: 1.08e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  567 GYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQ--------------GVTPLHLASQEGHTDMVTLLLDKGANIHMSTKS 632
Cdd:cd22194    141 GQTALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEIVQLLMEKESTDITSQDS 220

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  633 -GLTSLHLAaqedkVNVADiltkHGADQDAHTKLGYTPLIVACHYGNVKMVnfllkqganvnaKTKNGYTPLHQAAQQGH 711
Cdd:cd22194    221 rGNTVLHAL-----VTVAE----DSKTQNDFVKRMYDMILLKSENKNLETI------------RNNEGLTPLQLAAKMGK 279


                   ....*...
gi 1887789594  712 THIINVLL 719
Cdd:cd22194    280 AEILKYIL 287
Ank_5 pfam13857
Ankyrin repeats (many copies);
387-442 1.16e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.04  E-value: 1.16e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1887789594  387 LLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMA 442
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Death_p75NR cd08311
Death domain of p75 Neurotrophin Receptor; Death Domain (DD) found in p75 neurotrophin ...
 1382-1470 1.17e-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: 1.17e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594 1382 PQDEQERIEERLAyiADHLGFSWTELARELDFTEEQIHQIrienpNSLQDQSHALLKYWLERDGkhATDTNLVECLTKIN 1461
Cdd:cd08311      1 PPHKQEEVEKLLN--AGREGSDWRALAGELGYSAEEIDSF-----AREADPCRALLTDWSAQDG--ATLGVLLTALRKIG 71


                   ....*....
gi 1887789594 1462 RMDIVHLME 1470
Cdd:cd08311     72 RDDIVEILQ 80
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 536-655 1.24e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.83  E-value: 1.24e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  536 TPLHVAAKYGSLD--VAKLL----LQRRAAADSAGkngytplhiaakknqmqiASTLLNYGAETNIVTKQGVTPLHLASQ 609
Cdd:PTZ00322    63 TPDHNLTTEEVIDpvVAHMLtvelCQLAASGDAVG------------------ARILLTGGADPNCRDYDGRTPLHIACA 124

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1887789594  610 EGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADILTKH 655
Cdd:PTZ00322   125 NGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
Ank_5 pfam13857
Ankyrin repeats (many copies);
651-706 1.32e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 49.65  E-value: 1.32e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1887789594  651 ILTKHGADQDAHTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQA 706
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
685-739 1.40e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 49.65  E-value: 1.40e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1887789594  685 LLKQG-ANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTALAIA 739
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 329-422 1.49e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.45  E-value: 1.49e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  329 VDDVTLDYLTA--LHVAAHcGHYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPI 406
Cdd:PTZ00322    74 IDPVVAHMLTVelCQLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPL 152

                           90
                   ....*....|....*.
gi 1887789594  407 HVAAFMGHLNIVLLLL 422
Cdd:PTZ00322   153 ELAEENGFREVVQLLS 168
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 546-749 1.64e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 55.90  E-value: 1.64e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  546 SLDVAKLLLQRraAADSAGKnGY--TPL-------HIAAKKNQmQIASTLLNYGAETNIVTKQGVTPLH---LASQEGHT 613
Cdd:PHA02989    49 KIKIVKLLIDN--GADVNYK-GYieTPLcavlrnrEITSNKIK-KIVKLLLKFGADINLKTFNGVSPIVcfiYNSNINNC 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  614 DMVTLLLDKGANIH-MSTKSGLTSLHLAAQEDKVN--VADILTKHGADQDAHTKL-GYTPLIVACHYG----NVKMVNFL 685
Cdd:PHA02989   125 DMLRFLLSKGINVNdVKNSRGYNLLHMYLESFSVKkdVIKILLSFGVNLFEKTSLyGLTPMNIYLRNDidviSIKVIKYL 204

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  686 LKQGAN--------------------------------------VNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNA 727
Cdd:PHA02989   205 IKKGVNietnnngsesvlesfldnnkilskkefkvlnfilkyikINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYN 284

                          250       260
                   ....*....|....*....|..
gi 1887789594  728 TTANGNTALAIAKRLGYISVVD 749
Cdd:PHA02989   285 VSKDGDTVLTYAIKHGNIDMLN 306
Death_RAIDD cd08319
Death domain of RIP-associated ICH-1 homologous protein with a death domain; Death domain (DD) ...
 1390-1461 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 1887789594 1390 EERLAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKIN 1461
Cdd:cd08319      2 DRQLNKLAQRLGPEWEQVLLDLGLSKADIYRCKADHPYNVQSQIVEALVKWKQRQGKKATVQSLIQSLKAVE 73
NESP55 pfam06390
Neuroendocrine-specific golgi protein P55 (NESP55); This family consists of several mammalian ...
 1543-1680 2.19e-07

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: 54.10  E-value: 2.19e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594 1543 TFQDGVPKTEGDSSATALFPQTHKEQVQQDFSGKMQDLPEESSLEYQQEYFVTTPGTET-------SETQKAMIVPSSPS 1615
Cdd:pfam06390   62 SFLNAHHRSAAAAAAAQVFPEPSEPESDHEDEDFEPELARPECLEYDEDDFDTETDSETepesdieSETEFETEPETEPD 141

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594 1616 KTPE-EVSTPAEEEK--------------------LYLQTPTSSERGGSPIIQEPEEPSEHRE------ESSPR--KTSL 1666
Cdd:pfam06390  142 TAPTtEPETEPEDEPgpvvpkgatfhqslterlhaLKLQSADASPRRAPPSTQEPESAREGEEpergplDKDPRdpEEEE 221

                          170
                   ....*....|....
gi 1887789594 1667 VIVESADNQPETCE 1680
Cdd:pfam06390  222 EEKEEEKQQPHRCK 235
Ank_4 pfam13637
Ankyrin repeats (many copies);
111-162 2.49e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.81  E-value: 2.49e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1887789594  111 TPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHNQAVAILL 162
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 166-324 2.58e-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: 55.66  E-value: 2.58e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  166 TKGKVRLPALHIAARKDDT---KSAALLLQNDHNADVQSK-----------SGFTPLHIAAHYGNVNVATLLLNRGAAVD 231
Cdd:cd21882     21 QRGATGKTCLHKAALNLNDgvnEAIMLLLEAAPDSGNPKElvnapctdefyQGQTALHIAIENRNLNLVRLLVENGADVS 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  232 FTA---------RNGI----TPLHVASKRGNTNMVKLLLDRGGQI-DAKTRDGL--TPLHC----AARSGHD-----QVV 286
Cdd:cd21882    101 ARAtgrffrkspGNLFyfgeLPLSLAACTNQEEIVRLLLENGAQPaALEAQDSLgnTVLHAlvlqADNTPENsafvcQMY 180

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1887789594  287 ELLLERGAPL-------LARTKNGLSPLHMAAQGDHVECVKHLLQ 324
Cdd:cd21882    181 NLLLSYGAHLdptqqleEIPNHQGLTPLKLAAVEGKIVMFQHILQ 225
Ank_4 pfam13637
Ankyrin repeats (many copies);
699-751 2.71e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.81  E-value: 2.71e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1887789594  699 GYTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTALAIAKRLGYISVVDTL 751
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 75-259 2.77e-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: 2.77e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594   75 KGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGF-------------TPLYMAAQENHIDVVKYLLENGANQstated 141
Cdd:cd22197     93 RGHSALHIAIEKRSLQCVKLLVENGADVHARACGRFfqkkqgtcfyfgeLPLSLAACTKQWDVVNYLLENPHQP------ 166

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  142 gftplavalqqghnqavAILLENDTKGKVRLPALHIAArkDDTKSAALLLQNDHNADVQSKSGFTPlhiaahygnvnvaT 221
Cdd:cd22197    167 -----------------ASLQAQDSLGNTVLHALVMIA--DNSPENSALVIKMYDGLLQAGARLCP-------------T 214

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1887789594  222 LLLNrgaavDFTARNGITPLHVASKRGNTNMVKLLLDR 259
Cdd:cd22197    215 VQLE-----EISNHEGLTPLKLAAKEGKIEIFRHILQR 247
Ank_5 pfam13857
Ankyrin repeats (many copies);
586-640 3.03e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.88  E-value: 3.03e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1887789594  586 LLNYG-AETNIVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLA 640
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
421-475 3.12e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.88  E-value: 3.12e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1887789594  421 LLQNG-ASPDVTNIRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIA 475
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 387-495 3.36e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 55.29  E-value: 3.36e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  387 LLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNGAL---VDA 463
Cdd:PTZ00322   100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQChfeLGA 179

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1887789594  464 RAREEqtplhiaSRLGKTEIVQLLLQHMAHPD 495
Cdd:PTZ00322   180 NAKPD-------SFTGKPPSLEDSPISSHHPD 204
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 638-751 3.79e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 55.29  E-value: 3.79e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  638 HLAAQEDKVNVADILTKHGADQDAHTKLGYTPLIVA-CHY---GNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTH 713
Cdd:PTZ00322    50 HLEALEATENKDATPDHNLTTEEVIDPVVAHMLTVElCQLaasGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQ 129

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1887789594  714 IINVLLQHGAKPNATTANGNTALAIAKRLGYISVVDTL 751
Cdd:PTZ00322   130 VVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 48-129 4.16e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.90  E-value: 4.16e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594   48 HLAAKEGHVGlVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKY 127
Cdd:PTZ00322    88 QLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                   ..
gi 1887789594  128 LL 129
Cdd:PTZ00322   167 LS 168
Ank_4 pfam13637
Ankyrin repeats (many copies);
600-652 4.39e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.42  E-value: 4.39e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1887789594  600 GVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADIL 652
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 75-226 5.47e-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: 5.47e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594   75 KGNTALHIASLAGQAEVVKVLVKEGANINA----------QSQNGF----TPLYMAAQENHIDVVKYLLEN---GANQST 137
Cdd:cd22196     93 KGQTALHIAIERRNMHLVELLVQNGADVHArasgeffkkkKGGPGFyfgeLPLSLAACTNQLDIVKFLLENphsPADISA 172

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  138 ATEDGFTPL----AVALQQGHNQAVAILLEND--TKGKVRLPALHIAArkddtksaalllqndhnadVQSKSGFTPLHIA 211
Cdd:cd22196    173 RDSMGNTVLhalvEVADNTPENTKFVTKMYNEilILGAKIRPLLKLEE-------------------ITNKKGLTPLKLA 233

                          170
                   ....*....|....*
gi 1887789594  212 AHYGNVNVATLLLNR 226
Cdd:cd22196    234 AKTGKIGIFAYILGR 248
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 84-162 5.56e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.52  E-value: 5.56e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1887789594   84 SLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHNQAVAILL 162
Cdd:PTZ00322    90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
Death_NMPP84 cd08318
Death domain of Nuclear Matrix Protein P84; Death domain (DD) found in the Nuclear Matrix ...
 1386-1465 5.90e-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: 5.90e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594 1386 QERIEErlayIADHLGFSWTELARELDFTEEQIHQIRiENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDI 1465
Cdd:cd08318      7 SEQIDV----LANKLGEQWKTLAPYLEMKDKDIRQIE-SDSEDMKMRAKQLLVTWQDREGAQATPEILMTALNAAGLNEI 81
Ank_5 pfam13857
Ankyrin repeats (many copies);
256-310 7.11e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.73  E-value: 7.11e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1887789594  256 LLDRGGQ-IDAKTRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMA 310
Cdd:pfam13857    1 LLEHGPIdLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
32-83 7.92e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.73  E-value: 7.92e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1887789594   32 GGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIA 83
Cdd:pfam13857    5 GPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 75-226 8.43e-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: 8.43e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594   75 KGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGF--------------TPLYMAAQENHIDVVKYLLENganqstate 140
Cdd:cd22193     75 EGQTALHIAIERRQGDIVALLVENGADVHAHAKGRFfqpkyqgegfyfgeLPLSLAACTNQPDIVQYLLEN--------- 145

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  141 dgftplavalqqghNQAVAILLENDTKGKVRLPALHIAArkDDTKSAALLLQNDHNADVQ---------------SKSGF 205
Cdd:cd22193    146 --------------EHQPADIEAQDSRGNTVLHALVTVA--DNTKENTKFVTRMYDMILIrgaklcptveleeirNNDGL 209

                          170       180
                   ....*....|....*....|.
gi 1887789594  206 TPLHIAAHYGNVNVATLLLNR 226
Cdd:cd22193    210 TPLQLAAKMGKIEILKYILQR 230
PHA02798 PHA02798
ankyrin-like protein; Provisional
 217-442 9.35e-07

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 53.69  E-value: 9.35e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  217 VNVATLLLNRGAAVDFTARNGITPL-----HVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLL- 290
Cdd:PHA02798    51 TDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLf 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  291 --ERGAPLLARTKNGLSPLHMAAQGDH---VECVKHLLQHKAPVDDVT-LDYLTALHV----AAHCGHYRVTKLLLD--- 357
Cdd:PHA02798   131 miENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINTHNnKEKYDTLHCyfkyNIDRIDADILKLFVDngf 210

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  358 --KRANPNARA--LNGFTPLHIACKKNRIKVMELLVKYgASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNI 433
Cdd:PHA02798   211 iiNKENKSHKKkfMEYLNSLLYDNKRFKKNILDFIFSY-IDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITE 289


                   ....*....
gi 1887789594  434 RGETALHMA 442
Cdd:PHA02798   290 LGNTCLFTA 298
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 75-226 9.45e-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: 9.45e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594   75 KGNTALHIASLAGQAEVVKVLVKEGANINAQS---------QNGF----TPLYMAAQENHIDVVKYLLENGANqstated 141
Cdd:cd21882     72 QGQTALHIAIENRNLNLVRLLVENGADVSARAtgrffrkspGNLFyfgeLPLSLAACTNQEEIVRLLLENGAQ------- 144

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  142 gftplavalqqghnqaVAILLENDTKGKVRLPALHIAARKDDTKSA------ALLLQNDHNAD-------VQSKSGFTPL 208
Cdd:cd21882    145 ----------------PAALEAQDSLGNTVLHALVLQADNTPENSAfvcqmyNLLLSYGAHLDptqqleeIPNHQGLTPL 208

                          170
                   ....*....|....*...
gi 1887789594  209 HIAAHYGNVNVATLLLNR 226
Cdd:cd21882    209 KLAAVEGKIVMFQHILQR 226
Ank_5 pfam13857
Ankyrin repeats (many copies);
190-244 1.02e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.34  E-value: 1.02e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1887789594  190 LLQNDH-NADVQSKSGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVA 244
Cdd:pfam13857    1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 218-557 1.03e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 53.59  E-value: 1.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  218 NVATLLLNRGAAVDFTAR-NGITPLHVASKRGNTNMVKLLLDRGGQIDAKtrdGL--TPLHCAAR------SGHDQVVEL 288
Cdd:PHA02989    17 NALEFLLRTGFDVNEEYRgNSILLLYLKRKDVKIKIVKLLIDNGADVNYK---GYieTPLCAVLRnreitsNKIKKIVKL 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  289 LLERGAPLLARTKNGLSPLHMAAQGDHVEcvkhllqhkapvddvTLDYLtalhvaahcghyrvtKLLLDKRANPNA-RAL 367
Cdd:PHA02989    94 LLKFGADINLKTFNGVSPIVCFIYNSNIN---------------NCDML---------------RFLLSKGINVNDvKNS 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  368 NGFTPLHIACKK--NRIKVMELLVKYGASIQAITE-SGLTP--IHVAAFMGHLNIVLL--LLQNGASPDVTNIRGETALH 440
Cdd:PHA02989   144 RGYNLLHMYLESfsVKKDVIKILLSFGVNLFEKTSlYGLTPmnIYLRNDIDVISIKVIkyLIKKGVNIETNNNGSESVLE 223

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  441 maaragqvevvrCLLRNGALVdarAREEQTPLHIASRLGKTEIVQlllqhmahpdaatTNGYTPLHISAREGQVDVASVL 520
Cdd:PHA02989   224 ------------SFLDNNKIL---SKKEFKVLNFILKYIKINKKD-------------KKGFNPLLISAKVDNYEAFNYL 275

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1887789594  521 LEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRR 557
Cdd:PHA02989   276 LKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNRILQLK 312
Ank_4 pfam13637
Ankyrin repeats (many copies);
501-554 1.14e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.27  E-value: 1.14e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1887789594  501 GYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLL 554
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 269-301 1.22e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 46.51  E-value: 1.22e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1887789594  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 ...
 434-556 2.10e-06

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 52.49  E-value: 2.10e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  434 RGETALHMAARAGQVEVVRCLLRNGALVDARAREE--------------QTPLHIASRLGKTEIVQLLLQHMAHP---DA 496
Cdd:cd22193     75 EGQTALHIAIERRQGDIVALLVENGADVHAHAKGRffqpkyqgegfyfgELPLSLAACTNQPDIVQYLLENEHQPadiEA 154

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1887789594  497 ATTNGYTPLHI------SAREGQVDVASV---LLEAGAA-------HSLATKKGFTPLHVAAKYGSLDVAKLLLQR 556
Cdd:cd22193    155 QDSRGNTVLHAlvtvadNTKENTKFVTRMydmILIRGAKlcptvelEEIRNNDGLTPLQLAAKMGKIEILKYILQR 230
Ank_5 pfam13857
Ankyrin repeats (many copies);
322-376 2.24e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.19  E-value: 2.24e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1887789594  322 LLQHKaPVDDVTLDY--LTALHVAAHCGHYRVTKLLLDKRANPNARALNGFTPLHIA 376
Cdd:pfam13857    1 LLEHG-PIDLNRLDGegYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 160-264 2.25e-06

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 49.10  E-value: 2.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  160 ILLENDTKGKvrlPALHIAARKD--DTKSAALLLQnDHNADVQSKS---GFTPLHIAAHYGNVNVATLLLNRgAAVDFTA 234
Cdd:PHA02736    47 LVLEYNRHGK---QCVHIVSNPDkaDPQEKLKLLM-EWGADINGKErvfGNTPLHIAVYTQNYELATWLCNQ-PGVNMEI 121

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1887789594  235 RNGI--TPLHVASKRGNTNMVKLLLDRGGQID 264
Cdd:PHA02736   122 LNYAfkTPYYVACERHDAKMMNILRAKGAQCK 153
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: 45.66  E-value: 2.38e-06
                            10        20
                    ....*....|....*....|....*..
gi 1887789594   108 NGFTPLYMAAQENHIDVVKYLLENGAN 134
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 646-739 2.43e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 52.56  E-value: 2.43e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  646 VNVADILTKHGADQDahTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKP 725
Cdd:PLN03192   507 LNVGDLLGDNGGEHD--DPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNV 584

                           90
                   ....*....|....*.
gi 1887789594  726 NATTANGNTAL--AIA 739
Cdd:PLN03192   585 HIRDANGNTALwnAIS 600
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 30-259 2.48e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 52.05  E-value: 2.48e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594   30 LKGGIDINTCNQNGLNALHLAAKEGHVG---LVQELLGRGSSVDSATK-KGNTALHI--ASLAGQAEVVKVLVKEGANI- 102
Cdd:PHA02989    95 LKFGADINLKTFNGVSPIVCFIYNSNINncdMLRFLLSKGINVNDVKNsRGYNLLHMylESFSVKKDVIKILLSFGVNLf 174

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  103 NAQSQNGFTPL--YMAAQEN--HIDVVKYLLENGANQSTATedgftplavalqQGHNQAVAILLENdtkgkvrlpalHIA 178
Cdd:PHA02989   175 EKTSLYGLTPMniYLRNDIDviSIKVIKYLIKKGVNIETNN------------NGSESVLESFLDN-----------NKI 231

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  179 ARKDDTKSAALLLQ--NDHNADvqsKSGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLL 256
Cdd:PHA02989   232 LSKKEFKVLNFILKyiKINKKD---KKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNRI 308


                   ...
gi 1887789594  257 LDR 259
Cdd:PHA02989   309 LQL 311
PHA02946 PHA02946
ankyin-like protein; Provisional
 502-719 3.60e-06

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 51.59  E-value: 3.60e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  502 YTPLHISAREGQVDVASVLLEAgaahsLATKKGFTPLHVAAKYGSLD--VAKLLLQRRAAADSAGKNGYTPLHIAAKKNQ 579
Cdd:PHA02946    10 YLSLYAKYNSKNLDVFRNMLQA-----IEPSGNYHILHAYCGIKGLDerFVEELLHRGYSPNETDDDGNYPLHIASKINN 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  580 MQIASTLLNYGAETNIVTKQGVTPLHLAS--QEGHTDMVTLLLDKGANIHMST-KSGLTSL------------------- 637
Cdd:PHA02946    85 NRIVAMLLTHGADPNACDKQHKTPLYYLSgtDDEVIERINLLVQYGAKINNSVdEEGCGPLlactdpservfkkimsigf 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  638 ---------------HLAAQEDKVNVADILTKHGADQDAHTKLGYTPLIVACH--YGNVKMVNFLLKQgANVNAKTKNGY 700
Cdd:PHA02946   165 earivdkfgknhihrHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCSktVKNVDIINLLLPS-TDVNKQNKFGD 243

                          250       260
                   ....*....|....*....|
gi 1887789594  701 TPLHQAAQQ-GHTHIINVLL 719
Cdd:PHA02946   244 SPLTLLIKTlSPAHLINKLL 263
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 13-292 4.13e-06

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 51.84  E-value: 4.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594   13 SFLRAARAGNLDKVVEYLKGGIDINTCNQNGLNALH--LAAKEGHVGLVQELLGRGSSVDSATKKGNTALHiaSLAGQAE 90
Cdd:PHA02716   287 SYITLARNIDISVVYSFLQPGVKLHYKDSAGRTCLHqyILRHNISTDIIKLLHEYGNDLNEPDNIGNTVLH--TYLSMLS 364

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594   91 VVKVLVKEGAN-INaqsqngftplymaaqenhIDVVKYLLENGANQSTATEDGFTPLAVALQQGHN----QAVAILLEND 165
Cdd:PHA02716   365 VVNILDPETDNdIR------------------LDVIQCLISLGADITAVNCLGYTPLTSYICTAQNymyyDIIDCLISDK 426

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  166 TKGKVRLPALH-IAARKDDTKS------AALLLQNDHNADVQSKSGFTPLHIAAHYgnvnvATLLLNRGAAVDFTarnGI 238
Cdd:PHA02716   427 VLNMVKHRILQdLLIRVDDTPCiihhiiAKYNIPTDLYTDEYEPYDSTKIHDVYHC-----AIIERYNNAVCETS---GM 498

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1887789594  239 TPLHVA-SKRGNTNMV----KLLLDRGGQIDAKTRDGLTPLHCAAR----SGHD-QVVELLLER 292
Cdd:PHA02716   499 TPLHVSiISHTNANIVmdsfVYLLSIQYNINIPTKNGVTPLMLTMRnnrlSGHQwYIVKNILDK 562
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 666-697 4.20e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 44.97  E-value: 4.20e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1887789594  666 GYTPLIVAC-HYGNVKMVNFLLKQGANVNAKTK 697
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 511-652 4.30e-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: 51.73  E-value: 4.30e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  511 EGQVDVASVLLEAG-----------AAHSLATKKGFTPLHVAAKYGSLDVAKLLLQR----RAAAD------SAGKNGY- 568
Cdd:cd22196     60 NGQNDTISLLLDIAektgnlkefvnAAYTDSYYKGQTALHIAIERRNMHLVELLVQNgadvHARASgeffkkKKGGPGFy 139

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  569 ---TPLHIAAKKNQMQIASTLLN---YGAETNIVTKQGVTPLH---------LASQEGHTDMVTLLLDKGANIH------ 627
Cdd:cd22196    140 fgeLPLSLAACTNQLDIVKFLLEnphSPADISARDSMGNTVLHalvevadntPENTKFVTKMYNEILILGAKIRpllkle 219

                          170       180
                   ....*....|....*....|....*..
gi 1887789594  628 -MSTKSGLTSLHLAAQEDKVNV-ADIL 652
Cdd:cd22196    220 eITNKKGLTPLKLAAKTGKIGIfAYIL 246
Ank_4 pfam13637
Ankyrin repeats (many copies);
16-63 4.90e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.34  E-value: 4.90e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1887789594   16 RAARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELL 63
Cdd:pfam13637    7 AAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
633-686 5.30e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.34  E-value: 5.30e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1887789594  633 GLTSLHLAAQEDKVNVADILTKHGADQDAHTKLGYTPLIVACHYGNVKMVNFLL 686
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 698-729 5.37e-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: 5.37e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1887789594  698 NGYTPLHQAAQQ-GHTHIINVLLQHGAKPNATT 729
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 368-395 6.15e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 44.50  E-value: 6.15e-06
                            10        20
                    ....*....|....*....|....*...
gi 1887789594   368 NGFTPLHIACKKNRIKVMELLVKYGASI 395
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
Death_TRAILR_DR4_DR5 cd08315
Death domain of Tumor necrosis factor-Related Apoptosis-Inducing Ligand Receptors; Death ...
 1395-1461 6.79e-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: 6.79e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1887789594 1395 YIADHLGF-SWTELARELDFTEEQIHQIRIENPNSlQDQSHALLKYWLERDGKHATDTNLVECLTKIN 1461
Cdd:cd08315      4 YFEDIVPFkSWKRLMRALGLSDNEIKLAEANDPGS-QEPLYQMLNKWLNKTGRKASVNTLLDALEDLG 70
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 199-580 7.17e-06

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 51.07  E-value: 7.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  199 VQSKSGFTPLHiaAHYGNVNVAT----LLLNRGAAVDFTARNGITPLHVASKRGN--TNMVKLLLDRGGQIDAKTRDGLT 272
Cdd:PHA02716   172 VCKKTGYGILH--AYLGNMYVDIdileWLCNNGVNVNLQNNHLITPLHTYLITGNvcASVIKKIIELGGDMDMKCVNGMS 249

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  273 PLH---CAARSGHDQVVELLLERGAPllARTKNGLSPLHM---AAQGDHVECVKHLLQhkapvDDVTLDY-----LTALH 341
Cdd:PHA02716   250 PIMtyiINIDNINPEITNIYIESLDG--NKVKNIPMILHSyitLARNIDISVVYSFLQ-----PGVKLHYkdsagRTCLH 322

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  342 --VAAHCGHYRVTKLLLDKRANPNARALNGFTPLH----IACKKN----------RIKVMELLVKYGASIQAITESGLTP 405
Cdd:PHA02716   323 qyILRHNISTDIIKLLHEYGNDLNEPDNIGNTVLHtylsMLSVVNildpetdndiRLDVIQCLISLGADITAVNCLGYTP 402

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  406 ihvaafmghLNIVLLLLQNGASPDVTN-IRGETALHMaaragqvevvrclLRNGALVDARAREEQTPLHIASRLGKTEIv 484
Cdd:PHA02716   403 ---------LTSYICTAQNYMYYDIIDcLISDKVLNM-------------VKHRILQDLLIRVDDTPCIIHHIIAKYNI- 459

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  485 qlllqhmahPDAATTNGYTPLHISAREgqvDVASVLLEAGAAHSLATKKGFTPLHVAAKYGS-----LDVAKLLLQRRAA 559
Cdd:PHA02716   460 ---------PTDLYTDEYEPYDSTKIH---DVYHCAIIERYNNAVCETSGMTPLHVSIISHTnanivMDSFVYLLSIQYN 527

                          410       420
                   ....*....|....*....|.
gi 1887789594  560 ADSAGKNGYTPLHIAAKKNQM 580
Cdd:PHA02716   528 INIPTKNGVTPLMLTMRNNRL 548
Death_DRs cd08784
Death Domain of Death Receptors; Death domain (DD) found in death receptor proteins. Death ...
 1403-1470 7.72e-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: 7.72e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1887789594 1403 SWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLtkiNRMDIVHLME 1470
Cdd:cd08784     13 QWKGFVRKLGLNEAEIDEIKNDNVQDTAEAKYQMLRNWHQLTGRKAAYDTLIKDL---KKMNLCTLAE 77
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 369-508 8.15e-06

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 50.56  E-value: 8.15e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  369 GFTPLHIACKKNRIKVMELLVKYGASIQAITES--------------GLTPIHVAAFMGHLNIVLLLLQNG---ASPDVT 431
Cdd:cd22193     76 GQTALHIAIERRQGDIVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLSLAACTNQPDIVQYLLENEhqpADIEAQ 155

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  432 NIRGETALH--------------MAARAGQVEVVRC--LLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPD 495
Cdd:cd22193    156 DSRGNTVLHalvtvadntkentkFVTRMYDMILIRGakLCPTVELEEIRNNDGLTPLQLAAKMGKIEILKYILQREIKEP 235

                          170       180
                   ....*....|....*....|
gi 1887789594  496 AA-------TTNGYTPLHIS 508
Cdd:cd22193    236 ELrhlsrkfTDWAYGPVSSS 255
Ank_5 pfam13857
Ankyrin repeats (many copies);
95-149 8.68e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.64  E-value: 8.68e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1887789594   95 LVKEG-ANINAQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVA 149
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
454-507 9.57e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.64  E-value: 9.57e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1887789594  454 LLRNG-ALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHI 507
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 308-391 1.00e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.67  E-value: 1.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  308 HMAAQGDHVEcVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMEL 387
Cdd:PTZ00322    88 QLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                   ....
gi 1887789594  388 LVKY 391
Cdd:PTZ00322   167 LSRH 170
Ank_5 pfam13857
Ankyrin repeats (many copies);
552-607 1.04e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.64  E-value: 1.04e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1887789594  552 LLLQRRAAADSAGKNGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLA 607
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 698-727 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: 43.73  E-value: 1.14e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 1887789594   698 NGYTPLHQAAQQGHTHIINVLLQHGAKPNA 727
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 434-556 1.21e-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: 1.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  434 RGETALHMAARAGQVEVVRCLLRNGALVDARAREE-------------QTPLHIASRLGKTEIVQLLLQHMAHP---DAA 497
Cdd:cd22197     93 RGHSALHIAIEKRSLQCVKLLVENGADVHARACGRffqkkqgtcfyfgELPLSLAACTKQWDVVNYLLENPHQPaslQAQ 172

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1887789594  498 TTNGYTPLH---ISAREGQVDVASV------LLEAGAA-------HSLATKKGFTPLHVAAKYGSLDVAKLLLQR 556
Cdd:cd22197    173 DSLGNTVLHalvMIADNSPENSALVikmydgLLQAGARlcptvqlEEISNHEGLTPLKLAAKEGKIEIFRHILQR 247
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 442-631 1.24e-05

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 50.14  E-value: 1.24e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  442 AARAGQVEVVRCLLRNGALVDARAREEQTPLHI-----ASRLGKT--------------EIVQLLLQHMAHPD------- 495
Cdd:cd22194     52 KVSEAAVEELGELLKELKDLSRRRRKTDVPDFLmhkltASDTGKTclmkallninentkEIVRILLAFAEENGildrfin 131

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  496 AATTN----GYTPLHISAREGQVDVASVLLEAGA---AHSLAT-------KKGF----TPLHVAAKYGSLDVAKLLLQRR 557
Cdd:cd22194    132 AEYTEeayeGQTALNIAIERRQGDIVKLLIAKGAdvnAHAKGVffnpkykHEGFyfgeTPLALAACTNQPEIVQLLMEKE 211

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  558 ----AAADSAGKNGYTPLHIAAKKNQMQIAST-------LLNYGAET--NIVTKQGVTPLHLASQEGHTDMVTLLL---- 620
Cdd:cd22194    212 stdiTSQDSRGNTVLHALVTVAEDSKTQNDFVkrmydmiLLKSENKNleTIRNNEGLTPLQLAAKMGKAEILKYILsrei 291

                          250
                   ....*....|..
gi 1887789594  621 -DKGaNIHMSTK 631
Cdd:cd22194    292 kEKP-NRSLSRK 302
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 599-628 1.39e-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: 1.39e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 1887789594   599 QGVTPLHLASQEGHTDMVTLLLDKGANIHM 628
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 599-631 1.46e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 43.43  E-value: 1.46e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1887789594  599 QGVTPLHLAS-QEGHTDMVTLLLDKGANIHMSTK 631
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 236-265 1.69e-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: 42.96  E-value: 1.69e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 1887789594   236 NGITPLHVASKRGNTNMVKLLLDRGGQIDA 265
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02741 PHA02741
hypothetical protein; Provisional
 40-163 1.80e-05

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 46.96  E-value: 1.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594   40 NQNGLNALHLAAKEGHVGLVQELLG--RGSSVDSATK----KGNTALHIASLAGQA----EVVKVLVKEGANINAQ-SQN 108
Cdd:PHA02741    18 NSEGENFFHEAARCGCFDIIARFTPfiRGDCHAAALNatddAGQMCIHIAAEKHEAqlaaEIIDHLIELGADINAQeMLE 97

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1887789594  109 GFTPLYMAAQENHIDVVKYLL-ENGANQSTATEDGFTPLAVALQQGHNQAVAILLE 163
Cdd:PHA02741    98 GDTALHLAAHRRDHDLAEWLCcQPGIDLHFCNADNKSPFELAIDNEDVAMMQILRE 153
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 364-488 1.86e-05

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 49.76  E-value: 1.86e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  364 ARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITES--------------GLTPIHVAAFMGHLNIVLLLLQNGASP- 428
Cdd:cd22194    136 EEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEIVQLLMEKESTDi 215

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1887789594  429 DVTNIRGETALH---MAARAGQ------VEVVRCLLR---NGALVDARAREEQTPLHIASRLGKTEIVQLLL 488
Cdd:cd22194    216 TSQDSRGNTVLHalvTVAEDSKtqndfvKRMYDMILLkseNKNLETIRNNEGLTPLQLAAKMGKAEILKYIL 287
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 123-292 2.00e-05

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 49.49  E-value: 2.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  123 DVVKYLLENGANQSTATedGFTPLAVA---LQQGHNQAVAILLENDTKGKVRLP---------------ALHIAARKDDT 184
Cdd:cd21882      9 ECLRWYLTDSAYQRGAT--GKTCLHKAalnLNDGVNEAIMLLLEAAPDSGNPKElvnapctdefyqgqtALHIAIENRNL 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  185 KSAALLLQNdhNADVQSKS---------------GFTPLHIAAHYGNVNVATLLLNRGAAV-DFTARN--GITPLHVASK 246
Cdd:cd21882     87 NLVRLLVEN--GADVSARAtgrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPaALEAQDslGNTVLHALVL 164

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1887789594  247 RGN---------TNMVKLLLDRGGQID-------AKTRDGLTPLHCAARSGHDQVVELLLER 292
Cdd:cd21882    165 QADntpensafvCQMYNLLLSYGAHLDptqqleeIPNHQGLTPLKLAAVEGKIVMFQHILQR 226
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 1887789594    75 KGNTALHIASLAGQAEVVKVLVKEGANINA 104
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 534-688 2.37e-05

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 49.11  E-value: 2.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  534 GFTPLHVAAKY---GSLDVAKLLLQRRAAADSAGK-----------NGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQ 599
Cdd:cd21882     26 GKTCLHKAALNlndGVNEAIMLLLEAAPDSGNPKElvnapctdefyQGQTALHIAIENRNLNLVRLLVENGADVSARATG 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  600 -------------GVTPLHLASQEGHTDMVTLLLDKGANIHMSTKS---GLTSLH-LAAQEDK--------VNVADILTK 654
Cdd:cd21882    106 rffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPAALEAQdslGNTVLHaLVLQADNtpensafvCQMYNLLLS 185

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1887789594  655 HGADQDAHTKL-------GYTPLIVACHYGNVKMVNFLLKQ 688
Cdd:cd21882    186 YGAHLDPTQQLeeipnhqGLTPLKLAAVEGKIVMFQHILQR 226
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 369-489 2.62e-05

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


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 49.08  E-value: 2.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  369 GFTPLHIACKKNRIKVMELLVKYGASIQAITES-------------GLTPIHVAAFMGHLNIVLLLLQNGASP---DVTN 432
Cdd:cd22197     94 GHSALHIAIEKRSLQCVKLLVENGADVHARACGrffqkkqgtcfyfGELPLSLAACTKQWDVVNYLLENPHQPaslQAQD 173

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1887789594  433 IRGETALH----MAARAGQVEVVRC-----LLRNGALVDARAREEQ-------TPLHIASRLGKTEIVQLLLQ 489
Cdd:cd22197    174 SLGNTVLHalvmIADNSPENSALVIkmydgLLQAGARLCPTVQLEEisnheglTPLKLAAKEGKIEIFRHILQ 246
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 585-729 2.74e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 48.97  E-value: 2.74e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  585 TLLNYGAETNIVTK-QGVTPLHLASQEGHTDMVTLLLDKGANI----HMSTK--SGLTSLHLAAQEDKvNVADILTKHGA 657
Cdd:PHA02989    21 FLLRTGFDVNEEYRgNSILLLYLKRKDVKIKIVKLLIDNGADVnykgYIETPlcAVLRNREITSNKIK-KIVKLLLKFGA 99

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1887789594  658 DQDAHTKLGYTPL---IVACHYGNVKMVNFLLKQGANVNA-KTKNGYTPLHQAAQQG--HTHIINVLLQHGAKPNATT 729
Cdd:PHA02989   100 DINLKTFNGVSPIvcfIYNSNINNCDMLRFLLSKGINVNDvKNSRGYNLLHMYLESFsvKKDVIKILLSFGVNLFEKT 177
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 180-423 2.79e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 48.97  E-value: 2.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  180 RKD-DTKSAALLLQNdhNADVQSKSGF-TPL-------HIAAHYGNvNVATLLLNRGAAVDFTARNGITPLHV---ASKR 247
Cdd:PHA02989    45 RKDvKIKIVKLLIDN--GADVNYKGYIeTPLcavlrnrEITSNKIK-KIVKLLLKFGADINLKTFNGVSPIVCfiyNSNI 121

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  248 GNTNMVKLLLDRGGQI-DAKTRDGLTPLH-----CAARSghdQVVELLLERGAPLLARTK-NGLSPLHMAAQGD----HV 316
Cdd:PHA02989   122 NNCDMLRFLLSKGINVnDVKNSRGYNLLHmylesFSVKK---DVIKILLSFGVNLFEKTSlYGLTPMNIYLRNDidviSI 198

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  317 ECVKHLLQHKAPVDDVTLDYLTAL------HVAAHCGHYRVTKLLLdKRANPNARALNGFTPLHIACKKNRIKVMELLVK 390
Cdd:PHA02989   199 KVIKYLIKKGVNIETNNNGSESVLesfldnNKILSKKEFKVLNFIL-KYIKINKKDKKGFNPLLISAKVDNYEAFNYLLK 277

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1887789594  391 YGASIQAITESGLTPIHVAAFMGHLNIVLLLLQ 423
Cdd:PHA02989   278 LGDDIYNVSKDGDTVLTYAIKHGNIDMLNRILQ 310
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 538-624 2.79e-05

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 46.02  E-value: 2.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  538 LHVAAKYGSLD-VAKLLLQRRAAADSAGK---NGYTPLHIAAKKNQMQIASTLLNY-GAETNIVTKQGVTPLHLASQEGH 612
Cdd:PHA02736    59 VHIVSNPDKADpQEKLKLLMEWGADINGKervFGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERHD 138

                           90
                   ....*....|..
gi 1887789594  613 TDMVTLLLDKGA 624
Cdd:PHA02736   139 AKMMNILRAKGA 150
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 402-432 2.93e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 42.66  E-value: 2.93e-05
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1887789594  402 GLTPIHVAAFM-GHLNIVLLLLQNGASPDVTN 432
Cdd:pfam00023    2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 666-694 3.70e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.19  E-value: 3.70e-05
                            10        20
                    ....*....|....*....|....*....
gi 1887789594   666 GYTPLIVACHYGNVKMVNFLLKQGANVNA 694
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
68-116 3.86e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.72  E-value: 3.86e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1887789594   68 SVDSATKKGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMA 116
Cdd:pfam13857    8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 75-105 4.01e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 42.28  E-value: 4.01e-05
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1887789594   75 KGNTALHIASL-AGQAEVVKVLVKEGANINAQ 105
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNAR 32
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 269-298 4.29e-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: 4.29e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 1887789594  269 DGLTPLHCAARSGHDQVVELLLERGAPLLA 298
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 368-397 4.29e-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: 4.29e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 1887789594  368 NGFTPLHIACKKNRIKVMELLVKYGASIQA 397
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 236-268 4.70e-05

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. 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: 4.70e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1887789594  236 NGITPLHVASKR-GNTNMVKLLLDRGGQIDAKTR 268
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 206-342 5.24e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 46.35  E-value: 5.24e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  206 TPLH--IAAHYGNVNVATLLLNRGAAVDFTAR-NGITPLH---VASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLH---- 275
Cdd:PHA02859    53 TPIFscLEKDKVNVEILKFLIENGADVNFKTRdNNLSALHhylSFNKNVEPEILKILIDSGSSITEEDEDGKNLLHmymc 132

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1887789594  276 -CAARSghdQVVELLLERGAPLLARTKNGLSPLHmaaqgdhvecvKHLLQHKapvDDVTLDYLTALHV 342
Cdd:PHA02859   133 nFNVRI---NVIKLLIDSGVSFLNKDFDNNNILY-----------SYILFHS---DKKIFDFLTSLGI 183
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 666-694 5.27e-05

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 41.86  E-value: 5.27e-05
                           10        20
                   ....*....|....*....|....*....
gi 1887789594  666 GYTPLIVACHYGNVKMVNFLLKQGANVNA 694
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 90-150 5.69e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 46.35  E-value: 5.69e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1887789594   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 ...
 698-727 5.70e-05

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 41.47  E-value: 5.70e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 1887789594  698 NGYTPLHQAAQQGHTHIINVLLQHGAKPNA 727
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 5.92e-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: 5.92e-05
                            10        20
                    ....*....|....*....|....*.
gi 1887789594   269 DGLTPLHCAARSGHDQVVELLLERGA 294
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
PHA02946 PHA02946
ankyin-like protein; Provisional
 471-639 6.07e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 47.74  E-value: 6.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  471 PLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPL-HISAREGQV-DVASVLLEAGAA-HSLATKKGFTPLhVAAKYGSL 547
Cdd:PHA02946    75 PLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLyYLSGTDDEViERINLLVQYGAKiNNSVDEEGCGPL-LACTDPSE 153

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  548 DVAKLLLQ---RRAAADSAGKNgYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQE--GHTDMVTLLLdK 622
Cdd:PHA02946   154 RVFKKIMSigfEARIVDKFGKN-HIHRHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCSKtvKNVDIINLLL-P 231

                          170
                   ....*....|....*..
gi 1887789594  623 GANIHMSTKSGLTSLHL 639
Cdd:PHA02946   232 STDVNKQNKFGDSPLTL 248
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 650-741 6.80e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 47.94  E-value: 6.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  650 DILTKHGADQDAHTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATT 729
Cdd:PLN03192   542 EELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHA 621

                           90
                   ....*....|..
gi 1887789594  730 AnGNTALAIAKR 741
Cdd:PLN03192   622 A-GDLLCTAAKR 632
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 108-134 6.82e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 41.51  E-value: 6.82e-05
                           10        20
                   ....*....|....*....|....*...
gi 1887789594  108 NGFTPLYMAA-QENHIDVVKYLLENGAN 134
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGAD 28
Ank_5 pfam13857
Ankyrin repeats (many copies);
289-343 7.24e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 7.24e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1887789594  289 LLERG-APLLARTKNGLSPLHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVA 343
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 30-113 7.28e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.59  E-value: 7.28e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594   30 LKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKE-------GANI 102
Cdd:PTZ00322   102 LTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHsqchfelGANA 181

                           90
                   ....*....|.
gi 1887789594  103 NAQSQNGFTPL 113
Cdd:PTZ00322   182 KPDSFTGKPPS 192
PHA02795 PHA02795
ankyrin-like protein; Provisional
 90-153 8.00e-05

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 47.30  E-value: 8.00e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1887789594   90 EVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQG 153
Cdd:PHA02795   202 EIYKLCIPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRG 265
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 517-592 8.48e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.59  E-value: 8.48e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1887789594  517 ASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGYTPLHIAAKKNQMQIASTLLNYGAE 592
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQC 173
PHA02791 PHA02791
ankyrin-like protein; Provisional
 432-621 8.62e-05

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 46.57  E-value: 8.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  432 NIRGETALHMAARAGQVEVVRCLLRNGALVDARarEEQTPLHIASRLGKTEIVQlllqhmahpdaattngytplhisare 511
Cdd:PHA02791    27 DVHGHSALYYAIADNNVRLVCTLLNAGALKNLL--ENEFPLHQAATLEDTKIVK-------------------------- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  512 gqvdvasVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGY-TPLHIAAKKNQMQIASTLLNYG 590
Cdd:PHA02791    79 -------ILLFSGMDDSQFDDKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTGWkTSFYHAVMLNDVSIVSYFLSEI 151

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1887789594  591 AETNIVTKQgVTPLHLASQEGHTDMVTLLLD 621
Cdd:PHA02791   152 PSTFDLAIL-LSCIHITIKNGHVDMMILLLD 181
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 302-331 8.77e-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: 8.77e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 1887789594   302 NGLSPLHMAAQGDHVECVKHLLQHKAPVDD 331
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 36-134 9.20e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 45.58  E-value: 9.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594   36 INTCNQNGLNALH--LAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLA----GQAEVVKVLVKEGANINAQSQNG 109
Cdd:PHA02859    44 VNDCNDLYETPIFscLEKDKVNVEILKFLIENGADVNFKTRDNNLSALHHYLSfnknVEPEILKILIDSGSSITEEDEDG 123

                           90       100
                   ....*....|....*....|....*..
gi 1887789594  110 FTPL--YMAAQENHIDVVKYLLENGAN 134
Cdd:PHA02859   124 KNLLhmYMCNFNVRINVIKLLIDSGVS 150
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 515-622 1.03e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 46.51  E-value: 1.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  515 DVASVLLEAGA----AHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADS-AGKNGYTPLHIAAKKNQMQIASTLLNY 589
Cdd:PHA02884    47 DIIDAILKLGAdpeaPFPLSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRyAEEAKITPLYISVLHGCLKCLEILLSY 126

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1887789594  590 GAETNIVTKQGVTPLHLASQEGHTDMVTLLLDK 622
Cdd:PHA02884   127 GADINIQTNDMVTPIELALMICNNFLAFMICDN 159
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 434-464 1.04e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 41.12  E-value: 1.04e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1887789594  434 RGETALHMAA-RAGQVEVVRCLLRNGALVDAR 464
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNAR 32
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 338-365 1.15e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 40.74  E-value: 1.15e-04
                           10        20
                   ....*....|....*....|....*....
gi 1887789594  338 TALHVAA-HCGHYRVTKLLLDKRANPNAR 365
Cdd:pfam00023    4 TPLHLAAgRRGNLEIVKLLLSKGADVNAR 32
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 137-324 1.34e-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: 1.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  137 TATEDGFTPLAVA---LQQGHNQAVAILLEndtkgkvrlpalhIAARKDDTKSaallLQNDHNADVQSKsGFTPLHIAAH 213
Cdd:cd22193     24 TESSTGKTCLMKAllnLNPGTNDTIRILLD-------------IAEKTDNLKR----FINAEYTDEYYE-GQTALHIAIE 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  214 YGNVNVATLLLNRGAAVDFTARN--------------GITPLHVASKRGNTNMVKLLLDRGGQ-IDAKTRD--GLTPLHC 276
Cdd:cd22193     86 RRQGDIVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLSLAACTNQPDIVQYLLENEHQpADIEAQDsrGNTVLHA 165

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1887789594  277 AARSGHD---------QVVELLLERGAPLLA-------RTKNGLSPLHMAAQGDHVECVKHLLQ 324
Cdd:cd22193    166 LVTVADNtkentkfvtRMYDMILIRGAKLCPtveleeiRNNDGLTPLQLAAKMGKIEILKYILQ 229
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 612-706 1.50e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 45.74  E-value: 1.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  612 HTDMVTLLLDKGANIH----MSTKSGLTSLHLAAQEDKVNVADILTKHGADQDAHTK-LGYTPLIVACHYGNVKMVNFLL 686
Cdd:PHA02884    45 YTDIIDAILKLGADPEapfpLSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEeAKITPLYISVLHGCLKCLEILL 124

                           90       100
                   ....*....|....*....|
gi 1887789594  687 KQGANVNAKTKNGYTPLHQA 706
Cdd:PHA02884   125 SYGADINIQTNDMVTPIELA 144
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 566-598 1.51e-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: 1.51e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1887789594  566 NGYTPLHIAAKK-NQMQIASTLLNYGAETNIVTK 598
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
TRPV4 cd22195
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed ...
 75-226 1.75e-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: 1.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594   75 KGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGF--------------TPLYMAAQENHIDVVKYLLENganqstate 140
Cdd:cd22195    136 RGQTALHIAIERRCKHYVELLVEKGADVHAQARGRFfqpkdeggyfyfgeLPLSLAACTNQPDIVHYLTEN--------- 206

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  141 dgftplavalqqGHNQavAILLENDTKGKVRLPAL-HIAARKDD-----TKSAALLLQN------DHNAD-VQSKSGFTP 207
Cdd:cd22195    207 ------------AHKK--ADLRRQDSRGNTVLHALvAIADNTREntkfvTKMYDLLLIKcaklypDCNLEaILNNDGMSP 272

                          170
                   ....*....|....*....
gi 1887789594  208 LHIAAHYGNVNVATLLLNR 226
Cdd:cd22195    273 LMMAAKLGKIGIFQHIIRR 291
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 302-333 1.89e-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: 1.89e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1887789594  302 NGLSPLHMAA-QGDHVECVKHLLQHKAPVDDVT 333
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 566-595 1.94e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 40.26  E-value: 1.94e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 1887789594   566 NGYTPLHIAAKKNQMQIASTLLNYGAETNI 595
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 434-463 2.02e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 40.26  E-value: 2.02e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 1887789594   434 RGETALHMAARAGQVEVVRCLLRNGALVDA 463
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 351-645 2.73e-04

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 46.06  E-value: 2.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  351 VTKLLLDKRANPNARALNGFTPLHIACKKNRI--KVMELLVKYGASIQAITESGLTPI--HVAAFMG-HLNIVLLLLQNG 425
Cdd:PHA02716   194 ILEWLCNNGVNVNLQNNHLITPLHTYLITGNVcaSVIKKIIELGGDMDMKCVNGMSPImtYIINIDNiNPEITNIYIESL 273

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  426 ASPDVTNIRGETALHMA-ARAGQVEVVRCLLRNGALVDARAREEQTPLH--IASRLGKTEIVQLLLQHMAHPDAATTNGY 502
Cdd:PHA02716   274 DGNKVKNIPMILHSYITlARNIDISVVYSFLQPGVKLHYKDSAGRTCLHqyILRHNISTDIIKLLHEYGNDLNEPDNIGN 353

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  503 TPLHI--------------SAREGQVDVASVLLEAGAAHSLATKKGFTPLH----VAAKYGSLDVAKLLL--------QR 556
Cdd:PHA02716   354 TVLHTylsmlsvvnildpeTDNDIRLDVIQCLISLGADITAVNCLGYTPLTsyicTAQNYMYYDIIDCLIsdkvlnmvKH 433

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  557 RAAADSAGKNGYTPL---HIAAKKNqmqIASTLlnYGAE----------------------TNIVTKQGVTPLHLASQEg 611
Cdd:PHA02716   434 RILQDLLIRVDDTPCiihHIIAKYN---IPTDL--YTDEyepydstkihdvyhcaiierynNAVCETSGMTPLHVSIIS- 507

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 1887789594  612 HTDMVTL------LLDKGANIHMSTKSGLTSLHLAAQEDK 645
Cdd:PHA02716   508 HTNANIVmdsfvyLLSIQYNINIPTKNGVTPLMLTMRNNR 547
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 533-558 2.79e-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: 2.79e-04
                            10        20
                    ....*....|....*....|....*.
gi 1887789594   533 KGFTPLHVAAKYGSLDVAKLLLQRRA 558
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 368-400 2.95e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.58  E-value: 2.95e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1887789594  368 NGFTPLHIACKK-NRIKVMELLVKYGASIQAITE 400
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 204-231 2.96e-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: 2.96e-04
                            10        20
                    ....*....|....*....|....*...
gi 1887789594   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 2.97e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.55  E-value: 2.97e-04
                           10        20
                   ....*....|....*....|....*..
gi 1887789594  108 NGFTPLYMAAQENHIDVVKYLLENGAN 134
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGAD 27
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 598-690 3.57e-04

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 42.94  E-value: 3.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  598 KQGVTPLHLASQEGHTD---MVTLLLDKGANIH-MSTKSGLTSLHLAAQEDKVNVADILTKH-GADQDAHTKLGYTPLIV 672
Cdd:PHA02736    53 RHGKQCVHIVSNPDKADpqeKLKLLMEWGADINgKERVFGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYV 132

                           90
                   ....*....|....*...
gi 1887789594  673 ACHYGNVKMVNFLLKQGA 690
Cdd:PHA02736   133 ACERHDAKMMNILRAKGA 150
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 402-430 3.64e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.49  E-value: 3.64e-04
                            10        20
                    ....*....|....*....|....*....
gi 1887789594   402 GLTPIHVAAFMGHLNIVLLLLQNGASPDV 430
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 204-231 3.73e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.58  E-value: 3.73e-04
                           10        20
                   ....*....|....*....|....*....
gi 1887789594  204 GFTPLHIAA-HYGNVNVATLLLNRGAAVD 231
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVN 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 434-463 3.75e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.16  E-value: 3.75e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1887789594  434 RGETALHMAARAGQVEVVRCLLRNGALVDA 463
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 501-747 5.41e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 45.07  E-value: 5.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  501 GYTPLHISAREGQV-DVASVLLEagaaHSLATKKGFTPLHVAAKyGSLDVAKLLLQRRAAADsaGKNGYTPLHIAAKKNQ 579
Cdd:TIGR00870   52 GRSALFVAAIENENlELTELLLN----LSCRGAVGDTLLHAISL-EYVDAVEAILLHLLAAF--RKSGPLELANDQYTSE 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  580 MQiastllnygaetnivtkQGVTPLHLASQEGHTDMVTLLLDKGANIHMstksgltslhlaaqedKVNVADILTKHGADQ 659
Cdd:TIGR00870  125 FT-----------------PGITALHLAAHRQNYEIVKLLLERGASVPA----------------RACGDFFVKSQGVDS 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  660 DAHTKLgytPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGH---------THIINVLLQHGAKPNATTA 730
Cdd:TIGR00870  172 FYHGES---PLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVMENEfkaeyeelsCQMYNFALSLLDKLRDSKE 248

                          250       260
                   ....*....|....*....|....
gi 1887789594  731 -------NGNTALAIAKRLGYISV 747
Cdd:TIGR00870  249 levilnhQGLTPLKLAAKEGRIVL 272
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 335-364 6.31e-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: 6.31e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 1887789594   335 DYLTALHVAAHCGHYRVTKLLLDKRANPNA 364
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Death_PIDD cd08779
Death Domain of p53-induced protein with a death domain; Death domain (DD) found in PIDD ...
 1393-1466 7.25e-04

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


Pssm-ID: 260049  Cd Length: 86  Bit Score: 40.38  E-value: 7.25e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1887789594 1393 LAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLErdgKHATDTN----LVECLTKINRMDIV 1466
Cdd:cd08779      5 LLSLAKELGEDWQKLALHLGVSYSRIQRIKRKNRDDLDEQILDMLFSWAK---TLPTSPDkvglLVTALSKSGRSDLA 79
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 599-724 7.35e-04

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 41.79  E-value: 7.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  599 QGVTPLHLASQEGhtDMVTLLLDKGA----NIHMST---KSGLTSLHLAAQEDKV---NVADILTKHGADQDAH-TKLGY 667
Cdd:PHA02736    16 EGENILHYLCRNG--GVTDLLAFKNAisdeNRYLVLeynRHGKQCVHIVSNPDKAdpqEKLKLLMEWGADINGKeRVFGN 93

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1887789594  668 TPLIVACHYGNVKMVNFLLKQ-GANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAK 724
Cdd:PHA02736    94 TPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGAQ 151
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 75-104 8.24e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.39  E-value: 8.24e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1887789594   75 KGNTALHIASLAGQAEVVKVLVKEGANINA 104
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 567-720 8.64e-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: 8.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  567 GYTPLHIAAKKNQMQIASTLLNYGAETNIVT-------KQGVT------PLHLASQEGHTDMVTLLLDKG---ANIHMST 630
Cdd:cd22197     94 GHSALHIAIEKRSLQCVKLLVENGADVHARAcgrffqkKQGTCfyfgelPLSLAACTKQWDVVNYLLENPhqpASLQAQD 173

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  631 KSGLTSLHLAaqedkVNVADiltkhgaDQDAHTKLgytplivachygNVKMVNFLLKQGANVNAKTK-------NGYTPL 703
Cdd:cd22197    174 SLGNTVLHAL-----VMIAD-------NSPENSAL------------VIKMYDGLLQAGARLCPTVQleeisnhEGLTPL 229

                          170
                   ....*....|....*..
gi 1887789594  704 HQAAQQGHTHIINVLLQ 720
Cdd:cd22197    230 KLAAKEGKIEIFRHILQ 246
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 469-498 9.97e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.04  E-value: 9.97e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1887789594  469 QTPLHIAS-RLGKTEIVQLLLQHMAHPDAAT 498
Cdd:pfam00023    3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 533-558 1.09e-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: 1.09e-03
                           10        20
                   ....*....|....*....|....*..
gi 1887789594  533 KGFTPLHVAA-KYGSLDVAKLLLQRRA 558
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGA 27
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 140-292 1.19e-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: 1.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  140 EDGFTPLAVA---LQQGHNQAVAILLE------------------NDTKGKVrlpALHIAARKDDTKSAALLLQNdhNAD 198
Cdd:cd22196     45 ETGKTCLLKAmlnLHNGQNDTISLLLDiaektgnlkefvnaaytdSYYKGQT---ALHIAIERRNMHLVELLVQN--GAD 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  199 VQ------------SKSGF----TPLHIAAHYGNVNVATLLL-NRGAAVDFTARN--GITPLH---------VASKRGNT 250
Cdd:cd22196    120 VHarasgeffkkkkGGPGFyfgeLPLSLAACTNQLDIVKFLLeNPHSPADISARDsmGNTVLHalvevadntPENTKFVT 199

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1887789594  251 NMVKLLLDRGGQIDAK-------TRDGLTPLHCAARSGHDQVVELLLER 292
Cdd:cd22196    200 KMYNEILILGAKIRPLlkleeitNKKGLTPLKLAAKTGKIGIFAYILGR 248
Death_RIP1 cd08777
Death Domain of Receptor-Interacting Protein 1; Death domain (DD) found in ...
 1390-1469 1.20e-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: 1.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594 1390 EERLAYIADHLGFSWTELARELDFTEEQIHQIRIE-NPNSLQDQSHALLKYWLERDG-KHATDTNLVECLTKINRMDIVH 1467
Cdd:cd08777      2 EKHLDLLRENLGKKWKRCARRLGLTEVEIEEIDHDyERDGLKEKVHQMLEKWKMKEGsKGATVGKLAKALEGCIKSDLLV 81


                   ..
gi 1887789594 1468 LM 1469
Cdd:cd08777     82 SL 83
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 495-622 1.36e-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: 43.69  E-value: 1.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  495 DAATTN----GYTPLHISAREGQVDVASVLLEAGA-AHSLA------TKKGFT------PLHVAAKYGSLDVAKLLLQRR 557
Cdd:cd22197     84 NAQCTDeyyrGHSALHIAIEKRSLQCVKLLVENGAdVHARAcgrffqKKQGTCfyfgelPLSLAACTKQWDVVNYLLENP 163

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  558 ---AAADSAGKNGYTPLH----IAAKKNQ-----MQIASTLLNYGAETN-------IVTKQGVTPLHLASQEGHTDMVTL 618
Cdd:cd22197    164 hqpASLQAQDSLGNTVLHalvmIADNSPEnsalvIKMYDGLLQAGARLCptvqleeISNHEGLTPLKLAAKEGKIEIFRH 243


                   ....
gi 1887789594  619 LLDK 622
Cdd:cd22197    244 ILQR 247
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 567-720 1.48e-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: 1.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  567 GYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQ--------------GVTPLHLASQEGHTDMVTLLLD---KGANIHMS 629
Cdd:cd22193     76 GQTALHIAIERRQGDIVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLSLAACTNQPDIVQYLLEnehQPADIEAQ 155

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  630 TKSGLTSLHLAaqedkVNVADiltkhgaDQDAHTKLgytplivachygNVKMVNFLLKQGANVNAKTK-------NGYTP 702
Cdd:cd22193    156 DSRGNTVLHAL-----VTVAD-------NTKENTKF------------VTRMYDMILIRGAKLCPTVEleeirnnDGLTP 211

                          170
                   ....*....|....*...
gi 1887789594  703 LHQAAQQGHTHIINVLLQ 720
Cdd:cd22193    212 LQLAAKMGKIEILKYILQ 229
Death_MyD88 cd08312
Death domain of Myeloid Differentation primary response protein MyD88; Death Domain (DD) of ...
 1404-1467 1.52e-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: 1.52e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1887789594 1404 WTELARELDFTEEQIHQIRIENpnslqDQSHALLKYWLERDgKHATDTNLVECLTKINRMDIVH 1467
Cdd:cd08312     19 WRGLAELMGFDYLEIRNFERQS-----SPTERLLEDWETRP-PGATVGNLLEILEELERKDVLE 76
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 569-702 1.54e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 41.73  E-value: 1.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  569 TPLH--IAAKKNQMQIASTLLNYGAETNIVTK-QGVTPLH--LASQEG-HTDMVTLLLDKGANIHMSTKSGLTSLH--LA 640
Cdd:PHA02859    53 TPIFscLEKDKVNVEILKFLIENGADVNFKTRdNNLSALHhyLSFNKNvEPEILKILIDSGSSITEEDEDGKNLLHmyMC 132

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1887789594  641 AQEDKVNVADILTKHGA-----DQDAHTKLgYTPLIvacHYGNVKMVNFLLKQGANVNAKTKNGYTP 702
Cdd:PHA02859   133 NFNVRINVIKLLIDSGVsflnkDFDNNNIL-YSYIL---FHSDKKIFDFLTSLGIDINETNKSGYNC 195
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 236-265 1.65e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.62  E-value: 1.65e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1887789594  236 NGITPLHVASKRGNTNMVKLLLDRGGQIDA 265
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 402-430 1.72e-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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.62  E-value: 1.72e-03
                           10        20
                   ....*....|....*....|....*....
gi 1887789594  402 GLTPIHVAAFMGHLNIVLLLLQNGASPDV 430
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 204-231 1.81e-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: 1.81e-03
                           10        20
                   ....*....|....*....|....*...
gi 1887789594  204 GFTPLHIAAHYGNVNVATLLLNRGAAVD 231
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADIN 29
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 533-561 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 1887789594  533 KGFTPLHVAAKYGSLDVAKLLLQRRAAAD 561
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 327-456 1.98e-03

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 42.86  E-value: 1.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  327 APVDDVTLDYLTALHVAAH--CGHYrvTKLLLDKRANPNARALNGF--------------TPLHIACKKNRIKVMELLVK 390
Cdd:cd22193     67 AEYTDEYYEGQTALHIAIErrQGDI--VALLVENGADVHAHAKGRFfqpkyqgegfyfgeLPLSLAACTNQPDIVQYLLE 144

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  391 YG---ASIQAITESGLTPIH----VA-------AFMGHLNIVLLLLQNGASPDV-----TNIRGETALHMAARAGQVEVV 451
Cdd:cd22193    145 NEhqpADIEAQDSRGNTVLHalvtVAdntkentKFVTRMYDMILIRGAKLCPTVeleeiRNNDGLTPLQLAAKMGKIEIL 224


                   ....*
gi 1887789594  452 RCLLR 456
Cdd:cd22193    225 KYILQ 229
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 353-430 2.00e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 40.63  E-value: 2.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  353 KLLLDKRANPNAR-ALNGFTPLHIACKKNRIKVMELLVKY-GASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDV 430
Cdd:PHA02736    75 KLLMEWGADINGKeRVFGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGAQCKV 154
PHA02946 PHA02946
ankyin-like protein; Provisional
 344-543 2.10e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 42.73  E-value: 2.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  344 AHCG----HYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGHLNI-- 417
Cdd:PHA02946    43 AYCGikglDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIer 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  418 VLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNG--ALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPD 495
Cdd:PHA02946   123 INLLVQYGAKINNSVDEEGCGPLLACTDPSERVFKKIMSIGfeARIVDKFGKNHIHRHLMSDNPKASTISWMMKLGISPS 202

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1887789594  496 AATTNGYTPLHI--SAREGQVDVASVLLEAGAAHSlATKKGFTPLHVAAK 543
Cdd:PHA02946   203 KPDHDGNTPLHIvcSKTVKNVDIINLLLPSTDVNK-QNKFGDSPLTLLIK 251
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 566-595 2.12e-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: 2.12e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1887789594  566 NGYTPLHIAAKKNQMQIASTLLNYGAETNI 595
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 208-455 2.27e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 42.81  E-value: 2.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  208 LHIAAHYGNVNVATLLLNRGAAVDFtaRNGI-TPL-------HVASKRGNtNMVKLLLDRGGQIDAKTRDGLTPLHCAAR 279
Cdd:PHA02989    41 LYLKRKDVKIKIVKLLIDNGADVNY--KGYIeTPLcavlrnrEITSNKIK-KIVKLLLKFGADINLKTFNGVSPIVCFIY 117

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  280 SGH---DQVVELLLERGAPLLArTKN--GLSPLHMAAQGDHV--ECVKHLLQHKA-PVDDVTLDYLTALHV----AAHCG 347
Cdd:PHA02989   118 NSNinnCDMLRFLLSKGINVND-VKNsrGYNLLHMYLESFSVkkDVIKILLSFGVnLFEKTSLYGLTPMNIylrnDIDVI 196

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  348 HYRVTKLLLDKRA---NPNAR---ALNGFTPLHIACKKNRIKVMELLVKYgASIQAITESGLTPIHVAAFMGHLNIVLLL 421
Cdd:PHA02989   197 SIKVIKYLIKKGVnieTNNNGsesVLESFLDNNKILSKKEFKVLNFILKY-IKINKKDKKGFNPLLISAKVDNYEAFNYL 275

                          250       260       270
                   ....*....|....*....|....*....|....
gi 1887789594  422 LQNGASPDVTNIRGETALHMAARAGQVEVVRCLL 455
Cdd:PHA02989   276 LKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNRIL 309
Death_TNFR1 cd08313
Death domain of Tumor Necrosis Factor Receptor 1; Death Domain (DD) found in tumor necrosis ...
 1404-1470 2.63e-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: 2.63e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1887789594 1404 WTELARELDFTEEQIHQIRIENpNSLQDQSHALLKYWLERDGKHATDTNLVECltKINRMDIVHLME 1470
Cdd:cd08313     14 WKEFVRRLGLSDNEIERVELDH-RRCRDAQYQMLKVWKERGPRPYATLQHLLS--VLRDMELVGCAE 77
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 335-364 2.79e-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: 2.79e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1887789594  335 DYLTALHVAAHCGHYRVTKLLLDKRANPNA 364
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 600-628 2.79e-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: 2.79e-03
                           10        20
                   ....*....|....*....|....*....
gi 1887789594  600 GVTPLHLASQEGHTDMVTLLLDKGANIHM 628
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02791 PHA02791
ankyrin-like protein; Provisional
 367-522 3.10e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 41.57  E-value: 3.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  367 LNGFTPLHIACKKNRIKVMELLVKYGAsIQAITESGLtPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAG 446
Cdd:PHA02791    28 VHGHSALYYAIADNNVRLVCTLLNAGA-LKNLLENEF-PLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSG 105

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1887789594  447 QVEVVRCLL-RNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHP-DAATTngYTPLHISAREGQVDVASVLLE 522
Cdd:PHA02791   106 NMQTVKLFVkKNWRLMFYGKTGWKTSFYHAVMLNDVSIVSYFLSEIPSTfDLAIL--LSCIHITIKNGHVDMMILLLD 181
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 667-736 3.56e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 40.96  E-value: 3.56e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1887789594  667 YTPLIVAC---HYGNVKMVNFLLKQGANVNAKTK-NGYTPLH---QAAQQGHTHIINVLLQHGAKPNATTANGNTAL 736
Cdd:PHA02859    51 YETPIFSClekDKVNVEILKFLIENGADVNFKTRdNNLSALHhylSFNKNVEPEILKILIDSGSSITEEDEDGKNLL 127
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 500-525 3.59e-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: 3.59e-03
                            10        20
                    ....*....|....*....|....*.
gi 1887789594   500 NGYTPLHISAREGQVDVASVLLEAGA 525
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
PHA02791 PHA02791
ankyrin-like protein; Provisional
 47-196 3.73e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 41.57  E-value: 3.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594   47 LHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGF-TPLYMAAQENHIDVV 125
Cdd:PHA02791    65 LHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTGWkTSFYHAVMLNDVSIV 144

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1887789594  126 KYLLengaNQSTATEDGFTPLA---VALQQGHNQAVAILLE-----NDTKGKVRLPALHIAARKDDTKSAALLLQNDHN 196
Cdd:PHA02791   145 SYFL----SEIPSTFDLAILLScihITIKNGHVDMMILLLDymtstNTNNSLLFIPDIKLAIDNKDLEMLQALFKYDIN 219
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 42-74 3.99e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.50  E-value: 3.99e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1887789594   42 NGLNALHLAA-KEGHVGLVQELLGRGSSVDSATK 74
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 40-133 4.23e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 39.86  E-value: 4.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594   40 NQNGLNALHLAAKEGHVGLVQE---LLGRGSSVDSATKK-GNTALHIASLAGQAEVVKVLVKE-GANINAQSQNGFTPLY 114
Cdd:PHA02736    52 NRHGKQCVHIVSNPDKADPQEKlklLMEWGADINGKERVfGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYY 131

                           90
                   ....*....|....*....
gi 1887789594  115 MAAQENHIDVVKYLLENGA 133
Cdd:PHA02736   132 VACERHDAKMMNILRAKGA 150
PHA02791 PHA02791
ankyrin-like protein; Provisional
 560-736 4.41e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 41.18  E-value: 4.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  560 ADSAGKNGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQgvTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHL 639
Cdd:PHA02791    23 AFKADVHGHSALYYAIADNNVRLVCTLLNAGALKNLLENE--FPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYY 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  640 AAQEDKVNVADILTKHGADQDAHTKLGY-TPLIVACHYGNVKMVNFLLKQGANvNAKTKNGYTPLHQAAQQGHTHIINVL 718
Cdd:PHA02791   101 AVDSGNMQTVKLFVKKNWRLMFYGKTGWkTSFYHAVMLNDVSIVSYFLSEIPS-TFDLAILLSCIHITIKNGHVDMMILL 179

                          170
                   ....*....|....*...
gi 1887789594  719 LQHgakpnATTANGNTAL 736
Cdd:PHA02791   180 LDY-----MTSTNTNNSL 192
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 42-70 4.92e-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: 4.92e-03
                            10        20
                    ....*....|....*....|....*....
gi 1887789594    42 NGLNALHLAAKEGHVGLVQELLGRGSSVD 70
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 351-428 6.11e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 40.19  E-value: 6.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  351 VTKLLLDKRANPNARAL-NGFTPLH--IACKKN-RIKVMELLVKYGASIQAITESGLTPIHV--AAFMGHLNIVLLLLQN 424
Cdd:PHA02859    68 ILKFLIENGADVNFKTRdNNLSALHhyLSFNKNvEPEILKILIDSGSSITEEDEDGKNLLHMymCNFNVRINVIKLLIDS 147


                   ....
gi 1887789594  425 GASP 428
Cdd:PHA02859   148 GVSF 151
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 533-648 6.98e-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: 41.32  E-value: 6.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  533 KGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKN--------------GYTPLHIAAKKNQMQIASTLLNYGAETNIVTK 598
Cdd:cd22193     75 EGQTALHIAIERRQGDIVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLSLAACTNQPDIVQYLLENEHQPADIEA 154

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1887789594  599 Q---GVTPLHLA-----SQEGHTDMVT----LLLDKGANIH-------MSTKSGLTSLHLAAQEDKVNV 648
Cdd:cd22193    155 QdsrGNTVLHALvtvadNTKENTKFVTrmydMILIRGAKLCptveleeIRNNDGLTPLQLAAKMGKIEI 223
Death_FAS_TNFRSF6 cd08316
Death domain of FAS or TNF receptor superfamily member 6; Death Domain (DD) found in the ...
 1389-1467 7.07e-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: 7.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594 1389 IEERLAYIADHLGfsWTE---LARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINR--- 1462
Cdd:cd08316      4 LSKHIPDIAEIMG--WKDvkkFARKSGISETKIDEIQLDNPNDTAEQKVQLLRAWYQKHGKKGAYRTLIKTLRKAGKrak 81


                   ....*....
gi 1887789594 1463 ----MDIVH 1467
Cdd:cd08316     82 adkiQDIIK 90
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 206-279 7.42e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 40.35  E-value: 7.42e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1887789594  206 TPLHIAAHYGNVNVATLLLNRGAAVD-FTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAAR 279
Cdd:PHA02884    72 NPLIYAIDCDNDDAAKLLIRYGADVNrYAEEAKITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELALM 146
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 565-751 7.96e-03

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 41.05  E-value: 7.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  565 KNGYTPLH--IAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGH--TDMVTLLLDKGANIHMSTKSGLTSLhLA 640
Cdd:PHA02716   175 KTGYGILHayLGNMYVDIDILEWLCNNGVNVNLQNNHLITPLHTYLITGNvcASVIKKIIELGGDMDMKCVNGMSPI-MT 253

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  641 AQEDKVNVADILTKHGADQDAHTKLGYTPLIVACH-----YGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGH--TH 713
Cdd:PHA02716   254 YIINIDNINPEITNIYIESLDGNKVKNIPMILHSYitlarNIDISVVYSFLQPGVKLHYKDSAGRTCLHQYILRHNisTD 333

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1887789594  714 IINVLLQHGAKPNATTANGNTALaiAKRLGYISVVDTL 751
Cdd:PHA02716   334 IIKLLHEYGNDLNEPDNIGNTVL--HTYLSMLSVVNIL 369
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 338-456 9.10e-03

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


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 40.99  E-value: 9.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  338 TALHVAAHCGHYRVTKLLLDKRANPNARALNGF-------------TPLHIACKKNRIKVMELLVKYG---ASIQAITES 401
Cdd:cd22197     96 SALHIAIEKRSLQCVKLLVENGADVHARACGRFfqkkqgtcfyfgeLPLSLAACTKQWDVVNYLLENPhqpASLQAQDSL 175

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1887789594  402 GLTPIHVAAFMG---HLNIVLL------LLQNGASPD-------VTNIRGETALHMAARAGQVEVVRCLLR 456
Cdd:cd22197    176 GNTVLHALVMIAdnsPENSALVikmydgLLQAGARLCptvqleeISNHEGLTPLKLAAKEGKIEIFRHILQ 246
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 538-640 9.41e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 40.35  E-value: 9.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789594  538 LHVAAKYGSLDVAKLLLQRRA---AADSAGKNGYT-PLHIAAKKNQMQIASTLLNYGAETNIVTKQGV-TPLHLASQEGH 612
Cdd:PHA02884    37 LYSSIKFHYTDIIDAILKLGAdpeAPFPLSENSKTnPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLHGC 116

                           90       100
                   ....*....|....*....|....*...
gi 1887789594  613 TDMVTLLLDKGANIHMSTKSGLTSLHLA 640
Cdd:PHA02884   117 LKCLEILLSYGADINIQTNDMVTPIELA 144
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 500-525 9.49e-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: 35.34  E-value: 9.49e-03
                           10        20
                   ....*....|....*....|....*..
gi 1887789594  500 NGYTPLHISA-REGQVDVASVLLEAGA 525
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGA 27
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 302-330 9.81e-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: 9.81e-03
                           10        20
                   ....*....|....*....|....*....
gi 1887789594  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.
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