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Conserved domains on  [gi|2023156728|ref|XP_040461281|]
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ankyrin-3 isoform X4 [Falco naumanni]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
329-612 2.11e-62

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 216.74  E-value: 2.11e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  329 LLIQHNVPVDDVTNDYLTALHVAAHCGHYKVAKVLLDKKANPNAKALNGFTPLHIACKKNRIKVMELLLKHGASIQAVTE 408
Cdd:COG0666      6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  409 SGLTPIHVAAFMGHVNIVSQLMHHGASPNTTNVRGETALHMAARAGQTEVVRYLVQNGAQVEAKAKDDQTPLHISARLGK 488
Cdd:COG0666     86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  489 ADIVQQLLQQGASPNAATTSGYTPLHLSAREGHEDVASVLLDHGASLSIITKKGFTPLHVAAKYGKIEVANLLLQKNASP 568
Cdd:COG0666    166 LEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADL 245

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 2023156728  569 DASGKSGLTPLHVAAHYDNQKVALLLLDQGASPHASAKNGYTPL 612
Cdd:COG0666    246 NAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
528-793 2.84e-61

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 213.28  E-value: 2.84e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  528 LLDHGASLSIITKKGFTPLHVAAKYGKIEVANLLLQKNASPDASGKSGLTPLHVAAHYDNQKVALLLLDQGASPHASAKN 607
Cdd:COG0666      7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  608 GYTPLHIAAKKNQMDIATTLLEYGADANAVTRQGIAPVHLASQDGHVDMVSLLLTRNANVNLGNKSGLTPLHLAAQDDRV 687
Cdd:COG0666     87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  688 NVAEVLVNQGAAVDAQTKMGYTPLHVGCHYGNIKIVNFLLQHSAKVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAAPN 767
Cdd:COG0666    167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246

                          250       260
                   ....*....|....*....|....*.
gi 2023156728  768 ELTVNGNTALAIAKRLGYISVVDTLK 793
Cdd:COG0666    247 AKDKDGLTALLLAAAAGAALIVKLLL 272
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
168-447 1.49e-60

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 211.35  E-value: 1.49e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  168 LLLENDTKGKVRLPALHIAARKDDTKAAALLLQNDHNADVESKSGFTPLHIAAHYGNINVATLLLNRGAAVDFTARNDIT 247
Cdd:COG0666     10 LLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNT 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  248 PLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPLHCGARSGHEQVVEMLLDRGAPILSKTKNGLSPLHMATQGDHLNCV 327
Cdd:COG0666     90 LLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  328 QLLIQHNVPVDDVTNDYLTALHVAAHCGHYKVAKVLLDKKANPNAKALNGFTPLHIACKKNRIKVMELLLKHGASIQAVT 407
Cdd:COG0666    170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKD 249

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 2023156728  408 ESGLTPIHVAAFMGHVNIVSQLMHHGASPNTTNVRGETAL 447
Cdd:COG0666    250 KDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
UPA_2 super family cl39303
UPA domain; The UPA domain is conserved in UNC5, PIDD, and Ankyrins. It has a beta sandwich ...
 1295-1424 2.55e-57

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: 195.38  E-value: 2.55e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728 1295 VPYMAKFVIFAKMNDPVESNLRCFCMTDDKVDKTLEQQENFEEVARSKDIEVLEGKPIYVDCYGNLAPLTKGGQQLVFNF 1374
Cdd:pfam17809    1 VPYLAKFVVFAKRYDPGEARLRCACMTDDGEDKTLEFHEGFTEVARSRDVEVLEGSPVSIELSGNLVPIKKKSQSRQMDF 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2023156728 1375 YAFKENRLPFSIKVRDTSQEPCGRLSFLKEPKTTKGLPQTAVCNLNITLP 1424
Cdd:pfam17809   81 KAFRENRLDGSVRVKDPSDPPKGLLSFMRDAKVDGGTVSQPLCTLNIVLP 130
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
3-282 5.59e-54

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 192.48  E-value: 5.59e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728    3 VLLMLLDYILRKMSDTNASYLRAARAGNLEKALDYLKSGVDINISNQNGLNALHLASKEGHVEVVSELIQRGASVDAATK 82
Cdd:COG0666     39 LLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDK 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728   83 KGNTALHIASLAGQAEVVKVLVTNRANVNAQSQNGFTPLYMAAQENHLEVVKFLLDNGASQSLATEDGFTPLAVALQQGH 162
Cdd:COG0666    119 DGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGH 198

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  163 DQVVSLLLEndtkgkvrlpalhiaarkddtkaaalllqndHNADVE--SKSGFTPLHIAAHYGNINVATLLLNRGAAVDF 240
Cdd:COG0666    199 LEIVKLLLE-------------------------------AGADVNakDNDGKTALDLAAENGNLEIVKLLLEAGADLNA 247

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 2023156728  241 TARNDITPLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPL 282
Cdd:COG0666    248 KDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
 969-1073 8.16e-48

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


:

Pssm-ID: 128514  Cd Length: 104  Bit Score: 167.14  E-value: 8.16e-48
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728   969 SSFLVSFMVDARGGSMRGSRHhGMRIIIPPRKCTAPTRITCRLVKRHKLASPPPMVEGEGLASRLVEMGPSGAQFLGPVI 1048
Cdd:smart00218    1 PSFLVSGTFDARGGRLRGPRT-GVRLIIPPGAIPQGTRYTCYLVVHKTLSTPPPLEEGETLLSPVVECGPHGALFLRPVI 79

                            90       100
                    ....*....|....*....|....*
gi 2023156728  1049 VEIPHFGSMRGKERELIVLRSENGE 1073
Cdd:smart00218   80 LEVPHCASLRPRDWEIVLLRSENGG 104
Death_ank3 cd08803
Death domain of Ankyrin-3; Death Domain (DD) of the human protein ankyrin-3 (ANK-3) and ...
 4038-4121 3.89e-46

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: 161.76  E-value: 3.89e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728 4038 ERTDIRMAIVADHLGLSWTELARELNFSVDEINQIRVENPNSLIAQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIV 4117
Cdd:cd08803      1 ERTDIRMAIVADHLGLSWTELARELNFSVDEINQIRVENPNSLIAQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIV 80


                   ....
gi 2023156728 4118 TLLE 4121
Cdd:cd08803     81 TLLE 84
PLN03192 super family cl33658
Voltage-dependent potassium channel; Provisional
 691-903 2.00e-06

Voltage-dependent potassium channel; Provisional


The actual alignment was detected with superfamily member PLN03192:

Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.49  E-value: 2.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  691 EVLVNQGAAVDAQTKMGYTPLHVGCHYGNIKIVNFLLQHSAKVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAAPNELT 770
Cdd:PLN03192   542 EELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHA 621

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  771 vnGNTALAIAKRLGYISVVDT-----LKVVTEE----TMTTITVTEKHKmnvpeTMNEVLDMSDDEVRKANAPEILSDA- 840
Cdd:PLN03192   622 --AGDLLCTAAKRNDLTAMKEllkqgLNVDSEDhqgaTALQVAMAEDHV-----DMVRLLIMNGADVDKANTDDDFSPTe 694

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2023156728  841 --EYLSDVEEGEDAMTGDTDkylgPQDLKELGDDSLPAEGYMGFSLGARSASPKVSSDRSYTLNR 903
Cdd:PLN03192   695 lrELLQKRELGHSITIVDSV----PADEPDLGRDGGSRPGRLQGTSSDNQCRPRVSIYKGHPLLR 755
PTZ00121 super family cl31754
MAEBL; Provisional
 2561-2996 2.49e-04

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.83  E-value: 2.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728 2561 RVDRTVKEAEEKlTEVSQFFRDKTEKLNDELQSPEKKQH---KKNGKEIHSSQSSASSSPEKVLLSELPSSGDEWSK--- 2634
Cdd:PTZ00121  1330 KADAAKKKAEEA-KKAAEAAKAEAEAAADEAEAAEEKAEaaeKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKkad 1408

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728 2635 -VKQYAHDGKcfpKVDE--RKASSLPSSPEKRifvQPAEDSKQTMEHKGSAQQtgvpevsqtgfqlkQSKLSSIRLKFEQ 2711
Cdd:PTZ00121  1409 eLKKAAAAKK---KADEakKKAEEKKKADEAK---KKAEEAKKADEAKKKAEE--------------AKKAEEAKKKAEE 1468

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728 2712 SISPRSKDVTQEEKKLDGQSKipvKKSQESKLPVYQFYSREKHAKQVEvidgstalqkEVKIQEDfvpgKAKAIEDFRAS 2791
Cdd:PTZ00121  1469 AKKADEAKKKAEEAKKADEAK---KKAEEAKKKADEAKKAAEAKKKAD----------EAKKAEE----AKKADEAKKAE 1531

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728 2792 DAQKRPEMSKGvvpeyfSEPQAKDLVYGSDSTAKGHWDKKIYRTWESPGTSNHQTQKEKLSHVLVPDTVKENHVDHAETK 2871
Cdd:PTZ00121  1532 EAKKADEAKKA------EEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEK 1605

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728 2872 TDKKSEFATVTEHKLAANGIH-SEEVK---ELTVKSPSKRVLYREFVVREGERNGEVADKISKRKEEIAVSHIPVRIVEE 2947
Cdd:PTZ00121  1606 KMKAEEAKKAEEAKIKAEELKkAEEEKkkvEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEE 1685

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*....
gi 2023156728 2948 KrtmldgvyelsakvsqsaviKEKVERQIDYMEDEKIKCSEIRKVTKQQ 2996
Cdd:PTZ00121  1686 D--------------------EKKAAEALKKEAEEAKKAEELKKKEAEE 1714
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
329-612 2.11e-62

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 216.74  E-value: 2.11e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  329 LLIQHNVPVDDVTNDYLTALHVAAHCGHYKVAKVLLDKKANPNAKALNGFTPLHIACKKNRIKVMELLLKHGASIQAVTE 408
Cdd:COG0666      6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  409 SGLTPIHVAAFMGHVNIVSQLMHHGASPNTTNVRGETALHMAARAGQTEVVRYLVQNGAQVEAKAKDDQTPLHISARLGK 488
Cdd:COG0666     86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  489 ADIVQQLLQQGASPNAATTSGYTPLHLSAREGHEDVASVLLDHGASLSIITKKGFTPLHVAAKYGKIEVANLLLQKNASP 568
Cdd:COG0666    166 LEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADL 245

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 2023156728  569 DASGKSGLTPLHVAAHYDNQKVALLLLDQGASPHASAKNGYTPL 612
Cdd:COG0666    246 NAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
528-793 2.84e-61

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 213.28  E-value: 2.84e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  528 LLDHGASLSIITKKGFTPLHVAAKYGKIEVANLLLQKNASPDASGKSGLTPLHVAAHYDNQKVALLLLDQGASPHASAKN 607
Cdd:COG0666      7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  608 GYTPLHIAAKKNQMDIATTLLEYGADANAVTRQGIAPVHLASQDGHVDMVSLLLTRNANVNLGNKSGLTPLHLAAQDDRV 687
Cdd:COG0666     87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  688 NVAEVLVNQGAAVDAQTKMGYTPLHVGCHYGNIKIVNFLLQHSAKVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAAPN 767
Cdd:COG0666    167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246

                          250       260
                   ....*....|....*....|....*.
gi 2023156728  768 ELTVNGNTALAIAKRLGYISVVDTLK 793
Cdd:COG0666    247 AKDKDGLTALLLAAAAGAALIVKLLL 272
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
168-447 1.49e-60

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 211.35  E-value: 1.49e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  168 LLLENDTKGKVRLPALHIAARKDDTKAAALLLQNDHNADVESKSGFTPLHIAAHYGNINVATLLLNRGAAVDFTARNDIT 247
Cdd:COG0666     10 LLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNT 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  248 PLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPLHCGARSGHEQVVEMLLDRGAPILSKTKNGLSPLHMATQGDHLNCV 327
Cdd:COG0666     90 LLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  328 QLLIQHNVPVDDVTNDYLTALHVAAHCGHYKVAKVLLDKKANPNAKALNGFTPLHIACKKNRIKVMELLLKHGASIQAVT 407
Cdd:COG0666    170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKD 249

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 2023156728  408 ESGLTPIHVAAFMGHVNIVSQLMHHGASPNTTNVRGETAL 447
Cdd:COG0666    250 KDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
UPA_2 pfam17809
UPA domain; The UPA domain is conserved in UNC5, PIDD, and Ankyrins. It has a beta sandwich ...
 1295-1424 2.55e-57

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: 195.38  E-value: 2.55e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728 1295 VPYMAKFVIFAKMNDPVESNLRCFCMTDDKVDKTLEQQENFEEVARSKDIEVLEGKPIYVDCYGNLAPLTKGGQQLVFNF 1374
Cdd:pfam17809    1 VPYLAKFVVFAKRYDPGEARLRCACMTDDGEDKTLEFHEGFTEVARSRDVEVLEGSPVSIELSGNLVPIKKKSQSRQMDF 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2023156728 1375 YAFKENRLPFSIKVRDTSQEPCGRLSFLKEPKTTKGLPQTAVCNLNITLP 1424
Cdd:pfam17809   81 KAFRENRLDGSVRVKDPSDPPKGLLSFMRDAKVDGGTVSQPLCTLNIVLP 130
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
3-282 5.59e-54

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 192.48  E-value: 5.59e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728    3 VLLMLLDYILRKMSDTNASYLRAARAGNLEKALDYLKSGVDINISNQNGLNALHLASKEGHVEVVSELIQRGASVDAATK 82
Cdd:COG0666     39 LLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDK 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728   83 KGNTALHIASLAGQAEVVKVLVTNRANVNAQSQNGFTPLYMAAQENHLEVVKFLLDNGASQSLATEDGFTPLAVALQQGH 162
Cdd:COG0666    119 DGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGH 198

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  163 DQVVSLLLEndtkgkvrlpalhiaarkddtkaaalllqndHNADVE--SKSGFTPLHIAAHYGNINVATLLLNRGAAVDF 240
Cdd:COG0666    199 LEIVKLLLE-------------------------------AGADVNakDNDGKTALDLAAENGNLEIVKLLLEAGADLNA 247

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 2023156728  241 TARNDITPLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPL 282
Cdd:COG0666    248 KDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
 969-1073 8.16e-48

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


Pssm-ID: 128514  Cd Length: 104  Bit Score: 167.14  E-value: 8.16e-48
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728   969 SSFLVSFMVDARGGSMRGSRHhGMRIIIPPRKCTAPTRITCRLVKRHKLASPPPMVEGEGLASRLVEMGPSGAQFLGPVI 1048
Cdd:smart00218    1 PSFLVSGTFDARGGRLRGPRT-GVRLIIPPGAIPQGTRYTCYLVVHKTLSTPPPLEEGETLLSPVVECGPHGALFLRPVI 79

                            90       100
                    ....*....|....*....|....*
gi 2023156728  1049 VEIPHFGSMRGKERELIVLRSENGE 1073
Cdd:smart00218   80 LEVPHCASLRPRDWEIVLLRSENGG 104
Death_ank3 cd08803
Death domain of Ankyrin-3; Death Domain (DD) of the human protein ankyrin-3 (ANK-3) and ...
 4038-4121 3.89e-46

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: 161.76  E-value: 3.89e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728 4038 ERTDIRMAIVADHLGLSWTELARELNFSVDEINQIRVENPNSLIAQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIV 4117
Cdd:cd08803      1 ERTDIRMAIVADHLGLSWTELARELNFSVDEINQIRVENPNSLIAQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIV 80


                   ....
gi 2023156728 4118 TLLE 4121
Cdd:cd08803     81 TLLE 84
ZU5 pfam00791
ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.
 973-1070 1.77e-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: 148.83  E-value: 1.77e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  973 VSFMVDARGGSMRGSrHHGMRIIIPPRKCTAPTRITCRLVKRHKLASPPPMVEGEGLASRLVEMGPSGAQFLGPVIVEIP 1052
Cdd:pfam00791    1 VSGLVDSRGGRLVLP-NSGVSLLIPPGAIPEGTRIECYLAVNRDESSRPPLEEGETLLSPVVECGPPGLKFLKPVILEVP 79

                           90
                   ....*....|....*...
gi 2023156728 1053 HFGSMRGKERELIVLRSE 1070
Cdd:pfam00791   80 HCASLRPEEWEIVLKRSD 97
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 540-793 2.07e-38

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 151.36  E-value: 2.07e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  540 KKGFTPLHVAAKYGKIEVANLLLQKNASPDASGKSGLTPLHVAAHY-----DNQKVALLLLDQGASPHASAKNGYTPLHI 614
Cdd:PHA03100    33 KKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIkynltDVKEIVKLLLEYGANVNAPDNNGITPLLY 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  615 AA--KKNQMDIATTLLEYGADANAVTRQGIAPVHLASQDGHVD--MVSLLLTRNANVNlgnksgltplhlaaQDDRVNVa 690
Cdd:PHA03100   113 AIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDIN--------------AKNRVNY- 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  691 evLVNQGAAVDAQTKMGYTPLHVGCHYGNIKIVNFLLQHSAKVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGaaPNELT 770
Cdd:PHA03100   178 --LLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNG--PSIKT 253

                          250       260
                   ....*....|....*....|...
gi 2023156728  771 VNGNTALAIAKRLGYISVVDTLK 793
Cdd:PHA03100   254 IIETLLYFKDKDLNTITKIKMLK 276
PHA03095 PHA03095
ankyrin-like protein; Provisional
 346-637 1.83e-36

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 146.71  E-value: 1.83e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  346 TALHVAAHCGHYKVAKV---LLDKKANPNAKALNGFTPLHI-ACKKNRIKVMELLLKHGASIQAVTESGLTPIHV--AAF 419
Cdd:PHA03095    49 TPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHLyLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVylSGF 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  420 MGHVNIVSQLMHHGASPNTTNVRGETALH--MAARAGQTEVVRYLVQNGAQVEAKAKDDQTPLHISARLGK--ADIVQQL 495
Cdd:PHA03095   129 NINPKVIRLLLRKGADVNALDLYGMTPLAvlLKSRNANVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKprARIVREL 208

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  496 LQQGASPNAATTSGYTPLHLSAReGHEDVASVLLDhgaslsiitkkgftplhvaakygkievanlLLQKNASPDASGKSG 575
Cdd:PHA03095   209 IRAGCDPAATDMLGNTPLHSMAT-GSSCKRSLVLP------------------------------LLIAGISINARNRYG 257

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2023156728  576 LTPLHVAAHYDNQKVALLLLDQGASPHASAKNGYTPLHIAAKKNQMDIATTLLEYGADANAV 637
Cdd:PHA03095   258 QTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETV 319
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 198-438 2.51e-34

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 139.41  E-value: 2.51e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  198 LLQNDHNADVESKSGFTPLHIAAHYGNINVATLLLNRGAAVDFTARNDITPLH-----VASKRGNANMVKLLLDRGAKID 272
Cdd:PHA03100    21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGANVN 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  273 AKTRDGLTPLHCGA--RSGHEQVVEMLLDRGAPILSKTKNGLSPLHMATQGDH--LNCVQLLIQHNVPVDDVTN-DYlta 347
Cdd:PHA03100   101 APDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKNRvNY--- 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  348 lhvaahcghykvakvLLDKKANPNAKALNGFTPLHIACKKNRIKVMELLLKHGASIQAVTESGLTPIHVAAFMGHVNIVS 427
Cdd:PHA03100   178 ---------------LLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFK 242

                          250
                   ....*....|.
gi 2023156728  428 QLMHHGASPNT 438
Cdd:PHA03100   243 LLLNNGPSIKT 253
PHA03095 PHA03095
ankyrin-like protein; Provisional
 16-300 1.84e-27

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 119.74  E-value: 1.84e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728   16 SDTNASYLRAARAGN--LEKALDYLKSGVDINISNQNGLNALHLASKEGH---VEVVSELIQRGASVDAATKKGNTALHI 90
Cdd:PHA03095    10 IMEAALYDYLLNASNvtVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHL 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728   91 -ASLAGQAEVVKVLVTNRANVNAQSQNGFTPL--YMAAQENHLEVVKFLLDNGASQSLATEDGFTPLAVALQQGH--DQV 165
Cdd:PHA03095    90 yLYNATTLDVIKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanVEL 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  166 VSLLLEND----TKGKVRLPALHIAAR--KDDTKAAALLLQNDHNADVESKSGFTPLHIAAHYG---NINVATLLLNrGA 236
Cdd:PHA03095   170 LRLLIDAGadvyAVDDRFRSLLHHHLQsfKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSsckRSLVLPLLIA-GI 248

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2023156728  237 AVDFTARNDITPLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPLHCGARSGHEQVVEMLLDR 300
Cdd:PHA03095   249 SINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAK 312
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
 4037-4123 2.64e-25

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: 102.49  E-value: 2.64e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  4037 CERTDIRMAIVADH-LGLSWTELARELNFSVDEINQIRVENPNSLIAQSFMLLKKWVTRDGKNATTDALTSVLTKINRID 4115
Cdd:smart00005    1 PELTRQKLAKLLDHpLGLDWRELARKLGLSEADIDQIRTEAPRDLAEQSVQLLRLWEQREGKNATLGTLLEALRKMGRDD 80


                    ....*...
gi 2023156728  4116 IVTLLEGP 4123
Cdd:smart00005   81 AVELLRSE 88
Ank_2 pfam12796
Ankyrin repeats (3 copies);
55-142 3.70e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 96.34  E-value: 3.70e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728   55 LHLASKEGHVEVVSELIQRGASVDAATKKGNTALHIASLAGQAEVVKVLVtNRANVNAQSqNGFTPLYMAAQENHLEVVK 134
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78


                   ....*...
gi 2023156728  135 FLLDNGAS 142
Cdd:pfam12796   79 LLLEKGAD 86
Ank_2 pfam12796
Ankyrin repeats (3 copies);
348-440 2.59e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 94.03  E-value: 2.59e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  348 LHVAAHCGHYKVAKVLLDKKANPNAKALNGFTPLHIACKKNRIKVMELLLKHGAsiQAVTESGLTPIHVAAFMGHVNIVS 427
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 2023156728  428 QLMHHGASPNTTN 440
Cdd:pfam12796   79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
282-373 1.07e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.10  E-value: 1.07e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  282 LHCGARSGHEQVVEMLLDRGAPILSKTKNGLSPLHMATQGDHLNCVQLLIQHNVPvdDVTNDYLTALHVAAHCGHYKVAK 361
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 2023156728  362 VLLDKKANPNAK 373
Cdd:pfam12796   79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
646-736 1.23e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.40  E-value: 1.23e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  646 HLASQDGHVDMVSLLLTRNANVNLGNKSGLTPLHLAAQDDRVNVAEVLVNQgAAVDAQTKmGYTPLHVGCHYGNIKIVNF 725
Cdd:pfam12796    2 HLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKL 79

                           90
                   ....*....|.
gi 2023156728  726 LLQHSAKVNAK 736
Cdd:pfam12796   80 LLEKGADINVK 90
Death pfam00531
Death domain;
4043-4121 8.89e-17

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 78.18  E-value: 8.89e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728 4043 RMAIVADH---LGLSWTELARELNFSVDEINQIRVENPNsLIAQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIVTL 4119
Cdd:pfam00531    3 QLDRLLDPpppLGKDWRELARKLGLSENEIDEIESENPR-LRSQTYELLRLWEQREGKNATVGTLLEALRKLGRRDAAEK 81


                   ..
gi 2023156728 4120 LE 4121
Cdd:pfam00531   82 IQ 83
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 351-563 1.25e-14

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: 80.90  E-value: 1.25e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  351 AAHCGHYKVAKVLLD--KKANPNAKALNGFTPLHIACKKNRIK-VMELLLKHGASIqavtESGLTPIHVAAfMGHVNIVS 427
Cdd:TIGR00870   24 AAERGDLASVYRDLEepKKLNINCPDRLGRSALFVAAIENENLeLTELLLNLSCRG----AVGDTLLHAIS-LEYVDAVE 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  428 QLM-----HHGASPNTTNV---------RGETALHMAARAGQTEVVRYLVQNGAQVEAKAKDD--------------QTP 479
Cdd:TIGR00870   99 AILlhllaAFRKSGPLELAndqytseftPGITALHLAAHRQNYEIVKLLLERGASVPARACGDffvksqgvdsfyhgESP 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  480 LHISARLGKADIVQQLLQQGASPNAATTSGYTPLHLSAREGHEDVA---------SVLLDHGA------SLSIITK-KGF 543
Cdd:TIGR00870  179 LNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVMENEFKAEyeelscqmyNFALSLLDklrdskELEVILNhQGL 258

                          250       260
                   ....*....|....*....|
gi 2023156728  544 TPLHVAAKYGKIEVANLLLQ 563
Cdd:TIGR00870  259 TPLKLAAKEGRIVLFRLKLA 278
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 544-728 6.04e-14

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 78.52  E-value: 6.04e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  544 TPLHVAAKYGKIE-VANLLLQKNASPDASGKSGLTPLHVAAHYDNQKVALLLLDqgASPH-------ASAKNGYTPLHIA 615
Cdd:cd22192     19 SPLLLAAKENDVQaIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPElvnepmtSDLYQGETALHIA 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  616 AKKNQMDIATTLLEYGADANAVTRQGIA--------------PVHLASQDGHVDMVSLLLTRNANVNLGNKSGLTPLH-L 680
Cdd:cd22192     97 VVNQNLNLVRELIARGADVVSPRATGTFfrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHiL 176

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2023156728  681 AAQDDRVNVAEV---LVNQGAAVDAQT------KMGYTPLHVGCHYGNIKIVNFLLQ 728
Cdd:cd22192    177 VLQPNKTFACQMydlILSYDKEDDLQPldlvpnNQGLTPFKLAAKEGNIVMFQHLVQ 233
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 119-332 5.46e-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: 75.43  E-value: 5.46e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  119 TPLYMAAQENHLEVVKFLLDNgasqslATEDGFTplavalqqghdqvvslllendtKGKVRLPALHIAARKDDTKAAALL 198
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLLKC------PSCDLFQ----------------------RGALGETALHVAALYDNLEAAVVL 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  199 LQNDH---NADVESK--SGFTPLHIAAHYGNINVATLLLNRGAAVdFTARNDIT---------------PLHVASKRGNA 258
Cdd:cd22192     71 MEAAPelvNEPMTSDlyQGETALHIAVVNQNLNLVRELIARGADV-VSPRATGTffrpgpknliyygehPLSFAACVGNE 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  259 NMVKLLLDRGAKIDAKTRDGLTPLH-----------CgarsgheQVVEMLL-----DRGAPiLSKTKN--GLSPLHMATQ 320
Cdd:cd22192    150 EIVRLLIEHGADIRAQDSLGNTVLHilvlqpnktfaC-------QMYDLILsydkeDDLQP-LDLVPNnqGLTPFKLAAK 221

                          250
                   ....*....|..
gi 2023156728  321 GDHLNCVQLLIQ 332
Cdd:cd22192    222 EGNIVMFQHLVQ 233
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 440-564 6.68e-13

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 75.18  E-value: 6.68e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  440 NVRGETALHMAARAGQTEVVRYLVQNGAQVEAKAKDD--------------QTPLHISARLGKADIVQQLLQQGASPNAA 505
Cdd:cd22194    138 AYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVffnpkykhegfyfgETPLALAACTNQPEIVQLLMEKESTDITS 217

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2023156728  506 TTS-GYTPLH---LSAREGHEDVASV-------LLDH-GASLSIIT-KKGFTPLHVAAKYGKIEVANLLLQK 564
Cdd:cd22194    218 QDSrGNTVLHalvTVAEDSKTQNDFVkrmydmiLLKSeNKNLETIRnNEGLTPLQLAAKMGKAEILKYILSR 289
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 75-234 6.39e-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: 72.10  E-value: 6.39e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728   75 ASVDAATKKGNTALHIASLAGQAEVVKVLVTNRANVNAQSQNGF--------------TPLYMAAQENHLEVVKFLLDNG 140
Cdd:cd22194    132 AEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVFfnpkykhegfyfgeTPLALAACTNQPEIVQLLMEKE 211

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  141 asqslatedgftPLAVALQqghdqvvslllenDTKGKVRLPALHIAArkDDTKAAA--------LLLQNDHNADVE---S 209
Cdd:cd22194    212 ------------STDITSQ-------------DSRGNTVLHALVTVA--EDSKTQNdfvkrmydMILLKSENKNLEtirN 264

                          170       180
                   ....*....|....*....|....*
gi 2023156728  210 KSGFTPLHIAAHYGNINVATLLLNR 234
Cdd:cd22194    265 NEGLTPLQLAAKMGKAEILKYILSR 289
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 112-419 3.19e-09

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 63.56  E-value: 3.19e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  112 AQSQNGFTPlymAAQENHLEVVKFLLDNGASQSLATED--GFTPLAVALQQG-HDQVVSLLLENDTKGKVRLPALHiAAR 188
Cdd:TIGR00870   15 SDEEKAFLP---AAERGDLASVYRDLEEPKKLNINCPDrlGRSALFVAAIENeNLELTELLLNLSCRGAVGDTLLH-AIS 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  189 KDDTKAAALLLQndHNADVESKSGFTPLHIAAHYGninvatlllnrgaavDFTArnDITPLHVASKRGNANMVKLLLDRG 268
Cdd:TIGR00870   91 LEYVDAVEAILL--HLLAAFRKSGPLELANDQYTS---------------EFTP--GITALHLAAHRQNYEIVKLLLERG 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  269 AKIDAKT--------------RDGLTPLHCGARSGHEQVVEMLLDRGAPILSKTKNGLSPLHMAtqgdhlncvqlliqhn 334
Cdd:TIGR00870  152 ASVPARAcgdffvksqgvdsfYHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLL---------------- 215

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  335 VPVDDVTNDYLTalhVAAHCghYKVAKVLLDKKANPNAKAL----NGFTPLHIACKKNRIKVMELLLKHGASIQAVTESG 410
Cdd:TIGR00870  216 VMENEFKAEYEE---LSCQM--YNFALSLLDKLRDSKELEVilnhQGLTPLKLAAKEGRIVLFRLKLAIKYKQKKFVAWP 290


                   ....*....
gi 2023156728  411 LTPIHVAAF 419
Cdd:TIGR00870  291 NGQQLLSLY 299
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 376-403 1.42e-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: 47.20  E-value: 1.42e-06
                            10        20
                    ....*....|....*....|....*...
gi 2023156728   376 NGFTPLHIACKKNRIKVMELLLKHGASI 403
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 691-903 2.00e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.49  E-value: 2.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  691 EVLVNQGAAVDAQTKMGYTPLHVGCHYGNIKIVNFLLQHSAKVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAAPNELT 770
Cdd:PLN03192   542 EELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHA 621

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  771 vnGNTALAIAKRLGYISVVDT-----LKVVTEE----TMTTITVTEKHKmnvpeTMNEVLDMSDDEVRKANAPEILSDA- 840
Cdd:PLN03192   622 --AGDLLCTAAKRNDLTAMKEllkqgLNVDSEDhqgaTALQVAMAEDHV-----DMVRLLIMNGADVDKANTDDDFSPTe 694

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2023156728  841 --EYLSDVEEGEDAMTGDTDkylgPQDLKELGDDSLPAEGYMGFSLGARSASPKVSSDRSYTLNR 903
Cdd:PLN03192   695 lrELLQKRELGHSITIVDSV----PADEPDLGRDGGSRPGRLQGTSSDNQCRPRVSIYKGHPLLR 755
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 509-748 3.14e-06

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 53.55  E-value: 3.14e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  509 GYTPLHLSAREG-HEDVASVLLDHGASLSIitkkGFTPLHVAAK--YGKIEVANLLLQKNASPDASGK-----------S 574
Cdd:TIGR00870   52 GRSALFVAAIENeNLELTELLLNLSCRGAV----GDTLLHAISLeyVDAVEAILLHLLAAFRKSGPLElandqytseftP 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  575 GLTPLHVAAHYDNQKVALLLLDQGASPHASAK--------------NGYTPLHIAAKKNQMDIATTLLEYGADANAVTRQ 640
Cdd:TIGR00870  128 GITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADSL 207

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  641 GIAPVHLASqdghvdMVSLLLTRNANVNLGNKSGLTPlHLAAQDDRVNVAEVLVNQgaavdaqtkmGYTPLHVGCHYGNI 720
Cdd:TIGR00870  208 GNTLLHLLV------MENEFKAEYEELSCQMYNFALS-LLDKLRDSKELEVILNHQ----------GLTPLKLAAKEGRI 270

                          250       260       270
                   ....*....|....*....|....*....|.
gi 2023156728  721 KIVNFLLQ---HSAKVNAKTkngYTPLHQAA 748
Cdd:TIGR00870  271 VLFRLKLAikyKQKKFVAWP---NGQQLLSL 298
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 244-273 9.29e-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: 44.89  E-value: 9.29e-06
                            10        20        30
                    ....*....|....*....|....*....|
gi 2023156728   244 NDITPLHVASKRGNANMVKLLLDRGAKIDA 273
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 116-142 1.50e-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: 44.50  E-value: 1.50e-05
                            10        20
                    ....*....|....*....|....*..
gi 2023156728   116 NGFTPLYMAAQENHLEVVKFLLDNGAS 142
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 51-234 2.22e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 50.85  E-value: 2.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728   51 GLNALHLASKEgHVEVVSELIQRGASVDAATK--------------KGNTALHIASLAGQAEVVKVLVTNRANVNA---- 112
Cdd:TIGR00870   82 GDTLLHAISLE-YVDAVEAILLHLLAAFRKSGplelandqytseftPGITALHLAAHRQNYEIVKLLLERGASVPAracg 160

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  113 ------QSQNGF----TPLYMAAQENHLEVVKFLLDNGASQSLATEDGFTPLavalqqgHDQVVslllENDTKGK----- 177
Cdd:TIGR00870  161 dffvksQGVDSFyhgeSPLNAAACLGSPSIVALLSEDPADILTADSLGNTLL-------HLLVM----ENEFKAEyeels 229

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2023156728  178 --VRLPALHIAARKDDTKAAALLLQNDhnadvesksGFTPLHIAAHYGNINVATLLLNR 234
Cdd:TIGR00870  230 cqMYNFALSLLDKLRDSKELEVILNHQ---------GLTPLKLAAKEGRIVLFRLKLAI 279
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 739-768 5.32e-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: 5.32e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 2023156728   739 NGYTPLHQAAQQGHTHIINVLLQHGAAPNE 768
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00121 PTZ00121
MAEBL; Provisional
 2561-2996 2.49e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.83  E-value: 2.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728 2561 RVDRTVKEAEEKlTEVSQFFRDKTEKLNDELQSPEKKQH---KKNGKEIHSSQSSASSSPEKVLLSELPSSGDEWSK--- 2634
Cdd:PTZ00121  1330 KADAAKKKAEEA-KKAAEAAKAEAEAAADEAEAAEEKAEaaeKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKkad 1408

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728 2635 -VKQYAHDGKcfpKVDE--RKASSLPSSPEKRifvQPAEDSKQTMEHKGSAQQtgvpevsqtgfqlkQSKLSSIRLKFEQ 2711
Cdd:PTZ00121  1409 eLKKAAAAKK---KADEakKKAEEKKKADEAK---KKAEEAKKADEAKKKAEE--------------AKKAEEAKKKAEE 1468

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728 2712 SISPRSKDVTQEEKKLDGQSKipvKKSQESKLPVYQFYSREKHAKQVEvidgstalqkEVKIQEDfvpgKAKAIEDFRAS 2791
Cdd:PTZ00121  1469 AKKADEAKKKAEEAKKADEAK---KKAEEAKKKADEAKKAAEAKKKAD----------EAKKAEE----AKKADEAKKAE 1531

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728 2792 DAQKRPEMSKGvvpeyfSEPQAKDLVYGSDSTAKGHWDKKIYRTWESPGTSNHQTQKEKLSHVLVPDTVKENHVDHAETK 2871
Cdd:PTZ00121  1532 EAKKADEAKKA------EEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEK 1605

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728 2872 TDKKSEFATVTEHKLAANGIH-SEEVK---ELTVKSPSKRVLYREFVVREGERNGEVADKISKRKEEIAVSHIPVRIVEE 2947
Cdd:PTZ00121  1606 KMKAEEAKKAEEAKIKAEELKkAEEEKkkvEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEE 1685

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*....
gi 2023156728 2948 KrtmldgvyelsakvsqsaviKEKVERQIDYMEDEKIKCSEIRKVTKQQ 2996
Cdd:PTZ00121  1686 D--------------------EKKAAEALKKEAEEAKKAEELKKKEAEE 1714
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
329-612 2.11e-62

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 216.74  E-value: 2.11e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  329 LLIQHNVPVDDVTNDYLTALHVAAHCGHYKVAKVLLDKKANPNAKALNGFTPLHIACKKNRIKVMELLLKHGASIQAVTE 408
Cdd:COG0666      6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  409 SGLTPIHVAAFMGHVNIVSQLMHHGASPNTTNVRGETALHMAARAGQTEVVRYLVQNGAQVEAKAKDDQTPLHISARLGK 488
Cdd:COG0666     86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  489 ADIVQQLLQQGASPNAATTSGYTPLHLSAREGHEDVASVLLDHGASLSIITKKGFTPLHVAAKYGKIEVANLLLQKNASP 568
Cdd:COG0666    166 LEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADL 245

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 2023156728  569 DASGKSGLTPLHVAAHYDNQKVALLLLDQGASPHASAKNGYTPL 612
Cdd:COG0666    246 NAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
390-678 6.14e-62

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 215.20  E-value: 6.14e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  390 IKVMELLLKHGASIQAVTESGLTPIHVAAFMGHVNIVSQLMHHGASPNTTNVRGETALHMAARAGQTEVVRYLVQNGAQV 469
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  470 EAKAKDDQTPLHISARLGKADIVQQLLQQGASPNAATTSGYTPLHLSAREGHEDVASVLLDHGASLSIITKKGFTPLHVA 549
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  550 AKYGKIEVANLLLQKNASPDASGKSGLTPLHVAAHYDNQKVALLLLDQGASPHASAKNGYTPLHIAAKKNQMDIATTLLE 629
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 2023156728  630 YGADANAVTRQGIAPVHLASQDGHVDMVSLLLTRNANVNLGNKSGLTPL 678
Cdd:COG0666    241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
358-643 1.72e-61

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 214.05  E-value: 1.72e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  358 KVAKVLLDKKANPNAKALNGFTPLHIACKKNRIKVMELLLKHGASIQAVTESGLTPIHVAAFMGHVNIVSQLMHHGASPN 437
Cdd:COG0666      2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  438 TTNVRGETALHMAARAGQTEVVRYLVQNGAQVEAKAKDDQTPLHISARLGKADIVQQLLQQGASPNAATTSGYTPLHLSA 517
Cdd:COG0666     82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  518 REGHEDVASVLLDHGASLSIITKKGFTPLHVAAKYGKIEVANLLLQKNASPDASGKSGLTPLHVAAHYDNQKVALLLLDQ 597
Cdd:COG0666    162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 2023156728  598 GASPHASAKNGYTPLHIAAKKNQMDIATTLLEYGADANAVTRQGIA 643
Cdd:COG0666    242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
293-579 2.23e-61

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 213.66  E-value: 2.23e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  293 VVEMLLDRGAPILSKTKNGLSPLHMATQGDHLNCVQLLIQHNVPVDDVTNDYLTALHVAAHCGHYKVAKVLLDKKANPNA 372
Cdd:COG0666      3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  373 KALNGFTPLHIACKKNRIKVMELLLKHGASIQAVTESGLTPIHVAAFMGHVNIVSQLMHHGASPNTTNVRGETALHMAAR 452
Cdd:COG0666     83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  453 AGQTEVVRYLVQNGAQVEAKAKDDQTPLHISARLGKADIVQQLLQQGASPNAATTSGYTPLHLSAREGHEDVASVLLDHG 532
Cdd:COG0666    163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 2023156728  533 ASLSIITKKGFTPLHVAAKYGKIEVANLLLQKNASPDASGKSGLTPL 579
Cdd:COG0666    243 ADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
528-793 2.84e-61

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 213.28  E-value: 2.84e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  528 LLDHGASLSIITKKGFTPLHVAAKYGKIEVANLLLQKNASPDASGKSGLTPLHVAAHYDNQKVALLLLDQGASPHASAKN 607
Cdd:COG0666      7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  608 GYTPLHIAAKKNQMDIATTLLEYGADANAVTRQGIAPVHLASQDGHVDMVSLLLTRNANVNLGNKSGLTPLHLAAQDDRV 687
Cdd:COG0666     87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  688 NVAEVLVNQGAAVDAQTKMGYTPLHVGCHYGNIKIVNFLLQHSAKVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAAPN 767
Cdd:COG0666    167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246

                          250       260
                   ....*....|....*....|....*.
gi 2023156728  768 ELTVNGNTALAIAKRLGYISVVDTLK 793
Cdd:COG0666    247 AKDKDGLTALLLAAAAGAALIVKLLL 272
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
168-447 1.49e-60

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 211.35  E-value: 1.49e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  168 LLLENDTKGKVRLPALHIAARKDDTKAAALLLQNDHNADVESKSGFTPLHIAAHYGNINVATLLLNRGAAVDFTARNDIT 247
Cdd:COG0666     10 LLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNT 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  248 PLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPLHCGARSGHEQVVEMLLDRGAPILSKTKNGLSPLHMATQGDHLNCV 327
Cdd:COG0666     90 LLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  328 QLLIQHNVPVDDVTNDYLTALHVAAHCGHYKVAKVLLDKKANPNAKALNGFTPLHIACKKNRIKVMELLLKHGASIQAVT 407
Cdd:COG0666    170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKD 249

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 2023156728  408 ESGLTPIHVAAFMGHVNIVSQLMHHGASPNTTNVRGETAL 447
Cdd:COG0666    250 KDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
195-480 2.48e-60

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 210.58  E-value: 2.48e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  195 AALLLQNDHNADVESKSGFTPLHIAAHYGNINVATLLLNRGAAVDFTARNDITPLHVASKRGNANMVKLLLDRGAKIDAK 274
Cdd:COG0666      4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  275 TRDGLTPLHCGARSGHEQVVEMLLDRGAPILSKTKNGLSPLHMATQGDHLNCVQLLIQHNVPVDDVTNDYLTALHVAAHC 354
Cdd:COG0666     84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  355 GHYKVAKVLLDKKANPNAKALNGFTPLHIACKKNRIKVMELLLKHGASIQAVTESGLTPIHVAAFMGHVNIVSQLMHHGA 434
Cdd:COG0666    164 GNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 2023156728  435 SPNTTNVRGETALHMAARAGQTEVVRYLVQNGAQVEAKAKDDQTPL 480
Cdd:COG0666    244 DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
225-513 3.75e-60

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 210.20  E-value: 3.75e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  225 INVATLLLNRGAAVDFTARNDITPLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPLHCGARSGHEQVVEMLLDRGAPI 304
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  305 LSKTKNGLSPLHMATQGDHLNCVQLLIQHNVPVDDVTNDYLTALHVAAHCGHYKVAKVLLDKKANPNAKALNGFTPLHIA 384
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  385 CKKNRIKVMELLLKHGASIQAVTESGLTPIHVAAFMGHVNIVSQLMHHGASPNTTNVRGETALHMAARAGQTEVVRYLVQ 464
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 2023156728  465 NGAQVEAKAKDDQTPLHISARLGKADIVQQLLQQGASPNAATTSGYTPL 513
Cdd:COG0666    241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
489-777 7.01e-60

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 209.43  E-value: 7.01e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  489 ADIVQQLLQQGASPNAATTSGYTPLHLSAREGHEDVASVLLDHGASLSIITKKGFTPLHVAAKYGKIEVANLLLQKNASP 568
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  569 DASGKSGLTPLHVAAHYDNQKVALLLLDQGASPHASAKNGYTPLHIAAKKNQMDIATTLLEYGADANAVTRQGIAPVHLA 648
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  649 SQDGHVDMVSLLLTRNANVNLGNKSGLTPLHLAAQDDRVNVAEVLVNQGAAVDAQTKMGYTPLHVGCHYGNIKIVNFLLQ 728
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 2023156728  729 HSAKVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAAPNELTVNGNTAL 777
Cdd:COG0666    241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
258-546 1.34e-59

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 208.65  E-value: 1.34e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  258 ANMVKLLLDRGAKIDAKTRDGLTPLHCGARSGHEQVVEMLLDRGAPILSKTKNGLSPLHMATQGDHLNCVQLLIQHNVPV 337
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  338 DDVTNDYLTALHVAAHCGHYKVAKVLLDKKANPNAKALNGFTPLHIACKKNRIKVMELLLKHGASIQAVTESGLTPIHVA 417
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  418 AFMGHVNIVSQLMHHGASPNTTNVRGETALHMAARAGQTEVVRYLVQNGAQVEAKAKDDQTPLHISARLGKADIVQQLLQ 497
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 2023156728  498 QGASPNAATTSGYTPLHLSAREGHEDVASVLLDHGASLSIITKKGFTPL 546
Cdd:COG0666    241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
473-744 9.99e-59

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 205.96  E-value: 9.99e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  473 AKDDQTPLHISARLGKADIVQQLLQQGASPNAATTSGYTPLHLSAREGHEDVASVLLDHGASLSIITKKGFTPLHVAAKY 552
Cdd:COG0666     18 LLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARN 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  553 GKIEVANLLLQKNASPDASGKSGLTPLHVAAHYDNQKVALLLLDQGASPHASAKNGYTPLHIAAKKNQMDIATTLLEYGA 632
Cdd:COG0666     98 GDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  633 DANAVTRQGIAPVHLASQDGHVDMVSLLLTRNANVNLGNKSGLTPLHLAAQDDRVNVAEVLVNQGAAVDAQTKMGYTPLH 712
Cdd:COG0666    178 DVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALL 257

                          250       260       270
                   ....*....|....*....|....*....|..
gi 2023156728  713 VGCHYGNIKIVNFLLQHSAKVNAKTKNGYTPL 744
Cdd:COG0666    258 LAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
423-711 2.51e-57

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 202.11  E-value: 2.51e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  423 VNIVSQLMHHGASPNTTNVRGETALHMAARAGQTEVVRYLVQNGAQVEAKAKDDQTPLHISARLGKADIVQQLLQQGASP 502
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  503 NAATTSGYTPLHLSAREGHEDVASVLLDHGASLSIITKKGFTPLHVAAKYGKIEVANLLLQKNASPDASGKSGLTPLHVA 582
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  583 AHYDNQKVALLLLDQGASPHASAKNGYTPLHIAAKKNQMDIATTLLEYGADANAVTRQGIAPVHLASQDGHVDMVSLLLT 662
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 2023156728  663 RNANVNLGNKSGLTPLHLAAQDDRVNVAEVLVNQGAAVDAQTKMGYTPL 711
Cdd:COG0666    241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
UPA_2 pfam17809
UPA domain; The UPA domain is conserved in UNC5, PIDD, and Ankyrins. It has a beta sandwich ...
 1295-1424 2.55e-57

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: 195.38  E-value: 2.55e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728 1295 VPYMAKFVIFAKMNDPVESNLRCFCMTDDKVDKTLEQQENFEEVARSKDIEVLEGKPIYVDCYGNLAPLTKGGQQLVFNF 1374
Cdd:pfam17809    1 VPYLAKFVVFAKRYDPGEARLRCACMTDDGEDKTLEFHEGFTEVARSRDVEVLEGSPVSIELSGNLVPIKKKSQSRQMDF 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2023156728 1375 YAFKENRLPFSIKVRDTSQEPCGRLSFLKEPKTTKGLPQTAVCNLNITLP 1424
Cdd:pfam17809   81 KAFRENRLDGSVRVKDPSDPPKGLLSFMRDAKVDGGTVSQPLCTLNIVLP 130
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
4-348 4.76e-55

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 195.56  E-value: 4.76e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728    4 LLMLLDYILRKMSDTNASYLRAARAGNLEKALDYLKSGVDINISNQNGLNALHLASKEGHVEVVSELIQRGASVDAATKK 83
Cdd:COG0666      7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728   84 GNTALHIASLAGQAEVVKVLVTNRANVNAQSQNGFTPLYMAAQENHLEVVKFLLDNGAsqslatedgftplavalqqghd 163
Cdd:COG0666     87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGA---------------------- 144

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  164 qvvslllendtkgkvrlpalhiaarkddtkaaalllqndhNADVESKSGFTPLHIAAHYGNINVATLLLNRGAAVDFTAR 243
Cdd:COG0666    145 ----------------------------------------DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN 184

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  244 NDITPLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPLHCGARSGHEQVVEMLLDRGAPILSKTKNGLSPLHMATQGDH 323
Cdd:COG0666    185 DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGA 264

                          330       340
                   ....*....|....*....|....*
gi 2023156728  324 LNCVQLLIQHNVPVDDVTNDYLTAL 348
Cdd:COG0666    265 ALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
555-793 1.02e-54

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 194.40  E-value: 1.02e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  555 IEVANLLLQKNASPDASGKSGLTPLHVAAHYDNQKVALLLLDQGASPHASAKNGYTPLHIAAKKNQMDIATTLLEYGADA 634
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  635 NAVTRQGIAPVHLASQDGHVDMVSLLLTRNANVNLGNKSGLTPLHLAAQDDRVNVAEVLVNQGAAVDAQTKMGYTPLHVG 714
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2023156728  715 CHYGNIKIVNFLLQHSAKVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAAPNELTVNGNTALAIAKRLGYISVVDTLK 793
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
3-282 5.59e-54

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 192.48  E-value: 5.59e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728    3 VLLMLLDYILRKMSDTNASYLRAARAGNLEKALDYLKSGVDINISNQNGLNALHLASKEGHVEVVSELIQRGASVDAATK 82
Cdd:COG0666     39 LLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDK 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728   83 KGNTALHIASLAGQAEVVKVLVTNRANVNAQSQNGFTPLYMAAQENHLEVVKFLLDNGASQSLATEDGFTPLAVALQQGH 162
Cdd:COG0666    119 DGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGH 198

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  163 DQVVSLLLEndtkgkvrlpalhiaarkddtkaaalllqndHNADVE--SKSGFTPLHIAAHYGNINVATLLLNRGAAVDF 240
Cdd:COG0666    199 LEIVKLLLE-------------------------------AGADVNakDNDGKTALDLAAENGNLEIVKLLLEAGADLNA 247

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 2023156728  241 TARNDITPLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPL 282
Cdd:COG0666    248 KDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-216 3.44e-49

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 178.61  E-value: 3.44e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728    1 MQVLLMLLDYILRKMSDTNASYLRAARAGNLEKALDYLKSGVDINISNQNGLNALHLASKEGHVEVVSELIQRGASVDAA 80
Cdd:COG0666     70 ALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQ 149

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728   81 TKKGNTALHIASLAGQAEVVKVLVTNRANVNAQSQNGFTPLYMAAQENHLEVVKFLLDNGASQSLATEDGFTPLAVALQQ 160
Cdd:COG0666    150 DNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAEN 229

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  161 GHDQVVSLLLE----NDTKGKVRLPALHIAARKDDTKAAALLLQNDHNADVESKSGFTPL 216
Cdd:COG0666    230 GNLEIVKLLLEagadLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
 969-1073 8.16e-48

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


Pssm-ID: 128514  Cd Length: 104  Bit Score: 167.14  E-value: 8.16e-48
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728   969 SSFLVSFMVDARGGSMRGSRHhGMRIIIPPRKCTAPTRITCRLVKRHKLASPPPMVEGEGLASRLVEMGPSGAQFLGPVI 1048
Cdd:smart00218    1 PSFLVSGTFDARGGRLRGPRT-GVRLIIPPGAIPQGTRYTCYLVVHKTLSTPPPLEEGETLLSPVVECGPHGALFLRPVI 79

                            90       100
                    ....*....|....*....|....*
gi 2023156728  1049 VEIPHFGSMRGKERELIVLRSENGE 1073
Cdd:smart00218   80 LEVPHCASLRPRDWEIVLLRSENGG 104
Death_ank3 cd08803
Death domain of Ankyrin-3; Death Domain (DD) of the human protein ankyrin-3 (ANK-3) and ...
 4038-4121 3.89e-46

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: 161.76  E-value: 3.89e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728 4038 ERTDIRMAIVADHLGLSWTELARELNFSVDEINQIRVENPNSLIAQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIV 4117
Cdd:cd08803      1 ERTDIRMAIVADHLGLSWTELARELNFSVDEINQIRVENPNSLIAQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIV 80


                   ....
gi 2023156728 4118 TLLE 4121
Cdd:cd08803     81 TLLE 84
ZU5 pfam00791
ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.
 973-1070 1.77e-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: 148.83  E-value: 1.77e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  973 VSFMVDARGGSMRGSrHHGMRIIIPPRKCTAPTRITCRLVKRHKLASPPPMVEGEGLASRLVEMGPSGAQFLGPVIVEIP 1052
Cdd:pfam00791    1 VSGLVDSRGGRLVLP-NSGVSLLIPPGAIPEGTRIECYLAVNRDESSRPPLEEGETLLSPVVECGPPGLKFLKPVILEVP 79

                           90
                   ....*....|....*...
gi 2023156728 1053 HFGSMRGKERELIVLRSE 1070
Cdd:pfam00791   80 HCASLRPEEWEIVLKRSD 97
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 540-793 2.07e-38

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 151.36  E-value: 2.07e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  540 KKGFTPLHVAAKYGKIEVANLLLQKNASPDASGKSGLTPLHVAAHY-----DNQKVALLLLDQGASPHASAKNGYTPLHI 614
Cdd:PHA03100    33 KKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIkynltDVKEIVKLLLEYGANVNAPDNNGITPLLY 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  615 AA--KKNQMDIATTLLEYGADANAVTRQGIAPVHLASQDGHVD--MVSLLLTRNANVNlgnksgltplhlaaQDDRVNVa 690
Cdd:PHA03100   113 AIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDIN--------------AKNRVNY- 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  691 evLVNQGAAVDAQTKMGYTPLHVGCHYGNIKIVNFLLQHSAKVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGaaPNELT 770
Cdd:PHA03100   178 --LLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNG--PSIKT 253

                          250       260
                   ....*....|....*....|...
gi 2023156728  771 VNGNTALAIAKRLGYISVVDTLK 793
Cdd:PHA03100   254 IIETLLYFKDKDLNTITKIKMLK 276
PHA03095 PHA03095
ankyrin-like protein; Provisional
 346-637 1.83e-36

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 146.71  E-value: 1.83e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  346 TALHVAAHCGHYKVAKV---LLDKKANPNAKALNGFTPLHI-ACKKNRIKVMELLLKHGASIQAVTESGLTPIHV--AAF 419
Cdd:PHA03095    49 TPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHLyLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVylSGF 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  420 MGHVNIVSQLMHHGASPNTTNVRGETALH--MAARAGQTEVVRYLVQNGAQVEAKAKDDQTPLHISARLGK--ADIVQQL 495
Cdd:PHA03095   129 NINPKVIRLLLRKGADVNALDLYGMTPLAvlLKSRNANVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKprARIVREL 208

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  496 LQQGASPNAATTSGYTPLHLSAReGHEDVASVLLDhgaslsiitkkgftplhvaakygkievanlLLQKNASPDASGKSG 575
Cdd:PHA03095   209 IRAGCDPAATDMLGNTPLHSMAT-GSSCKRSLVLP------------------------------LLIAGISINARNRYG 257

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2023156728  576 LTPLHVAAHYDNQKVALLLLDQGASPHASAKNGYTPLHIAAKKNQMDIATTLLEYGADANAV 637
Cdd:PHA03095   258 QTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETV 319
PHA03095 PHA03095
ankyrin-like protein; Provisional
 383-669 1.54e-35

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 144.01  E-value: 1.54e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  383 IACKKNRIKVMELLLKHGASIQAVTESGLTPIHVaaFMGH-----VNIVSQLMHHGASPNTTNVRGETALHMAARAGQTE 457
Cdd:PHA03095    20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHL--YLHYssekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTL 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  458 -VVRYLVQNGAQVEAKAKDDQTPLHISARlGK---ADIVQQLLQQGASPNAATTSGYTPLHLSAREGHEDVASV--LLDH 531
Cdd:PHA03095    98 dVIKLLIKAGADVNAKDKVGRTPLHVYLS-GFninPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVELLrlLIDA 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  532 GAslSIITKK--GFTPLHVAAKYGKI--EVANLLLQKNASPDASGKSGLTPLHVAAHYDNQKVALL--LLDQGASPHASA 605
Cdd:PHA03095   177 GA--DVYAVDdrFRSLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARN 254

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2023156728  606 KNGYTPLHIAAKKNQMDIATTLLEYGADANAVTRQGIAPVHLASQDGHVDMVSLLLTRNANVNL 669
Cdd:PHA03095   255 RYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAET 318
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 221-471 1.29e-34

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 140.19  E-value: 1.29e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  221 HYGNINVATL--LLNRGAAVDFTARNDITPLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPLHCGARSGHEQ-----V 293
Cdd:PHA03100     9 KSRIIKVKNIkyIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLtdvkeI 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  294 VEMLLDRGAPILSKTKNGLSPLHMA--TQGDHLNCVQLLIQHNVPVDDVTNDYLTALHVAAHCGHY--KVAKVLLDKKAN 369
Cdd:PHA03100    89 VKLLLEYGANVNAPDNNGITPLLYAisKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVD 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  370 PNAKalngftplhiackkNRIKvmeLLLKHGASIQAVTESGLTPIHVAAFMGHVNIVSQLMHHGASPNTTNVRGETALHM 449
Cdd:PHA03100   169 INAK--------------NRVN---YLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHI 231

                          250       260
                   ....*....|....*....|..
gi 2023156728  450 AARAGQTEVVRYLVQNGAQVEA 471
Cdd:PHA03100   232 AILNNNKEIFKLLLNNGPSIKT 253
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 198-438 2.51e-34

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 139.41  E-value: 2.51e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  198 LLQNDHNADVESKSGFTPLHIAAHYGNINVATLLLNRGAAVDFTARNDITPLH-----VASKRGNANMVKLLLDRGAKID 272
Cdd:PHA03100    21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGANVN 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  273 AKTRDGLTPLHCGA--RSGHEQVVEMLLDRGAPILSKTKNGLSPLHMATQGDH--LNCVQLLIQHNVPVDDVTN-DYlta 347
Cdd:PHA03100   101 APDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKNRvNY--- 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  348 lhvaahcghykvakvLLDKKANPNAKALNGFTPLHIACKKNRIKVMELLLKHGASIQAVTESGLTPIHVAAFMGHVNIVS 427
Cdd:PHA03100   178 ---------------LLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFK 242

                          250
                   ....*....|.
gi 2023156728  428 QLMHHGASPNT 438
Cdd:PHA03100   243 LLLNNGPSIKT 253
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 386-733 2.52e-34

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 143.67  E-value: 2.52e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  386 KKNRIKVMELLLKHGASIQAVTESGLTPIHVAAFMGHVNIVSQLMHHGASPNTTNVRGETALHMAARAGQTEVVRYLVQN 465
Cdd:PHA02876   154 QQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDN 233

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  466 GAQVEakaKDDqtpLHISARLGKADIVQQLL--QQGASPNAATTSGYTPLHLSAREGH-EDVASVLLDHGASLSIITKKG 542
Cdd:PHA02876   234 RSNIN---KND---LSLLKAIRNEDLETSLLlyDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKG 307

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  543 FTPLHVAAKYG-KIEVANLLLQKNASPDASGKSGLTPLHVAAHYD-NQKVALLLLDQGASPHASAKNGYTPLHIAAKKNQ 620
Cdd:PHA02876   308 ETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNN 387

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  621 MDIATTLLEYGADANAVTRQGIAPVHLASQDGHVDM-VSLLLTRNANVNLGNKSGLTPLHLAAQDD-RVNVAEVLVNQGA 698
Cdd:PHA02876   388 VVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGA 467

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 2023156728  699 AVDAQTKMGYTPLHVGCHYGNikIVNFLLQHSAKV 733
Cdd:PHA02876   468 DVNAINIQNQYPLLIALEYHG--IVNILLHYGAEL 500
PHA03095 PHA03095
ankyrin-like protein; Provisional
 258-529 7.21e-34

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 139.00  E-value: 7.21e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  258 ANMVKLLLDRGAKIDAKTRDGLTPLHCGARSGHEQ---VVEMLLDRGAPILSKTKNGLSPLHM-ATQGDHLNCVQLLIQH 333
Cdd:PHA03095    27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKvkdIVRLLLEAGADVNAPERCGFTPLHLyLYNATTLDVIKLLIKA 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  334 NVPVDDVTNDYLTALHV--AAHCGHYKVAKVLLDKKANPNAKALNGFTPLHIACKKNR--IKVMELLLKHGASIQAVTES 409
Cdd:PHA03095   107 GADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanVELLRLLIDAGADVYAVDDR 186

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  410 GLTPIHVAAFMGHVN--IVSQLMHHGASPNTTNVRGETALHMAARAGQTE--VVRYLVQNGAQVEAKAKDDQTPLHISAR 485
Cdd:PHA03095   187 FRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLHYAAV 266

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 2023156728  486 LGKADIVQQLLQQGASPNAATTSGYTPLHLSAREGHEDVASVLL 529
Cdd:PHA03095   267 FNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
PHA03095 PHA03095
ankyrin-like protein; Provisional
 488-793 4.03e-33

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 136.69  E-value: 4.03e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  488 KADIVQQLLQQGASPNAATTSGYTPLHLSAREGHEDVASV---LLDHGASLSIITKKGFTPLHVAAKYG-KIEVANLLLQ 563
Cdd:PHA03095    26 TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHLYLYNAtTLDVIKLLIK 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  564 KNASPDASGKSGLTPLHVAAHYDN--QKVALLLLDQGASPHASAKNGYTPLHIAAKKNQMDIAT--TLLEYGADANAVT- 638
Cdd:PHA03095   106 AGADVNAKDKVGRTPLHVYLSGFNinPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVELlrLLIDAGADVYAVDd 185

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  639 -RQGIAPVHLASQDGHVDMVSLLLTRNANVNLGNKSGLTPLHLAAQDD---RVNVAEVLVNqGAAVDAQTKMGYTPLHVG 714
Cdd:PHA03095   186 rFRSLLHHHLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSsckRSLVLPLLIA-GISINARNRYGQTPLHYA 264

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2023156728  715 CHYGNIKIVNFLLQHSAKVNAKTKNGYTPLHQAAQQGHTHIINVLLQhgAAPNELTVNGntALAIAKRLGYISVVDTLK 793
Cdd:PHA03095   265 AVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALA--KNPSAETVAA--TLNTASVAGGDIPSDATR 339
Death_ank cd08317
Death domain associated with Ankyrins; Death Domain (DD) associated with Ankyrins. Ankyrins ...
 4038-4121 4.93e-33

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: 124.30  E-value: 4.93e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728 4038 ERTDIRMAIVADHLGLSWTELARELNFSVDEINQIRVENPNSLIAQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIV 4117
Cdd:cd08317      1 HRADLRLSDIANLLGSDWPELARELGVSEEDIDLIRSENPNSLAQQAMAMLRLWLEREGEKATGNALESALKKIGRDDIV 80


                   ....
gi 2023156728 4118 TLLE 4121
Cdd:cd08317     81 EKCE 84
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 227-667 5.87e-33

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 139.43  E-value: 5.87e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  227 VATLLLNRGAAVDFTARNDITPLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPLHCGARSGHEQVVEMLLDRGAPIls 306
Cdd:PHA02876   160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNI-- 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  307 kTKNGLSPLHmATQGDHLNCVQLLIQHNVPVDDVtNDYLTalhvaahcghykvakvlldkkanpnakalngfTPLHIAck 386
Cdd:PHA02876   238 -NKNDLSLLK-AIRNEDLETSLLLYDAGFSVNSI-DDCKN--------------------------------TPLHHA-- 280

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  387 knrikvmelllkhgasIQAVTESGLTPihvaafmghvnivsQLMHHGASPNTTNVRGETALHMAARAG-QTEVVRYLVQN 465
Cdd:PHA02876   281 ----------------SQAPSLSRLVP--------------KLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIML 330

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  466 GAQVEAKAKDDQTPLHISARLGK-ADIVQQLLQQGASPNAATTSGYTPLHLSAREGHEDVASVLLDHGASLSIITKKGFT 544
Cdd:PHA02876   331 GADVNAADRLYITPLHQASTLDRnKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGT 410

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  545 PLHVAAkYGkievanlllqknASPDASGKSgltplhvaahydnqkvallLLDQGASPHASAKNGYTPLHIAAKKN-QMDI 623
Cdd:PHA02876   411 ALHFAL-CG------------TNPYMSVKT-------------------LIDRGANVNSKNKDLSTPLHYACKKNcKLDV 458

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....
gi 2023156728  624 ATTLLEYGADANAVTRQGIAPVHLASqdGHVDMVSLLLTRNANV 667
Cdd:PHA02876   459 IEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGAEL 500
Death_ank1 cd08805
Death domain of Ankyrin-1; Death Domain (DD) of the human protein ankyrin-1 (ANK-1) and ...
 4038-4121 9.49e-33

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: 123.54  E-value: 9.49e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728 4038 ERTDIRMAIVADHLGLSWTELARELNFSVDEINQIRVENPNSLIAQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIV 4117
Cdd:cd08805      1 ERVEMKMAVIREHLGLSWAELARELQFSVEDINRIRVENPNSLLEQSTALLNLWVDREGENAKMEPLYPALYSIDRLTIV 80


                   ....
gi 2023156728 4118 TLLE 4121
Cdd:cd08805     81 NILE 84
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 38-547 3.30e-31

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 134.04  E-value: 3.30e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728   38 LKSGVDINISNQNGLNALHLASKEGHVEVVSELIQRGASVDAATKKGNTALHIASLAGQAEVVKVLVTNRANVNaqsQNG 117
Cdd:PHA02876   165 LEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNIN---KND 241

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  118 FTpLYMAAQENHLEVVKFLLDNGASQSLATEDGFTPLAVALQQghdqvvslllendtkgkvrlPALhiaarkddTKAAAL 197
Cdd:PHA02876   242 LS-LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQA--------------------PSL--------SRLVPK 292

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  198 LLQNDHNADVESKSGFTPLHIAAH--YGNINVATLLLnRGAAVDFTARNDITPLHVASKRG-NANMVKLLLDRGAKIDAK 274
Cdd:PHA02876   293 LLERGADVNAKNIKGETPLYLMAKngYDTENIRTLIM-LGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNAR 371

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  275 TRDGLTPLHCGARSGHEQVVEMLLDRGAPILSKTKNGLSPLHMATQGdhlncvqlliqhnvpvddvTNDYLTalhvaahc 354
Cdd:PHA02876   372 DYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCG-------------------TNPYMS-------- 424

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  355 ghykvAKVLLDKKANPNAKALNGFTPLHIACKKN-RIKVMELLLKHGASIQAVTESGLTPIHVAafMGHVNIVSQLMHHG 433
Cdd:PHA02876   425 -----VKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIA--LEYHGIVNILLHYG 497

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  434 ASPNTTNVRGETA-------LHMAARAGQTEVVRYLVQNGAQVEAKAKDDQTPLHISARlgkaDIVQqllqqgaspnaaT 506
Cdd:PHA02876   498 AELRDSRVLHKSLndnmfsfRYIIAHICIQDFIRHDIRNEVNPLKRVPTRFTSLRESFK----EIIQ------------S 561

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|..
gi 2023156728  507 TSGYTPLHLSAREGHEDVASVLLDHGASLSI-ITKKGFTPLH 547
Cdd:PHA02876   562 DDTFKRIWLRCKEELKDISKIRINMFYSLDIfIISKNMNLLH 603
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 458-792 4.01e-30

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 130.57  E-value: 4.01e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  458 VVRYLVQNGAQVEAKAKDDQTPLHISARLGKADIVQQLLQQGASPNAATTSGYTPLHLSAREGHEDVASVLLDHGASlsi 537
Cdd:PHA02876   160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSN--- 236

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  538 ITKKGFTPLHvAAKYGKIEVANLLLQKNASPDASGKSGLTPLHVAAHYDN-QKVALLLLDQGASPHASAKNGYTPLHIAA 616
Cdd:PHA02876   237 INKNDLSLLK-AIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMA 315

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  617 KkNQMDIAT--TLLEYGADANAVTRQGIAPVHLASQ-DGHVDMVSLLLTRNANVNLGNKSGLTPLHLAAQDDRVNVAEVL 693
Cdd:PHA02876   316 K-NGYDTENirTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTL 394

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  694 VNQGAAVDAQTKMGYTPLHVG-CHYGNIKIVNFLLQHSAKVNAKTKNGYTPLHQAAQQG-HTHIINVLLQHGAAPNELTV 771
Cdd:PHA02876   395 LDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINI 474

                          330       340
                   ....*....|....*....|.
gi 2023156728  772 NGNTALAIAkrLGYISVVDTL 792
Cdd:PHA02876   475 QNQYPLLIA--LEYHGIVNIL 493
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 188-535 7.17e-30

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 129.80  E-value: 7.17e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  188 RKDDTKAAALLLQNdhNADVESKSGF--TPLHIAAHYGNINVATLLLNRGAAVDFTARNDITPLHVASKRGNANMVKLLL 265
Cdd:PHA02876   154 QQDELLIAEMLLEG--GADVNAKDIYciTPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII 231

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  266 DRGAKIDAKTRDGL-----------------------------TPLHCGARSGH-EQVVEMLLDRGAPILSKTKNGLSPL 315
Cdd:PHA02876   232 DNRSNINKNDLSLLkairnedletslllydagfsvnsiddcknTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPL 311

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  316 H-MATQGDHLNCVQLLIQHNVPVDDVTNDYLTALHVAAHCGHYK-VAKVLLDKKANPNAKALNGFTPLHIACKKNRIKVM 393
Cdd:PHA02876   312 YlMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKdIVITLLELGANVNARDYCDKTPIHYAAVRNNVVII 391

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  394 ELLLKHGASIQAVTESGLTPIHVAAFmghvnivsqlmhhGASPNTTnvrgetalhmaaragqtevVRYLVQNGAQVEAKA 473
Cdd:PHA02876   392 NTLLDYGADIEALSQKIGTALHFALC-------------GTNPYMS-------------------VKTLIDRGANVNSKN 439

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2023156728  474 KDDQTPLHISARLG-KADIVQQLLQQGASPNAATTSGYTPLHLSAreGHEDVASVLLDHGASL 535
Cdd:PHA02876   440 KDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGAEL 500
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 358-538 2.30e-29

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 124.39  E-value: 2.30e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  358 KVAKVLLDKKANPNAKALNGFTPLHIAC-----KKNRIKVMELLLKHGASIQAVTESGLTPIHVAAF--MGHVNIVSQLM 430
Cdd:PHA03100    49 DVVKILLDNGADINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISkkSNSYSIVEYLL 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  431 HHGASPNTTNVRGETALHMAARAGQ--TEVVRYLVQNGAQVEAK--------------AKDDQ--TPLHISARLGKADIV 492
Cdd:PHA03100   129 DNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKnrvnyllsygvpinIKDVYgfTPLHYAVYNNNPEFV 208

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2023156728  493 QQLLQQGASPNAATTSGYTPLHLSAREGHEDVASVLLDHGASLSII 538
Cdd:PHA03100   209 KYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTI 254
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 379-600 4.88e-29

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 123.62  E-value: 4.88e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  379 TPLHIACKKNRIKVMELLLKHGASIQAVTESGLTPIHVAAFMGHV-----NIVSQLMHHGASPNTTNVRGETALHMAA-- 451
Cdd:PHA03100    37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAIsk 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  452 RAGQTEVVRYLVQNGAQVEAKAKDDQTPLHISARLGKAD--IVQQLLQQGASPNAATTSGYtplhlsareghedvasvLL 529
Cdd:PHA03100   117 KSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDINAKNRVNY-----------------LL 179

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2023156728  530 DHGASLSIITKKGFTPLHVAAKYGKIEVANLLLQKNASPDASGKSGLTPLHVAAHYDNQKVALLLLDQGAS 600
Cdd:PHA03100   180 SYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 447-747 8.85e-29

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 123.15  E-value: 8.85e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  447 LHMAARAGQTEVVRYLVQN-GAQVEAKAKDDQTPLHISARLGKADIVQQLLQQGASPNAATTSGYTPLHLSAREGHEDVA 525
Cdd:PHA02874     5 LRMCIYSGDIEAIEKIIKNkGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDII 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  526 SVLLDHGASLSIItkkgftPLHVAAKygkiEVANLLLQKNASPDASGKSGLTPLHVAAHYDNQKVALLLLDQGASPHASA 605
Cdd:PHA02874    85 KLLIDNGVDTSIL------PIPCIEK----DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIED 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  606 KNGYTPLHIAAKKNQMDIATTLLEYGADANAVTRQGIAPVHLASQDGHVDMVSLLLTRNANVNLGNKSGLTPLHLAAQDD 685
Cdd:PHA02874   155 DNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHN 234

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2023156728  686 RvNVAEVLVNQgAAVDAQTKMGYTPLHVGCHYG-NIKIVNFLLQHSAKVNAKTKNGYTPLHQA 747
Cdd:PHA02874   235 R-SAIELLINN-ASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTA 295
Death_ank2 cd08804
Death domain of Ankyrin-2; Death Domain (DD) of Ankyrin-2 (ANK-2) and related proteins. ...
 4038-4121 1.55e-27

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: 108.63  E-value: 1.55e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728 4038 ERTDIRMAIVADHLGLSWTELARELNFSVDEINQIRVENPNSLIAQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIV 4117
Cdd:cd08804      1 ERTEERLAHIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLTQCLTKINRMDIV 80


                   ....
gi 2023156728 4118 TLLE 4121
Cdd:cd08804     81 HLME 84
PHA03095 PHA03095
ankyrin-like protein; Provisional
 16-300 1.84e-27

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 119.74  E-value: 1.84e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728   16 SDTNASYLRAARAGN--LEKALDYLKSGVDINISNQNGLNALHLASKEGH---VEVVSELIQRGASVDAATKKGNTALHI 90
Cdd:PHA03095    10 IMEAALYDYLLNASNvtVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHL 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728   91 -ASLAGQAEVVKVLVTNRANVNAQSQNGFTPL--YMAAQENHLEVVKFLLDNGASQSLATEDGFTPLAVALQQGH--DQV 165
Cdd:PHA03095    90 yLYNATTLDVIKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanVEL 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  166 VSLLLEND----TKGKVRLPALHIAAR--KDDTKAAALLLQNDHNADVESKSGFTPLHIAAHYG---NINVATLLLNrGA 236
Cdd:PHA03095   170 LRLLIDAGadvyAVDDRFRSLLHHHLQsfKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSsckRSLVLPLLIA-GI 248

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2023156728  237 AVDFTARNDITPLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPLHCGARSGHEQVVEMLLDR 300
Cdd:PHA03095   249 SINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAK 312
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 379-637 2.52e-27

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 118.53  E-value: 2.52e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  379 TPLHIACKKNRIKVMELLLKHGASIQAVTESGLTPIHVAAFMGHVNIVSQLMHHGASP---------------------- 436
Cdd:PHA02874    37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTsilpipciekdmiktildcgid 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  437 -NTTNVRGETALHMAARAGQTEVVRYLVQNGAQVEAKAKDDQTPLHISARLGKADIVQQLLQQGASPNAATTSGYTPLHL 515
Cdd:PHA02874   117 vNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  516 SAREGHEDVASVLLDHGASLSIITKKGFTPLHVAAKYGKIEVAnlLLQKNASPDASGKSGLTPLHVAAHYDNQK-VALLL 594
Cdd:PHA02874   197 AAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIE--LLINNASINDQDIDGSTPLHHAINPPCDIdIIDIL 274

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 2023156728  595 LDQGASPHASAKNGYTPLHIAAKK-NQMDIATTLLeygadANAV 637
Cdd:PHA02874   275 LYHKADISIKDNKGENPIDTAFKYiNKDPVIKDII-----ANAV 313
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 444-669 3.18e-27

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 117.78  E-value: 3.18e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  444 ETALHMAARAGQTEVVRYLVQNGAQVEAKAKDDQTPLHISARLGKADIVQQLLQQGASPNAATTSGYTPLHLSAREGHED 523
Cdd:PHA02875     3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  524 VASVLLDHGASLS-IITKKGFTPLHVAAKYGKIEVANLLLQKNASPDASGKSGLTPLHVAAHYDNQKVALLLLDQGASPH 602
Cdd:PHA02875    83 AVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLD 162

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2023156728  603 ASAKNGYTPLHIAAKKNQMDIATTLLEYGADANAVTRQG-IAPVHLASQDGHVDMVSLLLTRNANVNL 669
Cdd:PHA02875   163 IEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNI 230
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 219-449 3.62e-27

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 117.78  E-value: 3.62e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  219 AAHYGNINVATLLLNRGAAVDFTARNDITPLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPLHCGARSGHEQVVEMLL 298
Cdd:PHA02875     9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  299 DRGAPILSKT-KNGLSPLHMATQGDHLNCVQLLIQHNVPVDDVTNDYLTALHVAAHCGHYKVAKVLLDKKANPNAKALNG 377
Cdd:PHA02875    89 DLGKFADDVFyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCG 168

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2023156728  378 FTPLHIACKKNRIKVMELLLKHGASIQAVTESG-LTPIHVAAFMGHVNIVSQLMHHGASPN-TTNVRGE--TALHM 449
Cdd:PHA02875   169 CTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNiMFMIEGEecTILDM 244
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 279-575 6.74e-27

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 118.06  E-value: 6.74e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  279 LTPLHCGARSGHEQVVEMLLDRGAPILSKTKNGLSPLHMATQGDHLNCVQLLIQHNVPvDDVTNDYlTALHVAAHCGHYK 358
Cdd:PHA02878    38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINK-CSVFYTL-VAIKDAFNNRNVE 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  359 VAKVLLDKKANPNAKalngfTPLHIACKKNR-----IKVMELLLKHGASIQAVTE-SGLTPIHVAAFMGHVNIVSQLMHH 432
Cdd:PHA02878   116 IFKIILTNRYKNIQT-----IDLVYIDKKSKddiieAEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSY 190

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  433 GASPNTTNVRGETALHMAARAGQTEVVRYLVQNGAQVEAKAKDDQTPLHIS-ARLGKADIVQQLLQQGASPNAATT-SGY 510
Cdd:PHA02878   191 GANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYiLGL 270

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2023156728  511 TPLHLSAREghEDVASVLLDHGASLSIITKKGFTPLHVAAKY------GKIEVANLLLQKNASPDASGKSG 575
Cdd:PHA02878   271 TALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAVKQylciniGRILISNICLLKRIKPDIKNSEG 339
PHA03095 PHA03095
ankyrin-like protein; Provisional
 97-409 7.80e-27

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 117.82  E-value: 7.80e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728   97 AEVVKVLVTNRANVNAQSQNGFTPL--YMA-AQENHLEVVKFLLDNGASQSLATEDGFTPLavalqqgHdqvvsLLLEND 173
Cdd:PHA03095    27 VEEVRRLLAAGADVNFRGEYGKTPLhlYLHySSEKVKDIVRLLLEAGADVNAPERCGFTPL-------H-----LYLYNA 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  174 TKGKVrlpalhiaarkddtkaAALLLqnDHNADVESKS--GFTPLHIAAHYGNIN--VATLLLNRGAAVDFTARNDITPL 249
Cdd:PHA03095    95 TTLDV----------------IKLLI--KAGADVNAKDkvGRTPLHVYLSGFNINpkVIRLLLRKGADVNALDLYGMTPL 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  250 HVASKRGNAN--MVKLLLDRGAKIDAKTRDGLTPLHCGARSGH--EQVVEMLLDRGAPILSKTKNGLSPLH-MATQGD-- 322
Cdd:PHA03095   157 AVLLKSRNANveLLRLLIDAGADVYAVDDRFRSLLHHHLQSFKprARIVRELIRAGCDPAATDMLGNTPLHsMATGSSck 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  323 HLNCVQLLIqHNVPVDdVTNDYL-TALHVAAHCGHYKVAKVLLDKKANPNAKALNGFTPLHIACKKNRIKVMELLLKHGA 401
Cdd:PHA03095   237 RSLVLPLLI-AGISIN-ARNRYGqTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNP 314


                   ....*...
gi 2023156728  402 SIQAVTES 409
Cdd:PHA03095   315 SAETVAAT 322
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 38-273 3.49e-26

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 115.15  E-value: 3.49e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728   38 LKSGVDINISNQNGLNALHLASKEGHVEVVSELIQRGASVDAATKKGNTALHIASLAGQA-----EVVKVLVTNRANVNA 112
Cdd:PHA03100    22 IMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNA 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  113 QSQNGFTPLYMAAQE--NHLEVVKFLLDNGASQSLATEDGFTPLAVALQQGHD--QVVSLLLEN----DTKGKVRlpalh 184
Cdd:PHA03100   102 PDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKgvdiNAKNRVN----- 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  185 iaarkddtkaaaLLLQNDHNADVESKSGFTPLHIAAHYGNINVATLLLNRGAAVDFTARNDITPLHVASKRGNANMVKLL 264
Cdd:PHA03100   177 ------------YLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLL 244


                   ....*....
gi 2023156728  265 LDRGAKIDA 273
Cdd:PHA03100   245 LNNGPSIKT 253
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 214-465 8.02e-26

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 114.29  E-value: 8.02e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  214 TPLHIAAHYGNINVATLLLNRGAAVDFTARNDITPLHVASKRGNANMVKLLLDRGA-----------------------K 270
Cdd:PHA02874    37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVdtsilpipciekdmiktildcgiD 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  271 IDAKTRDGLTPLHCGARSGHEQVVEMLLDRGAPILSKTKNGLSPLHMATQGDHLNCVQLLIQhNVPVDDVTNDYL-TALH 349
Cdd:PHA02874   117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLE-KGAYANVKDNNGeSPLH 195

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  350 VAAHCGHYKVAKVLLDKKANPNAKALNGFTPLHIACKKNRiKVMELLLKHgASIQAVTESGLTPIHVA-AFMGHVNIVSQ 428
Cdd:PHA02874   196 NAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLINN-ASINDQDIDGSTPLHHAiNPPCDIDIIDI 273

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 2023156728  429 LMHHGASPNTTNVRGETALHMAAR-AGQTEVVRYLVQN 465
Cdd:PHA02874   274 LLYHKADISIKDNKGENPIDTAFKyINKDPVIKDIIAN 311
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 512-785 2.20e-25

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 113.44  E-value: 2.20e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  512 PLHLSAREGHEDVASVLLDHGASLSIITKKGFTPLHVAAKY-GKIEVANLLLQKNASpdaSGKSGLTPLHVAAHYDNQKV 590
Cdd:PHA02878    40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEpNKLGMKEMIRSINKC---SVFYTLVAIKDAFNNRNVEI 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  591 A-LLLLDQgasphasAKNGYTPLHIAAKKNQMD------IATTLLEYGADANAVTR-QGIAPVHLASQDGHVDMVSLLLT 662
Cdd:PHA02878   117 FkIILTNR-------YKNIQTIDLVYIDKKSKDdiieaeITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLS 189

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  663 RNANVNLGNKSGLTPLHLAAQDDRVNVAEVLVNQGAAVDAQTKMGYTPLHVGCHY-GNIKIVNFLLQHSAKVNAK-TKNG 740
Cdd:PHA02878   190 YGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKsYILG 269

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 2023156728  741 YTPLHQAAQQghTHIINVLLQHGAAPNELTVNGNTALAIA--KRLGY 785
Cdd:PHA02878   270 LTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAvkQYLCI 314
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
 4037-4123 2.64e-25

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: 102.49  E-value: 2.64e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  4037 CERTDIRMAIVADH-LGLSWTELARELNFSVDEINQIRVENPNSLIAQSFMLLKKWVTRDGKNATTDALTSVLTKINRID 4115
Cdd:smart00005    1 PELTRQKLAKLLDHpLGLDWRELARKLGLSEADIDQIRTEAPRDLAEQSVQLLRLWEQREGKNATLGTLLEALRKMGRDD 80


                    ....*...
gi 2023156728  4116 IVTLLEGP 4123
Cdd:smart00005   81 AVELLRSE 88
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 128-350 1.05e-24

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 110.47  E-value: 1.05e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  128 NHLEVVKFLLDNGASQSLATEDGFTPLAVALQQGHDQVVSLLLENDTKGKVRLPA----LHIAARKDDTKAAALLLQ-ND 202
Cdd:PHA02875    13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDieseLHDAVEEGDVKAVEELLDlGK 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  203 HNADVESKSGFTPLHIAAHYGNINVATLLLNRGAAVDFTARNDITPLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPL 282
Cdd:PHA02875    93 FADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPL 172

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2023156728  283 HCGARSGHEQVVEMLLDRGAPILSKTKNG-LSPLHMATQGDHLNCVQLLIQHNVPVDDVT---NDYLTALHV 350
Cdd:PHA02875   173 IIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNIMFmieGEECTILDM 244
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 355-638 4.52e-24

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 108.54  E-value: 4.52e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  355 GHYKVAKVLLDKKANPNAKALNGFTPLHIACKKNRIKVMELLLKHGAsIQAVTESGL-TPIHVAAFMGHVNIVSQLMHHG 433
Cdd:PHA02875    13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGA-IPDVKYPDIeSELHDAVEEGDVKAVEELLDLG 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  434 ASPNTtnvrgetalhmaaragqtevVRYlvqngaqveakaKDDQTPLHISARLGKADIVQQLLQQGASPNAATTSGYTPL 513
Cdd:PHA02875    92 KFADD--------------------VFY------------KDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPL 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  514 HLSAREGHEDVASVLLDHGASLSIITKKGFTPLHVAAKYGKIEVANLLLQKNASPDASGKSGltplhvaahydnqKVALL 593
Cdd:PHA02875   140 HLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNG-------------CVAAL 206

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 2023156728  594 LLdqgasphasakngytplhiAAKKNQMDIATTLLEYGADANAVT 638
Cdd:PHA02875   207 CY-------------------AIENNKIDIVRLFIKRGADCNIMF 232
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 582-777 1.55e-23

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 107.00  E-value: 1.55e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  582 AAHYDNQKVALLLLDQGASPHASAKNGYTPLHIAAKKNQMDIATTLLEYGADANaVTRQGI-APVHLASQDGHVDMVSLL 660
Cdd:PHA02875     9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPD-VKYPDIeSELHDAVEEGDVKAVEEL 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  661 LTRNANVN-LGNKSGLTPLHLAAQDDRVNVAEVLVNQGAAVDAQTKMGYTPLHVGCHYGNIKIVNFLLQHSAKVNAKTKN 739
Cdd:PHA02875    88 LDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCC 167

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 2023156728  740 GYTPLHQAAQQGHTHIINVLLQHGAAPNELTVNGNTAL 777
Cdd:PHA02875   168 GCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAA 205
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 314-582 2.43e-23

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 107.27  E-value: 2.43e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  314 PLHMATQGDHLNCVQLLIQHNVPVDDVTNDYLTALHVAAHCGHYKVAKVLLDKKANpnAKALNGFTPLHIACKKNRIKVM 393
Cdd:PHA02878    40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINK--CSVFYTLVAIKDAFNNRNVEIF 117

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  394 E-LLLKHGASIQAVTESGLTPIHVAAFMgHVNIVSQLMHHGASPN-TTNVRGETALHMAARAGQTEVVRYLVQNGAQVEA 471
Cdd:PHA02878   118 KiILTNRYKNIQTIDLVYIDKKSKDDII-EAEITKLLLSYGADINmKDRHKGNTALHYATENKDQRLTELLLSYGANVNI 196

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  472 KAKDDQTPLHISARLGKADIVQQLLQQGASPNAATTSGYTPLHLS-AREGHEDVASVLLDHGASLSI-ITKKGFTPLHVA 549
Cdd:PHA02878   197 PDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAkSYILGLTALHSS 276

                          250       260       270
                   ....*....|....*....|....*....|...
gi 2023156728  550 AKygKIEVANLLLQKNASPDASGKSGLTPLHVA 582
Cdd:PHA02878   277 IK--SERKLKLLLEYGADINSLNSYKLTPLSSA 307
Ank_2 pfam12796
Ankyrin repeats (3 copies);
55-142 3.70e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 96.34  E-value: 3.70e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728   55 LHLASKEGHVEVVSELIQRGASVDAATKKGNTALHIASLAGQAEVVKVLVtNRANVNAQSqNGFTPLYMAAQENHLEVVK 134
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78


                   ....*...
gi 2023156728  135 FLLDNGAS 142
Cdd:pfam12796   79 LLLEKGAD 86
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 88-398 5.93e-23

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 106.12  E-value: 5.93e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728   88 LHIASLAGQAEVVKVLVTNRANVNAQSQNGFTPLYMAAQENHLEVVKFLLDNGASQSLATEdgFTPLAVALQQGHDQVVS 167
Cdd:PHA02878    41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFYT--LVAIKDAFNNRNVEIFK 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  168 LLLENDTKGKVRLPALHIAARKDD----TKAAALLLQndHNADVESK---SGFTPLHIAAHYGNINVATLLLNRGAAVDF 240
Cdd:PHA02878   119 IILTNRYKNIQTIDLVYIDKKSKDdiieAEITKLLLS--YGADINMKdrhKGNTALHYATENKDQRLTELLLSYGANVNI 196

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  241 TARNDITPLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPLHCG-ARSGHEQVVEMLLDRGAPILSK-TKNGLSPLHMA 318
Cdd:PHA02878   197 PDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKsYILGLTALHSS 276

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  319 TQGDHLncVQLLIQHNVPVDDVTNDYLTALHVAA------HCGHYKVAKVLLDKKANPNAKALNGFTpLHIACKKNRIKV 392
Cdd:PHA02878   277 IKSERK--LKLLLEYGADINSLNSYKLTPLSSAVkqylciNIGRILISNICLLKRIKPDIKNSEGFI-DNMDCITSNKRL 353


                   ....*.
gi 2023156728  393 MELLLK 398
Cdd:PHA02878   354 NQIKDK 359
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 522-792 7.52e-23

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 105.05  E-value: 7.52e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  522 EDVASVLLDHGASLSIITKKGFTPLHVAAKYGKIEVANLLLQKNASPDASGKSGLTPLHVAAHYDNQKVALLLLDQGASP 601
Cdd:PHA02874    15 EAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDT 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  602 hasakngyTPLHIAAKKNQMdiATTLLEYGADANAVTRQGIAPVHLASQDGHVDMVSLLLTRNANVNLGNKSGLTPLHLA 681
Cdd:PHA02874    95 --------SILPIPCIEKDM--IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIA 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  682 AQDDRVNVAEVLVNQGAAVDAQTKMGYTPLHVGCHYGNIKIVNFLLQHSAKVNAKTKNGYTPLHQAAQQGHTHIinVLLQ 761
Cdd:PHA02874   165 IKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAI--ELLI 242

                          250       260       270
                   ....*....|....*....|....*....|....
gi 2023156728  762 HGAAPNELTVNGNTALAIAkrLGY---ISVVDTL 792
Cdd:PHA02874   243 NNASINDQDIDGSTPLHHA--INPpcdIDIIDIL 274
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 62-351 2.43e-22

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 103.50  E-value: 2.43e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728   62 GHVEVVSELIQ-RGASVDAATKKGNTALHIASLAGQAEVVKVLVTNRANVNAQSQNGFTPLYMAAQENHLEVVKFLLDNG 140
Cdd:PHA02874    12 GDIEAIEKIIKnKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  141 ASQSLatedgfTPLAVALQQGHDQVVSLLLENDTKGKVRLPALHIAARKDDTKAAALLLQNDHNADVESKSGFTPLHIAA 220
Cdd:PHA02874    92 VDTSI------LPIPCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAI 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  221 HYGNINVATLLLNRGAAVDFTARNDITPLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPLHcGARSGHEQVVEMLLDr 300
Cdd:PHA02874   166 KHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLH-NAIIHNRSAIELLIN- 243

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2023156728  301 GAPILSKTKNGLSPLHMATQGD-HLNCVQLLIQHNVPVDDVTNDYLTALHVA 351
Cdd:PHA02874   244 NASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTA 295
Ank_2 pfam12796
Ankyrin repeats (3 copies);
348-440 2.59e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 94.03  E-value: 2.59e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  348 LHVAAHCGHYKVAKVLLDKKANPNAKALNGFTPLHIACKKNRIKVMELLLKHGAsiQAVTESGLTPIHVAAFMGHVNIVS 427
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 2023156728  428 QLMHHGASPNTTN 440
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 118-417 5.43e-22

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 103.04  E-value: 5.43e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  118 FTPLYMAAQENHLEVVKFLLDNGASQSLATEDGFTPLAVALQQGHDQVVSLLLENDTKGKVrlpalhiaarkddtkaaal 197
Cdd:PHA02878    38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSV------------------- 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  198 llqndHNADVESKSGFtplhiaaHYGNINVA-TLLLNRgaaVDFTARNDITPLHVASKRG--NANMVKLLLDRGAKIDAK 274
Cdd:PHA02878    99 -----FYTLVAIKDAF-------NNRNVEIFkIILTNR---YKNIQTIDLVYIDKKSKDDiiEAEITKLLLSYGADINMK 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  275 TRDGL-TPLHCGARSGHEQVVEMLLDRGAPILSKTKNGLSPLHMATQGDHLNCVQLLIQHNVPVDDVTNDYLTALHVA-A 352
Cdd:PHA02878   164 DRHKGnTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvG 243

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2023156728  353 HCGHYKVAKVLLDKKANPNAKA-LNGFTPLHIACKKNRikVMELLLKHGASIQAVTESGLTPIHVA 417
Cdd:PHA02878   244 YCKDYDILKLLLEHGVDVNAKSyILGLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPLSSA 307
Ank_2 pfam12796
Ankyrin repeats (3 copies);
315-405 6.77e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.87  E-value: 6.77e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  315 LHMATQGDHLNCVQLLIQHNVPVDDVTNDYLTALHVAAHCGHYKVAKVLLDkKANPNAKaLNGFTPLHIACKKNRIKVME 394
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLK-DNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|.
gi 2023156728  395 LLLKHGASIQA 405
Cdd:pfam12796   79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
282-373 1.07e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.10  E-value: 1.07e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  282 LHCGARSGHEQVVEMLLDRGAPILSKTKNGLSPLHMATQGDHLNCVQLLIQHNVPvdDVTNDYLTALHVAAHCGHYKVAK 361
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 2023156728  362 VLLDKKANPNAK 373
Cdd:pfam12796   79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
480-570 1.79e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 91.72  E-value: 1.79e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  480 LHISARLGKADIVQQLLQQGASPNAATTSGYTPLHLSAREGHEDVASVLLDHGASLsiITKKGFTPLHVAAKYGKIEVAN 559
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN--LKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|.
gi 2023156728  560 LLLQKNASPDA 570
Cdd:pfam12796   79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
216-307 2.42e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 91.33  E-value: 2.42e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  216 LHIAAHYGNINVATLLLNRGAAVDFTARNDITPLHVASKRGNANMVKLLLDRgAKIDAKTrDGLTPLHCGARSGHEQVVE 295
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 2023156728  296 MLLDRGAPILSK 307
Cdd:pfam12796   79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
381-472 2.94e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.95  E-value: 2.94e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  381 LHIACKKNRIKVMELLLKHGASIQAVTESGLTPIHVAAFMGHVNIVSQLMHHGASPNTTNvrGETALHMAARAGQTEVVR 460
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN--GRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 2023156728  461 YLVQNGAQVEAK 472
Cdd:pfam12796   79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
183-274 4.74e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.56  E-value: 4.74e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  183 LHIAARKDDTKAAALLLQNDHNADVESKSGFTPLHIAAHYGNINVATLLLNRGAAVDFTarNDITPLHVASKRGNANMVK 262
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD--NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 2023156728  263 LLLDRGAKIDAK 274
Cdd:pfam12796   79 LLLEKGADINVK 90
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 364-648 5.30e-21

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 99.95  E-value: 5.30e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  364 LDKKAN-PNAKALNGFTPLHIACKKNRIKVMELLLKHGASIQAVTESGLTPIHVAAFMGHVNIVSQLMhhgASPNTTNV- 441
Cdd:PHA02878    23 IDHTENySTSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMI---RSINKCSVf 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  442 RGETALHMAARAGQTEVVRYLVQNGAQVEAKAKDDQTPLHISARLGKADIVQQLLQQGASPNAATT-SGYTPLHLSAREG 520
Cdd:PHA02878   100 YTLVAIKDAFNNRNVEIFKIILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDRhKGNTALHYATENK 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  521 HEDVASVLLDHGASLSIITKKGFTPLHVAAKYGKIEVANLLLQKNASPDASGKSGLTPLHVAAHY-DNQKVALLLLDQGA 599
Cdd:PHA02878   180 DQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGV 259

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 2023156728  600 SPHA-SAKNGYTPLHIAAKKNQmdIATTLLEYGADANAVTRQGIAPVHLA 648
Cdd:PHA02878   260 DVNAkSYILGLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPLSSA 307
Ank_2 pfam12796
Ankyrin repeats (3 copies);
414-504 6.04e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.18  E-value: 6.04e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  414 IHVAAFMGHVNIVSQLMHHGASPNTTNVRGETALHMAARAGQTEVVRYLVQNgAQVEAKAkDDQTPLHISARLGKADIVQ 493
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|.
gi 2023156728  494 QLLQQGASPNA 504
Cdd:pfam12796   79 LLLEKGADINV 89
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 29-269 7.50e-21

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 98.91  E-value: 7.50e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728   29 GNLEKALDYLKSGVDINISNQNGLNALHLASKEGHVEVVSELIQRGASVDAATKKGNTALHIASLAGQAEVVKVLVTNRA 108
Cdd:PHA02875    13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  109 NVN-AQSQNGFTPLYMAAQENHLEVVKFLLDNGASQSLATEDGFTPlavalqqghdqvvslllendtkgkvrlpaLHIAA 187
Cdd:PHA02875    93 FADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSP-----------------------------LHLAV 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  188 RKDDTKAAALLLQNDHNADVESKSGFTPLHIAAHYGNINVATLLLNRGAAVDFTARN-DITPLHVASKRGNANMVKLLLD 266
Cdd:PHA02875   144 MMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNgCVAALCYAIENNKIDIVRLFIK 223


                   ...
gi 2023156728  267 RGA 269
Cdd:PHA02875   224 RGA 226
Ank_2 pfam12796
Ankyrin repeats (3 copies);
88-175 7.63e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.79  E-value: 7.63e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728   88 LHIASLAGQAEVVKVLVTNRANVNAQSQNGFTPLYMAAQENHLEVVKFLLDNGASQSlaTEDGFTPLAVALQQGHDQVVS 167
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78


                   ....*...
gi 2023156728  168 LLLENDTK 175
Cdd:pfam12796   79 LLLEKGAD 86
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 24-333 1.17e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 99.18  E-value: 1.17e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728   24 RAARAGNLEKALDYLKSGVDINISNQNGLNALHLASKE----GHVEVVSELIQRgaSVDAATKKGNTALHIASLagqaEV 99
Cdd:PHA02878    43 QAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEpnklGMKEMIRSINKC--SVFYTLVAIKDAFNNRNV----EI 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  100 VKVLVTNRANVNAQSQNGFTPLYMAAQENHLEVVKFLLDNGASQSLATEDgftplavalqqghdqvvslllendtKGKVr 179
Cdd:PHA02878   117 FKIILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDRH-------------------------KGNT- 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  180 lpALHIAARKDDTKAAALLLQNDHNADVESKSGFTPLHIAAHYGNINVATLLLNRGAAVDFTARNDITPLHVASKR-GNA 258
Cdd:PHA02878   171 --ALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDY 248

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2023156728  259 NMVKLLLDRGAKIDAK-TRDGLTPLHCGARSghEQVVEMLLDRGAPILSKTKNGLSPLHMAT-QGDHLNCVQLLIQH 333
Cdd:PHA02878   249 DILKLLLEHGVDVNAKsYILGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAVkQYLCINIGRILISN 323
Ank_2 pfam12796
Ankyrin repeats (3 copies);
646-736 1.23e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.40  E-value: 1.23e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  646 HLASQDGHVDMVSLLLTRNANVNLGNKSGLTPLHLAAQDDRVNVAEVLVNQgAAVDAQTKmGYTPLHVGCHYGNIKIVNF 725
Cdd:pfam12796    2 HLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKL 79

                           90
                   ....*....|.
gi 2023156728  726 LLQHSAKVNAK 736
Cdd:pfam12796   80 LLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
546-636 1.32e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.02  E-value: 1.32e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  546 LHVAAKYGKIEVANLLLQKNASPDASGKSGLTPLHVAAHYDNQKVALLLLDQGASphASAKNGYTPLHIAAKKNQMDIAT 625
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|.
gi 2023156728  626 TLLEYGADANA 636
Cdd:pfam12796   79 LLLEKGADINV 89
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 38-254 1.42e-20

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 98.11  E-value: 1.42e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728   38 LKSGVDINISNQNGLNALHLASKEGHVEVVSELIQRGASVDAATKKGNTALHIASLAGQAEVVKVLVTNRANVNAQSQNG 117
Cdd:PHA02874   111 LDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNG 190

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  118 FTPLYMAAQENHLEVVKFLLDNGASQSLATEDGFTPLAVALqqghdqvvslllendtkgkvrlpaLHiaarkddTKAAAL 197
Cdd:PHA02874   191 ESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI------------------------IH-------NRSAIE 239

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2023156728  198 LLQNDHNADVESKSGFTPLHIAAHYG-NINVATLLLNRGAAVDFTARNDITPLHVASK 254
Cdd:PHA02874   240 LLINNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAFK 297
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 17-282 1.83e-20

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 97.73  E-value: 1.83e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728   17 DTNASYLRAARAGNLEKALDYLKSGVDINISNQNGLNALHLASKEGHVEVVSELIQRGasVDAATkkgntaLHIASLagQ 96
Cdd:PHA02874    34 ETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG--VDTSI------LPIPCI--E 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728   97 AEVVKVLVTNRANVNAQSQNGFTPLYMAAQENHLEVVKFLLDNGASQSLATEDGFTPLAVALQQGHDQVVSLLLENDTKG 176
Cdd:PHA02874   104 KDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYA 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  177 KVR----LPALHIAARKDDTKAAALLLQNDHNADVESKSGFTPLHIAAHYgNINVATLLLNrGAAVDFTARNDITPLHVA 252
Cdd:PHA02874   184 NVKdnngESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIH-NRSAIELLIN-NASINDQDIDGSTPLHHA 261

                          250       260       270
                   ....*....|....*....|....*....|.
gi 2023156728  253 -SKRGNANMVKLLLDRGAKIDAKTRDGLTPL 282
Cdd:PHA02874   262 iNPPCDIDIIDILLYHKADISIKDNKGENPI 292
Death cd01670
Death Domain: a protein-protein interaction domain; Death Domains (DDs) are protein-protein ...
 4047-4121 7.56e-20

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


Pssm-ID: 260017 [Multi-domain]  Cd Length: 79  Bit Score: 86.57  E-value: 7.56e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2023156728 4047 VADHLGLSWTELARELNFSVDEINQIRVENPNSLIAQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIVTLLE 4121
Cdd:cd01670      5 VAEELGRDWKKLARKLGLSEGDIDQIEEDNRDDLKEQAYQMLERWREREGDEATLGRLIQALREIGRRDLAEKLE 79
Ank_2 pfam12796
Ankyrin repeats (3 copies);
678-767 1.95e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.94  E-value: 1.95e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  678 LHLAAQDDRVNVAEVLVNQGAAVDAQTKMGYTPLHVGCHYGNIKIVNFLLQHsAKVNAKTkNGYTPLHQAAQQGHTHIIN 757
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|
gi 2023156728  758 VLLQHGAAPN 767
Cdd:pfam12796   79 LLLEKGADIN 88
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 476-717 3.26e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 93.90  E-value: 3.26e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  476 DQTPLHISARLGKADIVQQLLQQGASPNAATTSGYTPLHLSAREGHEDVASVLLDHGASLSIITKKGFTPLHVAAKYGKI 555
Cdd:PHA02875     2 DQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDV 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  556 EVANLLLQKNA-SPDASGKSGLTPLHVAAHYDNQKVALLLLDQGASPHASAKNGYTPLHIAAKKNQMDIATTLLEYGADA 634
Cdd:PHA02875    82 KAVEELLDLGKfADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACL 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  635 NAVTRQGIAPVHLASQDGHVDMVSLLLTRNANVNLGNKSG-LTPLHLAAQDDRVNVAEVLVNQGAAVDAQTK-MG--YTP 710
Cdd:PHA02875   162 DIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNIMFMiEGeeCTI 241


                   ....*..
gi 2023156728  711 LHVGCHY 717
Cdd:PHA02875   242 LDMICNM 248
Ank_2 pfam12796
Ankyrin repeats (3 copies);
612-703 3.78e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.17  E-value: 3.78e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  612 LHIAAKKNQMDIATTLLEYGADANAVTRQGIAPVHLASQDGHVDMVSLLLtRNANVNLGNKsGLTPLHLAAQDDRVNVAE 691
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDN-GRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 2023156728  692 VLVNQGAAVDAQ 703
Cdd:pfam12796   79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
24-113 5.15e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.78  E-value: 5.15e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728   24 RAARAGNLEKALDYLKSGVDINISNQNGLNALHLASKEGHVEVVSELIQRgASVDAATkKGNTALHIASLAGQAEVVKVL 103
Cdd:pfam12796    3 LAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLL 80

                           90
                   ....*....|
gi 2023156728  104 VTNRANVNAQ 113
Cdd:pfam12796   81 LEKGADINVK 90
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 44-406 7.06e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 93.10  E-value: 7.06e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728   44 INISNQNGLNALHLASKEGHVEVVSELIQRGASVdaatkkgntalhiaslagqaevvkvlvtNRANVNAQSqngftPLYM 123
Cdd:PHA02874    28 INISVDETTTPLIDAIRSGDAKIVELFIKHGADI----------------------------NHINTKIPH-----PLLT 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  124 AAQENHLEVVKFLLDNGASQSLatedgftplaVALQQGHDQVVSLLLENDTKGKVRlpalhiaarkddtkaaalllqndh 203
Cdd:PHA02874    75 AIKIGAHDIIKLLIDNGVDTSI----------LPIPCIEKDMIKTILDCGIDVNIK------------------------ 120

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  204 naDVESKsgfTPLHIAAHYGNINVATLLLNRGAAVDFTARNDITPLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPLH 283
Cdd:PHA02874   121 --DAELK---TFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLH 195

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  284 CGARSGHEQVVEMLLDRGAPILSKTKNGLSPLHMATQGDHlNCVQLLIqHNVPVDDVTNDYLTALHVAAH--CGhYKVAK 361
Cdd:PHA02874   196 NAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLI-NNASINDQDIDGSTPLHHAINppCD-IDIID 272

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 2023156728  362 VLLDKKANPNAKALNGFTPLHIACKK-NRIKVMELLLKHGASIQAV 406
Cdd:PHA02874   273 ILLYHKADISIKDNKGENPIDTAFKYiNKDPVIKDIIANAVLIKEA 318
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 411-681 8.98e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 93.02  E-value: 8.98e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  411 LTPIHVAAFMGHVNIVSQLMHHGASPNTTNVRGETALHMAARA----GQTEVVRYLVQNGAQVEAKAKDDqtplhiSARL 486
Cdd:PHA02878    38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEpnklGMKEMIRSINKCSVFYTLVAIKD------AFNN 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  487 GKADIVQQLLQQGASPNAATTSGYTPLHLSAREGHEDVASVLLDHGASLSIITK-KGFTPLHVAAKYGKIEVANLLLQKN 565
Cdd:PHA02878   112 RNVEIFKIILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYG 191

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  566 ASPDASGKSGLTPLHVAAHYDNQKVALLLLDQGASPHASAKNGYTPLHIAAKK-NQMDIATTLLEYGADANA-VTRQGIA 643
Cdd:PHA02878   192 ANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAkSYILGLT 271

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 2023156728  644 PVHLASQDGhvDMVSLLLTRNANVNLGNKSGLTPLHLA 681
Cdd:PHA02878   272 ALHSSIKSE--RKLKLLLEYGADINSLNSYKLTPLSSA 307
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 447-741 1.88e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 92.25  E-value: 1.88e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  447 LHMAARAGQTEVVRYLVQNGAQVEAKAKDDQTPLHISA----RLGKADIVQQLLQQGAspnaattsGYTPLHLSAREGHE 522
Cdd:PHA02878    41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICkepnKLGMKEMIRSINKCSV--------FYTLVAIKDAFNNR 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  523 DV---ASVLLDHGASLSIITKKgftPLHVAAKYGKIE--VANLLLQKNASPDASGK-SGLTPLHVAAHYDNQKVALLLLD 596
Cdd:PHA02878   113 NVeifKIILTNRYKNIQTIDLV---YIDKKSKDDIIEaeITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLS 189

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  597 QGASPHASAKNGYTPLHIAAKKNQMDIATTLLEYGADANAVTRQGIAPVHLASqdGHV---DMVSLLLTRNANVNLgnKS 673
Cdd:PHA02878   190 YGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISV--GYCkdyDILKLLLEHGVDVNA--KS 265

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2023156728  674 ---GLTPLHLAAQDDRvnVAEVLVNQGAAVDAQTKMGYTPLHV------GCHYGNIKIVNFLLQHSAKVNAKTKNGY 741
Cdd:PHA02878   266 yilGLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPLSSavkqylCINIGRILISNICLLKRIKPDIKNSEGF 340
Death pfam00531
Death domain;
4043-4121 8.89e-17

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 78.18  E-value: 8.89e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728 4043 RMAIVADH---LGLSWTELARELNFSVDEINQIRVENPNsLIAQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIVTL 4119
Cdd:pfam00531    3 QLDRLLDPpppLGKDWRELARKLGLSENEIDEIESENPR-LRSQTYELLRLWEQREGKNATVGTLLEALRKLGRRDAAEK 81


                   ..
gi 2023156728 4120 LE 4121
Cdd:pfam00531   82 IQ 83
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 543-782 9.74e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 86.86  E-value: 9.74e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  543 FTPLHVAAKYGKIEVANLLLQKNASPDASGKSGLTPLHVAAHYDNQkvalllldQGASPHASAKN----GYTPLHI--AA 616
Cdd:PHA02878    38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNK--------LGMKEMIRSINkcsvFYTLVAIkdAF 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  617 KKNQMDIATTLLEYGADANavtrQGIAPVHL--ASQDGHVD--MVSLLLTRNANVNLGNK-SGLTPLHLAAQDDRVNVAE 691
Cdd:PHA02878   110 NNRNVEIFKIILTNRYKNI----QTIDLVYIdkKSKDDIIEaeITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTE 185

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  692 VLVNQGAAVDAQTKMGYTPLHVGCHYGNIKIVNFLLQHSAKVNAKTKNGYTPLHQAAQQGHTH-IINVLLQHGAAPN-EL 769
Cdd:PHA02878   186 LLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDYdILKLLLEHGVDVNaKS 265

                          250
                   ....*....|...
gi 2023156728  770 TVNGNTALAIAKR 782
Cdd:PHA02878   266 YILGLTALHSSIK 278
Ank_2 pfam12796
Ankyrin repeats (3 copies);
711-792 1.10e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.85  E-value: 1.10e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  711 LHVGCHYGNIKIVNFLLQHSAKVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAApnELTVNGNTALAIAKRLGYISVVD 790
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78


                   ..
gi 2023156728  791 TL 792
Cdd:pfam12796   79 LL 80
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 351-563 1.25e-14

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: 80.90  E-value: 1.25e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  351 AAHCGHYKVAKVLLD--KKANPNAKALNGFTPLHIACKKNRIK-VMELLLKHGASIqavtESGLTPIHVAAfMGHVNIVS 427
Cdd:TIGR00870   24 AAERGDLASVYRDLEepKKLNINCPDRLGRSALFVAAIENENLeLTELLLNLSCRG----AVGDTLLHAIS-LEYVDAVE 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  428 QLM-----HHGASPNTTNV---------RGETALHMAARAGQTEVVRYLVQNGAQVEAKAKDD--------------QTP 479
Cdd:TIGR00870   99 AILlhllaAFRKSGPLELAndqytseftPGITALHLAAHRQNYEIVKLLLERGASVPARACGDffvksqgvdsfyhgESP 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  480 LHISARLGKADIVQQLLQQGASPNAATTSGYTPLHLSAREGHEDVA---------SVLLDHGA------SLSIITK-KGF 543
Cdd:TIGR00870  179 LNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVMENEFKAEyeelscqmyNFALSLLDklrdskELEVILNhQGL 258

                          250       260
                   ....*....|....*....|
gi 2023156728  544 TPLHVAAKYGKIEVANLLLQ 563
Cdd:TIGR00870  259 TPLKLAAKEGRIVLFRLKLA 278
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 619-792 1.27e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 79.65  E-value: 1.27e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  619 NQMDIATTLLEYGADANAVTRQGIAPVHLASQDGHVDMVSLLLTRNANVNLGNKSGLTPLHLAAQDDRVNVAEVLVNQGA 698
Cdd:PHA02875    13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  699 -AVDAQTKMGYTPLHVGCHYGNIKIVNFLLQHSAKVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAAPNELTVNGNTAL 777
Cdd:PHA02875    93 fADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPL 172

                          170
                   ....*....|....*
gi 2023156728  778 AIAKRLGYISVVDTL 792
Cdd:PHA02875   173 IIAMAKGDIAICKML 187
PHA02798 PHA02798
ankyrin-like protein; Provisional
 46-366 4.22e-14

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 78.72  E-value: 4.22e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728   46 ISNQNGLNALHLASKEGHVEVVSELIQRGASVDAATKKGNTAL-----HIASLAGQAEVVKVLVTNRANVNAQSQNGFTP 120
Cdd:PHA02798    33 IVNEYSIFQKYLQRDSPSTDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETP 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  121 LYMAAQE---NHLEVVKFLLDNGASQSLATEDGFTPLAVALQQGHD---QVVSLLLEndtKGkvrlpaLHIaarkddtka 194
Cdd:PHA02798   113 LYCLLSNgyiNNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLE---KG------VDI--------- 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  195 aalllqNDHNadveSKSGFTPLHIAAHYG----NINVATLLLNRGAAVD----FTARNDI---TPLHVASKRGNANMVKL 263
Cdd:PHA02798   175 ------NTHN----NKEKYDTLHCYFKYNidriDADILKLFVDNGFIINkenkSHKKKFMeylNSLLYDNKRFKKNILDF 244

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  264 LLdrgAKIDAKTRD--GLTPLHCGARSGHEQVVEMLLDRGAPILSKTKNGLSPLHMATQGDHLNCVQLLIQHNVPVDDVT 341
Cdd:PHA02798   245 IF---SYIDINQVDelGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKPNKNTIS 321

                          330       340
                   ....*....|....*....|....*
gi 2023156728  342 NDYltalhvaahcghYKVAKVLLDK 366
Cdd:PHA02798   322 YTY------------YKLRKHILNV 334
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 544-728 6.04e-14

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 78.52  E-value: 6.04e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  544 TPLHVAAKYGKIE-VANLLLQKNASPDASGKSGLTPLHVAAHYDNQKVALLLLDqgASPH-------ASAKNGYTPLHIA 615
Cdd:cd22192     19 SPLLLAAKENDVQaIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPElvnepmtSDLYQGETALHIA 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  616 AKKNQMDIATTLLEYGADANAVTRQGIA--------------PVHLASQDGHVDMVSLLLTRNANVNLGNKSGLTPLH-L 680
Cdd:cd22192     97 VVNQNLNLVRELIARGADVVSPRATGTFfrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHiL 176

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2023156728  681 AAQDDRVNVAEV---LVNQGAAVDAQT------KMGYTPLHVGCHYGNIKIVNFLLQ 728
Cdd:cd22192    177 VLQPNKTFACQMydlILSYDKEDDLQPldlvpnNQGLTPFKLAAKEGNIVMFQHLVQ 233
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 484-671 6.29e-14

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 78.76  E-value: 6.29e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  484 ARLGKADIVQQLLQQGASPNAATTSGYTPLHLSAREGHEDVASVLLDHGASLSIITKKGFTPLHVAAKYGKIEVANLLLQ 563
Cdd:PLN03192   533 ASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYH 612

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  564 KNASPDasgksgltplhvaahydnqkvalllldqgasPHASAKngytPLHIAAKKNQMDIATTLLEYGADANAVTRQGIA 643
Cdd:PLN03192   613 FASISD-------------------------------PHAAGD----LLCTAAKRNDLTAMKELLKQGLNVDSEDHQGAT 657

                          170       180
                   ....*....|....*....|....*...
gi 2023156728  644 PVHLASQDGHVDMVSLLLTRNANVNLGN 671
Cdd:PLN03192   658 ALQVAMAEDHVDMVRLLIMNGADVDKAN 685
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 25-171 2.33e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 75.80  E-value: 2.33e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728   25 AARAGNLEKALDYLKSGVDIN-ISNQNGLNALHLASKEGHVEVVSELIQRGASVDAATKKGNTALHIASLAGQAEVVKVL 103
Cdd:PHA02875    75 AVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELL 154

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2023156728  104 VTNRANVNAQSQNGFTPLYMAAQENHLEVVKFLLDNGASQSLATEDG-FTPLAVALQQGHDQVVSLLLE 171
Cdd:PHA02875   155 IDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIK 223
PHA02946 PHA02946
ankyin-like protein; Provisional
 561-772 3.20e-13

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 75.48  E-value: 3.20e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  561 LLQKNASPDASGKSGLTPLHVAAHYDNQKVALLLLDQGASPHASAKNGYTPLHIAAKKNQ--MDIATTLLEYGADA-NAV 637
Cdd:PHA02946    58 LLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKInNSV 137

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  638 TRQGIAPVhLASQDGHVDMVSLLLTRNANVNLGNKSGLTPL--HLAAQDDRVNVAEVLVNQGAAVDAQTKMGYTPLHVGC 715
Cdd:PHA02946   138 DEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFGKNHIhrHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVC 216

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  716 H--YGNIKIVNFLLQhSAKVNAKTKNGYTPLHQAAQQ-GHTHIINVLLQHGAAPNELTVN 772
Cdd:PHA02946   217 SktVKNVDIINLLLP-STDVNKQNKFGDSPLTLLIKTlSPAHLINKLLSTSNVITDQTVN 275
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 119-332 5.46e-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: 75.43  E-value: 5.46e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  119 TPLYMAAQENHLEVVKFLLDNgasqslATEDGFTplavalqqghdqvvslllendtKGKVRLPALHIAARKDDTKAAALL 198
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLLKC------PSCDLFQ----------------------RGALGETALHVAALYDNLEAAVVL 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  199 LQNDH---NADVESK--SGFTPLHIAAHYGNINVATLLLNRGAAVdFTARNDIT---------------PLHVASKRGNA 258
Cdd:cd22192     71 MEAAPelvNEPMTSDlyQGETALHIAVVNQNLNLVRELIARGADV-VSPRATGTffrpgpknliyygehPLSFAACVGNE 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  259 NMVKLLLDRGAKIDAKTRDGLTPLH-----------CgarsgheQVVEMLL-----DRGAPiLSKTKN--GLSPLHMATQ 320
Cdd:cd22192    150 EIVRLLIEHGADIRAQDSLGNTVLHilvlqpnktfaC-------QMYDLILsydkeDDLQP-LDLVPNnqGLTPFKLAAK 221

                          250
                   ....*....|..
gi 2023156728  321 GDHLNCVQLLIQ 332
Cdd:cd22192    222 EGNIVMFQHLVQ 233
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 440-564 6.68e-13

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 75.18  E-value: 6.68e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  440 NVRGETALHMAARAGQTEVVRYLVQNGAQVEAKAKDD--------------QTPLHISARLGKADIVQQLLQQGASPNAA 505
Cdd:cd22194    138 AYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVffnpkykhegfyfgETPLALAACTNQPEIVQLLMEKESTDITS 217

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2023156728  506 TTS-GYTPLH---LSAREGHEDVASV-------LLDH-GASLSIIT-KKGFTPLHVAAKYGKIEVANLLLQK 564
Cdd:cd22194    218 QDSrGNTVLHalvTVAEDSKTQNDFVkrmydmiLLKSeNKNLETIRnNEGLTPLQLAAKMGKAEILKYILSR 289
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 346-564 1.62e-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: 73.89  E-value: 1.62e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  346 TALHVAAHCGHYKVAKVLLDKKA----NPNAKAL-NGFTPLHIACKKNRIKVMELLLKHGASIQAVTESGLtpihvaAFm 420
Cdd:cd22192     53 TALHVAALYDNLEAAVVLMEAAPelvnEPMTSDLyQGETALHIAVVNQNLNLVRELIARGADVVSPRATGT------FF- 125

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  421 ghvnivsqlmhhgaSPNTTNV--RGETALHMAARAGQTEVVRYLVQNGAQVEAKAKDDQTPLHISARLGKADIVQQLLQQ 498
Cdd:cd22192    126 --------------RPGPKNLiyYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFACQMYDL 191

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2023156728  499 gaspnaattsgytplhLSAREGHEDVASvlLDHgaslsIITKKGFTPLHVAAKYGKIEVANLLLQK 564
Cdd:cd22192    192 ----------------ILSYDKEDDLQP--LDL-----VPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 478-695 1.80e-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: 73.89  E-value: 1.80e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  478 TPLHISARLGKADIVQQLL-QQGASPNAATTSGYTPLHLSAREGHEDVASVLLDHGASL--SIITK---KGFTPLHVAAK 551
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELvnEPMTSdlyQGETALHIAVV 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  552 YGKIEVANLLLQKNA---SPDASG------KSGLT-----PLHVAAHYDNQKVALLLLDQGASPHASAKNGYTPLHIAAK 617
Cdd:cd22192     99 NQNLNLVRELIARGAdvvSPRATGtffrpgPKNLIyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVL 178

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2023156728  618 KNQMDIATTLLEYgadanavtrqgiapvhLASQDGHVDMVSLLLTRnanvnlgNKSGLTPLHLAAQDDRVNVAEVLVN 695
Cdd:cd22192    179 QPNKTFACQMYDL----------------ILSYDKEDDLQPLDLVP-------NNQGLTPFKLAAKEGNIVMFQHLVQ 233
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 617-792 2.05e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 73.56  E-value: 2.05e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  617 KKNQMDIATTLLEYGADANAVTRQGIAPVHLASQDGHVDMVSLLLTRNANVNLGNKSGLTPLHLAAQ-----------DD 685
Cdd:PHA02876   154 QQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDsknidtikaiiDN 233

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  686 RVNVAE------------------VLVNQGAAVDAQTKMGYTPLHVGCHYGNI-KIVNFLLQHSAKVNAKTKNGYTPLHQ 746
Cdd:PHA02876   234 RSNINKndlsllkairnedletslLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYL 313

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2023156728  747 AAQQGH-THIINVLLQHGAAPNELTVNGNTALAIAKRLG-YISVVDTL 792
Cdd:PHA02876   314 MAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITL 361
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 75-234 6.39e-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: 72.10  E-value: 6.39e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728   75 ASVDAATKKGNTALHIASLAGQAEVVKVLVTNRANVNAQSQNGF--------------TPLYMAAQENHLEVVKFLLDNG 140
Cdd:cd22194    132 AEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVFfnpkykhegfyfgeTPLALAACTNQPEIVQLLMEKE 211

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  141 asqslatedgftPLAVALQqghdqvvslllenDTKGKVRLPALHIAArkDDTKAAA--------LLLQNDHNADVE---S 209
Cdd:cd22194    212 ------------STDITSQ-------------DSRGNTVLHALVTVA--EDSKTQNdfvkrmydMILLKSENKNLEtirN 264

                          170       180
                   ....*....|....*....|....*
gi 2023156728  210 KSGFTPLHIAAHYGNINVATLLLNR 234
Cdd:cd22194    265 NEGLTPLQLAAKMGKAEILKYILSR 289
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 20-172 1.92e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 70.67  E-value: 1.92e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728   20 ASYLRAARAGNLEKALDYLKSGVDINISNQNGLNALHLASKEGHVEVVSELIQRGASVDAATKKGNTALHIASLAGQAEV 99
Cdd:PLN03192   527 SNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKI 606

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2023156728  100 VKVLVTNRANVNAQSqnGFTPLYMAAQENHLEVVKFLLDNGASQSLATEDGFTPLAVALQQGHDQVVSLLLEN 172
Cdd:PLN03192   607 FRILYHFASISDPHA--AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMN 677
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 346-567 1.93e-11

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: 70.29  E-value: 1.93e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  346 TALHVAA---HCGHYKVAKVLLD---KKANP----NAKALN----GFTPLHIACKKNRIKVMELLLKHGASIQAVTESgl 411
Cdd:cd21882     28 TCLHKAAlnlNDGVNEAIMLLLEaapDSGNPkelvNAPCTDefyqGQTALHIAIENRNLNLVRLLVENGADVSARATG-- 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  412 tpihvAAFMGHvnivsqlmhhgasPNTTNVRGETALHMAARAGQTEVVRYLVQNGAQVEAKAKDD---QTPLHIsarlgk 488
Cdd:cd21882    106 -----RFFRKS-------------PGNLFYFGELPLSLAACTNQEEIVRLLLENGAQPAALEAQDslgNTVLHA------ 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  489 adIVQQLLQQGASPNAATTSGYTPLHLSAReghedvasvlLDHGASLSIIT-KKGFTPLHVAAKYGKIEVANLLLQKNAS 567
Cdd:cd21882    162 --LVLQADNTPENSAFVCQMYNLLLSYGAH----------LDPTQQLEEIPnHQGLTPLKLAAVEGKIVMFQHILQREFS 229
PHA03095 PHA03095
ankyrin-like protein; Provisional
 682-779 3.20e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 69.28  E-value: 3.20e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  682 AQDDRVNVAEV--LVNQGAAVDAQTKMGYTPLHVGCHYGN---IKIVNFLLQHSAKVNAKTKNGYTPLHQAAQQGHT-HI 755
Cdd:PHA03095    20 LNASNVTVEEVrrLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDV 99

                           90       100
                   ....*....|....*....|....
gi 2023156728  756 INVLLQHGAAPNELTVNGNTALAI 779
Cdd:PHA03095   100 IKLLIKAGADVNAKDKVGRTPLHV 123
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 393-546 4.19e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 69.51  E-value: 4.19e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  393 MELLLKHGASIQAVTESGLTPIHVAAFMGHVNIVSQLMHHGASPNTTNVRGETALHMAARAGQTEVVRYLVQNGAQVEAK 472
Cdd:PLN03192   541 LEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPH 620

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2023156728  473 AKDDQtpLHISARLGKADIVQQLLQQGASPNAATTSGYTPLHLSAREGHEDVASVLLDHGASLSII-TKKGFTPL 546
Cdd:PLN03192   621 AAGDL--LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAnTDDDFSPT 693
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 693-792 4.23e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 68.54  E-value: 4.23e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  693 LVNQGAAVDAQTKMGYTPLHVGCHYGNIKIVNFLLQHSAKVNAKTKNGYTPLHQAAQQGH--TH---IINVLLQHGAAPN 767
Cdd:PHA03100    21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnlTDvkeIVKLLLEYGANVN 100

                           90       100
                   ....*....|....*....|....*..
gi 2023156728  768 ELTVNGNTALAIA--KRLGYISVVDTL 792
Cdd:PHA03100   101 APDNNGITPLLYAisKKSNSYSIVEYL 127
Ank_4 pfam13637
Ankyrin repeats (many copies);
410-463 4.56e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 60.75  E-value: 4.56e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2023156728  410 GLTPIHVAAFMGHVNIVSQLMHHGASPNTTNVRGETALHMAARAGQTEVVRYLV 463
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 8-171 6.30e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 68.51  E-value: 6.30e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728    8 LDYILRKMSDTNAS----------YLRAARAgNLEkALDYL-KSGVDINISNQNGLNALH--LASKEGHVEVVSELIQRG 74
Cdd:PHA03095   135 IRLLLRKGADVNALdlygmtplavLLKSRNA-NVE-LLRLLiDAGADVYAVDDRFRSLLHhhLQSFKPRARIVRELIRAG 212

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728   75 ASVDAATKKGNTALHIASLAGQAEVVKV--LVTNRANVNAQSQNGFTPLYMAAQENHLEVVKFLLDNGASQSLATEDGFT 152
Cdd:PHA03095   213 CDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNT 292

                          170
                   ....*....|....*....
gi 2023156728  153 PLAVALQQGHDQVVSLLLE 171
Cdd:PHA03095   293 PLSLMVRNNNGRAVRAALA 311
Ank_4 pfam13637
Ankyrin repeats (many copies);
344-397 7.01e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.98  E-value: 7.01e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2023156728  344 YLTALHVAAHCGHYKVAKVLLDKKANPNAKALNGFTPLHIACKKNRIKVMELLL 397
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
247-298 7.66e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.98  E-value: 7.66e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2023156728  247 TPLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPLHCGARSGHEQVVEMLL 298
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 30-170 7.70e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 68.55  E-value: 7.70e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728   30 NLEKALDYLKSGVDINISNQNGLNALHLASKEGHVEVVSELIQRGASVDAATKKGNTALHIAsLAGQAEV--VKVLVTNR 107
Cdd:PHA02876   354 NKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFA-LCGTNPYmsVKTLIDRG 432

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2023156728  108 ANVNAQSQNGFTPLYMAAQEN-HLEVVKFLLDNGASQSLATEDGFTPLAVALqqGHDQVVSLLL 170
Cdd:PHA02876   433 ANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILL 494
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 55-234 8.21e-11

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 68.50  E-value: 8.21e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728   55 LHLASKEGHVEVVSELI--------QRGASvdaatkkGNTALHIASLAGQAEVVKVLVTNR---ANVNAQSQ--NGFTPL 121
Cdd:cd22192     21 LLLAAKENDVQAIKKLLkcpscdlfQRGAL-------GETALHVAALYDNLEAAVVLMEAApelVNEPMTSDlyQGETAL 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  122 YMAAQENHLEVVKFLLDNGASQSLATEDG--FT------------PLAVALQQGHDQVVSLLLEN--DTKGKVRL--PAL 183
Cdd:cd22192     94 HIAVVNQNLNLVRELIARGADVVSPRATGtfFRpgpknliyygehPLSFAACVGNEEIVRLLIEHgaDIRAQDSLgnTVL 173

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2023156728  184 HIAARKDDTKAAA----LLLQNDHNAD------VESKSGFTPLHIAAHYGNINVATLLLNR 234
Cdd:cd22192    174 HILVLQPNKTFACqmydLILSYDKEDDlqpldlVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
PHA02946 PHA02946
ankyin-like protein; Provisional
 426-812 1.58e-10

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 67.00  E-value: 1.58e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  426 VSQLMHHGASPNTTNVRGETALHMAARAGQTEVVRYLVQNGAQVEAKAKDDQTPLHISARLGKADI--VQQLLQQGAS-P 502
Cdd:PHA02946    55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIerINLLVQYGAKiN 134

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  503 NAATTSGYTPLhLSAREGHEDVASVLLDHGASLSIITkkgftplhvaaKYGKIEVANLLLQKNasPDASGKSGLTPLhva 582
Cdd:PHA02946   135 NSVDEEGCGPL-LACTDPSERVFKKIMSIGFEARIVD-----------KFGKNHIHRHLMSDN--PKASTISWMMKL--- 197

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  583 ahydnqkvalllldqGASPHASAKNGYTPLHIAAKKN--QMDIATTLLEyGADANAVTRQGIAPVHLASQD-GHVDMVSL 659
Cdd:PHA02946   198 ---------------GISPSKPDHDGNTPLHIVCSKTvkNVDIINLLLP-STDVNKQNKFGDSPLTLLIKTlSPAHLINK 261

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  660 LLTrNANVNLGNKSGLTPLHlaaqdDRVNVAEVLVNQGAAVDAqtkmgyTPLHVGCHYGNIKIVNFLLQHSakVNAKTKN 739
Cdd:PHA02946   262 LLS-TSNVITDQTVNICIFY-----DRDDVLEIINDKGKQYDS------TDFKMAVEVGSIRCVKYLLDND--IICEDAM 327

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2023156728  740 GYTPLHQAaqqgHTHIINVLLQHGAApnELTVNGNTALAIAKRLGYISVVDTLKV--VTEETM-TTITVTEKHKMN 812
Cdd:PHA02946   328 YYAVLSEY----ETMVDYLLFNHFSV--DSVVNGHTCMSECVRLNNPVILSKLMLhnPTSETMyLTMKAIEKDKLD 397
PHA02798 PHA02798
ankyrin-like protein; Provisional
 456-758 1.84e-10

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 66.78  E-value: 1.84e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  456 TEVVRYLVQNGAQVEAKAKDDQTPL-----HISARLGKADIVQQLLQQGASPNAATTSGYTPLHLSAREGH---EDVASV 527
Cdd:PHA02798    51 TDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYinnLEILLF 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  528 LLDHGASLSIITKKGFTPLHVAAKYG---KIEVANLLLQKNASPDA-SGKSGLTPLHVAAHYD----NQKVALLLLDQGA 599
Cdd:PHA02798   131 MIENGADTTLLDKDGFTMLQVYLQSNhhiDIEIIKLLLEKGVDINThNNKEKYDTLHCYFKYNidriDADILKLFVDNGF 210

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  600 SPHASAKngytplhiAAKKNQMDIATTLLEYGADANAvtrqgiapvhlasqdghvDMVSLLLTRnANVNLGNKSGLTPLH 679
Cdd:PHA02798   211 IINKENK--------SHKKKFMEYLNSLLYDNKRFKK------------------NILDFIFSY-IDINQVDELGFNPLY 263

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  680 LAAQDDRVNVAEVLVNQGAAVDAQTKMGYTPLHVGCHYGNIKIVNFLLQHsaKVNAKT-KNGYTPLHQaaqqghtHIINV 758
Cdd:PHA02798   264 YSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNK--KPNKNTiSYTYYKLRK-------HILNV 334
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 286-440 1.89e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 67.59  E-value: 1.89e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  286 ARSGHEQVVEMLLDRG-APILSKTKnGLSPLHMATQGDHLNCVQLLIQH--NVPVDDVTNDylTALHVAAHCGHYKVAKV 362
Cdd:PLN03192   533 ASTGNAALLEELLKAKlDPDIGDSK-GRTPLHIAASKGYEDCVLVLLKHacNVHIRDANGN--TALWNAISAKHHKIFRI 609

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  363 L--LDKKANPNAkalnGFTPLHIACKKNRIKVMELLLKHGASIQAVTESGLTPIHVAAFMGHVNIVSQLMHHGASPNTTN 440
Cdd:PLN03192   610 LyhFASISDPHA----AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
Ank_4 pfam13637
Ankyrin repeats (many copies);
379-427 2.06e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.83  E-value: 2.06e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2023156728  379 TPLHIACKKNRIKVMELLLKHGASIQAVTESGLTPIHVAAFMGHVNIVS 427
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLK 51
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 225-497 2.06e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 66.69  E-value: 2.06e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  225 INVATLLLNRGAAVDFTAR-NDITPLHVASKRGNANMVKLLLDRGAKIDAKtrdGL--TPLHCGAR------SGHEQVVE 295
Cdd:PHA02989    16 KNALEFLLRTGFDVNEEYRgNSILLLYLKRKDVKIKIVKLLIDNGADVNYK---GYieTPLCAVLRnreitsNKIKKIVK 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  296 MLLDRGAPILSKTKNGLSPLHMATQGDHLNCV---QLLIQHNVPVDDVTND--------YLTALHVAAHcghykVAKVLL 364
Cdd:PHA02989    93 LLLKFGADINLKTFNGVSPIVCFIYNSNINNCdmlRFLLSKGINVNDVKNSrgynllhmYLESFSVKKD-----VIKILL 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  365 DKKANPNAKA-LNGFTPLHIACKKN----RIKVMELLLKHGASI-------QAVTESGLTPiHVAAFMGHVNIVSQLMHH 432
Cdd:PHA02989   168 SFGVNLFEKTsLYGLTPMNIYLRNDidviSIKVIKYLIKKGVNIetnnngsESVLESFLDN-NKILSKKEFKVLNFILKY 246

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2023156728  433 gASPNTTNVRGETALHMAARAGQTEVVRYLVQNGAQVEAKAKDDQTPLHISARLGKADIVQQLLQ 497
Cdd:PHA02989   247 -IKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNRILQ 310
Ank_4 pfam13637
Ankyrin repeats (many copies);
51-104 3.19e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.44  E-value: 3.19e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2023156728   51 GLNALHLASKEGHVEVVSELIQRGASVDAATKKGNTALHIASLAGQAEVVKVLV 104
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
707-760 3.70e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.05  E-value: 3.70e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2023156728  707 GYTPLHVGCHYGNIKIVNFLLQHSAKVNAKTKNGYTPLHQAAQQGHTHIINVLL 760
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 216-464 3.97e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 65.92  E-value: 3.97e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  216 LHIAAHYGNINVATLLLNRGAAVDFTARNDiTPL-------HVASKRGNaNMVKLLLDRGAKIDAKTRDGLTPLHCGARS 288
Cdd:PHA02989    41 LYLKRKDVKIKIVKLLIDNGADVNYKGYIE-TPLcavlrnrEITSNKIK-KIVKLLLKFGADINLKTFNGVSPIVCFIYN 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  289 GHEQVVEML---LDRGAPILS-KTKNGLSPLHMATQGDHLN--CVQLLIQHNVPVDDVTNDY-LTALHV----AAHCGHY 357
Cdd:PHA02989   119 SNINNCDMLrflLSKGINVNDvKNSRGYNLLHMYLESFSVKkdVIKILLSFGVNLFEKTSLYgLTPMNIylrnDIDVISI 198

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  358 KVAKVLLDKKA---NPNA---KALNGFTPLHIACKKNRIKVMELLLKHgASIQAVTESGLTPIHVAAFMGHVNIVSQLMH 431
Cdd:PHA02989   199 KVIKYLIKKGVnieTNNNgseSVLESFLDNNKILSKKEFKVLNFILKY-IKINKKDKKGFNPLLISAKVDNYEAFNYLLK 277

                          250       260       270
                   ....*....|....*....|....*....|...
gi 2023156728  432 HGASPNTTNVRGETALHMAARAGQTEVVRYLVQ 464
Cdd:PHA02989   278 LGDDIYNVSKDGDTVLTYAIKHGNIDMLNRILQ 310
PHA02798 PHA02798
ankyrin-like protein; Provisional
 225-450 4.32e-10

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 65.63  E-value: 4.32e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  225 INVATLLLNRGAAVDFTARNDITPL-----HVASKRGNANMVKLLLDRGAKIDAKTRDGLTPLHCGARSGHEQVVEMLL- 298
Cdd:PHA02798    51 TDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLf 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  299 --DRGAPILSKTKNGLSPLHMATQGDH---LNCVQLLIQHNVPVDDVTNDY-LTALHV----AAHCGHYKVAKVLLD--- 365
Cdd:PHA02798   131 miENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINTHNNKEkYDTLHCyfkyNIDRIDADILKLFVDngf 210

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  366 --KKANPNAKA--LNGFTPLHIACKKNRIKVMELLLKHgASIQAVTESGLTPIHVAAFMGHVNIVSQLMHHGASPNTTNV 441
Cdd:PHA02798   211 iiNKENKSHKKkfMEYLNSLLYDNKRFKKNILDFIFSY-IDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITE 289


                   ....*....
gi 2023156728  442 RGETALHMA 450
Cdd:PHA02798   290 LGNTCLFTA 298
Ank_4 pfam13637
Ankyrin repeats (many copies);
278-331 4.77e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 57.67  E-value: 4.77e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2023156728  278 GLTPLHCGARSGHEQVVEMLLDRGAPILSKTKNGLSPLHMATQGDHLNCVQLLI 331
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 82-414 4.99e-10

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 66.09  E-value: 4.99e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728   82 KKGNTALH--IASLAGQAEVVKVLVTNRANVNAQSQNGFTPL--YMAAQENHLEVVKFLLDNGASQSLATEDGFTPLAVA 157
Cdd:PHA02716   175 KTGYGILHayLGNMYVDIDILEWLCNNGVNVNLQNNHLITPLhtYLITGNVCASVIKKIIELGGDMDMKCVNGMSPIMTY 254

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  158 LQQG---HDQVVSLLLENDTKGKVR-LPA-LHI---AARKDDTKAAALLLQNDHNADVESKSGFTPLH--IAAHYGNINV 227
Cdd:PHA02716   255 IINIdniNPEITNIYIESLDGNKVKnIPMiLHSyitLARNIDISVVYSFLQPGVKLHYKDSAGRTCLHqyILRHNISTDI 334

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  228 ATLLLNRGAAVDFTARNDITPLHVASKRG--------------NANMVKLLLDRGAKIDAKTRDGLTPLH---CGARS-G 289
Cdd:PHA02716   335 IKLLHEYGNDLNEPDNIGNTVLHTYLSMLsvvnildpetdndiRLDVIQCLISLGADITAVNCLGYTPLTsyiCTAQNyM 414

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  290 HEQVVEMLLDRgaPILSKTKNGLSPlHMATQGDHLNCV--QLLIQHNVPVDDVTNDY----LTALHVAAHCGhykvakvl 363
Cdd:PHA02716   415 YYDIIDCLISD--KVLNMVKHRILQ-DLLIRVDDTPCIihHIIAKYNIPTDLYTDEYepydSTKIHDVYHCA-------- 483

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2023156728  364 LDKKANPNAKALNGFTPLHIA--CKKNRIKVME---LLLKHGASIQAVTESGLTPI 414
Cdd:PHA02716   484 IIERYNNAVCETSGMTPLHVSiiSHTNANIVMDsfvYLLSIQYNINIPTKNGVTPL 539
Ank_4 pfam13637
Ankyrin repeats (many copies);
84-137 7.77e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 57.28  E-value: 7.77e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2023156728   84 GNTALHIASLAGQAEVVKVLVTNRANVNAQSQNGFTPLYMAAQENHLEVVKFLL 137
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 442-564 9.77e-10

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: 64.82  E-value: 9.77e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  442 RGETALHMAARAGQTEVVRYLVQNGAQVEAKAKDD--------------QTPLHISARLGKADIVQQLLQ---QGASPNA 504
Cdd:cd22193     75 EGQTALHIAIERRQGDIVALLVENGADVHAHAKGRffqpkyqgegfyfgELPLSLAACTNQPDIVQYLLEnehQPADIEA 154

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2023156728  505 ATTSGYTPLHL------SAREGHEDVASV---LLDHGASL-------SIITKKGFTPLHVAAKYGKIEVANLLLQK 564
Cdd:cd22193    155 QDSRGNTVLHAlvtvadNTKENTKFVTRMydmILIRGAKLcptveleEIRNNDGLTPLQLAAKMGKIEILKYILQR 230
Ank_4 pfam13637
Ankyrin repeats (many copies);
608-661 1.72e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.13  E-value: 1.72e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2023156728  608 GYTPLHIAAKKNQMDIATTLLEYGADANAVTRQGIAPVHLASQDGHVDMVSLLL 661
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 112-419 3.19e-09

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 63.56  E-value: 3.19e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  112 AQSQNGFTPlymAAQENHLEVVKFLLDNGASQSLATED--GFTPLAVALQQG-HDQVVSLLLENDTKGKVRLPALHiAAR 188
Cdd:TIGR00870   15 SDEEKAFLP---AAERGDLASVYRDLEEPKKLNINCPDrlGRSALFVAAIENeNLELTELLLNLSCRGAVGDTLLH-AIS 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  189 KDDTKAAALLLQndHNADVESKSGFTPLHIAAHYGninvatlllnrgaavDFTArnDITPLHVASKRGNANMVKLLLDRG 268
Cdd:TIGR00870   91 LEYVDAVEAILL--HLLAAFRKSGPLELANDQYTS---------------EFTP--GITALHLAAHRQNYEIVKLLLERG 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  269 AKIDAKT--------------RDGLTPLHCGARSGHEQVVEMLLDRGAPILSKTKNGLSPLHMAtqgdhlncvqlliqhn 334
Cdd:TIGR00870  152 ASVPARAcgdffvksqgvdsfYHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLL---------------- 215

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  335 VPVDDVTNDYLTalhVAAHCghYKVAKVLLDKKANPNAKAL----NGFTPLHIACKKNRIKVMELLLKHGASIQAVTESG 410
Cdd:TIGR00870  216 VMENEFKAEYEE---LSCQM--YNFALSLLDKLRDSKELEVilnhQGLTPLKLAAKEGRIVLFRLKLAIKYKQKKFVAWP 290


                   ....*....
gi 2023156728  411 LTPIHVAAF 419
Cdd:TIGR00870  291 NGQQLLSLY 299
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 442-567 3.88e-09

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: 62.95  E-value: 3.88e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  442 RGETALHMAARAGQTEVVRYLVQNGAQVEAKAKDD-------------QTPLHISARLGKADIVQQLLQ---QGASPNAA 505
Cdd:cd22197     93 RGHSALHIAIEKRSLQCVKLLVENGADVHARACGRffqkkqgtcfyfgELPLSLAACTKQWDVVNYLLEnphQPASLQAQ 172

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2023156728  506 TTSGYTPLH---LSAREGHEDVASV------LLDHGASL-------SIITKKGFTPLHVAAKYGKIEVANLLLQKNAS 567
Cdd:cd22197    173 DSLGNTVLHalvMIADNSPENSALVikmydgLLQAGARLcptvqleEISNHEGLTPLKLAAKEGKIEIFRHILQREFS 250
Ank_4 pfam13637
Ankyrin repeats (many copies);
311-364 5.50e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.97  E-value: 5.50e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2023156728  311 GLSPLHMATQGDHLNCVQLLIQHNVPVDDVTNDYLTALHVAAHCGHYKVAKVLL 364
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 442-564 5.60e-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: 62.52  E-value: 5.60e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  442 RGETALHMAARAGQTEVVRYLVQNGAQVEAKAKDD--------------QTPLHISARLGKADIVQQLLQQGASPN--AA 505
Cdd:cd22196     93 KGQTALHIAIERRNMHLVELLVQNGADVHARASGEffkkkkggpgfyfgELPLSLAACTNQLDIVKFLLENPHSPAdiSA 172

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2023156728  506 TTS-GYTPLHL---SAREGHEDVASV------LLDHGASL-------SIITKKGFTPLHVAAKYGKIEVANLLLQK 564
Cdd:cd22196    173 RDSmGNTVLHAlveVADNTPENTKFVtkmyneILILGAKIrpllkleEITNKKGLTPLKLAAKTGKIGIFAYILGR 248
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 173-317 5.73e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 62.58  E-value: 5.73e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  173 DTKGKVrlpALHIAARKDDTKAAALLLQNDHNADVESKSGFTPLHIAAHYGNINVATLLLNRGAAVDFTARNDItpLHVA 252
Cdd:PLN03192   555 DSKGRT---PLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAGDL--LCTA 629

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2023156728  253 SKRGNANMVKLLLDRGAKIDAKTRDGLTPLHCGARSGHEQVVEMLLDRGAPIL-SKTKNGLSPLHM 317
Cdd:PLN03192   630 AKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDkANTDDDFSPTEL 695
Ank_5 pfam13857
Ankyrin repeats (many copies);
363-417 8.32e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 54.27  E-value: 8.32e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2023156728  363 LLDKK-ANPNAKALNGFTPLHIACKKNRIKVMELLLKHGASIQAVTESGLTPIHVA 417
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 588-790 8.67e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 61.68  E-value: 8.67e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  588 QKVALLLLDQGASPHASAKNGYTPL-------HIaakkNQMDIATTLLEYGADANAV-TRQGIAPVHLASQDGHV--DMV 657
Cdd:PHA02989    88 KKIVKLLLKFGADINLKTFNGVSPIvcfiynsNI----NNCDMLRFLLSKGINVNDVkNSRGYNLLHMYLESFSVkkDVI 163

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  658 SLLLtrNANVNLGNKS---GLTPLHLAAQDD----RVNVAEVLVNQGAAVDAQTKMGYTPL------HVGCHYGNIKIVN 724
Cdd:PHA02989   164 KILL--SFGVNLFEKTslyGLTPMNIYLRNDidviSIKVIKYLIKKGVNIETNNNGSESVLesfldnNKILSKKEFKVLN 241

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2023156728  725 FLLQHsAKVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAAPNELTVNGNTALAIAKRLGYISVVD 790
Cdd:PHA02989   242 FILKY-IKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLN 306
Ank_5 pfam13857
Ankyrin repeats (many copies);
528-582 1.24e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 53.89  E-value: 1.24e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2023156728  528 LLDHG-ASLSIITKKGFTPLHVAAKYGKIEVANLLLQKNASPDASGKSGLTPLHVA 582
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 481-586 1.29e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 61.45  E-value: 1.29e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  481 HISARlGKADIVQQLLQQGASPNAATTSGYTPLHLSAREGHEDVASVLLDHGASLSIITKKGFTPLHVAAKYGKIEVANL 560
Cdd:PTZ00322    88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2023156728  561 LLQ---------KNASPDA-SGKSGL---TPLhVAAHYD 586
Cdd:PTZ00322   167 LSRhsqchfelgANAKPDSfTGKPPSledSPI-SSHHPD 204
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 30-112 1.62e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 60.45  E-value: 1.62e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728   30 NLEKALDYL-KSGVDINISNQNGLNALHLASKEGHVEVVSELIQRGASVDAATKKGNTALHIASLAGQAEVVKVLVTNRA 108
Cdd:PHA03100   170 NAKNRVNYLlSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249


                   ....
gi 2023156728  109 NVNA 112
Cdd:PHA03100   250 SIKT 253
Ank_4 pfam13637
Ankyrin repeats (many copies);
575-628 1.82e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.43  E-value: 1.82e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2023156728  575 GLTPLHVAAHYDNQKVALLLLDQGASPHASAKNGYTPLHIAAKKNQMDIATTLL 628
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Death_FADD cd08306
Fas-associated Death Domain protein-protein interaction domain; Death domain (DD) found in ...
 4046-4122 2.24e-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: 54.22  E-value: 2.24e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2023156728 4046 IVADHLGLSWTELARELNFSVDEINQIRVENPNSLIAQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIVTLLEG 4122
Cdd:cd08306      7 VICENLGRDWRQLARKLGLSETKIESISEAHPRNLREQVRQSLREWKKIKKAEATVADLIKALRDCQLNLVADLVEK 83
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 530-661 2.78e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 60.30  E-value: 2.78e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  530 DHGASLSIITKKGFTPLHVAAKYGKIE--VANLL----LQKNASPDASGksgltplhvaahydnqkvALLLLDQGASPHA 603
Cdd:PTZ00322    49 THLEALEATENKDATPDHNLTTEEVIDpvVAHMLtvelCQLAASGDAVG------------------ARILLTGGADPNC 110

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2023156728  604 SAKNGYTPLHIAAKKNQMDIATTLLEYGADANAVTRQGIAPVHLASQDGHVDMVSLLL 661
Cdd:PTZ00322   111 RDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 1-147 2.91e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 59.62  E-value: 2.91e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728    1 MQVLLMLLDYILRKM-SDTNASYLRAARAGNLEKALDYLKSGVDINISNQNGLNALHLASKEGHVEVVSELIQRGASVDA 79
Cdd:PHA02875    84 VEELLDLGKFADDVFyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDI 163

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2023156728   80 ATKKGNTALHIASLAGQAEVVKVLVTNRANVNAQSQNG-FTPLYMAAQENHLEVVKFLLDNGASQSLAT 147
Cdd:PHA02875   164 EDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNIMF 232
PHA02798 PHA02798
ankyrin-like protein; Provisional
 590-780 3.30e-08

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 59.85  E-value: 3.30e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  590 VALLLLDQGASPHASAKNGYTPLHIAAKK---NQMDIATTLLEYGADANAVTRQGIAPVHLASQDGH---VDMVSLLLTR 663
Cdd:PHA02798    91 IVKILIENGADINKKNSDGETPLYCLLSNgyiNNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEK 170

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  664 NANVNL-GNKSGLTPLH--LAAQDDR--VNVAEVLVNQGAAV---DAQTKMGYTPLHVGCHYGNIK----IVNFLLQHsA 731
Cdd:PHA02798   171 GVDINThNNKEKYDTLHcyFKYNIDRidADILKLFVDNGFIInkeNKSHKKKFMEYLNSLLYDNKRfkknILDFIFSY-I 249

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 2023156728  732 KVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAAPNELTVNGNTALAIA 780
Cdd:PHA02798   250 DINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTA 298
Death_RAIDD cd08319
Death domain of RIP-associated ICH-1 homologous protein with a death domain; Death domain (DD) ...
 4040-4112 4.08e-08

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: 53.48  E-value: 4.08e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2023156728 4040 TDIRMAIVADHLGLSWTELARELNFSVDEINQIRVENPNSLIAQSFMLLKKWVTRDGKNATTDALTSVLTKIN 4112
Cdd:cd08319      1 TDRQLNKLAQRLGPEWEQVLLDLGLSKADIYRCKADHPYNVQSQIVEALVKWKQRQGKKATVQSLIQSLKAVE 73
Ank_4 pfam13637
Ankyrin repeats (many copies);
509-562 4.09e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 4.09e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2023156728  509 GYTPLHLSAREGHEDVASVLLDHGASLSIITKKGFTPLHVAAKYGKIEVANLLL 562
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
445-496 4.09e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 4.09e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2023156728  445 TALHMAARAGQTEVVRYLVQNGAQVEAKAKDDQTPLHISARLGKADIVQQLL 496
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
230-283 4.19e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 52.35  E-value: 4.19e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2023156728  230 LLLNRGAAVDFTARNDITPLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPLH 283
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
544-595 4.21e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 4.21e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2023156728  544 TPLHVAAKYGKIEVANLLLQKNASPDASGKSGLTPLHVAAHYDNQKVALLLL 595
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
214-265 4.30e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 4.30e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2023156728  214 TPLHIAAHYGNINVATLLLNRGAAVDFTARNDITPLHVASKRGNANMVKLLL 265
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 448-531 4.39e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 59.53  E-value: 4.39e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  448 HMAArAGQTEVVRYLVQNGAQVEAKAKDDQTPLHISARLGKADIVQQLLQQGASPNAATTSGYTPLHLSAREGHEDVASV 527
Cdd:PTZ00322    88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                   ....
gi 2023156728  528 LLDH 531
Cdd:PTZ00322   167 LSRH 170
Ank_4 pfam13637
Ankyrin repeats (many copies);
179-232 4.60e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 4.60e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2023156728  179 RLPALHIAARKDDTKAAALLLQNDHNADVESKSGFTPLHIAAHYGNINVATLLL 232
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 624-693 8.31e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 58.76  E-value: 8.31e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  624 ATTLLEYGADANAVTRQGIAPVHLASQDGHVDMVSLLLTRNANVNLGNKSGLTPLHLAAQDDRVNVAEVL 693
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 333-432 1.05e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 58.37  E-value: 1.05e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  333 HNVPVDDVTNDYLTAL------HVAAHcGHYKVAKVLLDKKANPNAKALNGFTPLHIACKKNRIKVMELLLKHGASIQAV 406
Cdd:PTZ00322    66 HNLTTEEVIDPVVAHMltvelcQLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLL 144

                           90       100
                   ....*....|....*....|....*.
gi 2023156728  407 TESGLTPIHVAAFMGHVNIVSQLMHH 432
Cdd:PTZ00322   145 DKDGKTPLELAEENGFREVVQLLSRH 170
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 558-760 1.32e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 58.10  E-value: 1.32e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  558 ANLLLQKNASpdasgksgLTPLHVAAHY-DNQKVALLLLDQGASPHASAKNGYTPLHIAAKKNQMDIATTLLEYGADA-- 634
Cdd:cd22192      8 LHLLQQKRIS--------ESPLLLAAKEnDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELvn 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  635 NAVTR---QGIAPVHLASQDGHVDMVSLLLTRNANVnlgnksgLTPlhlaaqddRVNVAEVLVNQGAAVdaqtKMGYTPL 711
Cdd:cd22192     80 EPMTSdlyQGETALHIAVVNQNLNLVRELIARGADV-------VSP--------RATGTFFRPGPKNLI----YYGEHPL 140

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2023156728  712 HVGCHYGNIKIVNFLLQHSAKVNAKTKNGYTPLH----QAAQQGHTHIINVLL 760
Cdd:cd22192    141 SFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHilvlQPNKTFACQMYDLIL 193
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 358-669 1.35e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 57.83  E-value: 1.35e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  358 KVAKVLLDKKANPNAKALNGfTPL-------HIACKKNRiKVMELLLKHGASIQAVTESGLTPIHVAAFMGHVN---IVS 427
Cdd:PHA02989    51 KIVKLLIDNGADVNYKGYIE-TPLcavlrnrEITSNKIK-KIVKLLLKFGADINLKTFNGVSPIVCFIYNSNINncdMLR 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  428 QLMHHGASPNTT-NVRGETALHMAARAG--QTEVVRYLVQNGAQV-EAKAKDDQTPLHISAR----LGKADIVQQLLQQG 499
Cdd:PHA02989   129 FLLSKGINVNDVkNSRGYNLLHMYLESFsvKKDVIKILLSFGVNLfEKTSLYGLTPMNIYLRndidVISIKVIKYLIKKG 208

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  500 ASPNAATtsgytplhlsarEGHEDVASVLLDHGASLSiitKKGFTPLHVAAKYGKIEVANlllqknaspdasgksgltpl 579
Cdd:PHA02989   209 VNIETNN------------NGSESVLESFLDNNKILS---KKEFKVLNFILKYIKINKKD-------------------- 253

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  580 hvaahydnqkvalllldqgasphasaKNGYTPLHIAAKKNQMDIATTLLEYGADANAVTRQGIAPVHLASQDGHVDMVSL 659
Cdd:PHA02989   254 --------------------------KKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNR 307

                          330
                   ....*....|
gi 2023156728  660 LLTRNANVNL 669
Cdd:PHA02989   308 ILQLKPGKYL 317
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 51-161 1.56e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 57.72  E-value: 1.56e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728   51 GLNALHLASKEGHVEVVSELIQRGASVDA--AT----KKGNTAL-----HIASLA---GQAEVVKVLVTNRANVNAQSQN 116
Cdd:cd22192     89 GETALHIAVVNQNLNLVRELIARGADVVSprATgtffRPGPKNLiyygeHPLSFAacvGNEEIVRLLIEHGADIRAQDSL 168

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2023156728  117 GFTPLYM-AAQENHL---EVVKFLLD---NGASQSLAT---EDGFTPLAVALQQG 161
Cdd:cd22192    169 GNTVLHIlVLQPNKTfacQMYDLILSydkEDDLQPLDLvpnNQGLTPFKLAAKEG 223
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 417-571 1.63e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 57.96  E-value: 1.63e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  417 AAFMGHVNIVSQLMHHGASPNTTNVRGETALHMAARAGQTEVVRYLVQNGAQVEAKAKDDQTPLHiSARLGKADIVQQLL 496
Cdd:PLN03192   532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALW-NAISAKHHKIFRIL 610

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2023156728  497 QQGASPNAATTSGyTPLHLSAREGHEDVASVLLDHGASLSIITKKGFTPLHVAAKYGKIEVANLLLQKNASPDAS 571
Cdd:PLN03192   611 YHFASISDPHAAG-DLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKA 684
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 92-170 1.70e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.60  E-value: 1.70e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2023156728   92 SLAGQAEVVKVLVTNRANVNAQSQNGFTPLYMAAQENHLEVVKFLLDNGASQSLATEDGFTPLAVALQQGHDQVVSLLL 170
Cdd:PTZ00322    90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PHA02798 PHA02798
ankyrin-like protein; Provisional
 423-668 1.73e-07

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 57.54  E-value: 1.73e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  423 VNIVSQLMHHGASPNTTNVRGETAL-----HMAARAGQTEVVRYLVQNGAQVEAKAKDDQTPLHI---SARLGKADIVQQ 494
Cdd:PHA02798    51 TDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCllsNGYINNLEILLF 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  495 LLQQGASPNAATTSGYTPLHLSAREGHE---DVASVLLDHGASLSIITKK-GFTPLHVAAKYG---------KIEVANLL 561
Cdd:PHA02798   131 MIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDINTHNNKeKYDTLHCYFKYNidridadilKLFVDNGF 210

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  562 LQKNAspDASGKSGLTPLHVAAHYDNQKVALLLLD-QGASPHASAKN--GYTPLHIAAKKNQMDIATTLLEYGADANAVT 638
Cdd:PHA02798   211 IINKE--NKSHKKKFMEYLNSLLYDNKRFKKNILDfIFSYIDINQVDelGFNPLYYSVSHNNRKIFEYLLQLGGDINIIT 288

                          250       260       270
                   ....*....|....*....|....*....|
gi 2023156728  639 RQGIAPVHLASQDGHVDMVSLLLTRNANVN 668
Cdd:PHA02798   289 ELGNTCLFTAFENESKFIFNSILNKKPNKN 318
Ank_4 pfam13637
Ankyrin repeats (many copies);
119-170 1.80e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.35  E-value: 1.80e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2023156728  119 TPLYMAAQENHLEVVKFLLDNGASQSLATEDGFTPLAVALQQGHDQVVSLLL 170
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 679-773 1.94e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.60  E-value: 1.94e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  679 HLAAQDDRVNvAEVLVNQGAAVDAQTKMGYTPLHVGCHYGNIKIVNFLLQHSAKVNAKTKNGYTPLHQAAQQGHTHIINV 758
Cdd:PTZ00322    88 QLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166

                           90
                   ....*....|....*
gi 2023156728  759 LLQHGAAPNELTVNG 773
Cdd:PTZ00322   167 LSRHSQCHFELGANA 181
Ank_5 pfam13857
Ankyrin repeats (many copies);
594-648 2.05e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.42  E-value: 2.05e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2023156728  594 LLDQG-ASPHASAKNGYTPLHIAAKKNQMDIATTLLEYGADANAVTRQGIAPVHLA 648
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
726-780 2.15e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.42  E-value: 2.15e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2023156728  726 LLQH-SAKVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAAPNELTVNGNTALAIA 780
Cdd:pfam13857    1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
431-482 2.21e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.42  E-value: 2.21e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2023156728  431 HHGASPNTTNVRGETALHMAARAGQTEVVRYLVQNGAQVEAKAKDDQTPLHI 482
Cdd:pfam13857    4 HGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
Ank_5 pfam13857
Ankyrin repeats (many copies);
659-713 2.37e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.42  E-value: 2.37e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2023156728  659 LLLTRNANVNLGNKSGLTPLHLAAQDDRVNVAEVLVNQGAAVDAQTKMGYTPLHV 713
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
Ank_4 pfam13637
Ankyrin repeats (many copies);
674-727 3.75e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.58  E-value: 3.75e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2023156728  674 GLTPLHLAAQDDRVNVAEVLVNQGAAVDAQTKMGYTPLHVGCHYGNIKIVNFLL 727
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 429-496 4.51e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.45  E-value: 4.51e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2023156728  429 LMHHGASPNTTNVRGETALHMAARAGQTEVVRYLVQNGAQVEAKAKDDQTPLHISARLGKADIVQQLL 496
Cdd:PTZ00322   101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 253-333 4.62e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.45  E-value: 4.62e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  253 SKRGNANMVKLLLDRGAKIDAKTRDGLTPLHCGARSGHEQVVEMLLDRGAPILSKTKNGLSPLHMATQGDHLNCVQLLIQ 332
Cdd:PTZ00322    90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169


                   .
gi 2023156728  333 H 333
Cdd:PTZ00322   170 H 170
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 168-272 4.83e-07

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 52.57  E-value: 4.83e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  168 LLLENDTKGKvrlPALHIAARKD--DTKAAALLLQnDHNADV---ESKSGFTPLHIAAHYGNINVATLLLNRgAAVDFTA 242
Cdd:PHA02736    47 LVLEYNRHGK---QCVHIVSNPDkaDPQEKLKLLM-EWGADIngkERVFGNTPLHIAVYTQNYELATWLCNQ-PGVNMEI 121

                           90       100       110
                   ....*....|....*....|....*....|..
gi 2023156728  243 RNDI--TPLHVASKRGNANMVKLLLDRGAKID 272
Cdd:PHA02736   122 LNYAfkTPYYVACERHDAKMMNILRAKGAQCK 153
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 83-234 5.37e-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: 56.04  E-value: 5.37e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728   83 KGNTALHIASLAGQAEVVKVLVTNRANVNAQS---------QNGF----TPLYMAAQENHLEVVKFLLDNGASqslated 149
Cdd:cd21882     72 QGQTALHIAIENRNLNLVRLLVENGADVSARAtgrffrkspGNLFyfgeLPLSLAACTNQEEIVRLLLENGAQ------- 144

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  150 gftPLAVALQqghdqvvslllenDTKGKVRLPALHIAARK--DDTKAAA----LLLQNDHNAD-------VESKSGFTPL 216
Cdd:cd21882    145 ---PAALEAQ-------------DSLGNTVLHALVLQADNtpENSAFVCqmynLLLSYGAHLDptqqleeIPNHQGLTPL 208

                          170
                   ....*....|....*...
gi 2023156728  217 HIAAHYGNINVATLLLNR 234
Cdd:cd21882    209 KLAAVEGKIVMFQHILQR 226
Ank_5 pfam13857
Ankyrin repeats (many copies);
560-615 5.45e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 49.27  E-value: 5.45e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2023156728  560 LLLQKNASPDASGKSGLTPLHVAAHYDNQKVALLLLDQGASPHASAKNGYTPLHIA 615
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 565-689 8.10e-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: 55.58  E-value: 8.10e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  565 NASPDASGKSGLTPLHVAAHYDNQKVALLLLDQGASPHASA----------KNGY----TPLHIAAKKNQMDIATTLLE- 629
Cdd:cd22196     84 NAAYTDSYYKGQTALHIAIERRNMHLVELLVQNGADVHARAsgeffkkkkgGPGFyfgeLPLSLAACTNQLDIVKFLLEn 163

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2023156728  630 --YGADANAVTRQGIAPVH--LASQDGHVD-------MVSLLLTRNANVN-------LGNKSGLTPLHLAAQDDRVNV 689
Cdd:cd22196    164 phSPADISARDSMGNTVLHalVEVADNTPEntkfvtkMYNEILILGAKIRpllkleeITNKKGLTPLKLAAKTGKIGI 241
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 21-300 9.00e-07

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 55.30  E-value: 9.00e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728   21 SYLRAARAGNLEKALDYLKSGVDINISNQNGLNALH--LASKEGHVEVVSELIQRGASVDAATKKGNTALHiaSLAGQAE 98
Cdd:PHA02716   287 SYITLARNIDISVVYSFLQPGVKLHYKDSAGRTCLHqyILRHNISTDIIKLLHEYGNDLNEPDNIGNTVLH--TYLSMLS 364

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728   99 VVKVLvtnranvNAQSQNGFtplymaaqenHLEVVKFLLDNGASQSLATEDGFTPLA----VALQQGHDQVVSLLLENDT 174
Cdd:PHA02716   365 VVNIL-------DPETDNDI----------RLDVIQCLISLGADITAVNCLGYTPLTsyicTAQNYMYYDIIDCLISDKV 427

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  175 KGKVRLPALH-IAARKDDTKA------AALLLQNDHNADVESKSGFTPLHIAAHYGNINVATlllnrGAAVDFTArndIT 247
Cdd:PHA02716   428 LNMVKHRILQdLLIRVDDTPCiihhiiAKYNIPTDLYTDEYEPYDSTKIHDVYHCAIIERYN-----NAVCETSG---MT 499

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2023156728  248 PLHVA-SKRGNANMV----KLLLDRGAKIDAKTRDGLTPLHCGAR----SGHE-QVVEMLLDR 300
Cdd:PHA02716   500 PLHVSiISHTNANIVmdsfVYLLSIQYNINIPTKNGVTPLMLTMRnnrlSGHQwYIVKNILDK 562
PHA02946 PHA02946
ankyin-like protein; Provisional
 67-339 9.04e-07

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 55.06  E-value: 9.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728   67 VSELIQRGASVDAATKKGNTALHIASLAGQAEVVKVLVTNRANVNAQSQNGFTPLYM--AAQENHLEVVKFLLDNGAS-Q 143
Cdd:PHA02946    55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYlsGTDDEVIERINLLVQYGAKiN 134

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  144 SLATEDGFTPLAVAL---QQGHDQVVSLLLENDTKGKVRLPALHIAARKDDTKAAAL--LLQNDHNADVESKSGFTPLHI 218
Cdd:PHA02946   135 NSVDEEGCGPLLACTdpsERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNPKASTIswMMKLGISPSKPDHDGNTPLHI 214

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  219 --AAHYGNINVATLLLnrgAAVDFTARNDI--TPLHVASKR-GNANMVKLLLDRGAKIDAKTrdgltpLHCGARSGHEQV 293
Cdd:PHA02946   215 vcSKTVKNVDIINLLL---PSTDVNKQNKFgdSPLTLLIKTlSPAHLINKLLSTSNVITDQT------VNICIFYDRDDV 285

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 2023156728  294 VEMLLDRGAPILSktknglSPLHMATQGDHLNCVQLLIQHNVPVDD 339
Cdd:PHA02946   286 LEIINDKGKQYDS------TDFKMAVEVGSIRCVKYLLDNDIICED 325
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 4-234 1.13e-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: 54.80  E-value: 1.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728    4 LLMLLDYILRKMSDTNASYLRAARAGN--LEKALdylksgvdINIsnQNGLNA-----LHLASKEGHVEvvsELIQrgAS 76
Cdd:cd22193      4 LLGFLQDLCRRRKDLTDSEFTESSTGKtcLMKAL--------LNL--NPGTNDtirilLDIAEKTDNLK---RFIN--AE 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728   77 VDAATKKGNTALHIASLAGQAEVVKVLVTNRANVNAQSQNGF--------------TPLYMAAQENHLEVVKFLLDNgaS 142
Cdd:cd22193     69 YTDEYYEGQTALHIAIERRQGDIVALLVENGADVHAHAKGRFfqpkyqgegfyfgeLPLSLAACTNQPDIVQYLLEN--E 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  143 QSLATedgftplavalqqghdqvvslLLENDTKGKVRLPALHIAArkDDTKAAALLLQNDHNA---------------DV 207
Cdd:cd22193    147 HQPAD---------------------IEAQDSRGNTVLHALVTVA--DNTKENTKFVTRMYDMilirgaklcptveleEI 203

                          250       260
                   ....*....|....*....|....*..
gi 2023156728  208 ESKSGFTPLHIAAHYGNINVATLLLNR 234
Cdd:cd22193    204 RNNDGLTPLQLAAKMGKIEILKYILQR 230
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 536-756 1.40e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.87  E-value: 1.40e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  536 SIITKKGFTPLHVAAKygKIEVANLLLQkNASPDASGKSGLTPLHVAAhydNQKVALL--LLDQGASPHASAKNGYTPLH 613
Cdd:PLN03192   490 NVVILKNFLQHHKELH--DLNVGDLLGD-NGGEHDDPNMASNLLTVAS---TGNAALLeeLLKAKLDPDIGDSKGRTPLH 563

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  614 IAAKKNQMDIATTLLEYGADANAVTRQGIAPVHLASQDGHVDMVSLL--LTRNANVNLGNKSgltpLHLAAQDDRVNVAE 691
Cdd:PLN03192   564 IAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILyhFASISDPHAAGDL----LCTAAKRNDLTAMK 639

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2023156728  692 VLVNQGAAVDAQTKMGYTPLHVGCHYGNIKIVNFLLQHSAKVN-AKTKNGYTP-----LHQAAQQGHTHII 756
Cdd:PLN03192   640 ELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDkANTDDDFSPtelreLLQKRELGHSITI 710
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 376-403 1.42e-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: 47.20  E-value: 1.42e-06
                            10        20
                    ....*....|....*....|....*...
gi 2023156728   376 NGFTPLHIACKKNRIKVMELLLKHGASI 403
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
Ank_5 pfam13857
Ankyrin repeats (many copies);
42-91 1.68e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.73  E-value: 1.68e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2023156728   42 VDINISNQNGLNALHLASKEGHVEVVSELIQRGASVDAATKKGNTALHIA 91
Cdd:pfam13857    7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
627-681 1.95e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.73  E-value: 1.95e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2023156728  627 LLEYG-ADANAVTRQGIAPVHLASQDGHVDMVSLLLTRNANVNLGNKSGLTPLHLA 681
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 691-903 2.00e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.49  E-value: 2.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  691 EVLVNQGAAVDAQTKMGYTPLHVGCHYGNIKIVNFLLQHSAKVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAAPNELT 770
Cdd:PLN03192   542 EELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHA 621

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  771 vnGNTALAIAKRLGYISVVDT-----LKVVTEE----TMTTITVTEKHKmnvpeTMNEVLDMSDDEVRKANAPEILSDA- 840
Cdd:PLN03192   622 --AGDLLCTAAKRNDLTAMKEllkqgLNVDSEDhqgaTALQVAMAEDHV-----DMVRLLIMNGADVDKANTDDDFSPTe 694

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2023156728  841 --EYLSDVEEGEDAMTGDTDkylgPQDLKELGDDSLPAEGYMGFSLGARSASPKVSSDRSYTLNR 903
Cdd:PLN03192   695 lrELLQKRELGHSITIVDSV----PADEPDLGRDGGSRPGRLQGTSSDNQCRPRVSIYKGHPLLR 755
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 207-546 2.00e-06

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 54.15  E-value: 2.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  207 VESKSGFTPLHiaAHYGNINVAT----LLLNRGAAVDFTARNDITPLHVASKRGN--ANMVKLLLDRGAKIDAKTRDGLT 280
Cdd:PHA02716   172 VCKKTGYGILH--AYLGNMYVDIdileWLCNNGVNVNLQNNHLITPLHTYLITGNvcASVIKKIIELGGDMDMKCVNGMS 249

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  281 PLH---CGARSGHEQVVEMLLDRGAPilSKTKNGLSPLH----MATQGDhLNCVQLLIQHNVPVDDVTNDYLTALH--VA 351
Cdd:PHA02716   250 PIMtyiINIDNINPEITNIYIESLDG--NKVKNIPMILHsyitLARNID-ISVVYSFLQPGVKLHYKDSAGRTCLHqyIL 326

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  352 AHCGHYKVAKVLLDKKANPNAKALNGFTPLH----IACKKN----------RIKVMELLLKHGASIQAVTESGLTP---- 413
Cdd:PHA02716   327 RHNISTDIIKLLHEYGNDLNEPDNIGNTVLHtylsMLSVVNildpetdndiRLDVIQCLISLGADITAVNCLGYTPltsy 406

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  414 IHVAAFMGHVNIVSQLMhhgaSPNTTN-VRGETALHMAARAGQTE------VVRYLVQNGAQVEAKAKDDQTPLHisarl 486
Cdd:PHA02716   407 ICTAQNYMYYDIIDCLI----SDKVLNmVKHRILQDLLIRVDDTPciihhiIAKYNIPTDLYTDEYEPYDSTKIH----- 477

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2023156728  487 gkaDIVQQLLQQGASPNAATTSGYTPLHLSAREgHEDVASV------LLDHGASLSIITKKGFTPL 546
Cdd:PHA02716   478 ---DVYHCAIIERYNNAVCETSGMTPLHVSIIS-HTNANIVmdsfvyLLSIQYNINIPTKNGVTPL 539
Ank_4 pfam13637
Ankyrin repeats (many copies);
740-792 2.46e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.27  E-value: 2.46e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2023156728  740 GYTPLHQAAQQGHTHIINVLLQHGAAPNELTVNGNTALAIAKRLGYISVVDTL 792
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank_5 pfam13857
Ankyrin repeats (many copies);
103-157 2.49e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.34  E-value: 2.49e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2023156728  103 LVTNR-ANVNAQSQNGFTPLYMAAQENHLEVVKFLLDNGASQSLATEDGFTPLAVA 157
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 184-265 2.68e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.75  E-value: 2.68e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  184 HIAArKDDTKAAALLLQNDHNADVESKSGFTPLHIAAHYGNINVATLLLNRGAAVDFTARNDITPLHVASKRGNANMVKL 263
Cdd:PTZ00322    88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                   ..
gi 2023156728  264 LL 265
Cdd:PTZ00322   167 LS 168
Ank_4 pfam13637
Ankyrin repeats (many copies);
24-71 2.72e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.27  E-value: 2.72e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2023156728   24 RAARAGNLEKALDYLKSGVDINISNQNGLNALHLASKEGHVEVVSELI 71
Cdd:pfam13637    7 AAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 509-748 3.14e-06

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 53.55  E-value: 3.14e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  509 GYTPLHLSAREG-HEDVASVLLDHGASLSIitkkGFTPLHVAAK--YGKIEVANLLLQKNASPDASGK-----------S 574
Cdd:TIGR00870   52 GRSALFVAAIENeNLELTELLLNLSCRGAV----GDTLLHAISLeyVDAVEAILLHLLAAFRKSGPLElandqytseftP 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  575 GLTPLHVAAHYDNQKVALLLLDQGASPHASAK--------------NGYTPLHIAAKKNQMDIATTLLEYGADANAVTRQ 640
Cdd:TIGR00870  128 GITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADSL 207

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  641 GIAPVHLASqdghvdMVSLLLTRNANVNLGNKSGLTPlHLAAQDDRVNVAEVLVNQgaavdaqtkmGYTPLHVGCHYGNI 720
Cdd:TIGR00870  208 GNTLLHLLV------MENEFKAEYEELSCQMYNFALS-LLDKLRDSKELEVILNHQ----------GLTPLKLAAKEGRI 270

                          250       260       270
                   ....*....|....*....|....*....|.
gi 2023156728  721 KIVNFLLQ---HSAKVNAKTkngYTPLHQAA 748
Cdd:TIGR00870  271 VLFRLKLAikyKQKKFVAWP---NGQQLLSL 298
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 179-298 3.23e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.36  E-value: 3.23e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  179 RLPALHIAARKDDTKAAALLLQNDHNADVESKSGFTPLHIAAHyGNINVATLLLNRGAAVDFTARNDITPLHVASKRGNA 258
Cdd:PTZ00322    50 HLEALEATENKDATPDHNLTTEEVIDPVVAHMLTVELCQLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHV 128

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2023156728  259 NMVKLLLDRGAKIDAKTRDGLTPLHCGARSGHEQVVEMLL 298
Cdd:PTZ00322   129 QVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PHA02946 PHA02946
ankyin-like protein; Provisional
 352-551 3.29e-06

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 53.13  E-value: 3.29e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  352 AHCG----HYKVAKVLLDKKANPNAKALNGFTPLHIACKKNRIKVMELLLKHGASIQAVTESGLTPIHVAAFMGH--VNI 425
Cdd:PHA02946    43 AYCGikglDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIER 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  426 VSQLMHHGASPNTTNVRGETALHMAARAGQTEVVRYLVQNG--AQVEAKAKDDQTPLHISARLGKADIVQQLLQQGASPN 503
Cdd:PHA02946   123 INLLVQYGAKINNSVDEEGCGPLLACTDPSERVFKKIMSIGfeARIVDKFGKNHIHRHLMSDNPKASTISWMMKLGISPS 202

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 2023156728  504 AATTSGYTPLHLSAREGHEDVASV-LLDHGASLSIITKKGFTPLHVAAK 551
Cdd:PHA02946   203 KPDHDGNTPLHIVCSKTVKNVDIInLLLPSTDVNKQNKFGDSPLTLLIK 251
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 395-477 3.43e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.36  E-value: 3.43e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  395 LLLKHGASIQAVTESGLTPIHVAAFMGHVNIVSQLMHHGASPNTTNVRGETALHMAARAGQTEVVRYLV---QNGAQVEA 471
Cdd:PTZ00322   100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSrhsQCHFELGA 179


                   ....*.
gi 2023156728  472 KAKDDQ 477
Cdd:PTZ00322   180 NAKPDS 185
Death_p75NR cd08311
Death domain of p75 Neurotrophin Receptor; Death Domain (DD) found in p75 neurotrophin ...
 4054-4121 4.31e-06

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: 47.28  E-value: 4.31e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2023156728 4054 SWTELARELNFSVDEINQI-RVENPnsliaqSFMLLKKWVTRDGknATTDALTSVLTKINRIDIVTLLE 4121
Cdd:cd08311     20 DWRALAGELGYSAEEIDSFaREADP------CRALLTDWSAQDG--ATLGVLLTALRKIGRDDIVEILQ 80
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 546-650 4.35e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 51.91  E-value: 4.35e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  546 LHVAAKYGKIEVANLLLQKNASPDA----SGKSGLTPLHVAAHYDNQKVALLLLDQGASPHASAKNG-YTPLHIAAKKNQ 620
Cdd:PHA02884    37 LYSSIKFHYTDIIDAILKLGADPEApfplSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAkITPLYISVLHGC 116

                           90       100       110
                   ....*....|....*....|....*....|
gi 2023156728  621 MDIATTLLEYGADANAVTRQGIAPVHLASQ 650
Cdd:PHA02884   117 LKCLEILLSYGADINIQTNDMVTPIELALM 146
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 572-761 4.79e-06

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 52.96  E-value: 4.79e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  572 GKSGLTPLHVAAHYDNQKV--ALLLLDQGASPHASAKN------------GYTPLHIAAKKNQMDIATTLLEYGADanav 637
Cdd:cd21882     23 GATGKTCLHKAALNLNDGVneAIMLLLEAAPDSGNPKElvnapctdefyqGQTALHIAIENRNLNLVRLLVENGAD---- 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  638 trqgiapVHLAsqdghvdmvsllltrnANVNLGNKSGLT-------PLHLAAQDDRVNVAEVLVNQG---AAVDAQTKMG 707
Cdd:cd21882     99 -------VSAR----------------ATGRFFRKSPGNlfyfgelPLSLAACTNQEEIVRLLLENGaqpAALEAQDSLG 155

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  708 YTPLHVGCHYGN---------IKIVNFLLQHSAKVNAKTK-------NGYTPLHQAAQQGHTHIINVLLQ 761
Cdd:cd21882    156 NTVLHALVLQADntpensafvCQMYNLLLSYGAHLDPTQQleeipnhQGLTPLKLAAVEGKIVMFQHILQ 225
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 7-234 5.00e-06

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: 52.93  E-value: 5.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728    7 LLDYILRKMSDTNASYLRAARAGN--LEKALDYLKSGVDINIsnqngLNALHLASKEGHVEVVseliqrgasVDAATK-- 82
Cdd:cd22197     25 LLEYLRRTSKYLTDSEYTEGSTGKtcLMKAVLNLQDGVNACI-----MPLLEIDKDSGNPKPL---------VNAQCTde 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728   83 --KGNTALHIASLAGQAEVVKVLVTNRANVNAQSQNGF-------------TPLYMAAQENHLEVVKFLLDNGASqslat 147
Cdd:cd22197     91 yyRGHSALHIAIEKRSLQCVKLLVENGADVHARACGRFfqkkqgtcfyfgeLPLSLAACTKQWDVVNYLLENPHQ----- 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  148 edgftPLAVALQQGHDQVV---SLLLENDTKGKVrlpALHIAARKDDTKAAALLLQNDHNADVESKSGFTPLHIAAHYGN 224
Cdd:cd22197    166 -----PASLQAQDSLGNTVlhaLVMIADNSPENS---ALVIKMYDGLLQAGARLCPTVQLEEISNHEGLTPLKLAAKEGK 237

                          250
                   ....*....|
gi 2023156728  225 INVATLLLNR 234
Cdd:cd22197    238 IEIFRHILQR 247
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 7-234 5.12e-06

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


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 52.89  E-value: 5.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728    7 LLDYILRKMSDTNASYLRAARAGN--LEKALDYLKSGVDINISNqnglnALHLASKEGHVEvvsELIQrgASVDAATKKG 84
Cdd:cd22196     25 LLEYLMRTKKRLTDSEFKDPETGKtcLLKAMLNLHNGQNDTISL-----LLDIAEKTGNLK---EFVN--AAYTDSYYKG 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728   85 NTALHIASLAGQAEVVKVLVTNRANVNA----------QSQNGF----TPLYMAAQENHLEVVKFLLDNGASQS-LATED 149
Cdd:cd22196     95 QTALHIAIERRNMHLVELLVQNGADVHArasgeffkkkKGGPGFyfgeLPLSLAACTNQLDIVKFLLENPHSPAdISARD 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  150 GF------TPLAVA--LQQGHDQVVSLLLENDTKGKVRLPALHIAArkddtkaaalllqndhnadVESKSGFTPLHIAAH 221
Cdd:cd22196    175 SMgntvlhALVEVAdnTPENTKFVTKMYNEILILGAKIRPLLKLEE-------------------ITNKKGLTPLKLAAK 235

                          250
                   ....*....|...
gi 2023156728  222 YGNINVATLLLNR 234
Cdd:cd22196    236 TGKIGIFAYILGR 248
Ank_5 pfam13857
Ankyrin repeats (many copies);
70-124 5.15e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.57  E-value: 5.15e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2023156728   70 LIQRG-ASVDAATKKGNTALHIASLAGQAEVVKVLVTNRANVNAQSQNGFTPLYMA 124
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
478-529 5.40e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.50  E-value: 5.40e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2023156728  478 TPLHISARLGKADIVQQLLQQGASPNAATTSGYTPLHLSAREGHEDVASVLL 529
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 439-612 6.57e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 52.56  E-value: 6.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  439 TNVRGETALHMAARAGQTEVVRYLVQNGAQVEAKAKDDQTPLHISARLGKADIVQQLLQQGASPNAATTSGYTPLHLSAR 518
Cdd:PLN03192   521 DDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAIS 600

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  519 EGHEDVASVLLdHGASLSIITKKGfTPLHVAAKYGKIEVANLLLQKNASPDASGKSGLTPLHVAAHYDNQKVALLLLDQG 598
Cdd:PLN03192   601 AKHHKIFRILY-HFASISDPHAAG-DLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNG 678

                          170
                   ....*....|....*
gi 2023156728  599 AS-PHASAKNGYTPL 612
Cdd:PLN03192   679 ADvDKANTDDDFSPT 693
Ank_5 pfam13857
Ankyrin repeats (many copies);
198-252 6.78e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.19  E-value: 6.78e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2023156728  198 LLQNDH-NADVESKSGFTPLHIAAHYGNINVATLLLNRGAAVDFTARNDITPLHVA 252
Cdd:pfam13857    1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 46-121 6.80e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 52.56  E-value: 6.80e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2023156728   46 ISN-QNGLNALHLASKEGHVEVVSELIQRGASVDAATKKGNTALHIASLAGQAEVVKVLVTNRANVN-AQSQNGFTPL 121
Cdd:PLN03192   616 ISDpHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDkANTDDDFSPT 693
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 25-80 7.65e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 52.56  E-value: 7.65e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2023156728   25 AARAGNLEKALDYLKSGVDINISNQNGLNALHLASKEGHVEVVSELIQRGASVDAA 80
Cdd:PLN03192   629 AAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKA 684
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 558-637 8.29e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.21  E-value: 8.29e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  558 ANLLLQKNASPDASGKSGLTPLHVAAHYDNQKVALLLLDQGASPHASAKNGYTPLHIAAKKNQMDIATTLLEYG-----A 632
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSqchfeL 177


                   ....*
gi 2023156728  633 DANAV 637
Cdd:PTZ00322   178 GANAK 182
Death_DRs cd08784
Death Domain of Death Receptors; Death domain (DD) found in death receptor proteins. Death ...
 4053-4112 9.10e-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: 46.42  E-value: 9.10e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728 4053 LSWTELARELNFSVDEINQIRVENPNSLIAQSFMLLKKWVTRDGKNATTDALTSVLTKIN 4112
Cdd:cd08784     12 SQWKGFVRKLGLNEAEIDEIKNDNVQDTAEAKYQMLRNWHQLTGRKAAYDTLIKDLKKMN 71
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 244-273 9.29e-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: 44.89  E-value: 9.29e-06
                            10        20        30
                    ....*....|....*....|....*....|
gi 2023156728   244 NDITPLHVASKRGNANMVKLLLDRGAKIDA 273
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 607-639 1.06e-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: 44.97  E-value: 1.06e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2023156728  607 NGYTPLHIAAKK-NQMDIATTLLEYGADANAVTR 639
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
330-384 1.10e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.42  E-value: 1.10e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2023156728  330 LIQH-NVPVDDVTNDYLTALHVAAHCGHYKVAKVLLDKKANPNAKALNGFTPLHIA 384
Cdd:pfam13857    1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 610-743 1.34e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 49.43  E-value: 1.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  610 TPLH--IAAKKNQMDIATTLLEYGADANAVTR-QGIAPVHL---ASQDGHVDMVSLLLTRNANVNLGNKSGLTPLH--LA 681
Cdd:PHA02859    53 TPIFscLEKDKVNVEILKFLIENGADVNFKTRdNNLSALHHylsFNKNVEPEILKILIDSGSSITEEDEDGKNLLHmyMC 132

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2023156728  682 AQDDRVNVAEVLVnqgaavdaqtKMGYTPLHVGCHYGNI-----------KIVNFLLQHSAKVNAKTKNGYTP 743
Cdd:PHA02859   133 NFNVRINVIKLLI----------DSGVSFLNKDFDNNNIlysyilfhsdkKIFDFLTSLGIDINETNKSGYNC 195
Ank_5 pfam13857
Ankyrin repeats (many copies);
693-747 1.47e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.03  E-value: 1.47e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2023156728  693 LVNQGAAVDAQTKMGYTPLHVGCHYGNIKIVNFLLQHSAKVNAKTKNGYTPLHQA 747
Cdd:pfam13857    2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 116-142 1.50e-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: 44.50  E-value: 1.50e-05
                            10        20
                    ....*....|....*....|....*..
gi 2023156728   116 NGFTPLYMAAQENHLEVVKFLLDNGAS 142
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 514-608 1.78e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.05  E-value: 1.78e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  514 HLSArEGHEDVASVLLDHGASLSIITKKGFTPLHVAAKYGKIEVANLLLQKNASPDASGKSGLTPLHVAAHYDNQKVALL 593
Cdd:PTZ00322    88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166

                           90
                   ....*....|....*
gi 2023156728  594 LLDQGASPHASAKNG 608
Cdd:PTZ00322   167 LSRHSQCHFELGANA 181
Ank_5 pfam13857
Ankyrin repeats (many copies);
396-450 1.96e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.64  E-value: 1.96e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2023156728  396 LLKHG-ASIQAVTESGLTPIHVAAFMGHVNIVSQLMHHGASPNTTNVRGETALHMA 450
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 376-408 2.00e-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: 44.20  E-value: 2.00e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2023156728  376 NGFTPLHIACKK-NRIKVMELLLKHGASIQAVTE 408
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 51-234 2.22e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 50.85  E-value: 2.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728   51 GLNALHLASKEgHVEVVSELIQRGASVDAATK--------------KGNTALHIASLAGQAEVVKVLVTNRANVNA---- 112
Cdd:TIGR00870   82 GDTLLHAISLE-YVDAVEAILLHLLAAFRKSGplelandqytseftPGITALHLAAHRQNYEIVKLLLERGASVPAracg 160

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  113 ------QSQNGF----TPLYMAAQENHLEVVKFLLDNGASQSLATEDGFTPLavalqqgHDQVVslllENDTKGK----- 177
Cdd:TIGR00870  161 dffvksQGVDSFyhgeSPLNAAACLGSPSIVALLSEDPADILTADSLGNTLL-------HLLVM----ENEFKAEyeels 229

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2023156728  178 --VRLPALHIAARKDDTKAAALLLQNDhnadvesksGFTPLHIAAHYGNINVATLLLNR 234
Cdd:TIGR00870  230 cqMYNFALSLLDKLRDSKELEVILNHQ---------GLTPLKLAAKEGRIVLFRLKLAI 279
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 38-103 2.24e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.67  E-value: 2.24e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2023156728   38 LKSGVDINISNQNGLNALHLASKEGHVEVVSELIQRGASVDAATKKGNTALHIASLAGQAEVVKVL 103
Cdd:PTZ00322   102 LTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 376-405 2.27e-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: 43.79  E-value: 2.27e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 2023156728  376 NGFTPLHIACKKNRIKVMELLLKHGASIQA 405
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 707-738 2.37e-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: 43.82  E-value: 2.37e-05
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2023156728  707 GYTPLHVGC-HYGNIKIVNFLLQHSAKVNAKTK 738
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 50-82 2.56e-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: 43.82  E-value: 2.56e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2023156728   50 NGLNALHLAS-KEGHVEVVSELIQRGASVDAATK 82
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 565-683 2.58e-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: 50.53  E-value: 2.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  565 NASPDASGKSGLTPLHVAAHYDNQKVALLLLDQGASPHASAKN--------------GYTPLHIAAKKNQMDIATTLLEY 630
Cdd:cd22194    131 NAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEIVQLLMEK 210

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2023156728  631 GadANAVTRQ---GIAPVH---LASQDGH------VDMVSLLLTRNANVNL---GNKSGLTPLHLAAQ 683
Cdd:cd22194    211 E--STDITSQdsrGNTVLHalvTVAEDSKtqndfvKRMYDMILLKSENKNLetiRNNEGLTPLQLAAK 276
Ank_4 pfam13637
Ankyrin repeats (many copies);
644-694 2.86e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.19  E-value: 2.86e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2023156728  644 PVHLASQDGHVDMVSLLLTRNANVNLGNKSGLTPLHLAAQDDRVNVAEVLV 694
Cdd:pfam13637    4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 541-570 2.98e-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: 2.98e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 2023156728   541 KGFTPLHVAAKYGKIEVANLLLQKNASPDA 570
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 631-730 3.22e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.28  E-value: 3.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  631 GADANAVTRQGIAPV----------HLASQDGHVDmVSLLLTRNANVNLGNKSGLTPLHLAAQDDRVNVAEVLVNQGAAV 700
Cdd:PTZ00322    63 TPDHNLTTEEVIDPVvahmltvelcQLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADP 141

                           90       100       110
                   ....*....|....*....|....*....|
gi 2023156728  701 DAQTKMGYTPLHVGCHYGNIKIVNFLLQHS 730
Cdd:PTZ00322   142 TLLDKDGKTPLELAEENGFREVVQLLSRHS 171
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 442-474 3.30e-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: 3.30e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2023156728  442 RGETALHMAA-RAGQTEVVRYLVQNGAQVEAKAK 474
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 316-399 3.57e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.28  E-value: 3.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  316 HMATQGDHLNcVQLLIQHNVPVDDVTNDYLTALHVAAHCGHYKVAKVLLDKKANPNAKALNGFTPLHIACKKNRIKVMEL 395
Cdd:PTZ00322    88 QLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                   ....
gi 2023156728  396 LLKH 399
Cdd:PTZ00322   167 LSRH 170
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 244-276 3.68e-05

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. 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: 3.68e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2023156728  244 NDITPLHVASKR-GNANMVKLLLDRGAKIDAKTR 276
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 247-421 4.72e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 47.89  E-value: 4.72e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  247 TPLH--VASKRGNANMVKLLLDRGAKIDAKTRD-GLTPLH---CGARSGHEQVVEMLLDRGAPILSKTKNGLSPLHMatq 320
Cdd:PHA02859    53 TPIFscLEKDKVNVEILKFLIENGADVNFKTRDnNLSALHhylSFNKNVEPEILKILIDSGSSITEEDEDGKNLLHM--- 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  321 gdhlncvqlliqhnvpvddvtndYLTALHVaahcgHYKVAKVLLDKKANPNAKALNGFTPLH-IACKKNRIKVMELLLKH 399
Cdd:PHA02859   130 -----------------------YMCNFNV-----RINVIKLLIDSGVSFLNKDFDNNNILYsYILFHSDKKIFDFLTSL 181

                          170       180
                   ....*....|....*....|..
gi 2023156728  400 GASIQAVTESGLTPIHVAAFMG 421
Cdd:PHA02859   182 GIDINETNKSGYNCYDLIKFRN 203
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 277-309 4.99e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 43.05  E-value: 4.99e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2023156728  277 DGLTPLHCGA-RSGHEQVVEMLLDRGAPILSKTK 309
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 739-767 5.19e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 43.05  E-value: 5.19e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 2023156728  739 NGYTPLHQAAQQ-GHTHIINVLLQHGAAPN 767
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVN 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 739-768 5.32e-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: 5.32e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 2023156728   739 NGYTPLHQAAQQGHTHIINVLLQHGAAPNE 768
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 214-316 6.12e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 47.51  E-value: 6.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  214 TPLH--IAAHYGNINVATLLLNRGAAVDFTAR-NDITPLH---VASKRGNANMVKLLLDRGAKIDAKTRDGLTPLH---- 283
Cdd:PHA02859    53 TPIFscLEKDKVNVEILKFLIENGADVNFKTRdNNLSALHhylSFNKNVEPEILKILIDSGSSITEEDEDGKNLLHmymc 132

                           90       100       110
                   ....*....|....*....|....*....|....
gi 2023156728  284 -CGARSgheQVVEMLLDRGAPILSKTKNGLSPLH 316
Cdd:PHA02859   133 nFNVRI---NVIKLLIDSGVSFLNKDFDNNNILY 163
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 607-636 6.23e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.57  E-value: 6.23e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 2023156728   607 NGYTPLHIAAKKNQMDIATTLLEYGADANA 636
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 723-792 6.57e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.13  E-value: 6.57e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  723 VNFLLQHSAKVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAAPNELTVNGNTALAIAKRLGYISVVDTL 792
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 377-497 7.02e-05

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 49.02  E-value: 7.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  377 GFTPLHIACKKNRIKVMELLLKHGASIQAVTES--------------GLTPIHVAAFMGHVNIVSQLM---HHGASPNTT 439
Cdd:cd22193     76 GQTALHIAIERRQGDIVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLSLAACTNQPDIVQYLLeneHQPADIEAQ 155

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2023156728  440 NVRGETALHMAARAGQ---------TEVVRYLVQNGAQV-------EAKAKDDQTPLHISARLGKADIVQQLLQ 497
Cdd:cd22193    156 DSRGNTVLHALVTVADntkentkfvTRMYDMILIRGAKLcptveleEIRNNDGLTPLQLAAKMGKIEILKYILQ 229
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 509-540 8.07e-05

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. 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: 8.07e-05
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2023156728  509 GYTPLHLSA-REGHEDVASVLLDHGASLSIITK 540
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 599-823 8.23e-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: 48.99  E-value: 8.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  599 ASPHASAKNGYTPLHIAAKKNQMDIATTLLEYGADANAVTRQ--------------GIAPVHLASQDGHVDMVSLLLTR- 663
Cdd:cd22194    132 AEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEIVQLLMEKe 211

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  664 NANVNLGNKSGLTPLHLAaqddrVNVAEVLVNQGAAVdaqtkmgytplhvgchygnIKIVNFLLQHSAKVNAKT---KNG 740
Cdd:cd22194    212 STDITSQDSRGNTVLHAL-----VTVAEDSKTQNDFV-------------------KRMYDMILLKSENKNLETirnNEG 267

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  741 YTPLHQAAQQGHTHIINVLLQHgaapnELTVNGNTALA----------IAKRLGYISVVDT------LKVVTEETmttiT 804
Cdd:cd22194    268 LTPLQLAAKMGKAEILKYILSR-----EIKEKPNRSLSrkftdwaygpVSSSLYDLTNVDTttdnsvLEIIVYNT----N 338

                          250
                   ....*....|....*....
gi 2023156728  805 VTEKHKMNVPETMNEVLDM 823
Cdd:cd22194    339 IDNRHEMLTLEPLHTLLHM 357
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 541-573 9.08e-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: 9.08e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2023156728  541 KGFTPLHVAA-KYGKIEVANLLLQKNASPDASGK 573
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 346-373 1.01e-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: 42.28  E-value: 1.01e-04
                           10        20
                   ....*....|....*....|....*....
gi 2023156728  346 TALHVAA-HCGHYKVAKVLLDKKANPNAK 373
Cdd:pfam00023    4 TPLHLAAgRRGNLEIVKLLLSKGADVNAR 32
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 509-537 1.09e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.80  E-value: 1.09e-04
                            10        20
                    ....*....|....*....|....*....
gi 2023156728   509 GYTPLHLSAREGHEDVASVLLDHGASLSI 537
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 706-735 1.13e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.80  E-value: 1.13e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 2023156728   706 MGYTPLHVGCHYGNIKIVNFLLQHSAKVNA 735
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 116-142 1.21e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 41.89  E-value: 1.21e-04
                           10        20
                   ....*....|....*....|....*...
gi 2023156728  116 NGFTPLYMAA-QENHLEVVKFLLDNGAS 142
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGAD 28
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 50-79 1.23e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.80  E-value: 1.23e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 2023156728    50 NGLNALHLASKEGHVEVVSELIQRGASVDA 79
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 604-821 1.29e-04

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 48.25  E-value: 1.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  604 SAKNGYTPLHIAAKKNQMDIATTLLEYGADANAVTRQ--------------GIAPVHLASQDGHVDMVSLLLtRNANvnl 669
Cdd:cd22193     72 EYYEGQTALHIAIERRQGDIVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLSLAACTNQPDIVQYLL-ENEH--- 147

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  670 gnksglTPLHLAAQDDRVN-VAEVLVNQGAAVDAQTKMgytplhvgchygNIKIVNFLLQHSAKVNAKTK-------NGY 741
Cdd:cd22193    148 ------QPADIEAQDSRGNtVLHALVTVADNTKENTKF------------VTRMYDMILIRGAKLCPTVEleeirnnDGL 209

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  742 TPLHQAAQQGHTHIINVLLQhgaapneLTVNGNTALAIAKR------------LGYISVVDTL--KVVTEETMTTITVTE 807
Cdd:cd22193    210 TPLQLAAKMGKIEILKYILQ-------REIKEPELRHLSRKftdwaygpvsssLYDLSNVDTCekNSVLEIIVYNSKIDN 282

                          250
                   ....*....|....
gi 2023156728  808 KHKMNVPETMNEVL 821
Cdd:cd22193    283 RHEMLTLEPLNTLL 296
Ank_5 pfam13857
Ankyrin repeats (many copies);
462-515 1.32e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 1.32e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2023156728  462 LVQNG-AQVEAKAKDDQTPLHISARLGKADIVQQLLQQGASPNAATTSGYTPLHL 515
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 83-113 1.39e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. 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: 1.39e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 2023156728   83 KGNTALHIASL-AGQAEVVKVLVTNRANVNAQ 113
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNAR 32
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 638-792 1.41e-04

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 48.37  E-value: 1.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  638 TRQGIAPVHLASQDGHVDMVSLLLTRNANVNLGNKSGLTPLHLAAQDDRV--NVAEVLVNQGAAVDAQTKMGYTP----- 710
Cdd:PHA02716   176 TGYGILHAYLGNMYVDIDILEWLCNNGVNVNLQNNHLITPLHTYLITGNVcaSVIKKIIELGGDMDMKCVNGMSPimtyi 255

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  711 ------------LHVGCHYGN--------------------IKIVNFLLQHSAKVNAKTKNGYTPLHQAAQQGH--THII 756
Cdd:PHA02716   256 inidninpeitnIYIESLDGNkvknipmilhsyitlarnidISVVYSFLQPGVKLHYKDSAGRTCLHQYILRHNisTDII 335

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 2023156728  757 NVLLQHGAAPNELTVNGNTALaiAKRLGYISVVDTL 792
Cdd:PHA02716   336 KLLHEYGNDLNEPDNIGNTVL--HTYLSMLSVVNIL 369
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 366-527 1.52e-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: 47.93  E-value: 1.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  366 KKANP----NAKALN----GFTPLHIACKKNRIKVMELLLKHGASIQAVTES-------------GLTPIHVAAFMGHVN 424
Cdd:cd22197     75 DSGNPkplvNAQCTDeyyrGHSALHIAIEKRSLQCVKLLVENGADVHARACGrffqkkqgtcfyfGELPLSLAACTKQWD 154

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  425 IVSQLM---HHGASPNTTNVRGETALH---MAA--RAGQTEVVRY----LVQNGAQVEAKAKDDQ-------TPLHISAR 485
Cdd:cd22197    155 VVNYLLenpHQPASLQAQDSLGNTVLHalvMIAdnSPENSALVIKmydgLLQAGARLCPTVQLEEisnheglTPLKLAAK 234

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2023156728  486 LGKADIVQQLLQQGAS------PNAATTSGYTPLHLSARegheDVASV 527
Cdd:cd22197    235 EGKIEIFRHILQREFSgpyqhlSRKFTEWCYGPVRVSLY----DLSSV 278
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 707-735 1.54e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 41.47  E-value: 1.54e-04
                           10        20
                   ....*....|....*....|....*....
gi 2023156728  707 GYTPLHVGCHYGNIKIVNFLLQHSAKVNA 735
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 343-372 1.69e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.42  E-value: 1.69e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 2023156728   343 DYLTALHVAAHCGHYKVAKVLLDKKANPNA 372
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 361-496 1.81e-04

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 47.83  E-value: 1.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  361 KVLLDkkANPNAKALNGFTPLHIACKKNRIKVMELLLKHGASIQAVTES--------------GLTPIHVAAFMGHVNIV 426
Cdd:cd22194    127 DRFIN--AEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEIV 204

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  427 SQLMHHGASPNTT-NVRGETALH---MAARAGQTE---VVR-----YLVQNGAQVEA-KAKDDQTPLHISARLGKADIVQ 493
Cdd:cd22194    205 QLLMEKESTDITSqDSRGNTVLHalvTVAEDSKTQndfVKRmydmiLLKSENKNLETiRNNEGLTPLQLAAKMGKAEILK 284


                   ...
gi 2023156728  494 QLL 496
Cdd:cd22194    285 YIL 287
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 639-732 1.81e-04

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 44.87  E-value: 1.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  639 RQGIAPVHLASQDGHVD---MVSLLLTRNANVNLGN-KSGLTPLHLAAQDDRVNVAEVLVNQ-GAAVDAQTKMGYTPLHV 713
Cdd:PHA02736    53 RHGKQCVHIVSNPDKADpqeKLKLLMEWGADINGKErVFGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYV 132

                           90
                   ....*....|....*....
gi 2023156728  714 GCHYGNIKIVNFLLQHSAK 732
Cdd:PHA02736   133 ACERHDAKMMNILRAKGAQ 151
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 212-239 1.87e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.42  E-value: 1.87e-04
                            10        20
                    ....*....|....*....|....*...
gi 2023156728   212 GFTPLHIAAHYGNINVATLLLNRGAAVD 239
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 565-689 1.95e-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: 47.48  E-value: 1.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  565 NASPDASGKSGLTPLHVAAHYDNQKVALLLLDQGASPHASAKN--------------GYTPLHIAAKKNQMDIATTLLEY 630
Cdd:cd22193     66 NAEYTDEYYEGQTALHIAIERRQGDIVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLSLAACTNQPDIVQYLLEN 145

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2023156728  631 G---ADANAVTRQGIAPVH--LASQDGHVD-------MVSLLLTRNANV-------NLGNKSGLTPLHLAAQDDRVNV 689
Cdd:cd22193    146 EhqpADIEAQDSRGNTVLHalVTVADNTKEntkfvtrMYDMILIRGAKLcptveleEIRNNDGLTPLQLAAKMGKIEI 223
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 38-267 2.17e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 47.43  E-value: 2.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728   38 LKSGVDINISNQNGLNALH---LASKEGHVEVVSELIQRGASV-DAATKKGNTALHI--ASLAGQAEVVKVLVtnRANVN 111
Cdd:PHA02989    95 LKFGADINLKTFNGVSPIVcfiYNSNINNCDMLRFLLSKGINVnDVKNSRGYNLLHMylESFSVKKDVIKILL--SFGVN 172

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  112 AQSQN---GFTPL--YMAAQEN--HLEVVKFLLDNGASqsLATEDgftplavalqQGHDQVVSLLLENdtkgkvrlpalH 184
Cdd:PHA02989   173 LFEKTslyGLTPMniYLRNDIDviSIKVIKYLIKKGVN--IETNN----------NGSESVLESFLDN-----------N 229

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  185 IAARKDDTKAAALLLQ--NDHNADvesKSGFTPLHIAAHYGNINVATLLLNRGAAVDFTARNDITPLHVASKRGNANMVK 262
Cdd:PHA02989   230 KILSKKEFKVLNFILKyiKINKKD---KKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLN 306


                   ....*
gi 2023156728  263 LLLDR 267
Cdd:PHA02989   307 RILQL 311
Ank_5 pfam13857
Ankyrin repeats (many copies);
297-351 2.26e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 2.26e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2023156728  297 LLDRG-APILSKTKNGLSPLHMATQGDHLNCVQLLIQHNVPVDDVTNDYLTALHVA 351
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 70-137 2.31e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.59  E-value: 2.31e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2023156728   70 LIQRGASVDAATKKGNTALHIASLAGQAEVVKVLVTNRANVNAQSQNGFTPLYMAAQENHLEVVKFLL 137
Cdd:PTZ00322   101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
Ank_5 pfam13857
Ankyrin repeats (many copies);
495-549 2.40e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 2.40e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2023156728  495 LLQQG-ASPNAATTSGYTPLHLSAREGHEDVASVLLDHGASLSIITKKGFTPLHVA 549
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00121 PTZ00121
MAEBL; Provisional
 2561-2996 2.49e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.83  E-value: 2.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728 2561 RVDRTVKEAEEKlTEVSQFFRDKTEKLNDELQSPEKKQH---KKNGKEIHSSQSSASSSPEKVLLSELPSSGDEWSK--- 2634
Cdd:PTZ00121  1330 KADAAKKKAEEA-KKAAEAAKAEAEAAADEAEAAEEKAEaaeKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKkad 1408

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728 2635 -VKQYAHDGKcfpKVDE--RKASSLPSSPEKRifvQPAEDSKQTMEHKGSAQQtgvpevsqtgfqlkQSKLSSIRLKFEQ 2711
Cdd:PTZ00121  1409 eLKKAAAAKK---KADEakKKAEEKKKADEAK---KKAEEAKKADEAKKKAEE--------------AKKAEEAKKKAEE 1468

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728 2712 SISPRSKDVTQEEKKLDGQSKipvKKSQESKLPVYQFYSREKHAKQVEvidgstalqkEVKIQEDfvpgKAKAIEDFRAS 2791
Cdd:PTZ00121  1469 AKKADEAKKKAEEAKKADEAK---KKAEEAKKKADEAKKAAEAKKKAD----------EAKKAEE----AKKADEAKKAE 1531

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728 2792 DAQKRPEMSKGvvpeyfSEPQAKDLVYGSDSTAKGHWDKKIYRTWESPGTSNHQTQKEKLSHVLVPDTVKENHVDHAETK 2871
Cdd:PTZ00121  1532 EAKKADEAKKA------EEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEK 1605

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728 2872 TDKKSEFATVTEHKLAANGIH-SEEVK---ELTVKSPSKRVLYREFVVREGERNGEVADKISKRKEEIAVSHIPVRIVEE 2947
Cdd:PTZ00121  1606 KMKAEEAKKAEEAKIKAEELKkAEEEKkkvEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEE 1685

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*....
gi 2023156728 2948 KrtmldgvyelsakvsqsaviKEKVERQIDYMEDEKIKCSEIRKVTKQQ 2996
Cdd:PTZ00121  1686 D--------------------EKKAAEALKKEAEEAKKAEELKKKEAEE 1714
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 739-768 2.69e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 40.70  E-value: 2.69e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 2023156728  739 NGYTPLHQAAQQGHTHIINVLLQHGAAPNE 768
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 442-471 2.88e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 40.65  E-value: 2.88e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 2023156728   442 RGETALHMAARAGQTEVVRYLVQNGAQVEA 471
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 410-440 3.16e-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: 3.16e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 2023156728  410 GLTPIHVAAFM-GHVNIVSQLMHHGASPNTTN 440
Cdd:pfam00023    2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
PHA02743 PHA02743
Viral ankyrin protein; Provisional
 168-272 3.28e-04

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 44.42  E-value: 3.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  168 LLLENDTKGKVrlpALHIAARKDDTKAA---ALLLQN--DHNADvESKSGFTPLHIAAHYGNINVATLLLnRGAAVDFTA 242
Cdd:PHA02743    49 LLHRYDHHGRQ---CTHMVAWYDRANAVmkiELLVNMgaDINAR-ELGTGNTLLHIAASTKNYELAEWLC-RQLGVNLGA 123

                           90       100       110
                   ....*....|....*....|....*....|..
gi 2023156728  243 RNDI--TPLHVASKRGNANMVKLLLDRGAKID 272
Cdd:PHA02743   124 INYQheTAYHIAYKMRDRRMMEILRANGAVCD 155
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 212-245 3.59e-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: 3.59e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 2023156728  212 GFTPLHIAA-HYGNINVATLLLNRGAAVDftARND 245
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVN--ARDK 34
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 607-636 3.61e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 40.32  E-value: 3.61e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 2023156728  607 NGYTPLHIAAKKNQMDIATTLLEYGADANA 636
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 442-471 3.72e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 40.32  E-value: 3.72e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 2023156728  442 RGETALHMAARAGQTEVVRYLVQNGAQVEA 471
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02791 PHA02791
ankyrin-like protein; Provisional
 375-545 3.88e-04

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 45.80  E-value: 3.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  375 LNGFTPLHIACKKNRIKVMELLLKHGAsIQAVTESGLtPIHVAAFMGHVNIVSQLMHHGASPNTTNVRGETALHMAARAG 454
Cdd:PHA02791    28 VHGHSALYYAIADNNVRLVCTLLNAGA-LKNLLENEF-PLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSG 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  455 QTEVVRYLVQNGAQVEAKAKDD-QTPLHISARLGKADIVQQLLQQGASPNAATTSgYTPLHLSAREGHEDVASVLLDHGA 533
Cdd:PHA02791   106 NMQTVKLFVKKNWRLMFYGKTGwKTSFYHAVMLNDVSIVSYFLSEIPSTFDLAIL-LSCIHITIKNGHVDMMILLLDYMT 184

                          170
                   ....*....|..
gi 2023156728  534 SLSIITKKGFTP 545
Cdd:PHA02791   185 STNTNNSLLFIP 196
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 475-506 4.04e-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: 40.35  E-value: 4.04e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2023156728  475 DDQTPLHISA-RLGKADIVQQLLQQGASPNAAT 506
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
Ank_5 pfam13857
Ankyrin repeats (many copies);
264-318 4.36e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.18  E-value: 4.36e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2023156728  264 LLDRG-AKIDAKTRDGLTPLHCGARSGHEQVVEMLLDRGAPILSKTKNGLSPLHMA 318
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 83-112 4.48e-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: 4.48e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 2023156728    83 KGNTALHIASLAGQAEVVKVLVTNRANVNA 112
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 14-175 4.60e-04

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: 46.34  E-value: 4.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728   14 KMSDTNASYLRAARAGnlekalDYLKSGVDINISNQ--NGLNALHLASKEGHVEVVSELIQRGASVDAAT-----KK--- 83
Cdd:cd22196     61 GQNDTISLLLDIAEKT------GNLKEFVNAAYTDSyyKGQTALHIAIERRNMHLVELLVQNGADVHARAsgeffKKkkg 134

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728   84 ------GNTALHIASLAGQAEVVKVLVTN---RANVNAQSQNGFTPLY--MAAQENHLEVVKF-------LLDNGAS--- 142
Cdd:cd22196    135 gpgfyfGELPLSLAACTNQLDIVKFLLENphsPADISARDSMGNTVLHalVEVADNTPENTKFvtkmyneILILGAKirp 214

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 2023156728  143 ----QSLATEDGFTPLAVALQQGHDQVVSLLLENDTK 175
Cdd:cd22196    215 llklEEITNKKGLTPLKLAAKTGKIGIFAYILGREIK 251
PTZ00121 PTZ00121
MAEBL; Provisional
 2543-3009 4.71e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.67  E-value: 4.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728 2543 RFTEDRldRGREKLMYED-RVDRTVKEAEEKLTEVSQFFRDKTEKLNDELQSPEKKQHKKNGKEIHSSQSSASSSPEKVL 2621
Cdd:PTZ00121  1207 KAEEER--KAEEARKAEDaKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELK 1284

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728 2622 LSELPSSGDEWSK---------VKQYAHDGKcfpKVDERKASSLPSSPEKRIFVQPAEDSKQTMEHKGSAQQTGVPEVSQ 2692
Cdd:PTZ00121  1285 KAEEKKKADEAKKaeekkkadeAKKKAEEAK---KADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA 1361

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728 2693 TGfqlKQSKLSSIRLKFEQSISPRSKDVTQEEKKLDGQSKI---PVKKSQESKLPVYQFYSREKHAKQVEVIDGSTALQK 2769
Cdd:PTZ00121  1362 AE---EKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKaeeDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKK 1438

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728 2770 EVKIQEDFVPGKAKAIEDFRASDAQKRPEMSKgvvpeyfsepQAKDLVYGSDSTAKGHWDKKIYRTWESPGTSNHQTQKE 2849
Cdd:PTZ00121  1439 KAEEAKKADEAKKKAEEAKKAEEAKKKAEEAK----------KADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA 1508

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728 2850 KlshvlvpdtVKENHVDHAETKTdKKSEFATVTEHKLAANGIHSEEVKELTVKSPSKRVLYREFVVREGERNGEVADK-I 2928
Cdd:PTZ00121  1509 K---------KKADEAKKAEEAK-KADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKnM 1578

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728 2929 SKRKEEIAvshipvRIVEEKRT-MLDGVYELSAKVSQSAVIKEkverqidymEDEKIKCSEIRKVTKQQSSIGLTPPIEE 3007
Cdd:PTZ00121  1579 ALRKAEEA------KKAEEARIeEVMKLYEEEKKMKAEEAKKA---------EEAKIKAEELKKAEEEKKKVEQLKKKEA 1643


                   ..
gi 2023156728 3008 ME 3009
Cdd:PTZ00121  1644 EE 1645
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 57-142 5.55e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 44.42  E-value: 5.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728   57 LASKEGHVEVVSELIQRGASVDAATKKGNTALHIASLA----GQAEVVKVLVTNRANVNAQSQNGFTPL--YMAAQENHL 130
Cdd:PHA02859    59 LEKDKVNVEILKFLIENGADVNFKTRDNNLSALHHYLSfnknVEPEILKILIDSGSSITEEDEDGKNLLhmYMCNFNVRI 138

                           90
                   ....*....|..
gi 2023156728  131 EVVKFLLDNGAS 142
Cdd:PHA02859   139 NVIKLLIDSGVS 150
PHA02798 PHA02798
ankyrin-like protein; Provisional
 654-812 5.78e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 45.98  E-value: 5.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  654 VDMVSLLL-TRNANVnLGNKSGLTPLHLAAQDDRVNVAEVLVNQGAAVDAQTKMGYTPLhvgCH-YGNIK-------IVN 724
Cdd:PHA02798    18 LSTVKLLIkSCNPNE-IVNEYSIFQKYLQRDSPSTDIVKLFINLGANVNGLDNEYSTPL---CTiLSNIKdykhmldIVK 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  725 FLLQHSAKVNAKTKNGYTPLHQAAQQGHTH---IINVLLQHGAAPNELTVNGNTALAIAKRLGYISVVDTLKVVTEETMT 801
Cdd:PHA02798    94 ILIENGADINKKNSDGETPLYCLLSNGYINnleILLFMIENGADTTLLDKDGFTMLQVYLQSNHHIDIEIIKLLLEKGVD 173

                          170
                   ....*....|.
gi 2023156728  802 TITVTEKHKMN 812
Cdd:PHA02798   174 INTHNNKEKYD 184
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 277-304 8.31e-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: 39.49  E-value: 8.31e-04
                            10        20
                    ....*....|....*....|....*...
gi 2023156728   277 DGLTPLHCGARSGHEQVVEMLLDRGAPI 304
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 208-398 8.43e-04

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 45.64  E-value: 8.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  208 ESKSGFTPLHIAA---HYGNINVATLLLNrgAAVDFTARNDI-------------TPLHVASKRGNANMVKLLLDRGAKI 271
Cdd:cd21882     22 RGATGKTCLHKAAlnlNDGVNEAIMLLLE--AAPDSGNPKELvnapctdefyqgqTALHIAIENRNLNLVRLLVENGADV 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  272 DAKTRD-------------GLTPLHCGARSGHEQVVEMLLDRGAPILSKTKN---GLSPLHMatqgdhlncvqLLIQHNV 335
Cdd:cd21882    100 SARATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPAALEAQdslGNTVLHA-----------LVLQADN 168

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2023156728  336 PVDD---VTNDYLTALHVAAHCGHykvakvLLDKKANPNAKalnGFTPLHIACKKNRIKVMELLLK 398
Cdd:cd21882    169 TPENsafVCQMYNLLLSYGAHLDP------TQQLEEIPNHQ---GLTPLKLAAVEGKIVMFQHILQ 225
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 359-516 8.64e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 44.04  E-value: 8.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  359 VAKVLLDKKANPNAKAL-NGFTPLH--IACKKN-RIKVMELLLKHGASIQAVTESGLTPIHVaaFMGHVNIvsqlmhhga 434
Cdd:PHA02859    68 ILKFLIENGADVNFKTRdNNLSALHhyLSFNKNvEPEILKILIDSGSSITEEDEDGKNLLHM--YMCNFNV--------- 136

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  435 spnttnvrgetalhmaaragQTEVVRYLVQNGAQVEAKAKDDQTPLHiSARLGKAD--IVQQLLQQGASPNAATTSGYTP 512
Cdd:PHA02859   137 --------------------RINVIKLLIDSGVSFLNKDFDNNNILY-SYILFHSDkkIFDFLTSLGIDINETNKSGYNC 195


                   ....
gi 2023156728  513 LHLS 516
Cdd:PHA02859   196 YDLI 199
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 346-401 1.00e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 42.94  E-value: 1.00e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2023156728  346 TALHVAAHCGHYKVAKVLLdKKANPNAKALNGF--TPLHIACKKNRIKVMELLLKHGA 401
Cdd:PHA02736    94 TPLHIAVYTQNYELATWLC-NQPGVNMEILNYAfkTPYYVACERHDAKMMNILRAKGA 150
PHA02917 PHA02917
ankyrin-like protein; Provisional
 342-780 1.02e-03

ankyrin-like protein; Provisional


Pssm-ID: 165231 [Multi-domain]  Cd Length: 661  Bit Score: 45.37  E-value: 1.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  342 NDYLTALHVAAHCGHYKVAKVLLDKKANPNAKALNGFTPLHIACKKNRIKVMELLLKhgASIQAVTESGLTPIHVAAFMG 421
Cdd:PHA02917    33 NNALHAYLFNEHCNNVEVVKLLLDSGTNPLHKNWRQLTPLEEYTNSRHVKVNKDIAM--ALLEATGYSNINDFNIFSYMK 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  422 H----VNIVSQLMHHG--ASPNTTNVRGETALHMAARAGQTEVVRYLVQNGAQVEAKAKDDQ--------------TPLH 481
Cdd:PHA02917   111 SknvdVDLIKVLVEHGfdLSVKCENHRSVIENYVMTDDPVPEIIDLFIENGCSVLYEDEDDEygyayddyqprncgTVLH 190

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  482 ---ISARLGKAD--------IVQQLLQQGASPNAATTSGYTPLHLSAREGHEDVASVLL-----DHGASLSI----ITKK 541
Cdd:PHA02917   191 lyiISHLYSESDtrayvrpeVVKCLINHGIKPSSIDKNYCTALQYYIKSSHIDIDIVKLlmkgiDNTAYSYIddltCCTR 270

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  542 GFTP--LHVAAKYGK---IEVANLLLQkNASPDASGKSgLTPLHvaaHYDNQKVALLLldqgasphaSAKNGYTPLHIAA 616
Cdd:PHA02917   271 GIMAdyLNSDYRYNKdvdLDLVKLFLE-NGKPHGIMCS-IVPLW---RNDKETISLIL---------KTMNSDVLQHILI 336

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  617 KKNQM-DIATTLLEYGADANAVTRQgiAPVHLASQDGHVDMVSLLLTrnanvnLGNKSGLTPLHLaaQDDRVNVAEVLVN 695
Cdd:PHA02917   337 EYMTFgDIDIPLVECMLEYGAVVNK--EAIHGYFRNINIDSYTMKYL------LKKEGGDAVNHL--DDGEIPIGHLCKS 406

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  696 QGAAVDAQT---KMGYTPLHVGCHYgnIKIVNFLLQHSAKVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAAPNELTVN 772
Cdd:PHA02917   407 NYGCYNFYTytyKKGLCDMSYACPI--LSTINICLPYLKDINMIDKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNN 484


                   ....*...
gi 2023156728  773 GNTALAIA 780
Cdd:PHA02917   485 GYTCIAIA 492
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 608-761 1.04e-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: 45.23  E-value: 1.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  608 GYTPLHIAAKKNQMDIATTLLEYGADanavtrqgiapVHlASQDGHvdmvslLLTRNANVNLgnKSGLTPLHLAAQDDRV 687
Cdd:cd22197     94 GHSALHIAIEKRSLQCVKLLVENGAD-----------VH-ARACGR------FFQKKQGTCF--YFGELPLSLAACTKQW 153

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  688 NVAEVLVN---QGAAVDAQTKMGYTPLHVGCHYGN---------IKIVNFLLQHSAKVNAKTK-------NGYTPLHQAA 748
Cdd:cd22197    154 DVVNYLLEnphQPASLQAQDSLGNTVLHALVMIADnspensalvIKMYDGLLQAGARLCPTVQleeisnhEGLTPLKLAA 233

                          170
                   ....*....|...
gi 2023156728  749 QQGHTHIINVLLQ 761
Cdd:cd22197    234 KEGKIEIFRHILQ 246
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 410-437 1.05e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.11  E-value: 1.05e-03
                            10        20
                    ....*....|....*....|....*...
gi 2023156728   410 GLTPIHVAAFMGHVNIVSQLMHHGASPN 437
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 575-603 1.42e-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: 38.81  E-value: 1.42e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 2023156728  575 GLTPLHVAA-HYDNQKVALLLLDQGASPHA 603
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNA 31
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 48-141 1.42e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 42.17  E-value: 1.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728   48 NQNGLNALHLASKEGHVEVVSE---LIQRGASVDAATKK-GNTALHIASLAGQAEVVKVLVtNRANVNAQSQNGF--TPL 121
Cdd:PHA02736    52 NRHGKQCVHIVSNPDKADPQEKlklLMEWGADINGKERVfGNTPLHIAVYTQNYELATWLC-NQPGVNMEILNYAfkTPY 130

                           90       100
                   ....*....|....*....|
gi 2023156728  122 YMAAQENHLEVVKFLLDNGA 141
Cdd:PHA02736   131 YVACERHDAKMMNILRAKGA 150
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 310-342 1.51e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.81  E-value: 1.51e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2023156728  310 NGLSPLHMA-TQGDHLNCVQLLIQHNVPVDDVTN 342
Cdd:pfam00023    1 DGNTPLHLAaGRRGNLEIVKLLLSKGADVNARDK 34
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 343-372 1.55e-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: 38.78  E-value: 1.55e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 2023156728  343 DYLTALHVAAHCGHYKVAKVLLDKKANPNA 372
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 674-705 1.60e-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: 38.81  E-value: 1.60e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2023156728  674 GLTPLHLAA-QDDRVNVAEVLVNQGAAVDAQTK 705
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
TRPV4 cd22195
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed ...
 442-557 1.77e-03

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: 44.46  E-value: 1.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  442 RGETALHMAARAGQTEVVRYLVQNGAQVEAKA-------KDD-------QTPLHISARLGKADIVQQLLQQG---ASPNA 504
Cdd:cd22195    136 RGQTALHIAIERRCKHYVELLVEKGADVHAQArgrffqpKDEggyfyfgELPLSLAACTNQPDIVHYLTENAhkkADLRR 215

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2023156728  505 ATTSGYTPLHL------SAREGHEDVASV---LLDHGASL-------SIITKKGFTPLHVAAKYGKIEV 557
Cdd:cd22195    216 QDSRGNTVLHAlvaiadNTRENTKFVTKMydlLLIKCAKLypdcnleAILNNDGMSPLMMAAKLGKIGI 284
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 277-304 1.92e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.39  E-value: 1.92e-03
                           10        20
                   ....*....|....*....|....*...
gi 2023156728  277 DGLTPLHCGARSGHEQVVEMLLDRGAPI 304
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 617-747 1.92e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 43.82  E-value: 1.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  617 KKNQMDIATTL-----LEYGADANAVTRQGIAPvhlasqdghvdmvsllltrNANVNLGNKSGLTPLHLAAQDDRVNVAE 691
Cdd:PHA02884    27 KKNKICIANILyssikFHYTDIIDAILKLGADP-------------------EAPFPLSENSKTNPLIYAIDCDNDDAAK 87

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2023156728  692 VLVNQGAAVDAQTK-MGYTPLHVGCHYGNIKIVNFLLQHSAKVNAKTKNGYTPLHQA 747
Cdd:PHA02884    88 LLIRYGADVNRYAEeAKITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELA 144
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 541-570 2.29e-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: 38.39  E-value: 2.29e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 2023156728  541 KGFTPLHVAAKYGKIEVANLLLQKNASPDA 570
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Death_NMPP84 cd08318
Death domain of Nuclear Matrix Protein P84; Death domain (DD) found in the Nuclear Matrix ...
 4040-4116 2.52e-03

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: 39.81  E-value: 2.52e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2023156728 4040 TDIRMAIVADHLGLSWTELARELNFSVDEINQIRvENPNSLIAQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDI 4116
Cdd:cd08318      6 TSEQIDVLANKLGEQWKTLAPYLEMKDKDIRQIE-SDSEDMKMRAKQLLVTWQDREGAQATPEILMTALNAAGLNEI 81
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 608-761 2.85e-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: 44.03  E-value: 2.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  608 GYTPLHIAAKKNQMDIATTLLEYGADANAVtrqgiapvhlASQDghvdmvsllLTRNANVNLGNKSGLTPLHLAAQDDRV 687
Cdd:cd22196     94 GQTALHIAIERRNMHLVELLVQNGADVHAR----------ASGE---------FFKKKKGGPGFYFGELPLSLAACTNQL 154

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  688 NVAEVLVN---QGAAVDAQTKMGYTPLH---------------VGCHYGNIKIVNFLLQHSAKVNAKT-KNGYTPLHQAA 748
Cdd:cd22196    155 DIVKFLLEnphSPADISARDSMGNTVLHalvevadntpentkfVTKMYNEILILGAKIRPLLKLEEITnKKGLTPLKLAA 234

                          170
                   ....*....|...
gi 2023156728  749 QQGHTHIINVLLQ 761
Cdd:cd22196    235 KTGKIGIFAYILG 247
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 116-142 2.96e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.01  E-value: 2.96e-03
                           10        20
                   ....*....|....*....|....*..
gi 2023156728  116 NGFTPLYMAAQENHLEVVKFLLDNGAS 142
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGAD 27
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 212-239 2.98e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.01  E-value: 2.98e-03
                           10        20
                   ....*....|....*....|....*...
gi 2023156728  212 GFTPLHIAAHYGNINVATLLLNRGAAVD 239
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADIN 29
PHA02791 PHA02791
ankyrin-like protein; Provisional
 205-403 3.00e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 43.11  E-value: 3.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  205 ADVEsksGFTPLHIAAHYGNINVATLLLNRGAAVDFTaRNDItPLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPLHC 284
Cdd:PHA02791    26 ADVH---GHSALYYAIADNNVRLVCTLLNAGALKNLL-ENEF-PLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYY 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  285 GARSGHEQVVEMLLDRGAPILSKTKNGL-SPLHMATQGDHLNCVQLLIQHnVPVDDVTNDYLTALHVAAHCGHYKVAKVL 363
Cdd:PHA02791   101 AVDSGNMQTVKLFVKKNWRLMFYGKTGWkTSFYHAVMLNDVSIVSYFLSE-IPSTFDLAILLSCIHITIKNGHVDMMILL 179

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 2023156728  364 LDKKANPNAKALNGFTP-LHIACKKNRIKVMELLLKHGASI 403
Cdd:PHA02791   180 LDYMTSTNTNNSLLFIPdIKLAIDNKDLEMLQALFKYDINI 220
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 98-158 3.15e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 42.11  E-value: 3.15e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2023156728   98 EVVKVLVTNRANVNAQSQ-NGFTPL--YMAAQEN-HLEVVKFLLDNGASQSLATEDGFTPLAVAL 158
Cdd:PHA02859    67 EILKFLIENGADVNFKTRdNNLSALhhYLSFNKNvEPEILKILIDSGSSITEEDEDGKNLLHMYM 131
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 718-780 3.45e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 43.70  E-value: 3.45e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2023156728  718 GNIKIVNFLLQHSAKVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAAPNELTVNGNTAL--AIA 780
Cdd:PLN03192   536 GNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnAIS 600
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 475-504 3.81e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.57  E-value: 3.81e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 2023156728   475 DDQTPLHISARLGKADIVQQLLQQGASPNA 504
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 509-537 3.85e-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: 3.85e-03
                           10        20
                   ....*....|....*....|....*....
gi 2023156728  509 GYTPLHLSAREGHEDVASVLLDHGASLSI 537
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 477-619 4.50e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 41.73  E-value: 4.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  477 QTPLHISARLGKA--DIVQQLLQQGASPNAATT-SGYTPLH--LSAREG-HEDVASVLLDHGASLSIITKKGFTPLHVAA 550
Cdd:PHA02859    52 ETPIFSCLEKDKVnvEILKFLIENGADVNFKTRdNNLSALHhyLSFNKNvEPEILKILIDSGSSITEEDEDGKNLLHMYM 131

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2023156728  551 K--YGKIEVANLLLQKNASPDASGKSGLTPLHVAAHY-DNQKVALLLLDQGASPHASAKNGYTPLHIAAKKN 619
Cdd:PHA02859   132 CnfNVRINVIKLLIDSGVSFLNKDFDNNNILYSYILFhSDKKIFDFLTSLGIDINETNKSGYNCYDLIKFRN 203
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 244-273 4.78e-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: 4.78e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 2023156728  244 NDITPLHVASKRGNANMVKLLLDRGAKIDA 273
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 310-339 5.70e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.18  E-value: 5.70e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 2023156728   310 NGLSPLHMATQGDHLNCVQLLIQHNVPVDD 339
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 130-300 6.00e-03

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: 42.94  E-value: 6.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  130 LEVVKFLLDNGASQSLATedGFTPLAVA---LQQGHDQVVSLLLENDTKGKVRLP---------------ALHIAARKDD 191
Cdd:cd21882      8 LECLRWYLTDSAYQRGAT--GKTCLHKAalnLNDGVNEAIMLLLEAAPDSGNPKElvnapctdefyqgqtALHIAIENRN 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  192 TKAAALLLQNdhNADVESKS---------------GFTPLHIAAHYGNINVATLLLNRGAAV-DFTARNDI--TPLHVAS 253
Cdd:cd21882     86 LNLVRLLVEN--GADVSARAtgrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPaALEAQDSLgnTVLHALV 163

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2023156728  254 KRGN---------ANMVKLLLDRGAKID-------AKTRDGLTPLHCGARSGHEQVVEMLLDR 300
Cdd:cd21882    164 LQADntpensafvCQMYNLLLSYGAHLDptqqleeIPNHQGLTPLKLAAVEGKIVMFQHILQR 226
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 214-310 6.13e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 42.28  E-value: 6.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  214 TPLHIAAHYGNINVATLLLNRGAAVD-FTARNDITPLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPLHCGARSGHEQ 292
Cdd:PHA02884    72 NPLIYAIDCDNDDAAKLLIRYGADVNrYAEEAKITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELALMICNNF 151

                           90
                   ....*....|....*...
gi 2023156728  293 VVEMLLDRGAPILSKTKN 310
Cdd:PHA02884   152 LAFMICDNEISNFYKHPK 169
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 475-504 6.18e-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: 6.18e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 2023156728  475 DDQTPLHISARLGKADIVQQLLQQGASPNA 504
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Death_MyD88 cd08312
Death domain of Myeloid Differentation primary response protein MyD88; Death Domain (DD) of ...
 4037-4120 7.76e-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: 38.35  E-value: 7.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728 4037 CERTDIRMAIVADhlglsWTELARELNFSVDEINQI-RVENPnsliaqSFMLLKKWVTRDgKNATTDALTSVLTKINRID 4115
Cdd:cd08312      6 SLYLNPEKVVAND-----WRGLAELMGFDYLEIRNFeRQSSP------TERLLEDWETRP-PGATVGNLLEILEELERKD 73


                   ....*
gi 2023156728 4116 IVTLL 4120
Cdd:cd08312     74 VLEDL 78
PHA02946 PHA02946
ankyin-like protein; Provisional
 216-465 7.87e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 42.35  E-value: 7.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  216 LHIAAHYGNINVaTLLLNRGAAVDFTARNDITPLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPLHCGARSGHEQVVE 295
Cdd:PHA02946    11 LSLYAKYNSKNL-DVFRNMLQAIEPSGNYHILHAYCGIKGLDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVA 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  296 MLLDRGAPILSKTKNGLSPLHM--ATQGDHLNCVQLLIQHNVPVDDVTNDYLTALHVAAHCGHYKVAKVLL--------- 364
Cdd:PHA02946    90 MLLTHGADPNACDKQHKTPLYYlsGTDDEVIERINLLVQYGAKINNSVDEEGCGPLLACTDPSERVFKKIMsigfeariv 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  365 DK-----------KANPNAKAL---------------NGFTPLHIACKKN--RIKVMELLL---------KHGASIQAVT 407
Cdd:PHA02946   170 DKfgknhihrhlmSDNPKASTIswmmklgispskpdhDGNTPLHIVCSKTvkNVDIINLLLpstdvnkqnKFGDSPLTLL 249

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  408 ESGLTPIH-VAAFMGHVNIVSQ-------LMHHGASPNTTNVRGE----TALHMAARAGQTEVVRYLVQN 465
Cdd:PHA02946   250 IKTLSPAHlINKLLSTSNVITDqtvniciFYDRDDVLEIINDKGKqydsTDFKMAVEVGSIRCVKYLLDN 319
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 469-610 8.47e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 41.51  E-value: 8.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156728  469 VEAKAKDDQTP-LHISARLGKADIVQQLLQQGASPNA----ATTSGYTPLHLSAREGHEDVASVLLDHGASLSIITKKG- 542
Cdd:PHA02884    25 IKKKNKICIANiLYSSIKFHYTDIIDAILKLGADPEApfplSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAk 104

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2023156728  543 FTPLHVAAKYGKIEVANLLLQKNASPDASGKSGLTPLHVAAHYDNQKVALLLLDQGASPHASAKNGYT 610
Cdd:PHA02884   105 ITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELALMICNNFLAFMICDNEISNFYKHPKKIL 172
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 575-603 9.41e-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: 9.41e-03
                            10        20
                    ....*....|....*....|....*....
gi 2023156728   575 GLTPLHVAAHYDNQKVALLLLDQGASPHA 603
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
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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