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Conserved domains on  [gi|2023156726|ref|XP_040461280|]
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ankyrin-3 isoform X3 [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];
352-635 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 2023156726  352 LLIQHNVPVDDVTNDYLTALHVAAHCGHYKVAKVLLDKKANPNAKALNGFTPLHIACKKNRIKVMELLLKHGASIQAVTE 431
Cdd:COG0666      6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  432 SGLTPIHVAAFMGHVNIVSQLMHHGASPNTTNVRGETALHMAARAGQTEVVRYLVQNGAQVEAKAKDDQTPLHISARLGK 511
Cdd:COG0666     86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  512 ADIVQQLLQQGASPNAATTSGYTPLHLSAREGHEDVASVLLDHGASLSIITKKGFTPLHVAAKYGKIEVANLLLQKNASP 591
Cdd:COG0666    166 LEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADL 245

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 2023156726  592 DASGKSGLTPLHVAAHYDNQKVALLLLDQGASPHASAKNGYTPL 635
Cdd:COG0666    246 NAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
551-816 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 2023156726  551 LLDHGASLSIITKKGFTPLHVAAKYGKIEVANLLLQKNASPDASGKSGLTPLHVAAHYDNQKVALLLLDQGASPHASAKN 630
Cdd:COG0666      7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  631 GYTPLHIAAKKNQMDIATTLLEYGADANAVTRQGIAPVHLASQDGHVDMVSLLLTRNANVNLGNKSGLTPLHLAAQDDRV 710
Cdd:COG0666     87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  711 NVAEVLVNQGAAVDAQTKMGYTPLHVGCHYGNIKIVNFLLQHSAKVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAAPN 790
Cdd:COG0666    167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246

                          250       260
                   ....*....|....*....|....*.
gi 2023156726  791 ELTVNGNTALAIAKRLGYISVVDTLK 816
Cdd:COG0666    247 AKDKDGLTALLLAAAAGAALIVKLLL 272
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
191-470 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 2023156726  191 LLLENDTKGKVRLPALHIAARKDDTKAAALLLQNDHNADVESKSGFTPLHIAAHYGNINVATLLLNRGAAVDFTARNDIT 270
Cdd:COG0666     10 LLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNT 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  271 PLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPLHCGARSGHEQVVEMLLDRGAPILSKTKNGLSPLHMATQGDHLNCV 350
Cdd:COG0666     90 LLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  351 QLLIQHNVPVDDVTNDYLTALHVAAHCGHYKVAKVLLDKKANPNAKALNGFTPLHIACKKNRIKVMELLLKHGASIQAVT 430
Cdd:COG0666    170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKD 249

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 2023156726  431 ESGLTPIHVAAFMGHVNIVSQLMHHGASPNTTNVRGETAL 470
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 ...
 1318-1447 2.36e-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: 195.77  E-value: 2.36e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726 1318 VPYMAKFVIFAKMNDPVESNLRCFCMTDDKVDKTLEQQENFEEVARSKDIEVLEGKPIYVDCYGNLAPLTKGGQQLVFNF 1397
Cdd:pfam17809    1 VPYLAKFVVFAKRYDPGEARLRCACMTDDGEDKTLEFHEGFTEVARSRDVEVLEGSPVSIELSGNLVPIKKKSQSRQMDF 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2023156726 1398 YAFKENRLPFSIKVRDTSQEPCGRLSFLKEPKTTKGLPQTAVCNLNITLP 1447
Cdd:pfam17809   81 KAFRENRLDGSVRVKDPSDPPKGLLSFMRDAKVDGGTVSQPLCTLNIVLP 130
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-305 3.07e-53

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 190.17  E-value: 3.07e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726    1 MAHAASQLKKNRDLEINADEETEKKRKHRKRSRDRKKKSDTNASYLRAARAGNLEKALDYLKSGVDINISNQNGLNALHL 80
Cdd:COG0666     14 ALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHA 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726   81 ASKEGHVEVVSELIQRGASVDAATKKGNTALHIASLAGQAEVVKVLVTNRANVNAQSQNGFTPLYMAAQENHLEVVKFLL 160
Cdd:COG0666     94 AARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLL 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  161 DNGASQSLATEDGFTPLAVALQQGHDQVVSLLLEndtkgkvrlpalhiaarkddtkaaalllqndHNADVE--SKSGFTP 238
Cdd:COG0666    174 EAGADVNARDNDGETPLHLAAENGHLEIVKLLLE-------------------------------AGADVNakDNDGKTA 222

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2023156726  239 LHIAAHYGNINVATLLLNRGAAVDFTARNDITPLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPL 305
Cdd:COG0666    223 LDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
 992-1096 8.17e-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: 8.17e-48
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726   992 SSFLVSFMVDARGGSMRGSRHhGMRIIIPPRKCTAPTRITCRLVKRHKLASPPPMVEGEGLASRLVEMGPSGAQFLGPVI 1071
Cdd:smart00218    1 PSFLVSGTFDARGGRLRGPRT-GVRLIIPPGAIPQGTRYTCYLVVHKTLSTPPPLEEGETLLSPVVECGPHGALFLRPVI 79

                            90       100
                    ....*....|....*....|....*
gi 2023156726  1072 VEIPHFGSMRGKERELIVLRSENGE 1096
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 ...
 4061-4144 3.93e-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: 3.93e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726 4061 ERTDIRMAIVADHLGLSWTELARELNFSVDEINQIRVENPNSLIAQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIV 4140
Cdd:cd08803      1 ERTDIRMAIVADHLGLSWTELARELNFSVDEINQIRVENPNSLIAQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIV 80


                   ....
gi 2023156726 4141 TLLE 4144
Cdd:cd08803     81 TLLE 84
PLN03192 super family cl33658
Voltage-dependent potassium channel; Provisional
 714-926 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 2023156726  714 EVLVNQGAAVDAQTKMGYTPLHVGCHYGNIKIVNFLLQHSAKVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAAPNELT 793
Cdd:PLN03192   542 EELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHA 621

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  794 vnGNTALAIAKRLGYISVVDT-----LKVVTEE----TMTTITVTEKHKmnvpeTMNEVLDMSDDEVRKANAPEILSDA- 863
Cdd:PLN03192   622 --AGDLLCTAAKRNDLTAMKEllkqgLNVDSEDhqgaTALQVAMAEDHV-----DMVRLLIMNGADVDKANTDDDFSPTe 694

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2023156726  864 --EYLSDVEEGEDAMTGDTDkylgPQDLKELGDDSLPAEGYMGFSLGARSASPKVSSDRSYTLNR 926
Cdd:PLN03192   695 lrELLQKRELGHSITIVDSV----PADEPDLGRDGGSRPGRLQGTSSDNQCRPRVSIYKGHPLLR 755
PTZ00121 super family cl31754
MAEBL; Provisional
 2584-3019 2.62e-04

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.44  E-value: 2.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726 2584 RVDRTVKEAEEKlTEVSQFFRDKTEKLNDELQSPEKKQH---KKNGKEIHSSQSSASSSPEKVLLSELPSSGDEWSK--- 2657
Cdd:PTZ00121  1330 KADAAKKKAEEA-KKAAEAAKAEAEAAADEAEAAEEKAEaaeKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKkad 1408

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726 2658 -VKQYAHDGKcfpKVDE--RKASSLPSSPEKRifvQPAEDSKQTMEHKGSAQQtgvpevsqtgfqlkQSKLSSIRLKFEQ 2734
Cdd:PTZ00121  1409 eLKKAAAAKK---KADEakKKAEEKKKADEAK---KKAEEAKKADEAKKKAEE--------------AKKAEEAKKKAEE 1468

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726 2735 SISPRSKDVTQEEKKLDGQSKipvKKSQESKLPVYQFYSREKHAKQVEvidgstalqkEVKIQEDfvpgKAKAIEDFRAS 2814
Cdd:PTZ00121  1469 AKKADEAKKKAEEAKKADEAK---KKAEEAKKKADEAKKAAEAKKKAD----------EAKKAEE----AKKADEAKKAE 1531

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726 2815 DAQKRPEMSKGvvpeyfSEPQAKDLVYGSDSTAKGHWDKKIYRTWESPGTSNHQTQKEKLSHVLVPDTVKENHVDHAETK 2894
Cdd:PTZ00121  1532 EAKKADEAKKA------EEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEK 1605

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726 2895 TDKKSEFATVTEHKLAANGIH-SEEVK---ELTVKSPSKRVLYREFVVREGERNGEVADKISKRKEEIAVSHIPVRIVEE 2970
Cdd:PTZ00121  1606 KMKAEEAKKAEEAKIKAEELKkAEEEKkkvEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEE 1685

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*....
gi 2023156726 2971 KrtmldgvyelsakvsqsaviKEKVERQIDYMEDEKIKCSEIRKVTKQQ 3019
Cdd:PTZ00121  1686 D--------------------EKKAAEALKKEAEEAKKAEELKKKEAEE 1714
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
352-635 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 2023156726  352 LLIQHNVPVDDVTNDYLTALHVAAHCGHYKVAKVLLDKKANPNAKALNGFTPLHIACKKNRIKVMELLLKHGASIQAVTE 431
Cdd:COG0666      6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  432 SGLTPIHVAAFMGHVNIVSQLMHHGASPNTTNVRGETALHMAARAGQTEVVRYLVQNGAQVEAKAKDDQTPLHISARLGK 511
Cdd:COG0666     86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  512 ADIVQQLLQQGASPNAATTSGYTPLHLSAREGHEDVASVLLDHGASLSIITKKGFTPLHVAAKYGKIEVANLLLQKNASP 591
Cdd:COG0666    166 LEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADL 245

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 2023156726  592 DASGKSGLTPLHVAAHYDNQKVALLLLDQGASPHASAKNGYTPL 635
Cdd:COG0666    246 NAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
551-816 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 2023156726  551 LLDHGASLSIITKKGFTPLHVAAKYGKIEVANLLLQKNASPDASGKSGLTPLHVAAHYDNQKVALLLLDQGASPHASAKN 630
Cdd:COG0666      7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  631 GYTPLHIAAKKNQMDIATTLLEYGADANAVTRQGIAPVHLASQDGHVDMVSLLLTRNANVNLGNKSGLTPLHLAAQDDRV 710
Cdd:COG0666     87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  711 NVAEVLVNQGAAVDAQTKMGYTPLHVGCHYGNIKIVNFLLQHSAKVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAAPN 790
Cdd:COG0666    167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246

                          250       260
                   ....*....|....*....|....*.
gi 2023156726  791 ELTVNGNTALAIAKRLGYISVVDTLK 816
Cdd:COG0666    247 AKDKDGLTALLLAAAAGAALIVKLLL 272
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
191-470 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 2023156726  191 LLLENDTKGKVRLPALHIAARKDDTKAAALLLQNDHNADVESKSGFTPLHIAAHYGNINVATLLLNRGAAVDFTARNDIT 270
Cdd:COG0666     10 LLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNT 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  271 PLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPLHCGARSGHEQVVEMLLDRGAPILSKTKNGLSPLHMATQGDHLNCV 350
Cdd:COG0666     90 LLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  351 QLLIQHNVPVDDVTNDYLTALHVAAHCGHYKVAKVLLDKKANPNAKALNGFTPLHIACKKNRIKVMELLLKHGASIQAVT 430
Cdd:COG0666    170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKD 249

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 2023156726  431 ESGLTPIHVAAFMGHVNIVSQLMHHGASPNTTNVRGETAL 470
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 ...
 1318-1447 2.36e-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: 195.77  E-value: 2.36e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726 1318 VPYMAKFVIFAKMNDPVESNLRCFCMTDDKVDKTLEQQENFEEVARSKDIEVLEGKPIYVDCYGNLAPLTKGGQQLVFNF 1397
Cdd:pfam17809    1 VPYLAKFVVFAKRYDPGEARLRCACMTDDGEDKTLEFHEGFTEVARSRDVEVLEGSPVSIELSGNLVPIKKKSQSRQMDF 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2023156726 1398 YAFKENRLPFSIKVRDTSQEPCGRLSFLKEPKTTKGLPQTAVCNLNITLP 1447
Cdd:pfam17809   81 KAFRENRLDGSVRVKDPSDPPKGLLSFMRDAKVDGGTVSQPLCTLNIVLP 130
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-305 3.07e-53

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 190.17  E-value: 3.07e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726    1 MAHAASQLKKNRDLEINADEETEKKRKHRKRSRDRKKKSDTNASYLRAARAGNLEKALDYLKSGVDINISNQNGLNALHL 80
Cdd:COG0666     14 ALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHA 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726   81 ASKEGHVEVVSELIQRGASVDAATKKGNTALHIASLAGQAEVVKVLVTNRANVNAQSQNGFTPLYMAAQENHLEVVKFLL 160
Cdd:COG0666     94 AARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLL 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  161 DNGASQSLATEDGFTPLAVALQQGHDQVVSLLLEndtkgkvrlpalhiaarkddtkaaalllqndHNADVE--SKSGFTP 238
Cdd:COG0666    174 EAGADVNARDNDGETPLHLAAENGHLEIVKLLLE-------------------------------AGADVNakDNDGKTA 222

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2023156726  239 LHIAAHYGNINVATLLLNRGAAVDFTARNDITPLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPL 305
Cdd:COG0666    223 LDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
 992-1096 8.17e-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: 8.17e-48
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726   992 SSFLVSFMVDARGGSMRGSRHhGMRIIIPPRKCTAPTRITCRLVKRHKLASPPPMVEGEGLASRLVEMGPSGAQFLGPVI 1071
Cdd:smart00218    1 PSFLVSGTFDARGGRLRGPRT-GVRLIIPPGAIPQGTRYTCYLVVHKTLSTPPPLEEGETLLSPVVECGPHGALFLRPVI 79

                            90       100
                    ....*....|....*....|....*
gi 2023156726  1072 VEIPHFGSMRGKERELIVLRSENGE 1096
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 ...
 4061-4144 3.93e-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: 3.93e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726 4061 ERTDIRMAIVADHLGLSWTELARELNFSVDEINQIRVENPNSLIAQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIV 4140
Cdd:cd08803      1 ERTDIRMAIVADHLGLSWTELARELNFSVDEINQIRVENPNSLIAQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIV 80


                   ....
gi 2023156726 4141 TLLE 4144
Cdd:cd08803     81 TLLE 84
ZU5 pfam00791
ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.
 996-1093 1.61e-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: 1.61e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  996 VSFMVDARGGSMRGSrHHGMRIIIPPRKCTAPTRITCRLVKRHKLASPPPMVEGEGLASRLVEMGPSGAQFLGPVIVEIP 1075
Cdd:pfam00791    1 VSGLVDSRGGRLVLP-NSGVSLLIPPGAIPEGTRIECYLAVNRDESSRPPLEEGETLLSPVVECGPPGLKFLKPVILEVP 79

                           90
                   ....*....|....*...
gi 2023156726 1076 HFGSMRGKERELIVLRSE 1093
Cdd:pfam00791   80 HCASLRPEEWEIVLKRSD 97
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 563-816 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 2023156726  563 KKGFTPLHVAAKYGKIEVANLLLQKNASPDASGKSGLTPLHVAAHY-----DNQKVALLLLDQGASPHASAKNGYTPLHI 637
Cdd:PHA03100    33 KKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIkynltDVKEIVKLLLEYGANVNAPDNNGITPLLY 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  638 AA--KKNQMDIATTLLEYGADANAVTRQGIAPVHLASQDGHVD--MVSLLLTRNANVNlgnksgltplhlaaQDDRVNVa 713
Cdd:PHA03100   113 AIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDIN--------------AKNRVNY- 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  714 evLVNQGAAVDAQTKMGYTPLHVGCHYGNIKIVNFLLQHSAKVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGaaPNELT 793
Cdd:PHA03100   178 --LLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNG--PSIKT 253

                          250       260
                   ....*....|....*....|...
gi 2023156726  794 VNGNTALAIAKRLGYISVVDTLK 816
Cdd:PHA03100   254 IIETLLYFKDKDLNTITKIKMLK 276
PHA03095 PHA03095
ankyrin-like protein; Provisional
 369-660 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 2023156726  369 TALHVAAHCGHYKVAKV---LLDKKANPNAKALNGFTPLHI-ACKKNRIKVMELLLKHGASIQAVTESGLTPIHV--AAF 442
Cdd:PHA03095    49 TPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHLyLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVylSGF 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  443 MGHVNIVSQLMHHGASPNTTNVRGETALH--MAARAGQTEVVRYLVQNGAQVEAKAKDDQTPLHISARLGK--ADIVQQL 518
Cdd:PHA03095   129 NINPKVIRLLLRKGADVNALDLYGMTPLAvlLKSRNANVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKprARIVREL 208

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  519 LQQGASPNAATTSGYTPLHLSAReGHEDVASVLLDhgaslsiitkkgftplhvaakygkievanlLLQKNASPDASGKSG 598
Cdd:PHA03095   209 IRAGCDPAATDMLGNTPLHSMAT-GSSCKRSLVLP------------------------------LLIAGISINARNRYG 257

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2023156726  599 LTPLHVAAHYDNQKVALLLLDQGASPHASAKNGYTPLHIAAKKNQMDIATTLLEYGADANAV 660
Cdd:PHA03095   258 QTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETV 319
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 221-461 2.52e-34

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 139.41  E-value: 2.52e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  221 LLQNDHNADVESKSGFTPLHIAAHYGNINVATLLLNRGAAVDFTARNDITPLH-----VASKRGNANMVKLLLDRGAKID 295
Cdd:PHA03100    21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGANVN 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  296 AKTRDGLTPLHCGA--RSGHEQVVEMLLDRGAPILSKTKNGLSPLHMATQGDH--LNCVQLLIQHNVPVDDVTN-DYlta 370
Cdd:PHA03100   101 APDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKNRvNY--- 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  371 lhvaahcghykvakvLLDKKANPNAKALNGFTPLHIACKKNRIKVMELLLKHGASIQAVTESGLTPIHVAAFMGHVNIVS 450
Cdd:PHA03100   178 ---------------LLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFK 242

                          250
                   ....*....|.
gi 2023156726  451 QLMHHGASPNT 461
Cdd:PHA03100   243 LLLNNGPSIKT 253
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 61-296 3.50e-26

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 115.15  E-value: 3.50e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726   61 LKSGVDINISNQNGLNALHLASKEGHVEVVSELIQRGASVDAATKKGNTALHIASLAGQA-----EVVKVLVTNRANVNA 135
Cdd:PHA03100    22 IMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNA 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  136 QSQNGFTPLYMAAQE--NHLEVVKFLLDNGASQSLATEDGFTPLAVALQQGHD--QVVSLLLEN----DTKGKVRlpalh 207
Cdd:PHA03100   102 PDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKgvdiNAKNRVN----- 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  208 iaarkddtkaaaLLLQNDHNADVESKSGFTPLHIAAHYGNINVATLLLNRGAAVDFTARNDITPLHVASKRGNANMVKLL 287
Cdd:PHA03100   177 ------------YLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLL 244


                   ....*....
gi 2023156726  288 LDRGAKIDA 296
Cdd:PHA03100   245 LNNGPSIKT 253
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
 4060-4146 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 2023156726  4060 CERTDIRMAIVADH-LGLSWTELARELNFSVDEINQIRVENPNSLIAQSFMLLKKWVTRDGKNATTDALTSVLTKINRID 4138
Cdd:smart00005    1 PELTRQKLAKLLDHpLGLDWRELARKLGLSEADIDQIRTEAPRDLAEQSVQLLRLWEQREGKNATLGTLLEALRKMGRDD 80


                    ....*...
gi 2023156726  4139 IVTLLEGP 4146
Cdd:smart00005   81 AVELLRSE 88
Ank_2 pfam12796
Ankyrin repeats (3 copies);
78-165 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 2023156726   78 LHLASKEGHVEVVSELIQRGASVDAATKKGNTALHIASLAGQAEVVKVLVtNRANVNAQSqNGFTPLYMAAQENHLEVVK 157
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78


                   ....*...
gi 2023156726  158 FLLDNGAS 165
Cdd:pfam12796   79 LLLEKGAD 86
Ank_2 pfam12796
Ankyrin repeats (3 copies);
371-463 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 2023156726  371 LHVAAHCGHYKVAKVLLDKKANPNAKALNGFTPLHIACKKNRIKVMELLLKHGAsiQAVTESGLTPIHVAAFMGHVNIVS 450
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 2023156726  451 QLMHHGASPNTTN 463
Cdd:pfam12796   79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
305-396 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 2023156726  305 LHCGARSGHEQVVEMLLDRGAPILSKTKNGLSPLHMATQGDHLNCVQLLIQHNVPvdDVTNDYLTALHVAAHCGHYKVAK 384
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 2023156726  385 VLLDKKANPNAK 396
Cdd:pfam12796   79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
669-759 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 2023156726  669 HLASQDGHVDMVSLLLTRNANVNLGNKSGLTPLHLAAQDDRVNVAEVLVNQgAAVDAQTKmGYTPLHVGCHYGNIKIVNF 748
Cdd:pfam12796    2 HLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKL 79

                           90
                   ....*....|.
gi 2023156726  749 LLQHSAKVNAK 759
Cdd:pfam12796   80 LLEKGADINVK 90
Death pfam00531
Death domain;
4066-4144 8.90e-17

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 78.18  E-value: 8.90e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726 4066 RMAIVADH---LGLSWTELARELNFSVDEINQIRVENPNsLIAQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIVTL 4142
Cdd:pfam00531    3 QLDRLLDPpppLGKDWRELARKLGLSENEIDEIESENPR-LRSQTYELLRLWEQREGKNATVGTLLEALRKLGRRDAAEK 81


                   ..
gi 2023156726 4143 LE 4144
Cdd:pfam00531   82 IQ 83
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 374-586 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 2023156726  374 AAHCGHYKVAKVLLD--KKANPNAKALNGFTPLHIACKKNRIK-VMELLLKHGASIqavtESGLTPIHVAAfMGHVNIVS 450
Cdd:TIGR00870   24 AAERGDLASVYRDLEepKKLNINCPDRLGRSALFVAAIENENLeLTELLLNLSCRG----AVGDTLLHAIS-LEYVDAVE 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  451 QLM-----HHGASPNTTNV---------RGETALHMAARAGQTEVVRYLVQNGAQVEAKAKDD--------------QTP 502
Cdd:TIGR00870   99 AILlhllaAFRKSGPLELAndqytseftPGITALHLAAHRQNYEIVKLLLERGASVPARACGDffvksqgvdsfyhgESP 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  503 LHISARLGKADIVQQLLQQGASPNAATTSGYTPLHLSAREGHEDVA---------SVLLDHGA------SLSIITK-KGF 566
Cdd:TIGR00870  179 LNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVMENEFKAEyeelscqmyNFALSLLDklrdskELEVILNhQGL 258

                          250       260
                   ....*....|....*....|
gi 2023156726  567 TPLHVAAKYGKIEVANLLLQ 586
Cdd:TIGR00870  259 TPLKLAAKEGRIVLFRLKLA 278
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 567-751 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 2023156726  567 TPLHVAAKYGKIE-VANLLLQKNASPDASGKSGLTPLHVAAHYDNQKVALLLLDqgASPH-------ASAKNGYTPLHIA 638
Cdd:cd22192     19 SPLLLAAKENDVQaIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPElvnepmtSDLYQGETALHIA 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  639 AKKNQMDIATTLLEYGADANAVTRQGIA--------------PVHLASQDGHVDMVSLLLTRNANVNLGNKSGLTPLH-L 703
Cdd:cd22192     97 VVNQNLNLVRELIARGADVVSPRATGTFfrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHiL 176

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2023156726  704 AAQDDRVNVAEV---LVNQGAAVDAQT------KMGYTPLHVGCHYGNIKIVNFLLQ 751
Cdd:cd22192    177 VLQPNKTFACQMydlILSYDKEDDLQPldlvpnNQGLTPFKLAAKEGNIVMFQHLVQ 233
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 142-355 5.47e-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: 5.47e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  142 TPLYMAAQENHLEVVKFLLDNgasqslATEDGFTplavalqqghdqvvslllendtKGKVRLPALHIAARKDDTKAAALL 221
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLLKC------PSCDLFQ----------------------RGALGETALHVAALYDNLEAAVVL 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  222 LQNDH---NADVESK--SGFTPLHIAAHYGNINVATLLLNRGAAVdFTARNDIT---------------PLHVASKRGNA 281
Cdd:cd22192     71 MEAAPelvNEPMTSDlyQGETALHIAVVNQNLNLVRELIARGADV-VSPRATGTffrpgpknliyygehPLSFAACVGNE 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  282 NMVKLLLDRGAKIDAKTRDGLTPLH-----------CgarsgheQVVEMLL-----DRGAPiLSKTKN--GLSPLHMATQ 343
Cdd:cd22192    150 EIVRLLIEHGADIRAQDSLGNTVLHilvlqpnktfaC-------QMYDLILsydkeDDLQP-LDLVPNnqGLTPFKLAAK 221

                          250
                   ....*....|..
gi 2023156726  344 GDHLNCVQLLIQ 355
Cdd:cd22192    222 EGNIVMFQHLVQ 233
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 463-587 6.69e-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: 6.69e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  463 NVRGETALHMAARAGQTEVVRYLVQNGAQVEAKAKDD--------------QTPLHISARLGKADIVQQLLQQGASPNAA 528
Cdd:cd22194    138 AYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVffnpkykhegfyfgETPLALAACTNQPEIVQLLMEKESTDITS 217

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2023156726  529 TTS-GYTPLH---LSAREGHEDVASV-------LLDH-GASLSIIT-KKGFTPLHVAAKYGKIEVANLLLQK 587
Cdd:cd22194    218 QDSrGNTVLHalvTVAEDSKTQNDFVkrmydmiLLKSeNKNLETIRnNEGLTPLQLAAKMGKAEILKYILSR 289
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 98-257 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 2023156726   98 ASVDAATKKGNTALHIASLAGQAEVVKVLVTNRANVNAQSQNGF--------------TPLYMAAQENHLEVVKFLLDNG 163
Cdd:cd22194    132 AEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVFfnpkykhegfyfgeTPLALAACTNQPEIVQLLMEKE 211

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  164 asqslatedgftPLAVALQqghdqvvslllenDTKGKVRLPALHIAArkDDTKAAA--------LLLQNDHNADVE---S 232
Cdd:cd22194    212 ------------STDITSQ-------------DSRGNTVLHALVTVA--EDSKTQNdfvkrmydMILLKSENKNLEtirN 264

                          170       180
                   ....*....|....*....|....*
gi 2023156726  233 KSGFTPLHIAAHYGNINVATLLLNR 257
Cdd:cd22194    265 NEGLTPLQLAAKMGKAEILKYILSR 289
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 135-442 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 2023156726  135 AQSQNGFTPlymAAQENHLEVVKFLLDNGASQSLATED--GFTPLAVALQQG-HDQVVSLLLENDTKGKVRLPALHiAAR 211
Cdd:TIGR00870   15 SDEEKAFLP---AAERGDLASVYRDLEEPKKLNINCPDrlGRSALFVAAIENeNLELTELLLNLSCRGAVGDTLLH-AIS 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  212 KDDTKAAALLLQndHNADVESKSGFTPLHIAAHYGninvatlllnrgaavDFTArnDITPLHVASKRGNANMVKLLLDRG 291
Cdd:TIGR00870   91 LEYVDAVEAILL--HLLAAFRKSGPLELANDQYTS---------------EFTP--GITALHLAAHRQNYEIVKLLLERG 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  292 AKIDAKT--------------RDGLTPLHCGARSGHEQVVEMLLDRGAPILSKTKNGLSPLHMAtqgdhlncvqlliqhn 357
Cdd:TIGR00870  152 ASVPARAcgdffvksqgvdsfYHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLL---------------- 215

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  358 VPVDDVTNDYLTalhVAAHCghYKVAKVLLDKKANPNAKAL----NGFTPLHIACKKNRIKVMELLLKHGASIQAVTESG 433
Cdd:TIGR00870  216 VMENEFKAEYEE---LSCQM--YNFALSLLDKLRDSKELEVilnhQGLTPLKLAAKEGRIVLFRLKLAIKYKQKKFVAWP 290


                   ....*....
gi 2023156726  434 LTPIHVAAF 442
Cdd:TIGR00870  291 NGQQLLSLY 299
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 399-426 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 2023156726   399 NGFTPLHIACKKNRIKVMELLLKHGASI 426
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 714-926 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 2023156726  714 EVLVNQGAAVDAQTKMGYTPLHVGCHYGNIKIVNFLLQHSAKVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAAPNELT 793
Cdd:PLN03192   542 EELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHA 621

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  794 vnGNTALAIAKRLGYISVVDT-----LKVVTEE----TMTTITVTEKHKmnvpeTMNEVLDMSDDEVRKANAPEILSDA- 863
Cdd:PLN03192   622 --AGDLLCTAAKRNDLTAMKEllkqgLNVDSEDhqgaTALQVAMAEDHV-----DMVRLLIMNGADVDKANTDDDFSPTe 694

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2023156726  864 --EYLSDVEEGEDAMTGDTDkylgPQDLKELGDDSLPAEGYMGFSLGARSASPKVSSDRSYTLNR 926
Cdd:PLN03192   695 lrELLQKRELGHSITIVDSV----PADEPDLGRDGGSRPGRLQGTSSDNQCRPRVSIYKGHPLLR 755
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 532-771 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 2023156726  532 GYTPLHLSAREG-HEDVASVLLDHGASLSIitkkGFTPLHVAAK--YGKIEVANLLLQKNASPDASGK-----------S 597
Cdd:TIGR00870   52 GRSALFVAAIENeNLELTELLLNLSCRGAV----GDTLLHAISLeyVDAVEAILLHLLAAFRKSGPLElandqytseftP 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  598 GLTPLHVAAHYDNQKVALLLLDQGASPHASAK--------------NGYTPLHIAAKKNQMDIATTLLEYGADANAVTRQ 663
Cdd:TIGR00870  128 GITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADSL 207

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  664 GIAPVHLASqdghvdMVSLLLTRNANVNLGNKSGLTPlHLAAQDDRVNVAEVLVNQgaavdaqtkmGYTPLHVGCHYGNI 743
Cdd:TIGR00870  208 GNTLLHLLV------MENEFKAEYEELSCQMYNFALS-LLDKLRDSKELEVILNHQ----------GLTPLKLAAKEGRI 270

                          250       260       270
                   ....*....|....*....|....*....|.
gi 2023156726  744 KIVNFLLQ---HSAKVNAKTkngYTPLHQAA 771
Cdd:TIGR00870  271 VLFRLKLAikyKQKKFVAWP---NGQQLLSL 298
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 267-296 9.30e-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: 9.30e-06
                            10        20        30
                    ....*....|....*....|....*....|
gi 2023156726   267 NDITPLHVASKRGNANMVKLLLDRGAKIDA 296
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 139-165 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 2023156726   139 NGFTPLYMAAQENHLEVVKFLLDNGAS 165
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 74-257 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 2023156726   74 GLNALHLASKEgHVEVVSELIQRGASVDAATK--------------KGNTALHIASLAGQAEVVKVLVTNRANVNA---- 135
Cdd:TIGR00870   82 GDTLLHAISLE-YVDAVEAILLHLLAAFRKSGplelandqytseftPGITALHLAAHRQNYEIVKLLLERGASVPAracg 160

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  136 ------QSQNGF----TPLYMAAQENHLEVVKFLLDNGASQSLATEDGFTPLavalqqgHDQVVslllENDTKGK----- 200
Cdd:TIGR00870  161 dffvksQGVDSFyhgeSPLNAAACLGSPSIVALLSEDPADILTADSLGNTLL-------HLLVM----ENEFKAEyeels 229

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2023156726  201 --VRLPALHIAARKDDTKAAALLLQNDhnadvesksGFTPLHIAAHYGNINVATLLLNR 257
Cdd:TIGR00870  230 cqMYNFALSLLDKLRDSKELEVILNHQ---------GLTPLKLAAKEGRIVLFRLKLAI 279
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 762-791 5.33e-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: 5.33e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 2023156726   762 NGYTPLHQAAQQGHTHIINVLLQHGAAPNE 791
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00121 PTZ00121
MAEBL; Provisional
 2584-3019 2.62e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.44  E-value: 2.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726 2584 RVDRTVKEAEEKlTEVSQFFRDKTEKLNDELQSPEKKQH---KKNGKEIHSSQSSASSSPEKVLLSELPSSGDEWSK--- 2657
Cdd:PTZ00121  1330 KADAAKKKAEEA-KKAAEAAKAEAEAAADEAEAAEEKAEaaeKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKkad 1408

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726 2658 -VKQYAHDGKcfpKVDE--RKASSLPSSPEKRifvQPAEDSKQTMEHKGSAQQtgvpevsqtgfqlkQSKLSSIRLKFEQ 2734
Cdd:PTZ00121  1409 eLKKAAAAKK---KADEakKKAEEKKKADEAK---KKAEEAKKADEAKKKAEE--------------AKKAEEAKKKAEE 1468

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726 2735 SISPRSKDVTQEEKKLDGQSKipvKKSQESKLPVYQFYSREKHAKQVEvidgstalqkEVKIQEDfvpgKAKAIEDFRAS 2814
Cdd:PTZ00121  1469 AKKADEAKKKAEEAKKADEAK---KKAEEAKKKADEAKKAAEAKKKAD----------EAKKAEE----AKKADEAKKAE 1531

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726 2815 DAQKRPEMSKGvvpeyfSEPQAKDLVYGSDSTAKGHWDKKIYRTWESPGTSNHQTQKEKLSHVLVPDTVKENHVDHAETK 2894
Cdd:PTZ00121  1532 EAKKADEAKKA------EEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEK 1605

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726 2895 TDKKSEFATVTEHKLAANGIH-SEEVK---ELTVKSPSKRVLYREFVVREGERNGEVADKISKRKEEIAVSHIPVRIVEE 2970
Cdd:PTZ00121  1606 KMKAEEAKKAEEAKIKAEELKkAEEEKkkvEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEE 1685

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*....
gi 2023156726 2971 KrtmldgvyelsakvsqsaviKEKVERQIDYMEDEKIKCSEIRKVTKQQ 3019
Cdd:PTZ00121  1686 D--------------------EKKAAEALKKEAEEAKKAEELKKKEAEE 1714
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
352-635 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 2023156726  352 LLIQHNVPVDDVTNDYLTALHVAAHCGHYKVAKVLLDKKANPNAKALNGFTPLHIACKKNRIKVMELLLKHGASIQAVTE 431
Cdd:COG0666      6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  432 SGLTPIHVAAFMGHVNIVSQLMHHGASPNTTNVRGETALHMAARAGQTEVVRYLVQNGAQVEAKAKDDQTPLHISARLGK 511
Cdd:COG0666     86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  512 ADIVQQLLQQGASPNAATTSGYTPLHLSAREGHEDVASVLLDHGASLSIITKKGFTPLHVAAKYGKIEVANLLLQKNASP 591
Cdd:COG0666    166 LEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADL 245

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 2023156726  592 DASGKSGLTPLHVAAHYDNQKVALLLLDQGASPHASAKNGYTPL 635
Cdd:COG0666    246 NAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
413-701 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 2023156726  413 IKVMELLLKHGASIQAVTESGLTPIHVAAFMGHVNIVSQLMHHGASPNTTNVRGETALHMAARAGQTEVVRYLVQNGAQV 492
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  493 EAKAKDDQTPLHISARLGKADIVQQLLQQGASPNAATTSGYTPLHLSAREGHEDVASVLLDHGASLSIITKKGFTPLHVA 572
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  573 AKYGKIEVANLLLQKNASPDASGKSGLTPLHVAAHYDNQKVALLLLDQGASPHASAKNGYTPLHIAAKKNQMDIATTLLE 652
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 2023156726  653 YGADANAVTRQGIAPVHLASQDGHVDMVSLLLTRNANVNLGNKSGLTPL 701
Cdd:COG0666    241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
381-666 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 2023156726  381 KVAKVLLDKKANPNAKALNGFTPLHIACKKNRIKVMELLLKHGASIQAVTESGLTPIHVAAFMGHVNIVSQLMHHGASPN 460
Cdd:COG0666      2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  461 TTNVRGETALHMAARAGQTEVVRYLVQNGAQVEAKAKDDQTPLHISARLGKADIVQQLLQQGASPNAATTSGYTPLHLSA 540
Cdd:COG0666     82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  541 REGHEDVASVLLDHGASLSIITKKGFTPLHVAAKYGKIEVANLLLQKNASPDASGKSGLTPLHVAAHYDNQKVALLLLDQ 620
Cdd:COG0666    162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 2023156726  621 GASPHASAKNGYTPLHIAAKKNQMDIATTLLEYGADANAVTRQGIA 666
Cdd:COG0666    242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
316-602 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 2023156726  316 VVEMLLDRGAPILSKTKNGLSPLHMATQGDHLNCVQLLIQHNVPVDDVTNDYLTALHVAAHCGHYKVAKVLLDKKANPNA 395
Cdd:COG0666      3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  396 KALNGFTPLHIACKKNRIKVMELLLKHGASIQAVTESGLTPIHVAAFMGHVNIVSQLMHHGASPNTTNVRGETALHMAAR 475
Cdd:COG0666     83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  476 AGQTEVVRYLVQNGAQVEAKAKDDQTPLHISARLGKADIVQQLLQQGASPNAATTSGYTPLHLSAREGHEDVASVLLDHG 555
Cdd:COG0666    163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 2023156726  556 ASLSIITKKGFTPLHVAAKYGKIEVANLLLQKNASPDASGKSGLTPL 602
Cdd:COG0666    243 ADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
551-816 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 2023156726  551 LLDHGASLSIITKKGFTPLHVAAKYGKIEVANLLLQKNASPDASGKSGLTPLHVAAHYDNQKVALLLLDQGASPHASAKN 630
Cdd:COG0666      7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  631 GYTPLHIAAKKNQMDIATTLLEYGADANAVTRQGIAPVHLASQDGHVDMVSLLLTRNANVNLGNKSGLTPLHLAAQDDRV 710
Cdd:COG0666     87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  711 NVAEVLVNQGAAVDAQTKMGYTPLHVGCHYGNIKIVNFLLQHSAKVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAAPN 790
Cdd:COG0666    167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246

                          250       260
                   ....*....|....*....|....*.
gi 2023156726  791 ELTVNGNTALAIAKRLGYISVVDTLK 816
Cdd:COG0666    247 AKDKDGLTALLLAAAAGAALIVKLLL 272
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
191-470 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 2023156726  191 LLLENDTKGKVRLPALHIAARKDDTKAAALLLQNDHNADVESKSGFTPLHIAAHYGNINVATLLLNRGAAVDFTARNDIT 270
Cdd:COG0666     10 LLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNT 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  271 PLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPLHCGARSGHEQVVEMLLDRGAPILSKTKNGLSPLHMATQGDHLNCV 350
Cdd:COG0666     90 LLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  351 QLLIQHNVPVDDVTNDYLTALHVAAHCGHYKVAKVLLDKKANPNAKALNGFTPLHIACKKNRIKVMELLLKHGASIQAVT 430
Cdd:COG0666    170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKD 249

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 2023156726  431 ESGLTPIHVAAFMGHVNIVSQLMHHGASPNTTNVRGETAL 470
Cdd:COG0666    250 KDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
218-503 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 2023156726  218 AALLLQNDHNADVESKSGFTPLHIAAHYGNINVATLLLNRGAAVDFTARNDITPLHVASKRGNANMVKLLLDRGAKIDAK 297
Cdd:COG0666      4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  298 TRDGLTPLHCGARSGHEQVVEMLLDRGAPILSKTKNGLSPLHMATQGDHLNCVQLLIQHNVPVDDVTNDYLTALHVAAHC 377
Cdd:COG0666     84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  378 GHYKVAKVLLDKKANPNAKALNGFTPLHIACKKNRIKVMELLLKHGASIQAVTESGLTPIHVAAFMGHVNIVSQLMHHGA 457
Cdd:COG0666    164 GNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 2023156726  458 SPNTTNVRGETALHMAARAGQTEVVRYLVQNGAQVEAKAKDDQTPL 503
Cdd:COG0666    244 DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
248-536 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 2023156726  248 INVATLLLNRGAAVDFTARNDITPLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPLHCGARSGHEQVVEMLLDRGAPI 327
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  328 LSKTKNGLSPLHMATQGDHLNCVQLLIQHNVPVDDVTNDYLTALHVAAHCGHYKVAKVLLDKKANPNAKALNGFTPLHIA 407
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  408 CKKNRIKVMELLLKHGASIQAVTESGLTPIHVAAFMGHVNIVSQLMHHGASPNTTNVRGETALHMAARAGQTEVVRYLVQ 487
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 2023156726  488 NGAQVEAKAKDDQTPLHISARLGKADIVQQLLQQGASPNAATTSGYTPL 536
Cdd:COG0666    241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
512-800 7.02e-60

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 209.43  E-value: 7.02e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  512 ADIVQQLLQQGASPNAATTSGYTPLHLSAREGHEDVASVLLDHGASLSIITKKGFTPLHVAAKYGKIEVANLLLQKNASP 591
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  592 DASGKSGLTPLHVAAHYDNQKVALLLLDQGASPHASAKNGYTPLHIAAKKNQMDIATTLLEYGADANAVTRQGIAPVHLA 671
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  672 SQDGHVDMVSLLLTRNANVNLGNKSGLTPLHLAAQDDRVNVAEVLVNQGAAVDAQTKMGYTPLHVGCHYGNIKIVNFLLQ 751
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 2023156726  752 HSAKVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAAPNELTVNGNTAL 800
Cdd:COG0666    241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
281-569 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 2023156726  281 ANMVKLLLDRGAKIDAKTRDGLTPLHCGARSGHEQVVEMLLDRGAPILSKTKNGLSPLHMATQGDHLNCVQLLIQHNVPV 360
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  361 DDVTNDYLTALHVAAHCGHYKVAKVLLDKKANPNAKALNGFTPLHIACKKNRIKVMELLLKHGASIQAVTESGLTPIHVA 440
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  441 AFMGHVNIVSQLMHHGASPNTTNVRGETALHMAARAGQTEVVRYLVQNGAQVEAKAKDDQTPLHISARLGKADIVQQLLQ 520
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 2023156726  521 QGASPNAATTSGYTPLHLSAREGHEDVASVLLDHGASLSIITKKGFTPL 569
Cdd:COG0666    241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
496-767 1.00e-58

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 205.96  E-value: 1.00e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  496 AKDDQTPLHISARLGKADIVQQLLQQGASPNAATTSGYTPLHLSAREGHEDVASVLLDHGASLSIITKKGFTPLHVAAKY 575
Cdd:COG0666     18 LLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARN 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  576 GKIEVANLLLQKNASPDASGKSGLTPLHVAAHYDNQKVALLLLDQGASPHASAKNGYTPLHIAAKKNQMDIATTLLEYGA 655
Cdd:COG0666     98 GDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  656 DANAVTRQGIAPVHLASQDGHVDMVSLLLTRNANVNLGNKSGLTPLHLAAQDDRVNVAEVLVNQGAAVDAQTKMGYTPLH 735
Cdd:COG0666    178 DVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALL 257

                          250       260       270
                   ....*....|....*....|....*....|..
gi 2023156726  736 VGCHYGNIKIVNFLLQHSAKVNAKTKNGYTPL 767
Cdd:COG0666    258 LAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
UPA_2 pfam17809
UPA domain; The UPA domain is conserved in UNC5, PIDD, and Ankyrins. It has a beta sandwich ...
 1318-1447 2.36e-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: 195.77  E-value: 2.36e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726 1318 VPYMAKFVIFAKMNDPVESNLRCFCMTDDKVDKTLEQQENFEEVARSKDIEVLEGKPIYVDCYGNLAPLTKGGQQLVFNF 1397
Cdd:pfam17809    1 VPYLAKFVVFAKRYDPGEARLRCACMTDDGEDKTLEFHEGFTEVARSRDVEVLEGSPVSIELSGNLVPIKKKSQSRQMDF 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2023156726 1398 YAFKENRLPFSIKVRDTSQEPCGRLSFLKEPKTTKGLPQTAVCNLNITLP 1447
Cdd:pfam17809   81 KAFRENRLDGSVRVKDPSDPPKGLLSFMRDAKVDGGTVSQPLCTLNIVLP 130
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
446-734 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 2023156726  446 VNIVSQLMHHGASPNTTNVRGETALHMAARAGQTEVVRYLVQNGAQVEAKAKDDQTPLHISARLGKADIVQQLLQQGASP 525
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  526 NAATTSGYTPLHLSAREGHEDVASVLLDHGASLSIITKKGFTPLHVAAKYGKIEVANLLLQKNASPDASGKSGLTPLHVA 605
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  606 AHYDNQKVALLLLDQGASPHASAKNGYTPLHIAAKKNQMDIATTLLEYGADANAVTRQGIAPVHLASQDGHVDMVSLLLT 685
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 2023156726  686 RNANVNLGNKSGLTPLHLAAQDDRVNVAEVLVNQGAAVDAQTKMGYTPL 734
Cdd:COG0666    241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
578-816 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 2023156726  578 IEVANLLLQKNASPDASGKSGLTPLHVAAHYDNQKVALLLLDQGASPHASAKNGYTPLHIAAKKNQMDIATTLLEYGADA 657
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  658 NAVTRQGIAPVHLASQDGHVDMVSLLLTRNANVNLGNKSGLTPLHLAAQDDRVNVAEVLVNQGAAVDAQTKMGYTPLHVG 737
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2023156726  738 CHYGNIKIVNFLLQHSAKVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAAPNELTVNGNTALAIAKRLGYISVVDTLK 816
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
54-371 1.30e-54

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 194.40  E-value: 1.30e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726   54 LEKALDYLKSGVDINISNQNGLNALHLASKEGHVEVVSELIQRGASVDAATKKGNTALHIASLAGQAEVVKVLVTNRANV 133
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  134 NAQSQNGFTPLYMAAQENHLEVVKFLLDNGASQSLATEDGFTPlavalqqghdqvvslllendtkgkvrlpaLHIAARKD 213
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETP-----------------------------LHLAAYNG 131

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  214 DTKAAALLLqnDHNADVE--SKSGFTPLHIAAHYGNINVATLLLNRGAAVDFTARNDITPLHVASKRGNANMVKLLLDRG 291
Cdd:COG0666    132 NLEIVKLLL--EAGADVNaqDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAG 209

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  292 AKIDAKTRDGLTPLHCGARSGHEQVVEMLLDRGAPILSKTKNGLSPLHMATQGDHLNCVQLLIQHNVPVDDVTNDYLTAL 371
Cdd:COG0666    210 ADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-305 3.07e-53

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 190.17  E-value: 3.07e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726    1 MAHAASQLKKNRDLEINADEETEKKRKHRKRSRDRKKKSDTNASYLRAARAGNLEKALDYLKSGVDINISNQNGLNALHL 80
Cdd:COG0666     14 ALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHA 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726   81 ASKEGHVEVVSELIQRGASVDAATKKGNTALHIASLAGQAEVVKVLVTNRANVNAQSQNGFTPLYMAAQENHLEVVKFLL 160
Cdd:COG0666     94 AARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLL 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  161 DNGASQSLATEDGFTPLAVALQQGHDQVVSLLLEndtkgkvrlpalhiaarkddtkaaalllqndHNADVE--SKSGFTP 238
Cdd:COG0666    174 EAGADVNARDNDGETPLHLAAENGHLEIVKLLLE-------------------------------AGADVNakDNDGKTA 222

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2023156726  239 LHIAAHYGNINVATLLLNRGAAVDFTARNDITPLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPL 305
Cdd:COG0666    223 LDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
 992-1096 8.17e-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: 8.17e-48
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726   992 SSFLVSFMVDARGGSMRGSRHhGMRIIIPPRKCTAPTRITCRLVKRHKLASPPPMVEGEGLASRLVEMGPSGAQFLGPVI 1071
Cdd:smart00218    1 PSFLVSGTFDARGGRLRGPRT-GVRLIIPPGAIPQGTRYTCYLVVHKTLSTPPPLEEGETLLSPVVECGPHGALFLRPVI 79

                            90       100
                    ....*....|....*....|....*
gi 2023156726  1072 VEIPHFGSMRGKERELIVLRSENGE 1096
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 ...
 4061-4144 3.93e-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: 3.93e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726 4061 ERTDIRMAIVADHLGLSWTELARELNFSVDEINQIRVENPNSLIAQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIV 4140
Cdd:cd08803      1 ERTDIRMAIVADHLGLSWTELARELNFSVDEINQIRVENPNSLIAQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIV 80


                   ....
gi 2023156726 4141 TLLE 4144
Cdd:cd08803     81 TLLE 84
ZU5 pfam00791
ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.
 996-1093 1.61e-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: 1.61e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  996 VSFMVDARGGSMRGSrHHGMRIIIPPRKCTAPTRITCRLVKRHKLASPPPMVEGEGLASRLVEMGPSGAQFLGPVIVEIP 1075
Cdd:pfam00791    1 VSGLVDSRGGRLVLP-NSGVSLLIPPGAIPEGTRIECYLAVNRDESSRPPLEEGETLLSPVVECGPPGLKFLKPVILEVP 79

                           90
                   ....*....|....*...
gi 2023156726 1076 HFGSMRGKERELIVLRSE 1093
Cdd:pfam00791   80 HCASLRPEEWEIVLKRSD 97
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 563-816 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 2023156726  563 KKGFTPLHVAAKYGKIEVANLLLQKNASPDASGKSGLTPLHVAAHY-----DNQKVALLLLDQGASPHASAKNGYTPLHI 637
Cdd:PHA03100    33 KKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIkynltDVKEIVKLLLEYGANVNAPDNNGITPLLY 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  638 AA--KKNQMDIATTLLEYGADANAVTRQGIAPVHLASQDGHVD--MVSLLLTRNANVNlgnksgltplhlaaQDDRVNVa 713
Cdd:PHA03100   113 AIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDIN--------------AKNRVNY- 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  714 evLVNQGAAVDAQTKMGYTPLHVGCHYGNIKIVNFLLQHSAKVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGaaPNELT 793
Cdd:PHA03100   178 --LLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNG--PSIKT 253

                          250       260
                   ....*....|....*....|...
gi 2023156726  794 VNGNTALAIAKRLGYISVVDTLK 816
Cdd:PHA03100   254 IIETLLYFKDKDLNTITKIKMLK 276
PHA03095 PHA03095
ankyrin-like protein; Provisional
 369-660 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 2023156726  369 TALHVAAHCGHYKVAKV---LLDKKANPNAKALNGFTPLHI-ACKKNRIKVMELLLKHGASIQAVTESGLTPIHV--AAF 442
Cdd:PHA03095    49 TPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHLyLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVylSGF 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  443 MGHVNIVSQLMHHGASPNTTNVRGETALH--MAARAGQTEVVRYLVQNGAQVEAKAKDDQTPLHISARLGK--ADIVQQL 518
Cdd:PHA03095   129 NINPKVIRLLLRKGADVNALDLYGMTPLAvlLKSRNANVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKprARIVREL 208

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  519 LQQGASPNAATTSGYTPLHLSAReGHEDVASVLLDhgaslsiitkkgftplhvaakygkievanlLLQKNASPDASGKSG 598
Cdd:PHA03095   209 IRAGCDPAATDMLGNTPLHSMAT-GSSCKRSLVLP------------------------------LLIAGISINARNRYG 257

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2023156726  599 LTPLHVAAHYDNQKVALLLLDQGASPHASAKNGYTPLHIAAKKNQMDIATTLLEYGADANAV 660
Cdd:PHA03095   258 QTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETV 319
PHA03095 PHA03095
ankyrin-like protein; Provisional
 406-692 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 2023156726  406 IACKKNRIKVMELLLKHGASIQAVTESGLTPIHVaaFMGH-----VNIVSQLMHHGASPNTTNVRGETALHMAARAGQTE 480
Cdd:PHA03095    20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHL--YLHYssekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTL 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  481 -VVRYLVQNGAQVEAKAKDDQTPLHISARlGK---ADIVQQLLQQGASPNAATTSGYTPLHLSAREGHEDVASV--LLDH 554
Cdd:PHA03095    98 dVIKLLIKAGADVNAKDKVGRTPLHVYLS-GFninPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVELLrlLIDA 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  555 GAslSIITKK--GFTPLHVAAKYGKI--EVANLLLQKNASPDASGKSGLTPLHVAAHYDNQKVALL--LLDQGASPHASA 628
Cdd:PHA03095   177 GA--DVYAVDdrFRSLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARN 254

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2023156726  629 KNGYTPLHIAAKKNQMDIATTLLEYGADANAVTRQGIAPVHLASQDGHVDMVSLLLTRNANVNL 692
Cdd:PHA03095   255 RYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAET 318
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 244-494 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 2023156726  244 HYGNINVATL--LLNRGAAVDFTARNDITPLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPLHCGARSGHEQ-----V 316
Cdd:PHA03100     9 KSRIIKVKNIkyIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLtdvkeI 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  317 VEMLLDRGAPILSKTKNGLSPLHMA--TQGDHLNCVQLLIQHNVPVDDVTNDYLTALHVAAHCGHY--KVAKVLLDKKAN 392
Cdd:PHA03100    89 VKLLLEYGANVNAPDNNGITPLLYAisKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVD 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  393 PNAKalngftplhiackkNRIKvmeLLLKHGASIQAVTESGLTPIHVAAFMGHVNIVSQLMHHGASPNTTNVRGETALHM 472
Cdd:PHA03100   169 INAK--------------NRVN---YLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHI 231

                          250       260
                   ....*....|....*....|..
gi 2023156726  473 AARAGQTEVVRYLVQNGAQVEA 494
Cdd:PHA03100   232 AILNNNKEIFKLLLNNGPSIKT 253
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 221-461 2.52e-34

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 139.41  E-value: 2.52e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  221 LLQNDHNADVESKSGFTPLHIAAHYGNINVATLLLNRGAAVDFTARNDITPLH-----VASKRGNANMVKLLLDRGAKID 295
Cdd:PHA03100    21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGANVN 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  296 AKTRDGLTPLHCGA--RSGHEQVVEMLLDRGAPILSKTKNGLSPLHMATQGDH--LNCVQLLIQHNVPVDDVTN-DYlta 370
Cdd:PHA03100   101 APDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKNRvNY--- 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  371 lhvaahcghykvakvLLDKKANPNAKALNGFTPLHIACKKNRIKVMELLLKHGASIQAVTESGLTPIHVAAFMGHVNIVS 450
Cdd:PHA03100   178 ---------------LLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFK 242

                          250
                   ....*....|.
gi 2023156726  451 QLMHHGASPNT 461
Cdd:PHA03100   243 LLLNNGPSIKT 253
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 409-756 2.68e-34

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 143.67  E-value: 2.68e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  409 KKNRIKVMELLLKHGASIQAVTESGLTPIHVAAFMGHVNIVSQLMHHGASPNTTNVRGETALHMAARAGQTEVVRYLVQN 488
Cdd:PHA02876   154 QQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDN 233

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  489 GAQVEakaKDDqtpLHISARLGKADIVQQLL--QQGASPNAATTSGYTPLHLSAREGH-EDVASVLLDHGASLSIITKKG 565
Cdd:PHA02876   234 RSNIN---KND---LSLLKAIRNEDLETSLLlyDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKG 307

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  566 FTPLHVAAKYG-KIEVANLLLQKNASPDASGKSGLTPLHVAAHYD-NQKVALLLLDQGASPHASAKNGYTPLHIAAKKNQ 643
Cdd:PHA02876   308 ETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNN 387

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  644 MDIATTLLEYGADANAVTRQGIAPVHLASQDGHVDM-VSLLLTRNANVNLGNKSGLTPLHLAAQDD-RVNVAEVLVNQGA 721
Cdd:PHA02876   388 VVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGA 467

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 2023156726  722 AVDAQTKMGYTPLHVGCHYGNikIVNFLLQHSAKV 756
Cdd:PHA02876   468 DVNAINIQNQYPLLIALEYHG--IVNILLHYGAEL 500
PHA03095 PHA03095
ankyrin-like protein; Provisional
 281-552 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 2023156726  281 ANMVKLLLDRGAKIDAKTRDGLTPLHCGARSGHEQ---VVEMLLDRGAPILSKTKNGLSPLHM-ATQGDHLNCVQLLIQH 356
Cdd:PHA03095    27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKvkdIVRLLLEAGADVNAPERCGFTPLHLyLYNATTLDVIKLLIKA 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  357 NVPVDDVTNDYLTALHV--AAHCGHYKVAKVLLDKKANPNAKALNGFTPLHIACKKNR--IKVMELLLKHGASIQAVTES 432
Cdd:PHA03095   107 GADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanVELLRLLIDAGADVYAVDDR 186

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  433 GLTPIHVAAFMGHVN--IVSQLMHHGASPNTTNVRGETALHMAARAGQTE--VVRYLVQNGAQVEAKAKDDQTPLHISAR 508
Cdd:PHA03095   187 FRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLHYAAV 266

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 2023156726  509 LGKADIVQQLLQQGASPNAATTSGYTPLHLSAREGHEDVASVLL 552
Cdd:PHA03095   267 FNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
PHA03095 PHA03095
ankyrin-like protein; Provisional
 511-816 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 2023156726  511 KADIVQQLLQQGASPNAATTSGYTPLHLSAREGHEDVASV---LLDHGASLSIITKKGFTPLHVAAKYG-KIEVANLLLQ 586
Cdd:PHA03095    26 TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHLYLYNAtTLDVIKLLIK 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  587 KNASPDASGKSGLTPLHVAAHYDN--QKVALLLLDQGASPHASAKNGYTPLHIAAKKNQMDIAT--TLLEYGADANAVT- 661
Cdd:PHA03095   106 AGADVNAKDKVGRTPLHVYLSGFNinPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVELlrLLIDAGADVYAVDd 185

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  662 -RQGIAPVHLASQDGHVDMVSLLLTRNANVNLGNKSGLTPLHLAAQDD---RVNVAEVLVNqGAAVDAQTKMGYTPLHVG 737
Cdd:PHA03095   186 rFRSLLHHHLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSsckRSLVLPLLIA-GISINARNRYGQTPLHYA 264

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2023156726  738 CHYGNIKIVNFLLQHSAKVNAKTKNGYTPLHQAAQQGHTHIINVLLQhgAAPNELTVNGntALAIAKRLGYISVVDTLK 816
Cdd:PHA03095   265 AVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALA--KNPSAETVAA--TLNTASVAGGDIPSDATR 339
Death_ank cd08317
Death domain associated with Ankyrins; Death Domain (DD) associated with Ankyrins. Ankyrins ...
 4061-4144 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 2023156726 4061 ERTDIRMAIVADHLGLSWTELARELNFSVDEINQIRVENPNSLIAQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIV 4140
Cdd:cd08317      1 HRADLRLSDIANLLGSDWPELARELGVSEEDIDLIRSENPNSLAQQAMAMLRLWLEREGEKATGNALESALKKIGRDDIV 80


                   ....
gi 2023156726 4141 TLLE 4144
Cdd:cd08317     81 EKCE 84
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 250-690 6.19e-33

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 139.43  E-value: 6.19e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  250 VATLLLNRGAAVDFTARNDITPLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPLHCGARSGHEQVVEMLLDRGAPIls 329
Cdd:PHA02876   160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNI-- 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  330 kTKNGLSPLHmATQGDHLNCVQLLIQHNVPVDDVtNDYLTalhvaahcghykvakvlldkkanpnakalngfTPLHIAck 409
Cdd:PHA02876   238 -NKNDLSLLK-AIRNEDLETSLLLYDAGFSVNSI-DDCKN--------------------------------TPLHHA-- 280

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  410 knrikvmelllkhgasIQAVTESGLTPihvaafmghvnivsQLMHHGASPNTTNVRGETALHMAARAG-QTEVVRYLVQN 488
Cdd:PHA02876   281 ----------------SQAPSLSRLVP--------------KLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIML 330

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  489 GAQVEAKAKDDQTPLHISARLGK-ADIVQQLLQQGASPNAATTSGYTPLHLSAREGHEDVASVLLDHGASLSIITKKGFT 567
Cdd:PHA02876   331 GADVNAADRLYITPLHQASTLDRnKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGT 410

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  568 PLHVAAkYGkievanlllqknASPDASGKSgltplhvaahydnqkvallLLDQGASPHASAKNGYTPLHIAAKKN-QMDI 646
Cdd:PHA02876   411 ALHFAL-CG------------TNPYMSVKT-------------------LIDRGANVNSKNKDLSTPLHYACKKNcKLDV 458

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....
gi 2023156726  647 ATTLLEYGADANAVTRQGIAPVHLASqdGHVDMVSLLLTRNANV 690
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 ...
 4061-4144 9.50e-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: 9.50e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726 4061 ERTDIRMAIVADHLGLSWTELARELNFSVDEINQIRVENPNSLIAQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIV 4140
Cdd:cd08805      1 ERVEMKMAVIREHLGLSWAELARELQFSVEDINRIRVENPNSLLEQSTALLNLWVDREGENAKMEPLYPALYSIDRLTIV 80


                   ....
gi 2023156726 4141 TLLE 4144
Cdd:cd08805     81 NILE 84
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 61-570 3.42e-31

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 134.04  E-value: 3.42e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726   61 LKSGVDINISNQNGLNALHLASKEGHVEVVSELIQRGASVDAATKKGNTALHIASLAGQAEVVKVLVTNRANVNaqsQNG 140
Cdd:PHA02876   165 LEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNIN---KND 241

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  141 FTpLYMAAQENHLEVVKFLLDNGASQSLATEDGFTPLAVALQQghdqvvslllendtkgkvrlPALhiaarkddTKAAAL 220
Cdd:PHA02876   242 LS-LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQA--------------------PSL--------SRLVPK 292

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  221 LLQNDHNADVESKSGFTPLHIAAH--YGNINVATLLLnRGAAVDFTARNDITPLHVASKRG-NANMVKLLLDRGAKIDAK 297
Cdd:PHA02876   293 LLERGADVNAKNIKGETPLYLMAKngYDTENIRTLIM-LGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNAR 371

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  298 TRDGLTPLHCGARSGHEQVVEMLLDRGAPILSKTKNGLSPLHMATQGdhlncvqlliqhnvpvddvTNDYLTalhvaahc 377
Cdd:PHA02876   372 DYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCG-------------------TNPYMS-------- 424

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  378 ghykvAKVLLDKKANPNAKALNGFTPLHIACKKN-RIKVMELLLKHGASIQAVTESGLTPIHVAafMGHVNIVSQLMHHG 456
Cdd:PHA02876   425 -----VKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIA--LEYHGIVNILLHYG 497

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  457 ASPNTTNVRGETA-------LHMAARAGQTEVVRYLVQNGAQVEAKAKDDQTPLHISARlgkaDIVQqllqqgaspnaaT 529
Cdd:PHA02876   498 AELRDSRVLHKSLndnmfsfRYIIAHICIQDFIRHDIRNEVNPLKRVPTRFTSLRESFK----EIIQ------------S 561

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|..
gi 2023156726  530 TSGYTPLHLSAREGHEDVASVLLDHGASLSI-ITKKGFTPLH 570
Cdd:PHA02876   562 DDTFKRIWLRCKEELKDISKIRINMFYSLDIfIISKNMNLLH 603
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 481-815 4.27e-30

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 130.57  E-value: 4.27e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  481 VVRYLVQNGAQVEAKAKDDQTPLHISARLGKADIVQQLLQQGASPNAATTSGYTPLHLSAREGHEDVASVLLDHGASlsi 560
Cdd:PHA02876   160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSN--- 236

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  561 ITKKGFTPLHvAAKYGKIEVANLLLQKNASPDASGKSGLTPLHVAAHYDN-QKVALLLLDQGASPHASAKNGYTPLHIAA 639
Cdd:PHA02876   237 INKNDLSLLK-AIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMA 315

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  640 KkNQMDIAT--TLLEYGADANAVTRQGIAPVHLASQ-DGHVDMVSLLLTRNANVNLGNKSGLTPLHLAAQDDRVNVAEVL 716
Cdd:PHA02876   316 K-NGYDTENirTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTL 394

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  717 VNQGAAVDAQTKMGYTPLHVG-CHYGNIKIVNFLLQHSAKVNAKTKNGYTPLHQAAQQG-HTHIINVLLQHGAAPNELTV 794
Cdd:PHA02876   395 LDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINI 474

                          330       340
                   ....*....|....*....|.
gi 2023156726  795 NGNTALAIAkrLGYISVVDTL 815
Cdd:PHA02876   475 QNQYPLLIA--LEYHGIVNIL 493
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 211-558 7.70e-30

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 129.80  E-value: 7.70e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  211 RKDDTKAAALLLQNdhNADVESKSGF--TPLHIAAHYGNINVATLLLNRGAAVDFTARNDITPLHVASKRGNANMVKLLL 288
Cdd:PHA02876   154 QQDELLIAEMLLEG--GADVNAKDIYciTPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII 231

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  289 DRGAKIDAKTRDGL-----------------------------TPLHCGARSGH-EQVVEMLLDRGAPILSKTKNGLSPL 338
Cdd:PHA02876   232 DNRSNINKNDLSLLkairnedletslllydagfsvnsiddcknTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPL 311

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  339 H-MATQGDHLNCVQLLIQHNVPVDDVTNDYLTALHVAAHCGHYK-VAKVLLDKKANPNAKALNGFTPLHIACKKNRIKVM 416
Cdd:PHA02876   312 YlMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKdIVITLLELGANVNARDYCDKTPIHYAAVRNNVVII 391

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  417 ELLLKHGASIQAVTESGLTPIHVAAFmghvnivsqlmhhGASPNTTnvrgetalhmaaragqtevVRYLVQNGAQVEAKA 496
Cdd:PHA02876   392 NTLLDYGADIEALSQKIGTALHFALC-------------GTNPYMS-------------------VKTLIDRGANVNSKN 439

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2023156726  497 KDDQTPLHISARLG-KADIVQQLLQQGASPNAATTSGYTPLHLSAreGHEDVASVLLDHGASL 558
Cdd:PHA02876   440 KDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGAEL 500
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 381-561 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 2023156726  381 KVAKVLLDKKANPNAKALNGFTPLHIAC-----KKNRIKVMELLLKHGASIQAVTESGLTPIHVAAF--MGHVNIVSQLM 453
Cdd:PHA03100    49 DVVKILLDNGADINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISkkSNSYSIVEYLL 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  454 HHGASPNTTNVRGETALHMAARAGQ--TEVVRYLVQNGAQVEAK--------------AKDDQ--TPLHISARLGKADIV 515
Cdd:PHA03100   129 DNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKnrvnyllsygvpinIKDVYgfTPLHYAVYNNNPEFV 208

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2023156726  516 QQLLQQGASPNAATTSGYTPLHLSAREGHEDVASVLLDHGASLSII 561
Cdd:PHA03100   209 KYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTI 254
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 402-623 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 2023156726  402 TPLHIACKKNRIKVMELLLKHGASIQAVTESGLTPIHVAAFMGHV-----NIVSQLMHHGASPNTTNVRGETALHMAA-- 474
Cdd:PHA03100    37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAIsk 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  475 RAGQTEVVRYLVQNGAQVEAKAKDDQTPLHISARLGKAD--IVQQLLQQGASPNAATTSGYtplhlsareghedvasvLL 552
Cdd:PHA03100   117 KSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDINAKNRVNY-----------------LL 179

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2023156726  553 DHGASLSIITKKGFTPLHVAAKYGKIEVANLLLQKNASPDASGKSGLTPLHVAAHYDNQKVALLLLDQGAS 623
Cdd:PHA03100   180 SYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 470-770 8.86e-29

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 123.15  E-value: 8.86e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  470 LHMAARAGQTEVVRYLVQN-GAQVEAKAKDDQTPLHISARLGKADIVQQLLQQGASPNAATTSGYTPLHLSAREGHEDVA 548
Cdd:PHA02874     5 LRMCIYSGDIEAIEKIIKNkGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDII 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  549 SVLLDHGASLSIItkkgftPLHVAAKygkiEVANLLLQKNASPDASGKSGLTPLHVAAHYDNQKVALLLLDQGASPHASA 628
Cdd:PHA02874    85 KLLIDNGVDTSIL------PIPCIEK----DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIED 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  629 KNGYTPLHIAAKKNQMDIATTLLEYGADANAVTRQGIAPVHLASQDGHVDMVSLLLTRNANVNLGNKSGLTPLHLAAQDD 708
Cdd:PHA02874   155 DNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHN 234

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2023156726  709 RvNVAEVLVNQgAAVDAQTKMGYTPLHVGCHYG-NIKIVNFLLQHSAKVNAKTKNGYTPLHQA 770
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. ...
 4061-4144 1.53e-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: 1.53e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726 4061 ERTDIRMAIVADHLGLSWTELARELNFSVDEINQIRVENPNSLIAQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIV 4140
Cdd:cd08804      1 ERTEERLAHIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLTQCLTKINRMDIV 80


                   ....
gi 2023156726 4141 TLLE 4144
Cdd:cd08804     81 HLME 84
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 402-660 2.53e-27

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 118.53  E-value: 2.53e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  402 TPLHIACKKNRIKVMELLLKHGASIQAVTESGLTPIHVAAFMGHVNIVSQLMHHGASP---------------------- 459
Cdd:PHA02874    37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTsilpipciekdmiktildcgid 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  460 -NTTNVRGETALHMAARAGQTEVVRYLVQNGAQVEAKAKDDQTPLHISARLGKADIVQQLLQQGASPNAATTSGYTPLHL 538
Cdd:PHA02874   117 vNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  539 SAREGHEDVASVLLDHGASLSIITKKGFTPLHVAAKYGKIEVAnlLLQKNASPDASGKSGLTPLHVAAHYDNQK-VALLL 617
Cdd:PHA02874   197 AAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIE--LLINNASINDQDIDGSTPLHHAINPPCDIdIIDIL 274

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 2023156726  618 LDQGASPHASAKNGYTPLHIAAKK-NQMDIATTLLeygadANAV 660
Cdd:PHA02874   275 LYHKADISIKDNKGENPIDTAFKYiNKDPVIKDII-----ANAV 313
PHA03095 PHA03095
ankyrin-like protein; Provisional
 60-323 2.83e-27

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 119.36  E-value: 2.83e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726   60 YLKSGVDINISNQNGLNALHLASKEGH---VEVVSELIQRGASVDAATKKGNTALHI-ASLAGQAEVVKVLVTNRANVNA 135
Cdd:PHA03095    33 LLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLyLYNATTLDVIKLLIKAGADVNA 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  136 QSQNGFTPL--YMAAQENHLEVVKFLLDNGASQSLATEDGFTPLAVALQQGH--DQVVSLLLEND----TKGKVRLPALH 207
Cdd:PHA03095   113 KDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanVELLRLLIDAGadvyAVDDRFRSLLH 192

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  208 IAAR--KDDTKAAALLLQNDHNADVESKSGFTPLHIAAHYG---NINVATLLLNrGAAVDFTARNDITPLHVASKRGNAN 282
Cdd:PHA03095   193 HHLQsfKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSsckRSLVLPLLIA-GISINARNRYGQTPLHYAAVFNNPR 271

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 2023156726  283 MVKLLLDRGAKIDAKTRDGLTPLHCGARSGHEQVVEMLLDR 323
Cdd:PHA03095   272 ACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAK 312
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 467-692 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 2023156726  467 ETALHMAARAGQTEVVRYLVQNGAQVEAKAKDDQTPLHISARLGKADIVQQLLQQGASPNAATTSGYTPLHLSAREGHED 546
Cdd:PHA02875     3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  547 VASVLLDHGASLS-IITKKGFTPLHVAAKYGKIEVANLLLQKNASPDASGKSGLTPLHVAAHYDNQKVALLLLDQGASPH 625
Cdd:PHA02875    83 AVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLD 162

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2023156726  626 ASAKNGYTPLHIAAKKNQMDIATTLLEYGADANAVTRQG-IAPVHLASQDGHVDMVSLLLTRNANVNL 692
Cdd:PHA02875   163 IEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNI 230
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 242-472 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 2023156726  242 AAHYGNINVATLLLNRGAAVDFTARNDITPLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPLHCGARSGHEQVVEMLL 321
Cdd:PHA02875     9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  322 DRGAPILSKT-KNGLSPLHMATQGDHLNCVQLLIQHNVPVDDVTNDYLTALHVAAHCGHYKVAKVLLDKKANPNAKALNG 400
Cdd:PHA02875    89 DLGKFADDVFyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCG 168

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2023156726  401 FTPLHIACKKNRIKVMELLLKHGASIQAVTESG-LTPIHVAAFMGHVNIVSQLMHHGASPN-TTNVRGE--TALHM 472
Cdd:PHA02875   169 CTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNiMFMIEGEecTILDM 244
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 302-598 6.68e-27

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 118.06  E-value: 6.68e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  302 LTPLHCGARSGHEQVVEMLLDRGAPILSKTKNGLSPLHMATQGDHLNCVQLLIQHNVPvDDVTNDYlTALHVAAHCGHYK 381
Cdd:PHA02878    38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINK-CSVFYTL-VAIKDAFNNRNVE 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  382 VAKVLLDKKANPNAKalngfTPLHIACKKNR-----IKVMELLLKHGASIQAVTE-SGLTPIHVAAFMGHVNIVSQLMHH 455
Cdd:PHA02878   116 IFKIILTNRYKNIQT-----IDLVYIDKKSKddiieAEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSY 190

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  456 GASPNTTNVRGETALHMAARAGQTEVVRYLVQNGAQVEAKAKDDQTPLHIS-ARLGKADIVQQLLQQGASPNAATT-SGY 533
Cdd:PHA02878   191 GANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYiLGL 270

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2023156726  534 TPLHLSAREghEDVASVLLDHGASLSIITKKGFTPLHVAAKY------GKIEVANLLLQKNASPDASGKSG 598
Cdd:PHA02878   271 TALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAVKQylciniGRILISNICLLKRIKPDIKNSEG 339
PHA03095 PHA03095
ankyrin-like protein; Provisional
 120-432 7.81e-27

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 117.82  E-value: 7.81e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  120 AEVVKVLVTNRANVNAQSQNGFTPL--YMA-AQENHLEVVKFLLDNGASQSLATEDGFTPLavalqqgHdqvvsLLLEND 196
Cdd:PHA03095    27 VEEVRRLLAAGADVNFRGEYGKTPLhlYLHySSEKVKDIVRLLLEAGADVNAPERCGFTPL-------H-----LYLYNA 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  197 TKGKVrlpalhiaarkddtkaAALLLqnDHNADVESKS--GFTPLHIAAHYGNIN--VATLLLNRGAAVDFTARNDITPL 272
Cdd:PHA03095    95 TTLDV----------------IKLLI--KAGADVNAKDkvGRTPLHVYLSGFNINpkVIRLLLRKGADVNALDLYGMTPL 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  273 HVASKRGNAN--MVKLLLDRGAKIDAKTRDGLTPLHCGARSGH--EQVVEMLLDRGAPILSKTKNGLSPLH-MATQGD-- 345
Cdd:PHA03095   157 AVLLKSRNANveLLRLLIDAGADVYAVDDRFRSLLHHHLQSFKprARIVRELIRAGCDPAATDMLGNTPLHsMATGSSck 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  346 HLNCVQLLIqHNVPVDdVTNDYL-TALHVAAHCGHYKVAKVLLDKKANPNAKALNGFTPLHIACKKNRIKVMELLLKHGA 424
Cdd:PHA03095   237 RSLVLPLLI-AGISIN-ARNRYGqTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNP 314


                   ....*...
gi 2023156726  425 SIQAVTES 432
Cdd:PHA03095   315 SAETVAAT 322
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 61-296 3.50e-26

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 115.15  E-value: 3.50e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726   61 LKSGVDINISNQNGLNALHLASKEGHVEVVSELIQRGASVDAATKKGNTALHIASLAGQA-----EVVKVLVTNRANVNA 135
Cdd:PHA03100    22 IMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNA 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  136 QSQNGFTPLYMAAQE--NHLEVVKFLLDNGASQSLATEDGFTPLAVALQQGHD--QVVSLLLEN----DTKGKVRlpalh 207
Cdd:PHA03100   102 PDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKgvdiNAKNRVN----- 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  208 iaarkddtkaaaLLLQNDHNADVESKSGFTPLHIAAHYGNINVATLLLNRGAAVDFTARNDITPLHVASKRGNANMVKLL 287
Cdd:PHA03100   177 ------------YLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLL 244


                   ....*....
gi 2023156726  288 LDRGAKIDA 296
Cdd:PHA03100   245 LNNGPSIKT 253
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 237-488 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 2023156726  237 TPLHIAAHYGNINVATLLLNRGAAVDFTARNDITPLHVASKRGNANMVKLLLDRGA-----------------------K 293
Cdd:PHA02874    37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVdtsilpipciekdmiktildcgiD 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  294 IDAKTRDGLTPLHCGARSGHEQVVEMLLDRGAPILSKTKNGLSPLHMATQGDHLNCVQLLIQhNVPVDDVTNDYL-TALH 372
Cdd:PHA02874   117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLE-KGAYANVKDNNGeSPLH 195

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  373 VAAHCGHYKVAKVLLDKKANPNAKALNGFTPLHIACKKNRiKVMELLLKHgASIQAVTESGLTPIHVA-AFMGHVNIVSQ 451
Cdd:PHA02874   196 NAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLINN-ASINDQDIDGSTPLHHAiNPPCDIDIIDI 273

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 2023156726  452 LMHHGASPNTTNVRGETALHMAAR-AGQTEVVRYLVQN 488
Cdd:PHA02874   274 LLYHKADISIKDNKGENPIDTAFKyINKDPVIKDIIAN 311
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 535-808 2.22e-25

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 113.44  E-value: 2.22e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  535 PLHLSAREGHEDVASVLLDHGASLSIITKKGFTPLHVAAKY-GKIEVANLLLQKNASpdaSGKSGLTPLHVAAHYDNQKV 613
Cdd:PHA02878    40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEpNKLGMKEMIRSINKC---SVFYTLVAIKDAFNNRNVEI 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  614 A-LLLLDQgasphasAKNGYTPLHIAAKKNQMD------IATTLLEYGADANAVTR-QGIAPVHLASQDGHVDMVSLLLT 685
Cdd:PHA02878   117 FkIILTNR-------YKNIQTIDLVYIDKKSKDdiieaeITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLS 189

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  686 RNANVNLGNKSGLTPLHLAAQDDRVNVAEVLVNQGAAVDAQTKMGYTPLHVGCHY-GNIKIVNFLLQHSAKVNAK-TKNG 763
Cdd:PHA02878   190 YGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKsYILG 269

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 2023156726  764 YTPLHQAAQQghTHIINVLLQHGAAPNELTVNGNTALAIA--KRLGY 808
Cdd:PHA02878   270 LTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAvkQYLCI 314
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
 4060-4146 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 2023156726  4060 CERTDIRMAIVADH-LGLSWTELARELNFSVDEINQIRVENPNSLIAQSFMLLKKWVTRDGKNATTDALTSVLTKINRID 4138
Cdd:smart00005    1 PELTRQKLAKLLDHpLGLDWRELARKLGLSEADIDQIRTEAPRDLAEQSVQLLRLWEQREGKNATLGTLLEALRKMGRDD 80


                    ....*...
gi 2023156726  4139 IVTLLEGP 4146
Cdd:smart00005   81 AVELLRSE 88
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 151-373 1.04e-24

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 110.47  E-value: 1.04e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  151 NHLEVVKFLLDNGASQSLATEDGFTPLAVALQQGHDQVVSLLLENDTKGKVRLPA----LHIAARKDDTKAAALLLQ-ND 225
Cdd:PHA02875    13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDieseLHDAVEEGDVKAVEELLDlGK 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  226 HNADVESKSGFTPLHIAAHYGNINVATLLLNRGAAVDFTARNDITPLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPL 305
Cdd:PHA02875    93 FADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPL 172

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2023156726  306 HCGARSGHEQVVEMLLDRGAPILSKTKNG-LSPLHMATQGDHLNCVQLLIQHNVPVDDVT---NDYLTALHV 373
Cdd:PHA02875   173 IIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNIMFmieGEECTILDM 244
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 378-661 4.48e-24

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 108.54  E-value: 4.48e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  378 GHYKVAKVLLDKKANPNAKALNGFTPLHIACKKNRIKVMELLLKHGAsIQAVTESGL-TPIHVAAFMGHVNIVSQLMHHG 456
Cdd:PHA02875    13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGA-IPDVKYPDIeSELHDAVEEGDVKAVEELLDLG 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  457 ASPNTtnvrgetalhmaaragqtevVRYlvqngaqveakaKDDQTPLHISARLGKADIVQQLLQQGASPNAATTSGYTPL 536
Cdd:PHA02875    92 KFADD--------------------VFY------------KDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPL 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  537 HLSAREGHEDVASVLLDHGASLSIITKKGFTPLHVAAKYGKIEVANLLLQKNASPDASGKSGltplhvaahydnqKVALL 616
Cdd:PHA02875   140 HLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNG-------------CVAAL 206

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 2023156726  617 LLdqgasphasakngytplhiAAKKNQMDIATTLLEYGADANAVT 661
Cdd:PHA02875   207 CY-------------------AIENNKIDIVRLFIKRGADCNIMF 232
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 605-800 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 2023156726  605 AAHYDNQKVALLLLDQGASPHASAKNGYTPLHIAAKKNQMDIATTLLEYGADANaVTRQGI-APVHLASQDGHVDMVSLL 683
Cdd:PHA02875     9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPD-VKYPDIeSELHDAVEEGDVKAVEEL 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  684 LTRNANVN-LGNKSGLTPLHLAAQDDRVNVAEVLVNQGAAVDAQTKMGYTPLHVGCHYGNIKIVNFLLQHSAKVNAKTKN 762
Cdd:PHA02875    88 LDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCC 167

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 2023156726  763 GYTPLHQAAQQGHTHIINVLLQHGAAPNELTVNGNTAL 800
Cdd:PHA02875   168 GCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAA 205
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 337-605 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 2023156726  337 PLHMATQGDHLNCVQLLIQHNVPVDDVTNDYLTALHVAAHCGHYKVAKVLLDKKANpnAKALNGFTPLHIACKKNRIKVM 416
Cdd:PHA02878    40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINK--CSVFYTLVAIKDAFNNRNVEIF 117

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  417 E-LLLKHGASIQAVTESGLTPIHVAAFMgHVNIVSQLMHHGASPN-TTNVRGETALHMAARAGQTEVVRYLVQNGAQVEA 494
Cdd:PHA02878   118 KiILTNRYKNIQTIDLVYIDKKSKDDII-EAEITKLLLSYGADINmKDRHKGNTALHYATENKDQRLTELLLSYGANVNI 196

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  495 KAKDDQTPLHISARLGKADIVQQLLQQGASPNAATTSGYTPLHLS-AREGHEDVASVLLDHGASLSI-ITKKGFTPLHVA 572
Cdd:PHA02878   197 PDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAkSYILGLTALHSS 276

                          250       260       270
                   ....*....|....*....|....*....|...
gi 2023156726  573 AKygKIEVANLLLQKNASPDASGKSGLTPLHVA 605
Cdd:PHA02878   277 IK--SERKLKLLLEYGADINSLNSYKLTPLSSA 307
Ank_2 pfam12796
Ankyrin repeats (3 copies);
78-165 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 2023156726   78 LHLASKEGHVEVVSELIQRGASVDAATKKGNTALHIASLAGQAEVVKVLVtNRANVNAQSqNGFTPLYMAAQENHLEVVK 157
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78


                   ....*...
gi 2023156726  158 FLLDNGAS 165
Cdd:pfam12796   79 LLLEKGAD 86
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 111-421 5.88e-23

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 106.12  E-value: 5.88e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  111 LHIASLAGQAEVVKVLVTNRANVNAQSQNGFTPLYMAAQENHLEVVKFLLDNGASQSLATEdgFTPLAVALQQGHDQVVS 190
Cdd:PHA02878    41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFYT--LVAIKDAFNNRNVEIFK 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  191 LLLENDTKGKVRLPALHIAARKDD----TKAAALLLQndHNADVESK---SGFTPLHIAAHYGNINVATLLLNRGAAVDF 263
Cdd:PHA02878   119 IILTNRYKNIQTIDLVYIDKKSKDdiieAEITKLLLS--YGADINMKdrhKGNTALHYATENKDQRLTELLLSYGANVNI 196

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  264 TARNDITPLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPLHCG-ARSGHEQVVEMLLDRGAPILSK-TKNGLSPLHMA 341
Cdd:PHA02878   197 PDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKsYILGLTALHSS 276

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  342 TQGDHLncVQLLIQHNVPVDDVTNDYLTALHVAA------HCGHYKVAKVLLDKKANPNAKALNGFTpLHIACKKNRIKV 415
Cdd:PHA02878   277 IKSERK--LKLLLEYGADINSLNSYKLTPLSSAVkqylciNIGRILISNICLLKRIKPDIKNSEGFI-DNMDCITSNKRL 353


                   ....*.
gi 2023156726  416 MELLLK 421
Cdd:PHA02878   354 NQIKDK 359
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 545-815 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 2023156726  545 EDVASVLLDHGASLSIITKKGFTPLHVAAKYGKIEVANLLLQKNASPDASGKSGLTPLHVAAHYDNQKVALLLLDQGASP 624
Cdd:PHA02874    15 EAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDT 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  625 hasakngyTPLHIAAKKNQMdiATTLLEYGADANAVTRQGIAPVHLASQDGHVDMVSLLLTRNANVNLGNKSGLTPLHLA 704
Cdd:PHA02874    95 --------SILPIPCIEKDM--IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIA 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  705 AQDDRVNVAEVLVNQGAAVDAQTKMGYTPLHVGCHYGNIKIVNFLLQHSAKVNAKTKNGYTPLHQAAQQGHTHIinVLLQ 784
Cdd:PHA02874   165 IKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAI--ELLI 242

                          250       260       270
                   ....*....|....*....|....*....|....
gi 2023156726  785 HGAAPNELTVNGNTALAIAkrLGY---ISVVDTL 815
Cdd:PHA02874   243 NNASINDQDIDGSTPLHHA--INPpcdIDIIDIL 274
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 85-374 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 2023156726   85 GHVEVVSELIQ-RGASVDAATKKGNTALHIASLAGQAEVVKVLVTNRANVNAQSQNGFTPLYMAAQENHLEVVKFLLDNG 163
Cdd:PHA02874    12 GDIEAIEKIIKnKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  164 ASQSLatedgfTPLAVALQQGHDQVVSLLLENDTKGKVRLPALHIAARKDDTKAAALLLQNDHNADVESKSGFTPLHIAA 243
Cdd:PHA02874    92 VDTSI------LPIPCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAI 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  244 HYGNINVATLLLNRGAAVDFTARNDITPLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPLHcGARSGHEQVVEMLLDr 323
Cdd:PHA02874   166 KHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLH-NAIIHNRSAIELLIN- 243

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2023156726  324 GAPILSKTKNGLSPLHMATQGD-HLNCVQLLIQHNVPVDDVTNDYLTALHVA 374
Cdd:PHA02874   244 NASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTA 295
Ank_2 pfam12796
Ankyrin repeats (3 copies);
371-463 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 2023156726  371 LHVAAHCGHYKVAKVLLDKKANPNAKALNGFTPLHIACKKNRIKVMELLLKHGAsiQAVTESGLTPIHVAAFMGHVNIVS 450
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 2023156726  451 QLMHHGASPNTTN 463
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 141-440 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 2023156726  141 FTPLYMAAQENHLEVVKFLLDNGASQSLATEDGFTPLAVALQQGHDQVVSLLLENDTKGKVrlpalhiaarkddtkaaal 220
Cdd:PHA02878    38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSV------------------- 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  221 llqndHNADVESKSGFtplhiaaHYGNINVA-TLLLNRgaaVDFTARNDITPLHVASKRG--NANMVKLLLDRGAKIDAK 297
Cdd:PHA02878    99 -----FYTLVAIKDAF-------NNRNVEIFkIILTNR---YKNIQTIDLVYIDKKSKDDiiEAEITKLLLSYGADINMK 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  298 TRDGL-TPLHCGARSGHEQVVEMLLDRGAPILSKTKNGLSPLHMATQGDHLNCVQLLIQHNVPVDDVTNDYLTALHVA-A 375
Cdd:PHA02878   164 DRHKGnTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvG 243

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2023156726  376 HCGHYKVAKVLLDKKANPNAKA-LNGFTPLHIACKKNRikVMELLLKHGASIQAVTESGLTPIHVA 440
Cdd:PHA02878   244 YCKDYDILKLLLEHGVDVNAKSyILGLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPLSSA 307
Ank_2 pfam12796
Ankyrin repeats (3 copies);
338-428 6.78e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.87  E-value: 6.78e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  338 LHMATQGDHLNCVQLLIQHNVPVDDVTNDYLTALHVAAHCGHYKVAKVLLDkKANPNAKaLNGFTPLHIACKKNRIKVME 417
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLK-DNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|.
gi 2023156726  418 LLLKHGASIQA 428
Cdd:pfam12796   79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
305-396 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 2023156726  305 LHCGARSGHEQVVEMLLDRGAPILSKTKNGLSPLHMATQGDHLNCVQLLIQHNVPvdDVTNDYLTALHVAAHCGHYKVAK 384
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 2023156726  385 VLLDKKANPNAK 396
Cdd:pfam12796   79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
503-593 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 2023156726  503 LHISARLGKADIVQQLLQQGASPNAATTSGYTPLHLSAREGHEDVASVLLDHGASLsiITKKGFTPLHVAAKYGKIEVAN 582
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN--LKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|.
gi 2023156726  583 LLLQKNASPDA 593
Cdd:pfam12796   79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
239-330 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 2023156726  239 LHIAAHYGNINVATLLLNRGAAVDFTARNDITPLHVASKRGNANMVKLLLDRgAKIDAKTrDGLTPLHCGARSGHEQVVE 318
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 2023156726  319 MLLDRGAPILSK 330
Cdd:pfam12796   79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
404-495 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 2023156726  404 LHIACKKNRIKVMELLLKHGASIQAVTESGLTPIHVAAFMGHVNIVSQLMHHGASPNTTNvrGETALHMAARAGQTEVVR 483
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN--GRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 2023156726  484 YLVQNGAQVEAK 495
Cdd:pfam12796   79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
206-297 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 2023156726  206 LHIAARKDDTKAAALLLQNDHNADVESKSGFTPLHIAAHYGNINVATLLLNRGAAVDFTarNDITPLHVASKRGNANMVK 285
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD--NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 2023156726  286 LLLDRGAKIDAK 297
Cdd:pfam12796   79 LLLEKGADINVK 90
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 387-671 5.31e-21

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 99.95  E-value: 5.31e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  387 LDKKAN-PNAKALNGFTPLHIACKKNRIKVMELLLKHGASIQAVTESGLTPIHVAAFMGHVNIVSQLMhhgASPNTTNV- 464
Cdd:PHA02878    23 IDHTENySTSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMI---RSINKCSVf 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  465 RGETALHMAARAGQTEVVRYLVQNGAQVEAKAKDDQTPLHISARLGKADIVQQLLQQGASPNAATT-SGYTPLHLSAREG 543
Cdd:PHA02878   100 YTLVAIKDAFNNRNVEIFKIILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDRhKGNTALHYATENK 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  544 HEDVASVLLDHGASLSIITKKGFTPLHVAAKYGKIEVANLLLQKNASPDASGKSGLTPLHVAAHY-DNQKVALLLLDQGA 622
Cdd:PHA02878   180 DQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGV 259

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 2023156726  623 SPHA-SAKNGYTPLHIAAKKNQmdIATTLLEYGADANAVTRQGIAPVHLA 671
Cdd:PHA02878   260 DVNAkSYILGLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPLSSA 307
Ank_2 pfam12796
Ankyrin repeats (3 copies);
437-527 6.05e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.18  E-value: 6.05e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  437 IHVAAFMGHVNIVSQLMHHGASPNTTNVRGETALHMAARAGQTEVVRYLVQNgAQVEAKAkDDQTPLHISARLGKADIVQ 516
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|.
gi 2023156726  517 QLLQQGASPNA 527
Cdd:pfam12796   79 LLLEKGADINV 89
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 52-292 7.43e-21

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 98.91  E-value: 7.43e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726   52 GNLEKALDYLKSGVDINISNQNGLNALHLASKEGHVEVVSELIQRGASVDAATKKGNTALHIASLAGQAEVVKVLVTNRA 131
Cdd:PHA02875    13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  132 NVN-AQSQNGFTPLYMAAQENHLEVVKFLLDNGASQSLATEDGFTPlavalqqghdqvvslllendtkgkvrlpaLHIAA 210
Cdd:PHA02875    93 FADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSP-----------------------------LHLAV 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  211 RKDDTKAAALLLQNDHNADVESKSGFTPLHIAAHYGNINVATLLLNRGAAVDFTARN-DITPLHVASKRGNANMVKLLLD 289
Cdd:PHA02875   144 MMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNgCVAALCYAIENNKIDIVRLFIK 223


                   ...
gi 2023156726  290 RGA 292
Cdd:PHA02875   224 RGA 226
Ank_2 pfam12796
Ankyrin repeats (3 copies);
111-198 7.64e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.79  E-value: 7.64e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  111 LHIASLAGQAEVVKVLVTNRANVNAQSQNGFTPLYMAAQENHLEVVKFLLDNGASQSlaTEDGFTPLAVALQQGHDQVVS 190
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78


                   ....*...
gi 2023156726  191 LLLENDTK 198
Cdd:pfam12796   79 LLLEKGAD 86
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 47-356 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 2023156726   47 RAARAGNLEKALDYLKSGVDINISNQNGLNALHLASKE----GHVEVVSELIQRgaSVDAATKKGNTALHIASLagqaEV 122
Cdd:PHA02878    43 QAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEpnklGMKEMIRSINKC--SVFYTLVAIKDAFNNRNV----EI 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  123 VKVLVTNRANVNAQSQNGFTPLYMAAQENHLEVVKFLLDNGASQSLATEDgftplavalqqghdqvvslllendtKGKVr 202
Cdd:PHA02878   117 FKIILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDRH-------------------------KGNT- 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  203 lpALHIAARKDDTKAAALLLQNDHNADVESKSGFTPLHIAAHYGNINVATLLLNRGAAVDFTARNDITPLHVASKR-GNA 281
Cdd:PHA02878   171 --ALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDY 248

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2023156726  282 NMVKLLLDRGAKIDAK-TRDGLTPLHCGARSghEQVVEMLLDRGAPILSKTKNGLSPLHMAT-QGDHLNCVQLLIQH 356
Cdd:PHA02878   249 DILKLLLEHGVDVNAKsYILGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAVkQYLCINIGRILISN 323
Ank_2 pfam12796
Ankyrin repeats (3 copies);
669-759 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 2023156726  669 HLASQDGHVDMVSLLLTRNANVNLGNKSGLTPLHLAAQDDRVNVAEVLVNQgAAVDAQTKmGYTPLHVGCHYGNIKIVNF 748
Cdd:pfam12796    2 HLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKL 79

                           90
                   ....*....|.
gi 2023156726  749 LLQHSAKVNAK 759
Cdd:pfam12796   80 LLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
569-659 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 2023156726  569 LHVAAKYGKIEVANLLLQKNASPDASGKSGLTPLHVAAHYDNQKVALLLLDQGASphASAKNGYTPLHIAAKKNQMDIAT 648
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|.
gi 2023156726  649 TLLEYGADANA 659
Cdd:pfam12796   79 LLLEKGADINV 89
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 61-277 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 2023156726   61 LKSGVDINISNQNGLNALHLASKEGHVEVVSELIQRGASVDAATKKGNTALHIASLAGQAEVVKVLVTNRANVNAQSQNG 140
Cdd:PHA02874   111 LDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNG 190

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  141 FTPLYMAAQENHLEVVKFLLDNGASQSLATEDGFTPLAVALqqghdqvvslllendtkgkvrlpaLHiaarkddTKAAAL 220
Cdd:PHA02874   191 ESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI------------------------IH-------NRSAIE 239

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2023156726  221 LLQNDHNADVESKSGFTPLHIAAHYG-NINVATLLLNRGAAVDFTARNDITPLHVASK 277
Cdd:PHA02874   240 LLINNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAFK 297
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 41-305 2.70e-20

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 97.34  E-value: 2.70e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726   41 TNASYLRAARAGNLEKALDYLKSGVDINISNQNGLNALHLASKEGHVEVVSELIQRGasVDAATkkgntaLHIASLagQA 120
Cdd:PHA02874    35 TTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG--VDTSI------LPIPCI--EK 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  121 EVVKVLVTNRANVNAQSQNGFTPLYMAAQENHLEVVKFLLDNGASQSLATEDGFTPLAVALQQGHDQVVSLLLENDTKGK 200
Cdd:PHA02874   105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  201 VR----LPALHIAARKDDTKAAALLLQNDHNADVESKSGFTPLHIAAHYgNINVATLLLNrGAAVDFTARNDITPLHVA- 275
Cdd:PHA02874   185 VKdnngESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIH-NRSAIELLIN-NASINDQDIDGSTPLHHAi 262

                          250       260       270
                   ....*....|....*....|....*....|
gi 2023156726  276 SKRGNANMVKLLLDRGAKIDAKTRDGLTPL 305
Cdd:PHA02874   263 NPPCDIDIIDILLYHKADISIKDNKGENPI 292
Death cd01670
Death Domain: a protein-protein interaction domain; Death Domains (DDs) are protein-protein ...
 4070-4144 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 2023156726 4070 VADHLGLSWTELARELNFSVDEINQIRVENPNSLIAQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIVTLLE 4144
Cdd:cd01670      5 VAEELGRDWKKLARKLGLSEGDIDQIEEDNRDDLKEQAYQMLERWREREGDEATLGRLIQALREIGRRDLAEKLE 79
Ank_2 pfam12796
Ankyrin repeats (3 copies);
701-790 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 2023156726  701 LHLAAQDDRVNVAEVLVNQGAAVDAQTKMGYTPLHVGCHYGNIKIVNFLLQHsAKVNAKTkNGYTPLHQAAQQGHTHIIN 780
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|
gi 2023156726  781 VLLQHGAAPN 790
Cdd:pfam12796   79 LLLEKGADIN 88
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 499-740 3.23e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 93.90  E-value: 3.23e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  499 DQTPLHISARLGKADIVQQLLQQGASPNAATTSGYTPLHLSAREGHEDVASVLLDHGASLSIITKKGFTPLHVAAKYGKI 578
Cdd:PHA02875     2 DQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDV 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  579 EVANLLLQKNA-SPDASGKSGLTPLHVAAHYDNQKVALLLLDQGASPHASAKNGYTPLHIAAKKNQMDIATTLLEYGADA 657
Cdd:PHA02875    82 KAVEELLDLGKfADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACL 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  658 NAVTRQGIAPVHLASQDGHVDMVSLLLTRNANVNLGNKSG-LTPLHLAAQDDRVNVAEVLVNQGAAVDAQTK-MG--YTP 733
Cdd:PHA02875   162 DIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNIMFMiEGeeCTI 241


                   ....*..
gi 2023156726  734 LHVGCHY 740
Cdd:PHA02875   242 LDMICNM 248
Ank_2 pfam12796
Ankyrin repeats (3 copies);
635-726 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 2023156726  635 LHIAAKKNQMDIATTLLEYGADANAVTRQGIAPVHLASQDGHVDMVSLLLtRNANVNLGNKsGLTPLHLAAQDDRVNVAE 714
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDN-GRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 2023156726  715 VLVNQGAAVDAQ 726
Cdd:pfam12796   79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
47-136 5.16e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.78  E-value: 5.16e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726   47 RAARAGNLEKALDYLKSGVDINISNQNGLNALHLASKEGHVEVVSELIQRgASVDAATkKGNTALHIASLAGQAEVVKVL 126
Cdd:pfam12796    3 LAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLL 80

                           90
                   ....*....|
gi 2023156726  127 VTNRANVNAQ 136
Cdd:pfam12796   81 LEKGADINVK 90
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 67-429 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 2023156726   67 INISNQNGLNALHLASKEGHVEVVSELIQRGASVdaatkkgntalhiaslagqaevvkvlvtNRANVNAQSqngftPLYM 146
Cdd:PHA02874    28 INISVDETTTPLIDAIRSGDAKIVELFIKHGADI----------------------------NHINTKIPH-----PLLT 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  147 AAQENHLEVVKFLLDNGASQSLatedgftplaVALQQGHDQVVSLLLENDTKGKVRlpalhiaarkddtkaaalllqndh 226
Cdd:PHA02874    75 AIKIGAHDIIKLLIDNGVDTSI----------LPIPCIEKDMIKTILDCGIDVNIK------------------------ 120

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  227 naDVESKsgfTPLHIAAHYGNINVATLLLNRGAAVDFTARNDITPLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPLH 306
Cdd:PHA02874   121 --DAELK---TFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLH 195

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  307 CGARSGHEQVVEMLLDRGAPILSKTKNGLSPLHMATQGDHlNCVQLLIqHNVPVDDVTNDYLTALHVAAH--CGhYKVAK 384
Cdd:PHA02874   196 NAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLI-NNASINDQDIDGSTPLHHAINppCD-IDIID 272

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 2023156726  385 VLLDKKANPNAKALNGFTPLHIACKK-NRIKVMELLLKHGASIQAV 429
Cdd:PHA02874   273 ILLYHKADISIKDNKGENPIDTAFKYiNKDPVIKDIIANAVLIKEA 318
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 434-704 9.06e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 93.02  E-value: 9.06e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  434 LTPIHVAAFMGHVNIVSQLMHHGASPNTTNVRGETALHMAARA----GQTEVVRYLVQNGAQVEAKAKDDqtplhiSARL 509
Cdd:PHA02878    38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEpnklGMKEMIRSINKCSVFYTLVAIKD------AFNN 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  510 GKADIVQQLLQQGASPNAATTSGYTPLHLSAREGHEDVASVLLDHGASLSIITK-KGFTPLHVAAKYGKIEVANLLLQKN 588
Cdd:PHA02878   112 RNVEIFKIILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYG 191

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  589 ASPDASGKSGLTPLHVAAHYDNQKVALLLLDQGASPHASAKNGYTPLHIAAKK-NQMDIATTLLEYGADANA-VTRQGIA 666
Cdd:PHA02878   192 ANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAkSYILGLT 271

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 2023156726  667 PVHLASQDGhvDMVSLLLTRNANVNLGNKSGLTPLHLA 704
Cdd:PHA02878   272 ALHSSIKSE--RKLKLLLEYGADINSLNSYKLTPLSSA 307
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 470-764 1.86e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 92.25  E-value: 1.86e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  470 LHMAARAGQTEVVRYLVQNGAQVEAKAKDDQTPLHISA----RLGKADIVQQLLQQGAspnaattsGYTPLHLSAREGHE 545
Cdd:PHA02878    41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICkepnKLGMKEMIRSINKCSV--------FYTLVAIKDAFNNR 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  546 DV---ASVLLDHGASLSIITKKgftPLHVAAKYGKIE--VANLLLQKNASPDASGK-SGLTPLHVAAHYDNQKVALLLLD 619
Cdd:PHA02878   113 NVeifKIILTNRYKNIQTIDLV---YIDKKSKDDIIEaeITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLS 189

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  620 QGASPHASAKNGYTPLHIAAKKNQMDIATTLLEYGADANAVTRQGIAPVHLASqdGHV---DMVSLLLTRNANVNLgnKS 696
Cdd:PHA02878   190 YGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISV--GYCkdyDILKLLLEHGVDVNA--KS 265

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2023156726  697 ---GLTPLHLAAQDDRvnVAEVLVNQGAAVDAQTKMGYTPLHV------GCHYGNIKIVNFLLQHSAKVNAKTKNGY 764
Cdd:PHA02878   266 yilGLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPLSSavkqylCINIGRILISNICLLKRIKPDIKNSEGF 340
Death pfam00531
Death domain;
4066-4144 8.90e-17

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 78.18  E-value: 8.90e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726 4066 RMAIVADH---LGLSWTELARELNFSVDEINQIRVENPNsLIAQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIVTL 4142
Cdd:pfam00531    3 QLDRLLDPpppLGKDWRELARKLGLSENEIDEIESENPR-LRSQTYELLRLWEQREGKNATVGTLLEALRKLGRRDAAEK 81


                   ..
gi 2023156726 4143 LE 4144
Cdd:pfam00531   82 IQ 83
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 566-805 9.75e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 86.86  E-value: 9.75e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  566 FTPLHVAAKYGKIEVANLLLQKNASPDASGKSGLTPLHVAAHYDNQkvalllldQGASPHASAKN----GYTPLHI--AA 639
Cdd:PHA02878    38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNK--------LGMKEMIRSINkcsvFYTLVAIkdAF 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  640 KKNQMDIATTLLEYGADANavtrQGIAPVHL--ASQDGHVD--MVSLLLTRNANVNLGNK-SGLTPLHLAAQDDRVNVAE 714
Cdd:PHA02878   110 NNRNVEIFKIILTNRYKNI----QTIDLVYIdkKSKDDIIEaeITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTE 185

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  715 VLVNQGAAVDAQTKMGYTPLHVGCHYGNIKIVNFLLQHSAKVNAKTKNGYTPLHQAAQQGHTH-IINVLLQHGAAPN-EL 792
Cdd:PHA02878   186 LLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDYdILKLLLEHGVDVNaKS 265

                          250
                   ....*....|...
gi 2023156726  793 TVNGNTALAIAKR 805
Cdd:PHA02878   266 YILGLTALHSSIK 278
Ank_2 pfam12796
Ankyrin repeats (3 copies);
734-815 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 2023156726  734 LHVGCHYGNIKIVNFLLQHSAKVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAApnELTVNGNTALAIAKRLGYISVVD 813
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78


                   ..
gi 2023156726  814 TL 815
Cdd:pfam12796   79 LL 80
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 44-362 3.63e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 82.80  E-value: 3.63e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726   44 SYLRAARAGNLEKALDYLKSGVDINISNQNGLNALHLASKEGHV-EVVSELIQRGASVDAATKKGNTALHIASLAG-QAE 121
Cdd:PHA02876   243 SLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAKNGyDTE 322

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  122 VVKVLVTNRANVNAQSQNGFTPLYMAAqenhlevvkflldngasqslatedgftplavALQQGHDQVVSLLlendtkgkv 201
Cdd:PHA02876   323 NIRTLIMLGADVNAADRLYITPLHQAS-------------------------------TLDRNKDIVITLL--------- 362

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  202 rlpalhiaarkddtkaaalllqnDHNADVESKSGF--TPLHIAAHYGNINVATLLLNRGAAVDFTARNDITPLHVASKRG 279
Cdd:PHA02876   363 -----------------------ELGANVNARDYCdkTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGT 419

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  280 NANM-VKLLLDRGAKIDAKTRDGLTPLHCGARSGHE-QVVEMLLDRGAPILSKTKNGLSPLHMATQgdHLNCVQLLIQHN 357
Cdd:PHA02876   420 NPYMsVKTLIDRGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAINIQNQYPLLIALE--YHGIVNILLHYG 497


                   ....*
gi 2023156726  358 VPVDD 362
Cdd:PHA02876   498 AELRD 502
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 374-586 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 2023156726  374 AAHCGHYKVAKVLLD--KKANPNAKALNGFTPLHIACKKNRIK-VMELLLKHGASIqavtESGLTPIHVAAfMGHVNIVS 450
Cdd:TIGR00870   24 AAERGDLASVYRDLEepKKLNINCPDRLGRSALFVAAIENENLeLTELLLNLSCRG----AVGDTLLHAIS-LEYVDAVE 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  451 QLM-----HHGASPNTTNV---------RGETALHMAARAGQTEVVRYLVQNGAQVEAKAKDD--------------QTP 502
Cdd:TIGR00870   99 AILlhllaAFRKSGPLELAndqytseftPGITALHLAAHRQNYEIVKLLLERGASVPARACGDffvksqgvdsfyhgESP 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  503 LHISARLGKADIVQQLLQQGASPNAATTSGYTPLHLSAREGHEDVA---------SVLLDHGA------SLSIITK-KGF 566
Cdd:TIGR00870  179 LNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVMENEFKAEyeelscqmyNFALSLLDklrdskELEVILNhQGL 258

                          250       260
                   ....*....|....*....|
gi 2023156726  567 TPLHVAAKYGKIEVANLLLQ 586
Cdd:TIGR00870  259 TPLKLAAKEGRIVLFRLKLA 278
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 642-815 1.29e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 79.65  E-value: 1.29e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  642 NQMDIATTLLEYGADANAVTRQGIAPVHLASQDGHVDMVSLLLTRNANVNLGNKSGLTPLHLAAQDDRVNVAEVLVNQGA 721
Cdd:PHA02875    13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  722 -AVDAQTKMGYTPLHVGCHYGNIKIVNFLLQHSAKVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAAPNELTVNGNTAL 800
Cdd:PHA02875    93 fADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPL 172

                          170
                   ....*....|....*
gi 2023156726  801 AIAKRLGYISVVDTL 815
Cdd:PHA02875   173 IIAMAKGDIAICKML 187
PHA02798 PHA02798
ankyrin-like protein; Provisional
 69-389 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 2023156726   69 ISNQNGLNALHLASKEGHVEVVSELIQRGASVDAATKKGNTAL-----HIASLAGQAEVVKVLVTNRANVNAQSQNGFTP 143
Cdd:PHA02798    33 IVNEYSIFQKYLQRDSPSTDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETP 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  144 LYMAAQE---NHLEVVKFLLDNGASQSLATEDGFTPLAVALQQGHD---QVVSLLLEndtKGkvrlpaLHIaarkddtka 217
Cdd:PHA02798   113 LYCLLSNgyiNNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLE---KG------VDI--------- 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  218 aalllqNDHNadveSKSGFTPLHIAAHYG----NINVATLLLNRGAAVD----FTARNDI---TPLHVASKRGNANMVKL 286
Cdd:PHA02798   175 ------NTHN----NKEKYDTLHCYFKYNidriDADILKLFVDNGFIINkenkSHKKKFMeylNSLLYDNKRFKKNILDF 244

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  287 LLdrgAKIDAKTRD--GLTPLHCGARSGHEQVVEMLLDRGAPILSKTKNGLSPLHMATQGDHLNCVQLLIQHNVPVDDVT 364
Cdd:PHA02798   245 IF---SYIDINQVDelGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKPNKNTIS 321

                          330       340
                   ....*....|....*....|....*
gi 2023156726  365 NDYltalhvaahcghYKVAKVLLDK 389
Cdd:PHA02798   322 YTY------------YKLRKHILNV 334
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 567-751 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 2023156726  567 TPLHVAAKYGKIE-VANLLLQKNASPDASGKSGLTPLHVAAHYDNQKVALLLLDqgASPH-------ASAKNGYTPLHIA 638
Cdd:cd22192     19 SPLLLAAKENDVQaIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPElvnepmtSDLYQGETALHIA 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  639 AKKNQMDIATTLLEYGADANAVTRQGIA--------------PVHLASQDGHVDMVSLLLTRNANVNLGNKSGLTPLH-L 703
Cdd:cd22192     97 VVNQNLNLVRELIARGADVVSPRATGTFfrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHiL 176

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2023156726  704 AAQDDRVNVAEV---LVNQGAAVDAQT------KMGYTPLHVGCHYGNIKIVNFLLQ 751
Cdd:cd22192    177 VLQPNKTFACQMydlILSYDKEDDLQPldlvpnNQGLTPFKLAAKEGNIVMFQHLVQ 233
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 507-694 6.30e-14

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 78.76  E-value: 6.30e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  507 ARLGKADIVQQLLQQGASPNAATTSGYTPLHLSAREGHEDVASVLLDHGASLSIITKKGFTPLHVAAKYGKIEVANLLLQ 586
Cdd:PLN03192   533 ASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYH 612

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  587 KNASPDasgksgltplhvaahydnqkvalllldqgasPHASAKngytPLHIAAKKNQMDIATTLLEYGADANAVTRQGIA 666
Cdd:PLN03192   613 FASISD-------------------------------PHAAGD----LLCTAAKRNDLTAMKELLKQGLNVDSEDHQGAT 657

                          170       180
                   ....*....|....*....|....*...
gi 2023156726  667 PVHLASQDGHVDMVSLLLTRNANVNLGN 694
Cdd:PLN03192   658 ALQVAMAEDHVDMVRLLIMNGADVDKAN 685
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 48-194 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 2023156726   48 AARAGNLEKALDYLKSGVDIN-ISNQNGLNALHLASKEGHVEVVSELIQRGASVDAATKKGNTALHIASLAGQAEVVKVL 126
Cdd:PHA02875    75 AVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELL 154

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2023156726  127 VTNRANVNAQSQNGFTPLYMAAQENHLEVVKFLLDNGASQSLATEDG-FTPLAVALQQGHDQVVSLLLE 194
Cdd:PHA02875   155 IDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIK 223
PHA02946 PHA02946
ankyin-like protein; Provisional
 584-795 3.21e-13

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 75.48  E-value: 3.21e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  584 LLQKNASPDASGKSGLTPLHVAAHYDNQKVALLLLDQGASPHASAKNGYTPLHIAAKKNQ--MDIATTLLEYGADA-NAV 660
Cdd:PHA02946    58 LLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKInNSV 137

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  661 TRQGIAPVhLASQDGHVDMVSLLLTRNANVNLGNKSGLTPL--HLAAQDDRVNVAEVLVNQGAAVDAQTKMGYTPLHVGC 738
Cdd:PHA02946   138 DEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFGKNHIhrHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVC 216

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  739 H--YGNIKIVNFLLQhSAKVNAKTKNGYTPLHQAAQQ-GHTHIINVLLQHGAAPNELTVN 795
Cdd:PHA02946   217 SktVKNVDIINLLLP-STDVNKQNKFGDSPLTLLIKTlSPAHLINKLLSTSNVITDQTVN 275
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 142-355 5.47e-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: 5.47e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  142 TPLYMAAQENHLEVVKFLLDNgasqslATEDGFTplavalqqghdqvvslllendtKGKVRLPALHIAARKDDTKAAALL 221
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLLKC------PSCDLFQ----------------------RGALGETALHVAALYDNLEAAVVL 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  222 LQNDH---NADVESK--SGFTPLHIAAHYGNINVATLLLNRGAAVdFTARNDIT---------------PLHVASKRGNA 281
Cdd:cd22192     71 MEAAPelvNEPMTSDlyQGETALHIAVVNQNLNLVRELIARGADV-VSPRATGTffrpgpknliyygehPLSFAACVGNE 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  282 NMVKLLLDRGAKIDAKTRDGLTPLH-----------CgarsgheQVVEMLL-----DRGAPiLSKTKN--GLSPLHMATQ 343
Cdd:cd22192    150 EIVRLLIEHGADIRAQDSLGNTVLHilvlqpnktfaC-------QMYDLILsydkeDDLQP-LDLVPNnqGLTPFKLAAK 221

                          250
                   ....*....|..
gi 2023156726  344 GDHLNCVQLLIQ 355
Cdd:cd22192    222 EGNIVMFQHLVQ 233
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 463-587 6.69e-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: 6.69e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  463 NVRGETALHMAARAGQTEVVRYLVQNGAQVEAKAKDD--------------QTPLHISARLGKADIVQQLLQQGASPNAA 528
Cdd:cd22194    138 AYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVffnpkykhegfyfgETPLALAACTNQPEIVQLLMEKESTDITS 217

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2023156726  529 TTS-GYTPLH---LSAREGHEDVASV-------LLDH-GASLSIIT-KKGFTPLHVAAKYGKIEVANLLLQK 587
Cdd:cd22194    218 QDSrGNTVLHalvTVAEDSKTQNDFVkrmydmiLLKSeNKNLETIRnNEGLTPLQLAAKMGKAEILKYILSR 289
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 369-587 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 2023156726  369 TALHVAAHCGHYKVAKVLLDKKA----NPNAKAL-NGFTPLHIACKKNRIKVMELLLKHGASIQAVTESGLtpihvaAFm 443
Cdd:cd22192     53 TALHVAALYDNLEAAVVLMEAAPelvnEPMTSDLyQGETALHIAVVNQNLNLVRELIARGADVVSPRATGT------FF- 125

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  444 ghvnivsqlmhhgaSPNTTNV--RGETALHMAARAGQTEVVRYLVQNGAQVEAKAKDDQTPLHISARLGKADIVQQLLQQ 521
Cdd:cd22192    126 --------------RPGPKNLiyYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFACQMYDL 191

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2023156726  522 gaspnaattsgytplhLSAREGHEDVASvlLDHgaslsIITKKGFTPLHVAAKYGKIEVANLLLQK 587
Cdd:cd22192    192 ----------------ILSYDKEDDLQP--LDL-----VPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 501-718 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 2023156726  501 TPLHISARLGKADIVQQLL-QQGASPNAATTSGYTPLHLSAREGHEDVASVLLDHGASL--SIITK---KGFTPLHVAAK 574
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELvnEPMTSdlyQGETALHIAVV 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  575 YGKIEVANLLLQKNA---SPDASG------KSGLT-----PLHVAAHYDNQKVALLLLDQGASPHASAKNGYTPLHIAAK 640
Cdd:cd22192     99 NQNLNLVRELIARGAdvvSPRATGtffrpgPKNLIyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVL 178

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2023156726  641 KNQMDIATTLLEYgadanavtrqgiapvhLASQDGHVDMVSLLLTRnanvnlgNKSGLTPLHLAAQDDRVNVAEVLVN 718
Cdd:cd22192    179 QPNKTFACQMYDL----------------ILSYDKEDDLQPLDLVP-------NNQGLTPFKLAAKEGNIVMFQHLVQ 233
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 640-815 2.12e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 73.56  E-value: 2.12e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  640 KKNQMDIATTLLEYGADANAVTRQGIAPVHLASQDGHVDMVSLLLTRNANVNLGNKSGLTPLHLAAQ-----------DD 708
Cdd:PHA02876   154 QQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDsknidtikaiiDN 233

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  709 RVNVAE------------------VLVNQGAAVDAQTKMGYTPLHVGCHYGNI-KIVNFLLQHSAKVNAKTKNGYTPLHQ 769
Cdd:PHA02876   234 RSNINKndlsllkairnedletslLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYL 313

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2023156726  770 AAQQGH-THIINVLLQHGAAPNELTVNGNTALAIAKRLG-YISVVDTL 815
Cdd:PHA02876   314 MAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITL 361
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 98-257 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 2023156726   98 ASVDAATKKGNTALHIASLAGQAEVVKVLVTNRANVNAQSQNGF--------------TPLYMAAQENHLEVVKFLLDNG 163
Cdd:cd22194    132 AEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVFfnpkykhegfyfgeTPLALAACTNQPEIVQLLMEKE 211

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  164 asqslatedgftPLAVALQqghdqvvslllenDTKGKVRLPALHIAArkDDTKAAA--------LLLQNDHNADVE---S 232
Cdd:cd22194    212 ------------STDITSQ-------------DSRGNTVLHALVTVA--EDSKTQNdfvkrmydMILLKSENKNLEtirN 264

                          170       180
                   ....*....|....*....|....*
gi 2023156726  233 KSGFTPLHIAAHYGNINVATLLLNR 257
Cdd:cd22194    265 NEGLTPLQLAAKMGKAEILKYILSR 289
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 43-195 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 2023156726   43 ASYLRAARAGNLEKALDYLKSGVDINISNQNGLNALHLASKEGHVEVVSELIQRGASVDAATKKGNTALHIASLAGQAEV 122
Cdd:PLN03192   527 SNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKI 606

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2023156726  123 VKVLVTNRANVNAQSqnGFTPLYMAAQENHLEVVKFLLDNGASQSLATEDGFTPLAVALQQGHDQVVSLLLEN 195
Cdd:PLN03192   607 FRILYHFASISDPHA--AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMN 677
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 369-590 1.94e-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: 1.94e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  369 TALHVAA---HCGHYKVAKVLLD---KKANP----NAKALN----GFTPLHIACKKNRIKVMELLLKHGASIQAVTESgl 434
Cdd:cd21882     28 TCLHKAAlnlNDGVNEAIMLLLEaapDSGNPkelvNAPCTDefyqGQTALHIAIENRNLNLVRLLVENGADVSARATG-- 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  435 tpihvAAFMGHvnivsqlmhhgasPNTTNVRGETALHMAARAGQTEVVRYLVQNGAQVEAKAKDD---QTPLHIsarlgk 511
Cdd:cd21882    106 -----RFFRKS-------------PGNLFYFGELPLSLAACTNQEEIVRLLLENGAQPAALEAQDslgNTVLHA------ 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  512 adIVQQLLQQGASPNAATTSGYTPLHLSAReghedvasvlLDHGASLSIIT-KKGFTPLHVAAKYGKIEVANLLLQKNAS 590
Cdd:cd21882    162 --LVLQADNTPENSAFVCQMYNLLLSYGAH----------LDPTQQLEEIPnHQGLTPLKLAAVEGKIVMFQHILQREFS 229
PHA03095 PHA03095
ankyrin-like protein; Provisional
 705-802 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 2023156726  705 AQDDRVNVAEV--LVNQGAAVDAQTKMGYTPLHVGCHYGN---IKIVNFLLQHSAKVNAKTKNGYTPLHQAAQQGHT-HI 778
Cdd:PHA03095    20 LNASNVTVEEVrrLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDV 99

                           90       100
                   ....*....|....*....|....
gi 2023156726  779 INVLLQHGAAPNELTVNGNTALAI 802
Cdd:PHA03095   100 IKLLIKAGADVNAKDKVGRTPLHV 123
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 416-569 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 2023156726  416 MELLLKHGASIQAVTESGLTPIHVAAFMGHVNIVSQLMHHGASPNTTNVRGETALHMAARAGQTEVVRYLVQNGAQVEAK 495
Cdd:PLN03192   541 LEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPH 620

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2023156726  496 AKDDQtpLHISARLGKADIVQQLLQQGASPNAATTSGYTPLHLSAREGHEDVASVLLDHGASLSII-TKKGFTPL 569
Cdd:PLN03192   621 AAGDL--LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAnTDDDFSPT 693
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 716-815 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 2023156726  716 LVNQGAAVDAQTKMGYTPLHVGCHYGNIKIVNFLLQHSAKVNAKTKNGYTPLHQAAQQGH--TH---IINVLLQHGAAPN 790
Cdd:PHA03100    21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnlTDvkeIVKLLLEYGANVN 100

                           90       100
                   ....*....|....*....|....*..
gi 2023156726  791 ELTVNGNTALAIA--KRLGYISVVDTL 815
Cdd:PHA03100   101 APDNNGITPLLYAisKKSNSYSIVEYL 127
Ank_4 pfam13637
Ankyrin repeats (many copies);
433-486 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 2023156726  433 GLTPIHVAAFMGHVNIVSQLMHHGASPNTTNVRGETALHMAARAGQTEVVRYLV 486
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
367-420 7.02e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.98  E-value: 7.02e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2023156726  367 YLTALHVAAHCGHYKVAKVLLDKKANPNAKALNGFTPLHIACKKNRIKVMELLL 420
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
270-321 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 2023156726  270 TPLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPLHCGARSGHEQVVEMLL 321
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 78-257 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 2023156726   78 LHLASKEGHVEVVSELI--------QRGASvdaatkkGNTALHIASLAGQAEVVKVLVTNR---ANVNAQSQ--NGFTPL 144
Cdd:cd22192     21 LLLAAKENDVQAIKKLLkcpscdlfQRGAL-------GETALHVAALYDNLEAAVVLMEAApelVNEPMTSDlyQGETAL 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  145 YMAAQENHLEVVKFLLDNGASQSLATEDG--FT------------PLAVALQQGHDQVVSLLLEN--DTKGKVRL--PAL 206
Cdd:cd22192     94 HIAVVNQNLNLVRELIARGADVVSPRATGtfFRpgpknliyygehPLSFAACVGNEEIVRLLIEHgaDIRAQDSLgnTVL 173

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2023156726  207 HIAARKDDTKAAA----LLLQNDHNAD------VESKSGFTPLHIAAHYGNINVATLLLNR 257
Cdd:cd22192    174 HILVLQPNKTFACqmydLILSYDKEDDlqpldlVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
PHA03095 PHA03095
ankyrin-like protein; Provisional
 43-194 1.50e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 66.97  E-value: 1.50e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726   43 ASYLRAARAgNLEkALDYL-KSGVDINISNQNGLNALH--LASKEGHVEVVSELIQRGASVDAATKKGNTALHIASLAGQ 119
Cdd:PHA03095   157 AVLLKSRNA-NVE-LLRLLiDAGADVYAVDDRFRSLLHhhLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSS 234

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2023156726  120 AEVVKV--LVTNRANVNAQSQNGFTPLYMAAQENHLEVVKFLLDNGASQSLATEDGFTPLAVALQQGHDQVVSLLLE 194
Cdd:PHA03095   235 CKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALA 311
PHA02946 PHA02946
ankyin-like protein; Provisional
 449-835 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 2023156726  449 VSQLMHHGASPNTTNVRGETALHMAARAGQTEVVRYLVQNGAQVEAKAKDDQTPLHISARLGKADI--VQQLLQQGAS-P 525
Cdd:PHA02946    55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIerINLLVQYGAKiN 134

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  526 NAATTSGYTPLhLSAREGHEDVASVLLDHGASLSIITkkgftplhvaaKYGKIEVANLLLQKNasPDASGKSGLTPLhva 605
Cdd:PHA02946   135 NSVDEEGCGPL-LACTDPSERVFKKIMSIGFEARIVD-----------KFGKNHIHRHLMSDN--PKASTISWMMKL--- 197

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  606 ahydnqkvalllldqGASPHASAKNGYTPLHIAAKKN--QMDIATTLLEyGADANAVTRQGIAPVHLASQD-GHVDMVSL 682
Cdd:PHA02946   198 ---------------GISPSKPDHDGNTPLHIVCSKTvkNVDIINLLLP-STDVNKQNKFGDSPLTLLIKTlSPAHLINK 261

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  683 LLTrNANVNLGNKSGLTPLHlaaqdDRVNVAEVLVNQGAAVDAqtkmgyTPLHVGCHYGNIKIVNFLLQHSakVNAKTKN 762
Cdd:PHA02946   262 LLS-TSNVITDQTVNICIFY-----DRDDVLEIINDKGKQYDS------TDFKMAVEVGSIRCVKYLLDND--IICEDAM 327

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2023156726  763 GYTPLHQAaqqgHTHIINVLLQHGAApnELTVNGNTALAIAKRLGYISVVDTLKV--VTEETM-TTITVTEKHKMN 835
Cdd:PHA02946   328 YYAVLSEY----ETMVDYLLFNHFSV--DSVVNGHTCMSECVRLNNPVILSKLMLhnPTSETMyLTMKAIEKDKLD 397
PHA02798 PHA02798
ankyrin-like protein; Provisional
 479-781 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 2023156726  479 TEVVRYLVQNGAQVEAKAKDDQTPL-----HISARLGKADIVQQLLQQGASPNAATTSGYTPLHLSAREGH---EDVASV 550
Cdd:PHA02798    51 TDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYinnLEILLF 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  551 LLDHGASLSIITKKGFTPLHVAAKYG---KIEVANLLLQKNASPDA-SGKSGLTPLHVAAHYD----NQKVALLLLDQGA 622
Cdd:PHA02798   131 MIENGADTTLLDKDGFTMLQVYLQSNhhiDIEIIKLLLEKGVDINThNNKEKYDTLHCYFKYNidriDADILKLFVDNGF 210

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  623 SPHASAKngytplhiAAKKNQMDIATTLLEYGADANAvtrqgiapvhlasqdghvDMVSLLLTRnANVNLGNKSGLTPLH 702
Cdd:PHA02798   211 IINKENK--------SHKKKFMEYLNSLLYDNKRFKK------------------NILDFIFSY-IDINQVDELGFNPLY 263

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  703 LAAQDDRVNVAEVLVNQGAAVDAQTKMGYTPLHVGCHYGNIKIVNFLLQHsaKVNAKT-KNGYTPLHQaaqqghtHIINV 781
Cdd:PHA02798   264 YSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNK--KPNKNTiSYTYYKLRK-------HILNV 334
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 309-463 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 2023156726  309 ARSGHEQVVEMLLDRG-APILSKTKnGLSPLHMATQGDHLNCVQLLIQH--NVPVDDVTNDylTALHVAAHCGHYKVAKV 385
Cdd:PLN03192   533 ASTGNAALLEELLKAKlDPDIGDSK-GRTPLHIAASKGYEDCVLVLLKHacNVHIRDANGN--TALWNAISAKHHKIFRI 609

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  386 L--LDKKANPNAkalnGFTPLHIACKKNRIKVMELLLKHGASIQAVTESGLTPIHVAAFMGHVNIVSQLMHHGASPNTTN 463
Cdd:PLN03192   610 LyhFASISDPHA----AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
Ank_4 pfam13637
Ankyrin repeats (many copies);
402-450 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 2023156726  402 TPLHIACKKNRIKVMELLLKHGASIQAVTESGLTPIHVAAFMGHVNIVS 450
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLK 51
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 248-520 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 2023156726  248 INVATLLLNRGAAVDFTAR-NDITPLHVASKRGNANMVKLLLDRGAKIDAKtrdGL--TPLHCGAR------SGHEQVVE 318
Cdd:PHA02989    16 KNALEFLLRTGFDVNEEYRgNSILLLYLKRKDVKIKIVKLLIDNGADVNYK---GYieTPLCAVLRnreitsNKIKKIVK 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  319 MLLDRGAPILSKTKNGLSPLHMATQGDHLNCV---QLLIQHNVPVDDVTND--------YLTALHVAAHcghykVAKVLL 387
Cdd:PHA02989    93 LLLKFGADINLKTFNGVSPIVCFIYNSNINNCdmlRFLLSKGINVNDVKNSrgynllhmYLESFSVKKD-----VIKILL 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  388 DKKANPNAKA-LNGFTPLHIACKKN----RIKVMELLLKHGASI-------QAVTESGLTPiHVAAFMGHVNIVSQLMHH 455
Cdd:PHA02989   168 SFGVNLFEKTsLYGLTPMNIYLRNDidviSIKVIKYLIKKGVNIetnnngsESVLESFLDN-NKILSKKEFKVLNFILKY 246

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2023156726  456 gASPNTTNVRGETALHMAARAGQTEVVRYLVQNGAQVEAKAKDDQTPLHISARLGKADIVQQLLQ 520
Cdd:PHA02989   247 -IKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNRILQ 310
Ank_4 pfam13637
Ankyrin repeats (many copies);
74-127 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 2023156726   74 GLNALHLASKEGHVEVVSELIQRGASVDAATKKGNTALHIASLAGQAEVVKVLV 127
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
730-783 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 2023156726  730 GYTPLHVGCHYGNIKIVNFLLQHSAKVNAKTKNGYTPLHQAAQQGHTHIINVLL 783
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 239-487 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 2023156726  239 LHIAAHYGNINVATLLLNRGAAVDFTARNDiTPL-------HVASKRGNaNMVKLLLDRGAKIDAKTRDGLTPLHCGARS 311
Cdd:PHA02989    41 LYLKRKDVKIKIVKLLIDNGADVNYKGYIE-TPLcavlrnrEITSNKIK-KIVKLLLKFGADINLKTFNGVSPIVCFIYN 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  312 GHEQVVEML---LDRGAPILS-KTKNGLSPLHMATQGDHLN--CVQLLIQHNVPVDDVTNDY-LTALHV----AAHCGHY 380
Cdd:PHA02989   119 SNINNCDMLrflLSKGINVNDvKNSRGYNLLHMYLESFSVKkdVIKILLSFGVNLFEKTSLYgLTPMNIylrnDIDVISI 198

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  381 KVAKVLLDKKA---NPNA---KALNGFTPLHIACKKNRIKVMELLLKHgASIQAVTESGLTPIHVAAFMGHVNIVSQLMH 454
Cdd:PHA02989   199 KVIKYLIKKGVnieTNNNgseSVLESFLDNNKILSKKEFKVLNFILKY-IKINKKDKKGFNPLLISAKVDNYEAFNYLLK 277

                          250       260       270
                   ....*....|....*....|....*....|...
gi 2023156726  455 HGASPNTTNVRGETALHMAARAGQTEVVRYLVQ 487
Cdd:PHA02989   278 LGDDIYNVSKDGDTVLTYAIKHGNIDMLNRILQ 310
PHA02798 PHA02798
ankyrin-like protein; Provisional
 248-473 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 2023156726  248 INVATLLLNRGAAVDFTARNDITPL-----HVASKRGNANMVKLLLDRGAKIDAKTRDGLTPLHCGARSGHEQVVEMLL- 321
Cdd:PHA02798    51 TDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLf 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  322 --DRGAPILSKTKNGLSPLHMATQGDH---LNCVQLLIQHNVPVDDVTNDY-LTALHV----AAHCGHYKVAKVLLD--- 388
Cdd:PHA02798   131 miENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINTHNNKEkYDTLHCyfkyNIDRIDADILKLFVDngf 210

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  389 --KKANPNAKA--LNGFTPLHIACKKNRIKVMELLLKHgASIQAVTESGLTPIHVAAFMGHVNIVSQLMHHGASPNTTNV 464
Cdd:PHA02798   211 iiNKENKSHKKkfMEYLNSLLYDNKRFKKNILDFIFSY-IDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITE 289


                   ....*....
gi 2023156726  465 RGETALHMA 473
Cdd:PHA02798   290 LGNTCLFTA 298
Ank_4 pfam13637
Ankyrin repeats (many copies);
301-354 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 2023156726  301 GLTPLHCGARSGHEQVVEMLLDRGAPILSKTKNGLSPLHMATQGDHLNCVQLLI 354
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 105-437 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 2023156726  105 KKGNTALH--IASLAGQAEVVKVLVTNRANVNAQSQNGFTPL--YMAAQENHLEVVKFLLDNGASQSLATEDGFTPLAVA 180
Cdd:PHA02716   175 KTGYGILHayLGNMYVDIDILEWLCNNGVNVNLQNNHLITPLhtYLITGNVCASVIKKIIELGGDMDMKCVNGMSPIMTY 254

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  181 LQQG---HDQVVSLLLENDTKGKVR-LPA-LHI---AARKDDTKAAALLLQNDHNADVESKSGFTPLH--IAAHYGNINV 250
Cdd:PHA02716   255 IINIdniNPEITNIYIESLDGNKVKnIPMiLHSyitLARNIDISVVYSFLQPGVKLHYKDSAGRTCLHqyILRHNISTDI 334

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  251 ATLLLNRGAAVDFTARNDITPLHVASKRG--------------NANMVKLLLDRGAKIDAKTRDGLTPLH---CGARS-G 312
Cdd:PHA02716   335 IKLLHEYGNDLNEPDNIGNTVLHTYLSMLsvvnildpetdndiRLDVIQCLISLGADITAVNCLGYTPLTsyiCTAQNyM 414

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  313 HEQVVEMLLDRgaPILSKTKNGLSPlHMATQGDHLNCV--QLLIQHNVPVDDVTNDY----LTALHVAAHCGhykvakvl 386
Cdd:PHA02716   415 YYDIIDCLISD--KVLNMVKHRILQ-DLLIRVDDTPCIihHIIAKYNIPTDLYTDEYepydSTKIHDVYHCA-------- 483

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2023156726  387 LDKKANPNAKALNGFTPLHIA--CKKNRIKVME---LLLKHGASIQAVTESGLTPI 437
Cdd:PHA02716   484 IIERYNNAVCETSGMTPLHVSiiSHTNANIVMDsfvYLLSIQYNINIPTKNGVTPL 539
Ank_4 pfam13637
Ankyrin repeats (many copies);
107-160 7.78e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 57.28  E-value: 7.78e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2023156726  107 GNTALHIASLAGQAEVVKVLVTNRANVNAQSQNGFTPLYMAAQENHLEVVKFLL 160
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 465-587 9.78e-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: 9.78e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  465 RGETALHMAARAGQTEVVRYLVQNGAQVEAKAKDD--------------QTPLHISARLGKADIVQQLLQ---QGASPNA 527
Cdd:cd22193     75 EGQTALHIAIERRQGDIVALLVENGADVHAHAKGRffqpkyqgegfyfgELPLSLAACTNQPDIVQYLLEnehQPADIEA 154

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2023156726  528 ATTSGYTPLHL------SAREGHEDVASV---LLDHGASL-------SIITKKGFTPLHVAAKYGKIEVANLLLQK 587
Cdd:cd22193    155 QDSRGNTVLHAlvtvadNTKENTKFVTRMydmILIRGAKLcptveleEIRNNDGLTPLQLAAKMGKIEILKYILQR 230
Ank_4 pfam13637
Ankyrin repeats (many copies);
631-684 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 2023156726  631 GYTPLHIAAKKNQMDIATTLLEYGADANAVTRQGIAPVHLASQDGHVDMVSLLL 684
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 135-442 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 2023156726  135 AQSQNGFTPlymAAQENHLEVVKFLLDNGASQSLATED--GFTPLAVALQQG-HDQVVSLLLENDTKGKVRLPALHiAAR 211
Cdd:TIGR00870   15 SDEEKAFLP---AAERGDLASVYRDLEEPKKLNINCPDrlGRSALFVAAIENeNLELTELLLNLSCRGAVGDTLLH-AIS 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  212 KDDTKAAALLLQndHNADVESKSGFTPLHIAAHYGninvatlllnrgaavDFTArnDITPLHVASKRGNANMVKLLLDRG 291
Cdd:TIGR00870   91 LEYVDAVEAILL--HLLAAFRKSGPLELANDQYTS---------------EFTP--GITALHLAAHRQNYEIVKLLLERG 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  292 AKIDAKT--------------RDGLTPLHCGARSGHEQVVEMLLDRGAPILSKTKNGLSPLHMAtqgdhlncvqlliqhn 357
Cdd:TIGR00870  152 ASVPARAcgdffvksqgvdsfYHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLL---------------- 215

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  358 VPVDDVTNDYLTalhVAAHCghYKVAKVLLDKKANPNAKAL----NGFTPLHIACKKNRIKVMELLLKHGASIQAVTESG 433
Cdd:TIGR00870  216 VMENEFKAEYEE---LSCQM--YNFALSLLDKLRDSKELEVilnhQGLTPLKLAAKEGRIVLFRLKLAIKYKQKKFVAWP 290


                   ....*....
gi 2023156726  434 LTPIHVAAF 442
Cdd:TIGR00870  291 NGQQLLSLY 299
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 465-590 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 2023156726  465 RGETALHMAARAGQTEVVRYLVQNGAQVEAKAKDD-------------QTPLHISARLGKADIVQQLLQ---QGASPNAA 528
Cdd:cd22197     93 RGHSALHIAIEKRSLQCVKLLVENGADVHARACGRffqkkqgtcfyfgELPLSLAACTKQWDVVNYLLEnphQPASLQAQ 172

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2023156726  529 TTSGYTPLH---LSAREGHEDVASV------LLDHGASL-------SIITKKGFTPLHVAAKYGKIEVANLLLQKNAS 590
Cdd:cd22197    173 DSLGNTVLHalvMIADNSPENSALVikmydgLLQAGARLcptvqleEISNHEGLTPLKLAAKEGKIEIFRHILQREFS 250
Ank_4 pfam13637
Ankyrin repeats (many copies);
334-387 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 2023156726  334 GLSPLHMATQGDHLNCVQLLIQHNVPVDDVTNDYLTALHVAAHCGHYKVAKVLL 387
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 465-587 5.61e-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: 5.61e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  465 RGETALHMAARAGQTEVVRYLVQNGAQVEAKAKDD--------------QTPLHISARLGKADIVQQLLQQGASPN--AA 528
Cdd:cd22196     93 KGQTALHIAIERRNMHLVELLVQNGADVHARASGEffkkkkggpgfyfgELPLSLAACTNQLDIVKFLLENPHSPAdiSA 172

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2023156726  529 TTS-GYTPLHL---SAREGHEDVASV------LLDHGASL-------SIITKKGFTPLHVAAKYGKIEVANLLLQK 587
Cdd:cd22196    173 RDSmGNTVLHAlveVADNTPENTKFVtkmyneILILGAKIrpllkleEITNKKGLTPLKLAAKTGKIGIFAYILGR 248
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 196-340 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 2023156726  196 DTKGKVrlpALHIAARKDDTKAAALLLQNDHNADVESKSGFTPLHIAAHYGNINVATLLLNRGAAVDFTARNDItpLHVA 275
Cdd:PLN03192   555 DSKGRT---PLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAGDL--LCTA 629

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2023156726  276 SKRGNANMVKLLLDRGAKIDAKTRDGLTPLHCGARSGHEQVVEMLLDRGAPIL-SKTKNGLSPLHM 340
Cdd:PLN03192   630 AKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDkANTDDDFSPTEL 695
Ank_5 pfam13857
Ankyrin repeats (many copies);
386-440 8.33e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 54.27  E-value: 8.33e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2023156726  386 LLDKK-ANPNAKALNGFTPLHIACKKNRIKVMELLLKHGASIQAVTESGLTPIHVA 440
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 611-813 8.68e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 61.68  E-value: 8.68e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  611 QKVALLLLDQGASPHASAKNGYTPL-------HIaakkNQMDIATTLLEYGADANAV-TRQGIAPVHLASQDGHV--DMV 680
Cdd:PHA02989    88 KKIVKLLLKFGADINLKTFNGVSPIvcfiynsNI----NNCDMLRFLLSKGINVNDVkNSRGYNLLHMYLESFSVkkDVI 163

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  681 SLLLtrNANVNLGNKS---GLTPLHLAAQDD----RVNVAEVLVNQGAAVDAQTKMGYTPL------HVGCHYGNIKIVN 747
Cdd:PHA02989   164 KILL--SFGVNLFEKTslyGLTPMNIYLRNDidviSIKVIKYLIKKGVNIETNNNGSESVLesfldnNKILSKKEFKVLN 241

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2023156726  748 FLLQHsAKVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAAPNELTVNGNTALAIAKRLGYISVVD 813
Cdd:PHA02989   242 FILKY-IKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLN 306
Ank_5 pfam13857
Ankyrin repeats (many copies);
551-605 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 2023156726  551 LLDHG-ASLSIITKKGFTPLHVAAKYGKIEVANLLLQKNASPDASGKSGLTPLHVA 605
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 504-609 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 2023156726  504 HISARlGKADIVQQLLQQGASPNAATTSGYTPLHLSAREGHEDVASVLLDHGASLSIITKKGFTPLHVAAKYGKIEVANL 583
Cdd:PTZ00322    88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2023156726  584 LLQ---------KNASPDA-SGKSGL---TPLhVAAHYD 609
Cdd:PTZ00322   167 LSRhsqchfelgANAKPDSfTGKPPSledSPI-SSHHPD 204
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 53-135 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 2023156726   53 NLEKALDYL-KSGVDINISNQNGLNALHLASKEGHVEVVSELIQRGASVDAATKKGNTALHIASLAGQAEVVKVLVTNRA 131
Cdd:PHA03100   170 NAKNRVNYLlSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249


                   ....
gi 2023156726  132 NVNA 135
Cdd:PHA03100   250 SIKT 253
Ank_4 pfam13637
Ankyrin repeats (many copies);
598-651 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 2023156726  598 GLTPLHVAAHYDNQKVALLLLDQGASPHASAKNGYTPLHIAAKKNQMDIATTLL 651
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Death_FADD cd08306
Fas-associated Death Domain protein-protein interaction domain; Death domain (DD) found in ...
 4069-4145 2.25e-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: 2.25e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2023156726 4069 IVADHLGLSWTELARELNFSVDEINQIRVENPNSLIAQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIVTLLEG 4145
Cdd:cd08306      7 VICENLGRDWRQLARKLGLSETKIESISEAHPRNLREQVRQSLREWKKIKKAEATVADLIKALRDCQLNLVADLVEK 83
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 553-684 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 2023156726  553 DHGASLSIITKKGFTPLHVAAKYGKIE--VANLL----LQKNASPDASGksgltplhvaahydnqkvALLLLDQGASPHA 626
Cdd:PTZ00322    49 THLEALEATENKDATPDHNLTTEEVIDpvVAHMLtvelCQLAASGDAVG------------------ARILLTGGADPNC 110

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2023156726  627 SAKNGYTPLHIAAKKNQMDIATTLLEYGADANAVTRQGIAPVHLASQDGHVDMVSLLL 684
Cdd:PTZ00322   111 RDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PHA02798 PHA02798
ankyrin-like protein; Provisional
 613-803 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 2023156726  613 VALLLLDQGASPHASAKNGYTPLHIAAKK---NQMDIATTLLEYGADANAVTRQGIAPVHLASQDGH---VDMVSLLLTR 686
Cdd:PHA02798    91 IVKILIENGADINKKNSDGETPLYCLLSNgyiNNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEK 170

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  687 NANVNL-GNKSGLTPLH--LAAQDDR--VNVAEVLVNQGAAV---DAQTKMGYTPLHVGCHYGNIK----IVNFLLQHsA 754
Cdd:PHA02798   171 GVDINThNNKEKYDTLHcyFKYNIDRidADILKLFVDNGFIInkeNKSHKKKFMEYLNSLLYDNKRfkknILDFIFSY-I 249

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 2023156726  755 KVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAAPNELTVNGNTALAIA 803
Cdd:PHA02798   250 DINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTA 298
Death_RAIDD cd08319
Death domain of RIP-associated ICH-1 homologous protein with a death domain; Death domain (DD) ...
 4063-4135 4.04e-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: 4.04e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2023156726 4063 TDIRMAIVADHLGLSWTELARELNFSVDEINQIRVENPNSLIAQSFMLLKKWVTRDGKNATTDALTSVLTKIN 4135
Cdd:cd08319      1 TDRQLNKLAQRLGPEWEQVLLDLGLSKADIYRCKADHPYNVQSQIVEALVKWKQRQGKKATVQSLIQSLKAVE 73
Ank_4 pfam13637
Ankyrin repeats (many copies);
532-585 4.10e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 4.10e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2023156726  532 GYTPLHLSAREGHEDVASVLLDHGASLSIITKKGFTPLHVAAKYGKIEVANLLL 585
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
468-519 4.10e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 4.10e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2023156726  468 TALHMAARAGQTEVVRYLVQNGAQVEAKAKDDQTPLHISARLGKADIVQQLL 519
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
253-306 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 2023156726  253 LLLNRGAAVDFTARNDITPLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPLH 306
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
567-618 4.22e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 4.22e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2023156726  567 TPLHVAAKYGKIEVANLLLQKNASPDASGKSGLTPLHVAAHYDNQKVALLLL 618
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
237-288 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 2023156726  237 TPLHIAAHYGNINVATLLLNRGAAVDFTARNDITPLHVASKRGNANMVKLLL 288
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 471-554 4.40e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 59.53  E-value: 4.40e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  471 HMAArAGQTEVVRYLVQNGAQVEAKAKDDQTPLHISARLGKADIVQQLLQQGASPNAATTSGYTPLHLSAREGHEDVASV 550
Cdd:PTZ00322    88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                   ....
gi 2023156726  551 LLDH 554
Cdd:PTZ00322   167 LSRH 170
Ank_4 pfam13637
Ankyrin repeats (many copies);
202-255 4.61e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 4.61e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2023156726  202 RLPALHIAARKDDTKAAALLLQNDHNADVESKSGFTPLHIAAHYGNINVATLLL 255
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 48-170 4.67e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.85  E-value: 4.67e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726   48 AARAGNLEKALDYLKSGVDINISNQNGLNALHLASKEGHVEVVSELIQRGASVDAATKKGNTALHIASLAGQAEVVKVLV 127
Cdd:PHA02875   109 ATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLL 188

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2023156726  128 TNRANVNAQSQNG-FTPLYMAAQENHLEVVKFLLDNGASQSLAT 170
Cdd:PHA02875   189 DSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNIMF 232
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 647-716 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 2023156726  647 ATTLLEYGADANAVTRQGIAPVHLASQDGHVDMVSLLLTRNANVNLGNKSGLTPLHLAAQDDRVNVAEVL 716
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 356-455 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 2023156726  356 HNVPVDDVTNDYLTAL------HVAAHcGHYKVAKVLLDKKANPNAKALNGFTPLHIACKKNRIKVMELLLKHGASIQAV 429
Cdd:PTZ00322    66 HNLTTEEVIDPVVAHMltvelcQLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLL 144

                           90       100
                   ....*....|....*....|....*.
gi 2023156726  430 TESGLTPIHVAAFMGHVNIVSQLMHH 455
Cdd:PTZ00322   145 DKDGKTPLELAEENGFREVVQLLSRH 170
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 581-783 1.33e-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: 1.33e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  581 ANLLLQKNASpdasgksgLTPLHVAAHY-DNQKVALLLLDQGASPHASAKNGYTPLHIAAKKNQMDIATTLLEYGADA-- 657
Cdd:cd22192      8 LHLLQQKRIS--------ESPLLLAAKEnDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELvn 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  658 NAVTR---QGIAPVHLASQDGHVDMVSLLLTRNANVnlgnksgLTPlhlaaqddRVNVAEVLVNQGAAVdaqtKMGYTPL 734
Cdd:cd22192     80 EPMTSdlyQGETALHIAVVNQNLNLVRELIARGADV-------VSP--------RATGTFFRPGPKNLI----YYGEHPL 140

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2023156726  735 HVGCHYGNIKIVNFLLQHSAKVNAKTKNGYTPLH----QAAQQGHTHIINVLL 783
Cdd:cd22192    141 SFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHilvlQPNKTFACQMYDLIL 193
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 381-692 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 2023156726  381 KVAKVLLDKKANPNAKALNGfTPL-------HIACKKNRiKVMELLLKHGASIQAVTESGLTPIHVAAFMGHVN---IVS 450
Cdd:PHA02989    51 KIVKLLIDNGADVNYKGYIE-TPLcavlrnrEITSNKIK-KIVKLLLKFGADINLKTFNGVSPIVCFIYNSNINncdMLR 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  451 QLMHHGASPNTT-NVRGETALHMAARAG--QTEVVRYLVQNGAQV-EAKAKDDQTPLHISAR----LGKADIVQQLLQQG 522
Cdd:PHA02989   129 FLLSKGINVNDVkNSRGYNLLHMYLESFsvKKDVIKILLSFGVNLfEKTSLYGLTPMNIYLRndidVISIKVIKYLIKKG 208

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  523 ASPNAATtsgytplhlsarEGHEDVASVLLDHGASLSiitKKGFTPLHVAAKYGKIEVANlllqknaspdasgksgltpl 602
Cdd:PHA02989   209 VNIETNN------------NGSESVLESFLDNNKILS---KKEFKVLNFILKYIKINKKD-------------------- 253

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  603 hvaahydnqkvalllldqgasphasaKNGYTPLHIAAKKNQMDIATTLLEYGADANAVTRQGIAPVHLASQDGHVDMVSL 682
Cdd:PHA02989   254 --------------------------KKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNR 307

                          330
                   ....*....|
gi 2023156726  683 LLTRNANVNL 692
Cdd:PHA02989   308 ILQLKPGKYL 317
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 74-184 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 2023156726   74 GLNALHLASKEGHVEVVSELIQRGASVDA--AT----KKGNTAL-----HIASLA---GQAEVVKVLVTNRANVNAQSQN 139
Cdd:cd22192     89 GETALHIAVVNQNLNLVRELIARGADVVSprATgtffRPGPKNLiyygeHPLSFAacvGNEEIVRLLIEHGADIRAQDSL 168

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2023156726  140 GFTPLYM-AAQENHL---EVVKFLLD---NGASQSLAT---EDGFTPLAVALQQG 184
Cdd:cd22192    169 GNTVLHIlVLQPNKTfacQMYDLILSydkEDDLQPLDLvpnNQGLTPFKLAAKEG 223
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 440-594 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 2023156726  440 AAFMGHVNIVSQLMHHGASPNTTNVRGETALHMAARAGQTEVVRYLVQNGAQVEAKAKDDQTPLHiSARLGKADIVQQLL 519
Cdd:PLN03192   532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALW-NAISAKHHKIFRIL 610

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2023156726  520 QQGASPNAATTSGyTPLHLSAREGHEDVASVLLDHGASLSIITKKGFTPLHVAAKYGKIEVANLLLQKNASPDAS 594
Cdd:PLN03192   611 YHFASISDPHAAG-DLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKA 684
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 115-193 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 2023156726  115 SLAGQAEVVKVLVTNRANVNAQSQNGFTPLYMAAQENHLEVVKFLLDNGASQSLATEDGFTPLAVALQQGHDQVVSLLL 193
Cdd:PTZ00322    90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PHA02798 PHA02798
ankyrin-like protein; Provisional
 446-691 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 2023156726  446 VNIVSQLMHHGASPNTTNVRGETAL-----HMAARAGQTEVVRYLVQNGAQVEAKAKDDQTPLHI---SARLGKADIVQQ 517
Cdd:PHA02798    51 TDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCllsNGYINNLEILLF 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  518 LLQQGASPNAATTSGYTPLHLSAREGHE---DVASVLLDHGASLSIITKK-GFTPLHVAAKYG---------KIEVANLL 584
Cdd:PHA02798   131 MIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDINTHNNKeKYDTLHCYFKYNidridadilKLFVDNGF 210

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  585 LQKNAspDASGKSGLTPLHVAAHYDNQKVALLLLD-QGASPHASAKN--GYTPLHIAAKKNQMDIATTLLEYGADANAVT 661
Cdd:PHA02798   211 IINKE--NKSHKKKFMEYLNSLLYDNKRFKKNILDfIFSYIDINQVDelGFNPLYYSVSHNNRKIFEYLLQLGGDINIIT 288

                          250       260       270
                   ....*....|....*....|....*....|
gi 2023156726  662 RQGIAPVHLASQDGHVDMVSLLLTRNANVN 691
Cdd:PHA02798   289 ELGNTCLFTAFENESKFIFNSILNKKPNKN 318
Ank_4 pfam13637
Ankyrin repeats (many copies);
142-193 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 2023156726  142 TPLYMAAQENHLEVVKFLLDNGASQSLATEDGFTPLAVALQQGHDQVVSLLL 193
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 702-796 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 2023156726  702 HLAAQDDRVNvAEVLVNQGAAVDAQTKMGYTPLHVGCHYGNIKIVNFLLQHSAKVNAKTKNGYTPLHQAAQQGHTHIINV 781
Cdd:PTZ00322    88 QLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166

                           90
                   ....*....|....*
gi 2023156726  782 LLQHGAAPNELTVNG 796
Cdd:PTZ00322   167 LSRHSQCHFELGANA 181
Ank_5 pfam13857
Ankyrin repeats (many copies);
617-671 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 2023156726  617 LLDQG-ASPHASAKNGYTPLHIAAKKNQMDIATTLLEYGADANAVTRQGIAPVHLA 671
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
749-803 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 2023156726  749 LLQH-SAKVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAAPNELTVNGNTALAIA 803
Cdd:pfam13857    1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
454-505 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 2023156726  454 HHGASPNTTNVRGETALHMAARAGQTEVVRYLVQNGAQVEAKAKDDQTPLHI 505
Cdd:pfam13857    4 HGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
Ank_5 pfam13857
Ankyrin repeats (many copies);
682-736 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 2023156726  682 LLLTRNANVNLGNKSGLTPLHLAAQDDRVNVAEVLVNQGAAVDAQTKMGYTPLHV 736
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
Ank_4 pfam13637
Ankyrin repeats (many copies);
697-750 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 2023156726  697 GLTPLHLAAQDDRVNVAEVLVNQGAAVDAQTKMGYTPLHVGCHYGNIKIVNFLL 750
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 452-519 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 2023156726  452 LMHHGASPNTTNVRGETALHMAARAGQTEVVRYLVQNGAQVEAKAKDDQTPLHISARLGKADIVQQLL 519
Cdd:PTZ00322   101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 276-356 4.63e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.45  E-value: 4.63e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  276 SKRGNANMVKLLLDRGAKIDAKTRDGLTPLHCGARSGHEQVVEMLLDRGAPILSKTKNGLSPLHMATQGDHLNCVQLLIQ 355
Cdd:PTZ00322    90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169


                   .
gi 2023156726  356 H 356
Cdd:PTZ00322   170 H 170
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 191-295 4.84e-07

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 52.57  E-value: 4.84e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  191 LLLENDTKGKvrlPALHIAARKD--DTKAAALLLQnDHNADV---ESKSGFTPLHIAAHYGNINVATLLLNRgAAVDFTA 265
Cdd:PHA02736    47 LVLEYNRHGK---QCVHIVSNPDkaDPQEKLKLLM-EWGADIngkERVFGNTPLHIAVYTQNYELATWLCNQ-PGVNMEI 121

                           90       100       110
                   ....*....|....*....|....*....|..
gi 2023156726  266 RNDI--TPLHVASKRGNANMVKLLLDRGAKID 295
Cdd:PHA02736   122 LNYAfkTPYYVACERHDAKMMNILRAKGAQCK 153
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 106-257 5.38e-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: 5.38e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  106 KGNTALHIASLAGQAEVVKVLVTNRANVNAQS---------QNGF----TPLYMAAQENHLEVVKFLLDNGASqslated 172
Cdd:cd21882     72 QGQTALHIAIENRNLNLVRLLVENGADVSARAtgrffrkspGNLFyfgeLPLSLAACTNQEEIVRLLLENGAQ------- 144

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  173 gftPLAVALQqghdqvvslllenDTKGKVRLPALHIAARK--DDTKAAA----LLLQNDHNAD-------VESKSGFTPL 239
Cdd:cd21882    145 ---PAALEAQ-------------DSLGNTVLHALVLQADNtpENSAFVCqmynLLLSYGAHLDptqqleeIPNHQGLTPL 208

                          170
                   ....*....|....*...
gi 2023156726  240 HIAAHYGNINVATLLLNR 257
Cdd:cd21882    209 KLAAVEGKIVMFQHILQR 226
Ank_5 pfam13857
Ankyrin repeats (many copies);
583-638 5.46e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 49.27  E-value: 5.46e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2023156726  583 LLLQKNASPDASGKSGLTPLHVAAHYDNQKVALLLLDQGASPHASAKNGYTPLHIA 638
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 588-712 8.11e-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: 8.11e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  588 NASPDASGKSGLTPLHVAAHYDNQKVALLLLDQGASPHASA----------KNGY----TPLHIAAKKNQMDIATTLLE- 652
Cdd:cd22196     84 NAAYTDSYYKGQTALHIAIERRNMHLVELLVQNGADVHARAsgeffkkkkgGPGFyfgeLPLSLAACTNQLDIVKFLLEn 163

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2023156726  653 --YGADANAVTRQGIAPVH--LASQDGHVD-------MVSLLLTRNANVN-------LGNKSGLTPLHLAAQDDRVNV 712
Cdd:cd22196    164 phSPADISARDSMGNTVLHalVEVADNTPEntkfvtkMYNEILILGAKIRpllkleeITNKKGLTPLKLAAKTGKIGI 241
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 44-323 9.01e-07

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 55.30  E-value: 9.01e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726   44 SYLRAARAGNLEKALDYLKSGVDINISNQNGLNALH--LASKEGHVEVVSELIQRGASVDAATKKGNTALHiaSLAGQAE 121
Cdd:PHA02716   287 SYITLARNIDISVVYSFLQPGVKLHYKDSAGRTCLHqyILRHNISTDIIKLLHEYGNDLNEPDNIGNTVLH--TYLSMLS 364

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  122 VVKVLvtnranvNAQSQNGFtplymaaqenHLEVVKFLLDNGASQSLATEDGFTPLA----VALQQGHDQVVSLLLENDT 197
Cdd:PHA02716   365 VVNIL-------DPETDNDI----------RLDVIQCLISLGADITAVNCLGYTPLTsyicTAQNYMYYDIIDCLISDKV 427

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  198 KGKVRLPALH-IAARKDDTKA------AALLLQNDHNADVESKSGFTPLHIAAHYGNINVATlllnrGAAVDFTArndIT 270
Cdd:PHA02716   428 LNMVKHRILQdLLIRVDDTPCiihhiiAKYNIPTDLYTDEYEPYDSTKIHDVYHCAIIERYN-----NAVCETSG---MT 499

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2023156726  271 PLHVA-SKRGNANMV----KLLLDRGAKIDAKTRDGLTPLHCGAR----SGHE-QVVEMLLDR 323
Cdd:PHA02716   500 PLHVSiISHTNANIVmdsfVYLLSIQYNINIPTKNGVTPLMLTMRnnrlSGHQwYIVKNILDK 562
PHA02946 PHA02946
ankyin-like protein; Provisional
 90-362 9.05e-07

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 55.06  E-value: 9.05e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726   90 VSELIQRGASVDAATKKGNTALHIASLAGQAEVVKVLVTNRANVNAQSQNGFTPLYM--AAQENHLEVVKFLLDNGAS-Q 166
Cdd:PHA02946    55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYlsGTDDEVIERINLLVQYGAKiN 134

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  167 SLATEDGFTPLAVAL---QQGHDQVVSLLLENDTKGKVRLPALHIAARKDDTKAAAL--LLQNDHNADVESKSGFTPLHI 241
Cdd:PHA02946   135 NSVDEEGCGPLLACTdpsERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNPKASTIswMMKLGISPSKPDHDGNTPLHI 214

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  242 --AAHYGNINVATLLLnrgAAVDFTARNDI--TPLHVASKR-GNANMVKLLLDRGAKIDAKTrdgltpLHCGARSGHEQV 316
Cdd:PHA02946   215 vcSKTVKNVDIINLLL---PSTDVNKQNKFgdSPLTLLIKTlSPAHLINKLLSTSNVITDQT------VNICIFYDRDDV 285

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 2023156726  317 VEMLLDRGAPILSktknglSPLHMATQGDHLNCVQLLIQHNVPVDD 362
Cdd:PHA02946   286 LEIINDKGKQYDS------TDFKMAVEVGSIRCVKYLLDNDIICED 325
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 559-779 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 2023156726  559 SIITKKGFTPLHVAAKygKIEVANLLLQkNASPDASGKSGLTPLHVAAhydNQKVALL--LLDQGASPHASAKNGYTPLH 636
Cdd:PLN03192   490 NVVILKNFLQHHKELH--DLNVGDLLGD-NGGEHDDPNMASNLLTVAS---TGNAALLeeLLKAKLDPDIGDSKGRTPLH 563

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  637 IAAKKNQMDIATTLLEYGADANAVTRQGIAPVHLASQDGHVDMVSLL--LTRNANVNLGNKSgltpLHLAAQDDRVNVAE 714
Cdd:PLN03192   564 IAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILyhFASISDPHAAGDL----LCTAAKRNDLTAMK 639

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2023156726  715 VLVNQGAAVDAQTKMGYTPLHVGCHYGNIKIVNFLLQHSAKVN-AKTKNGYTP-----LHQAAQQGHTHII 779
Cdd:PLN03192   640 ELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDkANTDDDFSPtelreLLQKRELGHSITI 710
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 399-426 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 2023156726   399 NGFTPLHIACKKNRIKVMELLLKHGASI 426
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
Ank_5 pfam13857
Ankyrin repeats (many copies);
65-114 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 2023156726   65 VDINISNQNGLNALHLASKEGHVEVVSELIQRGASVDAATKKGNTALHIA 114
Cdd:pfam13857    7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
650-704 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 2023156726  650 LLEYG-ADANAVTRQGIAPVHLASQDGHVDMVSLLLTRNANVNLGNKSGLTPLHLA 704
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 714-926 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 2023156726  714 EVLVNQGAAVDAQTKMGYTPLHVGCHYGNIKIVNFLLQHSAKVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAAPNELT 793
Cdd:PLN03192   542 EELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHA 621

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  794 vnGNTALAIAKRLGYISVVDT-----LKVVTEE----TMTTITVTEKHKmnvpeTMNEVLDMSDDEVRKANAPEILSDA- 863
Cdd:PLN03192   622 --AGDLLCTAAKRNDLTAMKEllkqgLNVDSEDhqgaTALQVAMAEDHV-----DMVRLLIMNGADVDKANTDDDFSPTe 694

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2023156726  864 --EYLSDVEEGEDAMTGDTDkylgPQDLKELGDDSLPAEGYMGFSLGARSASPKVSSDRSYTLNR 926
Cdd:PLN03192   695 lrELLQKRELGHSITIVDSV----PADEPDLGRDGGSRPGRLQGTSSDNQCRPRVSIYKGHPLLR 755
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 230-569 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 2023156726  230 VESKSGFTPLHiaAHYGNINVAT----LLLNRGAAVDFTARNDITPLHVASKRGN--ANMVKLLLDRGAKIDAKTRDGLT 303
Cdd:PHA02716   172 VCKKTGYGILH--AYLGNMYVDIdileWLCNNGVNVNLQNNHLITPLHTYLITGNvcASVIKKIIELGGDMDMKCVNGMS 249

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  304 PLH---CGARSGHEQVVEMLLDRGAPilSKTKNGLSPLH----MATQGDhLNCVQLLIQHNVPVDDVTNDYLTALH--VA 374
Cdd:PHA02716   250 PIMtyiINIDNINPEITNIYIESLDG--NKVKNIPMILHsyitLARNID-ISVVYSFLQPGVKLHYKDSAGRTCLHqyIL 326

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  375 AHCGHYKVAKVLLDKKANPNAKALNGFTPLH----IACKKN----------RIKVMELLLKHGASIQAVTESGLTP---- 436
Cdd:PHA02716   327 RHNISTDIIKLLHEYGNDLNEPDNIGNTVLHtylsMLSVVNildpetdndiRLDVIQCLISLGADITAVNCLGYTPltsy 406

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  437 IHVAAFMGHVNIVSQLMhhgaSPNTTN-VRGETALHMAARAGQTE------VVRYLVQNGAQVEAKAKDDQTPLHisarl 509
Cdd:PHA02716   407 ICTAQNYMYYDIIDCLI----SDKVLNmVKHRILQDLLIRVDDTPciihhiIAKYNIPTDLYTDEYEPYDSTKIH----- 477

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2023156726  510 gkaDIVQQLLQQGASPNAATTSGYTPLHLSAREgHEDVASV------LLDHGASLSIITKKGFTPL 569
Cdd:PHA02716   478 ---DVYHCAIIERYNNAVCETSGMTPLHVSIIS-HTNANIVmdsfvyLLSIQYNINIPTKNGVTPL 539
Ank_4 pfam13637
Ankyrin repeats (many copies);
763-815 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 2023156726  763 GYTPLHQAAQQGHTHIINVLLQHGAAPNELTVNGNTALAIAKRLGYISVVDTL 815
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank_5 pfam13857
Ankyrin repeats (many copies);
126-180 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 2023156726  126 LVTNR-ANVNAQSQNGFTPLYMAAQENHLEVVKFLLDNGASQSLATEDGFTPLAVA 180
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 207-288 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 2023156726  207 HIAArKDDTKAAALLLQNDHNADVESKSGFTPLHIAAHYGNINVATLLLNRGAAVDFTARNDITPLHVASKRGNANMVKL 286
Cdd:PTZ00322    88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                   ..
gi 2023156726  287 LL 288
Cdd:PTZ00322   167 LS 168
Ank_4 pfam13637
Ankyrin repeats (many copies);
47-94 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 2023156726   47 RAARAGNLEKALDYLKSGVDINISNQNGLNALHLASKEGHVEVVSELI 94
Cdd:pfam13637    7 AAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 532-771 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 2023156726  532 GYTPLHLSAREG-HEDVASVLLDHGASLSIitkkGFTPLHVAAK--YGKIEVANLLLQKNASPDASGK-----------S 597
Cdd:TIGR00870   52 GRSALFVAAIENeNLELTELLLNLSCRGAV----GDTLLHAISLeyVDAVEAILLHLLAAFRKSGPLElandqytseftP 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  598 GLTPLHVAAHYDNQKVALLLLDQGASPHASAK--------------NGYTPLHIAAKKNQMDIATTLLEYGADANAVTRQ 663
Cdd:TIGR00870  128 GITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADSL 207

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  664 GIAPVHLASqdghvdMVSLLLTRNANVNLGNKSGLTPlHLAAQDDRVNVAEVLVNQgaavdaqtkmGYTPLHVGCHYGNI 743
Cdd:TIGR00870  208 GNTLLHLLV------MENEFKAEYEELSCQMYNFALS-LLDKLRDSKELEVILNHQ----------GLTPLKLAAKEGRI 270

                          250       260       270
                   ....*....|....*....|....*....|.
gi 2023156726  744 KIVNFLLQ---HSAKVNAKTkngYTPLHQAA 771
Cdd:TIGR00870  271 VLFRLKLAikyKQKKFVAWP---NGQQLLSL 298
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 202-321 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 2023156726  202 RLPALHIAARKDDTKAAALLLQNDHNADVESKSGFTPLHIAAHyGNINVATLLLNRGAAVDFTARNDITPLHVASKRGNA 281
Cdd:PTZ00322    50 HLEALEATENKDATPDHNLTTEEVIDPVVAHMLTVELCQLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHV 128

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2023156726  282 NMVKLLLDRGAKIDAKTRDGLTPLHCGARSGHEQVVEMLL 321
Cdd:PTZ00322   129 QVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PHA02946 PHA02946
ankyin-like protein; Provisional
 375-574 3.30e-06

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 53.13  E-value: 3.30e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  375 AHCG----HYKVAKVLLDKKANPNAKALNGFTPLHIACKKNRIKVMELLLKHGASIQAVTESGLTPIHVAAFMGH--VNI 448
Cdd:PHA02946    43 AYCGikglDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIER 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  449 VSQLMHHGASPNTTNVRGETALHMAARAGQTEVVRYLVQNG--AQVEAKAKDDQTPLHISARLGKADIVQQLLQQGASPN 526
Cdd:PHA02946   123 INLLVQYGAKINNSVDEEGCGPLLACTDPSERVFKKIMSIGfeARIVDKFGKNHIHRHLMSDNPKASTISWMMKLGISPS 202

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 2023156726  527 AATTSGYTPLHLSAREGHEDVASV-LLDHGASLSIITKKGFTPLHVAAK 574
Cdd:PHA02946   203 KPDHDGNTPLHIVCSKTVKNVDIInLLLPSTDVNKQNKFGDSPLTLLIK 251
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 418-500 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 2023156726  418 LLLKHGASIQAVTESGLTPIHVAAFMGHVNIVSQLMHHGASPNTTNVRGETALHMAARAGQTEVVRYLV---QNGAQVEA 494
Cdd:PTZ00322   100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSrhsQCHFELGA 179


                   ....*.
gi 2023156726  495 KAKDDQ 500
Cdd:PTZ00322   180 NAKPDS 185
Death_p75NR cd08311
Death domain of p75 Neurotrophin Receptor; Death Domain (DD) found in p75 neurotrophin ...
 4077-4144 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 2023156726 4077 SWTELARELNFSVDEINQI-RVENPnsliaqSFMLLKKWVTRDGknATTDALTSVLTKINRIDIVTLLE 4144
Cdd:cd08311     20 DWRALAGELGYSAEEIDSFaREADP------CRALLTDWSAQDG--ATLGVLLTALRKIGRDDIVEILQ 80
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 569-673 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 2023156726  569 LHVAAKYGKIEVANLLLQKNASPDA----SGKSGLTPLHVAAHYDNQKVALLLLDQGASPHASAKNG-YTPLHIAAKKNQ 643
Cdd:PHA02884    37 LYSSIKFHYTDIIDAILKLGADPEApfplSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAkITPLYISVLHGC 116

                           90       100       110
                   ....*....|....*....|....*....|
gi 2023156726  644 MDIATTLLEYGADANAVTRQGIAPVHLASQ 673
Cdd:PHA02884   117 LKCLEILLSYGADINIQTNDMVTPIELALM 146
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 595-784 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 2023156726  595 GKSGLTPLHVAAHYDNQKV--ALLLLDQGASPHASAKN------------GYTPLHIAAKKNQMDIATTLLEYGADanav 660
Cdd:cd21882     23 GATGKTCLHKAALNLNDGVneAIMLLLEAAPDSGNPKElvnapctdefyqGQTALHIAIENRNLNLVRLLVENGAD---- 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  661 trqgiapVHLAsqdghvdmvsllltrnANVNLGNKSGLT-------PLHLAAQDDRVNVAEVLVNQG---AAVDAQTKMG 730
Cdd:cd21882     99 -------VSAR----------------ATGRFFRKSPGNlfyfgelPLSLAACTNQEEIVRLLLENGaqpAALEAQDSLG 155

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  731 YTPLHVGCHYGN---------IKIVNFLLQHSAKVNAKTK-------NGYTPLHQAAQQGHTHIINVLLQ 784
Cdd:cd21882    156 NTVLHALVLQADntpensafvCQMYNLLLSYGAHLDPTQQleeipnhQGLTPLKLAAVEGKIVMFQHILQ 225
Ank_5 pfam13857
Ankyrin repeats (many copies);
93-147 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 2023156726   93 LIQRG-ASVDAATKKGNTALHIASLAGQAEVVKVLVTNRANVNAQSQNGFTPLYMA 147
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
501-552 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 2023156726  501 TPLHISARLGKADIVQQLLQQGASPNAATTSGYTPLHLSAREGHEDVASVLL 552
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 462-635 6.58e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 52.56  E-value: 6.58e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  462 TNVRGETALHMAARAGQTEVVRYLVQNGAQVEAKAKDDQTPLHISARLGKADIVQQLLQQGASPNAATTSGYTPLHLSAR 541
Cdd:PLN03192   521 DDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAIS 600

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  542 EGHEDVASVLLdHGASLSIITKKGfTPLHVAAKYGKIEVANLLLQKNASPDASGKSGLTPLHVAAHYDNQKVALLLLDQG 621
Cdd:PLN03192   601 AKHHKIFRILY-HFASISDPHAAG-DLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNG 678

                          170
                   ....*....|....*
gi 2023156726  622 AS-PHASAKNGYTPL 635
Cdd:PLN03192   679 ADvDKANTDDDFSPT 693
Ank_5 pfam13857
Ankyrin repeats (many copies);
221-275 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 2023156726  221 LLQNDH-NADVESKSGFTPLHIAAHYGNINVATLLLNRGAAVDFTARNDITPLHVA 275
Cdd:pfam13857    1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 69-144 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 2023156726   69 ISN-QNGLNALHLASKEGHVEVVSELIQRGASVDAATKKGNTALHIASLAGQAEVVKVLVTNRANVN-AQSQNGFTPL 144
Cdd:PLN03192   616 ISDpHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDkANTDDDFSPT 693
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 48-103 7.66e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 52.56  E-value: 7.66e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2023156726   48 AARAGNLEKALDYLKSGVDINISNQNGLNALHLASKEGHVEVVSELIQRGASVDAA 103
Cdd:PLN03192   629 AAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKA 684
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 581-660 8.37e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.21  E-value: 8.37e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  581 ANLLLQKNASPDASGKSGLTPLHVAAHYDNQKVALLLLDQGASPHASAKNGYTPLHIAAKKNQMDIATTLLEYG-----A 655
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSqchfeL 177


                   ....*
gi 2023156726  656 DANAV 660
Cdd:PTZ00322   178 GANAK 182
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 54-257 8.46e-06

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


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 52.12  E-value: 8.46e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726   54 LEKALDYLKSGVDINISNqnglnALHLASKEGHVEvvsELIQrgASVDAATKKGNTALHIASLAGQAEVVKVLVTNRANV 133
Cdd:cd22196     51 LLKAMLNLHNGQNDTISL-----LLDIAEKTGNLK---EFVN--AAYTDSYYKGQTALHIAIERRNMHLVELLVQNGADV 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  134 NA----------QSQNGF----TPLYMAAQENHLEVVKFLLDNGASQS-LATEDGF------TPLAVA--LQQGHDQVVS 190
Cdd:cd22196    121 HArasgeffkkkKGGPGFyfgeLPLSLAACTNQLDIVKFLLENPHSPAdISARDSMgntvlhALVEVAdnTPENTKFVTK 200

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2023156726  191 LLLENDTKGKVRLPALHIAArkddtkaaalllqndhnadVESKSGFTPLHIAAHYGNINVATLLLNR 257
Cdd:cd22196    201 MYNEILILGAKIRPLLKLEE-------------------ITNKKGLTPLKLAAKTGKIGIFAYILGR 248
Death_DRs cd08784
Death Domain of Death Receptors; Death domain (DD) found in death receptor proteins. Death ...
 4076-4135 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 2023156726 4076 LSWTELARELNFSVDEINQIRVENPNSLIAQSFMLLKKWVTRDGKNATTDALTSVLTKIN 4135
Cdd:cd08784     12 SQWKGFVRKLGLNEAEIDEIKNDNVQDTAEAKYQMLRNWHQLTGRKAAYDTLIKDLKKMN 71
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 267-296 9.30e-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: 9.30e-06
                            10        20        30
                    ....*....|....*....|....*....|
gi 2023156726   267 NDITPLHVASKRGNANMVKLLLDRGAKIDA 296
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 630-662 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 2023156726  630 NGYTPLHIAAKK-NQMDIATTLLEYGADANAVTR 662
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
353-407 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 2023156726  353 LIQH-NVPVDDVTNDYLTALHVAAHCGHYKVAKVLLDKKANPNAKALNGFTPLHIA 407
Cdd:pfam13857    1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 633-766 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 2023156726  633 TPLH--IAAKKNQMDIATTLLEYGADANAVTR-QGIAPVHL---ASQDGHVDMVSLLLTRNANVNLGNKSGLTPLH--LA 704
Cdd:PHA02859    53 TPIFscLEKDKVNVEILKFLIENGADVNFKTRdNNLSALHHylsFNKNVEPEILKILIDSGSSITEEDEDGKNLLHmyMC 132

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2023156726  705 AQDDRVNVAEVLVnqgaavdaqtKMGYTPLHVGCHYGNI-----------KIVNFLLQHSAKVNAKTKNGYTP 766
Cdd:PHA02859   133 NFNVRINVIKLLI----------DSGVSFLNKDFDNNNIlysyilfhsdkKIFDFLTSLGIDINETNKSGYNC 195
Ank_5 pfam13857
Ankyrin repeats (many copies);
716-770 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 2023156726  716 LVNQGAAVDAQTKMGYTPLHVGCHYGNIKIVNFLLQHSAKVNAKTKNGYTPLHQA 770
Cdd:pfam13857    2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 139-165 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 2023156726   139 NGFTPLYMAAQENHLEVVKFLLDNGAS 165
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 537-631 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 2023156726  537 HLSArEGHEDVASVLLDHGASLSIITKKGFTPLHVAAKYGKIEVANLLLQKNASPDASGKSGLTPLHVAAHYDNQKVALL 616
Cdd:PTZ00322    88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166

                           90
                   ....*....|....*
gi 2023156726  617 LLDQGASPHASAKNG 631
Cdd:PTZ00322   167 LSRHSQCHFELGANA 181
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 106-257 1.79e-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: 50.95  E-value: 1.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  106 KGNTALHIASLAGQAEVVKVLVTNRANVNAQSQNGF--------------TPLYMAAQENHLEVVKFLLDNgaSQSLATe 171
Cdd:cd22193     75 EGQTALHIAIERRQGDIVALLVENGADVHAHAKGRFfqpkyqgegfyfgeLPLSLAACTNQPDIVQYLLEN--EHQPAD- 151

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  172 dgftplavalqqghdqvvslLLENDTKGKVRLPALHIAArkDDTKAAALLLQNDHNA---------------DVESKSGF 236
Cdd:cd22193    152 --------------------IEAQDSRGNTVLHALVTVA--DNTKENTKFVTRMYDMilirgaklcptveleEIRNNDGL 209

                          170       180
                   ....*....|....*....|.
gi 2023156726  237 TPLHIAAHYGNINVATLLLNR 257
Cdd:cd22193    210 TPLQLAAKMGKIEILKYILQR 230
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 106-257 1.85e-05

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


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 51.01  E-value: 1.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  106 KGNTALHIASLAGQAEVVKVLVTNRANVNAQSQNGF-------------TPLYMAAQENHLEVVKFLLDNGASqslated 172
Cdd:cd22197     93 RGHSALHIAIEKRSLQCVKLLVENGADVHARACGRFfqkkqgtcfyfgeLPLSLAACTKQWDVVNYLLENPHQ------- 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  173 gftPLAVALQQGHDQVV---SLLLENDTKGKVrlpALHIAARKDDTKAAALLLQNDHNADVESKSGFTPLHIAAHYGNIN 249
Cdd:cd22197    166 ---PASLQAQDSLGNTVlhaLVMIADNSPENS---ALVIKMYDGLLQAGARLCPTVQLEEISNHEGLTPLKLAAKEGKIE 239


                   ....*...
gi 2023156726  250 VATLLLNR 257
Cdd:cd22197    240 IFRHILQR 247
Ank_5 pfam13857
Ankyrin repeats (many copies);
419-473 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 2023156726  419 LLKHG-ASIQAVTESGLTPIHVAAFMGHVNIVSQLMHHGASPNTTNVRGETALHMA 473
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 399-431 2.01e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 44.20  E-value: 2.01e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2023156726  399 NGFTPLHIACKK-NRIKVMELLLKHGASIQAVTE 431
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 74-257 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 2023156726   74 GLNALHLASKEgHVEVVSELIQRGASVDAATK--------------KGNTALHIASLAGQAEVVKVLVTNRANVNA---- 135
Cdd:TIGR00870   82 GDTLLHAISLE-YVDAVEAILLHLLAAFRKSGplelandqytseftPGITALHLAAHRQNYEIVKLLLERGASVPAracg 160

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  136 ------QSQNGF----TPLYMAAQENHLEVVKFLLDNGASQSLATEDGFTPLavalqqgHDQVVslllENDTKGK----- 200
Cdd:TIGR00870  161 dffvksQGVDSFyhgeSPLNAAACLGSPSIVALLSEDPADILTADSLGNTLL-------HLLVM----ENEFKAEyeels 229

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2023156726  201 --VRLPALHIAARKDDTKAAALLLQNDhnadvesksGFTPLHIAAHYGNINVATLLLNR 257
Cdd:TIGR00870  230 cqMYNFALSLLDKLRDSKELEVILNHQ---------GLTPLKLAAKEGRIVLFRLKLAI 279
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 61-126 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 2023156726   61 LKSGVDINISNQNGLNALHLASKEGHVEVVSELIQRGASVDAATKKGNTALHIASLAGQAEVVKVL 126
Cdd:PTZ00322   102 LTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 399-428 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 2023156726  399 NGFTPLHIACKKNRIKVMELLLKHGASIQA 428
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 730-761 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 2023156726  730 GYTPLHVGC-HYGNIKIVNFLLQHSAKVNAKTK 761
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 73-105 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 2023156726   73 NGLNALHLAS-KEGHVEVVSELIQRGASVDAATK 105
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 588-706 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 2023156726  588 NASPDASGKSGLTPLHVAAHYDNQKVALLLLDQGASPHASAKN--------------GYTPLHIAAKKNQMDIATTLLEY 653
Cdd:cd22194    131 NAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEIVQLLMEK 210

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2023156726  654 GadANAVTRQ---GIAPVH---LASQDGH------VDMVSLLLTRNANVNL---GNKSGLTPLHLAAQ 706
Cdd:cd22194    211 E--STDITSQdsrGNTVLHalvTVAEDSKtqndfvKRMYDMILLKSENKNLetiRNNEGLTPLQLAAK 276
Ank_4 pfam13637
Ankyrin repeats (many copies);
667-717 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 2023156726  667 PVHLASQDGHVDMVSLLLTRNANVNLGNKSGLTPLHLAAQDDRVNVAEVLV 717
Cdd:pfam13637    4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 564-593 2.99e-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: 2.99e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 2023156726   564 KGFTPLHVAAKYGKIEVANLLLQKNASPDA 593
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 654-753 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 2023156726  654 GADANAVTRQGIAPV----------HLASQDGHVDmVSLLLTRNANVNLGNKSGLTPLHLAAQDDRVNVAEVLVNQGAAV 723
Cdd:PTZ00322    63 TPDHNLTTEEVIDPVvahmltvelcQLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADP 141

                           90       100       110
                   ....*....|....*....|....*....|
gi 2023156726  724 DAQTKMGYTPLHVGCHYGNIKIVNFLLQHS 753
Cdd:PTZ00322   142 TLLDKDGKTPLELAEENGFREVVQLLSRHS 171
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 465-497 3.31e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 43.43  E-value: 3.31e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2023156726  465 RGETALHMAA-RAGQTEVVRYLVQNGAQVEAKAK 497
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 339-422 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 2023156726  339 HMATQGDHLNcVQLLIQHNVPVDDVTNDYLTALHVAAHCGHYKVAKVLLDKKANPNAKALNGFTPLHIACKKNRIKVMEL 418
Cdd:PTZ00322    88 QLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                   ....
gi 2023156726  419 LLKH 422
Cdd:PTZ00322   167 LSRH 170
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 267-299 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 2023156726  267 NDITPLHVASKR-GNANMVKLLLDRGAKIDAKTR 299
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 270-444 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 2023156726  270 TPLH--VASKRGNANMVKLLLDRGAKIDAKTRD-GLTPLH---CGARSGHEQVVEMLLDRGAPILSKTKNGLSPLHMatq 343
Cdd:PHA02859    53 TPIFscLEKDKVNVEILKFLIENGADVNFKTRDnNLSALHhylSFNKNVEPEILKILIDSGSSITEEDEDGKNLLHM--- 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  344 gdhlncvqlliqhnvpvddvtndYLTALHVaahcgHYKVAKVLLDKKANPNAKALNGFTPLH-IACKKNRIKVMELLLKH 422
Cdd:PHA02859   130 -----------------------YMCNFNV-----RINVIKLLIDSGVSFLNKDFDNNNILYsYILFHSDKKIFDFLTSL 181

                          170       180
                   ....*....|....*....|..
gi 2023156726  423 GASIQAVTESGLTPIHVAAFMG 444
Cdd:PHA02859   182 GIDINETNKSGYNCYDLIKFRN 203
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 300-332 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 2023156726  300 DGLTPLHCGA-RSGHEQVVEMLLDRGAPILSKTK 332
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 762-790 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 2023156726  762 NGYTPLHQAAQQ-GHTHIINVLLQHGAAPN 790
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVN 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 762-791 5.33e-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: 5.33e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 2023156726   762 NGYTPLHQAAQQGHTHIINVLLQHGAAPNE 791
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 237-339 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 2023156726  237 TPLH--IAAHYGNINVATLLLNRGAAVDFTAR-NDITPLH---VASKRGNANMVKLLLDRGAKIDAKTRDGLTPLH---- 306
Cdd:PHA02859    53 TPIFscLEKDKVNVEILKFLIENGADVNFKTRdNNLSALHhylSFNKNVEPEILKILIDSGSSITEEDEDGKNLLHmymc 132

                           90       100       110
                   ....*....|....*....|....*....|....
gi 2023156726  307 -CGARSgheQVVEMLLDRGAPILSKTKNGLSPLH 339
Cdd:PHA02859   133 nFNVRI---NVIKLLIDSGVSFLNKDFDNNNILY 163
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 630-659 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 2023156726   630 NGYTPLHIAAKKNQMDIATTLLEYGADANA 659
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 746-815 6.58e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.13  E-value: 6.58e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  746 VNFLLQHSAKVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAAPNELTVNGNTALAIAKRLGYISVVDTL 815
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 400-520 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 2023156726  400 GFTPLHIACKKNRIKVMELLLKHGASIQAVTES--------------GLTPIHVAAFMGHVNIVSQLM---HHGASPNTT 462
Cdd:cd22193     76 GQTALHIAIERRQGDIVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLSLAACTNQPDIVQYLLeneHQPADIEAQ 155

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2023156726  463 NVRGETALHMAARAGQ---------TEVVRYLVQNGAQV-------EAKAKDDQTPLHISARLGKADIVQQLLQ 520
Cdd:cd22193    156 DSRGNTVLHALVTVADntkentkfvTRMYDMILIRGAKLcptveleEIRNNDGLTPLQLAAKMGKIEILKYILQ 229
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 532-563 8.08e-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: 8.08e-05
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2023156726  532 GYTPLHLSA-REGHEDVASVLLDHGASLSIITK 563
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 622-846 8.24e-05

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 48.99  E-value: 8.24e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  622 ASPHASAKNGYTPLHIAAKKNQMDIATTLLEYGADANAVTRQ--------------GIAPVHLASQDGHVDMVSLLLTR- 686
Cdd:cd22194    132 AEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEIVQLLMEKe 211

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  687 NANVNLGNKSGLTPLHLAaqddrVNVAEVLVNQGAAVdaqtkmgytplhvgchygnIKIVNFLLQHSAKVNAKT---KNG 763
Cdd:cd22194    212 STDITSQDSRGNTVLHAL-----VTVAEDSKTQNDFV-------------------KRMYDMILLKSENKNLETirnNEG 267

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  764 YTPLHQAAQQGHTHIINVLLQHgaapnELTVNGNTALA----------IAKRLGYISVVDT------LKVVTEETmttiT 827
Cdd:cd22194    268 LTPLQLAAKMGKAEILKYILSR-----EIKEKPNRSLSrkftdwaygpVSSSLYDLTNVDTttdnsvLEIIVYNT----N 338

                          250
                   ....*....|....*....
gi 2023156726  828 VTEKHKMNVPETMNEVLDM 846
Cdd:cd22194    339 IDNRHEMLTLEPLHTLLHM 357
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 564-596 9.09e-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: 9.09e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2023156726  564 KGFTPLHVAA-KYGKIEVANLLLQKNASPDASGK 596
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 369-396 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 2023156726  369 TALHVAA-HCGHYKVAKVLLDKKANPNAK 396
Cdd:pfam00023    4 TPLHLAAgRRGNLEIVKLLLSKGADVNAR 32
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 532-560 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 2023156726   532 GYTPLHLSAREGHEDVASVLLDHGASLSI 560
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 729-758 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 2023156726   729 MGYTPLHVGCHYGNIKIVNFLLQHSAKVNA 758
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 139-165 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 2023156726  139 NGFTPLYMAA-QENHLEVVKFLLDNGAS 165
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGAD 28
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 73-102 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 2023156726    73 NGLNALHLASKEGHVEVVSELIQRGASVDA 102
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 627-844 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 2023156726  627 SAKNGYTPLHIAAKKNQMDIATTLLEYGADANAVTRQ--------------GIAPVHLASQDGHVDMVSLLLtRNANvnl 692
Cdd:cd22193     72 EYYEGQTALHIAIERRQGDIVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLSLAACTNQPDIVQYLL-ENEH--- 147

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  693 gnksglTPLHLAAQDDRVN-VAEVLVNQGAAVDAQTKMgytplhvgchygNIKIVNFLLQHSAKVNAKTK-------NGY 764
Cdd:cd22193    148 ------QPADIEAQDSRGNtVLHALVTVADNTKENTKF------------VTRMYDMILIRGAKLCPTVEleeirnnDGL 209

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  765 TPLHQAAQQGHTHIINVLLQhgaapneLTVNGNTALAIAKR------------LGYISVVDTL--KVVTEETMTTITVTE 830
Cdd:cd22193    210 TPLQLAAKMGKIEILKYILQ-------REIKEPELRHLSRKftdwaygpvsssLYDLSNVDTCekNSVLEIIVYNSKIDN 282

                          250
                   ....*....|....
gi 2023156726  831 KHKMNVPETMNEVL 844
Cdd:cd22193    283 RHEMLTLEPLNTLL 296
Ank_5 pfam13857
Ankyrin repeats (many copies);
485-538 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 2023156726  485 LVQNG-AQVEAKAKDDQTPLHISARLGKADIVQQLLQQGASPNAATTSGYTPLHL 538
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 106-136 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 2023156726  106 KGNTALHIASL-AGQAEVVKVLVTNRANVNAQ 136
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNAR 32
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 661-815 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 2023156726  661 TRQGIAPVHLASQDGHVDMVSLLLTRNANVNLGNKSGLTPLHLAAQDDRV--NVAEVLVNQGAAVDAQTKMGYTP----- 733
Cdd:PHA02716   176 TGYGILHAYLGNMYVDIDILEWLCNNGVNVNLQNNHLITPLHTYLITGNVcaSVIKKIIELGGDMDMKCVNGMSPimtyi 255

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  734 ------------LHVGCHYGN--------------------IKIVNFLLQHSAKVNAKTKNGYTPLHQAAQQGH--THII 779
Cdd:PHA02716   256 inidninpeitnIYIESLDGNkvknipmilhsyitlarnidISVVYSFLQPGVKLHYKDSAGRTCLHQYILRHNisTDII 335

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 2023156726  780 NVLLQHGAAPNELTVNGNTALaiAKRLGYISVVDTL 815
Cdd:PHA02716   336 KLLHEYGNDLNEPDNIGNTVL--HTYLSMLSVVNIL 369
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 389-550 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 2023156726  389 KKANP----NAKALN----GFTPLHIACKKNRIKVMELLLKHGASIQAVTES-------------GLTPIHVAAFMGHVN 447
Cdd:cd22197     75 DSGNPkplvNAQCTDeyyrGHSALHIAIEKRSLQCVKLLVENGADVHARACGrffqkkqgtcfyfGELPLSLAACTKQWD 154

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  448 IVSQLM---HHGASPNTTNVRGETALH---MAA--RAGQTEVVRY----LVQNGAQVEAKAKDDQ-------TPLHISAR 508
Cdd:cd22197    155 VVNYLLenpHQPASLQAQDSLGNTVLHalvMIAdnSPENSALVIKmydgLLQAGARLCPTVQLEEisnheglTPLKLAAK 234

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2023156726  509 LGKADIVQQLLQQGAS------PNAATTSGYTPLHLSARegheDVASV 550
Cdd:cd22197    235 EGKIEIFRHILQREFSgpyqhlSRKFTEWCYGPVRVSLY----DLSSV 278
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 730-758 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 2023156726  730 GYTPLHVGCHYGNIKIVNFLLQHSAKVNA 758
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 366-395 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 2023156726   366 DYLTALHVAAHCGHYKVAKVLLDKKANPNA 395
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 384-519 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 2023156726  384 KVLLDkkANPNAKALNGFTPLHIACKKNRIKVMELLLKHGASIQAVTES--------------GLTPIHVAAFMGHVNIV 449
Cdd:cd22194    127 DRFIN--AEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEIV 204

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  450 SQLMHHGASPNTT-NVRGETALH---MAARAGQTE---VVR-----YLVQNGAQVEA-KAKDDQTPLHISARLGKADIVQ 516
Cdd:cd22194    205 QLLMEKESTDITSqDSRGNTVLHalvTVAEDSKTQndfVKRmydmiLLKSENKNLETiRNNEGLTPLQLAAKMGKAEILK 284


                   ...
gi 2023156726  517 QLL 519
Cdd:cd22194    285 YIL 287
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 662-755 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 2023156726  662 RQGIAPVHLASQDGHVD---MVSLLLTRNANVNLGN-KSGLTPLHLAAQDDRVNVAEVLVNQ-GAAVDAQTKMGYTPLHV 736
Cdd:PHA02736    53 RHGKQCVHIVSNPDKADpqeKLKLLMEWGADINGKErVFGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYV 132

                           90
                   ....*....|....*....
gi 2023156726  737 GCHYGNIKIVNFLLQHSAK 755
Cdd:PHA02736   133 ACERHDAKMMNILRAKGAQ 151
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 235-262 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 2023156726   235 GFTPLHIAAHYGNINVATLLLNRGAAVD 262
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 588-712 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 2023156726  588 NASPDASGKSGLTPLHVAAHYDNQKVALLLLDQGASPHASAKN--------------GYTPLHIAAKKNQMDIATTLLEY 653
Cdd:cd22193     66 NAEYTDEYYEGQTALHIAIERRQGDIVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLSLAACTNQPDIVQYLLEN 145

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2023156726  654 G---ADANAVTRQGIAPVH--LASQDGHVD-------MVSLLLTRNANV-------NLGNKSGLTPLHLAAQDDRVNV 712
Cdd:cd22193    146 EhqpADIEAQDSRGNTVLHalVTVADNTKEntkfvtrMYDMILIRGAKLcptveleEIRNNDGLTPLQLAAKMGKIEI 223
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 61-290 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 2023156726   61 LKSGVDINISNQNGLNALH---LASKEGHVEVVSELIQRGASV-DAATKKGNTALHI--ASLAGQAEVVKVLVtnRANVN 134
Cdd:PHA02989    95 LKFGADINLKTFNGVSPIVcfiYNSNINNCDMLRFLLSKGINVnDVKNSRGYNLLHMylESFSVKKDVIKILL--SFGVN 172

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  135 AQSQN---GFTPL--YMAAQEN--HLEVVKFLLDNGASqsLATEDgftplavalqQGHDQVVSLLLENdtkgkvrlpalH 207
Cdd:PHA02989   173 LFEKTslyGLTPMniYLRNDIDviSIKVIKYLIKKGVN--IETNN----------NGSESVLESFLDN-----------N 229

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  208 IAARKDDTKAAALLLQ--NDHNADvesKSGFTPLHIAAHYGNINVATLLLNRGAAVDFTARNDITPLHVASKRGNANMVK 285
Cdd:PHA02989   230 KILSKKEFKVLNFILKyiKINKKD---KKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLN 306


                   ....*
gi 2023156726  286 LLLDR 290
Cdd:PHA02989   307 RILQL 311
Ank_5 pfam13857
Ankyrin repeats (many copies);
320-374 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 2023156726  320 LLDRG-APILSKTKNGLSPLHMATQGDHLNCVQLLIQHNVPVDDVTNDYLTALHVA 374
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 93-160 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 2023156726   93 LIQRGASVDAATKKGNTALHIASLAGQAEVVKVLVTNRANVNAQSQNGFTPLYMAAQENHLEVVKFLL 160
Cdd:PTZ00322   101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
Ank_5 pfam13857
Ankyrin repeats (many copies);
518-572 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 2023156726  518 LLQQG-ASPNAATTSGYTPLHLSAREGHEDVASVLLDHGASLSIITKKGFTPLHVA 572
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00121 PTZ00121
MAEBL; Provisional
 2584-3019 2.62e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.44  E-value: 2.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726 2584 RVDRTVKEAEEKlTEVSQFFRDKTEKLNDELQSPEKKQH---KKNGKEIHSSQSSASSSPEKVLLSELPSSGDEWSK--- 2657
Cdd:PTZ00121  1330 KADAAKKKAEEA-KKAAEAAKAEAEAAADEAEAAEEKAEaaeKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKkad 1408

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726 2658 -VKQYAHDGKcfpKVDE--RKASSLPSSPEKRifvQPAEDSKQTMEHKGSAQQtgvpevsqtgfqlkQSKLSSIRLKFEQ 2734
Cdd:PTZ00121  1409 eLKKAAAAKK---KADEakKKAEEKKKADEAK---KKAEEAKKADEAKKKAEE--------------AKKAEEAKKKAEE 1468

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726 2735 SISPRSKDVTQEEKKLDGQSKipvKKSQESKLPVYQFYSREKHAKQVEvidgstalqkEVKIQEDfvpgKAKAIEDFRAS 2814
Cdd:PTZ00121  1469 AKKADEAKKKAEEAKKADEAK---KKAEEAKKKADEAKKAAEAKKKAD----------EAKKAEE----AKKADEAKKAE 1531

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726 2815 DAQKRPEMSKGvvpeyfSEPQAKDLVYGSDSTAKGHWDKKIYRTWESPGTSNHQTQKEKLSHVLVPDTVKENHVDHAETK 2894
Cdd:PTZ00121  1532 EAKKADEAKKA------EEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEK 1605

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726 2895 TDKKSEFATVTEHKLAANGIH-SEEVK---ELTVKSPSKRVLYREFVVREGERNGEVADKISKRKEEIAVSHIPVRIVEE 2970
Cdd:PTZ00121  1606 KMKAEEAKKAEEAKIKAEELKkAEEEKkkvEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEE 1685

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*....
gi 2023156726 2971 KrtmldgvyelsakvsqsaviKEKVERQIDYMEDEKIKCSEIRKVTKQQ 3019
Cdd:PTZ00121  1686 D--------------------EKKAAEALKKEAEEAKKAEELKKKEAEE 1714
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 762-791 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 2023156726  762 NGYTPLHQAAQQGHTHIINVLLQHGAAPNE 791
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 465-494 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 2023156726   465 RGETALHMAARAGQTEVVRYLVQNGAQVEA 494
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 433-463 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 2023156726  433 GLTPIHVAAFM-GHVNIVSQLMHHGASPNTTN 463
Cdd:pfam00023    2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
PHA02743 PHA02743
Viral ankyrin protein; Provisional
 191-295 3.29e-04

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 44.42  E-value: 3.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  191 LLLENDTKGKVrlpALHIAARKDDTKAA---ALLLQN--DHNADvESKSGFTPLHIAAHYGNINVATLLLnRGAAVDFTA 265
Cdd:PHA02743    49 LLHRYDHHGRQ---CTHMVAWYDRANAVmkiELLVNMgaDINAR-ELGTGNTLLHIAASTKNYELAEWLC-RQLGVNLGA 123

                           90       100       110
                   ....*....|....*....|....*....|..
gi 2023156726  266 RNDI--TPLHVASKRGNANMVKLLLDRGAKID 295
Cdd:PHA02743   124 INYQheTAYHIAYKMRDRRMMEILRANGAVCD 155
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 235-268 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 2023156726  235 GFTPLHIAA-HYGNINVATLLLNRGAAVDftARND 268
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVN--ARDK 34
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 630-659 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 2023156726  630 NGYTPLHIAAKKNQMDIATTLLEYGADANA 659
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 465-494 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 2023156726  465 RGETALHMAARAGQTEVVRYLVQNGAQVEA 494
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02791 PHA02791
ankyrin-like protein; Provisional
 398-568 3.84e-04

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 45.80  E-value: 3.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  398 LNGFTPLHIACKKNRIKVMELLLKHGAsIQAVTESGLtPIHVAAFMGHVNIVSQLMHHGASPNTTNVRGETALHMAARAG 477
Cdd:PHA02791    28 VHGHSALYYAIADNNVRLVCTLLNAGA-LKNLLENEF-PLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSG 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  478 QTEVVRYLVQNGAQVEAKAKDD-QTPLHISARLGKADIVQQLLQQGASPNAATTSgYTPLHLSAREGHEDVASVLLDHGA 556
Cdd:PHA02791   106 NMQTVKLFVKKNWRLMFYGKTGwKTSFYHAVMLNDVSIVSYFLSEIPSTFDLAIL-LSCIHITIKNGHVDMMILLLDYMT 184

                          170
                   ....*....|..
gi 2023156726  557 SLSIITKKGFTP 568
Cdd:PHA02791   185 STNTNNSLLFIP 196
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 498-529 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 2023156726  498 DDQTPLHISA-RLGKADIVQQLLQQGASPNAAT 529
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
Ank_5 pfam13857
Ankyrin repeats (many copies);
287-341 4.37e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.18  E-value: 4.37e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2023156726  287 LLDRG-AKIDAKTRDGLTPLHCGARSGHEQVVEMLLDRGAPILSKTKNGLSPLHMA 341
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 106-135 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 2023156726   106 KGNTALHIASLAGQAEVVKVLVTNRANVNA 135
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00121 PTZ00121
MAEBL; Provisional
 2566-3032 4.91e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.67  E-value: 4.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726 2566 RFTEDRldRGREKLMYED-RVDRTVKEAEEKLTEVSQFFRDKTEKLNDELQSPEKKQHKKNGKEIHSSQSSASSSPEKVL 2644
Cdd:PTZ00121  1207 KAEEER--KAEEARKAEDaKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELK 1284

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726 2645 LSELPSSGDEWSK---------VKQYAHDGKcfpKVDERKASSLPSSPEKRIFVQPAEDSKQTMEHKGSAQQTGVPEVSQ 2715
Cdd:PTZ00121  1285 KAEEKKKADEAKKaeekkkadeAKKKAEEAK---KADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA 1361

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726 2716 TGfqlKQSKLSSIRLKFEQSISPRSKDVTQEEKKLDGQSKI---PVKKSQESKLPVYQFYSREKHAKQVEVIDGSTALQK 2792
Cdd:PTZ00121  1362 AE---EKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKaeeDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKK 1438

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726 2793 EVKIQEDFVPGKAKAIEDFRASDAQKRPEMSKgvvpeyfsepQAKDLVYGSDSTAKGHWDKKIYRTWESPGTSNHQTQKE 2872
Cdd:PTZ00121  1439 KAEEAKKADEAKKKAEEAKKAEEAKKKAEEAK----------KADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA 1508

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726 2873 KlshvlvpdtVKENHVDHAETKTdKKSEFATVTEHKLAANGIHSEEVKELTVKSPSKRVLYREFVVREGERNGEVADK-I 2951
Cdd:PTZ00121  1509 K---------KKADEAKKAEEAK-KADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKnM 1578

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726 2952 SKRKEEIAvshipvRIVEEKRT-MLDGVYELSAKVSQSAVIKEkverqidymEDEKIKCSEIRKVTKQQSSIGLTPPIEE 3030
Cdd:PTZ00121  1579 ALRKAEEA------KKAEEARIeEVMKLYEEEKKMKAEEAKKA---------EEAKIKAEELKKAEEEKKKVEQLKKKEA 1643


                   ..
gi 2023156726 3031 ME 3032
Cdd:PTZ00121  1644 EE 1645
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 80-165 5.56e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 44.42  E-value: 5.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726   80 LASKEGHVEVVSELIQRGASVDAATKKGNTALHIASLA----GQAEVVKVLVTNRANVNAQSQNGFTPL--YMAAQENHL 153
Cdd:PHA02859    59 LEKDKVNVEILKFLIENGADVNFKTRDNNLSALHHYLSfnknVEPEILKILIDSGSSITEEDEDGKNLLhmYMCNFNVRI 138

                           90
                   ....*....|..
gi 2023156726  154 EVVKFLLDNGAS 165
Cdd:PHA02859   139 NVIKLLIDSGVS 150
PHA02798 PHA02798
ankyrin-like protein; Provisional
 677-835 5.79e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 45.98  E-value: 5.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  677 VDMVSLLL-TRNANVnLGNKSGLTPLHLAAQDDRVNVAEVLVNQGAAVDAQTKMGYTPLhvgCH-YGNIK-------IVN 747
Cdd:PHA02798    18 LSTVKLLIkSCNPNE-IVNEYSIFQKYLQRDSPSTDIVKLFINLGANVNGLDNEYSTPL---CTiLSNIKdykhmldIVK 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  748 FLLQHSAKVNAKTKNGYTPLHQAAQQGHTH---IINVLLQHGAAPNELTVNGNTALAIAKRLGYISVVDTLKVVTEETMT 824
Cdd:PHA02798    94 ILIENGADINKKNSDGETPLYCLLSNGYINnleILLFMIENGADTTLLDKDGFTMLQVYLQSNHHIDIEIIKLLLEKGVD 173

                          170
                   ....*....|.
gi 2023156726  825 TITVTEKHKMN 835
Cdd:PHA02798   174 INTHNNKEKYD 184
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 300-327 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 2023156726   300 DGLTPLHCGARSGHEQVVEMLLDRGAPI 327
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 231-421 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 2023156726  231 ESKSGFTPLHIAA---HYGNINVATLLLNrgAAVDFTARNDI-------------TPLHVASKRGNANMVKLLLDRGAKI 294
Cdd:cd21882     22 RGATGKTCLHKAAlnlNDGVNEAIMLLLE--AAPDSGNPKELvnapctdefyqgqTALHIAIENRNLNLVRLLVENGADV 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  295 DAKTRD-------------GLTPLHCGARSGHEQVVEMLLDRGAPILSKTKN---GLSPLHMatqgdhlncvqLLIQHNV 358
Cdd:cd21882    100 SARATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPAALEAQdslGNTVLHA-----------LVLQADN 168

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2023156726  359 PVDD---VTNDYLTALHVAAHCGHykvakvLLDKKANPNAKalnGFTPLHIACKKNRIKVMELLLK 421
Cdd:cd21882    169 TPENsafVCQMYNLLLSYGAHLDP------TQQLEEIPNHQ---GLTPLKLAAVEGKIVMFQHILQ 225
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 382-539 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 2023156726  382 VAKVLLDKKANPNAKAL-NGFTPLH--IACKKN-RIKVMELLLKHGASIQAVTESGLTPIHVaaFMGHVNIvsqlmhhga 457
Cdd:PHA02859    68 ILKFLIENGADVNFKTRdNNLSALHhyLSFNKNvEPEILKILIDSGSSITEEDEDGKNLLHM--YMCNFNV--------- 136

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  458 spnttnvrgetalhmaaragQTEVVRYLVQNGAQVEAKAKDDQTPLHiSARLGKAD--IVQQLLQQGASPNAATTSGYTP 535
Cdd:PHA02859   137 --------------------RINVIKLLIDSGVSFLNKDFDNNNILY-SYILFHSDkkIFDFLTSLGIDINETNKSGYNC 195


                   ....
gi 2023156726  536 LHLS 539
Cdd:PHA02859   196 YDLI 199
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 369-424 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 2023156726  369 TALHVAAHCGHYKVAKVLLdKKANPNAKALNGF--TPLHIACKKNRIKVMELLLKHGA 424
Cdd:PHA02736    94 TPLHIAVYTQNYELATWLC-NQPGVNMEILNYAfkTPYYVACERHDAKMMNILRAKGA 150
PHA02917 PHA02917
ankyrin-like protein; Provisional
 365-803 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 2023156726  365 NDYLTALHVAAHCGHYKVAKVLLDKKANPNAKALNGFTPLHIACKKNRIKVMELLLKhgASIQAVTESGLTPIHVAAFMG 444
Cdd:PHA02917    33 NNALHAYLFNEHCNNVEVVKLLLDSGTNPLHKNWRQLTPLEEYTNSRHVKVNKDIAM--ALLEATGYSNINDFNIFSYMK 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  445 H----VNIVSQLMHHG--ASPNTTNVRGETALHMAARAGQTEVVRYLVQNGAQVEAKAKDDQ--------------TPLH 504
Cdd:PHA02917   111 SknvdVDLIKVLVEHGfdLSVKCENHRSVIENYVMTDDPVPEIIDLFIENGCSVLYEDEDDEygyayddyqprncgTVLH 190

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  505 ---ISARLGKAD--------IVQQLLQQGASPNAATTSGYTPLHLSAREGHEDVASVLL-----DHGASLSI----ITKK 564
Cdd:PHA02917   191 lyiISHLYSESDtrayvrpeVVKCLINHGIKPSSIDKNYCTALQYYIKSSHIDIDIVKLlmkgiDNTAYSYIddltCCTR 270

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  565 GFTP--LHVAAKYGK---IEVANLLLQkNASPDASGKSgLTPLHvaaHYDNQKVALLLldqgasphaSAKNGYTPLHIAA 639
Cdd:PHA02917   271 GIMAdyLNSDYRYNKdvdLDLVKLFLE-NGKPHGIMCS-IVPLW---RNDKETISLIL---------KTMNSDVLQHILI 336

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  640 KKNQM-DIATTLLEYGADANAVTRQgiAPVHLASQDGHVDMVSLLLTrnanvnLGNKSGLTPLHLaaQDDRVNVAEVLVN 718
Cdd:PHA02917   337 EYMTFgDIDIPLVECMLEYGAVVNK--EAIHGYFRNINIDSYTMKYL------LKKEGGDAVNHL--DDGEIPIGHLCKS 406

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  719 QGAAVDAQT---KMGYTPLHVGCHYgnIKIVNFLLQHSAKVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAAPNELTVN 795
Cdd:PHA02917   407 NYGCYNFYTytyKKGLCDMSYACPI--LSTINICLPYLKDINMIDKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNN 484


                   ....*...
gi 2023156726  796 GNTALAIA 803
Cdd:PHA02917   485 GYTCIAIA 492
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 631-784 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 2023156726  631 GYTPLHIAAKKNQMDIATTLLEYGADanavtrqgiapVHlASQDGHvdmvslLLTRNANVNLgnKSGLTPLHLAAQDDRV 710
Cdd:cd22197     94 GHSALHIAIEKRSLQCVKLLVENGAD-----------VH-ARACGR------FFQKKQGTCF--YFGELPLSLAACTKQW 153

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  711 NVAEVLVN---QGAAVDAQTKMGYTPLHVGCHYGN---------IKIVNFLLQHSAKVNAKTK-------NGYTPLHQAA 771
Cdd:cd22197    154 DVVNYLLEnphQPASLQAQDSLGNTVLHALVMIADnspensalvIKMYDGLLQAGARLCPTVQleeisnhEGLTPLKLAA 233

                          170
                   ....*....|...
gi 2023156726  772 QQGHTHIINVLLQ 784
Cdd:cd22197    234 KEGKIEIFRHILQ 246
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 433-460 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 2023156726   433 GLTPIHVAAFMGHVNIVSQLMHHGASPN 460
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 598-626 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 2023156726  598 GLTPLHVAA-HYDNQKVALLLLDQGASPHA 626
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNA 31
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 71-164 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 2023156726   71 NQNGLNALHLASKEGHVEVVSE---LIQRGASVDAATKK-GNTALHIASLAGQAEVVKVLVtNRANVNAQSQNGF--TPL 144
Cdd:PHA02736    52 NRHGKQCVHIVSNPDKADPQEKlklLMEWGADINGKERVfGNTPLHIAVYTQNYELATWLC-NQPGVNMEILNYAfkTPY 130

                           90       100
                   ....*....|....*....|
gi 2023156726  145 YMAAQENHLEVVKFLLDNGA 164
Cdd:PHA02736   131 YVACERHDAKMMNILRAKGA 150
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 333-365 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 2023156726  333 NGLSPLHMA-TQGDHLNCVQLLIQHNVPVDDVTN 365
Cdd:pfam00023    1 DGNTPLHLAaGRRGNLEIVKLLLSKGADVNARDK 34
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 366-395 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 2023156726  366 DYLTALHVAAHCGHYKVAKVLLDKKANPNA 395
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 697-728 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 2023156726  697 GLTPLHLAA-QDDRVNVAEVLVNQGAAVDAQTK 728
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
TRPV4 cd22195
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed ...
 465-580 1.78e-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: 1.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  465 RGETALHMAARAGQTEVVRYLVQNGAQVEAKA-------KDD-------QTPLHISARLGKADIVQQLLQQG---ASPNA 527
Cdd:cd22195    136 RGQTALHIAIERRCKHYVELLVEKGADVHAQArgrffqpKDEggyfyfgELPLSLAACTNQPDIVHYLTENAhkkADLRR 215

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2023156726  528 ATTSGYTPLHL------SAREGHEDVASV---LLDHGASL-------SIITKKGFTPLHVAAKYGKIEV 580
Cdd:cd22195    216 QDSRGNTVLHAlvaiadNTRENTKFVTKMydlLLIKCAKLypdcnleAILNNDGMSPLMMAAKLGKIGI 284
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 300-327 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 2023156726  300 DGLTPLHCGARSGHEQVVEMLLDRGAPI 327
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 640-770 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 2023156726  640 KKNQMDIATTL-----LEYGADANAVTRQGIAPvhlasqdghvdmvsllltrNANVNLGNKSGLTPLHLAAQDDRVNVAE 714
Cdd:PHA02884    27 KKNKICIANILyssikFHYTDIIDAILKLGADP-------------------EAPFPLSENSKTNPLIYAIDCDNDDAAK 87

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2023156726  715 VLVNQGAAVDAQTK-MGYTPLHVGCHYGNIKIVNFLLQHSAKVNAKTKNGYTPLHQA 770
Cdd:PHA02884    88 LLIRYGADVNRYAEeAKITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELA 144
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 564-593 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 2023156726  564 KGFTPLHVAAKYGKIEVANLLLQKNASPDA 593
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Death_NMPP84 cd08318
Death domain of Nuclear Matrix Protein P84; Death domain (DD) found in the Nuclear Matrix ...
 4063-4139 2.65e-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: 2.65e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2023156726 4063 TDIRMAIVADHLGLSWTELARELNFSVDEINQIRvENPNSLIAQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDI 4139
Cdd:cd08318      6 TSEQIDVLANKLGEQWKTLAPYLEMKDKDIRQIE-SDSEDMKMRAKQLLVTWQDREGAQATPEILMTALNAAGLNEI 81
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 59-198 2.78e-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: 2.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726   59 DYLKSGVDINISNQ--NGLNALHLASKEGHVEVVSELIQRGASVDAAT-----KK---------GNTALHIASLAGQAEV 122
Cdd:cd22196     77 GNLKEFVNAAYTDSyyKGQTALHIAIERRNMHLVELLVQNGADVHARAsgeffKKkkggpgfyfGELPLSLAACTNQLDI 156

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  123 VKVLVTN---RANVNAQSQNGFTPLY--MAAQENHLEVVKF-------LLDNGAS-------QSLATEDGFTPLAVALQQ 183
Cdd:cd22196    157 VKFLLENphsPADISARDSMGNTVLHalVEVADNTPENTKFvtkmyneILILGAKirpllklEEITNKKGLTPLKLAAKT 236

                          170
                   ....*....|....*
gi 2023156726  184 GHDQVVSLLLENDTK 198
Cdd:cd22196    237 GKIGIFAYILGREIK 251
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 631-784 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 2023156726  631 GYTPLHIAAKKNQMDIATTLLEYGADANAVtrqgiapvhlASQDghvdmvsllLTRNANVNLGNKSGLTPLHLAAQDDRV 710
Cdd:cd22196     94 GQTALHIAIERRNMHLVELLVQNGADVHAR----------ASGE---------FFKKKKGGPGFYFGELPLSLAACTNQL 154

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  711 NVAEVLVN---QGAAVDAQTKMGYTPLH---------------VGCHYGNIKIVNFLLQHSAKVNAKT-KNGYTPLHQAA 771
Cdd:cd22196    155 DIVKFLLEnphSPADISARDSMGNTVLHalvevadntpentkfVTKMYNEILILGAKIRPLLKLEEITnKKGLTPLKLAA 234

                          170
                   ....*....|...
gi 2023156726  772 QQGHTHIINVLLQ 784
Cdd:cd22196    235 KTGKIGIFAYILG 247
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 139-165 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 2023156726  139 NGFTPLYMAAQENHLEVVKFLLDNGAS 165
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGAD 27
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 235-262 2.99e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.01  E-value: 2.99e-03
                           10        20
                   ....*....|....*....|....*...
gi 2023156726  235 GFTPLHIAAHYGNINVATLLLNRGAAVD 262
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADIN 29
PHA02791 PHA02791
ankyrin-like protein; Provisional
 228-426 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 2023156726  228 ADVEsksGFTPLHIAAHYGNINVATLLLNRGAAVDFTaRNDItPLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPLHC 307
Cdd:PHA02791    26 ADVH---GHSALYYAIADNNVRLVCTLLNAGALKNLL-ENEF-PLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYY 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  308 GARSGHEQVVEMLLDRGAPILSKTKNGL-SPLHMATQGDHLNCVQLLIQHnVPVDDVTNDYLTALHVAAHCGHYKVAKVL 386
Cdd:PHA02791   101 AVDSGNMQTVKLFVKKNWRLMFYGKTGWkTSFYHAVMLNDVSIVSYFLSE-IPSTFDLAILLSCIHITIKNGHVDMMILL 179

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 2023156726  387 LDKKANPNAKALNGFTP-LHIACKKNRIKVMELLLKHGASI 426
Cdd:PHA02791   180 LDYMTSTNTNNSLLFIPdIKLAIDNKDLEMLQALFKYDINI 220
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 121-181 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 2023156726  121 EVVKVLVTNRANVNAQSQ-NGFTPL--YMAAQEN-HLEVVKFLLDNGASQSLATEDGFTPLAVAL 181
Cdd:PHA02859    67 EILKFLIENGADVNFKTRdNNLSALhhYLSFNKNvEPEILKILIDSGSSITEEDEDGKNLLHMYM 131
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 741-803 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 2023156726  741 GNIKIVNFLLQHSAKVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAAPNELTVNGNTAL--AIA 803
Cdd:PLN03192   536 GNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnAIS 600
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 498-527 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 2023156726   498 DDQTPLHISARLGKADIVQQLLQQGASPNA 527
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 532-560 3.86e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.62  E-value: 3.86e-03
                           10        20
                   ....*....|....*....|....*....
gi 2023156726  532 GYTPLHLSAREGHEDVASVLLDHGASLSI 560
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 500-642 4.51e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 41.73  E-value: 4.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  500 QTPLHISARLGKA--DIVQQLLQQGASPNAATT-SGYTPLH--LSAREG-HEDVASVLLDHGASLSIITKKGFTPLHVAA 573
Cdd:PHA02859    52 ETPIFSCLEKDKVnvEILKFLIENGADVNFKTRdNNLSALHhyLSFNKNvEPEILKILIDSGSSITEEDEDGKNLLHMYM 131

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2023156726  574 K--YGKIEVANLLLQKNASPDASGKSGLTPLHVAAHY-DNQKVALLLLDQGASPHASAKNGYTPLHIAAKKN 642
Cdd:PHA02859   132 CnfNVRINVIKLLIDSGVSFLNKDFDNNNILYSYILFhSDKKIFDFLTSLGIDINETNKSGYNCYDLIKFRN 203
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 267-296 4.79e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.24  E-value: 4.79e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 2023156726  267 NDITPLHVASKRGNANMVKLLLDRGAKIDA 296
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 333-362 5.71e-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: 5.71e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 2023156726   333 NGLSPLHMATQGDHLNCVQLLIQHNVPVDD 362
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 153-323 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 2023156726  153 LEVVKFLLDNGASQSLATedGFTPLAVA---LQQGHDQVVSLLLENDTKGKVRLP---------------ALHIAARKDD 214
Cdd:cd21882      8 LECLRWYLTDSAYQRGAT--GKTCLHKAalnLNDGVNEAIMLLLEAAPDSGNPKElvnapctdefyqgqtALHIAIENRN 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  215 TKAAALLLQNdhNADVESKS---------------GFTPLHIAAHYGNINVATLLLNRGAAV-DFTARNDI--TPLHVAS 276
Cdd:cd21882     86 LNLVRLLVEN--GADVSARAtgrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPaALEAQDSLgnTVLHALV 163

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2023156726  277 KRGN---------ANMVKLLLDRGAKID-------AKTRDGLTPLHCGARSGHEQVVEMLLDR 323
Cdd:cd21882    164 LQADntpensafvCQMYNLLLSYGAHLDptqqleeIPNHQGLTPLKLAAVEGKIVMFQHILQR 226
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 237-333 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 2023156726  237 TPLHIAAHYGNINVATLLLNRGAAVD-FTARNDITPLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPLHCGARSGHEQ 315
Cdd:PHA02884    72 NPLIYAIDCDNDDAAKLLIRYGADVNrYAEEAKITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELALMICNNF 151

                           90
                   ....*....|....*...
gi 2023156726  316 VVEMLLDRGAPILSKTKN 333
Cdd:PHA02884   152 LAFMICDNEISNFYKHPK 169
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 498-527 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 2023156726  498 DDQTPLHISARLGKADIVQQLLQQGASPNA 527
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Death_MyD88 cd08312
Death domain of Myeloid Differentation primary response protein MyD88; Death Domain (DD) of ...
 4060-4143 7.77e-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: 7.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726 4060 CERTDIRMAIVADhlglsWTELARELNFSVDEINQI-RVENPnsliaqSFMLLKKWVTRDgKNATTDALTSVLTKINRID 4138
Cdd:cd08312      6 SLYLNPEKVVAND-----WRGLAELMGFDYLEIRNFeRQSSP------TERLLEDWETRP-PGATVGNLLEILEELERKD 73


                   ....*
gi 2023156726 4139 IVTLL 4143
Cdd:cd08312     74 VLEDL 78
PHA02946 PHA02946
ankyin-like protein; Provisional
 239-488 7.81e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 42.35  E-value: 7.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  239 LHIAAHYGNINVaTLLLNRGAAVDFTARNDITPLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPLHCGARSGHEQVVE 318
Cdd:PHA02946    11 LSLYAKYNSKNL-DVFRNMLQAIEPSGNYHILHAYCGIKGLDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVA 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  319 MLLDRGAPILSKTKNGLSPLHM--ATQGDHLNCVQLLIQHNVPVDDVTNDYLTALHVAAHCGHYKVAKVLL--------- 387
Cdd:PHA02946    90 MLLTHGADPNACDKQHKTPLYYlsGTDDEVIERINLLVQYGAKINNSVDEEGCGPLLACTDPSERVFKKIMsigfeariv 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  388 DK-----------KANPNAKAL---------------NGFTPLHIACKKN--RIKVMELLL---------KHGASIQAVT 430
Cdd:PHA02946   170 DKfgknhihrhlmSDNPKASTIswmmklgispskpdhDGNTPLHIVCSKTvkNVDIINLLLpstdvnkqnKFGDSPLTLL 249

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  431 ESGLTPIH-VAAFMGHVNIVSQ-------LMHHGASPNTTNVRGE----TALHMAARAGQTEVVRYLVQN 488
Cdd:PHA02946   250 IKTLSPAHlINKLLSTSNVITDqtvniciFYDRDDVLEIINDKGKqydsTDFKMAVEVGSIRCVKYLLDN 319
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 492-633 8.48e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 41.51  E-value: 8.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156726  492 VEAKAKDDQTP-LHISARLGKADIVQQLLQQGASPNA----ATTSGYTPLHLSAREGHEDVASVLLDHGASLSIITKKG- 565
Cdd:PHA02884    25 IKKKNKICIANiLYSSIKFHYTDIIDAILKLGADPEApfplSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAk 104

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2023156726  566 FTPLHVAAKYGKIEVANLLLQKNASPDASGKSGLTPLHVAAHYDNQKVALLLLDQGASPHASAKNGYT 633
Cdd:PHA02884   105 ITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELALMICNNFLAFMICDNEISNFYKHPKKIL 172
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 598-626 9.42e-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: 9.42e-03
                            10        20
                    ....*....|....*....|....*....
gi 2023156726   598 GLTPLHVAAHYDNQKVALLLLDQGASPHA 626
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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