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Conserved domains on  [gi|1831513053|ref|NP_001368407|]
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Ankyrin-2 [Caenorhabditis elegans]

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];
345-627 5.00e-59

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 205.57  E-value: 5.00e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  345 LLYHRAPVDDVTVDYLTPLHVAAHCGHVRVAKLLLDRSADPNSRALNGFTPLHIACKKNRIKVVELLLKYRAAIEATTES 424
Cdd:COG0666      7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  425 GLTPLHVAAFMGAINIVIYLLQQGANPDVETVRGETPLHLAARANQTDVVRVLIRNGAKVDAQARELQTPLHIASRLGNT 504
Cdd:COG0666     87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  505 DIVILLLQAGANSNATTRDNYSPLHIAAKEGQEEVAGILLDHNADKTLLTKKGFTPLHLASKYGNLEVVRLLLERGTPVD 584
Cdd:COG0666    167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1831513053  585 IEGKNQVTPLHVAAHYNNDKVAMLLLENGASAKAAAKNGYTPL 627
Cdd:COG0666    247 AKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
505-792 1.33e-53

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 190.17  E-value: 1.33e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  505 DIVILLLQAGANSNATTRDNYSPLHIAAKEGQEEVAGILLDHNADKTLLTKKGFTPLHLASKYGNLEVVRLLLERGTPVD 584
Cdd:COG0666      2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  585 IEGKNQVTPLHVAAHYNNDKVAMLLLENGASAKAAAKNGYTPLHIAAKKNQMEIASTLLQFKADPNAKSRAGFTPLHLSA 664
Cdd:COG0666     82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  665 QEGHKEISGLLIENGSDVGAKANNGLTAMHLCAQEDHVPVAQILYNNGAEINSKTNAGYTPLHVACHFGQLNMVKFLVEN 744
Cdd:COG0666    162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1831513053  745 GADVGEKTRASYTPLHQAAQQGHNNCVRYLLENGASPNEQTATGQTPL 792
Cdd:COG0666    242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
184-462 1.12e-51

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 184.39  E-value: 1.12e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  184 LLENDSKGKVRLPALHIAAKKDDTTAATLLLQNEHNPDVTSKSGFTPLHIAAHYGHENVGQLLLEKGANVNYQARHNISP 263
Cdd:COG0666     11 LLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTL 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  264 LHVATKWGRTNMANLLLSRGAIIDSRTKDLLTPLHCAARSGHDQVVDLLVVQGAPISAKTKNGLAPLHMAAQGDHVDAAR 343
Cdd:COG0666     91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  344 TLLYHRAPVDDVTVDYLTPLHVAAHCGHVRVAKLLLDRSADPNSRALNGFTPLHIACKKNRIKVVELLLKYRAAIEATTE 423
Cdd:COG0666    171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1831513053  424 SGLTPLHVAAFMGAINIVIYLLQQGANPDVETVRGETPL 462
Cdd:COG0666    251 DGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
UPA_2 super family cl39303
UPA domain; The UPA domain is conserved in UNC5, PIDD, and Ankyrins. It has a beta sandwich ...
1337-1472 2.99e-48

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: 168.42  E-value: 2.99e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053 1337 IPYMAKFAVFARRTFPVEGQLRVFCMTDDKEDKTLEKQEHFKLIAKSRDVEVLKGKHQFLEFSGNLVPITKSGDQLSLFF 1416
Cdd:pfam17809    1 VPYLAKFVVFAKRYDPGEARLRCACMTDDGEDKTLEFHEGFTEVARSRDVEVLEGSPVSIELSGNLVPIKKKSQSRQMDF 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1831513053 1417 LPFQENRLAFMVKTRsndDNEAATEGRIGFMAEPKIRSDAlpPQQPICTLAISLPE 1472
Cdd:pfam17809   81 KAFRENRLDGSVRVK---DPSDPPKGLLSFMRDAKVDGGT--VSQPLCTLNIVLPQ 131
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
1008-1110 1.98e-47

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


:

Pssm-ID: 128514  Cd Length: 104  Bit Score: 164.83  E-value: 1.98e-47
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  1008 FLISFLVDARGGAMRGCRhSGVRIIVPPRKASQPIRVTCRYLRKDKLAHPPPLSEGEELASRILEMAPAGAKFLGPVILE 1087
Cdd:smart00218    3 FLVSGTFDARGGRLRGPR-TGVRLIIPPGAIPQGTRYTCYLVVHKTLSTPPPLEEGETLLSPVVECGPHGALFLRPVILE 81
                            90       100
                    ....*....|....*....|...
gi 1831513053  1088 VPHFASLRDREREIVILRSDDGQ 1110
Cdd:smart00218   82 VPHCASLRPRDWEIVLLRSENGG 104
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
30-297 6.81e-47

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 170.52  E-value: 6.81e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053   30 RAEGSASFLRAARAGDLEKVLELLRAGTDINTSNANGLNSLHLASKEGHSEVVRELIKRQAQVDAATRKGNTALHIASLA 109
Cdd:COG0666     51 DALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYN 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  110 GQSLIVTILVENGANVNVQSVNGFTPLYMAAQENHEEVVKYLLKHGANQALSTEDGFTPLAVALQQGHDRVVAVLLENDS 189
Cdd:COG0666    131 GNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA 210
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  190 kgkvrlpalhiaakkddttaatlllqnehNPDVTSKSGFTPLHIAAHYGHENVGQLLLEKGANVNYQARHNISPLHVATK 269
Cdd:COG0666    211 -----------------------------DVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAA 261
                          250       260
                   ....*....|....*....|....*...
gi 1831513053  270 WGRTNMANLLLSRGAIIDSRTKDLLTPL 297
Cdd:COG0666    262 AGAALIVKLLLLALLLLAAALLDLLTLL 289
Death_ank cd08317
Death domain associated with Ankyrins; Death Domain (DD) associated with Ankyrins. Ankyrins ...
1503-1580 5.31e-26

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: 103.11  E-value: 5.31e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053 1503 PEFVHQNVLKGIGADWPRLGRALEVPHRDIQHIRQNYPG---QECKNTLKIWIHLKKEDANQDNLDQALRQIGRDDIVRS 1579
Cdd:cd08317      3 ADLRLSDIANLLGSDWPELARELGVSEEDIDLIRSENPNslaQQAMAMLRLWLEREGEKATGNALESALKKIGRDDIVEK 82

                   .
gi 1831513053 1580 I 1580
Cdd:cd08317     83 C 83
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
345-627 5.00e-59

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 205.57  E-value: 5.00e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  345 LLYHRAPVDDVTVDYLTPLHVAAHCGHVRVAKLLLDRSADPNSRALNGFTPLHIACKKNRIKVVELLLKYRAAIEATTES 424
Cdd:COG0666      7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  425 GLTPLHVAAFMGAINIVIYLLQQGANPDVETVRGETPLHLAARANQTDVVRVLIRNGAKVDAQARELQTPLHIASRLGNT 504
Cdd:COG0666     87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  505 DIVILLLQAGANSNATTRDNYSPLHIAAKEGQEEVAGILLDHNADKTLLTKKGFTPLHLASKYGNLEVVRLLLERGTPVD 584
Cdd:COG0666    167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1831513053  585 IEGKNQVTPLHVAAHYNNDKVAMLLLENGASAKAAAKNGYTPL 627
Cdd:COG0666    247 AKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
505-792 1.33e-53

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 190.17  E-value: 1.33e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  505 DIVILLLQAGANSNATTRDNYSPLHIAAKEGQEEVAGILLDHNADKTLLTKKGFTPLHLASKYGNLEVVRLLLERGTPVD 584
Cdd:COG0666      2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  585 IEGKNQVTPLHVAAHYNNDKVAMLLLENGASAKAAAKNGYTPLHIAAKKNQMEIASTLLQFKADPNAKSRAGFTPLHLSA 664
Cdd:COG0666     82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  665 QEGHKEISGLLIENGSDVGAKANNGLTAMHLCAQEDHVPVAQILYNNGAEINSKTNAGYTPLHVACHFGQLNMVKFLVEN 744
Cdd:COG0666    162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1831513053  745 GADVGEKTRASYTPLHQAAQQGHNNCVRYLLENGASPNEQTATGQTPL 792
Cdd:COG0666    242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
184-462 1.12e-51

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 184.39  E-value: 1.12e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  184 LLENDSKGKVRLPALHIAAKKDDTTAATLLLQNEHNPDVTSKSGFTPLHIAAHYGHENVGQLLLEKGANVNYQARHNISP 263
Cdd:COG0666     11 LLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTL 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  264 LHVATKWGRTNMANLLLSRGAIIDSRTKDLLTPLHCAARSGHDQVVDLLVVQGAPISAKTKNGLAPLHMAAQGDHVDAAR 343
Cdd:COG0666     91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  344 TLLYHRAPVDDVTVDYLTPLHVAAHCGHVRVAKLLLDRSADPNSRALNGFTPLHIACKKNRIKVVELLLKYRAAIEATTE 423
Cdd:COG0666    171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1831513053  424 SGLTPLHVAAFMGAINIVIYLLQQGANPDVETVRGETPL 462
Cdd:COG0666    251 DGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
UPA_2 pfam17809
UPA domain; The UPA domain is conserved in UNC5, PIDD, and Ankyrins. It has a beta sandwich ...
1337-1472 2.99e-48

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: 168.42  E-value: 2.99e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053 1337 IPYMAKFAVFARRTFPVEGQLRVFCMTDDKEDKTLEKQEHFKLIAKSRDVEVLKGKHQFLEFSGNLVPITKSGDQLSLFF 1416
Cdd:pfam17809    1 VPYLAKFVVFAKRYDPGEARLRCACMTDDGEDKTLEFHEGFTEVARSRDVEVLEGSPVSIELSGNLVPIKKKSQSRQMDF 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1831513053 1417 LPFQENRLAFMVKTRsndDNEAATEGRIGFMAEPKIRSDAlpPQQPICTLAISLPE 1472
Cdd:pfam17809   81 KAFRENRLDGSVRVK---DPSDPPKGLLSFMRDAKVDGGT--VSQPLCTLNIVLPQ 131
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
1008-1110 1.98e-47

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


Pssm-ID: 128514  Cd Length: 104  Bit Score: 164.83  E-value: 1.98e-47
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  1008 FLISFLVDARGGAMRGCRhSGVRIIVPPRKASQPIRVTCRYLRKDKLAHPPPLSEGEELASRILEMAPAGAKFLGPVILE 1087
Cdd:smart00218    3 FLVSGTFDARGGRLRGPR-TGVRLIIPPGAIPQGTRYTCYLVVHKTLSTPPPLEEGETLLSPVVECGPHGALFLRPVILE 81
                            90       100
                    ....*....|....*....|...
gi 1831513053  1088 VPHFASLRDREREIVILRSDDGQ 1110
Cdd:smart00218   82 VPHCASLRPRDWEIVLLRSENGG 104
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
30-297 6.81e-47

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 170.52  E-value: 6.81e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053   30 RAEGSASFLRAARAGDLEKVLELLRAGTDINTSNANGLNSLHLASKEGHSEVVRELIKRQAQVDAATRKGNTALHIASLA 109
Cdd:COG0666     51 DALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYN 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  110 GQSLIVTILVENGANVNVQSVNGFTPLYMAAQENHEEVVKYLLKHGANQALSTEDGFTPLAVALQQGHDRVVAVLLENDS 189
Cdd:COG0666    131 GNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA 210
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  190 kgkvrlpalhiaakkddttaatlllqnehNPDVTSKSGFTPLHIAAHYGHENVGQLLLEKGANVNYQARHNISPLHVATK 269
Cdd:COG0666    211 -----------------------------DVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAA 261
                          250       260
                   ....*....|....*....|....*...
gi 1831513053  270 WGRTNMANLLLSRGAIIDSRTKDLLTPL 297
Cdd:COG0666    262 AGAALIVKLLLLALLLLAAALLDLLTLL 289
ZU5 pfam00791
ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.
1011-1107 7.09e-42

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: 7.09e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053 1011 SFLVDARGGAMRGCrHSGVRIIVPPRKASQPIRVTCRYLRKDKLAHPPPLSEGEELASRILEMAPAGAKFLGPVILEVPH 1090
Cdd:pfam00791    2 SGLVDSRGGRLVLP-NSGVSLLIPPGAIPEGTRIECYLAVNRDESSRPPLEEGETLLSPVVECGPPGLKFLKPVILEVPH 80
                           90
                   ....*....|....*..
gi 1831513053 1091 FASLRDREREIVILRSD 1107
Cdd:pfam00791   81 CASLRPEEWEIVLKRSD 97
PHA02876 PHA02876
ankyrin repeat protein; Provisional
242-648 1.69e-36

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 149.06  E-value: 1.69e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  242 VGQLLLEKGANVNYQARHNISPLHVATKWGRTNMANLLLSRGAIIDSRTKDLLTPLHCAARSGHDQVVDLLVVQGAPISa 321
Cdd:PHA02876   160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNIN- 238
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  322 ktKNGLAPLHMAAQGDhvdaartllyhrapvddvtvdyltplhvaahcghVRVAKLLLDRSADPNSRALNGFTPLHiack 401
Cdd:PHA02876   239 --KNDLSLLKAIRNED----------------------------------LETSLLLYDAGFSVNSIDDCKNTPLH---- 278
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  402 knrikvvelllkyrAAIEATTESGLTPlhvaafmgainiviYLLQQGANPDVETVRGETPLHLAAR-ANQTDVVRVLIRN 480
Cdd:PHA02876   279 --------------HASQAPSLSRLVP--------------KLLERGADVNAKNIKGETPLYLMAKnGYDTENIRTLIML 330
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  481 GAKVDAQARELQTPLHIASRLG-NTDIVILLLQAGANSNATTRDNYSPLHIAAKEGQEEVAGILLDHNADKTLLTKKGFT 559
Cdd:PHA02876   331 GADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGT 410
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  560 PLHLAsKYGN--LEVVRLLLERGTPVDIEGKNQVTPLHVAAHYN-NDKVAMLLLENGASAKAAAKNGYTPLHIAAKKNQm 636
Cdd:PHA02876   411 ALHFA-LCGTnpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIALEYHG- 488
                          410
                   ....*....|..
gi 1831513053  637 eIASTLLQFKAD 648
Cdd:PHA02876   489 -IVNILLHYGAE 499
PHA03100 PHA03100
ankyrin repeat protein; Provisional
555-780 7.94e-36

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 142.50  E-value: 7.94e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  555 KKGFTPLHLASKYGNLEVVRLLLERGTPVDIEGKNQVTPLHVAAHY-----NNDKVAMLLLENGASAKAAAKNGYTPLHI 629
Cdd:PHA03100    33 KKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIkynltDVKEIVKLLLEYGANVNAPDNNGITPLLY 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  630 AA--KKNQMEIASTLLQFKADPNAKSRAGFTPLHLSAQEGH--KEISGLLIENGSDVGAKanngltamhlcaqeDHVpva 705
Cdd:PHA03100   113 AIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAK--------------NRV--- 175
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1831513053  706 QILYNNGAEINSKTNAGYTPLHVACHFGQLNMVKFLVENGADVGEKTRASYTPLHQAAQQGHNNCVRYLLENGAS 780
Cdd:PHA03100   176 NYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
PHA03095 PHA03095
ankyrin-like protein; Provisional
37-387 2.27e-29

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 123.98  E-value: 2.27e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053   37 FLRAARAgDLEKVLELLRAGTDINTSNANGLNSLHLASKEGHS---EVVRELIKRQAQVDAATRKGNTALHIASLAGQSL 113
Cdd:PHA03095    19 LLNASNV-TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEkvkDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTL 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  114 -IVTILVENGANVNVQSVNGFTPL--YMAAQENHEEVVKYLLKHGANQALSTEDGFTPLAVALQQGH--DRVVAVLLEND 188
Cdd:PHA03095    98 dVIKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanVELLRLLIDAG 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  189 SkgkvrlpalHIAAKKDDttaatlllqnehnpdvtsksGFTPLHIAAHYGHENVGQL--LLEKGANVNYQARHNISPLHV 266
Cdd:PHA03095   178 A---------DVYAVDDR--------------------FRSLLHHHLQSFKPRARIVreLIRAGCDPAATDMLGNTPLHS 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  267 ATKWG---RTNMANLLLsRGAIIDSRTKDLLTPLHCAARSGHDQVVDLLVVQGAPISAKTKNGLAPLHMAAQGDHVDAAR 343
Cdd:PHA03095   229 MATGSsckRSLVLPLLI-AGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVR 307
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 1831513053  344 TLLYHRAPVDDV--TVDYLTPLHVAAHCGHVR--VAKLLLDR--SADPNS 387
Cdd:PHA03095   308 AALAKNPSAETVaaTLNTASVAGGDIPSDATRlcVAKVVLRGafSLLPEP 357
PHA03100 PHA03100
ankyrin repeat protein; Provisional
47-287 1.99e-26

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 114.38  E-value: 1.99e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053   47 EKVLE-LLRAGTDINTSNANGLNSLHLASKEGHSEV-VRELIKrqaqvdaatrkgntalhiaslagqslivtILVENGAN 124
Cdd:PHA03100    48 IDVVKiLLDNGADINSSTKNNSTPLHYLSNIKYNLTdVKEIVK-----------------------------LLLEYGAN 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  125 VNVQSVNGFTPLYMAAQE--NHEEVVKYLLKHGANQALSTEDGFTPLAVALQQGHD--RVVAVLLENDSKgkvrlpalhI 200
Cdd:PHA03100    99 VNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVD---------I 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  201 AAKkddtTAATLLLQNEHNPDVTSKSGFTPLHIAAHYGHENVGQLLLEKGANVNYQARHNISPLHVATKWGRTNMANLLL 280
Cdd:PHA03100   170 NAK----NRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLL 245

                   ....*..
gi 1831513053  281 SRGAIID 287
Cdd:PHA03100   246 NNGPSIK 252
Death_ank cd08317
Death domain associated with Ankyrins; Death Domain (DD) associated with Ankyrins. Ankyrins ...
1503-1580 5.31e-26

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: 103.11  E-value: 5.31e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053 1503 PEFVHQNVLKGIGADWPRLGRALEVPHRDIQHIRQNYPG---QECKNTLKIWIHLKKEDANQDNLDQALRQIGRDDIVRS 1579
Cdd:cd08317      3 ADLRLSDIANLLGSDWPELARELGVSEEDIDLIRSENPNslaQQAMAMLRLWLEREGEKATGNALESALKKIGRDDIVEK 82

                   .
gi 1831513053 1580 I 1580
Cdd:cd08317     83 C 83
Ank_2 pfam12796
Ankyrin repeats (3 copies);
693-784 7.36e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 94.41  E-value: 7.36e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  693 MHLCAQEDHVPVAQILYNNGAEINSKTNAGYTPLHVACHFGQLNMVKFLVENgADVGEKTRaSYTPLHQAAQQGHNNCVR 772
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
                           90
                   ....*....|..
gi 1831513053  773 YLLENGASPNEQ 784
Cdd:pfam12796   79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
363-453 8.86e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 94.03  E-value: 8.86e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  363 LHVAAHCGHVRVAKLLLDRSADPNSRALNGFTPLHIACKKNRIKVVELLLKYrAAIEATTEsGLTPLHVAAFMGAINIVI 442
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
                           90
                   ....*....|.
gi 1831513053  443 YLLQQGANPDV 453
Cdd:pfam12796   79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
103-190 7.35e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.94  E-value: 7.35e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  103 LHIASLAGQSLIVTILVENGANVNVQSVNGFTPLYMAAQENHEEVVKYLLKHgaNQALSTEDGFTPLAVALQQGHDRVVA 182
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH--ADVNLKDNGRTALHYAARSGHLEIVK 78

                   ....*...
gi 1831513053  183 VLLENDSK 190
Cdd:pfam12796   79 LLLEKGAD 86
Ank_2 pfam12796
Ankyrin repeats (3 copies);
297-388 9.11e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.55  E-value: 9.11e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  297 LHCAARSGHDQVVDLLVVQGAPISAKTKNGLAPLHMAAQGDHVDAARTLLYHRAPvdDVTVDYLTPLHVAAHCGHVRVAK 376
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|..
gi 1831513053  377 LLLDRSADPNSR 388
Cdd:pfam12796   79 LLLEKGADINVK 90
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
361-579 7.78e-18

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: 89.69  E-value: 7.78e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  361 TPLHVAAHCGHVR-VAKLLLDRSADPNSRALNGFTPLHIACKKNRIKVVELLLkyRAAIE-----ATTE--SGLTPLHVA 432
Cdd:cd22192     19 SPLLLAAKENDVQaIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLM--EAAPElvnepMTSDlyQGETALHIA 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  433 AFMGAINIVIYLLQQGAnpDVETVR----------------GETPLHLAARANQTDVVRVLIRNGAKVDAQarelqtplh 496
Cdd:cd22192     97 VVNQNLNLVRELIARGA--DVVSPRatgtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQ--------- 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  497 iaSRLGNTDIVILLLQAGANSNATTRDnyspLHIAAKEGQEEVAgilLDHnadktLLTKKGFTPLHLASKYGNLEVVRLL 576
Cdd:cd22192    166 --DSLGNTVLHILVLQPNKTFACQMYD----LILSYDKEDDLQP---LDL-----VPNNQGLTPFKLAAKEGNIVMFQHL 231

                   ...
gi 1831513053  577 LER 579
Cdd:cd22192    232 VQK 234
Death pfam00531
Death domain;
1499-1582 1.03e-15

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 73.94  E-value: 1.03e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053 1499 EKDLPEFVhqNVLKGIGADWPRLGRALEVPHRDIQHIRQNYP--GQECKNTLKIWIHLKKEDANQDNLDQALRQIGRDDI 1576
Cdd:pfam00531    1 RKQLDRLL--DPPPPLGKDWRELARKLGLSENEIDEIESENPrlRSQTYELLRLWEQREGKNATVGTLLEALRKLGRRDA 78

                   ....*.
gi 1831513053 1577 VRSIAY 1582
Cdd:pfam00531   79 AEKIQS 84
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
1501-1582 1.28e-15

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: 73.60  E-value: 1.28e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  1501 DLPEFVHQNVLKG-IGADWPRLGRALEVPHRDIQHIRQNYPG---QECKNTLKIWIHLKKEDANQDNLDQALRQIGRDDI 1576
Cdd:smart00005    2 ELTRQKLAKLLDHpLGLDWRELARKLGLSEADIDQIRTEAPRdlaEQSVQLLRLWEQREGKNATLGTLLEALRKMGRDDA 81

                    ....*.
gi 1831513053  1577 VRSIAY 1582
Cdd:smart00005   82 VELLRS 87
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
658-794 6.45e-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: 76.98  E-value: 6.45e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  658 TPLHLSAQEGHKE-ISGLLIENGSDVGAKANNGLTAMHLCAQEDHVPVAQILYNNGAE-----INSKTNAGYTPLHVACH 731
Cdd:cd22192     19 SPLLLAAKENDVQaIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElvnepMTSDLYQGETALHIAVV 98
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1831513053  732 FGQLNMVKFLVENGADVgEKTRASYT---------------PLHQAAQQGHNNCVRYLLENGASPNEQTATGQTPLSI 794
Cdd:cd22192     99 NQNLNLVRELIARGADV-VSPRATGTffrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
392-579 5.32e-10

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 64.33  E-value: 5.32e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  392 GFTPLHIACKKNRIK-VVELLLKYRAAIEAttesGLTPLHVAA--FMGAINIVIYLLQQGANPDV-----------ETVR 457
Cdd:TIGR00870   52 GRSALFVAAIENENLeLTELLLNLSCRGAV----GDTLLHAISleYVDAVEAILLHLLAAFRKSGplelandqytsEFTP 127
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  458 GETPLHLAARANQTDVVRVLIRNGAKVDAQA--RELQT------------PLHIASRLGNTDIVILLLQAGANSNATTRD 523
Cdd:TIGR00870  128 GITALHLAAHRQNYEIVKLLLERGASVPARAcgDFFVKsqgvdsfyhgesPLNAAACLGSPSIVALLSEDPADILTADSL 207
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1831513053  524 NYSPLHIAAKEGQEEV------------AGILLDHNADKT----LLTKKGFTPLHLASKYGNLEVVRLLLER 579
Cdd:TIGR00870  208 GNTLLHLLVMENEFKAeyeelscqmynfALSLLDKLRDSKelevILNHQGLTPLKLAAKEGRIVLFRLKLAI 279
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
134-421 1.28e-09

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 63.11  E-value: 1.28e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  134 TPLYMAAQENHEEVVKYLLKHganqalSTEDGFTplavalqqghdrvvavllendsKGKVRLPALHIAAKKDDTTAATLL 213
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLLKC------PSCDLFQ----------------------RGALGETALHVAALYDNLEAAVVL 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  214 LQNEH---NPDVTSK--SGFTPLHIAAHYGHENVGQLLLEKGANVnyqarhnISPLhvATkwgrtnmanlllsrGAIIDS 288
Cdd:cd22192     71 MEAAPelvNEPMTSDlyQGETALHIAVVNQNLNLVRELIARGADV-------VSPR--AT--------------GTFFRP 127
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  289 RTKDLLT----PLHCAARSGHDQVVDLLVVQGAPISAKTKNGLAPLHM-AAQGDHVDAART---LLYHRAPVDDVTVDYL 360
Cdd:cd22192    128 GPKNLIYygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHIlVLQPNKTFACQMydlILSYDKEDDLQPLDLV 207
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1831513053  361 tplhvaahcghvrvakllldrsadPNSRalnGFTPLHIACKKNRIKVVELLLKYRAAIEAT 421
Cdd:cd22192    208 ------------------------PNNQ---GLTPFKLAAKEGNIVMFQHLVQKRRHIQWT 241
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
38-249 2.22e-09

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 62.34  E-value: 2.22e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053   38 LRAARAGDLEKVLELLR-AGTDINTSNANGLNSLHLASKEGHSEVVRELIkrqaqvDAATR-----------KGNTALHI 105
Cdd:cd22192     22 LLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLM------EAAPElvnepmtsdlyQGETALHI 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  106 ASLAGQSLIVTILVENGANVNVQSVNG--FT------------PLYMAAQENHEEVVKYLLKHGANqalstedgftplav 171
Cdd:cd22192     96 AVVNQNLNLVRELIARGADVVSPRATGtfFRpgpknliyygehPLSFAACVGNEEIVRLLIEHGAD-------------- 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  172 alqqghdrvvavLLENDSKGKVrlpALHIAAKKDDTTAAT----LLL-----QNEHNPD-VTSKSGFTPLHIAAHYGHEN 241
Cdd:cd22192    162 ------------IRAQDSLGNT---VLHILVLQPNKTFACqmydLILsydkeDDLQPLDlVPNNQGLTPFKLAAKEGNIV 226

                   ....*...
gi 1831513053  242 VGQLLLEK 249
Cdd:cd22192    227 MFQHLVQK 234
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
110-415 5.75e-07

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 54.70  E-value: 5.75e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  110 GQSLIVTILVENGANVNVQSVN--GFTPLYMAAQEN-HEEVVKYLLKHGANQALstedGFTPLAVALQQGHDRVVAVL-L 185
Cdd:TIGR00870   28 GDLASVYRDLEEPKKLNINCPDrlGRSALFVAAIENeNLELTELLLNLSCRGAV----GDTLLHAISLEYVDAVEAILlH 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  186 ENDSKGKVRLPALHIAAKKDDTTAatlllqnehnpdvtsksGFTPLHIAAHYGHENVGQLLLEKGANVNYQARHN---IS 262
Cdd:TIGR00870  104 LLAAFRKSGPLELANDQYTSEFTP-----------------GITALHLAAHRQNYEIVKLLLERGASVPARACGDffvKS 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  263 PLHVATKWGRtnmanlllsrgaiidsrtkdllTPLHCAARSGHDQVVDLLVVQGAPISAKTKNGLAPLHMAA-QGDHVDA 341
Cdd:TIGR00870  167 QGVDSFYHGE----------------------SPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVmENEFKAE 224
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1831513053  342 ARTLLYHrapVDDVTVDYLtplhvaAHCGHVRVAKLLLDRsadpnsralNGFTPLHIACKKNRIKVVELLL--KYR 415
Cdd:TIGR00870  225 YEELSCQ---MYNFALSLL------DKLRDSKELEVILNH---------QGLTPLKLAAKEGRIVLFRLKLaiKYK 282
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
131-157 1.06e-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: 46.43  E-value: 1.06e-06
                            10        20
                    ....*....|....*....|....*..
gi 1831513053   131 NGFTPLYMAAQENHEEVVKYLLKHGAN 157
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
646-795 3.45e-06

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 52.01  E-value: 3.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  646 KADPNAKSRAGFTPLHLSAQEG-HKEISGLLIENGSDVGAkannGLTAMHLCAQEDHVPVAQIL----------YNNGAE 714
Cdd:TIGR00870   42 KLNINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAV----GDTLLHAISLEYVDAVEAILlhllaafrksGPLELA 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  715 INSKTN---AGYTPLHVACHFGQLNMVKFLVENGADV------GEKTRASYT--------PLHQAAQQGHNNCVRYLLEN 777
Cdd:TIGR00870  118 NDQYTSeftPGITALHLAAHRQNYEIVKLLLERGASVparacgDFFVKSQGVdsfyhgesPLNAAACLGSPSIVALLSED 197
                          170
                   ....*....|....*...
gi 1831513053  778 GASPNEQTATGQTPLSIA 795
Cdd:TIGR00870  198 PADILTADSLGNTLLHLL 215
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
722-748 1.02e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 43.73  E-value: 1.02e-05
                            10        20
                    ....*....|....*....|....*..
gi 1831513053   722 GYTPLHVACHFGQLNMVKFLVENGADV 748
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADI 28
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
391-420 1.81e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.96  E-value: 1.81e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 1831513053   391 NGFTPLHIACKKNRIKVVELLLKYRAAIEA 420
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
227-255 1.38e-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: 1.38e-04
                            10        20
                    ....*....|....*....|....*....
gi 1831513053   227 GFTPLHIAAHYGHENVGQLLLEKGANVNY 255
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
345-627 5.00e-59

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 205.57  E-value: 5.00e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  345 LLYHRAPVDDVTVDYLTPLHVAAHCGHVRVAKLLLDRSADPNSRALNGFTPLHIACKKNRIKVVELLLKYRAAIEATTES 424
Cdd:COG0666      7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  425 GLTPLHVAAFMGAINIVIYLLQQGANPDVETVRGETPLHLAARANQTDVVRVLIRNGAKVDAQARELQTPLHIASRLGNT 504
Cdd:COG0666     87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  505 DIVILLLQAGANSNATTRDNYSPLHIAAKEGQEEVAGILLDHNADKTLLTKKGFTPLHLASKYGNLEVVRLLLERGTPVD 584
Cdd:COG0666    167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1831513053  585 IEGKNQVTPLHVAAHYNNDKVAMLLLENGASAKAAAKNGYTPL 627
Cdd:COG0666    247 AKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
374-660 1.24e-58

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 204.42  E-value: 1.24e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  374 VAKLLLDRSADPNSRALNGFTPLHIACKKNRIKVVELLLKYRAAIEATTESGLTPLHVAAFMGAINIVIYLLQQGANPDV 453
Cdd:COG0666      3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  454 ETVRGETPLHLAARANQTDVVRVLIRNGAKVDAQARELQTPLHIASRLGNTDIVILLLQAGANSNATTRDNYSPLHIAAK 533
Cdd:COG0666     83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  534 EGQEEVAGILLDHNADKTLLTKKGFTPLHLASKYGNLEVVRLLLERGTPVDIEGKNQVTPLHVAAHYNNDKVAMLLLENG 613
Cdd:COG0666    163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1831513053  614 ASAKAAAKNGYTPLHIAAKKNQMEIASTLLQFKADPNAKSRAGFTPL 660
Cdd:COG0666    243 ADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
405-693 3.92e-58

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 203.26  E-value: 3.92e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  405 IKVVELLLKYRAAIEATTESGLTPLHVAAFMGAINIVIYLLQQGANPDVETVRGETPLHLAARANQTDVVRVLIRNGAKV 484
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  485 DAQARELQTPLHIASRLGNTDIVILLLQAGANSNATTRDNYSPLHIAAKEGQEEVAGILLDHNADKTLLTKKGFTPLHLA 564
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  565 SKYGNLEVVRLLLERGTPVDIEGKNQVTPLHVAAHYNNDKVAMLLLENGASAKAAAKNGYTPLHIAAKKNQMEIASTLLQ 644
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1831513053  645 FKADPNAKSRAGFTPLHLSAQEGHKEISGLLIENGSDVGAKANNGLTAM 693
Cdd:COG0666    241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
306-580 5.02e-57

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 199.80  E-value: 5.02e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  306 DQVVDLLVVQGAPISAKTKNGLAPLHMAAQGDHVDAARTLLYHRAPVDDVTVDYLTPLHVAAHCGHVRVAKLLLDRSADP 385
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  386 NSRALNGFTPLHIACKKNRIKVVELLLKYRAAIEATTESGLTPLHVAAFMGAINIVIYLLQQGANPDVETVRGETPLHLA 465
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  466 ARANQTDVVRVLIRNGAKVDAQARELQTPLHIASRLGNTDIVILLLQAGANSNATTRDNYSPLHIAAKEGQEEVAGILLD 545
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1831513053  546 HNADKTLLTKKGFTPLHLASKYGNLEVVRLLLERG 580
Cdd:COG0666    241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLAL 275
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
274-561 8.13e-57

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 199.41  E-value: 8.13e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  274 NMANLLLSRGAIIDSRTKDLLTPLHCAARSGHDQVVDLLVVQGAPISAKTKNGLAPLHMAAQGDHVDAARTLLYHRAPVD 353
Cdd:COG0666      2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  354 DVTVDYLTPLHVAAHCGHVRVAKLLLDRSADPNSRALNGFTPLHIACKKNRIKVVELLLKYRAAIEATTESGLTPLHVAA 433
Cdd:COG0666     82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  434 FMGAINIVIYLLQQGANPDVETVRGETPLHLAARANQTDVVRVLIRNGAKVDAQARELQTPLHIASRLGNTDIVILLLQA 513
Cdd:COG0666    162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1831513053  514 GANSNATTRDNYSPLHIAAKEGQEEVAGILLDHNADKTLLTKKGFTPL 561
Cdd:COG0666    242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
472-759 2.81e-56

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 197.87  E-value: 2.81e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  472 DVVRVLIRNGAKVDAQARELQTPLHIASRLGNTDIVILLLQAGANSNATTRDNYSPLHIAAKEGQEEVAGILLDHNADKT 551
Cdd:COG0666      2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  552 LLTKKGFTPLHLASKYGNLEVVRLLLERGTPVDIEGKNQVTPLHVAAHYNNDKVAMLLLENGASAKAAAKNGYTPLHIAA 631
Cdd:COG0666     82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  632 KKNQMEIASTLLQFKADPNAKSRAGFTPLHLSAQEGHKEISGLLIENGSDVGAKANNGLTAMHLCAQEDHVPVAQILYNN 711
Cdd:COG0666    162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1831513053  712 GAEINSKTNAGYTPLHVACHFGQLNMVKFLVENGADVGEKTRASYTPL 759
Cdd:COG0666    242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
245-524 1.94e-55

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 195.17  E-value: 1.94e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  245 LLLEKGANVNYQARHNISPLHVATKWGRTNMANLLLSRGAIIDSRTKDLLTPLHCAARSGHDQVVDLLVVQGAPISAKTK 324
Cdd:COG0666      6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  325 NGLAPLHMAAQGDHVDAARTLLYHRAPVDDVTVDYLTPLHVAAHCGHVRVAKLLLDRSADPNSRALNGFTPLHIACKKNR 404
Cdd:COG0666     86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  405 IKVVELLLKYRAAIEATTESGLTPLHVAAFMGAINIVIYLLQQGANPDVETVRGETPLHLAARANQTDVVRVLIRNGAKV 484
Cdd:COG0666    166 LEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADL 245
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1831513053  485 DAQARELQTPLHIASRLGNTDIVILLLQAGANSNATTRDN 524
Cdd:COG0666    246 NAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
438-726 4.52e-54

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 191.32  E-value: 4.52e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  438 INIVIYLLQQGANPDVETVRGETPLHLAARANQTDVVRVLIRNGAKVDAQARELQTPLHIASRLGNTDIVILLLQAGANS 517
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  518 NATTRDNYSPLHIAAKEGQEEVAGILLDHNADKTLLTKKGFTPLHLASKYGNLEVVRLLLERGTPVDIEGKNQVTPLHVA 597
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  598 AHYNNDKVAMLLLENGASAKAAAKNGYTPLHIAAKKNQMEIASTLLQFKADPNAKSRAGFTPLHLSAQEGHKEISGLLIE 677
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1831513053  678 NGSDVGAKANNGLTAMHLCAQEDHVPVAQILYNNGAEINSKTNAGYTPL 726
Cdd:COG0666    241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
505-792 1.33e-53

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 190.17  E-value: 1.33e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  505 DIVILLLQAGANSNATTRDNYSPLHIAAKEGQEEVAGILLDHNADKTLLTKKGFTPLHLASKYGNLEVVRLLLERGTPVD 584
Cdd:COG0666      2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  585 IEGKNQVTPLHVAAHYNNDKVAMLLLENGASAKAAAKNGYTPLHIAAKKNQMEIASTLLQFKADPNAKSRAGFTPLHLSA 664
Cdd:COG0666     82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  665 QEGHKEISGLLIENGSDVGAKANNGLTAMHLCAQEDHVPVAQILYNNGAEINSKTNAGYTPLHVACHFGQLNMVKFLVEN 744
Cdd:COG0666    162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1831513053  745 GADVGEKTRASYTPLHQAAQQGHNNCVRYLLENGASPNEQTATGQTPL 792
Cdd:COG0666    242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
212-495 2.25e-53

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 189.39  E-value: 2.25e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  212 LLLQNEHNPDVTSKSGFTPLHIAAHYGHENVGQLLLEKGANVNYQARHNISPLHVATKWGRTNMANLLLSRGAIIDSRTK 291
Cdd:COG0666      6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  292 DLLTPLHCAARSGHDQVVDLLVVQGAPISAKTKNGLAPLHMAAQGDHVDAARTLLYHRAPVDDVTVDYLTPLHVAAHCGH 371
Cdd:COG0666     86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  372 VRVAKLLLDRSADPNSRALNGFTPLHIACKKNRIKVVELLLKYRAAIEATTESGLTPLHVAAFMGAINIVIYLLQQGANP 451
Cdd:COG0666    166 LEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADL 245
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1831513053  452 DVETVRGETPLHLAARANQTDVVRVLIRNGAKVDAQARELQTPL 495
Cdd:COG0666    246 NAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
537-807 6.00e-53

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 188.24  E-value: 6.00e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  537 EEVAGILLDHNADKTLLTKKGFTPLHLASKYGNLEVVRLLLERGTPVDIEGKNQVTPLHVAAHYNNDKVAMLLLENGASA 616
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  617 KAAAKNGYTPLHIAAKKNQMEIASTLLQFKADPNAKSRAGFTPLHLSAQEGHKEISGLLIENGSDVGAKANNGLTAMHLC 696
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  697 AQEDHVPVAQILYNNGAEINSKTNAGYTPLHVACHFGQLNMVKFLVENGADVGEKTRASYTPLHQAAQQGHNNCVRYLLE 776
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1831513053  777 NGASPNEQTATGQTPLSIAQRLGYVSVVETL 807
Cdd:COG0666    241 AGADLNAKDKDGLTALLLAAAAGAALIVKLL 271
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
184-462 1.12e-51

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 184.39  E-value: 1.12e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  184 LLENDSKGKVRLPALHIAAKKDDTTAATLLLQNEHNPDVTSKSGFTPLHIAAHYGHENVGQLLLEKGANVNYQARHNISP 263
Cdd:COG0666     11 LLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTL 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  264 LHVATKWGRTNMANLLLSRGAIIDSRTKDLLTPLHCAARSGHDQVVDLLVVQGAPISAKTKNGLAPLHMAAQGDHVDAAR 343
Cdd:COG0666     91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  344 TLLYHRAPVDDVTVDYLTPLHVAAHCGHVRVAKLLLDRSADPNSRALNGFTPLHIACKKNRIKVVELLLKYRAAIEATTE 423
Cdd:COG0666    171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1831513053  424 SGLTPLHVAAFMGAINIVIYLLQQGANPDVETVRGETPL 462
Cdd:COG0666    251 DGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
570-808 1.43e-48

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 175.53  E-value: 1.43e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  570 LEVVRLLLERGTPVDIEGKNQVTPLHVAAHYNNDKVAMLLLENGASAKAAAKNGYTPLHIAAKKNQMEIASTLLQFKADP 649
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  650 NAKSRAGFTPLHLSAQEGHKEISGLLIENGSDVGAKANNGLTAMHLCAQEDHVPVAQILYNNGAEINSKTNAGYTPLHVA 729
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1831513053  730 CHFGQLNMVKFLVENGADVGEKTRASYTPLHQAAQQGHNNCVRYLLENGASPNEQTATGQTPLSIAQRLGYVSVVETLR 808
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
37-330 2.86e-48

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 174.76  E-value: 2.86e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053   37 FLRAARAGDLEKVLELLRAGTDINTSNANGLNSLHLASKEGHSEVVRELIKRQAQVDAATRKGNTALHIASLAGQSLIVT 116
Cdd:COG0666     25 LLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVK 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  117 ILVENGANVNVQSVNGFTPLYMAAQENHEEVVKYLLKHGANQALSTEDGFTPlavalqqghdrvvavllendskgkvrlp 196
Cdd:COG0666    105 LLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTP---------------------------- 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  197 aLHIAAKKDDTTAATLLLQNEHNPDVTSKSGFTPLHIAAHYGHENVGQLLLEKGANVNYQARHNISPLHVATKWGRTNMA 276
Cdd:COG0666    157 -LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIV 235
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1831513053  277 NLLLSRGAIIDSRTKDLLTPLHCAARSGHDQVVDLLVVQGAPISAKTKNGLAPL 330
Cdd:COG0666    236 KLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
46-363 2.86e-48

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 174.76  E-value: 2.86e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053   46 LEKVLELLRAGTDINTSNANGLNSLHLASKEGHSEVVRELIKRQAQVDAATRKGNTALHIASLAGQSLIVTILVENGANV 125
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  126 NVQSVNGFTPLYMAAQENHEEVVKYLLKHGANQALSTEDGFTPlavalqqghdrvvavllendskgkvrlpaLHIAAKKD 205
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETP-----------------------------LHLAAYNG 131
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  206 DTTAATLLLQNEHNPDVTSKSGFTPLHIAAHYGHENVGQLLLEKGANVNYQARHNISPLHVATKWGRTNMANLLLSRGAI 285
Cdd:COG0666    132 NLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGAD 211
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1831513053  286 IDSRTKDLLTPLHCAARSGHDQVVDLLVVQGAPISAKTKNGLAPLHMAAQGDHVDAARTLLYHRAPVDDVTVDYLTPL 363
Cdd:COG0666    212 VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
UPA_2 pfam17809
UPA domain; The UPA domain is conserved in UNC5, PIDD, and Ankyrins. It has a beta sandwich ...
1337-1472 2.99e-48

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: 168.42  E-value: 2.99e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053 1337 IPYMAKFAVFARRTFPVEGQLRVFCMTDDKEDKTLEKQEHFKLIAKSRDVEVLKGKHQFLEFSGNLVPITKSGDQLSLFF 1416
Cdd:pfam17809    1 VPYLAKFVVFAKRYDPGEARLRCACMTDDGEDKTLEFHEGFTEVARSRDVEVLEGSPVSIELSGNLVPIKKKSQSRQMDF 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1831513053 1417 LPFQENRLAFMVKTRsndDNEAATEGRIGFMAEPKIRSDAlpPQQPICTLAISLPE 1472
Cdd:pfam17809   81 KAFRENRLDGSVRVK---DPSDPPKGLLSFMRDAKVDGGT--VSQPLCTLNIVLPQ 131
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
1008-1110 1.98e-47

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


Pssm-ID: 128514  Cd Length: 104  Bit Score: 164.83  E-value: 1.98e-47
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  1008 FLISFLVDARGGAMRGCRhSGVRIIVPPRKASQPIRVTCRYLRKDKLAHPPPLSEGEELASRILEMAPAGAKFLGPVILE 1087
Cdd:smart00218    3 FLVSGTFDARGGRLRGPR-TGVRLIIPPGAIPQGTRYTCYLVVHKTLSTPPPLEEGETLLSPVVECGPHGALFLRPVILE 81
                            90       100
                    ....*....|....*....|...
gi 1831513053  1088 VPHFASLRDREREIVILRSDDGQ 1110
Cdd:smart00218   82 VPHCASLRPRDWEIVLLRSENGG 104
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
30-297 6.81e-47

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 170.52  E-value: 6.81e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053   30 RAEGSASFLRAARAGDLEKVLELLRAGTDINTSNANGLNSLHLASKEGHSEVVRELIKRQAQVDAATRKGNTALHIASLA 109
Cdd:COG0666     51 DALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYN 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  110 GQSLIVTILVENGANVNVQSVNGFTPLYMAAQENHEEVVKYLLKHGANQALSTEDGFTPLAVALQQGHDRVVAVLLENDS 189
Cdd:COG0666    131 GNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA 210
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  190 kgkvrlpalhiaakkddttaatlllqnehNPDVTSKSGFTPLHIAAHYGHENVGQLLLEKGANVNYQARHNISPLHVATK 269
Cdd:COG0666    211 -----------------------------DVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAA 261
                          250       260
                   ....*....|....*....|....*...
gi 1831513053  270 WGRTNMANLLLSRGAIIDSRTKDLLTPL 297
Cdd:COG0666    262 AGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
22-219 1.03e-44

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 164.36  E-value: 1.03e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053   22 APAAPEPGRAEGSASFLRAARAGDLEKVLELLRAGTDINTSNANGLNSLHLASKEGHSEVVRELIKRQAQVDAATRKGNT 101
Cdd:COG0666     76 AGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNT 155
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  102 ALHIASLAGQSLIVTILVENGANVNVQSVNGFTPLYMAAQENHEEVVKYLLKHGANQALSTEDGFTPLAVALQQGHDRVV 181
Cdd:COG0666    156 PLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIV 235
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1831513053  182 AVLLE----NDSKGKVRLPALHIAAKKDDTTAATLLLQNEHN 219
Cdd:COG0666    236 KLLLEagadLNAKDKDGLTALLLAAAAGAALIVKLLLLALLL 277
ZU5 pfam00791
ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.
1011-1107 7.09e-42

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: 7.09e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053 1011 SFLVDARGGAMRGCrHSGVRIIVPPRKASQPIRVTCRYLRKDKLAHPPPLSEGEELASRILEMAPAGAKFLGPVILEVPH 1090
Cdd:pfam00791    2 SGLVDSRGGRLVLP-NSGVSLLIPPGAIPEGTRIECYLAVNRDESSRPPLEEGETLLSPVVECGPPGLKFLKPVILEVPH 80
                           90
                   ....*....|....*..
gi 1831513053 1091 FASLRDREREIVILRSD 1107
Cdd:pfam00791   81 CASLRPEEWEIVLKRSD 97
PHA02876 PHA02876
ankyrin repeat protein; Provisional
242-648 1.69e-36

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 149.06  E-value: 1.69e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  242 VGQLLLEKGANVNYQARHNISPLHVATKWGRTNMANLLLSRGAIIDSRTKDLLTPLHCAARSGHDQVVDLLVVQGAPISa 321
Cdd:PHA02876   160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNIN- 238
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  322 ktKNGLAPLHMAAQGDhvdaartllyhrapvddvtvdyltplhvaahcghVRVAKLLLDRSADPNSRALNGFTPLHiack 401
Cdd:PHA02876   239 --KNDLSLLKAIRNED----------------------------------LETSLLLYDAGFSVNSIDDCKNTPLH---- 278
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  402 knrikvvelllkyrAAIEATTESGLTPlhvaafmgainiviYLLQQGANPDVETVRGETPLHLAAR-ANQTDVVRVLIRN 480
Cdd:PHA02876   279 --------------HASQAPSLSRLVP--------------KLLERGADVNAKNIKGETPLYLMAKnGYDTENIRTLIML 330
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  481 GAKVDAQARELQTPLHIASRLG-NTDIVILLLQAGANSNATTRDNYSPLHIAAKEGQEEVAGILLDHNADKTLLTKKGFT 559
Cdd:PHA02876   331 GADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGT 410
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  560 PLHLAsKYGN--LEVVRLLLERGTPVDIEGKNQVTPLHVAAHYN-NDKVAMLLLENGASAKAAAKNGYTPLHIAAKKNQm 636
Cdd:PHA02876   411 ALHFA-LCGTnpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIALEYHG- 488
                          410
                   ....*....|..
gi 1831513053  637 eIASTLLQFKAD 648
Cdd:PHA02876   489 -IVNILLHYGAE 499
PHA03100 PHA03100
ankyrin repeat protein; Provisional
555-780 7.94e-36

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 142.50  E-value: 7.94e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  555 KKGFTPLHLASKYGNLEVVRLLLERGTPVDIEGKNQVTPLHVAAHY-----NNDKVAMLLLENGASAKAAAKNGYTPLHI 629
Cdd:PHA03100    33 KKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIkynltDVKEIVKLLLEYGANVNAPDNNGITPLLY 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  630 AA--KKNQMEIASTLLQFKADPNAKSRAGFTPLHLSAQEGH--KEISGLLIENGSDVGAKanngltamhlcaqeDHVpva 705
Cdd:PHA03100   113 AIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAK--------------NRV--- 175
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1831513053  706 QILYNNGAEINSKTNAGYTPLHVACHFGQLNMVKFLVENGADVGEKTRASYTPLHQAAQQGHNNCVRYLLENGAS 780
Cdd:PHA03100   176 NYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
PHA03100 PHA03100
ankyrin repeat protein; Provisional
440-720 1.30e-35

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 141.73  E-value: 1.30e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  440 IVIYLLQQGANPDVETVRGETPLHLAARANQTDVVRVLIRNGAKVDAQARELQTPLHIASRLG-----NTDIVILLLQAG 514
Cdd:PHA03100    17 NIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKynltdVKEIVKLLLEYG 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  515 ANSNATTRDNYSPLHIAA--KEGQEEVAGILLDHNADKTLLTKKGFTPLHLASKYG--NLEVVRLLLERGtpVDIEGKNQ 590
Cdd:PHA03100    97 ANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNkiDLKILKLLIDKG--VDINAKNR 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  591 VTplhvaahynndkvamLLLENGASAKAAAKNGYTPLHIAAKKNQMEIASTLLQFKADPNAKSRAGFTPLHLSAQEGHKE 670
Cdd:PHA03100   175 VN---------------YLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKE 239
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1831513053  671 ISGLLIENGSDVGAKanngltamhlcaqedhvpVAQILYNNGAEINSKTN 720
Cdd:PHA03100   240 IFKLLLNNGPSIKTI------------------IETLLYFKDKDLNTITK 271
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
20-202 5.87e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.16  E-value: 5.87e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053   20 VQAPAAPEPGRAEGSASFLRAARAGDLEKVLELLRAGTDINTSNANGLNSLHLASKEGHSEVVRELIKRQAQVDAATRKG 99
Cdd:COG0666    107 LEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDG 186
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  100 NTALHIASLAGQSLIVTILVENGANVNVQSVNGFTPLYMAAQENHEEVVKYLLKHGANQALSTEDGFTPLAVALQQGHDR 179
Cdd:COG0666    187 ETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAAL 266
                          170       180
                   ....*....|....*....|...
gi 1831513053  180 VVAVLLENDSKGKVRLPALHIAA 202
Cdd:COG0666    267 IVKLLLLALLLLAAALLDLLTLL 289
PHA02876 PHA02876
ankyrin repeat protein; Provisional
473-807 3.70e-33

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 138.66  E-value: 3.70e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  473 VVRVLIRNGAKVDAQARELQTPLHIASRLGNTDIVILLLQAGANSNATTRDNYSPLHIAAKEGQEEVAGILLDHNADktl 552
Cdd:PHA02876   160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSN--- 236
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  553 LTKKGFTPLHlASKYGNLEVVRLLLERGTPVDIEGKNQVTPLHVAAHYNN-DKVAMLLLENGASAKAAAKNGYTPLHIAA 631
Cdd:PHA02876   237 INKNDLSLLK-AIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMA 315
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  632 KKN-QMEIASTLLQFKADPNAKSRAGFTPLH-LSAQEGHKEISGLLIENGSDVGAKANNGLTAMHLCAQEDHVPVAQILY 709
Cdd:PHA02876   316 KNGyDTENIRTLIMLGADVNAADRLYITPLHqASTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLL 395
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  710 NNGAEINSKTNAGYTPLHVA-CHFGQLNMVKFLVENGADVGEKTRASYTPLHQAAQqghNNC----VRYLLENGASPNEQ 784
Cdd:PHA02876   396 DYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACK---KNCkldvIEMLLDNGADVNAI 472
                          330       340
                   ....*....|....*....|...
gi 1831513053  785 TATGQTPLSIAqrLGYVSVVETL 807
Cdd:PHA02876   473 NIQNQYPLLIA--LEYHGIVNIL 493
PHA03100 PHA03100
ankyrin repeat protein; Provisional
246-486 2.23e-31

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 129.01  E-value: 2.23e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  246 LLEKGANVNYQARHNISPLHVATKWGRTNMANLLLSRGAIIDSRTKDLLTPLHCAARSGHDQ-----VVDLLVVQGAPIS 320
Cdd:PHA03100    21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLtdvkeIVKLLLEYGANVN 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  321 AKTKNGLAPLHMAAQG--DHVDAARTLLYHRAPVDDVTVDYLTPLHVAAHCGHV--RVAKLLLDRSADPNsralngftpl 396
Cdd:PHA03100   101 APDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDIN---------- 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  397 hiacKKNRikvVELLLKYRAAIEATTESGLTPLHVAAFMGAINIVIYLLQQGANPDVETVRGETPLHLAARANQTDVVRV 476
Cdd:PHA03100   171 ----AKNR---VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKL 243
                          250
                   ....*....|
gi 1831513053  477 LIRNGAKVDA 486
Cdd:PHA03100   244 LLNNGPSIKT 253
PHA03095 PHA03095
ankyrin-like protein; Provisional
398-660 3.34e-31

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 129.76  E-value: 3.34e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  398 IACKKNRIKVVELLLKYRAAIEATTESGLTPLHVaaFMGAIN-----IVIYLLQQGANPDVETVRGETPLHLAARANQT- 471
Cdd:PHA03095    20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHL--YLHYSSekvkdIVRLLLEAGADVNAPERCGFTPLHLYLYNATTl 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  472 DVVRVLIRNGAKVDAQARELQTPLHI--ASRLGNTDIVILLLQAGANSNATTRDNYSPLHIAAKEGQEEVAGI--LLDHN 547
Cdd:PHA03095    98 DVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVELLrlLIDAG 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  548 ADktLLTKK--GFTPLH--LASKYGNLEVVRLLLERGTPVDIEGKNQVTPLHVAAHYNNDKVAML--LLENGASAKAAAK 621
Cdd:PHA03095   178 AD--VYAVDdrFRSLLHhhLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNR 255
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1831513053  622 NGYTPLHIAAKKNQMEIASTLLQFKADPNAKSRAGFTPL 660
Cdd:PHA03095   256 YGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294
PHA02876 PHA02876
ankyrin repeat protein; Provisional
356-779 3.76e-31

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 132.49  E-value: 3.76e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  356 TVDYLTPLHVAAHCGHVRVAKLLLDRSADPNSRALNGFTPLHIACKKNRIKVVELLLKYraaieattesgltplhvaafm 435
Cdd:PHA02876   142 SIEYMKLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSY--------------------- 200
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  436 gainiviyllqqGANPDVETVRGETPLHLAARANQTDVVRVLIRNGAKVDaqarelQTPLHIASRLGNTDI--VILLLQA 513
Cdd:PHA02876   201 ------------GADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNIN------KNDLSLLKAIRNEDLetSLLLYDA 262
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  514 GANSNATTRDNYSPLHIAAKEGQ-EEVAGILLDHNADKTLLTKKGFTPLHLASKYG-NLEVVRLLLERGTPVDIEGKNQV 591
Cdd:PHA02876   263 GFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYI 342
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  592 TPLHVAAHYNNDK-VAMLLLENGASAKAAAKNGYTPLHIAAKKNQMEIASTLLQFKADPNAKSRAGFTPLHLSaqeghke 670
Cdd:PHA02876   343 TPLHQASTLDRNKdIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFA------- 415
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  671 isglliengsdvgakanngltamhLCAQEDHVPVaQILYNNGAEINSKTNAGYTPLHVACHFG-QLNMVKFLVENGADVG 749
Cdd:PHA02876   416 ------------------------LCGTNPYMSV-KTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVN 470
                          410       420       430
                   ....*....|....*....|....*....|
gi 1831513053  750 EKTRASYTPLHQAAqqGHNNCVRYLLENGA 779
Cdd:PHA02876   471 AINIQNQYPLLIAL--EYHGIVNILLHYGA 498
PHA03095 PHA03095
ankyrin-like protein; Provisional
245-528 9.72e-31

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 128.22  E-value: 9.72e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  245 LLLEKGANVNYQARHNISPLHVATKWG---RTNMANLLLSRGAIIDSRTKDLLTPLHCAARSGHD-QVVDLLVVQGAPIS 320
Cdd:PHA03095    32 RLLAAGADVNFRGEYGKTPLHLYLHYSsekVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGADVN 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  321 AKTKNGLAPLHMaaqgdhvdaartllyhrapvddvtvdYLTPLHVaahcgHVRVAKLLLDRSADPNSRALNGFTPLHIAC 400
Cdd:PHA03095   112 AKDKVGRTPLHV--------------------------YLSGFNI-----NPKVIRLLLRKGADVNALDLYGMTPLAVLL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  401 KKNR--IKVVELLLKYRAAIEATTESGLTPLHVAA--FMGAINIVIYLLQQGANPDVETVRGETPLHLAARANQTD--VV 474
Cdd:PHA03095   161 KSRNanVELLRLLIDAGADVYAVDDRFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLV 240
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1831513053  475 RVLIRNGAKVDAQARELQTPLHIASRLGNTDIVILLLQAGANSNATTRDNYSPL 528
Cdd:PHA03095   241 LPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294
PHA02874 PHA02874
ankyrin repeat protein; Provisional
394-660 6.67e-30

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 125.08  E-value: 6.67e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  394 TPLHIACKKNRIKVVELLLKYRAAIEATTESGLTPLHVAAFMGAINIVIYLLQQGANPDVetvrgetplhLAARANQTDV 473
Cdd:PHA02874    37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSI----------LPIPCIEKDM 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  474 VRVLIRNGAKVDAQARELQTPLHIASRLGNTDIVILLLQAGANSNATTRDNYSPLHIAAKEGQEEVAGILLDHNADKTLL 553
Cdd:PHA02874   107 IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVK 186
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  554 TKKGFTPLHLASKYGNLEVVRLLLERGTPVDIEGKNQVTPLHVAAHYNNDKVAMLLleNGASAKAAAKNGYTPLHIAAKK 633
Cdd:PHA02874   187 DNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIELLI--NNASINDQDIDGSTPLHHAINP 264
                          250       260
                   ....*....|....*....|....*...
gi 1831513053  634 N-QMEIASTLLQFKADPNAKSRAGFTPL 660
Cdd:PHA02874   265 PcDIDIIDILLYHKADISIKDNKGENPI 292
PHA02874 PHA02874
ankyrin repeat protein; Provisional
472-793 9.84e-30

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 124.69  E-value: 9.84e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  472 DVVRVLIRN-GAKVDAQARELQTPLHIASRLGNTDIVILLLQAGANSNATTRDNYSPLHIAAKEGQEEVAGILLDHNADK 550
Cdd:PHA02874    15 EAIEKIIKNkGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDT 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  551 TLLtkkgftPLHLASKygnlEVVRLLLERGTPVDIEGKNQVTPLHVAAHYNNDKVAMLLLENGASAKAAAKNGYTPLHIA 630
Cdd:PHA02874    95 SIL------PIPCIEK----DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIA 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  631 AKKNQMEIASTLLQFKADPNAKSRAGFTPLHLSAQEGHKEISGLLIENGSDVGAKANNGLTAMHLCAQEDHvPVAQILYN 710
Cdd:PHA02874   165 IKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLIN 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  711 NgAEINSKTNAGYTPLHVACHFG-QLNMVKFLVENGADVGEKTRASYTPLHQAAQQ-GHNNCVRYLLENGASPNEqtaTG 788
Cdd:PHA02874   244 N-ASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAFKYiNKDPVIKDIIANAVLIKE---AD 319

                   ....*
gi 1831513053  789 QTPLS 793
Cdd:PHA02874   320 KLKDS 324
PHA03095 PHA03095
ankyrin-like protein; Provisional
361-621 1.53e-29

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 124.75  E-value: 1.53e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  361 TPLHVAAHCGH---VRVAKLLLDRSADPNSRALNGFTPLHI-ACKKNRIKVVELLLKYRAAIEATTESGLTPLHVAAFMG 436
Cdd:PHA03095    49 TPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLyLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVYLSGF 128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  437 AIN--IVIYLLQQGANPDVETVRGETPLHLAARANQTDV--VRVLIRNGAKVDAQARELQTPLHI--ASRLGNTDIVILL 510
Cdd:PHA03095   129 NINpkVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVYAVDDRFRSLLHHhlQSFKPRARIVREL 208
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  511 LQAGANSNATTRDNYSPLHIAAKEGQEEVAGI--LLDHNADKTLLTKKGFTPLHLASKYGNLEVVRLLLERGTPVDIEGK 588
Cdd:PHA03095   209 IRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSS 288
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1831513053  589 NQVTPLHVAAHYNNDKVAMLLLENGASAKAAAK 621
Cdd:PHA03095   289 DGNTPLSLMVRNNNGRAVRAALAKNPSAETVAA 321
PHA03095 PHA03095
ankyrin-like protein; Provisional
505-795 1.96e-29

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 124.37  E-value: 1.96e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  505 DIVILLLQAGANSNATTRDNYSPLHIAAKEGQEEVAGI---LLDHNADKTLLTKKGFTPLHLASKYGN-LEVVRLLLERG 580
Cdd:PHA03095    28 EEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAG 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  581 TPVDIEGKNQVTPLHV-AAHYN-NDKVAMLLLENGASAKAAAKNGYTPLHIAAKKNQMEIastllqfkadpnaksragft 658
Cdd:PHA03095   108 ADVNAKDKVGRTPLHVyLSGFNiNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANV-------------------- 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  659 plhlsaqeghkEISGLLIENGSDVGAKANNGLTAMHLCAQEDHvPVAQI---LYNNGAEINSKTNAGYTPLHVACHFG-- 733
Cdd:PHA03095   168 -----------ELLRLLIDAGADVYAVDDRFRSLLHHHLQSFK-PRARIvreLIRAGCDPAATDMLGNTPLHSMATGSsc 235
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1831513053  734 -QLNMVKFLvENGADVGEKTRASYTPLHQAAqqGHNN--CVRYLLENGASPNEQTATGQTPLSIA 795
Cdd:PHA03095   236 kRSLVLPLL-IAGISINARNRYGQTPLHYAA--VFNNprACRRLIALGADINAVSSDGNTPLSLM 297
PHA03095 PHA03095
ankyrin-like protein; Provisional
37-387 2.27e-29

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 123.98  E-value: 2.27e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053   37 FLRAARAgDLEKVLELLRAGTDINTSNANGLNSLHLASKEGHS---EVVRELIKRQAQVDAATRKGNTALHIASLAGQSL 113
Cdd:PHA03095    19 LLNASNV-TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEkvkDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTL 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  114 -IVTILVENGANVNVQSVNGFTPL--YMAAQENHEEVVKYLLKHGANQALSTEDGFTPLAVALQQGH--DRVVAVLLEND 188
Cdd:PHA03095    98 dVIKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanVELLRLLIDAG 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  189 SkgkvrlpalHIAAKKDDttaatlllqnehnpdvtsksGFTPLHIAAHYGHENVGQL--LLEKGANVNYQARHNISPLHV 266
Cdd:PHA03095   178 A---------DVYAVDDR--------------------FRSLLHHHLQSFKPRARIVreLIRAGCDPAATDMLGNTPLHS 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  267 ATKWG---RTNMANLLLsRGAIIDSRTKDLLTPLHCAARSGHDQVVDLLVVQGAPISAKTKNGLAPLHMAAQGDHVDAAR 343
Cdd:PHA03095   229 MATGSsckRSLVLPLLI-AGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVR 307
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 1831513053  344 TLLYHRAPVDDV--TVDYLTPLHVAAHCGHVR--VAKLLLDR--SADPNS 387
Cdd:PHA03095   308 AALAKNPSAETVaaTLNTASVAGGDIPSDATRlcVAKVVLRGafSLLPEP 357
PHA02876 PHA02876
ankyrin repeat protein; Provisional
113-449 7.60e-29

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 125.18  E-value: 7.60e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  113 LIVTILVENGANVNVQSVNGFTPLYMAAQENHEEVVKYLLKHGANQALSTEDGFTPLAVALQQGHDRVVAVLLENDSKGK 192
Cdd:PHA02876   159 LIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNIN 238
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  193 VRLPALHIAAKKDDTTAATLLLQNEHNPDVTSKSGFTPLHIAAHygHENVGQL---LLEKGANVNYQARHNISPLHVATK 269
Cdd:PHA02876   239 KNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQ--APSLSRLvpkLLERGADVNAKNIKGETPLYLMAK 316
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  270 WG-RTNMANLLLSRGAIIDSRTKDLLTPLHCAAR--SGHDQVVDLLVVqGAPISAKTKNGLAPLHMAAQGDHVDAARTLL 346
Cdd:PHA02876   317 NGyDTENIRTLIMLGADVNAADRLYITPLHQASTldRNKDIVITLLEL-GANVNARDYCDKTPIHYAAVRNNVVIINTLL 395
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  347 YHRAPVDDVTVDYLTPLHVAAhCGH--VRVAKLLLDRSADPNSRALNGFTPLHIACKKN-RIKVVELLLKYRAAIEATTE 423
Cdd:PHA02876   396 DYGADIEALSQKIGTALHFAL-CGTnpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINI 474
                          330       340
                   ....*....|....*....|....*.
gi 1831513053  424 SGLTPLHVAafMGAINIVIYLLQQGA 449
Cdd:PHA02876   475 QNQYPLLIA--LEYHGIVNILLHYGA 498
PHA02874 PHA02874
ankyrin repeat protein; Provisional
277-569 2.22e-28

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 120.45  E-value: 2.22e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  277 NLLLSRGAIIDSRTKDLLTPLHCAARSGHDQVVDLLVVQGAPISAKTKNGLAPLHMAAQGDHVDAARTLLYHRA-----P 351
Cdd:PHA02874    19 KIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVdtsilP 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  352 VDDVTVDYLtplhvaahcghvrvaKLLLDRSADPNSRALNGFTPLHIACKKNRIKVVELLLKYRAAIEATTESGLTPLHV 431
Cdd:PHA02874    99 IPCIEKDMI---------------KTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHI 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  432 AAFMGAINIVIYLLQQGANPDVETVRGETPLHLAARANQTDVVRVLIRNGAKVDAQARELQTPLHIASrLGNTDIVILLL 511
Cdd:PHA02874   164 AIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI-IHNRSAIELLI 242
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1831513053  512 QaGANSNATTRDNYSPLHIAAK-EGQEEVAGILLDHNADKTLLTKKGFTPLHLASKYGN 569
Cdd:PHA02874   243 N-NASINDQDIDGSTPLHHAINpPCDIDIIDILLYHKADISIKDNKGENPIDTAFKYIN 300
PHA03100 PHA03100
ankyrin repeat protein; Provisional
47-287 1.99e-26

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 114.38  E-value: 1.99e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053   47 EKVLE-LLRAGTDINTSNANGLNSLHLASKEGHSEV-VRELIKrqaqvdaatrkgntalhiaslagqslivtILVENGAN 124
Cdd:PHA03100    48 IDVVKiLLDNGADINSSTKNNSTPLHYLSNIKYNLTdVKEIVK-----------------------------LLLEYGAN 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  125 VNVQSVNGFTPLYMAAQE--NHEEVVKYLLKHGANQALSTEDGFTPLAVALQQGHD--RVVAVLLENDSKgkvrlpalhI 200
Cdd:PHA03100    99 VNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVD---------I 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  201 AAKkddtTAATLLLQNEHNPDVTSKSGFTPLHIAAHYGHENVGQLLLEKGANVNYQARHNISPLHVATKWGRTNMANLLL 280
Cdd:PHA03100   170 NAK----NRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLL 245

                   ....*..
gi 1831513053  281 SRGAIID 287
Cdd:PHA03100   246 NNGPSIK 252
PHA02875 PHA02875
ankyrin repeat protein; Provisional
234-482 3.02e-26

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 113.55  E-value: 3.02e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  234 AAHYGHENVGQLLLEKGANVNYQARHNISPLHVATKWGRTNMANLLLSRGAIIDSRTKDLLTPLHCAARSGHDQVVDLLV 313
Cdd:PHA02875     9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  314 VQGAPIsaktknglaplhmaaqgdhvdaartllyhrapvDDVTV-DYLTPLHVAAHCGHVRVAKLLLDRSADPNSRALNG 392
Cdd:PHA02875    89 DLGKFA---------------------------------DDVFYkDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDK 135
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  393 FTPLHIACKKNRIKVVELLLKYRAAIEATTESGLTPLHVAAFMGAINIVIYLLQQGANPDVETVRGE-TPLHLAARANQT 471
Cdd:PHA02875   136 FSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKI 215
                          250
                   ....*....|.
gi 1831513053  472 DVVRVLIRNGA 482
Cdd:PHA02875   216 DIVRLFIKRGA 226
Death_ank cd08317
Death domain associated with Ankyrins; Death Domain (DD) associated with Ankyrins. Ankyrins ...
1503-1580 5.31e-26

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: 103.11  E-value: 5.31e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053 1503 PEFVHQNVLKGIGADWPRLGRALEVPHRDIQHIRQNYPG---QECKNTLKIWIHLKKEDANQDNLDQALRQIGRDDIVRS 1579
Cdd:cd08317      3 ADLRLSDIANLLGSDWPELARELGVSEEDIDLIRSENPNslaQQAMAMLRLWLEREGEKATGNALESALKKIGRDDIVEK 82

                   .
gi 1831513053 1580 I 1580
Cdd:cd08317     83 C 83
PHA02874 PHA02874
ankyrin repeat protein; Provisional
559-795 5.55e-26

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 113.13  E-value: 5.55e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  559 TPLHLASKYGNLEVVRLLLERGTPVDIEGKNQVTPLHVAAHYNNDKVAMLLLENGASAKAaakngytpLHIAAKKNQMei 638
Cdd:PHA02874    37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSI--------LPIPCIEKDM-- 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  639 ASTLLQFKADPNAKSRAGFTPLHLSAQEGHKEISGLLIENGSDVGAKANNGLTAMHLCAQEDHVPVAQILYNNGAEINSK 718
Cdd:PHA02874   107 IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVK 186
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1831513053  719 TNAGYTPLHVACHFGQLNMVKFLVENGADVGEKTRASYTPLHQAAQqgHNNCVRYLLENGASPNEQTATGQTPLSIA 795
Cdd:PHA02874   187 DNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHA 261
PHA02875 PHA02875
ankyrin repeat protein; Provisional
432-681 1.94e-25

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 111.24  E-value: 1.94e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  432 AAFMGAINIVIYLLQQGANPDVETVRGETPLHLAARANQTDVVRVLIRNGAKVDAQARELQTPLHIASRLGNTDIVILLL 511
Cdd:PHA02875     9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  512 QAGANSNattrdnysplhiaakegqeevagilldhnadkTLLTKKGFTPLHLASKYGNLEVVRLLLERGTPVDIEGKNQV 591
Cdd:PHA02875    89 DLGKFAD--------------------------------DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKF 136
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  592 TPLHVAAHYNNDKVAMLLLENGASAKAAAKNGYTPLHIAAKKNQMEIASTLLQFKADPNAKSRAGFTPLHLSAQEGHK-E 670
Cdd:PHA02875   137 SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKiD 216
                          250
                   ....*....|.
gi 1831513053  671 ISGLLIENGSD 681
Cdd:PHA02875   217 IVRLFIKRGAD 227
PHA02878 PHA02878
ankyrin repeat protein; Provisional
294-577 1.01e-24

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 109.97  E-value: 1.01e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  294 LTPLHCAARSGHDQVVDLLVVQGAPISAKTKNGLAPLHMAAQGDHVDAARTLLyhRAPVDDVTVDYLTPLHVAAHCGHVR 373
Cdd:PHA02878    38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMI--RSINKCSVFYTLVAIKDAFNNRNVE 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  374 VAKLLLDRSADpNSRALNgftpLHIACKKNR-----IKVVELLLKYRAAIEATTE-SGLTPLHVAAFMGAINIVIYLLQQ 447
Cdd:PHA02878   116 IFKIILTNRYK-NIQTID----LVYIDKKSKddiieAEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSY 190
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  448 GANPDVETVRGETPLHLAARANQTDVVRVLIRNGAKVDAQARELQTPLHIA-SRLGNTDIVILLLQAGANSNA-TTRDNY 525
Cdd:PHA02878   191 GANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAkSYILGL 270
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1831513053  526 SPLHIAAKEgqEEVAGILLDHNADKTLLTKKGFTPLHLASK-YGNLEVVRLLL 577
Cdd:PHA02878   271 TALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAVKqYLCINIGRILI 321
PHA02875 PHA02875
ankyrin repeat protein; Provisional
370-614 4.87e-24

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 107.00  E-value: 4.87e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  370 GHVRVAKLLLDRSADPNSRALNGFTPLHIACKKNRIKVVELLLKYraaieattesgltplhvaafmgainiviyllqqGA 449
Cdd:PHA02875    13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKH---------------------------------GA 59
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  450 NPDVETVRGETPLHLAARANQTDVVRVLIRNGAKV-DAQARELQTPLHIASRLGNTDIVILLLQAGANSNATTRDNYSPL 528
Cdd:PHA02875    60 IPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAdDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPL 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  529 HIAAKEGQEEVAGILLDHNADKTLLTKKGFTPLHLASKYGNLEVVRLLLERGTPVDIEGKN-QVTPLHVAAHYNNDKVAM 607
Cdd:PHA02875   140 HLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNgCVAALCYAIENNKIDIVR 219

                   ....*..
gi 1831513053  608 LLLENGA 614
Cdd:PHA02875   220 LFIKRGA 226
PHA02878 PHA02878
ankyrin repeat protein; Provisional
426-684 2.80e-23

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 105.73  E-value: 2.80e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  426 LTPLHVAAFMGAINIVIYLLQQGANPDVETVRGETPLHLAARANQTDVVRVLIR--NGAKVDAQARELQTPLHIAsrlgN 503
Cdd:PHA02878    38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRsiNKCSVFYTLVAIKDAFNNR----N 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  504 TDIVILLLQAGANSNATTRDNYSPLHIAAKEGQEEVAGILLDHNADKTLLTK-KGFTPLHLASKYGNLEVVRLLLERGTP 582
Cdd:PHA02878   114 VEIFKIILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGAN 193
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  583 VDIEGKNQVTPLHVAAHYNNDKVAMLLLENGASAKAAAKNGYTPLHIAAKK-NQMEIASTLLQFKADPNAKSRA-GFTPL 660
Cdd:PHA02878   194 VNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYIlGLTAL 273
                          250       260
                   ....*....|....*....|....
gi 1831513053  661 HLSAQEGHKeiSGLLIENGSDVGA 684
Cdd:PHA02878   274 HSSIKSERK--LKLLLEYGADINS 295
PHA02874 PHA02874
ankyrin repeat protein; Provisional
112-412 3.88e-23

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 104.66  E-value: 3.88e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  112 SLIVTILVENGANVNVQSVNGFTPLYMAAQENHEEVVKYLLKHGANQALSTEDGFTPLAVALQQGHDRVVAVLLENDSKG 191
Cdd:PHA02874    15 EAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDT 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  192 KVrLPALHIaakkDDTTAATLLlqnEHNPDVTSKSG--FTPLHIAAHYGHENVGQLLLEKGANVNYQARHNISPLHVATK 269
Cdd:PHA02874    95 SI-LPIPCI----EKDMIKTIL---DCGIDVNIKDAelKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIK 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  270 WGRTNMANLLLSRGAIIDSRTKDLLTPLHCAARSGHDQVVDLLVVQGAPISAKTKNGLAPLHMAAQgdHVDAARTLLYHR 349
Cdd:PHA02874   167 HNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINN 244
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1831513053  350 APVDDVTVDYLTPLHVAAH--CGhVRVAKLLLDRSADPNSRALNGFTPLHIACKK-NRIKVVELLL 412
Cdd:PHA02874   245 ASINDQDIDGSTPLHHAINppCD-IDIIDILLYHKADISIKDNKGENPIDTAFKYiNKDPVIKDII 309
Ank_2 pfam12796
Ankyrin repeats (3 copies);
693-784 7.36e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 94.41  E-value: 7.36e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  693 MHLCAQEDHVPVAQILYNNGAEINSKTNAGYTPLHVACHFGQLNMVKFLVENgADVGEKTRaSYTPLHQAAQQGHNNCVR 772
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
                           90
                   ....*....|..
gi 1831513053  773 YLLENGASPNEQ 784
Cdd:pfam12796   79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
363-453 8.86e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 94.03  E-value: 8.86e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  363 LHVAAHCGHVRVAKLLLDRSADPNSRALNGFTPLHIACKKNRIKVVELLLKYrAAIEATTEsGLTPLHVAAFMGAINIVI 442
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
                           90
                   ....*....|.
gi 1831513053  443 YLLQQGANPDV 453
Cdd:pfam12796   79 LLLEKGADINV 89
PHA02878 PHA02878
ankyrin repeat protein; Provisional
133-458 3.07e-22

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 102.65  E-value: 3.07e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  133 FTPLYMAAQENHEEVVKYLLKHGANQALSTEDGFTPLAVALQQGHDRVVAVLLENDSKGKV--RLPALHIAAKKDDTTAA 210
Cdd:PHA02878    38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVfyTLVAIKDAFNNRNVEIF 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  211 TLLLQNEHNPDVTSKSGFTPLHIAAHYGHENVGQLLLEKGANVNYQARHNI-SPLHVATKWGRTNMANLLLSRGAIIDSR 289
Cdd:PHA02878   118 KIILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDRHKGnTALHYATENKDQRLTELLLSYGANVNIP 197
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  290 TKDLLTPLHCAARSGHDQVVDLLVVQGAPISAKTKNGLAPLHMAaqgdhvdaartllyhrapvddvtvdyltplhvAAHC 369
Cdd:PHA02878   198 DKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIS--------------------------------VGYC 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  370 GHVRVAKLLLDRSADPNSRA-LNGFTPLHIACKKNRikVVELLLKYRAAIEATTESGLTPLHVAAF----MGAINIVIY- 443
Cdd:PHA02878   246 KDYDILKLLLEHGVDVNAKSyILGLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPLSSAVKqylcINIGRILISn 323
                          330
                   ....*....|....*.
gi 1831513053  444 -LLQQGANPDVETVRG 458
Cdd:PHA02878   324 iCLLKRIKPDIKNSEG 339
PHA03100 PHA03100
ankyrin repeat protein; Provisional
134-355 3.28e-22

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 101.67  E-value: 3.28e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  134 TPLYMAAQENHEEVVKYLLKHGANQALSTEDGFTPLAVALQQGHD-----RVVAVLLEN----DSKGKVRLPALHIAA-- 202
Cdd:PHA03100    37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYganvNAPDNNGITPLLYAIsk 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  203 KKDDTTAATLLLQNEHNPDVTSKSGFTPLHIAAHYGHE--NVGQLLLEKGANVNyqarhnisplhvatkwgRTNMANLLL 280
Cdd:PHA03100   117 KSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDIN-----------------AKNRVNYLL 179
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1831513053  281 SRGAIIDSRTKDLLTPLHCAARSGHDQVVDLLVVQGAPISAKTKNGLAPLHMAAQGDHVDAARTLLYHRAPVDDV 355
Cdd:PHA03100   180 SYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTI 254
PHA02878 PHA02878
ankyrin repeat protein; Provisional
494-777 5.92e-22

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 101.50  E-value: 5.92e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  494 PLHIASRLGNTDIVILLLQAGANSNATTRDNYSPLHIAAKE-GQEEVAGILLDHNADKTLLTKKGFTPlhlASKYGNLEV 572
Cdd:PHA02878    40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEpNKLGMKEMIRSINKCSVFYTLVAIKD---AFNNRNVEI 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  573 VRLLLergtpVDIEGKNQVTPLHVAAHYNND-----KVAMLLLENGASAKAAAKN-GYTPLHIAAKKNQMEIASTLLQFK 646
Cdd:PHA02878   117 FKIIL-----TNRYKNIQTIDLVYIDKKSKDdiieaEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYG 191
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  647 ADPNAKSRAGFTPLHLSAQEGHKEISGLLIENGSDVGAKANNGLTAMHLCAQE-DHVPVAQILYNNGAEINSKTNA-GYT 724
Cdd:PHA02878   192 ANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYIlGLT 271
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1831513053  725 PLHVACHFGQlnMVKFLVENGADVGEKTRASYTPLHQAAQQGHN-NCVRYLLEN 777
Cdd:PHA02878   272 ALHSSIKSER--KLKLLLEYGADINSLNSYKLTPLSSAVKQYLCiNIGRILISN 323
PHA03100 PHA03100
ankyrin repeat protein; Provisional
621-807 2.79e-21

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 98.97  E-value: 2.79e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  621 KNGYTPLHIAAKKNQMEIASTLLQFKADPNAKSRAGFTPLHLSAQEGH-----KEISGLLIENGSDVGAKANNGLTAMHL 695
Cdd:PHA03100    33 KKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITPLLY 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  696 CAQE--DHVPVAQILYNNGAEINSKTNAGYTPLHVA--CHFGQLNMVKFLVENGADVGEKTRasytplhqaaqqghnncV 771
Cdd:PHA03100   113 AISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYleSNKIDLKILKLLIDKGVDINAKNR-----------------V 175
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1831513053  772 RYLLENGASPNEQTATGQTPLSIAQRLGYVSVVETL 807
Cdd:PHA03100   176 NYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYL 211
PHA02875 PHA02875
ankyrin repeat protein; Provisional
325-521 4.56e-21

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 98.14  E-value: 4.56e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  325 NGLAPLHMAAQGDHVDAARTLLYHRAPVDDVTVDYLTPLHVAAHCGHVRVAKLLLDRSADPNSRAL-NGFTPLHIACKKN 403
Cdd:PHA02875    34 DGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYkDGMTPLHLATILK 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  404 RIKVVELLLKYRAAIEATTESGLTPLHVAAFMGAINIVIYLLQQGANPDVETVRGETPLHLAARANQTDVVRVLIRNGAK 483
Cdd:PHA02875   114 KLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGAN 193
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1831513053  484 VDAQARE-LQTPLHIASRLGNTDIVILLLQAGANSNATT 521
Cdd:PHA02875   194 IDYFGKNgCVAALCYAIENNKIDIVRLFIKRGADCNIMF 232
Ank_2 pfam12796
Ankyrin repeats (3 copies);
429-520 5.86e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.02  E-value: 5.86e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  429 LHVAAFMGAINIVIYLLQQGANPDVETVRGETPLHLAARANQTDVVRVLIRNgAKVDAQArELQTPLHIASRLGNTDIVI 508
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|..
gi 1831513053  509 LLLQAGANSNAT 520
Cdd:pfam12796   79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
495-585 6.52e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.02  E-value: 6.52e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  495 LHIASRLGNTDIVILLLQAGANSNATTRDNYSPLHIAAKEGQEEVAGILLDH-NADKTLltkKGFTPLHLASKYGNLEVV 573
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHaDVNLKD---NGRTALHYAARSGHLEIV 77
                           90
                   ....*....|..
gi 1831513053  574 RLLLERGTPVDI 585
Cdd:pfam12796   78 KLLLEKGADINV 89
PHA02875 PHA02875
ankyrin repeat protein; Provisional
535-747 9.71e-21

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 96.98  E-value: 9.71e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  535 GQEEVAGILLDHNADKTLLTKKGFTPLHLASKYGNLEVVRLLLERGTPVDIEGKNQVTPLHVAAHYNN-DKVAMLLLENG 613
Cdd:PHA02875    13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDvKAVEELLDLGK 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  614 ASAKAAAKNGYTPLHIAAKKNQMEIASTLLQFKADPNAKSRAGFTPLHLSAQEGHKEISGLLIENGSDVGAKANNGLTAM 693
Cdd:PHA02875    93 FADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPL 172
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1831513053  694 HLCAQEDHVPVAQILYNNGAEINS-KTNAGYTPLHVACHFGQLNMVKFLVENGAD 747
Cdd:PHA02875   173 IIAMAKGDIAICKMLLDSGANIDYfGKNGCVAALCYAIENNKIDIVRLFIKRGAD 227
PHA02874 PHA02874
ankyrin repeat protein; Provisional
45-270 1.10e-20

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 97.34  E-value: 1.10e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053   45 DLEK--VLELLRAGTDINTSNANGLNSLHLASKEGHSEVVRELIKRQAQVDAATRKGNTALHIASLAGQSLIVTILVENG 122
Cdd:PHA02874   101 CIEKdmIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKG 180
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  123 ANVNVQSVNGFTPLYMAAQENHEEVVKYLLKHGANQALSTEDGFTPLAVALQqgHDRVVAVLLENDskgkvrlpalhiaa 202
Cdd:PHA02874   181 AYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINN-------------- 244
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1831513053  203 kkddttaATLllqnehnpDVTSKSGFTPLHIAAHYG-HENVGQLLLEKGANVNYQARHNISPLHVATKW 270
Cdd:PHA02874   245 -------ASI--------NDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAFKY 298
PHA02878 PHA02878
ankyrin repeat protein; Provisional
103-442 3.10e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 96.10  E-value: 3.10e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  103 LHIASLAGQSLIVTILVENGANVNVQSVNGFTPLYMAAQENHEEVVKYLLKHGANQALSTEdgFTPLAVALQQGHDRVVA 182
Cdd:PHA02878    41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFYT--LVAIKDAFNNRNVEIFK 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  183 VLLENDSKGKVRLPALHIAAK-KDDTTAATLL-LQNEHNPDVTSK---SGFTPLHIAAHYGHENVGQLLLEKGANVNYQA 257
Cdd:PHA02878   119 IILTNRYKNIQTIDLVYIDKKsKDDIIEAEITkLLLSYGADINMKdrhKGNTALHYATENKDQRLTELLLSYGANVNIPD 198
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  258 RHNISPLHVATKWGRTNMANLLLSRGAIIDSRTKDLLTPLHCAARSGHD-QVVDLLVVQGAPISAK-TKNGLAPLHMAAQ 335
Cdd:PHA02878   199 KTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDyDILKLLLEHGVDVNAKsYILGLTALHSSIK 278
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  336 GDhvDAARTLLYHRAPVDDVTVDYLTPLHVAA------HCGHVRVAKLLLDRSADPNSRALNGFTpLHIACKKNRIKVVE 409
Cdd:PHA02878   279 SE--RKLKLLLEYGADINSLNSYKLTPLSSAVkqylciNIGRILISNICLLKRIKPDIKNSEGFI-DNMDCITSNKRLNQ 355
                          330       340       350
                   ....*....|....*....|....*....|....
gi 1831513053  410 LLLKYRAAIEATTESGLTPLHVAA-FMGAINIVI 442
Cdd:PHA02878   356 IKDKCEDELNRLASIKITNTYSFDdFLKCDNSTL 389
Ank_2 pfam12796
Ankyrin repeats (3 copies);
660-751 3.83e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.71  E-value: 3.83e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  660 LHLSAQEGHKEISGLLIENGSDVGAKANNGLTAMHLCAQEDHVPVAQILYNNgAEINSKTNaGYTPLHVACHFGQLNMVK 739
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
                           90
                   ....*....|..
gi 1831513053  740 FLVENGADVGEK 751
Cdd:pfam12796   79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
103-190 7.35e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.94  E-value: 7.35e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  103 LHIASLAGQSLIVTILVENGANVNVQSVNGFTPLYMAAQENHEEVVKYLLKHgaNQALSTEDGFTPLAVALQQGHDRVVA 182
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH--ADVNLKDNGRTALHYAARSGHLEIVK 78

                   ....*...
gi 1831513053  183 VLLENDSK 190
Cdd:pfam12796   79 LLLEKGAD 86
Ank_2 pfam12796
Ankyrin repeats (3 copies);
37-128 7.79e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.94  E-value: 7.79e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053   37 FLRAARAGDLEKVLELLRAGTDINTSNANGLNSLHLASKEGHSEVVRELIKrQAQVDAATrKGNTALHIASLAGQSLIVT 116
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|..
gi 1831513053  117 ILVENGANVNVQ 128
Cdd:pfam12796   79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
330-421 8.51e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.55  E-value: 8.51e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  330 LHMAAQGDHVDAARTLLYHRAPVDDVTVDYLTPLHVAAHCGHVRVAKLLLDRsADPNSRaLNGFTPLHIACKKNRIKVVE 409
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLK-DNGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|..
gi 1831513053  410 LLLKYRAAIEAT 421
Cdd:pfam12796   79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
297-388 9.11e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.55  E-value: 9.11e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  297 LHCAARSGHDQVVDLLVVQGAPISAKTKNGLAPLHMAAQGDHVDAARTLLYHRAPvdDVTVDYLTPLHVAAHCGHVRVAK 376
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|..
gi 1831513053  377 LLLDRSADPNSR 388
Cdd:pfam12796   79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
594-685 1.22e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.17  E-value: 1.22e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  594 LHVAAHYNNDKVAMLLLENGASAKAAAKNGYTPLHIAAKKNQMEIASTLLQfKADPNAKSRaGFTPLHLSAQEGHKEISG 673
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVK 78
                           90
                   ....*....|..
gi 1831513053  674 LLIENGSDVGAK 685
Cdd:pfam12796   79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
198-289 1.42e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.17  E-value: 1.42e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  198 LHIAAKKDDTTAATLLLQNEHNPDVTSKSGFTPLHIAAHYGHENVGQLLLEKgANVNYQARHNiSPLHVATKWGRTNMAN 277
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGR-TALHYAARSGHLEIVK 78
                           90
                   ....*....|..
gi 1831513053  278 LLLSRGAIIDSR 289
Cdd:pfam12796   79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
528-615 2.51e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.40  E-value: 2.51e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  528 LHIAAKEGQEEVAGILLDHNADKTLLTKKGFTPLHLASKYGNLEVVRLLLERGtPVDIEGKNQvTPLHVAAHYNNDKVAM 607
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKDNGR-TALHYAARSGHLEIVK 78

                   ....*...
gi 1831513053  608 LLLENGAS 615
Cdd:pfam12796   79 LLLEKGAD 86
PHA02874 PHA02874
ankyrin repeat protein; Provisional
43-333 8.36e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 91.56  E-value: 8.36e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053   43 AGDLEKVLELLRAGTD-INTSNANGLNSLHLASKEGHSEVVRELIKRQAQVDAATRKGNTALHIASLAGQSLIVTILVEN 121
Cdd:PHA02874    11 SGDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDN 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  122 GAN-----------------------VNVQSVNGFTPLYMAAQENHEEVVKYLLKHGANQALSTEDGFTPLAVALQQGHD 178
Cdd:PHA02874    91 GVDtsilpipciekdmiktildcgidVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFF 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  179 RVVAVLLENDSKGKVrlpalhiaakkddttaatlllqNEHNpdvtsksGFTPLHIAAHYGHENVGQLLLEKGANVNYQAR 258
Cdd:PHA02874   171 DIIKLLLEKGAYANV----------------------KDNN-------GESPLHNAAEYGDYACIKLLIDHGNHIMNKCK 221
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1831513053  259 HNISPLHVATKWGRTNMAnlLLSRGAIIDSRTKDLLTPLHCAARSGHDQ-VVDLLVVQGAPISAKTKNGLAPLHMA 333
Cdd:PHA02874   222 NGFTPLHNAIIHNRSAIE--LLINNASINDQDIDGSTPLHHAINPPCDIdIIDILLYHKADISIKDNKGENPIDTA 295
PHA03095 PHA03095
ankyrin-like protein; Provisional
35-186 1.23e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 91.24  E-value: 1.23e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053   35 ASFLRAARAgDLEKVLELLRAGTDINTSNANGLNSLH--LASKEGHSEVVRELIKRQAQVDAATRKGNTALHiaSLAGQS 112
Cdd:PHA03095   157 AVLLKSRNA-NVELLRLLIDAGADVYAVDDRFRSLLHhhLQSFKPRARIVRELIRAGCDPAATDMLGNTPLH--SMATGS 233
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1831513053  113 ----LIVTILVENGANVNVQSVNGFTPLYMAAQENHEEVVKYLLKHGANQALSTEDGFTPLAVALQQGHDRVVAVLLE 186
Cdd:PHA03095   234 sckrSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALA 311
PHA02875 PHA02875
ankyrin repeat protein; Provisional
44-284 1.40e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 90.44  E-value: 1.40e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053   44 GDLEKVLELLRAGTDINTSNANGLNSLHLASKEGHSEVVRELIKRQAQVDAATRKGNTALHIASLAGQSLIVTILVENGA 123
Cdd:PHA02875    13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  124 NVN-VQSVNGFTPLYMAAQENHEEVVKYLLKHGANQALSTEDGFTPlavalqqghdrvvavllendskgkvrlpaLHIAA 202
Cdd:PHA02875    93 FADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSP-----------------------------LHLAV 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  203 KKDDTTAATLLLQNEHNPDVTSKSGFTPLHIAAHYGHENVGQLLLEKGANVNYQARH-NISPLHVATKWGRTNMANLLLS 281
Cdd:PHA02875   144 MMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNgCVAALCYAIENNKIDIVRLFIK 223

                   ...
gi 1831513053  282 RGA 284
Cdd:PHA02875   224 RGA 226
Ank_2 pfam12796
Ankyrin repeats (3 copies);
726-807 1.69e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.09  E-value: 1.69e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  726 LHVACHFGQLNMVKFLVENGADVGEKTRASYTPLHQAAQQGHNNCVRYLLENgASPNEQTAtGQTPLSIAQRLGYVSVVE 805
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                   ..
gi 1831513053  806 TL 807
Cdd:pfam12796   79 LL 80
PHA02878 PHA02878
ankyrin repeat protein; Provisional
37-302 1.80e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 90.71  E-value: 1.80e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053   37 FLRAARAGDLEKVLELLRAGTDINTSNANGLNSLHLASKE----GHSEVVRELIKRqaQVDAATRKGNTALHIASLAGQS 112
Cdd:PHA02878    41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEpnklGMKEMIRSINKC--SVFYTLVAIKDAFNNRNVEIFK 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  113 LIVTILVENGANVNVQSVNgfTPLYMAAQENheEVVKYLLKHGANQALSTED-GFTPLAVALQQGHDRVVAVLLendSKG 191
Cdd:PHA02878   119 IILTNRYKNIQTIDLVYID--KKSKDDIIEA--EITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLL---SYG 191
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  192 -KVRLP------ALHIAAKKDDTTAATLLLQNEHNPDVTSKSGFTPLHIAAHYGHE-NVGQLLLEKGANVNYQAR-HNIS 262
Cdd:PHA02878   192 aNVNIPdktnnsPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDyDILKLLLEHGVDVNAKSYiLGLT 271
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1831513053  263 PLHVATKWGRTnmANLLLSRGAIIDSRTKDLLTPLHCAAR 302
Cdd:PHA02878   272 ALHSSIKSERK--LKLLLEYGADINSLNSYKLTPLSSAVK 309
PHA02875 PHA02875
ankyrin repeat protein; Provisional
358-554 4.95e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 88.89  E-value: 4.95e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  358 DYLTPLHVAAHCGHVRVAKLLLDRSADPNSRALNGFTPLHIACKKNRIKVVELLLKYRAAI-EATTESGLTPLHVAAFMG 436
Cdd:PHA02875    34 DGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAdDVFYKDGMTPLHLATILK 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  437 AINIVIYLLQQGANPDVETVRGETPLHLAARANQTDVVRVLIRNGAKVDAQARELQTPLHIASRLGNTDIVILLLQAGAN 516
Cdd:PHA02875   114 KLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGAN 193
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1831513053  517 SNATTRD-NYSPLHIAAKEGQEEVAGILLDHNADKTLLT 554
Cdd:PHA02875   194 IDYFGKNgCVAALCYAIENNKIDIVRLFIKRGADCNIMF 232
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
361-579 7.78e-18

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: 89.69  E-value: 7.78e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  361 TPLHVAAHCGHVR-VAKLLLDRSADPNSRALNGFTPLHIACKKNRIKVVELLLkyRAAIE-----ATTE--SGLTPLHVA 432
Cdd:cd22192     19 SPLLLAAKENDVQaIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLM--EAAPElvnepMTSDlyQGETALHIA 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  433 AFMGAINIVIYLLQQGAnpDVETVR----------------GETPLHLAARANQTDVVRVLIRNGAKVDAQarelqtplh 496
Cdd:cd22192     97 VVNQNLNLVRELIARGA--DVVSPRatgtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQ--------- 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  497 iaSRLGNTDIVILLLQAGANSNATTRDnyspLHIAAKEGQEEVAgilLDHnadktLLTKKGFTPLHLASKYGNLEVVRLL 576
Cdd:cd22192    166 --DSLGNTVLHILVLQPNKTFACQMYD----LILSYDKEDDLQP---LDL-----VPNNQGLTPFKLAAKEGNIVMFQHL 231

                   ...
gi 1831513053  577 LER 579
Cdd:cd22192    232 VQK 234
PHA02875 PHA02875
ankyrin repeat protein; Provisional
106-317 8.74e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 88.12  E-value: 8.74e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  106 ASLAGQSLIVTILVENGANVNVQSVNGFTPLYMAAQENHEEVVKYLLKHGANQALSTEDGFTPLAVALQQGHDRVVAVLL 185
Cdd:PHA02875     9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  186 E-----NDSKGKVRLPALHIAAKKDDTTAATLLLQNEHNPDVTSKSGFTPLHIAAHYGHENVGQLLLEKGANVNYQARHN 260
Cdd:PHA02875    89 DlgkfaDDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCG 168
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1831513053  261 ISPLHVATKWGRTNMANLLLSRGAIIDSRTKDLLTPLHCAA-RSGHDQVVDLLVVQGA 317
Cdd:PHA02875   169 CTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAiENNKIDIVRLFIKRGA 226
PHA02874 PHA02874
ankyrin repeat protein; Provisional
568-795 2.66e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 86.56  E-value: 2.66e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  568 GNLEVVRLLLE-RGTPVDIEGKNQVTPLHVAAHYNNDKVAMLLLENGASAKAAAKNGYTPLHIAAKKNQMEIASTLLQFK 646
Cdd:PHA02874    12 GDIEAIEKIIKnKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  647 ADPNAksragftplhLSAQEGHKEISGLLIENGSDVGAKANNGLTAMHLCAQEDHVPVAQILYNNGAEINSKTNAGYTPL 726
Cdd:PHA02874    92 VDTSI----------LPIPCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPI 161
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1831513053  727 HVACHFGQLNMVKFLVENGADVGEKTRASYTPLHQAAQQGHNNCVRYLLENGASPNEQTATGQTPLSIA 795
Cdd:PHA02874   162 HIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA 230
PHA03100 PHA03100
ankyrin repeat protein; Provisional
44-187 5.62e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 85.49  E-value: 5.62e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053   44 GDLEKVLELLRAGTDINTSNANGLNSLHLASKEGH--SEVVRELIKRQAQVDAATRkgntalhiaslagqsliVTILVEN 121
Cdd:PHA03100   119 NSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKNR-----------------VNYLLSY 181
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1831513053  122 GANVNVQSVNGFTPLYMAAQENHEEVVKYLLKHGANQALSTEDGFTPLAVALQQGHDRVVAVLLEN 187
Cdd:PHA03100   182 GVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNN 247
PHA02876 PHA02876
ankyrin repeat protein; Provisional
40-289 1.17e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 85.89  E-value: 1.17e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053   40 AARAGDLEKVL-ELLRAGTDINTSNANGLNSLHLASKEGH-SEVVRELIKRQAQVDAATRKGNTALHIAS-LAGQSLIVT 116
Cdd:PHA02876   280 ASQAPSLSRLVpKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQAStLDRNKDIVI 359
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  117 ILVENGANVNVQSVNGFTPLYMAAQENHEEVVKYLLKHGAN-QALSTEDGftplavalqqghdrvvavllendskgkvrl 195
Cdd:PHA02876   360 TLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADiEALSQKIG------------------------------ 409
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  196 PALHIA-AKKDDTTAATLLLQNEHNPDVTSKSGFTPLHIAAHYGHE-NVGQLLLEKGANVNYQARHNISPLHVATkwGRT 273
Cdd:PHA02876   410 TALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAINIQNQYPLLIAL--EYH 487
                          250
                   ....*....|....*..
gi 1831513053  274 NMANLLLSRGA-IIDSR 289
Cdd:PHA02876   488 GIVNILLHYGAeLRDSR 504
PHA02798 PHA02798
ankyrin-like protein; Provisional
471-682 1.23e-16

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 85.27  E-value: 1.23e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  471 TDVVRVLIRNGAKVDAQARELQTPL-----HIASRLGNTDIVILLLQAGANSNATTRDNYSPLHIAAKEG---QEEVAGI 542
Cdd:PHA02798    51 TDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGyinNLEILLF 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  543 LLDHNADKTLLTKKGFTPLHLASKYGN---LEVVRLLLERGTPVD-IEGKNQVTPLHVAAHYNNDKVAM----LLLENGA 614
Cdd:PHA02798   131 MIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINtHNNKEKYDTLHCYFKYNIDRIDAdilkLFVDNGF 210
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  615 SAKAAAKngytplhiAAKKNQMEIASTLL----QFKA----------DPNAKSRAGFTPLHLSAQEGHKEISGLLIENGS 680
Cdd:PHA02798   211 IINKENK--------SHKKKFMEYLNSLLydnkRFKKnildfifsyiDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGG 282

                   ..
gi 1831513053  681 DV 682
Cdd:PHA02798   283 DI 284
Ank_2 pfam12796
Ankyrin repeats (3 copies);
231-322 3.21e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.54  E-value: 3.21e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  231 LHIAAHYGHENVGQLLLEKGANVNYQARHNISPLHVATKWGRTNMANLLLSRgAIIDSRTKDLlTPLHCAARSGHDQVVD 310
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGR-TALHYAARSGHLEIVK 78
                           90
                   ....*....|..
gi 1831513053  311 LLVVQGAPISAK 322
Cdd:pfam12796   79 LLLEKGADINVK 90
Death pfam00531
Death domain;
1499-1582 1.03e-15

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 73.94  E-value: 1.03e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053 1499 EKDLPEFVhqNVLKGIGADWPRLGRALEVPHRDIQHIRQNYP--GQECKNTLKIWIHLKKEDANQDNLDQALRQIGRDDI 1576
Cdd:pfam00531    1 RKQLDRLL--DPPPPLGKDWRELARKLGLSENEIDEIESENPrlRSQTYELLRLWEQREGKNATVGTLLEALRKLGRRDA 78

                   ....*.
gi 1831513053 1577 VRSIAY 1582
Cdd:pfam00531   79 AEKIQS 84
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
1501-1582 1.28e-15

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: 73.60  E-value: 1.28e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  1501 DLPEFVHQNVLKG-IGADWPRLGRALEVPHRDIQHIRQNYPG---QECKNTLKIWIHLKKEDANQDNLDQALRQIGRDDI 1576
Cdd:smart00005    2 ELTRQKLAKLLDHpLGLDWRELARKLGLSEADIDQIRTEAPRdlaEQSVQLLRLWEQREGKNATLGTLLEALRKMGRDDA 81

                    ....*.
gi 1831513053  1577 VRSIAY 1582
Cdd:smart00005   82 VELLRS 87
PHA02874 PHA02874
ankyrin repeat protein; Provisional
34-194 1.94e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 80.78  E-value: 1.94e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053   34 SASFLR-AARAGDLEKVLELLRAGTDINTSNANGLNSLHLASKEGHSEVVRELIKRQAQVDAATRKGNTALHIASLAGQS 112
Cdd:PHA02874   124 LKTFLHyAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDY 203
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  113 LIVTILVENGANVNVQSVNGFTPLYMAAQENHEEVVkyLLKHGANQALSTEDGFTPLAVALQQGHDR-VVAVLLENDSKG 191
Cdd:PHA02874   204 ACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIE--LLINNASINDQDIDGSTPLHHAINPPCDIdIIDILLYHKADI 281

                   ...
gi 1831513053  192 KVR 194
Cdd:PHA02874   282 SIK 284
PHA02875 PHA02875
ankyrin repeat protein; Provisional
597-782 2.90e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 80.04  E-value: 2.90e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  597 AAHYNNDKVAMLLLENGASAKAAAKNGYTPLHIAAKKNQMEIASTLLQFKADPNAKSRAGFTPLHLSAQEGH-KEISGLL 675
Cdd:PHA02875     9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDvKAVEELL 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  676 IEN--GSDVGAKanNGLTAMHLCAQEDHVPVAQILYNNGAEINSKTNAGYTPLHVACHFGQLNMVKFLVENGADVGEKTR 753
Cdd:PHA02875    89 DLGkfADDVFYK--DGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDC 166
                          170       180
                   ....*....|....*....|....*....
gi 1831513053  754 ASYTPLHQAAQQGHNNCVRYLLENGASPN 782
Cdd:PHA02875   167 CGCTPLIIAMAKGDIAICKMLLDSGANID 195
PHA02878 PHA02878
ankyrin repeat protein; Provisional
558-808 1.33e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 78.77  E-value: 1.33e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  558 FTPLHLASKYGNLEVVRLLLERGTPVDIEGKNQVTPLHVAAHYNNdKVAMLLLengASAKAAAKNGYTPLHI--AAKKNQ 635
Cdd:PHA02878    38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPN-KLGMKEM---IRSINKCSVFYTLVAIkdAFNNRN 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  636 MEIASTLLqfkadpnaksragftplhLSAQEGHKEISGLLIENGSdvgakanngltamhlcaQEDHV--PVAQILYNNGA 713
Cdd:PHA02878   114 VEIFKIIL------------------TNRYKNIQTIDLVYIDKKS-----------------KDDIIeaEITKLLLSYGA 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  714 EINSKT-NAGYTPLHVACHFGQLNMVKFLVENGADVGEKTRASYTPLHQAAQQGHNNCVRYLLENGASPNEQTATGQTPL 792
Cdd:PHA02878   159 DINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPL 238
                          250
                   ....*....|....*.
gi 1831513053  793 SIAqrLGYVSVVETLR 808
Cdd:PHA02878   239 HIS--VGYCKDYDILK 252
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
658-794 6.45e-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: 76.98  E-value: 6.45e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  658 TPLHLSAQEGHKE-ISGLLIENGSDVGAKANNGLTAMHLCAQEDHVPVAQILYNNGAE-----INSKTNAGYTPLHVACH 731
Cdd:cd22192     19 SPLLLAAKENDVQaIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElvnepMTSDLYQGETALHIAVV 98
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1831513053  732 FGQLNMVKFLVENGADVgEKTRASYT---------------PLHQAAQQGHNNCVRYLLENGASPNEQTATGQTPLSI 794
Cdd:cd22192     99 NQNLNLVRELIARGADV-VSPRATGTffrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175
PHA02878 PHA02878
ankyrin repeat protein; Provisional
79-281 6.74e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 76.46  E-value: 6.74e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053   79 SEVVRELIKRQAQVDAATR-KGNTALHIASLAGQSLIVTILVENGANVNVQSVNGFTPLYMAAQENHEEVVKYLLKHGAN 157
Cdd:PHA02878   147 AEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS 226
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  158 QALSTEDGFTPlavalqqghdrvvavllendskgkvrlpaLHIAAKK-DDTTAATLLLqnEHNPDVTSKS---GFTPLHI 233
Cdd:PHA02878   227 TDARDKCGNTP-----------------------------LHISVGYcKDYDILKLLL--EHGVDVNAKSyilGLTALHS 275
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1831513053  234 AAHygHENVGQLLLEKGANVNYQARHNISPLHVATK-WGRTNMANLLLS 281
Cdd:PHA02878   276 SIK--SERKLKLLLEYGADINSLNSYKLTPLSSAVKqYLCINIGRILIS 322
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
27-187 2.23e-13

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 75.67  E-value: 2.23e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053   27 EPGRAEGSASFLRAARAGDLEKVLELLRAGTDINTSNANGLNSLHLASKEGHSEVVRELIKRQAQVDAATRKGNTALHIA 106
Cdd:PLN03192   519 EHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNA 598
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  107 SLAGQSLIVTILVENGANVNVQSvnGFTPLYMAAQENHEEVVKYLLKHGANQALSTEDGFTPLAVALQQGHDRVVAVLLE 186
Cdd:PLN03192   599 ISAKHHKIFRILYHFASISDPHA--AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIM 676

                   .
gi 1831513053  187 N 187
Cdd:PLN03192   677 N 677
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
459-671 2.95e-13

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 74.66  E-value: 2.95e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  459 ETPLHLAARANQTDVVRVLIRNgAKVDAQAREL--QTPLHIASRLGNTDIVILLLQAGAN--SNATTRDNYsplhiaake 534
Cdd:cd22192     18 ESPLLLAAKENDVQAIKKLLKC-PSCDLFQRGAlgETALHVAALYDNLEAAVVLMEAAPElvNEPMTSDLY--------- 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  535 gqeevagilldhnadktlltkKGFTPLHLASKYGNLEVVRLLLERGTPVDiegKNQVT-----------------PLHVA 597
Cdd:cd22192     88 ---------------------QGETALHIAVVNQNLNLVRELIARGADVV---SPRATgtffrpgpknliyygehPLSFA 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  598 AHYNNDKVAMLLLENGASAKAAAKNGYTPLHIAAKKNQMEIASTLLQF--KADPNAKS--------RAGFTPLHLSAQEG 667
Cdd:cd22192    144 ACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFACQMYDLilSYDKEDDLqpldlvpnNQGLTPFKLAAKEG 223

                   ....
gi 1831513053  668 HKEI 671
Cdd:cd22192    224 NIVM 227
Death cd01670
Death Domain: a protein-protein interaction domain; Death Domains (DDs) are protein-protein ...
1512-1580 4.99e-13

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: 66.15  E-value: 4.99e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1831513053 1512 KGIGADWPRLGRALEVPHRDIQHIRQNYPGQE---CKNTLKIWIHLKKEDANQDNLDQALRQIGRDDIVRSI 1580
Cdd:cd01670      7 EELGRDWKKLARKLGLSEGDIDQIEEDNRDDLkeqAYQMLERWREREGDEATLGRLIQALREIGRRDLAEKL 78
PHA02876 PHA02876
ankyrin repeat protein; Provisional
632-807 9.01e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 73.56  E-value: 9.01e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  632 KKNQMEIASTLLQFKADPNAKSRAGFTPLHLSAQEGHKEISGLLIENGSDVGAKANNGLTAMHLCAQEDHVPVAQ----- 706
Cdd:PHA02876   154 QQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKaiidn 233
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  707 ------------------------ILYNNGAEINSKTNAGYTPLHVACHFGQLN-MVKFLVENGADVGEKTRASYTPLHQ 761
Cdd:PHA02876   234 rsninkndlsllkairnedletslLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYL 313
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1831513053  762 AAQQGHNN-CVRYLLENGASPNEQTATGQTPLSIAQRLG-YVSVVETL 807
Cdd:PHA02876   314 MAKNGYDTeNIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITL 361
PHA02875 PHA02875
ankyrin repeat protein; Provisional
40-186 2.19e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 71.18  E-value: 2.19e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053   40 AARAGDLEKVLELLRAGTDIN-TSNANGLNSLHLASKEGHSEVVRELIKRQAQVDAATRKGNTALHIASLAGQSLIVTIL 118
Cdd:PHA02875    75 AVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELL 154
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1831513053  119 VENGANVNVQSVNGFTPLYMAAQENHEEVVKYLLKHGANQALSTEDG-FTPLAVALQQGHDRVVAVLLE 186
Cdd:PHA02875   155 IDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIK 223
PHA02875 PHA02875
ankyrin repeat protein; Provisional
634-807 1.01e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 69.25  E-value: 1.01e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  634 NQMEIASTLLQFKADPNAKSRAGFTPLHLSAQEGHKEISGLLIENGSDVGAKANNGLTAMHLCAQEDHVPVAQILYNNGA 713
Cdd:PHA02875    13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  714 EINSKT-NAGYTPLHVACHFGQLNMVKFLVENGADVGEKTRASYTPLHQAAQQGHNNCVRYLLENGASPNEQTATGQTPL 792
Cdd:PHA02875    93 FADDVFyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPL 172
                          170
                   ....*....|....*
gi 1831513053  793 SIAQRLGYVSVVETL 807
Cdd:PHA02875   173 IIAMAKGDIAICKML 187
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
454-579 1.86e-11

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 69.02  E-value: 1.86e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  454 ETVRGETPLHLAARANQTDVVRVLIRNGAKVDAQAREL--------------QTPLHIASRLGNTDIVILLLQAGANsNA 519
Cdd:cd22194    137 EAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVffnpkykhegfyfgETPLALAACTNQPEIVQLLMEKEST-DI 215
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1831513053  520 TTRDNY--SPLH---IAAKEGQEEVA-------GILLDHNaDKTLLT---KKGFTPLHLASKYGNLEVVRLLLER 579
Cdd:cd22194    216 TSQDSRgnTVLHalvTVAEDSKTQNDfvkrmydMILLKSE-NKNLETirnNEGLTPLQLAAKMGKAEILKYILSR 289
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
213-358 2.43e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 69.13  E-value: 2.43e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  213 LLQNEHNPDVTSKSGFTPLHIAAHYGHENVGQLLLEKGANVNYQARHNISPLHVATKWGRTNMANLLLSRGAIIDSRTK- 291
Cdd:PLN03192   544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAg 623
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1831513053  292 DLLtplhC-AARSGHDQVVDLLVVQGAPISAKTKNGLAPLHMAAQGDHVDAARTLLYHRAPVDDVTVD 358
Cdd:PLN03192   624 DLL----CtAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTD 687
Ank_4 pfam13637
Ankyrin repeats (many copies);
722-775 3.04e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.98  E-value: 3.04e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1831513053  722 GYTPLHVACHFGQLNMVKFLVENGADVGEKTRASYTPLHQAAQQGHNNCVRYLL 775
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
642-780 3.52e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 68.36  E-value: 3.52e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  642 LLQFKADPNAKSRAGFTPLHLSAQEGHKEISGLLIENGSDVGAKANNGLTAMHLCAQEDHVPVAQILYNNGAEinSKTNA 721
Cdd:PLN03192   544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASI--SDPHA 621
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1831513053  722 GYTPLHVACHFGQLNMVKFLVENGADVGEKTRASYTPLHQAAQQGHNNCVRYLLENGAS 780
Cdd:PLN03192   622 AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGAD 680
Ank_4 pfam13637
Ankyrin repeats (many copies);
359-412 7.04e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.21  E-value: 7.04e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1831513053  359 YLTPLHVAAHCGHVRVAKLLLDRSADPNSRALNGFTPLHIACKKNRIKVVELLL 412
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02798 PHA02798
ankyrin-like protein; Provisional
45-287 8.33e-11

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 66.78  E-value: 8.33e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053   45 DLEKVLELLRAGTDINTSNANGLNSLHLASKEGHSEVVRELIKRQAQVDAATRKGNTAL-----HIASLAGQSLIVTILV 119
Cdd:PHA02798    17 KLSTVKLLIKSCNPNEIVNEYSIFQKYLQRDSPSTDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILI 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  120 ENGANVNVQSVNGFTPLYMAAQE---NHEEVVKYLLKHGANQALSTEDGFTPLAVALQQGHD---RVVAVLLE-----ND 188
Cdd:PHA02798    97 ENGADINKKNSDGETPLYCLLSNgyiNNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEkgvdiNT 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  189 SKGKVRLPALHIAAKKD----DTTAATLLLQNE---HNPDVTSKSGFTPLHIAAHYGHENVGQLLLE---KGANVNYQAR 258
Cdd:PHA02798   177 HNNKEKYDTLHCYFKYNidriDADILKLFVDNGfiiNKENKSHKKKFMEYLNSLLYDNKRFKKNILDfifSYIDINQVDE 256
                          250       260
                   ....*....|....*....|....*....
gi 1831513053  259 HNISPLHVATKWGRTNMANLLLSRGAIID 287
Cdd:PHA02798   257 LGFNPLYYSVSHNNRKIFEYLLQLGGDIN 285
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
75-264 8.38e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 67.20  E-value: 8.38e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053   75 KEGHSEVVRELIKRQAQVDAATRKGNTALHIASLaGQSLIVTILVENGANVNVQSVNGFTPLYMAAQENHEEVVKYLLKH 154
Cdd:PLN03192   502 KELHDLNVGDLLGDNGGEHDDPNMASNLLTVAST-GNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKH 580
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  155 GANQALSTEDGFTPLAVALQQGHDRVVAVL--LENDSKGKVRLPALHIAAKKDDTTAATLLLQNEHNPDVTSKSGFTPLH 232
Cdd:PLN03192   581 ACNVHIRDANGNTALWNAISAKHHKIFRILyhFASISDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQ 660
                          170       180       190
                   ....*....|....*....|....*....|...
gi 1831513053  233 IAAHYGHENVGQLLLEKGANVNYQARHN-ISPL 264
Cdd:PLN03192   661 VAMAEDHVDMVRLLIMNGADVDKANTDDdFSPT 693
Ank_5 pfam13857
Ankyrin repeats (many copies);
377-432 1.23e-10

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 58.51  E-value: 1.23e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1831513053  377 LLLDRSADPNSRALNGFTPLHIACKKNRIKVVELLLKYRAAIEATTESGLTPLHVA 432
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
361-579 1.23e-10

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: 66.44  E-value: 1.23e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  361 TPLHVAA---HCGHVRVAKLLLDrsADPNSRALN-------------GFTPLHIACKKNRIKVVELLLKYRAAIEATTES 424
Cdd:cd21882     28 TCLHKAAlnlNDGVNEAIMLLLE--AAPDSGNPKelvnapctdefyqGQTALHIAIENRNLNLVRLLVENGADVSARATG 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  425 gltplhvAAFMGAINIVIYLlqqganpdvetvrGETPLHLAARANQTDVVRVLIRNGAKVDAqarelqtpLHIASRLGNT 504
Cdd:cd21882    106 -------RFFRKSPGNLFYF-------------GELPLSLAACTNQEEIVRLLLENGAQPAA--------LEAQDSLGNT 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  505 DIVILLLQAgansNATTRDNYSPLHIaakegqeeVAGIL-----LDHNADKTLLT-KKGFTPLHLASKYGNLEVVRLLLE 578
Cdd:cd21882    158 VLHALVLQA----DNTPENSAFVCQM--------YNLLLsygahLDPTQQLEEIPnHQGLTPLKLAAVEGKIVMFQHILQ 225

                   .
gi 1831513053  579 R 579
Cdd:cd21882    226 R 226
PHA02798 PHA02798
ankyrin-like protein; Provisional
570-795 1.69e-10

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 65.63  E-value: 1.69e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  570 LEVVRLLLERGTPVDIEgkNQVTPLHVAAHYNNDKVAM--LLLENGASAKAAAKNGYTPL-----HIAAKKNQMEIASTL 642
Cdd:PHA02798    18 LSTVKLLIKSCNPNEIV--NEYSIFQKYLQRDSPSTDIvkLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKIL 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  643 LQFKADPNAKSRAGFTPLHLSAQEGH---KEISGLLIENGSDVGAKANNGLTAMHLCAQEDH---VPVAQILYNNGAEIN 716
Cdd:PHA02798    96 IENGADINKKNSDGETPLYCLLSNGYinnLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDIN 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  717 SKTNA-GYTPLHvaCHFGQ------LNMVKFLVENG---------------------------------------ADVGE 750
Cdd:PHA02798   176 THNNKeKYDTLH--CYFKYnidridADILKLFVDNGfiinkenkshkkkfmeylnsllydnkrfkknildfifsyIDINQ 253
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1831513053  751 KTRASYTPLHQAAQQGHNNCVRYLLENGASPNEQTATGQTPLSIA 795
Cdd:PHA02798   254 VDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTA 298
Ank_4 pfam13637
Ankyrin repeats (many copies);
689-742 2.10e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 57.67  E-value: 2.10e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1831513053  689 GLTAMHLCAQEDHVPVAQILYNNGAEINSKTNAGYTPLHVACHFGQLNMVKFLV 742
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
326-379 2.46e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 57.67  E-value: 2.46e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1831513053  326 GLAPLHMAAQGDHVDAARTLLYHRAPVDDVTVDYLTPLHVAAHCGHVRVAKLLL 379
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
392-579 5.32e-10

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 64.33  E-value: 5.32e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  392 GFTPLHIACKKNRIK-VVELLLKYRAAIEAttesGLTPLHVAA--FMGAINIVIYLLQQGANPDV-----------ETVR 457
Cdd:TIGR00870   52 GRSALFVAAIENENLeLTELLLNLSCRGAV----GDTLLHAISleYVDAVEAILLHLLAAFRKSGplelandqytsEFTP 127
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  458 GETPLHLAARANQTDVVRVLIRNGAKVDAQA--RELQT------------PLHIASRLGNTDIVILLLQAGANSNATTRD 523
Cdd:TIGR00870  128 GITALHLAAHRQNYEIVKLLLERGASVPARAcgDFFVKsqgvdsfyhgesPLNAAACLGSPSIVALLSEDPADILTADSL 207
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1831513053  524 NYSPLHIAAKEGQEEV------------AGILLDHNADKT----LLTKKGFTPLHLASKYGNLEVVRLLLER 579
Cdd:TIGR00870  208 GNTLLHLLVMENEFKAeyeelscqmynfALSLLDKLRDSKelevILNHQGLTPLKLAAKEGRIVLFRLKLAI 279
Ank_4 pfam13637
Ankyrin repeats (many copies);
394-445 6.29e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.51  E-value: 6.29e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1831513053  394 TPLHIACKKNRIKVVELLLKYRAAIEATTESGLTPLHVAAFMGAINIVIYLL 445
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
331-414 6.61e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 64.15  E-value: 6.61e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  331 HMAAQGDHVdAARTLLYHRAPVDDVTVDYLTPLHVAAHCGHVRVAKLLLDRSADPNSRALNGFTPLHIACKKNRIKVVEL 410
Cdd:PTZ00322    88 QLAASGDAV-GARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166

                   ....
gi 1831513053  411 LLKY 414
Cdd:PTZ00322   167 LSRH 170
Ank_4 pfam13637
Ankyrin repeats (many copies);
99-152 7.21e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.13  E-value: 7.21e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1831513053   99 GNTALHIASLAGQSLIVTILVENGANVNVQSVNGFTPLYMAAQENHEEVVKYLL 152
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
623-676 1.08e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.74  E-value: 1.08e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1831513053  623 GYTPLHIAAKKNQMEIASTLLQFKADPNAKSRAGFTPLHLSAQEGHKEISGLLI 676
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
134-421 1.28e-09

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 63.11  E-value: 1.28e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  134 TPLYMAAQENHEEVVKYLLKHganqalSTEDGFTplavalqqghdrvvavllendsKGKVRLPALHIAAKKDDTTAATLL 213
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLLKC------PSCDLFQ----------------------RGALGETALHVAALYDNLEAAVVL 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  214 LQNEH---NPDVTSK--SGFTPLHIAAHYGHENVGQLLLEKGANVnyqarhnISPLhvATkwgrtnmanlllsrGAIIDS 288
Cdd:cd22192     71 MEAAPelvNEPMTSDlyQGETALHIAVVNQNLNLVRELIARGADV-------VSPR--AT--------------GTFFRP 127
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  289 RTKDLLT----PLHCAARSGHDQVVDLLVVQGAPISAKTKNGLAPLHM-AAQGDHVDAART---LLYHRAPVDDVTVDYL 360
Cdd:cd22192    128 GPKNLIYygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHIlVLQPNKTFACQMydlILSYDKEDDLQPLDLV 207
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1831513053  361 tplhvaahcghvrvakllldrsadPNSRalnGFTPLHIACKKNRIKVVELLLKYRAAIEAT 421
Cdd:cd22192    208 ------------------------PNNQ---GLTPFKLAAKEGNIVMFQHLVQKRRHIQWT 241
PHA02946 PHA02946
ankyin-like protein; Provisional
494-744 1.72e-09

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 62.38  E-value: 1.72e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  494 PLHIASRLGNTDIVILLLQAGANSNATTRDNYSPLHIAAKEGQE--EVAGILLDHNAD-KTLLTKKGFTPLhLASKYGNL 570
Cdd:PHA02946    75 PLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEviERINLLVQYGAKiNNSVDEEGCGPL-LACTDPSE 153
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  571 EVVRLLLERGTP---VDIEGKNQVtplHVAAHYNNDKVAML--LLENGASAKAAAKNGYTPLHIAAKKN--QMEIASTLL 643
Cdd:PHA02946   154 RVFKKIMSIGFEariVDKFGKNHI---HRHLMSDNPKASTIswMMKLGISPSKPDHDGNTPLHIVCSKTvkNVDIINLLL 230
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  644 QfKADPNAKSRAGFTPLHL---SAQEGHKeISGLLiengsdvgaKANNGLT--AMHLCAQEDHVPVAQILYNNGAEINSk 718
Cdd:PHA02946   231 P-STDVNKQNKFGDSPLTLlikTLSPAHL-INKLL---------STSNVITdqTVNICIFYDRDDVLEIINDKGKQYDS- 298
                          250       260
                   ....*....|....*....|....*.
gi 1831513053  719 tnagyTPLHVACHFGQLNMVKFLVEN 744
Cdd:PHA02946   299 -----TDFKMAVEVGSIRCVKYLLDN 319
PHA02989 PHA02989
ankyrin repeat protein; Provisional
372-646 2.00e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 62.07  E-value: 2.00e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  372 VRVAKLLLDRSADPNSRALNGfTPL-------HIACKKNRiKVVELLLKYRAAIEATTESGLTPlhVAAFM-----GAIN 439
Cdd:PHA02989    50 IKIVKLLIDNGADVNYKGYIE-TPLcavlrnrEITSNKIK-KIVKLLLKFGADINLKTFNGVSP--IVCFIynsniNNCD 125
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  440 IVIYLLQQGAN-PDVETVRGETPLH--LAARANQTDVVRVLIRNGAKVDAQARELQ-TPLHIASR----LGNTDIVILLL 511
Cdd:PHA02989   126 MLRFLLSKGINvNDVKNSRGYNLLHmyLESFSVKKDVIKILLSFGVNLFEKTSLYGlTPMNIYLRndidVISIKVIKYLI 205
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  512 QAGANSNATTrdnysplhiaakEGQEEVAGILLDHNadKTLLTKKgFTPLHLASKYgnlevvrlllergTPVDIEGKNQV 591
Cdd:PHA02989   206 KKGVNIETNN------------NGSESVLESFLDNN--KILSKKE-FKVLNFILKY-------------IKINKKDKKGF 257
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1831513053  592 TPLHVAAHYNNDKVAMLLLENGASAKAAAKNGYTPLHIAAKKNQMEIASTLLQFK 646
Cdd:PHA02989   258 NPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNRILQLK 312
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
516-666 2.07e-09

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 62.41  E-value: 2.07e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  516 NSNATTRDNYSPLHIAAKEGQ-EEVAGILLDHNADKTLltkkGFTPLHLASK--YGNLEVVRLLLE-----RGTP---VD 584
Cdd:TIGR00870   44 NINCPDRLGRSALFVAAIENEnLELTELLLNLSCRGAV----GDTLLHAISLeyVDAVEAILLHLLaafrkSGPLelaND 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  585 IEGKN---QVTPLHVAAHYNNDKVAMLLLENGASAKAAAK--------------NGYTPLHIAAKKNQMEIASTLLQFKA 647
Cdd:TIGR00870  120 QYTSEftpGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPA 199
                          170
                   ....*....|....*....
gi 1831513053  648 DPNAKSRAGFTPLHLSAQE 666
Cdd:TIGR00870  200 DILTADSLGNTLLHLLVME 218
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
38-249 2.22e-09

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 62.34  E-value: 2.22e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053   38 LRAARAGDLEKVLELLR-AGTDINTSNANGLNSLHLASKEGHSEVVRELIkrqaqvDAATR-----------KGNTALHI 105
Cdd:cd22192     22 LLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLM------EAAPElvnepmtsdlyQGETALHI 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  106 ASLAGQSLIVTILVENGANVNVQSVNG--FT------------PLYMAAQENHEEVVKYLLKHGANqalstedgftplav 171
Cdd:cd22192     96 AVVNQNLNLVRELIARGADVVSPRATGtfFRpgpknliyygehPLSFAACVGNEEIVRLLIEHGAD-------------- 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  172 alqqghdrvvavLLENDSKGKVrlpALHIAAKKDDTTAAT----LLL-----QNEHNPD-VTSKSGFTPLHIAAHYGHEN 241
Cdd:cd22192    162 ------------IRAQDSLGNT---VLHILVLQPNKTFACqmydLILsydkeDDLQPLDlVPNNQGLTPFKLAAKEGNIV 226

                   ....*...
gi 1831513053  242 VGQLLLEK 249
Cdd:cd22192    227 MFQHLVQK 234
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
545-726 2.37e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 62.58  E-value: 2.37e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  545 DHNADKTLLTkkgftplhlASKYGNLEVVRLLLERGTPVDIEGKNQVTPLHVAAHYNNDKVAMLLLENGASAKAAAKNGY 624
Cdd:PLN03192   522 DPNMASNLLT---------VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGN 592
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  625 TPLHIAAKKNQMEIASTLLQFKADPNakSRAGFTPLHLSAQEGHKEISGLLIENGSDVGAKANNGLTAMHLCAQEDHVPV 704
Cdd:PLN03192   593 TALWNAISAKHHKIFRILYHFASISD--PHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDM 670
                          170       180
                   ....*....|....*....|...
gi 1831513053  705 AQILYNNGAEIN-SKTNAGYTPL 726
Cdd:PLN03192   671 VRLLIMNGADVDkANTDDDFSPT 693
Ank_5 pfam13857
Ankyrin repeats (many copies);
741-795 2.51e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 54.66  E-value: 2.51e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1831513053  741 LVENG-ADVGEKTRASYTPLHQAAQQGHNNCVRYLLENGASPNEQTATGQTPLSIA 795
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
16-249 3.02e-09

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: 62.08  E-value: 3.02e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053   16 ESQEVQAPAAPEPGRAEGSASFLRAARAGDLEKVLELLR---------AGTDIN-------TSNANGLNSLH---LASKE 76
Cdd:cd22194     28 PSNPNSPSAELAKEEQRDKKKRLKKVSEAAVEELGELLKelkdlsrrrRKTDVPdflmhklTASDTGKTCLMkalLNINE 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053   77 GHSEVVRELI---------KR--QAQVDAATRKGNTALHIASLAGQSLIVTILVENGANVNVQSVNGF------------ 133
Cdd:cd22194    108 NTKEIVRILLafaeengilDRfiNAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVFfnpkykhegfyf 187
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  134 --TPLYMAAQENHEEVVKYLLKHGANQalstedgftplaVALQqghdrvvavllenDSKGKVRLPALHIAAKKDDTTAA- 210
Cdd:cd22194    188 geTPLALAACTNQPEIVQLLMEKESTD------------ITSQ-------------DSRGNTVLHALVTVAEDSKTQNDf 242
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1831513053  211 ------TLLL--QNEHNPDVTSKSGFTPLHIAAHYGHENVGQLLLEK 249
Cdd:cd22194    243 vkrmydMILLksENKNLETIRNNEGLTPLQLAAKMGKAEILKYILSR 289
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
432-627 3.31e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 61.81  E-value: 3.31e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  432 AAFMGAINIVIYLLQQGANPDVETVRGETPLHLAARANQTDVVRVLIRNGAKVDAQARELQTPLHIASRLGNTDIVILLL 511
Cdd:PLN03192   532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY 611
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  512 QAGANSNATTrdnysplhiaakegqeevAGILldhnadktlltkkgftpLHLASKYGNLEVVRLLLERGTPVDIEGKNQV 591
Cdd:PLN03192   612 HFASISDPHA------------------AGDL-----------------LCTAAKRNDLTAMKELLKQGLNVDSEDHQGA 656
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1831513053  592 TPLHVAAHYNNDKVAMLLLENGASA-KAAAKNGYTPL 627
Cdd:PLN03192   657 TALQVAMAEDHVDMVRLLIMNGADVdKANTDDDFSPT 693
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
416-546 4.31e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 61.45  E-value: 4.31e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  416 AAIEATTESGLTPLHVAAFMGAIN-IVIYLLQqganpdVETVrgetplHLAARANQTDVvRVLIRNGAKVDAQARELQTP 494
Cdd:PTZ00322    52 EALEATENKDATPDHNLTTEEVIDpVVAHMLT------VELC------QLAASGDAVGA-RILLTGGADPNCRDYDGRTP 118
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1831513053  495 LHIASRLGNTDIVILLLQAGANSNATTRDNYSPLHIAAKEGQEEVAGILLDH 546
Cdd:PTZ00322   119 LHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
Ank_4 pfam13637
Ankyrin repeats (many copies);
294-346 5.11e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.82  E-value: 5.11e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1831513053  294 LTPLHCAARSGHDQVVDLLVVQGAPISAKTKNGLAPLHMAAQGDHVDAARTLL 346
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
519-711 5.26e-09

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 61.18  E-value: 5.26e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  519 ATTRDNYSPLHIAAKEGQ-EEVAGILLDHNADktLLTKK--GFTPLHLASKYGNLEVVRLLLErGTPVDI---------E 586
Cdd:cd22192     12 QQKRISESPLLLAAKENDvQAIKKLLKCPSCD--LFQRGalGETALHVAALYDNLEAAVVLME-AAPELVnepmtsdlyQ 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  587 GKnqvTPLHVAAHYNNDKVAMLLLENGAS-AKAAA---------KN----GYTPLHIAAKKNQMEIASTLLQFKADPNAK 652
Cdd:cd22192     89 GE---TALHIAVVNQNLNLVRELIARGADvVSPRAtgtffrpgpKNliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQ 165
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1831513053  653 SRAGFTPLHLSAQEGHKEISGLLIE---------NGSDVGAKANN-GLTAMHLCAQEDHVPVAQILYNN 711
Cdd:cd22192    166 DSLGNTVLHILVLQPNKTFACQMYDlilsydkedDLQPLDLVPNNqGLTPFKLAAKEGNIVMFQHLVQK 234
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
361-486 5.69e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 61.04  E-value: 5.69e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  361 TPLHVAAHCGHVRVAKLLLDRSADPNSRALNGFTPLHIACKKNRIKVVELLLKYRAAIEATTESGLtpLHVAAFMGAINI 440
Cdd:PLN03192   560 TPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAGDL--LCTAAKRNDLTA 637
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1831513053  441 VIYLLQQGANPDVETVRGETPLHLAARANQTDVVRVLIRNGAKVDA 486
Cdd:PLN03192   638 MKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDK 683
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
502-577 6.60e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 60.68  E-value: 6.60e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1831513053  502 GNTDIVILLLQAGANSNATTRDNYSPLHIAAKEGQEEVAGILLDHNADKTLLTKKGFTPLHLASKYGNLEVVRLLL 577
Cdd:PTZ00322    93 GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
Ank_4 pfam13637
Ankyrin repeats (many copies);
524-577 7.41e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.43  E-value: 7.41e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1831513053  524 NYSPLHIAAKEGQEEVAGILLDHNADKTLLTKKGFTPLHLASKYGNLEVVRLLL 577
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
592-643 1.01e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.05  E-value: 1.01e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1831513053  592 TPLHVAAHYNNDKVAMLLLENGASAKAAAKNGYTPLHIAAKKNQMEIASTLL 643
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
543-687 1.54e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 59.88  E-value: 1.54e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  543 LLDHNADKTLLTKKGFTPLHLASKYGNLEVVRLLLERGTPVDIEGKNQVTPLHVAAHYNNDKVAMLLLENgasakAAAKN 622
Cdd:PLN03192   544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHF-----ASISD 618
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1831513053  623 GYTP---LHIAAKKNQMEIASTLLQFKADPNAKSRAGFTPLHLSAQEGHKEISGLLIENGSDVgAKAN 687
Cdd:PLN03192   619 PHAAgdlLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV-DKAN 685
Ank_4 pfam13637
Ankyrin repeats (many copies);
460-511 1.64e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 1.64e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1831513053  460 TPLHLAARANQTDVVRVLIRNGAKVDAQARELQTPLHIASRLGNTDIVILLL 511
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02946 PHA02946
ankyin-like protein; Provisional
82-293 1.66e-08

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 58.91  E-value: 1.66e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053   82 VRELIKRQAQVDAATRKGNTALHIASLAGQSLIVTILVENGANVNVQSVNGFTPLYMAAQENHE--EVVKYLLKHGANQA 159
Cdd:PHA02946    55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEviERINLLVQYGAKIN 134
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  160 LST-EDGFTPLAVAL---QQGHDRVVAVLLENDSKGKVRLPALHIAAKKDDTTAATL--LLQNEHNPDVTSKSGFTPLHI 233
Cdd:PHA02946   135 NSVdEEGCGPLLACTdpsERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNPKASTIswMMKLGISPSKPDHDGNTPLHI 214
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1831513053  234 AAHYGHENVGQL-LLEKGANVNYQARHNISPLHVATK-WGRTNMANLLLSRGAIIDSRTKDL 293
Cdd:PHA02946   215 VCSKTVKNVDIInLLLPSTDVNKQNKFGDSPLTLLIKtLSPAHLINKLLSTSNVITDQTVNI 276
Ank_4 pfam13637
Ankyrin repeats (many copies);
194-247 1.69e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 1.69e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1831513053  194 RLPALHIAAKKDDTTAATLLLQNEHNPDVTSKSGFTPLHIAAHYGHENVGQLLL 247
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
375-445 1.77e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 59.53  E-value: 1.77e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1831513053  375 AKLLLDRSADPNSRALNGFTPLHIACKKNRIKVVELLLKYRAAIEATTESGLTPLHVAAFMGAINIVIYLL 445
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
378-528 2.51e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 59.11  E-value: 2.51e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  378 LLDRSADPNSRALNGFTPLHIACKKNRIKVVELLLKYRAAIEATTESGLTPL--HVAAFMGAINIVIYLLQQGANPDVet 455
Cdd:PLN03192   544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnAISAKHHKIFRILYHFASISDPHA-- 621
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1831513053  456 vrGETPLHLAARANQTDVVRVLIRNGAKVDAQARELQTPLHIASRLGNTDIVILLLQAGAN-SNATTRDNYSPL 528
Cdd:PLN03192   622 --AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADvDKANTDDDFSPT 693
Ank_4 pfam13637
Ankyrin repeats (many copies);
756-807 2.67e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.89  E-value: 2.67e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1831513053  756 YTPLHQAAQQGHNNCVRYLLENGASPNEQTATGQTPLSIAQRLGYVSVVETL 807
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA02989 PHA02989
ankyrin repeat protein; Provisional
241-568 2.95e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 58.60  E-value: 2.95e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  241 NVGQLLLEKGANVNYQARHN-ISPLHVATKWGRTNMANLLLSRGAIIDSRTKdLLTPLHCAAR------SGHDQVVDLLV 313
Cdd:PHA02989    17 NALEFLLRTGFDVNEEYRGNsILLLYLKRKDVKIKIVKLLIDNGADVNYKGY-IETPLCAVLRnreitsNKIKKIVKLLL 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  314 VQGAPISAKTKNGLAPLHMAAQGDHVDaartllyhrapvddvTVDYLtplhvaahcghvrvaKLLLDRSADPNS-RALNG 392
Cdd:PHA02989    96 KFGADINLKTFNGVSPIVCFIYNSNIN---------------NCDML---------------RFLLSKGINVNDvKNSRG 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  393 FTPLHIACKK--NRIKVVELLLKYRAAI-EATTESGLTPLHV--AAFMGAINI-VI-YLLQQGANPDVETVRGETPLHLA 465
Cdd:PHA02989   146 YNLLHMYLESfsVKKDVIKILLSFGVNLfEKTSLYGLTPMNIylRNDIDVISIkVIkYLIKKGVNIETNNNGSESVLESF 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  466 ARANQ---TDVVRVL--IRNGAKVDAQARELQTPLHIASRLGNTDIVILLLQAGANSNATTRDNYSPLHIAAKEGQEEVA 540
Cdd:PHA02989   226 LDNNKilsKKEFKVLnfILKYIKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDML 305
                          330       340
                   ....*....|....*....|....*...
gi 1831513053  541 GILLDHNADKTLLtKKGFTPLhlaSKYG 568
Cdd:PHA02989   306 NRILQLKPGKYLI-KKTFEYF---SEHG 329
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
408-563 3.29e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 58.73  E-value: 3.29e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  408 VELLLKYRAAIEATTESGLTPLHVAAFMGAINIVIYLLQQGANPDVETVRGETPLHLAARANQTDVVRVLIRNGAKVDAQ 487
Cdd:PLN03192   541 LEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPH 620
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1831513053  488 ARelQTPLHIASRLGNTDIVILLLQAGANSNATTRDNYSPLHIAAKEGQEEVAGILLDHNADKTLL-TKKGFTPLHL 563
Cdd:PLN03192   621 AA--GDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAnTDDDFSPTEL 695
PHA02798 PHA02798
ankyrin-like protein; Provisional
405-650 4.14e-08

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 57.92  E-value: 4.14e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  405 IKVVELLLKYRAAIEATTESGLTPL-----HVAAFMGAINIVIYLLQQGANPDVETVRGETPLHLA---ARANQTDVVRV 476
Cdd:PHA02798    51 TDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLlsnGYINNLEILLF 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  477 LIRNGAKVDAQARELQTPLHIASRLGNT---DIVILLLQAGANSNA-TTRDNYSPLHIAAKEGQEEVAGILLDHNADKTL 552
Cdd:PHA02798   131 MIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDINThNNKEKYDTLHCYFKYNIDRIDADILKLFVDNGF 210
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  553 L-------TKKGF----TPLHLASKYGNLEVVRLLLergTPVDIEGKNQ--VTPLHVAAHYNNDKVAMLLLENGASAKAA 619
Cdd:PHA02798   211 IinkenksHKKKFmeylNSLLYDNKRFKKNILDFIF---SYIDINQVDElgFNPLYYSVSHNNRKIFEYLLQLGGDINII 287
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1831513053  620 AKNGYTPLHIAAKKNQMEIASTLLQFKADPN 650
Cdd:PHA02798   288 TELGNTCLFTAFENESKFIFNSILNKKPNKN 318
Ank_4 pfam13637
Ankyrin repeats (many copies);
229-280 4.32e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.12  E-value: 4.32e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1831513053  229 TPLHIAAHYGHENVGQLLLEKGANVNYQARHNISPLHVATKWGRTNMANLLL 280
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
98-256 4.74e-08

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 57.97  E-value: 4.74e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053   98 KGNTALHIASLAGQSLIVTILVENGANVNVQSVNGF-------------TPLYMAAQENHEEVVKYLLKHGANqalsted 164
Cdd:cd21882     72 QGQTALHIAIENRNLNLVRLLVENGADVSARATGRFfrkspgnlfyfgeLPLSLAACTNQEEIVRLLLENGAQ------- 144
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  165 gftplavalqqghdrvVAVLLENDSKGKVRLPALHIAAKK--DDTTAAT----LLLQNEHNPD-------VTSKSGFTPL 231
Cdd:cd21882    145 ----------------PAALEAQDSLGNTVLHALVLQADNtpENSAFVCqmynLLLSYGAHLDptqqleeIPNHQGLTPL 208
                          170       180
                   ....*....|....*....|....*
gi 1831513053  232 HIAAHYGHENVGQLLLEKGANVNYQ 256
Cdd:cd21882    209 KLAAVEGKIVMFQHILQREFSGPYQ 233
Ank_5 pfam13857
Ankyrin repeats (many copies);
707-762 7.27e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.42  E-value: 7.27e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1831513053  707 ILYNNGAEINSKTNAGYTPLHVACHFGQLNMVKFLVENGADVGEKTRASYTPLHQA 762
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
694-792 8.22e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.22  E-value: 8.22e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  694 HLCAQEDHVPvAQILYNNGAEINSKTNAGYTPLHVACHFGQLNMVKFLVENGADVGEKTRASYTPLHQAAQQGHNNCVRY 773
Cdd:PTZ00322    88 QLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166
                           90       100
                   ....*....|....*....|....*.
gi 1831513053  774 LL-------ENGASPNEQTATGQTPL 792
Cdd:PTZ00322   167 LSrhsqchfELGANAKPDSFTGKPPS 192
PHA02859 PHA02859
ankyrin repeat protein; Provisional
492-634 8.57e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 54.44  E-value: 8.57e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  492 QTPLH--IASRLGNTDIVILLLQAGANSNATTRD-NYSPLH---IAAKEGQEEVAGILLDHNADKTLLTKKGFTPLH--L 563
Cdd:PHA02859    52 ETPIFscLEKDKVNVEILKFLIENGADVNFKTRDnNLSALHhylSFNKNVEPEILKILIDSGSSITEEDEDGKNLLHmyM 131
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1831513053  564 ASKYGNLEVVRLLLERGTPVDIEGKNQVTPLHVAAHYNND-KVAMLLLENGASAKAAAKNGYTPLHIAAKKN 634
Cdd:PHA02859   132 CNFNVRINVIKLLIDSGVSFLNKDFDNNNILYSYILFHSDkKIFDFLTSLGIDINETNKSGYNCYDLIKFRN 203
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
114-485 1.03e-07

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 57.23  E-value: 1.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  114 IVTILVENGANVNVQSVNGFTPL--YMAAQENHEEVVKYLLKHGANQALSTEDGFTPLAVALQQG---HDRVVAVLLEND 188
Cdd:PHA02716   194 ILEWLCNNGVNVNLQNNHLITPLhtYLITGNVCASVIKKIIELGGDMDMKCVNGMSPIMTYIINIdniNPEITNIYIESL 273
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  189 SKGKVR-LPA-LHI---AAKKDDTTAATLLLQNEHNPDVTSKSGFTPLH--IAAHYGHENVGQLLLEKGANVNYQARHNI 261
Cdd:PHA02716   274 DGNKVKnIPMiLHSyitLARNIDISVVYSFLQPGVKLHYKDSAGRTCLHqyILRHNISTDIIKLLHEYGNDLNEPDNIGN 353
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  262 SPLHvaTKWGRTNMANlllsrgaIIDSRTKDLLtplhcaarsgHDQVVDLLVVQGAPISAKTKNGLAPLhmaaqGDHVDA 341
Cdd:PHA02716   354 TVLH--TYLSMLSVVN-------ILDPETDNDI----------RLDVIQCLISLGADITAVNCLGYTPL-----TSYICT 409
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  342 ARTLLYHrapvdDVtVDYLTPLHVAAHCGHvRVAKLLLDRSAD--------------PNSRALNGFTPLHiACKKNRIKV 407
Cdd:PHA02716   410 AQNYMYY-----DI-IDCLISDKVLNMVKH-RILQDLLIRVDDtpciihhiiakyniPTDLYTDEYEPYD-STKIHDVYH 481
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  408 VELLLKYRAAIEATteSGLTPLHVAAFM-GAINIV----IYLLQQGANPDVETVRGETPLHLAARAN-----QTDVVRVL 477
Cdd:PHA02716   482 CAIIERYNNAVCET--SGMTPLHVSIIShTNANIVmdsfVYLLSIQYNINIPTKNGVTPLMLTMRNNrlsghQWYIVKNI 559

                   ....*...
gi 1831513053  478 IRNGAKVD 485
Cdd:PHA02716   560 LDKRPNVD 567
PHA02875 PHA02875
ankyrin repeat protein; Provisional
32-157 1.21e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 56.15  E-value: 1.21e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053   32 EGSASFLRAARAGDLEKVLELLRAGTDINTSNANGLNSLHLASKEGHSEVVRELIKRQAQVDAATRKGNTALHIASLAGQ 111
Cdd:PHA02875   101 DGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGD 180
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1831513053  112 SLIVTILVENGANVNVQSVNG-FTPLYMAAQENHEEVVKYLLKHGAN 157
Cdd:PHA02875   181 IAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGAD 227
PHA02859 PHA02859
ankyrin repeat protein; Provisional
658-794 1.90e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 53.67  E-value: 1.90e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  658 TPLH--LSAQEGHKEISGLLIENGSDVGAKA-NNGLTAMH--LCAQEDHVP-VAQILYNNGAEINSKTNAGYTPLHV-AC 730
Cdd:PHA02859    53 TPIFscLEKDKVNVEILKFLIENGADVNFKTrDNNLSALHhyLSFNKNVEPeILKILIDSGSSITEEDEDGKNLLHMyMC 132
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1831513053  731 HFG-QLNMVKFLVENGADVGEKTRA------SYTPLHQaaqqgHNNCVRYLLENGASPNEQTATGQTPLSI 794
Cdd:PHA02859   133 NFNvRINVIKLLIDSGVSFLNKDFDnnnilySYILFHS-----DKKIFDFLTSLGIDINETNKSGYNCYDL 198
Ank_4 pfam13637
Ankyrin repeats (many copies);
425-478 2.01e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.20  E-value: 2.01e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1831513053  425 GLTPLHVAAFMGAINIVIYLLQQGANPDVETVRGETPLHLAARANQTDVVRVLI 478
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
134-185 2.73e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.81  E-value: 2.73e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1831513053  134 TPLYMAAQENHEEVVKYLLKHGANQALSTEDGFTPLAVALQQGHDRVVAVLL 185
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
595-686 2.97e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 55.29  E-value: 2.97e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  595 HVAAhyNNDKV-AMLLLENGASAKAAAKNGYTPLHIAAKKNQMEIASTLLQFKADPNAKSRAGFTPLHLSAQEGHKEISG 673
Cdd:PTZ00322    88 QLAA--SGDAVgARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165
                           90
                   ....*....|....*.
gi 1831513053  674 LLI---ENGSDVGAKA 686
Cdd:PTZ00322   166 LLSrhsQCHFELGANA 181
Death_FADD cd08306
Fas-associated Death Domain protein-protein interaction domain; Death domain (DD) found in ...
1504-1569 4.26e-07

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: 49.22  E-value: 4.26e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1831513053 1504 EFVHQNVlkgiGADWPRLGRALEVPHRDIQHIRQNYP------GQECkntLKIWIHLKKEDANQDNLDQALR 1569
Cdd:cd08306      6 DVICENL----GRDWRQLARKLGLSETKIESISEAHPrnlreqVRQS---LREWKKIKKAEATVADLIKALR 70
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
110-415 5.75e-07

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 54.70  E-value: 5.75e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  110 GQSLIVTILVENGANVNVQSVN--GFTPLYMAAQEN-HEEVVKYLLKHGANQALstedGFTPLAVALQQGHDRVVAVL-L 185
Cdd:TIGR00870   28 GDLASVYRDLEEPKKLNINCPDrlGRSALFVAAIENeNLELTELLLNLSCRGAV----GDTLLHAISLEYVDAVEAILlH 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  186 ENDSKGKVRLPALHIAAKKDDTTAatlllqnehnpdvtsksGFTPLHIAAHYGHENVGQLLLEKGANVNYQARHN---IS 262
Cdd:TIGR00870  104 LLAAFRKSGPLELANDQYTSEFTP-----------------GITALHLAAHRQNYEIVKLLLERGASVPARACGDffvKS 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  263 PLHVATKWGRtnmanlllsrgaiidsrtkdllTPLHCAARSGHDQVVDLLVVQGAPISAKTKNGLAPLHMAA-QGDHVDA 341
Cdd:TIGR00870  167 QGVDSFYHGE----------------------SPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVmENEFKAE 224
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1831513053  342 ARTLLYHrapVDDVTVDYLtplhvaAHCGHVRVAKLLLDRsadpnsralNGFTPLHIACKKNRIKVVELLL--KYR 415
Cdd:TIGR00870  225 YEELSCQ---MYNFALSLL------DKLRDSKELEVILNH---------QGLTPLKLAAKEGRIVLFRLKLaiKYK 282
Ank_4 pfam13637
Ankyrin repeats (many copies);
493-544 5.80e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.04  E-value: 5.80e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1831513053  493 TPLHIASRLGNTDIVILLLQAGANSNATTRDNYSPLHIAAKEGQEEVAGILL 544
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
52-106 6.10e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.11  E-value: 6.10e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1831513053   52 LLRAGT-DINTSNANGLNSLHLASKEGHSEVVRELIKRQAQVDAATRKGNTALHIA 106
Cdd:pfam13857    1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
107-185 7.46e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.13  E-value: 7.46e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1831513053  107 SLAGQSLIVTILVENGANVNVQSVNGFTPLYMAAQENHEEVVKYLLKHGANQALSTEDGFTPLAVALQQGHDRVVAVLL 185
Cdd:PTZ00322    90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
181-312 7.65e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.13  E-value: 7.65e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  181 VAVLLENDSKGKVRLPALHIAAKKDDTTAATLLLQNEHNPDVTSKSGFTPLHIAAhyGHENVG-QLLLEKGANVNYQARH 259
Cdd:PTZ00322    37 MAAIQEEIARIDTHLEALEATENKDATPDHNLTTEEVIDPVVAHMLTVELCQLAA--SGDAVGaRILLTGGADPNCRDYD 114
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1831513053  260 NISPLHVATKWGRTNMANLLLSRGAIIDSRTKDLLTPLHCAARSGHDQVVDLL 312
Cdd:PTZ00322   115 GRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
Ank_5 pfam13857
Ankyrin repeats (many copies);
213-267 8.11e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.73  E-value: 8.11e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1831513053  213 LLQNEH-NPDVTSKSGFTPLHIAAHYGHENVGQLLLEKGANVNYQARHNISPLHVA 267
Cdd:pfam13857    1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
614-743 9.05e-07

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 53.99  E-value: 9.05e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  614 ASAKAAAKNGYTPLHIAAKKNQMEIASTLLQFKADPNAKSRAGF--------------TPLHLSAQEGHKEISGLLIENG 679
Cdd:cd22194    132 AEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVFfnpkykhegfyfgeTPLALAACTNQPEIVQLLMEKE 211
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1831513053  680 SDVGA----KANNGLTAMHLCAQEDHVPVA-------QILYNNGAEINSKT--NAGYTPLHVACHFGQLNMVKFLVE 743
Cdd:cd22194    212 STDITsqdsRGNTVLHALVTVAEDSKTQNDfvkrmydMILLKSENKNLETIrnNEGLTPLQLAAKMGKAEILKYILS 288
Ank_5 pfam13857
Ankyrin repeats (many copies);
477-531 1.03e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.34  E-value: 1.03e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1831513053  477 LIRNG-AKVDAQARELQTPLHIASRLGNTDIVILLLQAGANSNATTRDNYSPLHIA 531
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
20-136 1.06e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 53.72  E-value: 1.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053   20 VQAPAAPEPGRAEGSASFLRAARAGDLEKVLELLRAGTDINTSNANG---------------LNSLH------------- 71
Cdd:PLN03192   545 LKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGntalwnaisakhhkiFRILYhfasisdphaagd 624
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1831513053   72 ---LASKEGHSEVVRELIKRQAQVDAATRKGNTALHIASLAGQSLIVTILVENGANVNVQSV-NGFTPL 136
Cdd:PLN03192   625 llcTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTdDDFSPT 693
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
131-157 1.06e-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: 46.43  E-value: 1.06e-06
                            10        20
                    ....*....|....*....|....*..
gi 1831513053   131 NGFTPLYMAAQENHEEVVKYLLKHGAN 157
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
Ank_5 pfam13857
Ankyrin repeats (many copies);
444-498 1.20e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.96  E-value: 1.20e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1831513053  444 LLQQG-ANPDVETVRGETPLHLAARANQTDVVRVLIRNGAKVDAQARELQTPLHIA 498
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
513-610 1.28e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.36  E-value: 1.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  513 AGANSNATTRDNYSP--LHIAAKE-------GQEEVAGILLDHNADKTLLTKKGFTPLHLASKYGNLEVVRLLLERGTPV 583
Cdd:PTZ00322    62 ATPDHNLTTEEVIDPvvAHMLTVElcqlaasGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADP 141
                           90       100
                   ....*....|....*....|....*..
gi 1831513053  584 DIEGKNQVTPLHVAAHYNNDKVAMLLL 610
Cdd:PTZ00322   142 TLLDKDGKTPLELAEENGFREVVQLLS 168
PHA02946 PHA02946
ankyin-like protein; Provisional
561-794 1.41e-06

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 52.75  E-value: 1.41e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  561 LHLASKYG--NLEVVRLLLERGTPvdiEGKNQVTPLHVAAHYNNDKVAMLLLENGASAKAAAKNGYTPLHIAAKKNQMEI 638
Cdd:PHA02946    11 LSLYAKYNskNLDVFRNMLQAIEP---SGNYHILHAYCGIKGLDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRI 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  639 ASTLLQFKADPNAKSRAGFTPLHLSAQEGHKEIS--GLLIEngsdVGAKANN-----GLTAMHLCAQEDHVPVAQIL-YN 710
Cdd:PHA02946    88 VAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIEriNLLVQ----YGAKINNsvdeeGCGPLLACTDPSERVFKKIMsIG 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  711 NGAEINSKTNAGYTPLHVACHFGQLNMVKFLVENGADVGEKTRASYTPLHQAAQQGHNNC-VRYLLENGASPNEQTATGQ 789
Cdd:PHA02946   164 FEARIVDKFGKNHIHRHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCSKTVKNVdIINLLLPSTDVNKQNKFGD 243

                   ....*
gi 1831513053  790 TPLSI 794
Cdd:PHA02946   244 SPLTL 248
Ank_4 pfam13637
Ankyrin repeats (many copies);
262-313 1.42e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.88  E-value: 1.42e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1831513053  262 SPLHVATKWGRTNMANLLLSRGAIIDSRTKDLLTPLHCAARSGHDQVVDLLV 313
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
52-127 1.45e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 52.75  E-value: 1.45e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1831513053   52 LLRAGTDINTSNANGLNSLHLASKEGHSEVVRELIKRQAQVDAATRKGNTALHIASLAGQSLIVTILVENGANVNV 127
Cdd:PHA03100   178 LLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
Ank_5 pfam13857
Ankyrin repeats (many copies);
576-630 1.68e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.57  E-value: 1.68e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1831513053  576 LLERGTP-VDIEGKNQVTPLHVAAHYNNDKVAMLLLENGASAKAAAKNGYTPLHIA 630
Cdd:pfam13857    1 LLEHGPIdLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
543-597 1.88e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.57  E-value: 1.88e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1831513053  543 LLDH-NADKTLLTKKGFTPLHLASKYGNLEVVRLLLERGTPVDIEGKNQVTPLHVA 597
Cdd:pfam13857    1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
98-249 1.97e-06

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 52.88  E-value: 1.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053   98 KGNTALHIASLAGQSLIVTILVENGANVNVQSVNGF--------------TPLYMAAQENHEEVVKYLLkhganqalstE 163
Cdd:cd22193     75 EGQTALHIAIERRQGDIVALLVENGADVHAHAKGRFfqpkyqgegfyfgeLPLSLAACTNQPDIVQYLL----------E 144
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  164 DGFTPLAVALQqghdrvvavllenDSKGKVRLPALHIAAkkDDTTAATLLLQNEHN----------PDV-----TSKSGF 228
Cdd:cd22193    145 NEHQPADIEAQ-------------DSRGNTVLHALVTVA--DNTKENTKFVTRMYDmilirgaklcPTVeleeiRNNDGL 209
                          170       180
                   ....*....|....*....|.
gi 1831513053  229 TPLHIAAHYGHENVGQLLLEK 249
Cdd:cd22193    210 TPLQLAAKMGKIEILKYILQR 230
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
562-672 2.33e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.59  E-value: 2.33e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  562 HLASKyGNLEVVRLLLERGTPVDIEGKNQVTPLHVAAHYNNDKVAMLLLENGASAKAAAKNGYTPLHIAAKKNQMEIAST 641
Cdd:PTZ00322    88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1831513053  642 LL-----QFKADPNAKsragftPLHLSAQEGHKEIS 672
Cdd:PTZ00322   167 LSrhsqcHFELGANAK------PDSFTGKPPSLEDS 196
Ank_4 pfam13637
Ankyrin repeats (many copies);
66-119 2.33e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.11  E-value: 2.33e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1831513053   66 GLNSLHLASKEGHSEVVRELIKRQAQVDAATRKGNTALHIASLAGQSLIVTILV 119
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
559-610 2.48e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.11  E-value: 2.48e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1831513053  559 TPLHLASKYGNLEVVRLLLERGTPVDIEGKNQVTPLHVAAHYNNDKVAMLLL 610
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
410-465 2.58e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.19  E-value: 2.58e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1831513053  410 LLLKYRAAIEATTESGLTPLHVAAFMGAINIVIYLLQQGANPDVETVRGETPLHLA 465
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
199-281 2.72e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.21  E-value: 2.72e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  199 HIAAKkDDTTAATLLLQNEHNPDVTSKSGFTPLHIAAHYGHENVGQLLLEKGANVNYQARHNISPLHVATKWGRTNMANL 278
Cdd:PTZ00322    88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166

                   ...
gi 1831513053  279 LLS 281
Cdd:PTZ00322   167 LSR 169
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
98-238 2.77e-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: 2.77e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053   98 KGNTALHIASLAGQSLIVTILVENGANVN----------VQSVNGF----TPLYMAAQENHEEVVKYLLkhganqalstE 163
Cdd:cd22196     93 KGQTALHIAIERRNMHLVELLVQNGADVHarasgeffkkKKGGPGFyfgeLPLSLAACTNQLDIVKFLL----------E 162
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  164 DGFTPLAVALQqghdrvvavllenDSKGKVRLPALHIAA--KKDDTTAAT------LLLQNEHNP-----DVTSKSGFTP 230
Cdd:cd22196    163 NPHSPADISAR-------------DSMGNTVLHALVEVAdnTPENTKFVTkmyneiLILGAKIRPllkleEITNKKGLTP 229

                   ....*...
gi 1831513053  231 LHIAAHYG 238
Cdd:cd22196    230 LKLAAKTG 237
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
528-671 2.83e-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: 52.19  E-value: 2.83e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  528 LHIAA---KEGQEEVAGILLDHNADKTLLTK-----------KGFTPLHLASKYGNLEVVRLLLERGTPVDIEG------ 587
Cdd:cd21882     30 LHKAAlnlNDGVNEAIMLLLEAAPDSGNPKElvnapctdefyQGQTALHIAIENRNLNLVRLLVENGADVSARAtgrffr 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  588 KNQVT-------PLHVAAHYNNDKVAMLLLENGASAKAAAKN---GYTPLHI---AAKKNQMEIA------STLLQF--K 646
Cdd:cd21882    110 KSPGNlfyfgelPLSLAACTNQEEIVRLLLENGAQPAALEAQdslGNTVLHAlvlQADNTPENSAfvcqmyNLLLSYgaH 189
                          170       180       190
                   ....*....|....*....|....*....|
gi 1831513053  647 ADPNAK-----SRAGFTPLHLSAQEGHKEI 671
Cdd:cd21882    190 LDPTQQleeipNHQGLTPLKLAAVEGKIVM 219
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
392-579 3.13e-06

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


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 52.16  E-value: 3.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  392 GFTPLHIACKKNRIKVVELLLKYRAAIEATTESGLtplhvaaFMGAINIVIYLlqqganpdvetvrGETPLHLAARANQT 471
Cdd:cd22197     94 GHSALHIAIEKRSLQCVKLLVENGADVHARACGRF-------FQKKQGTCFYF-------------GELPLSLAACTKQW 153
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  472 DVVRVLIRNG---AKVDAQARELQTPLH----IASRLG-NTDIVIL----LLQAGANSNATTRdnysplhiaakegQEEV 539
Cdd:cd22197    154 DVVNYLLENPhqpASLQAQDSLGNTVLHalvmIADNSPeNSALVIKmydgLLQAGARLCPTVQ-------------LEEI 220
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1831513053  540 AgilldhnadktllTKKGFTPLHLASKYGNLEVVRLLLER 579
Cdd:cd22197    221 S-------------NHEGLTPLKLAAKEGKIEIFRHILQR 247
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
71-169 3.45e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.82  E-value: 3.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053   71 HLASkEGHSEVVRELIKRQAQVDAATRKGNTALHIASLAGQSLIVTILVENGANVNVQSVNGFTPLYMAAQENHEEVVKY 150
Cdd:PTZ00322    88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166
                           90       100
                   ....*....|....*....|....*.
gi 1831513053  151 LLKH-------GANQALSTEDGFTPL 169
Cdd:PTZ00322   167 LSRHsqchfelGANAKPDSFTGKPPS 192
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
646-795 3.45e-06

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 52.01  E-value: 3.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  646 KADPNAKSRAGFTPLHLSAQEG-HKEISGLLIENGSDVGAkannGLTAMHLCAQEDHVPVAQIL----------YNNGAE 714
Cdd:TIGR00870   42 KLNINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAV----GDTLLHAISLEYVDAVEAILlhllaafrksGPLELA 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  715 INSKTN---AGYTPLHVACHFGQLNMVKFLVENGADV------GEKTRASYT--------PLHQAAQQGHNNCVRYLLEN 777
Cdd:TIGR00870  118 NDQYTSeftPGITALHLAAHRQNYEIVKLLLERGASVparacgDFFVKSQGVdsfyhgesPLNAAACLGSPSIVALLSED 197
                          170
                   ....*....|....*...
gi 1831513053  778 GASPNEQTATGQTPLSIA 795
Cdd:TIGR00870  198 PADILTADSLGNTLLHLL 215
PHA02989 PHA02989
ankyrin repeat protein; Provisional
670-797 4.70e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 51.28  E-value: 4.70e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  670 EISGLLIENGSDVGAKannGLTAMHLCA--------QEDHVPVAQILYNNGAEINSKTNAGYTPlhVAC-----HFGQLN 736
Cdd:PHA02989    51 KIVKLLIDNGADVNYK---GYIETPLCAvlrnreitSNKIKKIVKLLLKFGADINLKTFNGVSP--IVCfiynsNINNCD 125
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1831513053  737 MVKFLVENGADVGE-KTRASYTPLHQAAQQGHNN--CVRYLLENGASPNEQTAT-GQTPLSIAQR 797
Cdd:PHA02989   126 MLRFLLSKGINVNDvKNSRGYNLLHMYLESFSVKkdVIKILLSFGVNLFEKTSLyGLTPMNIYLR 190
Death_PIDD cd08779
Death Domain of p53-induced protein with a death domain; Death domain (DD) found in PIDD ...
1508-1581 5.01e-06

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


Pssm-ID: 260049  Cd Length: 86  Bit Score: 46.15  E-value: 5.01e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1831513053 1508 QNVLKGIGADWPRLGRALEVPHRDIQHIRQNYPG--QECK-NTLKIWIHLKKEDAN-QDNLDQALRQIGRDDIVRSIA 1581
Cdd:cd08779      6 LSLAKELGEDWQKLALHLGVSYSRIQRIKRKNRDdlDEQIlDMLFSWAKTLPTSPDkVGLLVTALSKSGRSDLAEELR 83
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
425-579 5.12e-06

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


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 51.35  E-value: 5.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  425 GLTPLHVAAFMGAINIVIYLLQQGAnpDVETVR----------------GETPLHLAARANQTDVVRVLIRN---GAKVD 485
Cdd:cd22196     94 GQTALHIAIERRNMHLVELLVQNGA--DVHARAsgeffkkkkggpgfyfGELPLSLAACTNQLDIVKFLLENphsPADIS 171
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  486 AQARELQTPLH----IA-SRLGNTDIV------ILLLQAgansnattrdnysplHIAAKEGQEEVAgilldhnadktllT 554
Cdd:cd22196    172 ARDSMGNTVLHalveVAdNTPENTKFVtkmyneILILGA---------------KIRPLLKLEEIT-------------N 223
                          170       180
                   ....*....|....*....|....*
gi 1831513053  555 KKGFTPLHLASKYGNLEVVRLLLER 579
Cdd:cd22196    224 KKGLTPLKLAAKTGKIGIFAYILGR 248
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
271-348 5.95e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.05  E-value: 5.95e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1831513053  271 GRTNMANLLLSRGAIIDSRTKDLLTPLHCAARSGHDQVVDLLVVQGAPISAKTKNGLAPLHMAAQGDHVDAARTLLYH 348
Cdd:PTZ00322    93 GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
722-748 6.62e-06

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 44.17  E-value: 6.62e-06
                           10        20
                   ....*....|....*....|....*..
gi 1831513053  722 GYTPLHVACHFGQLNMVKFLVENGADV 748
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADI 28
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
738-807 6.99e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.05  E-value: 6.99e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  738 VKFLVENGADVGEKTRASYTPLHQAAQQGHNNCVRYLLENGASPNEQTATGQTPLSIAQRLGYVSVVETL 807
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
602-760 8.17e-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: 50.96  E-value: 8.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  602 NDKVAMLL--LENGASAK----AAAKNGY----TPLHIAAKKNQMEIASTLLQFKADPNA----------KSRAGF---- 657
Cdd:cd22196     63 NDTISLLLdiAEKTGNLKefvnAAYTDSYykgqTALHIAIERRNMHLVELLVQNGADVHArasgeffkkkKGGPGFyfge 142
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  658 TPLHLSAQEGHKEISGLLIEN---GSDVGAKANNGLTAMH-LCAQEDHVPV----AQILYNN----GAEINSK------- 718
Cdd:cd22196    143 LPLSLAACTNQLDIVKFLLENphsPADISARDSMGNTVLHaLVEVADNTPEntkfVTKMYNEililGAKIRPLlkleeit 222
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1831513053  719 TNAGYTPLHVACHFGQLNMVKFLVenGADVGEK---------TRASYTPLH 760
Cdd:cd22196    223 NKKGLTPLKLAAKTGKIGIFAYIL--GREIKEPecrhlsrkfTEWAYGPVH 271
PHA02884 PHA02884
ankyrin repeat protein; Provisional
438-533 1.01e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 49.60  E-value: 1.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  438 INIVIYLlqqGANPDVETVRGE----TPLHLAARANQTDVVRVLIRNGAKVDAQARELQ-TPLHIASRLGNTDIVILLLQ 512
Cdd:PHA02884    49 IDAILKL---GADPEAPFPLSEnsktNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLHGCLKCLEILLS 125
                           90       100
                   ....*....|....*....|.
gi 1831513053  513 AGANSNATTRDNYSPLHIAAK 533
Cdd:PHA02884   126 YGADINIQTNDMVTPIELALM 146
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
722-748 1.02e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 43.73  E-value: 1.02e-05
                            10        20
                    ....*....|....*....|....*..
gi 1831513053   722 GYTPLHVACHFGQLNMVKFLVENGADV 748
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADI 28
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
464-658 1.14e-05

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 50.14  E-value: 1.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  464 LAARANQTDVVRVLIrnGAKVDAQARELQTPLHIASRLGNTDIVILLLQAGANSNATTR-DNYSPLHiaakegqeevagi 542
Cdd:cd22194    116 LLAFAEENGILDRFI--NAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKgVFFNPKY------------- 180
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  543 lldhnadktllTKKGF----TPLHLASKYGNLEVVRLLLERG-TPVDIEGKNQVTPLH----VA--AHYNNDKVA----M 607
Cdd:cd22194    181 -----------KHEGFyfgeTPLALAACTNQPEIVQLLMEKEsTDITSQDSRGNTVLHalvtVAedSKTQNDFVKrmydM 249
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1831513053  608 LLL--ENGASAKAAAKNGYTPLHIAAKKNQMEIASTLL--QFKADPNAKSRAGFT 658
Cdd:cd22194    250 ILLksENKNLETIRNNEGLTPLQLAAKMGKAEILKYILsrEIKEKPNRSLSRKFT 304
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
227-256 1.19e-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: 43.82  E-value: 1.19e-05
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1831513053  227 GFTPLHIAA-HYGHENVGQLLLEKGANVNYQ 256
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNAR 32
Ank_5 pfam13857
Ankyrin repeats (many copies);
345-399 1.25e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.26  E-value: 1.25e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1831513053  345 LLYHR-APVDDVTVDYLTPLHVAAHCGHVRVAKLLLDRSADPNSRALNGFTPLHIA 399
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
722-753 1.36e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 43.43  E-value: 1.36e-05
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1831513053  722 GYTPLHVAC-HFGQLNMVKFLVENGADVGEKTR 753
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
118-172 1.70e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.87  E-value: 1.70e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1831513053  118 LVENG-ANVNVQSVNGFTPLYMAAQENHEEVVKYLLKHGANQALSTEDGFTPLAVA 172
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
391-420 1.81e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.96  E-value: 1.81e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 1831513053   391 NGFTPLHIACKKNRIKVVELLLKYRAAIEA 420
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
556-585 1.83e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.96  E-value: 1.83e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 1831513053   556 KGFTPLHLASKYGNLEVVRLLLERGTPVDI 585
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
622-651 1.94e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.96  E-value: 1.94e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 1831513053   622 NGYTPLHIAAKKNQMEIASTLLQFKADPNA 651
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
556-588 2.03e-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: 2.03e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1831513053  556 KGFTPLHLAS-KYGNLEVVRLLLERGTPVDIEGK 588
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
425-539 2.63e-05

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 49.02  E-value: 2.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  425 GLTPLHVAAFMGAINIVIYLLQQGAnpDVETVR----------------GETPLHLAARANQTDVVRVLIRNG---AKVD 485
Cdd:cd22193     76 GQTALHIAIERRQGDIVALLVENGA--DVHAHAkgrffqpkyqgegfyfGELPLSLAACTNQPDIVQYLLENEhqpADIE 153
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  486 AQARELQTPLH----IASRL-GNTDIVI----LLLQAGANSNATT-------RDNYSPLHIAAKEGQEEV 539
Cdd:cd22193    154 AQDSRGNTVLHalvtVADNTkENTKFVTrmydMILIRGAKLCPTVeleeirnNDGLTPLQLAAKMGKIEI 223
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
457-487 2.94e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 42.66  E-value: 2.94e-05
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1831513053  457 RGETPLHLAA-RANQTDVVRVLIRNGAKVDAQ 487
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNAR 32
Ank_4 pfam13637
Ankyrin repeats (many copies);
39-86 3.03e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.03  E-value: 3.03e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1831513053   39 RAARAGDLEKVLELLRAGTDINTSNANGLNSLHLASKEGHSEVVRELI 86
Cdd:pfam13637    7 AAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
361-388 3.03e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 42.66  E-value: 3.03e-05
                           10        20
                   ....*....|....*....|....*....
gi 1831513053  361 TPLHVAA-HCGHVRVAKLLLDRSADPNSR 388
Cdd:pfam00023    4 TPLHLAAgRRGNLEIVKLLLSKGADVNAR 32
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
457-486 3.24e-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: 42.24  E-value: 3.24e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 1831513053  457 RGETPLHLAARANQTDVVRVLIRNGAKVDA 486
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
622-654 3.48e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 42.28  E-value: 3.48e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1831513053  622 NGYTPLHIAAKK-NQMEIASTLLQFKADPNAKSR 654
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
471-777 4.20e-05

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 48.37  E-value: 4.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  471 TDVVRVLIRNGAKVDAQARELQTPLHIASRLGN--TDIVILLLQAGANSNATTRDNYSPLH---IAAKEGQEEVAGI--- 542
Cdd:PHA02716   192 IDILEWLCNNGVNVNLQNNHLITPLHTYLITGNvcASVIKKIIELGGDMDMKCVNGMSPIMtyiINIDNINPEITNIyie 271
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  543 LLDHNADKTLltkkgftPLHLAS-----KYGNLEVVRLLLERGTPVDIEGKNQVTPLH--VAAHYNNDKVAMLLLENGAS 615
Cdd:PHA02716   272 SLDGNKVKNI-------PMILHSyitlaRNIDISVVYSFLQPGVKLHYKDSAGRTCLHqyILRHNISTDIIKLLHEYGND 344
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  616 AKAAAKNGYTPLHI------------AAKKN--QMEIASTLLQFKADPNAKSRAGFTPLH---LSAQE-GHKEISGLLIE 677
Cdd:PHA02716   345 LNEPDNIGNTVLHTylsmlsvvnildPETDNdiRLDVIQCLISLGADITAVNCLGYTPLTsyiCTAQNyMYYDIIDCLIS 424
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  678 NG----------SDVGAKANNGLTAMHLCAQEDHVPVAqiLYNNGAEINSKTN--------------------AGYTPLH 727
Cdd:PHA02716   425 DKvlnmvkhrilQDLLIRVDDTPCIIHHIIAKYNIPTD--LYTDEYEPYDSTKihdvyhcaiierynnavcetSGMTPLH 502
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1831513053  728 VA-CHFGQLNMV----KFLVENGADVGEKTRASYTPLHQAAQQG-HNNCVRYLLEN 777
Cdd:PHA02716   503 VSiISHTNANIVmdsfVYLLSIQYNINIPTKNGVTPLMLTMRNNrLSGHQWYIVKN 558
PHA02798 PHA02798
ankyrin-like protein; Provisional
219-465 4.32e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 48.29  E-value: 4.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  219 NPDVTSKSgftpLHIAAHYGHEN-----VGQLLLEKGANVNYQARHNISPL-----HVATKWGRTNMANLLLSRGAIIDS 288
Cdd:PHA02798    29 NPNEIVNE----YSIFQKYLQRDspstdIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINK 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  289 RTKDLLTPLHCAARSGH---DQVVDLLVVQGAPISAKTKNGLAPLHMAAQ-GDHVDAARTLLYHRAPVDDVTVD---YLT 361
Cdd:PHA02798   105 KNSDGETPLYCLLSNGYinnLEILLFMIENGADTTLLDKDGFTMLQVYLQsNHHIDIEIIKLLLEKGVDINTHNnkeKYD 184
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  362 PLHV----AAHCGHVRVAKLLLDRSADPN-------SRALNGFTPLHIACKKNRIKVVELLLKYrAAIEATTESGLTPLH 430
Cdd:PHA02798   185 TLHCyfkyNIDRIDADILKLFVDNGFIINkenkshkKKFMEYLNSLLYDNKRFKKNILDFIFSY-IDINQVDELGFNPLY 263
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1831513053  431 VAAFMGAINIVIYLLQQGANPDVETVRGETPLHLA 465
Cdd:PHA02798   264 YSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTA 298
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
131-157 4.76e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 41.89  E-value: 4.76e-05
                           10        20
                   ....*....|....*....|....*...
gi 1831513053  131 NGFTPLYMAA-QENHEEVVKYLLKHGAN 157
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGAD 28
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
756-783 5.08e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.80  E-value: 5.08e-05
                            10        20
                    ....*....|....*....|....*...
gi 1831513053   756 YTPLHQAAQQGHNNCVRYLLENGASPNE 783
Cdd:smart00248    3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
358-386 5.49e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.80  E-value: 5.49e-05
                            10        20
                    ....*....|....*....|....*....
gi 1831513053   358 DYLTPLHVAAHCGHVRVAKLLLDRSADPN 386
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank_5 pfam13857
Ankyrin repeats (many copies);
510-564 5.63e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 5.63e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1831513053  510 LLQAG-ANSNATTRDNYSPLHIAAKEGQEEVAGILLDHNADKTLLTKKGFTPLHLA 564
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
586-776 5.88e-05

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 47.95  E-value: 5.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  586 EGKNQVTPLHVAAHYNNDKV---AMLLLENG-----------ASAKAAAKNGYTPLHIAAKKNQMEIASTLLQFKADPNA 651
Cdd:cd21882     22 RGATGKTCLHKAALNLNDGVneaIMLLLEAApdsgnpkelvnAPCTDEFYQGQTALHIAIENRNLNLVRLLVENGADVSA 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  652 KSRAGF-------------TPLHLSAQEGHKEISGLLIENGSDVGAKANN---GLTAMH-LCAQEDHVPVAQIL----YN 710
Cdd:cd21882    102 RATGRFfrkspgnlfyfgeLPLSLAACTNQEEIVRLLLENGAQPAALEAQdslGNTVLHaLVLQADNTPENSAFvcqmYN 181
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1831513053  711 NGAEINSKtnagytplhvACHFGQLNMVkflvengadvgeKTRASYTPLHQAAQQGHNNCVRYLLE 776
Cdd:cd21882    182 LLLSYGAH----------LDPTQQLEEI------------PNHQGLTPLKLAAVEGKIVMFQHILQ 225
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
556-585 6.13e-05

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 41.47  E-value: 6.13e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 1831513053  556 KGFTPLHLASKYGNLEVVRLLLERGTPVDI 585
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
756-785 6.27e-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. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 41.51  E-value: 6.27e-05
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1831513053  756 YTPLHQAAQQ-GHNNCVRYLLENGASPNEQT 785
Cdd:pfam00023    3 NTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
391-420 6.63e-05

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 41.47  E-value: 6.63e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 1831513053  391 NGFTPLHIACKKNRIKVVELLLKYRAAIEA 420
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02741 PHA02741
hypothetical protein; Provisional
59-186 7.00e-05

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 45.42  E-value: 7.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053   59 INTSNANGLNSLHLASKEGHSEVVRELIK------RQAQVDAATRKGNTALHIASLAGQSL----IVTILVENGANVNVQ 128
Cdd:PHA02741    14 IAEKNSEGENFFHEAARCGCFDIIARFTPfirgdcHAAALNATDDAGQMCIHIAAEKHEAQlaaeIIDHLIELGADINAQ 93
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  129 -SVNGFTPLYMAAQENHEEVVKYLLKH-GANQALSTEDGFTPLAVALQQGHDRVVAVLLE 186
Cdd:PHA02741    94 eMLEGDTALHLAAHRRDHDLAEWLCCQpGIDLHFCNADNKSPFELAIDNEDVAMMQILRE 153
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
454-579 7.89e-05

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 47.48  E-value: 7.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  454 ETVRGETPLHLAARANQTDVVRVLIRNGAKVDAQAREL--------------QTPLHIASRLGNTDIVILLLQ---AGAN 516
Cdd:cd22193     72 EYYEGQTALHIAIERRQGDIVALLVENGADVHAHAKGRffqpkyqgegfyfgELPLSLAACTNQPDIVQYLLEnehQPAD 151
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1831513053  517 SNATTRDNYSPLH----IA--AKEGQEEV----------AGILLDHNADKTLLTKKGFTPLHLASKYGNLEVVRLLLER 579
Cdd:cd22193    152 IEAQDSRGNTVLHalvtVAdnTKENTKFVtrmydmilirGAKLCPTVELEEIRNNDGLTPLQLAAKMGKIEILKYILQR 230
PHA02917 PHA02917
ankyrin-like protein; Provisional
339-795 8.35e-05

ankyrin-like protein; Provisional


Pssm-ID: 165231 [Multi-domain]  Cd Length: 661  Bit Score: 47.69  E-value: 8.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  339 VDAARTLLYHRAPVDDVTVDYLTPLHV---AAHCGHVRVAKLLLDRSADPNSRALNGFTPLHIACKKNRIKVVELLLKyr 415
Cdd:PHA02917    12 LDELKQMLRDRDPNDTRNQFKNNALHAylfNEHCNNVEVVKLLLDSGTNPLHKNWRQLTPLEEYTNSRHVKVNKDIAM-- 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  416 AAIEATTESGLTPLHVAAFMGA----INIVIYLLQQGANPDV--ETVRGETPLHLAARANQTDVVRVLIRNGAKV----- 484
Cdd:PHA02917    90 ALLEATGYSNINDFNIFSYMKSknvdVDLIKVLVEHGFDLSVkcENHRSVIENYVMTDDPVPEIIDLFIENGCSVlyede 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  485 ---------DAQARELQTPLH--IASRLG---------NTDIVILLLQAGANSNATTRDNYSPLHIAAKEGQEEVAGILL 544
Cdd:PHA02917   170 ddeygyaydDYQPRNCGTVLHlyIISHLYsesdtrayvRPEVVKCLINHGIKPSSIDKNYCTALQYYIKSSHIDIDIVKL 249
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  545 -----DHNA----DKTLLTKKGFTPLHLASKYG-----NLEVVRLLLERGTPVDIegKNQVTPLhvaahYNNDKVAMLLL 610
Cdd:PHA02917   250 lmkgiDNTAysyiDDLTCCTRGIMADYLNSDYRynkdvDLDLVKLFLENGKPHGI--MCSIVPL-----WRNDKETISLI 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  611 ENGASAKAAAKngYTPLHIAAKKNQMEIASTLLQFKADPNAKSRAG-FTPLHLSAQeghkEISGLLIENGSDVGAKANNG 689
Cdd:PHA02917   323 LKTMNSDVLQH--ILIEYMTFGDIDIPLVECMLEYGAVVNKEAIHGyFRNINIDSY----TMKYLLKKEGGDAVNHLDDG 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  690 ltamhlcaqedHVPVAQILYNNGAEINSKTNA---GYTPLHVACHFgqLNMVKFLVENGADVGEKTRASYTPLHQAAQQG 766
Cdd:PHA02917   397 -----------EIPIGHLCKSNYGCYNFYTYTykkGLCDMSYACPI--LSTINICLPYLKDINMIDKRGETLLHKAVRYN 463
                          490       500
                   ....*....|....*....|....*....
gi 1831513053  767 HNNCVRYLLENGASPNEQTATGQTPLSIA 795
Cdd:PHA02917   464 KQSLVSLLLESGSDVNIRSNNGYTCIAIA 492
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
41-136 8.38e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.59  E-value: 8.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053   41 ARAGDLEKVLELLRAGTDINTSNANGLNSLHLASKEGHSEVVRELIKRQAQVDAATRKGNTALHIASLAGQSLIVTILV- 119
Cdd:PTZ00322    90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSr 169
                           90       100
                   ....*....|....*....|...
gi 1831513053  120 ------ENGANVNVQSVNGFTPL 136
Cdd:PTZ00322   170 hsqchfELGANAKPDSFTGKPPS 192
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
457-486 8.54e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.03  E-value: 8.54e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 1831513053   457 RGETPLHLAARANQTDVVRVLIRNGAKVDA 486
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
722-794 8.93e-05

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 47.18  E-value: 8.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  722 GYTPLHVACHFGQLNMVKFLVENGADVgeKTRASYT---------------PLHQAAQQGHNNCVRYLLENGASPNEQTA 786
Cdd:cd21882     73 GQTALHIAIENRNLNLVRLLVENGADV--SARATGRffrkspgnlfyfgelPLSLAACTNQEEIVRLLLENGAQPAALEA 150
                           90
                   ....*....|.
gi 1831513053  787 T---GQTPLSI 794
Cdd:cd21882    151 QdslGNTVLHA 161
Ank_4 pfam13637
Ankyrin repeats (many copies);
658-708 9.46e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.88  E-value: 9.46e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1831513053  658 TPLHLSAQEGHKEISGLLIENGSDVGAKANNGLTAMHLCAQEDHVPVAQIL 708
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
492-522 1.33e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 40.74  E-value: 1.33e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1831513053  492 QTPLHIAS-RLGNTDIVILLLQAGANSNATTR 522
Cdd:pfam00023    3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
227-255 1.38e-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: 1.38e-04
                            10        20
                    ....*....|....*....|....*....
gi 1831513053   227 GFTPLHIAAHYGHENVGQLLLEKGANVNY 255
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02884 PHA02884
ankyrin repeat protein; Provisional
229-302 1.38e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 46.13  E-value: 1.38e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1831513053  229 TPLHIAAHYGHENVGQLLLEKGANVN-YQARHNISPLHVATKWGRTNMANLLLSRGAIIDSRTKDLLTPLHCAAR 302
Cdd:PHA02884    72 NPLIYAIDCDNDDAAKLLIRYGADVNrYAEEAKITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELALM 146
PHA02736 PHA02736
Viral ankyrin protein; Provisional
450-585 1.44e-04

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 44.10  E-value: 1.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  450 NPDVEtvrGETPLHLAARanQTDVVRVLIRNGAKVDAQA-------RELQTPLHIASRLGNTD---IVILLLQAGANSNA 519
Cdd:PHA02736    12 EPDIE---GENILHYLCR--NGGVTDLLAFKNAISDENRylvleynRHGKQCVHIVSNPDKADpqeKLKLLMEWGADING 86
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1831513053  520 TTR-DNYSPLHIAAKEGQEEVAGILLDH-NADKTLLTKKGFTPLHLASKYGNLEVVRLLLERGTPVDI 585
Cdd:PHA02736    87 KERvFGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGAQCKV 154
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
227-254 1.51e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 40.32  E-value: 1.51e-04
                           10        20
                   ....*....|....*....|....*...
gi 1831513053  227 GFTPLHIAAHYGHENVGQLLLEKGANVN 254
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADIN 29
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
622-651 1.75e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 40.32  E-value: 1.75e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1831513053  622 NGYTPLHIAAKKNQMEIASTLLQFKADPNA 651
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
98-256 1.85e-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: 46.39  E-value: 1.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053   98 KGNTALHIASLAGQSLIVTILVENGANVNVQSVNGF-------------TPLYMAAQENHEEVVKYLLKHGANQAlsted 164
Cdd:cd22197     93 RGHSALHIAIEKRSLQCVKLLVENGADVHARACGRFfqkkqgtcfyfgeLPLSLAACTKQWDVVNYLLENPHQPA----- 167
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  165 gftplavALQqghdrvvavllENDSKGKVRLPALHIAAkkDDTT---------------AATLLLQNEHNPDVTSKSGFT 229
Cdd:cd22197    168 -------SLQ-----------AQDSLGNTVLHALVMIA--DNSPensalvikmydgllqAGARLCPTVQLEEISNHEGLT 227
                          170       180
                   ....*....|....*....|....*..
gi 1831513053  230 PLHIAAHYGHENVGQLLLEKGANVNYQ 256
Cdd:cd22197    228 PLKLAAKEGKIEIFRHILQREFSGPYQ 254
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
639-708 2.03e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.43  E-value: 2.03e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  639 ASTLLQFKADPNAKSRAGFTPLHLSAQEGHKEISGLLIENGSDVGAKANNGLTAMHLCAQEDHVPVAQIL 708
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
PHA02989 PHA02989
ankyrin repeat protein; Provisional
561-804 2.10e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 45.89  E-value: 2.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  561 LHLASKYGNLEVVRLLLERGTPVDIEGKNQvTPLhvAAHYNN--------DKVAMLLLENGASAKAAAKNGYTPL----- 627
Cdd:PHA02989    41 LYLKRKDVKIKIVKLLIDNGADVNYKGYIE-TPL--CAVLRNreitsnkiKKIVKLLLKFGADINLKTFNGVSPIvcfiy 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  628 --HIaakkNQMEIASTLLQFKADPNA-KSRAGFTPLHLSAQEG--HKEISGLLIENGSDVGAKAN-NGLTAMHLCAQED- 700
Cdd:PHA02989   118 nsNI----NNCDMLRFLLSKGINVNDvKNSRGYNLLHMYLESFsvKKDVIKILLSFGVNLFEKTSlYGLTPMNIYLRNDi 193
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  701 ---HVPVAQILYNNGAEINSKTNAGYTPL------HVACHFGQLNMVKFLVENgADVGEKTRASYTPLHQAAQQGHNNCV 771
Cdd:PHA02989   194 dviSIKVIKYLIKKGVNIETNNNGSESVLesfldnNKILSKKEFKVLNFILKY-IKINKKDKKGFNPLLISAKVDNYEAF 272
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1831513053  772 RYLLENGASPNEQTATGQTPLSIAQRLGYVSVV 804
Cdd:PHA02989   273 NYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDML 305
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
425-453 2.17e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.88  E-value: 2.17e-04
                            10        20
                    ....*....|....*....|....*....
gi 1831513053   425 GLTPLHVAAFMGAINIVIYLLQQGANPDV 453
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
609-662 2.21e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.79  E-value: 2.21e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1831513053  609 LLENG-ASAKAAAKNGYTPLHIAAKKNQMEIASTLLQFKADPNAKSRAGFTPLHL 662
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
391-423 2.27e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.97  E-value: 2.27e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1831513053  391 NGFTPLHIACKK-NRIKVVELLLKYRAAIEATTE 423
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
556-671 2.42e-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: 46.00  E-value: 2.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  556 KGFTPLHLASKYGNLEVVRLLLERGTPV------DIEGKNQVT-------PLHVAAHYNNDKVAMLLLENG---ASAKAA 619
Cdd:cd22197     93 RGHSALHIAIEKRSLQCVKLLVENGADVharacgRFFQKKQGTcfyfgelPLSLAACTKQWDVVNYLLENPhqpASLQAQ 172
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1831513053  620 AKNGYTPLH----IAAKKNQ-----MEIASTLLQF--KADPNAK-----SRAGFTPLHLSAQEGHKEI 671
Cdd:cd22197    173 DSLGNTVLHalvmIADNSPEnsalvIKMYDGLLQAgaRLCPTVQleeisNHEGLTPLKLAAKEGKIEI 240
PHA02791 PHA02791
ankyrin-like protein; Provisional
492-659 2.47e-04

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 45.03  E-value: 2.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  492 QTPLHIASRLGNTDIVILLLQAGANSNATtrDNYSPLHIAAKEGQEEVAGILLDHNADKTLLTKKGFTPLHLASKYGNLE 571
Cdd:PHA02791    31 HSALYYAIADNNVRLVCTLLNAGALKNLL--ENEFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGNMQ 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  572 VVRLLLERGTPVDIEGKNQ-VTPLHVAAHYNNDKVAMLLLENGASAKAAAKNgYTPLHIAAKKNQMEIASTLLQFKADPN 650
Cdd:PHA02791   109 TVKLFVKKNWRLMFYGKTGwKTSFYHAVMLNDVSIVSYFLSEIPSTFDLAIL-LSCIHITIKNGHVDMMILLLDYMTSTN 187

                   ....*....
gi 1831513053  651 AKSRAGFTP 659
Cdd:PHA02791   188 TNNSLLFIP 196
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
358-386 2.62e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.93  E-value: 2.62e-04
                           10        20
                   ....*....|....*....|....*....
gi 1831513053  358 DYLTPLHVAAHCGHVRVAKLLLDRSADPN 386
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
Ank_5 pfam13857
Ankyrin repeats (many copies);
675-729 2.85e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.41  E-value: 2.85e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1831513053  675 LIENGS-DVGAKANNGLTAMHLCAQEDHVPVAQILYNNGAEINSKTNAGYTPLHVA 729
Cdd:pfam13857    1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
469-644 3.01e-04

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 45.56  E-value: 3.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  469 NQTDVVRVLIRNGAK-------VDAQAREL----QTPLHIASRLGNTDIVILLLQAGANSNATTRDNYSPLHiaaKEGQe 537
Cdd:cd22193     43 GTNDTIRILLDIAEKtdnlkrfINAEYTDEyyegQTALHIAIERRQGDIVALLVENGADVHAHAKGRFFQPK---YQGE- 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  538 evaGILLdhnadktlltkkGFTPLHLASKYGNLEVVRLLLERG-TPVDIEGKNQV--TPLH----VAAHY--NND---KV 605
Cdd:cd22193    119 ---GFYF------------GELPLSLAACTNQPDIVQYLLENEhQPADIEAQDSRgnTVLHalvtVADNTkeNTKfvtRM 183
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1831513053  606 AMLLLENGASAKAAAK-------NGYTPLHIAAKKNQMEIASTLLQ 644
Cdd:cd22193    184 YDMILIRGAKLCPTVEleeirnnDGLTPLQLAAKMGKIEILKYILQ 229
PHA02946 PHA02946
ankyin-like protein; Provisional
330-566 3.41e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 45.43  E-value: 3.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  330 LHMAAQGDHVDAARTLLYHRAPVDDVTVdyltpLHvaAHCG----HVRVAKLLLDRSADPNSRALNGFTPLHIACKKNRI 405
Cdd:PHA02946    13 LYAKYNSKNLDVFRNMLQAIEPSGNYHI-----LH--AYCGikglDERFVEELLHRGYSPNETDDDGNYPLHIASKINNN 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  406 KVVELLLKYRAAIEATTESGLTPLHVAAFMG--AINIVIYLLQQGA--NPDVETvRGETPLhLAARANQTDVVRVLIRNG 481
Cdd:PHA02946    86 RIVAMLLTHGADPNACDKQHKTPLYYLSGTDdeVIERINLLVQYGAkiNNSVDE-EGCGPL-LACTDPSERVFKKIMSIG 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  482 --AKVDAQARELQTPLHIASRLGNTDIVILLLQAGANSNATTRDNYSPLHIAAKEGQEEVAGI-LLDHNADKTLLTKKGF 558
Cdd:PHA02946   164 feARIVDKFGKNHIHRHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCSKTVKNVDIInLLLPSTDVNKQNKFGD 243

                   ....*...
gi 1831513053  559 TPLHLASK 566
Cdd:PHA02946   244 SPLTLLIK 251
PHA02884 PHA02884
ankyrin repeat protein; Provisional
504-625 4.06e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 44.59  E-value: 4.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  504 TDIVILLLQAGANSNA----TTRDNYSPLHIAAKEGQEEVAGILLDHNAD-KTLLTKKGFTPLHLASKYGNLEVVRLLLE 578
Cdd:PHA02884    46 TDIIDAILKLGADPEApfplSENSKTNPLIYAIDCDNDDAAKLLIRYGADvNRYAEEAKITPLYISVLHGCLKCLEILLS 125
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1831513053  579 RGTPVDIEGKNQVTPLHVAAHYNNDKVAMLLLENGASAKAAAKNGYT 625
Cdd:PHA02884   126 YGADINIQTNDMVTPIELALMICNNFLAFMICDNEISNFYKHPKKIL 172
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
756-783 4.59e-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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.16  E-value: 4.59e-04
                           10        20
                   ....*....|....*....|....*...
gi 1831513053  756 YTPLHQAAQQGHNNCVRYLLENGASPNE 783
Cdd:pfam13606    3 NTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02946 PHA02946
ankyin-like protein; Provisional
213-412 4.72e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 44.66  E-value: 4.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  213 LLQNEHNPDVTSKSGFTPLHIAAHYGHENVGQLLLEKGANVNYQARHNISPLHV--ATKWGRTNMANLLLSRGAIIDSRT 290
Cdd:PHA02946    58 LLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYlsGTDDEVIERINLLVQYGAKINNSV 137
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  291 KDLLTPLHCAARSGHDQVVDLLVVQGAPISAKTKNGLAPLHMAAQGDHVDAArtllyhrapvddvTVDYLTPLHVAahcg 370
Cdd:PHA02946   138 DEEGCGPLLACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNPKAS-------------TISWMMKLGIS---- 200
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1831513053  371 hvrvakllldrsadPNSRALNGFTPLHIACKKN--RIKVVELLL 412
Cdd:PHA02946   201 --------------PSKPDHDGNTPLHIVCSKTvkNVDIINLLL 230
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
425-455 4.83e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.19  E-value: 4.83e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1831513053  425 GLTPLHVAAFM-GAINIVIYLLQQGANPDVET 455
Cdd:pfam00023    2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
131-157 5.92e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.78  E-value: 5.92e-04
                           10        20
                   ....*....|....*....|....*..
gi 1831513053  131 NGFTPLYMAAQENHEEVVKYLLKHGAN 157
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGAD 27
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
98-128 6.06e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.81  E-value: 6.06e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1831513053   98 KGNTALHIASL-AGQSLIVTILVENGANVNVQ 128
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNAR 32
Ank_5 pfam13857
Ankyrin repeats (many copies);
88-139 6.65e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 6.65e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1831513053   88 RQAQVDAATRKGNTALHIASLAGQSLIVTILVENGANVNVQSVNGFTPLYMA 139
Cdd:pfam13857    5 GPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02859 PHA02859
ankyrin repeat protein; Provisional
114-173 7.00e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 42.88  E-value: 7.00e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1831513053  114 IVTILVENGANVNVQSV-NGFTPL--YMAAQEN-HEEVVKYLLKHGANQALSTEDGFTPLAVAL 173
Cdd:PHA02859    68 ILKFLIENGADVNFKTRdNNLSALhhYLSFNKNvEPEILKILIDSGSSITEEDEDGKNLLHMYM 131
Ank_5 pfam13857
Ankyrin repeats (many copies);
647-696 7.05e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 7.05e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1831513053  647 ADPNAKSRAGFTPLHLSAQEGHKEISGLLIENGSDVGAKANNGLTAMHLC 696
Cdd:pfam13857    7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
721-792 7.70e-04

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


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 44.46  E-value: 7.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  721 AGYTPLHVACHFGQLNMVKFLVENGADVGEKTRASY-------------TPLHQAAQQGHNNCVRYLLENGASP---NEQ 784
Cdd:cd22197     93 RGHSALHIAIEKRSLQCVKLLVENGADVHARACGRFfqkkqgtcfyfgeLPLSLAACTKQWDVVNYLLENPHQPaslQAQ 172

                   ....*...
gi 1831513053  785 TATGQTPL 792
Cdd:cd22197    173 DSLGNTVL 180
Ank_5 pfam13857
Ankyrin repeats (many copies);
246-300 8.17e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 8.17e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1831513053  246 LLEKG-ANVNYQARHNISPLHVATKWGRTNMANLLLSRGAIIDSRTKDLLTPLHCA 300
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02989 PHA02989
ankyrin repeat protein; Provisional
52-282 8.83e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 43.96  E-value: 8.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053   52 LLRAGTDINTS-NANGLNSLHLASKEGHSEVVRELIKRQAQVDaatRKGNTALHIASLAGQSLI--------VTILVENG 122
Cdd:PHA02989    22 LLRTGFDVNEEyRGNSILLLYLKRKDVKIKIVKLLIDNGADVN---YKGYIETPLCAVLRNREItsnkikkiVKLLLKFG 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  123 ANVNVQSVNGFTP-----------------------LYMAAQENH----------------EEVVKYLLKHGANQALSTE 163
Cdd:PHA02989    99 ADINLKTFNGVSPivcfiynsninncdmlrfllskgINVNDVKNSrgynllhmylesfsvkKDVIKILLSFGVNLFEKTS 178
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  164 -DGFTPLAVALQQGHD----RVVAVLL-------ENDSKGKVRLPAL---HIAAKKDDTTAATLLLQ--NEHNPDvtsKS 226
Cdd:PHA02989   179 lYGLTPMNIYLRNDIDvisiKVIKYLIkkgvnieTNNNGSESVLESFldnNKILSKKEFKVLNFILKyiKINKKD---KK 255
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1831513053  227 GFTPLHIAAHYGHENVGQLLLEKGANVNYQARHNISPLHVATKWGRTNMANLLLSR 282
Cdd:PHA02989   256 GFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNRILQL 311
PHA02736 PHA02736
Viral ankyrin protein; Provisional
489-617 9.09e-04

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 41.79  E-value: 9.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  489 RELQTPLHIASRlgNTDIVILLLQAGANSNAT-------TRDNYSPLHIAAKEGQ---EEVAGILLDHNAD-KTLLTKKG 557
Cdd:PHA02736    15 IEGENILHYLCR--NGGVTDLLAFKNAISDENrylvleyNRHGKQCVHIVSNPDKadpQEKLKLLMEWGADiNGKERVFG 92
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1831513053  558 FTPLHLASKYGNLEVVRLLLeRGTPVDIEGKN--QVTPLHVAAHYNNDKVAMLLLENGASAK 617
Cdd:PHA02736    93 NTPLHIAVYTQNYELATWLC-NQPGVNMEILNyaFKTPYYVACERHDAKMMNILRAKGAQCK 153
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
555-807 1.07e-03

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 44.13  E-value: 1.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  555 KKGFTPLH--LASKYGNLEVVRLLLERGTPVDIEGKNQVTPLHVAAHYNNDKVAML--LLENGASAKAAAKNGYTPLhIA 630
Cdd:PHA02716   175 KTGYGILHayLGNMYVDIDILEWLCNNGVNVNLQNNHLITPLHTYLITGNVCASVIkkIIELGGDMDMKCVNGMSPI-MT 253
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  631 AKKNQMEIastllqfkaDPnaksragftplhlsaqeghkEISGLLIEngSDVGAKANNGLTAMHL---CAQEDHVPVAQI 707
Cdd:PHA02716   254 YIINIDNI---------NP--------------------EITNIYIE--SLDGNKVKNIPMILHSyitLARNIDISVVYS 302
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  708 LYNNGAEINSKTNAGYTPLH--VACHFGQLNMVKFLVENGADVGEKTRASYTPLHQAAQ----------QGHNN----CV 771
Cdd:PHA02716   303 FLQPGVKLHYKDSAGRTCLHqyILRHNISTDIIKLLHEYGNDLNEPDNIGNTVLHTYLSmlsvvnildpETDNDirldVI 382
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1831513053  772 RYLLENGASPNEQTATGQTPLS----IAQRLGYVSVVETL 807
Cdd:PHA02716   383 QCLISLGADITAVNCLGYTPLTsyicTAQNYMYYDIIDCL 422
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
292-324 1.21e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.04  E-value: 1.21e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1831513053  292 DLLTPLHCAA-RSGHDQVVDLLVVQGAPISAKTK 324
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
279-333 1.21e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.48  E-value: 1.21e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1831513053  279 LLSRGAI-IDSRTKDLLTPLHCAARSGHDQVVDLLVVQGAPISAKTKNGLAPLHMA 333
Cdd:pfam13857    1 LLEHGPIdLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
493-519 1.26e-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: 37.95  E-value: 1.26e-03
                            10        20
                    ....*....|....*....|....*..
gi 1831513053   493 TPLHIASRLGNTDIVILLLQAGANSNA 519
Cdd:smart00248    4 TPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
295-447 1.36e-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: 43.33  E-value: 1.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  295 TPLHCAARSGHDQVVDLLVVQGAPISAktknglaplhmAAQGDHVD-AARTLLYHRApvddvtvdylTPLHVAAHCGHVR 373
Cdd:cd21882     75 TALHIAIENRNLNLVRLLVENGADVSA-----------RATGRFFRkSPGNLFYFGE----------LPLSLAACTNQEE 133
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  374 VAKLLLDRSADPNSRALN---GFTPLHI---------ACKKNRIKVVELLLKYRAAI-------EATTESGLTPLHVAAF 434
Cdd:cd21882    134 IVRLLLENGAQPAALEAQdslGNTVLHAlvlqadntpENSAFVCQMYNLLLSYGAHLdptqqleEIPNHQGLTPLKLAAV 213
                          170
                   ....*....|...
gi 1831513053  435 MGAINIVIYLLQQ 447
Cdd:cd21882    214 EGKIVMFQHILQR 226
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
425-453 1.74e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.62  E-value: 1.74e-03
                           10        20
                   ....*....|....*....|....*....
gi 1831513053  425 GLTPLHVAAFMGAINIVIYLLQQGANPDV 453
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
713-792 1.79e-03

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: 43.21  E-value: 1.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  713 AEINSKTNAGYTPLHVACHFGQLNMVKFLVENGADVGEKTRASY--------------TPLHQAAQQGHNNCVRYLLENG 778
Cdd:cd22194    132 AEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVFfnpkykhegfyfgeTPLALAACTNQPEIVQLLMEKE 211
                           90
                   ....*....|....*
gi 1831513053  779 ASP-NEQTATGQTPL 792
Cdd:cd22194    212 STDiTSQDSRGNTVL 226
PHA02736 PHA02736
Viral ankyrin protein; Provisional
59-193 1.88e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 40.63  E-value: 1.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053   59 INTSNAN--GLNSLHLASKEGhsEVVRELIKRQAQVDAA-------TRKGNTALHIASLAGQS---LIVTILVENGANVN 126
Cdd:PHA02736     8 IFASEPDieGENILHYLCRNG--GVTDLLAFKNAISDENrylvleyNRHGKQCVHIVSNPDKAdpqEKLKLLMEWGADIN 85
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1831513053  127 VQ-SVNGFTPLYMAAQENHEEVVKYLLKH-GANQALSTEDGFTPLAVALQQGHDRVVAVLLENDSKGKV 193
Cdd:PHA02736    86 GKeRVFGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGAQCKV 154
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
492-519 2.41e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.24  E-value: 2.41e-03
                           10        20
                   ....*....|....*....|....*...
gi 1831513053  492 QTPLHIASRLGNTDIVILLLQAGANSNA 519
Cdd:pfam13606    3 NTPLHLAARNGRLEIVKLLLENGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
523-552 2.43e-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: 2.43e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 1831513053   523 DNYSPLHIAAKEGQEEVAGILLDHNADKTL 552
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
350-479 2.92e-03

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 42.48  E-value: 2.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  350 APVDDVTVDYLTPLHVAAHCGHVRVAKLLLDRSADPNSRALNGF--------------TPLHIACKKNRIKVVELLLK-- 413
Cdd:cd22193     67 AEYTDEYYEGQTALHIAIERRQGDIVALLVENGADVHAHAKGRFfqpkyqgegfyfgeLPLSLAACTNQPDIVQYLLEne 146
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  414 -YRAAIEATTESGLTPLHvAAFMGAINIV--------IY--LLQQGAN--PDV--ETVR---GETPLHLAARANQTDVVR 475
Cdd:cd22193    147 hQPADIEAQDSRGNTVLH-ALVTVADNTKentkfvtrMYdmILIRGAKlcPTVelEEIRnndGLTPLQLAAKMGKIEILK 225

                   ....
gi 1831513053  476 VLIR 479
Cdd:cd22193    226 YILQ 229
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
561-661 3.02e-03

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 42.48  E-value: 3.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  561 LHLASKYGNLEvvRLLLERGTPVDIEGKnqvTPLHVAAHYNNDKVAMLLLENGASAKAAAKN--------------GYTP 626
Cdd:cd22193     52 LDIAEKTDNLK--RFINAEYTDEYYEGQ---TALHIAIERRQGDIVALLVENGADVHAHAKGrffqpkyqgegfyfGELP 126
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1831513053  627 LHIAAKKNQMEIASTLLQ---FKADPNAKSRAGFTPLH 661
Cdd:cd22193    127 LSLAACTNQPDIVQYLLEnehQPADIEAQDSRGNTVLH 164
PHA02736 PHA02736
Viral ankyrin protein; Provisional
594-680 3.17e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 40.24  E-value: 3.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  594 LHVAAhyNNDKV-----AMLLLENGASAKAA-AKNGYTPLHIAAKKNQMEIASTLL-QFKADPNAKSRAGFTPLHLSAQE 666
Cdd:PHA02736    59 VHIVS--NPDKAdpqekLKLLMEWGADINGKeRVFGNTPLHIAVYTQNYELATWLCnQPGVNMEILNYAFKTPYYVACER 136
                           90
                   ....*....|....
gi 1831513053  667 GHKEISGLLIENGS 680
Cdd:PHA02736   137 HDAKMMNILRAKGA 150
PHA02859 PHA02859
ankyrin repeat protein; Provisional
229-365 3.21e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 40.96  E-value: 3.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  229 TPLH--IAAHYGHENVGQLLLEKGANVNYQARH-NISPLHVATKWGRT---NMANLLLSRGAIIDSRTKDLLTPLH---- 298
Cdd:PHA02859    53 TPIFscLEKDKVNVEILKFLIENGADVNFKTRDnNLSALHHYLSFNKNvepEILKILIDSGSSITEEDEDGKNLLHmymc 132
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1831513053  299 -CAARSghdQVVDLLVVQGAPISAKTKNGLAPLHmaaqgdhvdaaRTLLYHRapvDDVTVDYLTPLHV 365
Cdd:PHA02859   133 nFNVRI---NVIKLLIDSGVSFLNKDFDNNNILY-----------SYILFHS---DKKIFDFLTSLGI 183
Death_ank1 cd08805
Death domain of Ankyrin-1; Death Domain (DD) of the human protein ankyrin-1 (ANK-1) and ...
1514-1577 3.53e-03

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: 38.41  E-value: 3.53e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1831513053 1514 IGADWPRLGRALEVPHRDIQHIRQNYPG---QECKNTLKIWIHLKKEDANQDNLDQALRQIGRDDIV 1577
Cdd:cd08805     14 LGLSWAELARELQFSVEDINRIRVENPNsllEQSTALLNLWVDREGENAKMEPLYPALYSIDRLTIV 80
PHA02859 PHA02859
ankyrin repeat protein; Provisional
359-451 4.34e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 40.57  E-value: 4.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  359 YLTPLH--VAAHCGHVRVAKLLLDRSADPNSRAL-NGFTPLH--IACKKN-RIKVVELLLKYRAAIEATTESGLTPLHV- 431
Cdd:PHA02859    51 YETPIFscLEKDKVNVEILKFLIENGADVNFKTRdNNLSALHhyLSFNKNvEPEILKILIDSGSSITEEDEDGKNLLHMy 130
                           90       100
                   ....*....|....*....|.
gi 1831513053  432 -AAFMGAINIVIYLLQQGANP 451
Cdd:PHA02859   131 mCNFNVRINVIKLLIDSGVSF 151
Death_p75NR cd08311
Death domain of p75 Neurotrophin Receptor; Death Domain (DD) found in p75 neurotrophin ...
1515-1580 4.59e-03

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: 37.65  E-value: 4.59e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1831513053 1515 GADWPRLGRALEVPHRDIQHI-RQNYPgqeCKNTLKIWIHlkKEDANQDNLDQALRQIGRDDIVRSI 1580
Cdd:cd08311     18 GSDWRALAGELGYSAEEIDSFaREADP---CRALLTDWSA--QDGATLGVLLTALRKIGRDDIVEIL 79
PHA02884 PHA02884
ankyrin repeat protein; Provisional
561-663 4.77e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 41.12  E-value: 4.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  561 LHLASKYGNLEVVRLLLERGT----PVDIEGKNQVTPLHVAAHYNNDKVAMLLLENGASAKAAAKNG-YTPLHIAAKKNQ 635
Cdd:PHA02884    37 LYSSIKFHYTDIIDAILKLGAdpeaPFPLSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAkITPLYISVLHGC 116
                           90       100
                   ....*....|....*....|....*...
gi 1831513053  636 MEIASTLLQFKADPNAKSRAGFTPLHLS 663
Cdd:PHA02884   117 LKCLEILLSYGADINIQTNDMVTPIELA 144
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
722-792 5.12e-03

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 41.70  E-value: 5.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  722 GYTPLHVACHFGQLNMVKFLVENGADVGEKTRASY--------------TPLHQAAQQGHNNCVRYLLENG---ASPNEQ 784
Cdd:cd22193     76 GQTALHIAIERRQGDIVALLVENGADVHAHAKGRFfqpkyqgegfyfgeLPLSLAACTNQPDIVQYLLENEhqpADIEAQ 155

                   ....*...
gi 1831513053  785 TATGQTPL 792
Cdd:cd22193    156 DSRGNTVL 163
PHA02917 PHA02917
ankyrin-like protein; Provisional
92-154 5.24e-03

ankyrin-like protein; Provisional


Pssm-ID: 165231 [Multi-domain]  Cd Length: 661  Bit Score: 41.52  E-value: 5.24e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1831513053   92 VDAATRKGNTALHIASLAGQSLIVTILVENGANVNVQSVNGFTPLYMAAQENHE-EVVKYLLKH 154
Cdd:PHA02917   445 INMIDKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYTCIAIAINESRNiELLKMLLCH 508
PHA02736 PHA02736
Viral ankyrin protein; Provisional
396-485 5.70e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 39.47  E-value: 5.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  396 LHIACKKNRI---KVVELLLKYRAAIEATTE-SGLTPLHVAAFMGAINIVIYLLQQ-GANPDVETVRGETPLHLAARANQ 470
Cdd:PHA02736    59 VHIVSNPDKAdpqEKLKLLMEWGADINGKERvFGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERHD 138
                           90
                   ....*....|....*
gi 1831513053  471 TDVVRVLIRNGAKVD 485
Cdd:PHA02736   139 AKMMNILRAKGAQCK 153
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
510-671 6.44e-03

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 41.32  E-value: 6.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  510 LLQAGANSNATTRDNYSPLHIAAKEgqeevAGILLDH-NADKTLLTKKGFTPLHLASKYGNLEVVRLLLERGTPVDIEGK 588
Cdd:cd22193     33 LMKALLNLNPGTNDTIRILLDIAEK-----TDNLKRFiNAEYTDEYYEGQTALHIAIERRQGDIVALLVENGADVHAHAK 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  589 NQV--------------TPLHVAAHYNNDKVAMLLLENG---ASAKAAAKNGYTPLH--IAAKKNQME-------IASTL 642
Cdd:cd22193    108 GRFfqpkyqgegfyfgeLPLSLAACTNQPDIVQYLLENEhqpADIEAQDSRGNTVLHalVTVADNTKEntkfvtrMYDMI 187
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1831513053  643 LQFKAD--PNAK-----SRAGFTPLHLSAQEGHKEI 671
Cdd:cd22193    188 LIRGAKlcPTVEleeirNNDGLTPLQLAAKMGKIEI 223
PHA02859 PHA02859
ankyrin repeat protein; Provisional
44-157 6.66e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 39.80  E-value: 6.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053   44 GDLEKVLELLRAGTDINTSNANGLNSLhLASKEGHSEVVRELIKRQAQVDAATRKGN-TALHIASLAGQSL---IVTILV 119
Cdd:PHA02859    32 DDIEGVKKWIKFVNDCNDLYETPIFSC-LEKDKVNVEILKFLIENGADVNFKTRDNNlSALHHYLSFNKNVepeILKILI 110
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1831513053  120 ENGANVNVQSVNGFTPL--YMAAQENHEEVVKYLLKHGAN 157
Cdd:PHA02859   111 DSGSSITEEDEDGKNLLhmYMCNFNVRINVIKLLIDSGVS 150
PHA02736 PHA02736
Viral ankyrin protein; Provisional
571-647 6.82e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 39.09  E-value: 6.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513053  571 EVVRLLLERGTpvDIEGKNQV---TPLHVAAHYNNDKVAMLLLEN-GASAKAAAKNGYTPLHIAAKKNQMEIAsTLLQFK 646
Cdd:PHA02736    72 EKLKLLMEWGA--DINGKERVfgnTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERHDAKMM-NILRAK 148

                   .
gi 1831513053  647 A 647
Cdd:PHA02736   149 G 149
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
656-687 6.89e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.73  E-value: 6.89e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1831513053  656 GFTPLHLSA-QEGHKEISGLLIENGSDVGAKAN 687
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
329-366 8.44e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.17  E-value: 8.44e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1831513053  329 PLHMAAQGDHVDAARTLLYHRAPVDDVTVDYLTPLHVA 366
Cdd:pfam13857   19 PLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
759-807 9.69e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 40.65  E-value: 9.69e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1831513053  759 LHQAAQQGHNNCVRYLLENGASPNEQTATGQTPLSIAQRLGYVSVVETL 807
Cdd:PTZ00322    86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVL 134
 
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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